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Gene Information
Gene symbol: SIRT1
Gene name: sirtuin 1
HGNC ID: 14929
Synonyms: SIR2L1
Related Genes
Related Sentences
| # | PMID | Sentence |
| 1 | 35264015 | Retraction for Su et al., SHP-1 aggravates obesity-related glomerulopathy and palmitic acid-induced podocyte injury via regulating the PI3K/Nrf2/SIRT1 axis. |
| 2 | 35222713 | At the molecular level, TUG1 was revealed to promote sirtuin 1 (SIRT1) expression by sponging microRNA (miR)-9, and SIRT1 OE reversed the HG-induced apoptosis and mitochondrial dysfunction increased by TUG1 KD. |
| 3 | 34974186 | Various key findings in podocyte autophagy were reported in the past ten years, such as the role of endoplasmic reticulum (ER) stress in podocyte autophagy impairment, podocyte autophagy-related gene, essential roles of the signaling pathways: Mammalian Target of Rapamycin (mTOR)/ Phosphoinositide 3-kinase (PI3k)/ serine/threonine kinase 1 (Akt) in podocyte autophagy. |
| 4 | 34974186 | Sirtuin-1 was reported to have a vital key role in mTOR signaling, 5'AMP-activated protein kinase (AMPK) regulation, autophagy activation, and various critical pathways associated with podocyte's function and health; it has potential value to podocyte injury pathogenesis investigation. |
| 5 | 34746831 | SIRT1 improves insulin resistance by reducing OS and regulating mitochondrial biogenesis and function. |
| 6 | 34580283 | The results of MeRIP-qPCR and dual-luciferase reporter assay indicated METTL14 promoted Sirt1 mRNA m6A modification and degradation in injured podocytes. |
| 7 | 34580283 | The results of MeRIP-qPCR and dual-luciferase reporter assay indicated METTL14 promoted Sirt1 mRNA m6A modification and degradation in injured podocytes. |
| 8 | 34580283 | Our findings suggest METTL14-dependent RNA m6A modification contributes to podocyte injury through posttranscriptional regulation of Sirt1 mRNA, which provide a potential approach for the diagnosis and treatment of podocytopathies. |
| 9 | 34580283 | Our findings suggest METTL14-dependent RNA m6A modification contributes to podocyte injury through posttranscriptional regulation of Sirt1 mRNA, which provide a potential approach for the diagnosis and treatment of podocytopathies. |
| 10 | 34396581 | Exercise training ameliorates early diabetic kidney injury by regulating the H2 S/SIRT1/p53 pathway. |
| 11 | 34396581 | Exercise training ameliorates early diabetic kidney injury by regulating the H2 S/SIRT1/p53 pathway. |
| 12 | 34396581 | Exercise training ameliorates early diabetic kidney injury by regulating the H2 S/SIRT1/p53 pathway. |
| 13 | 34396581 | Exercise training ameliorates early diabetic kidney injury by regulating the H2 S/SIRT1/p53 pathway. |
| 14 | 34396581 | Exercise training ameliorates early diabetic kidney injury by regulating the H2 S/SIRT1/p53 pathway. |
| 15 | 34396581 | Exercise training enhanced renal sirtuin 1 (SIRT1) expression in diabetic mice, accompanied by an inhibition of the p53-#ediated pro-apoptotic pathway. |
| 16 | 34396581 | Exercise training enhanced renal sirtuin 1 (SIRT1) expression in diabetic mice, accompanied by an inhibition of the p53-#ediated pro-apoptotic pathway. |
| 17 | 34396581 | Exercise training enhanced renal sirtuin 1 (SIRT1) expression in diabetic mice, accompanied by an inhibition of the p53-#ediated pro-apoptotic pathway. |
| 18 | 34396581 | Exercise training enhanced renal sirtuin 1 (SIRT1) expression in diabetic mice, accompanied by an inhibition of the p53-#ediated pro-apoptotic pathway. |
| 19 | 34396581 | Exercise training enhanced renal sirtuin 1 (SIRT1) expression in diabetic mice, accompanied by an inhibition of the p53-#ediated pro-apoptotic pathway. |
| 20 | 34396581 | NaHS treatment restored SIRT1 expression, inhibited the p53-mediated pro-apoptotic pathway and attenuated diabetes-associated apoptosis and renal injury. |
| 21 | 34396581 | NaHS treatment restored SIRT1 expression, inhibited the p53-mediated pro-apoptotic pathway and attenuated diabetes-associated apoptosis and renal injury. |
| 22 | 34396581 | NaHS treatment restored SIRT1 expression, inhibited the p53-mediated pro-apoptotic pathway and attenuated diabetes-associated apoptosis and renal injury. |
| 23 | 34396581 | NaHS treatment restored SIRT1 expression, inhibited the p53-mediated pro-apoptotic pathway and attenuated diabetes-associated apoptosis and renal injury. |
| 24 | 34396581 | NaHS treatment restored SIRT1 expression, inhibited the p53-mediated pro-apoptotic pathway and attenuated diabetes-associated apoptosis and renal injury. |
| 25 | 34396581 | In high glucose-treated MPC5 podocytes, NaHS treatment inhibited the p53-mediated pro-apoptotic pathway and podocyte apoptosis in a SIRT1-dependent manner. |
| 26 | 34396581 | In high glucose-treated MPC5 podocytes, NaHS treatment inhibited the p53-mediated pro-apoptotic pathway and podocyte apoptosis in a SIRT1-dependent manner. |
| 27 | 34396581 | In high glucose-treated MPC5 podocytes, NaHS treatment inhibited the p53-mediated pro-apoptotic pathway and podocyte apoptosis in a SIRT1-dependent manner. |
| 28 | 34396581 | In high glucose-treated MPC5 podocytes, NaHS treatment inhibited the p53-mediated pro-apoptotic pathway and podocyte apoptosis in a SIRT1-dependent manner. |
| 29 | 34396581 | In high glucose-treated MPC5 podocytes, NaHS treatment inhibited the p53-mediated pro-apoptotic pathway and podocyte apoptosis in a SIRT1-dependent manner. |
| 30 | 34396581 | Collectively, exercise training upregulated CBS/CSE expression and enhanced the endogenous H2 S production in renal tissues, thereby contributing to the modulation of the SIRT1/p53 apoptosis pathway and improvement of diabetic nephropathy. |
| 31 | 34396581 | Collectively, exercise training upregulated CBS/CSE expression and enhanced the endogenous H2 S production in renal tissues, thereby contributing to the modulation of the SIRT1/p53 apoptosis pathway and improvement of diabetic nephropathy. |
| 32 | 34396581 | Collectively, exercise training upregulated CBS/CSE expression and enhanced the endogenous H2 S production in renal tissues, thereby contributing to the modulation of the SIRT1/p53 apoptosis pathway and improvement of diabetic nephropathy. |
| 33 | 34396581 | Collectively, exercise training upregulated CBS/CSE expression and enhanced the endogenous H2 S production in renal tissues, thereby contributing to the modulation of the SIRT1/p53 apoptosis pathway and improvement of diabetic nephropathy. |
| 34 | 34396581 | Collectively, exercise training upregulated CBS/CSE expression and enhanced the endogenous H2 S production in renal tissues, thereby contributing to the modulation of the SIRT1/p53 apoptosis pathway and improvement of diabetic nephropathy. |
| 35 | 34371008 | High glucose concentrations stimulated reactive oxygen species production through NADPH oxidase activation, decreased adenosine monophosphate-activated protein kinase (AMPK) phosphorylation, and reduced deacetylase sirtuin 1 (SIRT1) protein levels and activity. |
| 36 | 34371008 | Calcium signaling involving transient receptor potential cation channel C, member 6 (TRPC6) also was demonstrated to play an essential role in the regulation of insulin-dependent signaling and glucose uptake in podocytes. |
| 37 | 34364389 | Regarding inflammatory responses, IL-1, IL-6β, TNF-α, SIRT1, NF-κB, and TGF-β1/smad are thought to be essential. |
| 38 | 34252390 | The protein deacetylase sirtuin 1 (SIRT1) and adenosine monophosphate-dependent protein kinase (AMPK) play important roles in the development of insulin resistance. |
| 39 | 34252390 | The protein deacetylase sirtuin 1 (SIRT1) and adenosine monophosphate-dependent protein kinase (AMPK) play important roles in the development of insulin resistance. |
| 40 | 34252390 | The protein deacetylase sirtuin 1 (SIRT1) and adenosine monophosphate-dependent protein kinase (AMPK) play important roles in the development of insulin resistance. |
| 41 | 34252390 | The protein deacetylase sirtuin 1 (SIRT1) and adenosine monophosphate-dependent protein kinase (AMPK) play important roles in the development of insulin resistance. |
| 42 | 34252390 | The protein deacetylase sirtuin 1 (SIRT1) and adenosine monophosphate-dependent protein kinase (AMPK) play important roles in the development of insulin resistance. |
| 43 | 34252390 | The protein deacetylase sirtuin 1 (SIRT1) and adenosine monophosphate-dependent protein kinase (AMPK) play important roles in the development of insulin resistance. |
| 44 | 34252390 | SIRT1 protein levels and activity and AMPK phosphorylation decrease under hyperglycemic conditions, with concomitant inhibition of the effect of insulin on glucose uptake into these cells. |
| 45 | 34252390 | SIRT1 protein levels and activity and AMPK phosphorylation decrease under hyperglycemic conditions, with concomitant inhibition of the effect of insulin on glucose uptake into these cells. |
| 46 | 34252390 | SIRT1 protein levels and activity and AMPK phosphorylation decrease under hyperglycemic conditions, with concomitant inhibition of the effect of insulin on glucose uptake into these cells. |
| 47 | 34252390 | SIRT1 protein levels and activity and AMPK phosphorylation decrease under hyperglycemic conditions, with concomitant inhibition of the effect of insulin on glucose uptake into these cells. |
| 48 | 34252390 | SIRT1 protein levels and activity and AMPK phosphorylation decrease under hyperglycemic conditions, with concomitant inhibition of the effect of insulin on glucose uptake into these cells. |
| 49 | 34252390 | SIRT1 protein levels and activity and AMPK phosphorylation decrease under hyperglycemic conditions, with concomitant inhibition of the effect of insulin on glucose uptake into these cells. |
| 50 | 34252390 | We examined the effects of NOS/NO pathway alterations on SIRT1/AMPK signaling and glucose uptake using pharmacological tools and a small-interfering transfection approach. |
| 51 | 34252390 | We examined the effects of NOS/NO pathway alterations on SIRT1/AMPK signaling and glucose uptake using pharmacological tools and a small-interfering transfection approach. |
| 52 | 34252390 | We examined the effects of NOS/NO pathway alterations on SIRT1/AMPK signaling and glucose uptake using pharmacological tools and a small-interfering transfection approach. |
| 53 | 34252390 | We examined the effects of NOS/NO pathway alterations on SIRT1/AMPK signaling and glucose uptake using pharmacological tools and a small-interfering transfection approach. |
| 54 | 34252390 | We examined the effects of NOS/NO pathway alterations on SIRT1/AMPK signaling and glucose uptake using pharmacological tools and a small-interfering transfection approach. |
| 55 | 34252390 | We examined the effects of NOS/NO pathway alterations on SIRT1/AMPK signaling and glucose uptake using pharmacological tools and a small-interfering transfection approach. |
| 56 | 34252390 | We also examined the ability of the NOS/NO pathway to protect podocytes against high glucose-induced alterations of SIRT1/AMPK signaling and insulin-dependent glucose uptake. |
| 57 | 34252390 | We also examined the ability of the NOS/NO pathway to protect podocytes against high glucose-induced alterations of SIRT1/AMPK signaling and insulin-dependent glucose uptake. |
| 58 | 34252390 | We also examined the ability of the NOS/NO pathway to protect podocytes against high glucose-induced alterations of SIRT1/AMPK signaling and insulin-dependent glucose uptake. |
| 59 | 34252390 | We also examined the ability of the NOS/NO pathway to protect podocytes against high glucose-induced alterations of SIRT1/AMPK signaling and insulin-dependent glucose uptake. |
| 60 | 34252390 | We also examined the ability of the NOS/NO pathway to protect podocytes against high glucose-induced alterations of SIRT1/AMPK signaling and insulin-dependent glucose uptake. |
| 61 | 34252390 | We also examined the ability of the NOS/NO pathway to protect podocytes against high glucose-induced alterations of SIRT1/AMPK signaling and insulin-dependent glucose uptake. |
| 62 | 34252390 | Inhibition of the NOS/NO pathway reduced SIRT1 protein levels and activity, leading to a decrease in AMPK phosphorylation and blockade of the effect of insulin on glucose uptake. |
| 63 | 34252390 | Inhibition of the NOS/NO pathway reduced SIRT1 protein levels and activity, leading to a decrease in AMPK phosphorylation and blockade of the effect of insulin on glucose uptake. |
| 64 | 34252390 | Inhibition of the NOS/NO pathway reduced SIRT1 protein levels and activity, leading to a decrease in AMPK phosphorylation and blockade of the effect of insulin on glucose uptake. |
| 65 | 34252390 | Inhibition of the NOS/NO pathway reduced SIRT1 protein levels and activity, leading to a decrease in AMPK phosphorylation and blockade of the effect of insulin on glucose uptake. |
| 66 | 34252390 | Inhibition of the NOS/NO pathway reduced SIRT1 protein levels and activity, leading to a decrease in AMPK phosphorylation and blockade of the effect of insulin on glucose uptake. |
| 67 | 34252390 | Inhibition of the NOS/NO pathway reduced SIRT1 protein levels and activity, leading to a decrease in AMPK phosphorylation and blockade of the effect of insulin on glucose uptake. |
| 68 | 34252390 | Treatment with the NO donor S-nitroso-N-acetylpenicillamine (SNAP) prevented high glucose-induced decreases in SIRT1 and AMPK activity and increased GLUT4 protein expression, thereby improving glucose uptake in podocytes. |
| 69 | 34252390 | Treatment with the NO donor S-nitroso-N-acetylpenicillamine (SNAP) prevented high glucose-induced decreases in SIRT1 and AMPK activity and increased GLUT4 protein expression, thereby improving glucose uptake in podocytes. |
| 70 | 34252390 | Treatment with the NO donor S-nitroso-N-acetylpenicillamine (SNAP) prevented high glucose-induced decreases in SIRT1 and AMPK activity and increased GLUT4 protein expression, thereby improving glucose uptake in podocytes. |
| 71 | 34252390 | Treatment with the NO donor S-nitroso-N-acetylpenicillamine (SNAP) prevented high glucose-induced decreases in SIRT1 and AMPK activity and increased GLUT4 protein expression, thereby improving glucose uptake in podocytes. |
| 72 | 34252390 | Treatment with the NO donor S-nitroso-N-acetylpenicillamine (SNAP) prevented high glucose-induced decreases in SIRT1 and AMPK activity and increased GLUT4 protein expression, thereby improving glucose uptake in podocytes. |
| 73 | 34252390 | Treatment with the NO donor S-nitroso-N-acetylpenicillamine (SNAP) prevented high glucose-induced decreases in SIRT1 and AMPK activity and increased GLUT4 protein expression, thereby improving glucose uptake in podocytes. |
| 74 | 34252390 | These findings suggest that inhibition of the NOS/NO pathway may result in alterations of the effects of insulin on glucose uptake in podocytes. |
| 75 | 34252390 | These findings suggest that inhibition of the NOS/NO pathway may result in alterations of the effects of insulin on glucose uptake in podocytes. |
| 76 | 34252390 | These findings suggest that inhibition of the NOS/NO pathway may result in alterations of the effects of insulin on glucose uptake in podocytes. |
| 77 | 34252390 | These findings suggest that inhibition of the NOS/NO pathway may result in alterations of the effects of insulin on glucose uptake in podocytes. |
| 78 | 34252390 | These findings suggest that inhibition of the NOS/NO pathway may result in alterations of the effects of insulin on glucose uptake in podocytes. |
| 79 | 34252390 | These findings suggest that inhibition of the NOS/NO pathway may result in alterations of the effects of insulin on glucose uptake in podocytes. |
| 80 | 33957017 | Faster lipid β-oxidation rate by acetyl-CoA carboxylase 2 inhibition alleviates high-glucose-induced insulin resistance via SIRT1/PGC-1α in human podocytes. |
| 81 | 33957017 | Faster lipid β-oxidation rate by acetyl-CoA carboxylase 2 inhibition alleviates high-glucose-induced insulin resistance via SIRT1/PGC-1α in human podocytes. |
| 82 | 33957017 | Faster lipid β-oxidation rate by acetyl-CoA carboxylase 2 inhibition alleviates high-glucose-induced insulin resistance via SIRT1/PGC-1α in human podocytes. |
| 83 | 33957017 | Faster lipid β-oxidation rate by acetyl-CoA carboxylase 2 inhibition alleviates high-glucose-induced insulin resistance via SIRT1/PGC-1α in human podocytes. |
| 84 | 33957017 | Faster lipid β-oxidation rate by acetyl-CoA carboxylase 2 inhibition alleviates high-glucose-induced insulin resistance via SIRT1/PGC-1α in human podocytes. |
| 85 | 33957017 | Increasing evidence shows that acetyl-CoA carboxylase 2 (ACC2) plays a crucial role in the metabolism of fatty acid, but its effect in podocyte injury of DN is still unclear. |
| 86 | 33957017 | Increasing evidence shows that acetyl-CoA carboxylase 2 (ACC2) plays a crucial role in the metabolism of fatty acid, but its effect in podocyte injury of DN is still unclear. |
| 87 | 33957017 | Increasing evidence shows that acetyl-CoA carboxylase 2 (ACC2) plays a crucial role in the metabolism of fatty acid, but its effect in podocyte injury of DN is still unclear. |
| 88 | 33957017 | Increasing evidence shows that acetyl-CoA carboxylase 2 (ACC2) plays a crucial role in the metabolism of fatty acid, but its effect in podocyte injury of DN is still unclear. |
| 89 | 33957017 | Increasing evidence shows that acetyl-CoA carboxylase 2 (ACC2) plays a crucial role in the metabolism of fatty acid, but its effect in podocyte injury of DN is still unclear. |
| 90 | 33957017 | In this study, we investigated whether ACC2 could be a therapeutic target of lipid deposition induced by hyperglycemia in the human podocytes. |
| 91 | 33957017 | In this study, we investigated whether ACC2 could be a therapeutic target of lipid deposition induced by hyperglycemia in the human podocytes. |
| 92 | 33957017 | In this study, we investigated whether ACC2 could be a therapeutic target of lipid deposition induced by hyperglycemia in the human podocytes. |
| 93 | 33957017 | In this study, we investigated whether ACC2 could be a therapeutic target of lipid deposition induced by hyperglycemia in the human podocytes. |
| 94 | 33957017 | In this study, we investigated whether ACC2 could be a therapeutic target of lipid deposition induced by hyperglycemia in the human podocytes. |
| 95 | 33957017 | It also contributed to the downregulation of phosphorylated ACC2 (p-ACC2), which is an inactive form of ACC2. |
| 96 | 33957017 | It also contributed to the downregulation of phosphorylated ACC2 (p-ACC2), which is an inactive form of ACC2. |
| 97 | 33957017 | It also contributed to the downregulation of phosphorylated ACC2 (p-ACC2), which is an inactive form of ACC2. |
| 98 | 33957017 | It also contributed to the downregulation of phosphorylated ACC2 (p-ACC2), which is an inactive form of ACC2. |
| 99 | 33957017 | It also contributed to the downregulation of phosphorylated ACC2 (p-ACC2), which is an inactive form of ACC2. |
| 100 | 33957017 | Knockdown of ACC2 by sh-RNA reduced lipid deposition induced by HG. |
| 101 | 33957017 | Knockdown of ACC2 by sh-RNA reduced lipid deposition induced by HG. |
| 102 | 33957017 | Knockdown of ACC2 by sh-RNA reduced lipid deposition induced by HG. |
| 103 | 33957017 | Knockdown of ACC2 by sh-RNA reduced lipid deposition induced by HG. |
| 104 | 33957017 | Knockdown of ACC2 by sh-RNA reduced lipid deposition induced by HG. |
| 105 | 33957017 | Additionally, ACC2-shRNA restored the expression of glucose transporter 4 (GLUT4) on the cell surface, which was downregulated in HG and normalized in the insulin signaling pathway. |
| 106 | 33957017 | Additionally, ACC2-shRNA restored the expression of glucose transporter 4 (GLUT4) on the cell surface, which was downregulated in HG and normalized in the insulin signaling pathway. |
| 107 | 33957017 | Additionally, ACC2-shRNA restored the expression of glucose transporter 4 (GLUT4) on the cell surface, which was downregulated in HG and normalized in the insulin signaling pathway. |
| 108 | 33957017 | Additionally, ACC2-shRNA restored the expression of glucose transporter 4 (GLUT4) on the cell surface, which was downregulated in HG and normalized in the insulin signaling pathway. |
| 109 | 33957017 | Additionally, ACC2-shRNA restored the expression of glucose transporter 4 (GLUT4) on the cell surface, which was downregulated in HG and normalized in the insulin signaling pathway. |
| 110 | 33957017 | Mechanistically, SIRT1/PGC-1α is close related to the insulin metabolism pathway. |
| 111 | 33957017 | Mechanistically, SIRT1/PGC-1α is close related to the insulin metabolism pathway. |
| 112 | 33957017 | Mechanistically, SIRT1/PGC-1α is close related to the insulin metabolism pathway. |
| 113 | 33957017 | Mechanistically, SIRT1/PGC-1α is close related to the insulin metabolism pathway. |
| 114 | 33957017 | Mechanistically, SIRT1/PGC-1α is close related to the insulin metabolism pathway. |
| 115 | 33957017 | ACC2-shRNA could restore the expression of SIRT1/PGC-1α, which was downregulated in HG. |
| 116 | 33957017 | ACC2-shRNA could restore the expression of SIRT1/PGC-1α, which was downregulated in HG. |
| 117 | 33957017 | ACC2-shRNA could restore the expression of SIRT1/PGC-1α, which was downregulated in HG. |
| 118 | 33957017 | ACC2-shRNA could restore the expression of SIRT1/PGC-1α, which was downregulated in HG. |
| 119 | 33957017 | ACC2-shRNA could restore the expression of SIRT1/PGC-1α, which was downregulated in HG. |
| 120 | 33957017 | Rescue experiment revealed that inhibition of SIRT1 by EX-527 counteracted the effect of ACC2-shRNA. |
| 121 | 33957017 | Rescue experiment revealed that inhibition of SIRT1 by EX-527 counteracted the effect of ACC2-shRNA. |
| 122 | 33957017 | Rescue experiment revealed that inhibition of SIRT1 by EX-527 counteracted the effect of ACC2-shRNA. |
| 123 | 33957017 | Rescue experiment revealed that inhibition of SIRT1 by EX-527 counteracted the effect of ACC2-shRNA. |
| 124 | 33957017 | Rescue experiment revealed that inhibition of SIRT1 by EX-527 counteracted the effect of ACC2-shRNA. |
| 125 | 33957017 | Taken together, our data suggest that podocyte injury mediated by HG-induced insulin resistance and lipotoxicity could be alleviated by ACC2 inhibition via SIRT1/PGC-1α. |
| 126 | 33957017 | Taken together, our data suggest that podocyte injury mediated by HG-induced insulin resistance and lipotoxicity could be alleviated by ACC2 inhibition via SIRT1/PGC-1α. |
| 127 | 33957017 | Taken together, our data suggest that podocyte injury mediated by HG-induced insulin resistance and lipotoxicity could be alleviated by ACC2 inhibition via SIRT1/PGC-1α. |
| 128 | 33957017 | Taken together, our data suggest that podocyte injury mediated by HG-induced insulin resistance and lipotoxicity could be alleviated by ACC2 inhibition via SIRT1/PGC-1α. |
| 129 | 33957017 | Taken together, our data suggest that podocyte injury mediated by HG-induced insulin resistance and lipotoxicity could be alleviated by ACC2 inhibition via SIRT1/PGC-1α. |
| 130 | 33932899 | Inhibition of p53/miR-34a/SIRT1 axis ameliorates podocyte injury in diabetic nephropathy. |
| 131 | 33932899 | Inhibition of p53/miR-34a/SIRT1 axis ameliorates podocyte injury in diabetic nephropathy. |
| 132 | 33932899 | Inhibition of p53/miR-34a/SIRT1 axis ameliorates podocyte injury in diabetic nephropathy. |
| 133 | 33932899 | Inhibition of p53/miR-34a/SIRT1 axis ameliorates podocyte injury in diabetic nephropathy. |
| 134 | 33932899 | Inhibition of p53/miR-34a/SIRT1 axis ameliorates podocyte injury in diabetic nephropathy. |
| 135 | 33932899 | Inhibition of p53/miR-34a/SIRT1 axis ameliorates podocyte injury in diabetic nephropathy. |
| 136 | 33932899 | Inhibition of p53/miR-34a/SIRT1 axis ameliorates podocyte injury in diabetic nephropathy. |
| 137 | 33932899 | Inhibition of p53/miR-34a/SIRT1 axis ameliorates podocyte injury in diabetic nephropathy. |
| 138 | 33932899 | Inhibition of p53/miR-34a/SIRT1 axis ameliorates podocyte injury in diabetic nephropathy. |
| 139 | 33932899 | Inhibition of p53/miR-34a/SIRT1 axis ameliorates podocyte injury in diabetic nephropathy. |
| 140 | 33932899 | MiR-34a, a p53-regulated miRNA, directly targets SIRT1 and contributed to DN progression. |
| 141 | 33932899 | MiR-34a, a p53-regulated miRNA, directly targets SIRT1 and contributed to DN progression. |
| 142 | 33932899 | MiR-34a, a p53-regulated miRNA, directly targets SIRT1 and contributed to DN progression. |
| 143 | 33932899 | MiR-34a, a p53-regulated miRNA, directly targets SIRT1 and contributed to DN progression. |
| 144 | 33932899 | MiR-34a, a p53-regulated miRNA, directly targets SIRT1 and contributed to DN progression. |
| 145 | 33932899 | MiR-34a, a p53-regulated miRNA, directly targets SIRT1 and contributed to DN progression. |
| 146 | 33932899 | MiR-34a, a p53-regulated miRNA, directly targets SIRT1 and contributed to DN progression. |
| 147 | 33932899 | MiR-34a, a p53-regulated miRNA, directly targets SIRT1 and contributed to DN progression. |
| 148 | 33932899 | MiR-34a, a p53-regulated miRNA, directly targets SIRT1 and contributed to DN progression. |
| 149 | 33932899 | MiR-34a, a p53-regulated miRNA, directly targets SIRT1 and contributed to DN progression. |
| 150 | 33932899 | MiR-34a represses SIRT1 to activate p53 and establish a positive feedback loop. |
| 151 | 33932899 | MiR-34a represses SIRT1 to activate p53 and establish a positive feedback loop. |
| 152 | 33932899 | MiR-34a represses SIRT1 to activate p53 and establish a positive feedback loop. |
| 153 | 33932899 | MiR-34a represses SIRT1 to activate p53 and establish a positive feedback loop. |
| 154 | 33932899 | MiR-34a represses SIRT1 to activate p53 and establish a positive feedback loop. |
| 155 | 33932899 | MiR-34a represses SIRT1 to activate p53 and establish a positive feedback loop. |
| 156 | 33932899 | MiR-34a represses SIRT1 to activate p53 and establish a positive feedback loop. |
| 157 | 33932899 | MiR-34a represses SIRT1 to activate p53 and establish a positive feedback loop. |
| 158 | 33932899 | MiR-34a represses SIRT1 to activate p53 and establish a positive feedback loop. |
| 159 | 33932899 | MiR-34a represses SIRT1 to activate p53 and establish a positive feedback loop. |
| 160 | 33932899 | However, whether p53/miR-34a/SIRT1 signaling is activated in podocytes and contributes to DN pathogenesis remains elusive. |
| 161 | 33932899 | However, whether p53/miR-34a/SIRT1 signaling is activated in podocytes and contributes to DN pathogenesis remains elusive. |
| 162 | 33932899 | However, whether p53/miR-34a/SIRT1 signaling is activated in podocytes and contributes to DN pathogenesis remains elusive. |
| 163 | 33932899 | However, whether p53/miR-34a/SIRT1 signaling is activated in podocytes and contributes to DN pathogenesis remains elusive. |
| 164 | 33932899 | However, whether p53/miR-34a/SIRT1 signaling is activated in podocytes and contributes to DN pathogenesis remains elusive. |
| 165 | 33932899 | However, whether p53/miR-34a/SIRT1 signaling is activated in podocytes and contributes to DN pathogenesis remains elusive. |
| 166 | 33932899 | However, whether p53/miR-34a/SIRT1 signaling is activated in podocytes and contributes to DN pathogenesis remains elusive. |
| 167 | 33932899 | However, whether p53/miR-34a/SIRT1 signaling is activated in podocytes and contributes to DN pathogenesis remains elusive. |
| 168 | 33932899 | However, whether p53/miR-34a/SIRT1 signaling is activated in podocytes and contributes to DN pathogenesis remains elusive. |
| 169 | 33932899 | However, whether p53/miR-34a/SIRT1 signaling is activated in podocytes and contributes to DN pathogenesis remains elusive. |
| 170 | 33932899 | The expression of acetylated p53 and miR-34a was upregulated, SIRT1was downregulated in glomeruli from patients with DN and STZ induced diabetic mice, as well as in human podocytes treated with advanced glycation end (AGE). |
| 171 | 33932899 | The expression of acetylated p53 and miR-34a was upregulated, SIRT1was downregulated in glomeruli from patients with DN and STZ induced diabetic mice, as well as in human podocytes treated with advanced glycation end (AGE). |
| 172 | 33932899 | The expression of acetylated p53 and miR-34a was upregulated, SIRT1was downregulated in glomeruli from patients with DN and STZ induced diabetic mice, as well as in human podocytes treated with advanced glycation end (AGE). |
| 173 | 33932899 | The expression of acetylated p53 and miR-34a was upregulated, SIRT1was downregulated in glomeruli from patients with DN and STZ induced diabetic mice, as well as in human podocytes treated with advanced glycation end (AGE). |
| 174 | 33932899 | The expression of acetylated p53 and miR-34a was upregulated, SIRT1was downregulated in glomeruli from patients with DN and STZ induced diabetic mice, as well as in human podocytes treated with advanced glycation end (AGE). |
| 175 | 33932899 | The expression of acetylated p53 and miR-34a was upregulated, SIRT1was downregulated in glomeruli from patients with DN and STZ induced diabetic mice, as well as in human podocytes treated with advanced glycation end (AGE). |
| 176 | 33932899 | The expression of acetylated p53 and miR-34a was upregulated, SIRT1was downregulated in glomeruli from patients with DN and STZ induced diabetic mice, as well as in human podocytes treated with advanced glycation end (AGE). |
| 177 | 33932899 | The expression of acetylated p53 and miR-34a was upregulated, SIRT1was downregulated in glomeruli from patients with DN and STZ induced diabetic mice, as well as in human podocytes treated with advanced glycation end (AGE). |
| 178 | 33932899 | The expression of acetylated p53 and miR-34a was upregulated, SIRT1was downregulated in glomeruli from patients with DN and STZ induced diabetic mice, as well as in human podocytes treated with advanced glycation end (AGE). |
| 179 | 33932899 | The expression of acetylated p53 and miR-34a was upregulated, SIRT1was downregulated in glomeruli from patients with DN and STZ induced diabetic mice, as well as in human podocytes treated with advanced glycation end (AGE). |
| 180 | 33932899 | In human podocyte, inhibition of AGE formation by pyridoxamine prevented miR-34a dependent repression of SIRT1, p53 acetylation and activate podocyte autophagy in a dose-dependent manner. |
| 181 | 33932899 | In human podocyte, inhibition of AGE formation by pyridoxamine prevented miR-34a dependent repression of SIRT1, p53 acetylation and activate podocyte autophagy in a dose-dependent manner. |
| 182 | 33932899 | In human podocyte, inhibition of AGE formation by pyridoxamine prevented miR-34a dependent repression of SIRT1, p53 acetylation and activate podocyte autophagy in a dose-dependent manner. |
| 183 | 33932899 | In human podocyte, inhibition of AGE formation by pyridoxamine prevented miR-34a dependent repression of SIRT1, p53 acetylation and activate podocyte autophagy in a dose-dependent manner. |
| 184 | 33932899 | In human podocyte, inhibition of AGE formation by pyridoxamine prevented miR-34a dependent repression of SIRT1, p53 acetylation and activate podocyte autophagy in a dose-dependent manner. |
| 185 | 33932899 | In human podocyte, inhibition of AGE formation by pyridoxamine prevented miR-34a dependent repression of SIRT1, p53 acetylation and activate podocyte autophagy in a dose-dependent manner. |
| 186 | 33932899 | In human podocyte, inhibition of AGE formation by pyridoxamine prevented miR-34a dependent repression of SIRT1, p53 acetylation and activate podocyte autophagy in a dose-dependent manner. |
| 187 | 33932899 | In human podocyte, inhibition of AGE formation by pyridoxamine prevented miR-34a dependent repression of SIRT1, p53 acetylation and activate podocyte autophagy in a dose-dependent manner. |
| 188 | 33932899 | In human podocyte, inhibition of AGE formation by pyridoxamine prevented miR-34a dependent repression of SIRT1, p53 acetylation and activate podocyte autophagy in a dose-dependent manner. |
| 189 | 33932899 | In human podocyte, inhibition of AGE formation by pyridoxamine prevented miR-34a dependent repression of SIRT1, p53 acetylation and activate podocyte autophagy in a dose-dependent manner. |
| 190 | 33932899 | MiR-34a overexpression increases acetylation of p53 by translational repression of SIRT1. |
| 191 | 33932899 | MiR-34a overexpression increases acetylation of p53 by translational repression of SIRT1. |
| 192 | 33932899 | MiR-34a overexpression increases acetylation of p53 by translational repression of SIRT1. |
| 193 | 33932899 | MiR-34a overexpression increases acetylation of p53 by translational repression of SIRT1. |
| 194 | 33932899 | MiR-34a overexpression increases acetylation of p53 by translational repression of SIRT1. |
| 195 | 33932899 | MiR-34a overexpression increases acetylation of p53 by translational repression of SIRT1. |
| 196 | 33932899 | MiR-34a overexpression increases acetylation of p53 by translational repression of SIRT1. |
| 197 | 33932899 | MiR-34a overexpression increases acetylation of p53 by translational repression of SIRT1. |
| 198 | 33932899 | MiR-34a overexpression increases acetylation of p53 by translational repression of SIRT1. |
| 199 | 33932899 | MiR-34a overexpression increases acetylation of p53 by translational repression of SIRT1. |
| 200 | 33932899 | SIRT1 overexpression also impacts AGE induced apoptosis through deacetylating p53, whereas silencing of SIRT1 by EX527 attenuated the cytoprotective functions of miR-34a knockdown. |
| 201 | 33932899 | SIRT1 overexpression also impacts AGE induced apoptosis through deacetylating p53, whereas silencing of SIRT1 by EX527 attenuated the cytoprotective functions of miR-34a knockdown. |
| 202 | 33932899 | SIRT1 overexpression also impacts AGE induced apoptosis through deacetylating p53, whereas silencing of SIRT1 by EX527 attenuated the cytoprotective functions of miR-34a knockdown. |
| 203 | 33932899 | SIRT1 overexpression also impacts AGE induced apoptosis through deacetylating p53, whereas silencing of SIRT1 by EX527 attenuated the cytoprotective functions of miR-34a knockdown. |
| 204 | 33932899 | SIRT1 overexpression also impacts AGE induced apoptosis through deacetylating p53, whereas silencing of SIRT1 by EX527 attenuated the cytoprotective functions of miR-34a knockdown. |
| 205 | 33932899 | SIRT1 overexpression also impacts AGE induced apoptosis through deacetylating p53, whereas silencing of SIRT1 by EX527 attenuated the cytoprotective functions of miR-34a knockdown. |
| 206 | 33932899 | SIRT1 overexpression also impacts AGE induced apoptosis through deacetylating p53, whereas silencing of SIRT1 by EX527 attenuated the cytoprotective functions of miR-34a knockdown. |
| 207 | 33932899 | SIRT1 overexpression also impacts AGE induced apoptosis through deacetylating p53, whereas silencing of SIRT1 by EX527 attenuated the cytoprotective functions of miR-34a knockdown. |
| 208 | 33932899 | SIRT1 overexpression also impacts AGE induced apoptosis through deacetylating p53, whereas silencing of SIRT1 by EX527 attenuated the cytoprotective functions of miR-34a knockdown. |
| 209 | 33932899 | SIRT1 overexpression also impacts AGE induced apoptosis through deacetylating p53, whereas silencing of SIRT1 by EX527 attenuated the cytoprotective functions of miR-34a knockdown. |
| 210 | 33932899 | Moreover, blockade of p53 acetylation significantly rescued miR-34a-induced apoptosis through SIRT1 restoration. |
| 211 | 33932899 | Moreover, blockade of p53 acetylation significantly rescued miR-34a-induced apoptosis through SIRT1 restoration. |
| 212 | 33932899 | Moreover, blockade of p53 acetylation significantly rescued miR-34a-induced apoptosis through SIRT1 restoration. |
| 213 | 33932899 | Moreover, blockade of p53 acetylation significantly rescued miR-34a-induced apoptosis through SIRT1 restoration. |
| 214 | 33932899 | Moreover, blockade of p53 acetylation significantly rescued miR-34a-induced apoptosis through SIRT1 restoration. |
| 215 | 33932899 | Moreover, blockade of p53 acetylation significantly rescued miR-34a-induced apoptosis through SIRT1 restoration. |
| 216 | 33932899 | Moreover, blockade of p53 acetylation significantly rescued miR-34a-induced apoptosis through SIRT1 restoration. |
| 217 | 33932899 | Moreover, blockade of p53 acetylation significantly rescued miR-34a-induced apoptosis through SIRT1 restoration. |
| 218 | 33932899 | Moreover, blockade of p53 acetylation significantly rescued miR-34a-induced apoptosis through SIRT1 restoration. |
| 219 | 33932899 | Moreover, blockade of p53 acetylation significantly rescued miR-34a-induced apoptosis through SIRT1 restoration. |
| 220 | 33932899 | Collectively, we demonstrate that by activation of p53, AGE induced the transcription of miR-34a, miR-34a in turn repressed SIRT1 to activate p53, resulting in a positive-feedback loop and contributing to podocyte injury. |
| 221 | 33932899 | Collectively, we demonstrate that by activation of p53, AGE induced the transcription of miR-34a, miR-34a in turn repressed SIRT1 to activate p53, resulting in a positive-feedback loop and contributing to podocyte injury. |
| 222 | 33932899 | Collectively, we demonstrate that by activation of p53, AGE induced the transcription of miR-34a, miR-34a in turn repressed SIRT1 to activate p53, resulting in a positive-feedback loop and contributing to podocyte injury. |
| 223 | 33932899 | Collectively, we demonstrate that by activation of p53, AGE induced the transcription of miR-34a, miR-34a in turn repressed SIRT1 to activate p53, resulting in a positive-feedback loop and contributing to podocyte injury. |
| 224 | 33932899 | Collectively, we demonstrate that by activation of p53, AGE induced the transcription of miR-34a, miR-34a in turn repressed SIRT1 to activate p53, resulting in a positive-feedback loop and contributing to podocyte injury. |
| 225 | 33932899 | Collectively, we demonstrate that by activation of p53, AGE induced the transcription of miR-34a, miR-34a in turn repressed SIRT1 to activate p53, resulting in a positive-feedback loop and contributing to podocyte injury. |
| 226 | 33932899 | Collectively, we demonstrate that by activation of p53, AGE induced the transcription of miR-34a, miR-34a in turn repressed SIRT1 to activate p53, resulting in a positive-feedback loop and contributing to podocyte injury. |
| 227 | 33932899 | Collectively, we demonstrate that by activation of p53, AGE induced the transcription of miR-34a, miR-34a in turn repressed SIRT1 to activate p53, resulting in a positive-feedback loop and contributing to podocyte injury. |
| 228 | 33932899 | Collectively, we demonstrate that by activation of p53, AGE induced the transcription of miR-34a, miR-34a in turn repressed SIRT1 to activate p53, resulting in a positive-feedback loop and contributing to podocyte injury. |
| 229 | 33932899 | Collectively, we demonstrate that by activation of p53, AGE induced the transcription of miR-34a, miR-34a in turn repressed SIRT1 to activate p53, resulting in a positive-feedback loop and contributing to podocyte injury. |
| 230 | 33932899 | Targeting modulation of p53/miR-34a/SIRT1 feedback by miR-34a knockdown or overexpression of SIRT1 could rescue podocyte injury during DN. |
| 231 | 33932899 | Targeting modulation of p53/miR-34a/SIRT1 feedback by miR-34a knockdown or overexpression of SIRT1 could rescue podocyte injury during DN. |
| 232 | 33932899 | Targeting modulation of p53/miR-34a/SIRT1 feedback by miR-34a knockdown or overexpression of SIRT1 could rescue podocyte injury during DN. |
| 233 | 33932899 | Targeting modulation of p53/miR-34a/SIRT1 feedback by miR-34a knockdown or overexpression of SIRT1 could rescue podocyte injury during DN. |
| 234 | 33932899 | Targeting modulation of p53/miR-34a/SIRT1 feedback by miR-34a knockdown or overexpression of SIRT1 could rescue podocyte injury during DN. |
| 235 | 33932899 | Targeting modulation of p53/miR-34a/SIRT1 feedback by miR-34a knockdown or overexpression of SIRT1 could rescue podocyte injury during DN. |
| 236 | 33932899 | Targeting modulation of p53/miR-34a/SIRT1 feedback by miR-34a knockdown or overexpression of SIRT1 could rescue podocyte injury during DN. |
| 237 | 33932899 | Targeting modulation of p53/miR-34a/SIRT1 feedback by miR-34a knockdown or overexpression of SIRT1 could rescue podocyte injury during DN. |
| 238 | 33932899 | Targeting modulation of p53/miR-34a/SIRT1 feedback by miR-34a knockdown or overexpression of SIRT1 could rescue podocyte injury during DN. |
| 239 | 33932899 | Targeting modulation of p53/miR-34a/SIRT1 feedback by miR-34a knockdown or overexpression of SIRT1 could rescue podocyte injury during DN. |
| 240 | 33897448 | Silencing of miR-150-5p Ameliorates Diabetic Nephropathy by Targeting SIRT1/p53/AMPK Pathway. |
| 241 | 33897448 | Silencing of miR-150-5p Ameliorates Diabetic Nephropathy by Targeting SIRT1/p53/AMPK Pathway. |
| 242 | 33897448 | Importantly, we found that the silencing of miR-150-5p promoted the interaction between SIRT1 and p53, causing the suppression of p53 acetylation in podocytes and kidney tissue. |
| 243 | 33897448 | Importantly, we found that the silencing of miR-150-5p promoted the interaction between SIRT1 and p53, causing the suppression of p53 acetylation in podocytes and kidney tissue. |
| 244 | 33843045 | Sirtuin 1 (SIRT1) and tristetraprolin (TTP) are two important protective factors in DN; however, the regulatory relationship between SIRT1 and TTP, and the underneath mechanism are interesting but still unclear. |
| 245 | 33843045 | Sirtuin 1 (SIRT1) and tristetraprolin (TTP) are two important protective factors in DN; however, the regulatory relationship between SIRT1 and TTP, and the underneath mechanism are interesting but still unclear. |
| 246 | 33843045 | Furthermore, our in vitro and in vivo experiments also indicated miR-138 could target SIRT1 and affect TTP through p38 pathway. |
| 247 | 33843045 | Furthermore, our in vitro and in vivo experiments also indicated miR-138 could target SIRT1 and affect TTP through p38 pathway. |
| 248 | 33748285 | Inhibition of miRNA-155 Alleviates High Glucose-Induced Podocyte Inflammation by Targeting SIRT1 in Diabetic Mice. |
| 249 | 33427556 | We found that Yishen capsule relieved pathological changes, decreased urine protein, increased SIRT1, LC3-II, and Beclin-1 expression, and reduced acetylated NF-κB p65 expression in vivo. |
| 250 | 33427556 | We found that Yishen capsule relieved pathological changes, decreased urine protein, increased SIRT1, LC3-II, and Beclin-1 expression, and reduced acetylated NF-κB p65 expression in vivo. |
| 251 | 33427556 | In addition, rat serum containing Yishen capsule showed improved podocyte proliferation, promoted the mRNA and protein levels of LC3-II and Beclin-1, and induced nuclear translocation of SIRT1. |
| 252 | 33427556 | In addition, rat serum containing Yishen capsule showed improved podocyte proliferation, promoted the mRNA and protein levels of LC3-II and Beclin-1, and induced nuclear translocation of SIRT1. |
| 253 | 33359498 | Mechanistically, diabetes and HIV-1 synergistically increased the glomerular expression of microRNA-34a (miR-34a), thereby reducing the expression of Sirtuin-1 (SIRT1) deacetylase. |
| 254 | 33359498 | These changes were also associated with increased acetylation and activation of p53 and p65 NF-κB and with enhanced expression of senescence and inflammatory markers. |
| 255 | 33186558 | We further demonstrated a novel role of JAML in regulating podocyte lipid metabolism through SIRT1-mediated SREBP1 signaling. |
| 256 | 33121427 | Sirt1 exerts renoprotective effects in DKD in part through the deacetylation of transcription factors involved in the disease pathogenesis, such as NF-кB, Smad3, FOXO and p53. |
| 257 | 33116729 | Mogroside IIIE Alleviates High Glucose-Induced Inflammation, Oxidative Stress and Apoptosis of Podocytes by the Activation of AMPK/SIRT1 Signaling Pathway. |
| 258 | 33049148 | Cyanidin-3-O-glucoside attenuates high glucose-induced podocyte dysfunction by inhibiting apoptosis and promoting autophagy via activation of SIRT1/AMPK pathway. |
| 259 | 33049148 | Cyanidin-3-O-glucoside attenuates high glucose-induced podocyte dysfunction by inhibiting apoptosis and promoting autophagy via activation of SIRT1/AMPK pathway. |
| 260 | 33049148 | Cyanidin-3-O-glucoside attenuates high glucose-induced podocyte dysfunction by inhibiting apoptosis and promoting autophagy via activation of SIRT1/AMPK pathway. |
| 261 | 33049148 | MTT, flow cytometry assay, and Western blot analysis showed that C3G could reverse the increase of cell apoptosis under high glucose treatment in MPC5 cells by upregulation of Bcl2 and downregulation of Bax and cleaved caspase-3. |
| 262 | 33049148 | MTT, flow cytometry assay, and Western blot analysis showed that C3G could reverse the increase of cell apoptosis under high glucose treatment in MPC5 cells by upregulation of Bcl2 and downregulation of Bax and cleaved caspase-3. |
| 263 | 33049148 | MTT, flow cytometry assay, and Western blot analysis showed that C3G could reverse the increase of cell apoptosis under high glucose treatment in MPC5 cells by upregulation of Bcl2 and downregulation of Bax and cleaved caspase-3. |
| 264 | 33049148 | By further study of the mechanisms, we found C3G activated the SIRT1 and AMPK which were inhibited in high glucose condition. |
| 265 | 33049148 | By further study of the mechanisms, we found C3G activated the SIRT1 and AMPK which were inhibited in high glucose condition. |
| 266 | 33049148 | By further study of the mechanisms, we found C3G activated the SIRT1 and AMPK which were inhibited in high glucose condition. |
| 267 | 33049148 | In summary, our current findings suggest the protective effect of C3G against high glucose-induced podocyte dysfunction is by improving autophagy and reducing apoptosis and EMT via activating SIRT1/AMPK pathway. |
| 268 | 33049148 | In summary, our current findings suggest the protective effect of C3G against high glucose-induced podocyte dysfunction is by improving autophagy and reducing apoptosis and EMT via activating SIRT1/AMPK pathway. |
| 269 | 33049148 | In summary, our current findings suggest the protective effect of C3G against high glucose-induced podocyte dysfunction is by improving autophagy and reducing apoptosis and EMT via activating SIRT1/AMPK pathway. |
| 270 | 32887498 | We quantified urinary SIRT1 and claudin 1 (CLDN1) mRNA and miR34-a and miR-200a levels by quantitative real-time polymerase chain reaction (RT-qPCR) from patients and in cultured podocytes treated with high glucose and angiotensin II. |
| 271 | 32887498 | We quantified urinary SIRT1 and claudin 1 (CLDN1) mRNA and miR34-a and miR-200a levels by quantitative real-time polymerase chain reaction (RT-qPCR) from patients and in cultured podocytes treated with high glucose and angiotensin II. |
| 272 | 32887498 | We found decreased SIRT1 levels in patients with increased urinary albumin excretion (UAE), the lowest with diabetes presence, and a strong association with UAE, discriminating incipient renal damage. |
| 273 | 32887498 | We found decreased SIRT1 levels in patients with increased urinary albumin excretion (UAE), the lowest with diabetes presence, and a strong association with UAE, discriminating incipient renal damage. |
| 274 | 32758570 | Geniposide alleviates diabetic nephropathy of mice through AMPK/SIRT1/NF-κB pathway. |
| 275 | 32758570 | Geniposide alleviates diabetic nephropathy of mice through AMPK/SIRT1/NF-κB pathway. |
| 276 | 32758570 | Geniposide alleviates diabetic nephropathy of mice through AMPK/SIRT1/NF-κB pathway. |
| 277 | 32758570 | Geniposide alleviates diabetic nephropathy of mice through AMPK/SIRT1/NF-κB pathway. |
| 278 | 32758570 | Renal inflammation was appraised by pro-inflammatory cytokines: Tumor necrosis factor α (TNF-α), Interleukin 6 (IL-6) and IL-1β via ELISA assay. |
| 279 | 32758570 | Renal inflammation was appraised by pro-inflammatory cytokines: Tumor necrosis factor α (TNF-α), Interleukin 6 (IL-6) and IL-1β via ELISA assay. |
| 280 | 32758570 | Renal inflammation was appraised by pro-inflammatory cytokines: Tumor necrosis factor α (TNF-α), Interleukin 6 (IL-6) and IL-1β via ELISA assay. |
| 281 | 32758570 | Renal inflammation was appraised by pro-inflammatory cytokines: Tumor necrosis factor α (TNF-α), Interleukin 6 (IL-6) and IL-1β via ELISA assay. |
| 282 | 32758570 | Moreover, the related proteins p-NF-κB, ASC, Cleave-IL-1β, NLRP3, Cleave-Caspase-1 and GSDMD-N in AMPK/SIRT1/NF-κB pathway were assayed by Western blotting. |
| 283 | 32758570 | Moreover, the related proteins p-NF-κB, ASC, Cleave-IL-1β, NLRP3, Cleave-Caspase-1 and GSDMD-N in AMPK/SIRT1/NF-κB pathway were assayed by Western blotting. |
| 284 | 32758570 | Moreover, the related proteins p-NF-κB, ASC, Cleave-IL-1β, NLRP3, Cleave-Caspase-1 and GSDMD-N in AMPK/SIRT1/NF-κB pathway were assayed by Western blotting. |
| 285 | 32758570 | Moreover, the related proteins p-NF-κB, ASC, Cleave-IL-1β, NLRP3, Cleave-Caspase-1 and GSDMD-N in AMPK/SIRT1/NF-κB pathway were assayed by Western blotting. |
| 286 | 32758570 | In order to further investigate the effects of GE on podocytes, we also assessed these protein levels in AMPK/SIRT1/NF-κB pathway after siRNA-AMPK intervention by Western blotting. |
| 287 | 32758570 | In order to further investigate the effects of GE on podocytes, we also assessed these protein levels in AMPK/SIRT1/NF-κB pathway after siRNA-AMPK intervention by Western blotting. |
| 288 | 32758570 | In order to further investigate the effects of GE on podocytes, we also assessed these protein levels in AMPK/SIRT1/NF-κB pathway after siRNA-AMPK intervention by Western blotting. |
| 289 | 32758570 | In order to further investigate the effects of GE on podocytes, we also assessed these protein levels in AMPK/SIRT1/NF-κB pathway after siRNA-AMPK intervention by Western blotting. |
| 290 | 32758570 | GE alleviated renal dysfunction as evidenced by decreased levels of Scr, BUN, TNF-α, IL-6 and IL-1β. |
| 291 | 32758570 | GE alleviated renal dysfunction as evidenced by decreased levels of Scr, BUN, TNF-α, IL-6 and IL-1β. |
| 292 | 32758570 | GE alleviated renal dysfunction as evidenced by decreased levels of Scr, BUN, TNF-α, IL-6 and IL-1β. |
| 293 | 32758570 | GE alleviated renal dysfunction as evidenced by decreased levels of Scr, BUN, TNF-α, IL-6 and IL-1β. |
| 294 | 32758570 | AMPK, p-AMPK and SIRT1 levels were obviously decreased both in DN mice and in podocyte model, but GE reversed these changes. |
| 295 | 32758570 | AMPK, p-AMPK and SIRT1 levels were obviously decreased both in DN mice and in podocyte model, but GE reversed these changes. |
| 296 | 32758570 | AMPK, p-AMPK and SIRT1 levels were obviously decreased both in DN mice and in podocyte model, but GE reversed these changes. |
| 297 | 32758570 | AMPK, p-AMPK and SIRT1 levels were obviously decreased both in DN mice and in podocyte model, but GE reversed these changes. |
| 298 | 32660255 | Cdk5-Mediated Phosphorylation of Sirt1 Contributes to Podocyte Mitochondrial Dysfunction in Diabetic Nephropathy. |
| 299 | 32660255 | Cdk5-Mediated Phosphorylation of Sirt1 Contributes to Podocyte Mitochondrial Dysfunction in Diabetic Nephropathy. |
| 300 | 32660255 | Cdk5-Mediated Phosphorylation of Sirt1 Contributes to Podocyte Mitochondrial Dysfunction in Diabetic Nephropathy. |
| 301 | 32660255 | Cdk5-Mediated Phosphorylation of Sirt1 Contributes to Podocyte Mitochondrial Dysfunction in Diabetic Nephropathy. |
| 302 | 32660255 | Results: Our results showed that the expression and activity of Cdk5 were significantly upregulated in vivo and in vitro under diabetic conditions, accompanied by the downregulation of synaptopodin and nephrin, as well as structural and functional mitochondrial dysfunction. |
| 303 | 32660255 | Results: Our results showed that the expression and activity of Cdk5 were significantly upregulated in vivo and in vitro under diabetic conditions, accompanied by the downregulation of synaptopodin and nephrin, as well as structural and functional mitochondrial dysfunction. |
| 304 | 32660255 | Results: Our results showed that the expression and activity of Cdk5 were significantly upregulated in vivo and in vitro under diabetic conditions, accompanied by the downregulation of synaptopodin and nephrin, as well as structural and functional mitochondrial dysfunction. |
| 305 | 32660255 | Results: Our results showed that the expression and activity of Cdk5 were significantly upregulated in vivo and in vitro under diabetic conditions, accompanied by the downregulation of synaptopodin and nephrin, as well as structural and functional mitochondrial dysfunction. |
| 306 | 32660255 | Inhibition of Cdk5 with roscovitine or dominant-negative Cdk5 led to the attenuation of podocyte injury by upregulating synaptopodin and nephrin. |
| 307 | 32660255 | Inhibition of Cdk5 with roscovitine or dominant-negative Cdk5 led to the attenuation of podocyte injury by upregulating synaptopodin and nephrin. |
| 308 | 32660255 | Inhibition of Cdk5 with roscovitine or dominant-negative Cdk5 led to the attenuation of podocyte injury by upregulating synaptopodin and nephrin. |
| 309 | 32660255 | Inhibition of Cdk5 with roscovitine or dominant-negative Cdk5 led to the attenuation of podocyte injury by upregulating synaptopodin and nephrin. |
| 310 | 32660255 | The inhibition of Cdk5 also ameliorated mitochondrial dysfunction by decreasing reactive oxygen species levels and cytochrome c release, while increasing adenosine triphosphate production. |
| 311 | 32660255 | The inhibition of Cdk5 also ameliorated mitochondrial dysfunction by decreasing reactive oxygen species levels and cytochrome c release, while increasing adenosine triphosphate production. |
| 312 | 32660255 | The inhibition of Cdk5 also ameliorated mitochondrial dysfunction by decreasing reactive oxygen species levels and cytochrome c release, while increasing adenosine triphosphate production. |
| 313 | 32660255 | The inhibition of Cdk5 also ameliorated mitochondrial dysfunction by decreasing reactive oxygen species levels and cytochrome c release, while increasing adenosine triphosphate production. |
| 314 | 32660255 | We demonstrated that HG levels cause overactive Cdk5 to phosphorylate Sirt1 at S47. |
| 315 | 32660255 | We demonstrated that HG levels cause overactive Cdk5 to phosphorylate Sirt1 at S47. |
| 316 | 32660255 | We demonstrated that HG levels cause overactive Cdk5 to phosphorylate Sirt1 at S47. |
| 317 | 32660255 | We demonstrated that HG levels cause overactive Cdk5 to phosphorylate Sirt1 at S47. |
| 318 | 32660255 | Suppression of Cdk5 reduced Sirt1 phosphorylation levels and mutation of S47 to nonphosphorable alanine (S47A), significantly attenuated podocyte injury and mitochondrial dysfunction in diabetic condition in vivo and in vitro. |
| 319 | 32660255 | Suppression of Cdk5 reduced Sirt1 phosphorylation levels and mutation of S47 to nonphosphorable alanine (S47A), significantly attenuated podocyte injury and mitochondrial dysfunction in diabetic condition in vivo and in vitro. |
| 320 | 32660255 | Suppression of Cdk5 reduced Sirt1 phosphorylation levels and mutation of S47 to nonphosphorable alanine (S47A), significantly attenuated podocyte injury and mitochondrial dysfunction in diabetic condition in vivo and in vitro. |
| 321 | 32660255 | Suppression of Cdk5 reduced Sirt1 phosphorylation levels and mutation of S47 to nonphosphorable alanine (S47A), significantly attenuated podocyte injury and mitochondrial dysfunction in diabetic condition in vivo and in vitro. |
| 322 | 32660255 | Innovation and Conclusion: Our study has demonstrated the role of Cdk5 in regulating mitochondrial function through Sirt1 phosphorylation and thus can potentially be a new therapeutic target for DN treatment. |
| 323 | 32660255 | Innovation and Conclusion: Our study has demonstrated the role of Cdk5 in regulating mitochondrial function through Sirt1 phosphorylation and thus can potentially be a new therapeutic target for DN treatment. |
| 324 | 32660255 | Innovation and Conclusion: Our study has demonstrated the role of Cdk5 in regulating mitochondrial function through Sirt1 phosphorylation and thus can potentially be a new therapeutic target for DN treatment. |
| 325 | 32660255 | Innovation and Conclusion: Our study has demonstrated the role of Cdk5 in regulating mitochondrial function through Sirt1 phosphorylation and thus can potentially be a new therapeutic target for DN treatment. |
| 326 | 32657157 | We have previously shown that the acetylation and activation of key inflammatory regulators, NF-κB p65 and STAT3, were increased in HIVAN kidneys. |
| 327 | 32657157 | We have previously shown that the acetylation and activation of key inflammatory regulators, NF-κB p65 and STAT3, were increased in HIVAN kidneys. |
| 328 | 32657157 | We have previously shown that the acetylation and activation of key inflammatory regulators, NF-κB p65 and STAT3, were increased in HIVAN kidneys. |
| 329 | 32657157 | We have previously shown that the acetylation and activation of key inflammatory regulators, NF-κB p65 and STAT3, were increased in HIVAN kidneys. |
| 330 | 32657157 | Here, we demonstrate the key role of sirtuin 1 (SIRT1) deacetylase in the regulation of NF-κB and STAT3 activity in HIVAN. |
| 331 | 32657157 | Here, we demonstrate the key role of sirtuin 1 (SIRT1) deacetylase in the regulation of NF-κB and STAT3 activity in HIVAN. |
| 332 | 32657157 | Here, we demonstrate the key role of sirtuin 1 (SIRT1) deacetylase in the regulation of NF-κB and STAT3 activity in HIVAN. |
| 333 | 32657157 | Here, we demonstrate the key role of sirtuin 1 (SIRT1) deacetylase in the regulation of NF-κB and STAT3 activity in HIVAN. |
| 334 | 32657157 | We found that SIRT1 expression was reduced in the glomeruli of human and mouse HIVAN kidneys and that HIV-1 gene expression was associated with reduced SIRT1 expression and increased acetylation of NF-κB p65 and STAT3 in cultured podocytes. |
| 335 | 32657157 | We found that SIRT1 expression was reduced in the glomeruli of human and mouse HIVAN kidneys and that HIV-1 gene expression was associated with reduced SIRT1 expression and increased acetylation of NF-κB p65 and STAT3 in cultured podocytes. |
| 336 | 32657157 | We found that SIRT1 expression was reduced in the glomeruli of human and mouse HIVAN kidneys and that HIV-1 gene expression was associated with reduced SIRT1 expression and increased acetylation of NF-κB p65 and STAT3 in cultured podocytes. |
| 337 | 32657157 | We found that SIRT1 expression was reduced in the glomeruli of human and mouse HIVAN kidneys and that HIV-1 gene expression was associated with reduced SIRT1 expression and increased acetylation of NF-κB p65 and STAT3 in cultured podocytes. |
| 338 | 32657157 | Finally, we showed that the reduction in SIRT1 expression by HIV-1 is in part mediated through miR-34a expression. |
| 339 | 32657157 | Finally, we showed that the reduction in SIRT1 expression by HIV-1 is in part mediated through miR-34a expression. |
| 340 | 32657157 | Finally, we showed that the reduction in SIRT1 expression by HIV-1 is in part mediated through miR-34a expression. |
| 341 | 32657157 | Finally, we showed that the reduction in SIRT1 expression by HIV-1 is in part mediated through miR-34a expression. |
| 342 | 32657157 | Together, our data provide a new mechanism of SIRT1 regulation and its downstream effects in HIV-1-infected kidney cells and indicate that SIRT1/miR-34a are potential drug targets to treat HIV-related kidney disease. |
| 343 | 32657157 | Together, our data provide a new mechanism of SIRT1 regulation and its downstream effects in HIV-1-infected kidney cells and indicate that SIRT1/miR-34a are potential drug targets to treat HIV-related kidney disease. |
| 344 | 32657157 | Together, our data provide a new mechanism of SIRT1 regulation and its downstream effects in HIV-1-infected kidney cells and indicate that SIRT1/miR-34a are potential drug targets to treat HIV-related kidney disease. |
| 345 | 32657157 | Together, our data provide a new mechanism of SIRT1 regulation and its downstream effects in HIV-1-infected kidney cells and indicate that SIRT1/miR-34a are potential drug targets to treat HIV-related kidney disease. |
| 346 | 32604897 | High-glucose stress initiated stress response by increasing intracellular heat shock protein 70 (Hsp70), sirtuin-1 (Sirt-1), thioredoxin (Trx), glutamate-cysteine ligase (gamma-glutamyl cysteine synthetase; γ-GCS) and heme oxygenase-1 (HO-1) in podocytes by 30-50% compared to untreated cells. |
| 347 | 32604897 | High-glucose stress initiated stress response by increasing intracellular heat shock protein 70 (Hsp70), sirtuin-1 (Sirt-1), thioredoxin (Trx), glutamate-cysteine ligase (gamma-glutamyl cysteine synthetase; γ-GCS) and heme oxygenase-1 (HO-1) in podocytes by 30-50% compared to untreated cells. |
| 348 | 32604897 | High-glucose stress initiated stress response by increasing intracellular heat shock protein 70 (Hsp70), sirtuin-1 (Sirt-1), thioredoxin (Trx), glutamate-cysteine ligase (gamma-glutamyl cysteine synthetase; γ-GCS) and heme oxygenase-1 (HO-1) in podocytes by 30-50% compared to untreated cells. |
| 349 | 32604897 | Carnosine (1 mM) also induced a corresponding upregulation of these intracellular stress markers, which was even more prominent compared to glucose for Hsp70 (21%), γ-GCS and HO-1 (13% and 20%, respectively; all p < 0.001). |
| 350 | 32604897 | Carnosine (1 mM) also induced a corresponding upregulation of these intracellular stress markers, which was even more prominent compared to glucose for Hsp70 (21%), γ-GCS and HO-1 (13% and 20%, respectively; all p < 0.001). |
| 351 | 32604897 | Carnosine (1 mM) also induced a corresponding upregulation of these intracellular stress markers, which was even more prominent compared to glucose for Hsp70 (21%), γ-GCS and HO-1 (13% and 20%, respectively; all p < 0.001). |
| 352 | 32604897 | Co-incubation of carnosine (1 mM) and glucose (25 mM) induced further upregulation of Hsp70 (84%), Sirt-1 (52%), Trx (35%), γ-GCS (90%) and HO-1 (73%) concentrations compared to untreated cells (all p < 0.001). |
| 353 | 32604897 | Co-incubation of carnosine (1 mM) and glucose (25 mM) induced further upregulation of Hsp70 (84%), Sirt-1 (52%), Trx (35%), γ-GCS (90%) and HO-1 (73%) concentrations compared to untreated cells (all p < 0.001). |
| 354 | 32604897 | Co-incubation of carnosine (1 mM) and glucose (25 mM) induced further upregulation of Hsp70 (84%), Sirt-1 (52%), Trx (35%), γ-GCS (90%) and HO-1 (73%) concentrations compared to untreated cells (all p < 0.001). |
| 355 | 32604897 | Although podocytes tolerated high carnosine concentrations (10 mM), high carnosine levels only slightly increased Trx and γ-GCS (10% and 19%, respectively, compared to controls; p < 0.001), but not Hsp70, Sirt-1 and HO-1 proteins (p not significant), and did not modify the glucose-induced oxidative stress response. |
| 356 | 32604897 | Although podocytes tolerated high carnosine concentrations (10 mM), high carnosine levels only slightly increased Trx and γ-GCS (10% and 19%, respectively, compared to controls; p < 0.001), but not Hsp70, Sirt-1 and HO-1 proteins (p not significant), and did not modify the glucose-induced oxidative stress response. |
| 357 | 32604897 | Although podocytes tolerated high carnosine concentrations (10 mM), high carnosine levels only slightly increased Trx and γ-GCS (10% and 19%, respectively, compared to controls; p < 0.001), but not Hsp70, Sirt-1 and HO-1 proteins (p not significant), and did not modify the glucose-induced oxidative stress response. |
| 358 | 32328877 | We found that LXR activation could inhibit autophagic flux through blocking the formation of autophagosome in podocytes in vitro which was possibly achieved by affecting AMPK, mTOR, and SIRT1 signaling pathways. |
| 359 | 32276962 | The primary drivers of autophagy in states of nutrient and oxygen deprivation-sirtuin-1 (SIRT1), AMP-activated protein kinase (AMPK), and hypoxia-inducible factors (HIF-1α and HIF-2α)-can exert renoprotective effects by promoting autophagic flux and by exerting direct effects on sodium transport and inflammasome activation. |
| 360 | 32276962 | The primary drivers of autophagy in states of nutrient and oxygen deprivation-sirtuin-1 (SIRT1), AMP-activated protein kinase (AMPK), and hypoxia-inducible factors (HIF-1α and HIF-2α)-can exert renoprotective effects by promoting autophagic flux and by exerting direct effects on sodium transport and inflammasome activation. |
| 361 | 32276962 | The primary drivers of autophagy in states of nutrient and oxygen deprivation-sirtuin-1 (SIRT1), AMP-activated protein kinase (AMPK), and hypoxia-inducible factors (HIF-1α and HIF-2α)-can exert renoprotective effects by promoting autophagic flux and by exerting direct effects on sodium transport and inflammasome activation. |
| 362 | 32276962 | Type 2 diabetes is characterized by marked suppression of SIRT1 and AMPK, leading to a diminution in autophagic flux in glomerular podocytes and renal tubules and markedly increasing their susceptibility to renal injury. |
| 363 | 32276962 | Type 2 diabetes is characterized by marked suppression of SIRT1 and AMPK, leading to a diminution in autophagic flux in glomerular podocytes and renal tubules and markedly increasing their susceptibility to renal injury. |
| 364 | 32276962 | Type 2 diabetes is characterized by marked suppression of SIRT1 and AMPK, leading to a diminution in autophagic flux in glomerular podocytes and renal tubules and markedly increasing their susceptibility to renal injury. |
| 365 | 32276962 | In contrast, the effects of sodium-glucose cotransporter-2 (SGLT2) inhibitors may be related primarily to enhanced SIRT1 and HIF-2α signaling; this can explain the effects of SGLT2 inhibitors to promote ketonemia and erythrocytosis and potentially underlies their actions to increase autophagy and mute inflammation in the diabetic kidney. |
| 366 | 32276962 | In contrast, the effects of sodium-glucose cotransporter-2 (SGLT2) inhibitors may be related primarily to enhanced SIRT1 and HIF-2α signaling; this can explain the effects of SGLT2 inhibitors to promote ketonemia and erythrocytosis and potentially underlies their actions to increase autophagy and mute inflammation in the diabetic kidney. |
| 367 | 32276962 | In contrast, the effects of sodium-glucose cotransporter-2 (SGLT2) inhibitors may be related primarily to enhanced SIRT1 and HIF-2α signaling; this can explain the effects of SGLT2 inhibitors to promote ketonemia and erythrocytosis and potentially underlies their actions to increase autophagy and mute inflammation in the diabetic kidney. |
| 368 | 32172502 | In addition, the expression of COXIV and cytochrome c was significantly downregulated in the Se-deficient group. |
| 369 | 32172502 | In addition, the expression of COXIV and cytochrome c was significantly downregulated in the Se-deficient group. |
| 370 | 32172502 | Importantly, the mRNA levels of silent mating type information regulation 2 homolog 1 (SIRT1) and peroxisome proliferator-activated receptor gamma coactivator 1-alpha (PGC-1α) and the protein levels of SIRT1 were increased in the Se-deficient group compared with the normal control group. |
| 371 | 32172502 | Importantly, the mRNA levels of silent mating type information regulation 2 homolog 1 (SIRT1) and peroxisome proliferator-activated receptor gamma coactivator 1-alpha (PGC-1α) and the protein levels of SIRT1 were increased in the Se-deficient group compared with the normal control group. |
| 372 | 32172502 | Moreover, the SIRT1/PGC1α axis likely plays an important role in the compensatory mechanism of mitochondrial dysfunction. |
| 373 | 32172502 | Moreover, the SIRT1/PGC1α axis likely plays an important role in the compensatory mechanism of mitochondrial dysfunction. |
| 374 | 32116781 | We found that expression of heme oxygenase 1 (HMOX-1) and Sirt1 was suppressed in diabetic glomeruli but restored by puerarin treatment at both mRNA and protein levels. |
| 375 | 32116781 | We found that expression of heme oxygenase 1 (HMOX-1) and Sirt1 was suppressed in diabetic glomeruli but restored by puerarin treatment at both mRNA and protein levels. |
| 376 | 32116781 | We found that expression of heme oxygenase 1 (HMOX-1) and Sirt1 was suppressed in diabetic glomeruli but restored by puerarin treatment at both mRNA and protein levels. |
| 377 | 32116781 | In conditionally immortalized mouse podocytes, puerarin inhibited HG-induced apoptosis and restored the mRNA and protein levels of HMOX-1 and Sirt1. |
| 378 | 32116781 | In conditionally immortalized mouse podocytes, puerarin inhibited HG-induced apoptosis and restored the mRNA and protein levels of HMOX-1 and Sirt1. |
| 379 | 32116781 | In conditionally immortalized mouse podocytes, puerarin inhibited HG-induced apoptosis and restored the mRNA and protein levels of HMOX-1 and Sirt1. |
| 380 | 32116781 | Knockdown of HMOX-1 and Sirt1 expression or treatment with the autophagy inhibitor 3-methyladenine abolished the protective effects of puerarin in HG-treated podocytes. |
| 381 | 32116781 | Knockdown of HMOX-1 and Sirt1 expression or treatment with the autophagy inhibitor 3-methyladenine abolished the protective effects of puerarin in HG-treated podocytes. |
| 382 | 32116781 | Knockdown of HMOX-1 and Sirt1 expression or treatment with the autophagy inhibitor 3-methyladenine abolished the protective effects of puerarin in HG-treated podocytes. |
| 383 | 32000560 | Cabin1 involves in renal tubular epithelial cells mitochondrial dysfunction through SIRT1/p53 pathway. |
| 384 | 32000560 | Cabin1 involves in renal tubular epithelial cells mitochondrial dysfunction through SIRT1/p53 pathway. |
| 385 | 32000560 | Cabin1 involves in renal tubular epithelial cells mitochondrial dysfunction through SIRT1/p53 pathway. |
| 386 | 32000560 | Cabin1 involves in renal tubular epithelial cells mitochondrial dysfunction through SIRT1/p53 pathway. |
| 387 | 32000560 | In comparison with control, Cabin1, p53 and cyto C level were significantly increased in AngII treated cells, while SIRT1 level was obviously decreased. |
| 388 | 32000560 | In comparison with control, Cabin1, p53 and cyto C level were significantly increased in AngII treated cells, while SIRT1 level was obviously decreased. |
| 389 | 32000560 | In comparison with control, Cabin1, p53 and cyto C level were significantly increased in AngII treated cells, while SIRT1 level was obviously decreased. |
| 390 | 32000560 | In comparison with control, Cabin1, p53 and cyto C level were significantly increased in AngII treated cells, while SIRT1 level was obviously decreased. |
| 391 | 32000560 | Knocked down Cabin1 plus AngII stimulated, SIRT1 was further decreased, while p53 and cyto C were significantly increased. |
| 392 | 32000560 | Knocked down Cabin1 plus AngII stimulated, SIRT1 was further decreased, while p53 and cyto C were significantly increased. |
| 393 | 32000560 | Knocked down Cabin1 plus AngII stimulated, SIRT1 was further decreased, while p53 and cyto C were significantly increased. |
| 394 | 32000560 | Knocked down Cabin1 plus AngII stimulated, SIRT1 was further decreased, while p53 and cyto C were significantly increased. |
| 395 | 32000560 | Conclusions: Cabin1 involves in RTEC mitochondrial dysfunction through SIRT1/p53 pathway. |
| 396 | 32000560 | Conclusions: Cabin1 involves in RTEC mitochondrial dysfunction through SIRT1/p53 pathway. |
| 397 | 32000560 | Conclusions: Cabin1 involves in RTEC mitochondrial dysfunction through SIRT1/p53 pathway. |
| 398 | 32000560 | Conclusions: Cabin1 involves in RTEC mitochondrial dysfunction through SIRT1/p53 pathway. |
| 399 | 31321239 | In elafibranor-treated HFD mice, increased insulin sensitivity, reduced obesity and body fat mass, decreased severity of steatohepatitis, increased renal expression of PPARα, PPARδ, SIRT1, and autophagy (Beclin-1 and LC3-II) as well as glomerular/renal tubular barrier markers [synaptopodin (podocyte marker), zona occludin-1, and cubulin], reduced renal oxidative stress and caspase-3, and less urinary 8-isoprostanes excretion were observed. |
| 400 | 31321239 | In elafibranor-treated HFD mice, increased insulin sensitivity, reduced obesity and body fat mass, decreased severity of steatohepatitis, increased renal expression of PPARα, PPARδ, SIRT1, and autophagy (Beclin-1 and LC3-II) as well as glomerular/renal tubular barrier markers [synaptopodin (podocyte marker), zona occludin-1, and cubulin], reduced renal oxidative stress and caspase-3, and less urinary 8-isoprostanes excretion were observed. |
| 401 | 31321239 | In elafibranor-treated HFD mice, increased insulin sensitivity, reduced obesity and body fat mass, decreased severity of steatohepatitis, increased renal expression of PPARα, PPARδ, SIRT1, and autophagy (Beclin-1 and LC3-II) as well as glomerular/renal tubular barrier markers [synaptopodin (podocyte marker), zona occludin-1, and cubulin], reduced renal oxidative stress and caspase-3, and less urinary 8-isoprostanes excretion were observed. |
| 402 | 31321239 | Acute incubation of podocytes and HK-2 cells with elafibranor or recombinant SIRT1 reversed the HFD-sera-induced oxidative stress, autophagy dysfunction, cell apoptosis, barrier marker loss, albumin endocytosis, and reuptake reduction. |
| 403 | 31321239 | Acute incubation of podocytes and HK-2 cells with elafibranor or recombinant SIRT1 reversed the HFD-sera-induced oxidative stress, autophagy dysfunction, cell apoptosis, barrier marker loss, albumin endocytosis, and reuptake reduction. |
| 404 | 31321239 | Acute incubation of podocytes and HK-2 cells with elafibranor or recombinant SIRT1 reversed the HFD-sera-induced oxidative stress, autophagy dysfunction, cell apoptosis, barrier marker loss, albumin endocytosis, and reuptake reduction. |
| 405 | 31321239 | Besides hepatoprotective and metabolic beneficial effects, current study showed that elafibranor inhibited the progression of HFD-induced CKD through activation of renal PPARα, PPARδ, SIRT1, autophagy, reduction of oxidative stress, and apoptosis in mice with steatohepatitis. |
| 406 | 31321239 | Besides hepatoprotective and metabolic beneficial effects, current study showed that elafibranor inhibited the progression of HFD-induced CKD through activation of renal PPARα, PPARδ, SIRT1, autophagy, reduction of oxidative stress, and apoptosis in mice with steatohepatitis. |
| 407 | 31321239 | Besides hepatoprotective and metabolic beneficial effects, current study showed that elafibranor inhibited the progression of HFD-induced CKD through activation of renal PPARα, PPARδ, SIRT1, autophagy, reduction of oxidative stress, and apoptosis in mice with steatohepatitis. |
| 408 | 31301307 | LncRNA SOX2OT alleviates the high glucose-induced podocytes injury through autophagy induction by the miR-9/SIRT1 axis. |
| 409 | 30765684 | Resveratrol Reduces Oxidative Stress and Apoptosis in Podocytes via Sir2-Related Enzymes, Sirtuins1 (SIRT1)/Peroxisome Proliferator-Activated Receptor γ Co-Activator 1α (PGC-1α) Axis. |
| 410 | 30765684 | Resveratrol Reduces Oxidative Stress and Apoptosis in Podocytes via Sir2-Related Enzymes, Sirtuins1 (SIRT1)/Peroxisome Proliferator-Activated Receptor γ Co-Activator 1α (PGC-1α) Axis. |
| 411 | 30765684 | Resveratrol Reduces Oxidative Stress and Apoptosis in Podocytes via Sir2-Related Enzymes, Sirtuins1 (SIRT1)/Peroxisome Proliferator-Activated Receptor γ Co-Activator 1α (PGC-1α) Axis. |
| 412 | 30765684 | Resveratrol Reduces Oxidative Stress and Apoptosis in Podocytes via Sir2-Related Enzymes, Sirtuins1 (SIRT1)/Peroxisome Proliferator-Activated Receptor γ Co-Activator 1α (PGC-1α) Axis. |
| 413 | 30765684 | Resveratrol Reduces Oxidative Stress and Apoptosis in Podocytes via Sir2-Related Enzymes, Sirtuins1 (SIRT1)/Peroxisome Proliferator-Activated Receptor γ Co-Activator 1α (PGC-1α) Axis. |
| 414 | 30765684 | Resveratrol Reduces Oxidative Stress and Apoptosis in Podocytes via Sir2-Related Enzymes, Sirtuins1 (SIRT1)/Peroxisome Proliferator-Activated Receptor γ Co-Activator 1α (PGC-1α) Axis. |
| 415 | 30765684 | BACKGROUND PGC-1α can be activated by deacetylation reactions catalyzed by SIRT1. |
| 416 | 30765684 | BACKGROUND PGC-1α can be activated by deacetylation reactions catalyzed by SIRT1. |
| 417 | 30765684 | BACKGROUND PGC-1α can be activated by deacetylation reactions catalyzed by SIRT1. |
| 418 | 30765684 | BACKGROUND PGC-1α can be activated by deacetylation reactions catalyzed by SIRT1. |
| 419 | 30765684 | BACKGROUND PGC-1α can be activated by deacetylation reactions catalyzed by SIRT1. |
| 420 | 30765684 | BACKGROUND PGC-1α can be activated by deacetylation reactions catalyzed by SIRT1. |
| 421 | 30765684 | However, it is unknown whether the renal-protective effect of resveratrol is further related to activation of the podocyte SIRT1/PGC-1α pathway. |
| 422 | 30765684 | However, it is unknown whether the renal-protective effect of resveratrol is further related to activation of the podocyte SIRT1/PGC-1α pathway. |
| 423 | 30765684 | However, it is unknown whether the renal-protective effect of resveratrol is further related to activation of the podocyte SIRT1/PGC-1α pathway. |
| 424 | 30765684 | However, it is unknown whether the renal-protective effect of resveratrol is further related to activation of the podocyte SIRT1/PGC-1α pathway. |
| 425 | 30765684 | However, it is unknown whether the renal-protective effect of resveratrol is further related to activation of the podocyte SIRT1/PGC-1α pathway. |
| 426 | 30765684 | However, it is unknown whether the renal-protective effect of resveratrol is further related to activation of the podocyte SIRT1/PGC-1α pathway. |
| 427 | 30765684 | The protein and mRNA expression levels of SIRT1, PGC-1α, NRF1, and TFAM were detect by immunofluorescence, Western blot analysis, and qRT-PCR in the podocytes, respectively. |
| 428 | 30765684 | The protein and mRNA expression levels of SIRT1, PGC-1α, NRF1, and TFAM were detect by immunofluorescence, Western blot analysis, and qRT-PCR in the podocytes, respectively. |
| 429 | 30765684 | The protein and mRNA expression levels of SIRT1, PGC-1α, NRF1, and TFAM were detect by immunofluorescence, Western blot analysis, and qRT-PCR in the podocytes, respectively. |
| 430 | 30765684 | The protein and mRNA expression levels of SIRT1, PGC-1α, NRF1, and TFAM were detect by immunofluorescence, Western blot analysis, and qRT-PCR in the podocytes, respectively. |
| 431 | 30765684 | The protein and mRNA expression levels of SIRT1, PGC-1α, NRF1, and TFAM were detect by immunofluorescence, Western blot analysis, and qRT-PCR in the podocytes, respectively. |
| 432 | 30765684 | The protein and mRNA expression levels of SIRT1, PGC-1α, NRF1, and TFAM were detect by immunofluorescence, Western blot analysis, and qRT-PCR in the podocytes, respectively. |
| 433 | 30765684 | RESULTS We found that high-glucose stimulation results in time-dependent decreases in the expression of SIRT1, PGC-1α, and its downstream genes NRF1 and mitochondrial transcription factor A (TFAM) for mouse podocytes, and increases ROS levels in cells and mitochondria. |
| 434 | 30765684 | RESULTS We found that high-glucose stimulation results in time-dependent decreases in the expression of SIRT1, PGC-1α, and its downstream genes NRF1 and mitochondrial transcription factor A (TFAM) for mouse podocytes, and increases ROS levels in cells and mitochondria. |
| 435 | 30765684 | RESULTS We found that high-glucose stimulation results in time-dependent decreases in the expression of SIRT1, PGC-1α, and its downstream genes NRF1 and mitochondrial transcription factor A (TFAM) for mouse podocytes, and increases ROS levels in cells and mitochondria. |
| 436 | 30765684 | RESULTS We found that high-glucose stimulation results in time-dependent decreases in the expression of SIRT1, PGC-1α, and its downstream genes NRF1 and mitochondrial transcription factor A (TFAM) for mouse podocytes, and increases ROS levels in cells and mitochondria. |
| 437 | 30765684 | RESULTS We found that high-glucose stimulation results in time-dependent decreases in the expression of SIRT1, PGC-1α, and its downstream genes NRF1 and mitochondrial transcription factor A (TFAM) for mouse podocytes, and increases ROS levels in cells and mitochondria. |
| 438 | 30765684 | RESULTS We found that high-glucose stimulation results in time-dependent decreases in the expression of SIRT1, PGC-1α, and its downstream genes NRF1 and mitochondrial transcription factor A (TFAM) for mouse podocytes, and increases ROS levels in cells and mitochondria. |
| 439 | 30765684 | In addition, it can also reduce the release of mitochondrial cytochrome C and DIABLO proteins to the cytoplasm and increase respiratory chain complex I and III activity and mitochondrial membrane potential. |
| 440 | 30765684 | In addition, it can also reduce the release of mitochondrial cytochrome C and DIABLO proteins to the cytoplasm and increase respiratory chain complex I and III activity and mitochondrial membrane potential. |
| 441 | 30765684 | In addition, it can also reduce the release of mitochondrial cytochrome C and DIABLO proteins to the cytoplasm and increase respiratory chain complex I and III activity and mitochondrial membrane potential. |
| 442 | 30765684 | In addition, it can also reduce the release of mitochondrial cytochrome C and DIABLO proteins to the cytoplasm and increase respiratory chain complex I and III activity and mitochondrial membrane potential. |
| 443 | 30765684 | In addition, it can also reduce the release of mitochondrial cytochrome C and DIABLO proteins to the cytoplasm and increase respiratory chain complex I and III activity and mitochondrial membrane potential. |
| 444 | 30765684 | In addition, it can also reduce the release of mitochondrial cytochrome C and DIABLO proteins to the cytoplasm and increase respiratory chain complex I and III activity and mitochondrial membrane potential. |
| 445 | 30765684 | CONCLUSIONS Resveratrol can reduce the oxidative damage and apoptosis of podocytes induced by high-glucose stimulation via SIRT1/PGC-1α-mediated mitochondrial protection. |
| 446 | 30765684 | CONCLUSIONS Resveratrol can reduce the oxidative damage and apoptosis of podocytes induced by high-glucose stimulation via SIRT1/PGC-1α-mediated mitochondrial protection. |
| 447 | 30765684 | CONCLUSIONS Resveratrol can reduce the oxidative damage and apoptosis of podocytes induced by high-glucose stimulation via SIRT1/PGC-1α-mediated mitochondrial protection. |
| 448 | 30765684 | CONCLUSIONS Resveratrol can reduce the oxidative damage and apoptosis of podocytes induced by high-glucose stimulation via SIRT1/PGC-1α-mediated mitochondrial protection. |
| 449 | 30765684 | CONCLUSIONS Resveratrol can reduce the oxidative damage and apoptosis of podocytes induced by high-glucose stimulation via SIRT1/PGC-1α-mediated mitochondrial protection. |
| 450 | 30765684 | CONCLUSIONS Resveratrol can reduce the oxidative damage and apoptosis of podocytes induced by high-glucose stimulation via SIRT1/PGC-1α-mediated mitochondrial protection. |
| 451 | 30707256 | Increasing amounts of evidence show that silent information regulator 2 homolog 1 (sirtuin-1), a nicotinamide adenine dinucleotide (NAD+)-dependent protein deacetylase, plays a crucial role in the pathogenesis and development of DN. |
| 452 | 30707256 | Increasing amounts of evidence show that silent information regulator 2 homolog 1 (sirtuin-1), a nicotinamide adenine dinucleotide (NAD+)-dependent protein deacetylase, plays a crucial role in the pathogenesis and development of DN. |
| 453 | 30707256 | Mechanistically, sirtuin-1 has its renoprotective effects by modulating metabolic homeostasis and autophagy, resisting apoptosis and oxidative stress, and inhibiting inflammation through deacetylation of histones and the transcription factors p53, forkhead box group O, nuclear factor-κB, hypoxia-inducible factor-1α, and others. |
| 454 | 30707256 | Mechanistically, sirtuin-1 has its renoprotective effects by modulating metabolic homeostasis and autophagy, resisting apoptosis and oxidative stress, and inhibiting inflammation through deacetylation of histones and the transcription factors p53, forkhead box group O, nuclear factor-κB, hypoxia-inducible factor-1α, and others. |
| 455 | 30668374 | Salidroside stimulates the Sirt1/PGC-1α axis and ameliorates diabetic nephropathy in mice. |
| 456 | 30187480 | Resveratrol ameliorates podocyte damage in diabetic mice via SIRT1/PGC-1α mediated attenuation of mitochondrial oxidative stress. |
| 457 | 30187480 | Resveratrol ameliorates podocyte damage in diabetic mice via SIRT1/PGC-1α mediated attenuation of mitochondrial oxidative stress. |
| 458 | 30187480 | Resveratrol ameliorates podocyte damage in diabetic mice via SIRT1/PGC-1α mediated attenuation of mitochondrial oxidative stress. |
| 459 | 30187480 | Mitochondrial biosynthesis mediated by coactivator PGC-1α and its downstream transcription factors NRF1 and TFAM may be a key target in maintaining mitochondrial function. |
| 460 | 30187480 | Mitochondrial biosynthesis mediated by coactivator PGC-1α and its downstream transcription factors NRF1 and TFAM may be a key target in maintaining mitochondrial function. |
| 461 | 30187480 | Mitochondrial biosynthesis mediated by coactivator PGC-1α and its downstream transcription factors NRF1 and TFAM may be a key target in maintaining mitochondrial function. |
| 462 | 30187480 | We found that RESV alleviated proteinuria of diabetic mice, decreased malondialdehyde content while increased Mn-SOD activity in renal cortex, inhibited the apoptosis of glomerular podocytes and renal tubular epithelial cells, ameliorated pathological manifestations, and restored the expression of SIRT1 and PGC-1α in renal tissues of DN mice. |
| 463 | 30187480 | We found that RESV alleviated proteinuria of diabetic mice, decreased malondialdehyde content while increased Mn-SOD activity in renal cortex, inhibited the apoptosis of glomerular podocytes and renal tubular epithelial cells, ameliorated pathological manifestations, and restored the expression of SIRT1 and PGC-1α in renal tissues of DN mice. |
| 464 | 30187480 | We found that RESV alleviated proteinuria of diabetic mice, decreased malondialdehyde content while increased Mn-SOD activity in renal cortex, inhibited the apoptosis of glomerular podocytes and renal tubular epithelial cells, ameliorated pathological manifestations, and restored the expression of SIRT1 and PGC-1α in renal tissues of DN mice. |
| 465 | 30187480 | Taken together, our findings suggest that RESV ameliorates podocyte damage in diabetic mice via SIRT1/PGC-1α mediated attenuation of mitochondrial oxidative stress. |
| 466 | 30187480 | Taken together, our findings suggest that RESV ameliorates podocyte damage in diabetic mice via SIRT1/PGC-1α mediated attenuation of mitochondrial oxidative stress. |
| 467 | 30187480 | Taken together, our findings suggest that RESV ameliorates podocyte damage in diabetic mice via SIRT1/PGC-1α mediated attenuation of mitochondrial oxidative stress. |
| 468 | 29845208 | Notably, treatment with GLP‑1 attenuated HG‑induced increases in ROS production and podocyte apoptosis, which may occur via downregulation of the expression of caspase‑3 and caspase‑9, and increased expression of nephrin, podocin and SIRT1, as determined by reverse transcription‑quantitative polymerase chain reaction and western blot analysis. |
| 469 | 29608912 | In addition, histological, western blot and PCR analysis of the Tg26 mice kidneys showed a downregulation of NAMPT, SIRT1, and SIRT3 expressions levels. |
| 470 | 29593530 | However, it is not clear that whether p53-induced mitochondrial fission is critical for hypertensive Angiotensin II (AngII)-induced cardiomyocyte apoptosis. |
| 471 | 29593530 | However, it is not clear that whether p53-induced mitochondrial fission is critical for hypertensive Angiotensin II (AngII)-induced cardiomyocyte apoptosis. |
| 472 | 29593530 | However, it is not clear that whether p53-induced mitochondrial fission is critical for hypertensive Angiotensin II (AngII)-induced cardiomyocyte apoptosis. |
| 473 | 29593530 | In this study, we found that inhibition of the mitochondrial fission protein Drp1 (dynamin-related protein 1) by Mdivi-1 prevented cardiomyocyte apoptosis and cardiac remodeling in SHRs. |
| 474 | 29593530 | In this study, we found that inhibition of the mitochondrial fission protein Drp1 (dynamin-related protein 1) by Mdivi-1 prevented cardiomyocyte apoptosis and cardiac remodeling in SHRs. |
| 475 | 29593530 | In this study, we found that inhibition of the mitochondrial fission protein Drp1 (dynamin-related protein 1) by Mdivi-1 prevented cardiomyocyte apoptosis and cardiac remodeling in SHRs. |
| 476 | 29593530 | In vitro we found that treatment of cultured neonatal rat cardiomyocytes with AngII induced Drp1 expression, mitochondrial fission, and apoptosis. |
| 477 | 29593530 | In vitro we found that treatment of cultured neonatal rat cardiomyocytes with AngII induced Drp1 expression, mitochondrial fission, and apoptosis. |
| 478 | 29593530 | In vitro we found that treatment of cultured neonatal rat cardiomyocytes with AngII induced Drp1 expression, mitochondrial fission, and apoptosis. |
| 479 | 29593530 | Knockdown of Drp1 inhibited AngII-induced mitochondrial fission and cardiomyocyte apoptosis. |
| 480 | 29593530 | Knockdown of Drp1 inhibited AngII-induced mitochondrial fission and cardiomyocyte apoptosis. |
| 481 | 29593530 | Knockdown of Drp1 inhibited AngII-induced mitochondrial fission and cardiomyocyte apoptosis. |
| 482 | 29593530 | Furthermore, AngII induced p53 acetylation. |
| 483 | 29593530 | Furthermore, AngII induced p53 acetylation. |
| 484 | 29593530 | Furthermore, AngII induced p53 acetylation. |
| 485 | 29593530 | Knockdown of p53 inhibited AngII-induced Drp1 expression, mitochondrial fission, and cardiomyocyte apoptosis. |
| 486 | 29593530 | Knockdown of p53 inhibited AngII-induced Drp1 expression, mitochondrial fission, and cardiomyocyte apoptosis. |
| 487 | 29593530 | Knockdown of p53 inhibited AngII-induced Drp1 expression, mitochondrial fission, and cardiomyocyte apoptosis. |
| 488 | 29593530 | Besides, we found that Sirt1 was able to reverse AngII-induced p53 acetylation and its binding to the Drp1 promoter, which subsequently inhibited mitochondrial fission and eventually attenuated cardiomyocyte apoptosis. |
| 489 | 29593530 | Besides, we found that Sirt1 was able to reverse AngII-induced p53 acetylation and its binding to the Drp1 promoter, which subsequently inhibited mitochondrial fission and eventually attenuated cardiomyocyte apoptosis. |
| 490 | 29593530 | Besides, we found that Sirt1 was able to reverse AngII-induced p53 acetylation and its binding to the Drp1 promoter, which subsequently inhibited mitochondrial fission and eventually attenuated cardiomyocyte apoptosis. |
| 491 | 29593530 | Collectively, these results suggest that AngII degrades Sirt1 to increase p53 acetylation, which induces Drp1 expression and eventually results in cardiomyocyte apoptosis. |
| 492 | 29593530 | Collectively, these results suggest that AngII degrades Sirt1 to increase p53 acetylation, which induces Drp1 expression and eventually results in cardiomyocyte apoptosis. |
| 493 | 29593530 | Collectively, these results suggest that AngII degrades Sirt1 to increase p53 acetylation, which induces Drp1 expression and eventually results in cardiomyocyte apoptosis. |
| 494 | 29593530 | Sirt1/p53/Drp1dependent mitochondrial fission may be a valuable therapeutic target for hypertension induced heart failure. |
| 495 | 29593530 | Sirt1/p53/Drp1dependent mitochondrial fission may be a valuable therapeutic target for hypertension induced heart failure. |
| 496 | 29593530 | Sirt1/p53/Drp1dependent mitochondrial fission may be a valuable therapeutic target for hypertension induced heart failure. |
| 497 | 29477240 | SIRT1 encodes an NAD-dependent deacetylase that modifies the activity of key transcriptional regulators affected in diabetic kidneys, including NF-κB, STAT3, p53, FOXO4, and PGC1-α. |
| 498 | 29477240 | SIRT1 encodes an NAD-dependent deacetylase that modifies the activity of key transcriptional regulators affected in diabetic kidneys, including NF-κB, STAT3, p53, FOXO4, and PGC1-α. |
| 499 | 29477240 | In cultured podocytes BF175 increased SIRT1-mediated activation of PGC1-α and protected against high glucose-mediated mitochondrial injury. |
| 500 | 29477240 | In cultured podocytes BF175 increased SIRT1-mediated activation of PGC1-α and protected against high glucose-mediated mitochondrial injury. |
| 501 | 29097815 | Puerarin treatment of diabetic eNOS-/- mice significantly attenuated albuminuria and diabetic kidney injury, which were associated with reduced oxidative stress and reduced NAPDH oxidase 4 (NOX4) in glomeruli of diabetic eNOS-/- mice. |
| 502 | 29097815 | We further determined that that puerarin treatment increased both mRNA and protein levels of SIRT1 in podocytes and that puerarin led to SIRT1-mediated deacetylation of NF-κB and suppression of NOX4 expression. |
| 503 | 29089371 | FXR/TGR5 Dual Agonist Prevents Progression of Nephropathy in Diabetes and Obesity. |
| 504 | 29089371 | Bile acids are ligands for the nuclear hormone receptor farnesoid X receptor (FXR) and the G protein-coupled receptor TGR5. |
| 505 | 29089371 | We have shown that FXR and TGR5 have renoprotective roles in diabetes- and obesity-related kidney disease. |
| 506 | 29089371 | We administered the FXR/TGR5 dual agonist INT-767 to DBA/2J mice with streptozotocin-induced diabetes, db/db mice with type 2 diabetes, and C57BL/6J mice with high-fat diet-induced obesity. |
| 507 | 29089371 | We also examined the individual effects of the selective FXR agonist obeticholic acid (OCA) and the TGR5 agonist INT-777 in diabetic mice. |
| 508 | 29089371 | The FXR agonist OCA and the TGR5 agonist INT-777 modulated distinct renal signaling pathways involved in the pathogenesis and treatment of diabetic nephropathy. |
| 509 | 29089371 | Treatment of diabetic DBA/2J and db/db mice with the dual FXR/TGR5 agonist INT-767 improved proteinuria and prevented podocyte injury, mesangial expansion, and tubulointerstitial fibrosis. |
| 510 | 29089371 | INT-767 exerted coordinated effects on multiple pathways, including stimulation of a signaling cascade involving AMP-activated protein kinase, sirtuin 1, PGC-1α, sirtuin 3, estrogen-related receptor-α, and Nrf-1; inhibition of endoplasmic reticulum stress; and inhibition of enhanced renal fatty acid and cholesterol metabolism. |
| 511 | 29089371 | These results identify the renal signaling pathways regulated by FXR and TGR5, which may be promising targets for the treatment of nephropathy in diabetes and obesity. |
| 512 | 29032153 | Metformin overcomes high glucose-induced insulin resistance of podocytes by pleiotropic effects on SIRT1 and AMPK. |
| 513 | 29032153 | Metformin overcomes high glucose-induced insulin resistance of podocytes by pleiotropic effects on SIRT1 and AMPK. |
| 514 | 29032153 | Metformin overcomes high glucose-induced insulin resistance of podocytes by pleiotropic effects on SIRT1 and AMPK. |
| 515 | 29032153 | Metformin overcomes high glucose-induced insulin resistance of podocytes by pleiotropic effects on SIRT1 and AMPK. |
| 516 | 29032153 | Metformin overcomes high glucose-induced insulin resistance of podocytes by pleiotropic effects on SIRT1 and AMPK. |
| 517 | 29032153 | Metformin overcomes high glucose-induced insulin resistance of podocytes by pleiotropic effects on SIRT1 and AMPK. |
| 518 | 29032153 | Metformin overcomes high glucose-induced insulin resistance of podocytes by pleiotropic effects on SIRT1 and AMPK. |
| 519 | 29032153 | Energy-sensing pathways, such as AMP-dependent protein kinase (AMPK) and protein deacetylase SIRT1, have been shown to play an important role in insulin resistance. |
| 520 | 29032153 | Energy-sensing pathways, such as AMP-dependent protein kinase (AMPK) and protein deacetylase SIRT1, have been shown to play an important role in insulin resistance. |
| 521 | 29032153 | Energy-sensing pathways, such as AMP-dependent protein kinase (AMPK) and protein deacetylase SIRT1, have been shown to play an important role in insulin resistance. |
| 522 | 29032153 | Energy-sensing pathways, such as AMP-dependent protein kinase (AMPK) and protein deacetylase SIRT1, have been shown to play an important role in insulin resistance. |
| 523 | 29032153 | Energy-sensing pathways, such as AMP-dependent protein kinase (AMPK) and protein deacetylase SIRT1, have been shown to play an important role in insulin resistance. |
| 524 | 29032153 | Energy-sensing pathways, such as AMP-dependent protein kinase (AMPK) and protein deacetylase SIRT1, have been shown to play an important role in insulin resistance. |
| 525 | 29032153 | Energy-sensing pathways, such as AMP-dependent protein kinase (AMPK) and protein deacetylase SIRT1, have been shown to play an important role in insulin resistance. |
| 526 | 29032153 | The absence of a stimulating effect of insulin on glucose uptake into podocytes after exposure to hyperglycemic conditions has been demonstrated to be related to a decreased level and activity of SIRT1 protein, leading to reduced AMPK phosphorylation. |
| 527 | 29032153 | The absence of a stimulating effect of insulin on glucose uptake into podocytes after exposure to hyperglycemic conditions has been demonstrated to be related to a decreased level and activity of SIRT1 protein, leading to reduced AMPK phosphorylation. |
| 528 | 29032153 | The absence of a stimulating effect of insulin on glucose uptake into podocytes after exposure to hyperglycemic conditions has been demonstrated to be related to a decreased level and activity of SIRT1 protein, leading to reduced AMPK phosphorylation. |
| 529 | 29032153 | The absence of a stimulating effect of insulin on glucose uptake into podocytes after exposure to hyperglycemic conditions has been demonstrated to be related to a decreased level and activity of SIRT1 protein, leading to reduced AMPK phosphorylation. |
| 530 | 29032153 | The absence of a stimulating effect of insulin on glucose uptake into podocytes after exposure to hyperglycemic conditions has been demonstrated to be related to a decreased level and activity of SIRT1 protein, leading to reduced AMPK phosphorylation. |
| 531 | 29032153 | The absence of a stimulating effect of insulin on glucose uptake into podocytes after exposure to hyperglycemic conditions has been demonstrated to be related to a decreased level and activity of SIRT1 protein, leading to reduced AMPK phosphorylation. |
| 532 | 29032153 | The absence of a stimulating effect of insulin on glucose uptake into podocytes after exposure to hyperglycemic conditions has been demonstrated to be related to a decreased level and activity of SIRT1 protein, leading to reduced AMPK phosphorylation. |
| 533 | 29032153 | The present work was undertaken to investigate metformin's ability to restore the insulin responsiveness of podocytes by regulating SIRT1 and AMPK activities. |
| 534 | 29032153 | The present work was undertaken to investigate metformin's ability to restore the insulin responsiveness of podocytes by regulating SIRT1 and AMPK activities. |
| 535 | 29032153 | The present work was undertaken to investigate metformin's ability to restore the insulin responsiveness of podocytes by regulating SIRT1 and AMPK activities. |
| 536 | 29032153 | The present work was undertaken to investigate metformin's ability to restore the insulin responsiveness of podocytes by regulating SIRT1 and AMPK activities. |
| 537 | 29032153 | The present work was undertaken to investigate metformin's ability to restore the insulin responsiveness of podocytes by regulating SIRT1 and AMPK activities. |
| 538 | 29032153 | The present work was undertaken to investigate metformin's ability to restore the insulin responsiveness of podocytes by regulating SIRT1 and AMPK activities. |
| 539 | 29032153 | The present work was undertaken to investigate metformin's ability to restore the insulin responsiveness of podocytes by regulating SIRT1 and AMPK activities. |
| 540 | 29032153 | Our results demonstrated that metformin activated SIRT1 and AMPK, prevented hyperglycemia-induced reduction of SIRT1 protein levels, ameliorated glucose uptake into podocytes, and decreased glomerular filtration barrier permeability. |
| 541 | 29032153 | Our results demonstrated that metformin activated SIRT1 and AMPK, prevented hyperglycemia-induced reduction of SIRT1 protein levels, ameliorated glucose uptake into podocytes, and decreased glomerular filtration barrier permeability. |
| 542 | 29032153 | Our results demonstrated that metformin activated SIRT1 and AMPK, prevented hyperglycemia-induced reduction of SIRT1 protein levels, ameliorated glucose uptake into podocytes, and decreased glomerular filtration barrier permeability. |
| 543 | 29032153 | Our results demonstrated that metformin activated SIRT1 and AMPK, prevented hyperglycemia-induced reduction of SIRT1 protein levels, ameliorated glucose uptake into podocytes, and decreased glomerular filtration barrier permeability. |
| 544 | 29032153 | Our results demonstrated that metformin activated SIRT1 and AMPK, prevented hyperglycemia-induced reduction of SIRT1 protein levels, ameliorated glucose uptake into podocytes, and decreased glomerular filtration barrier permeability. |
| 545 | 29032153 | Our results demonstrated that metformin activated SIRT1 and AMPK, prevented hyperglycemia-induced reduction of SIRT1 protein levels, ameliorated glucose uptake into podocytes, and decreased glomerular filtration barrier permeability. |
| 546 | 29032153 | Our results demonstrated that metformin activated SIRT1 and AMPK, prevented hyperglycemia-induced reduction of SIRT1 protein levels, ameliorated glucose uptake into podocytes, and decreased glomerular filtration barrier permeability. |
| 547 | 29032153 | Furthermore, metformin activated AMPK in a SIRT1-independent manner, as the increase in AMPK phosphorylation after metformin treatment was not affected by SIRT1 downregulation. |
| 548 | 29032153 | Furthermore, metformin activated AMPK in a SIRT1-independent manner, as the increase in AMPK phosphorylation after metformin treatment was not affected by SIRT1 downregulation. |
| 549 | 29032153 | Furthermore, metformin activated AMPK in a SIRT1-independent manner, as the increase in AMPK phosphorylation after metformin treatment was not affected by SIRT1 downregulation. |
| 550 | 29032153 | Furthermore, metformin activated AMPK in a SIRT1-independent manner, as the increase in AMPK phosphorylation after metformin treatment was not affected by SIRT1 downregulation. |
| 551 | 29032153 | Furthermore, metformin activated AMPK in a SIRT1-independent manner, as the increase in AMPK phosphorylation after metformin treatment was not affected by SIRT1 downregulation. |
| 552 | 29032153 | Furthermore, metformin activated AMPK in a SIRT1-independent manner, as the increase in AMPK phosphorylation after metformin treatment was not affected by SIRT1 downregulation. |
| 553 | 29032153 | Furthermore, metformin activated AMPK in a SIRT1-independent manner, as the increase in AMPK phosphorylation after metformin treatment was not affected by SIRT1 downregulation. |
| 554 | 29032153 | Therefore, the potentiating effect of metformin on insulin-resistant podocytes seemed to be dependent on AMPK, as well as SIRT1 activity, establishing multilateral effects of metformin action. |
| 555 | 29032153 | Therefore, the potentiating effect of metformin on insulin-resistant podocytes seemed to be dependent on AMPK, as well as SIRT1 activity, establishing multilateral effects of metformin action. |
| 556 | 29032153 | Therefore, the potentiating effect of metformin on insulin-resistant podocytes seemed to be dependent on AMPK, as well as SIRT1 activity, establishing multilateral effects of metformin action. |
| 557 | 29032153 | Therefore, the potentiating effect of metformin on insulin-resistant podocytes seemed to be dependent on AMPK, as well as SIRT1 activity, establishing multilateral effects of metformin action. |
| 558 | 29032153 | Therefore, the potentiating effect of metformin on insulin-resistant podocytes seemed to be dependent on AMPK, as well as SIRT1 activity, establishing multilateral effects of metformin action. |
| 559 | 29032153 | Therefore, the potentiating effect of metformin on insulin-resistant podocytes seemed to be dependent on AMPK, as well as SIRT1 activity, establishing multilateral effects of metformin action. |
| 560 | 29032153 | Therefore, the potentiating effect of metformin on insulin-resistant podocytes seemed to be dependent on AMPK, as well as SIRT1 activity, establishing multilateral effects of metformin action. |
| 561 | 28615249 | Finally, we confirmed that Pod-Sirt1RNAi glomeruli were associated with reduced activation of the transcription factors peroxisome proliferator-activated receptor (PPAR)-α coactivador-1 (PGC1α)/PPARγ, forkhead box O (FOXO)3, FOXO4, and p65 NF-κB, through SIRT1-mediated deacetylation. |
| 562 | 28069388 | Vitamin D receptor deficit induces activation of renin angiotensin system via SIRT1 modulation in podocytes. |
| 563 | 28069388 | Vitamin D receptor deficit induces activation of renin angiotensin system via SIRT1 modulation in podocytes. |
| 564 | 28069388 | Vitamin D receptor deficit induces activation of renin angiotensin system via SIRT1 modulation in podocytes. |
| 565 | 28069388 | Vitamin D receptor deficit induces activation of renin angiotensin system via SIRT1 modulation in podocytes. |
| 566 | 28069388 | Vitamin D receptor deficit induces activation of renin angiotensin system via SIRT1 modulation in podocytes. |
| 567 | 28069388 | Vitamin D receptor deficit induces activation of renin angiotensin system via SIRT1 modulation in podocytes. |
| 568 | 28069388 | Vitamin D receptor deficit induces activation of renin angiotensin system via SIRT1 modulation in podocytes. |
| 569 | 28069388 | Vitamin D receptor (VDR) deficient status has been shown to be associated with the activation of renin angiotensin system (RAS). |
| 570 | 28069388 | Vitamin D receptor (VDR) deficient status has been shown to be associated with the activation of renin angiotensin system (RAS). |
| 571 | 28069388 | Vitamin D receptor (VDR) deficient status has been shown to be associated with the activation of renin angiotensin system (RAS). |
| 572 | 28069388 | Vitamin D receptor (VDR) deficient status has been shown to be associated with the activation of renin angiotensin system (RAS). |
| 573 | 28069388 | Vitamin D receptor (VDR) deficient status has been shown to be associated with the activation of renin angiotensin system (RAS). |
| 574 | 28069388 | Vitamin D receptor (VDR) deficient status has been shown to be associated with the activation of renin angiotensin system (RAS). |
| 575 | 28069388 | Vitamin D receptor (VDR) deficient status has been shown to be associated with the activation of renin angiotensin system (RAS). |
| 576 | 28069388 | We hypothesized that lack of VDR would enhance p53 expression in podocytes through down regulation of SIRT1; the former would enhance the transcription of angiotensinogen (Agt) and angiotensinogen II type 1 receptor (AT1R) leading to the activation of RAS. |
| 577 | 28069388 | We hypothesized that lack of VDR would enhance p53 expression in podocytes through down regulation of SIRT1; the former would enhance the transcription of angiotensinogen (Agt) and angiotensinogen II type 1 receptor (AT1R) leading to the activation of RAS. |
| 578 | 28069388 | We hypothesized that lack of VDR would enhance p53 expression in podocytes through down regulation of SIRT1; the former would enhance the transcription of angiotensinogen (Agt) and angiotensinogen II type 1 receptor (AT1R) leading to the activation of RAS. |
| 579 | 28069388 | We hypothesized that lack of VDR would enhance p53 expression in podocytes through down regulation of SIRT1; the former would enhance the transcription of angiotensinogen (Agt) and angiotensinogen II type 1 receptor (AT1R) leading to the activation of RAS. |
| 580 | 28069388 | We hypothesized that lack of VDR would enhance p53 expression in podocytes through down regulation of SIRT1; the former would enhance the transcription of angiotensinogen (Agt) and angiotensinogen II type 1 receptor (AT1R) leading to the activation of RAS. |
| 581 | 28069388 | We hypothesized that lack of VDR would enhance p53 expression in podocytes through down regulation of SIRT1; the former would enhance the transcription of angiotensinogen (Agt) and angiotensinogen II type 1 receptor (AT1R) leading to the activation of RAS. |
| 582 | 28069388 | We hypothesized that lack of VDR would enhance p53 expression in podocytes through down regulation of SIRT1; the former would enhance the transcription of angiotensinogen (Agt) and angiotensinogen II type 1 receptor (AT1R) leading to the activation of RAS. |
| 583 | 28069388 | Renal tissues of VDR mutant (M) mice displayed increased expression of p53, Agt, renin, and AT1R. |
| 584 | 28069388 | Renal tissues of VDR mutant (M) mice displayed increased expression of p53, Agt, renin, and AT1R. |
| 585 | 28069388 | Renal tissues of VDR mutant (M) mice displayed increased expression of p53, Agt, renin, and AT1R. |
| 586 | 28069388 | Renal tissues of VDR mutant (M) mice displayed increased expression of p53, Agt, renin, and AT1R. |
| 587 | 28069388 | Renal tissues of VDR mutant (M) mice displayed increased expression of p53, Agt, renin, and AT1R. |
| 588 | 28069388 | Renal tissues of VDR mutant (M) mice displayed increased expression of p53, Agt, renin, and AT1R. |
| 589 | 28069388 | Renal tissues of VDR mutant (M) mice displayed increased expression of p53, Agt, renin, and AT1R. |
| 590 | 28069388 | In vitro studies, VDR knockout podocytes not only displayed up regulation p53 but also displayed enhanced expression of Agt, renin and AT1R. |
| 591 | 28069388 | In vitro studies, VDR knockout podocytes not only displayed up regulation p53 but also displayed enhanced expression of Agt, renin and AT1R. |
| 592 | 28069388 | In vitro studies, VDR knockout podocytes not only displayed up regulation p53 but also displayed enhanced expression of Agt, renin and AT1R. |
| 593 | 28069388 | In vitro studies, VDR knockout podocytes not only displayed up regulation p53 but also displayed enhanced expression of Agt, renin and AT1R. |
| 594 | 28069388 | In vitro studies, VDR knockout podocytes not only displayed up regulation p53 but also displayed enhanced expression of Agt, renin and AT1R. |
| 595 | 28069388 | In vitro studies, VDR knockout podocytes not only displayed up regulation p53 but also displayed enhanced expression of Agt, renin and AT1R. |
| 596 | 28069388 | In vitro studies, VDR knockout podocytes not only displayed up regulation p53 but also displayed enhanced expression of Agt, renin and AT1R. |
| 597 | 28069388 | VDR deficient podocytes also displayed an increase in mRNA expression for p53, Agt, renin, and AT1R. |
| 598 | 28069388 | VDR deficient podocytes also displayed an increase in mRNA expression for p53, Agt, renin, and AT1R. |
| 599 | 28069388 | VDR deficient podocytes also displayed an increase in mRNA expression for p53, Agt, renin, and AT1R. |
| 600 | 28069388 | VDR deficient podocytes also displayed an increase in mRNA expression for p53, Agt, renin, and AT1R. |
| 601 | 28069388 | VDR deficient podocytes also displayed an increase in mRNA expression for p53, Agt, renin, and AT1R. |
| 602 | 28069388 | VDR deficient podocytes also displayed an increase in mRNA expression for p53, Agt, renin, and AT1R. |
| 603 | 28069388 | VDR deficient podocytes also displayed an increase in mRNA expression for p53, Agt, renin, and AT1R. |
| 604 | 28069388 | Interestingly, renal tissues of VDR-M as well as VDR heterozygous (h) mice displayed attenuated expression of deacetylase SIRT1. |
| 605 | 28069388 | Interestingly, renal tissues of VDR-M as well as VDR heterozygous (h) mice displayed attenuated expression of deacetylase SIRT1. |
| 606 | 28069388 | Interestingly, renal tissues of VDR-M as well as VDR heterozygous (h) mice displayed attenuated expression of deacetylase SIRT1. |
| 607 | 28069388 | Interestingly, renal tissues of VDR-M as well as VDR heterozygous (h) mice displayed attenuated expression of deacetylase SIRT1. |
| 608 | 28069388 | Interestingly, renal tissues of VDR-M as well as VDR heterozygous (h) mice displayed attenuated expression of deacetylase SIRT1. |
| 609 | 28069388 | Interestingly, renal tissues of VDR-M as well as VDR heterozygous (h) mice displayed attenuated expression of deacetylase SIRT1. |
| 610 | 28069388 | Interestingly, renal tissues of VDR-M as well as VDR heterozygous (h) mice displayed attenuated expression of deacetylase SIRT1. |
| 611 | 28069388 | Renal tissues of VDR-M mice showed acetylation of p53 at lysine (K) 382 residues inferring that enhanced p53 expression in renal tissues could be the result of ongoing acetylation, a consequence of SIRT1 deficient state. |
| 612 | 28069388 | Renal tissues of VDR-M mice showed acetylation of p53 at lysine (K) 382 residues inferring that enhanced p53 expression in renal tissues could be the result of ongoing acetylation, a consequence of SIRT1 deficient state. |
| 613 | 28069388 | Renal tissues of VDR-M mice showed acetylation of p53 at lysine (K) 382 residues inferring that enhanced p53 expression in renal tissues could be the result of ongoing acetylation, a consequence of SIRT1 deficient state. |
| 614 | 28069388 | Renal tissues of VDR-M mice showed acetylation of p53 at lysine (K) 382 residues inferring that enhanced p53 expression in renal tissues could be the result of ongoing acetylation, a consequence of SIRT1 deficient state. |
| 615 | 28069388 | Renal tissues of VDR-M mice showed acetylation of p53 at lysine (K) 382 residues inferring that enhanced p53 expression in renal tissues could be the result of ongoing acetylation, a consequence of SIRT1 deficient state. |
| 616 | 28069388 | Renal tissues of VDR-M mice showed acetylation of p53 at lysine (K) 382 residues inferring that enhanced p53 expression in renal tissues could be the result of ongoing acetylation, a consequence of SIRT1 deficient state. |
| 617 | 28069388 | Renal tissues of VDR-M mice showed acetylation of p53 at lysine (K) 382 residues inferring that enhanced p53 expression in renal tissues could be the result of ongoing acetylation, a consequence of SIRT1 deficient state. |
| 618 | 28069388 | Notably, podocytes lacking SIRT1 not only showed acetylation of p53 at lysine (K) 382 residues but also displayed enhanced p53 expression. |
| 619 | 28069388 | Notably, podocytes lacking SIRT1 not only showed acetylation of p53 at lysine (K) 382 residues but also displayed enhanced p53 expression. |
| 620 | 28069388 | Notably, podocytes lacking SIRT1 not only showed acetylation of p53 at lysine (K) 382 residues but also displayed enhanced p53 expression. |
| 621 | 28069388 | Notably, podocytes lacking SIRT1 not only showed acetylation of p53 at lysine (K) 382 residues but also displayed enhanced p53 expression. |
| 622 | 28069388 | Notably, podocytes lacking SIRT1 not only showed acetylation of p53 at lysine (K) 382 residues but also displayed enhanced p53 expression. |
| 623 | 28069388 | Notably, podocytes lacking SIRT1 not only showed acetylation of p53 at lysine (K) 382 residues but also displayed enhanced p53 expression. |
| 624 | 28069388 | Notably, podocytes lacking SIRT1 not only showed acetylation of p53 at lysine (K) 382 residues but also displayed enhanced p53 expression. |
| 625 | 28069388 | Either silencing of SIRT1/VDR or treatment with high glucose enhanced podocyte PPAR-y expression, whereas, immunoprecipitation (IP) of their lysates with anti-retinoid X receptor (RXR) antibody revealed presence of PPAR-y. |
| 626 | 28069388 | Either silencing of SIRT1/VDR or treatment with high glucose enhanced podocyte PPAR-y expression, whereas, immunoprecipitation (IP) of their lysates with anti-retinoid X receptor (RXR) antibody revealed presence of PPAR-y. |
| 627 | 28069388 | Either silencing of SIRT1/VDR or treatment with high glucose enhanced podocyte PPAR-y expression, whereas, immunoprecipitation (IP) of their lysates with anti-retinoid X receptor (RXR) antibody revealed presence of PPAR-y. |
| 628 | 28069388 | Either silencing of SIRT1/VDR or treatment with high glucose enhanced podocyte PPAR-y expression, whereas, immunoprecipitation (IP) of their lysates with anti-retinoid X receptor (RXR) antibody revealed presence of PPAR-y. |
| 629 | 28069388 | Either silencing of SIRT1/VDR or treatment with high glucose enhanced podocyte PPAR-y expression, whereas, immunoprecipitation (IP) of their lysates with anti-retinoid X receptor (RXR) antibody revealed presence of PPAR-y. |
| 630 | 28069388 | Either silencing of SIRT1/VDR or treatment with high glucose enhanced podocyte PPAR-y expression, whereas, immunoprecipitation (IP) of their lysates with anti-retinoid X receptor (RXR) antibody revealed presence of PPAR-y. |
| 631 | 28069388 | Either silencing of SIRT1/VDR or treatment with high glucose enhanced podocyte PPAR-y expression, whereas, immunoprecipitation (IP) of their lysates with anti-retinoid X receptor (RXR) antibody revealed presence of PPAR-y. |
| 632 | 28069388 | It appears that either the deficit of SIRT1 has de-repressed expression of PPAR-y or enhanced podocyte expression of PPAR-y (in the absence of VDR) has contributed to the down regulation of SIRT1. |
| 633 | 28069388 | It appears that either the deficit of SIRT1 has de-repressed expression of PPAR-y or enhanced podocyte expression of PPAR-y (in the absence of VDR) has contributed to the down regulation of SIRT1. |
| 634 | 28069388 | It appears that either the deficit of SIRT1 has de-repressed expression of PPAR-y or enhanced podocyte expression of PPAR-y (in the absence of VDR) has contributed to the down regulation of SIRT1. |
| 635 | 28069388 | It appears that either the deficit of SIRT1 has de-repressed expression of PPAR-y or enhanced podocyte expression of PPAR-y (in the absence of VDR) has contributed to the down regulation of SIRT1. |
| 636 | 28069388 | It appears that either the deficit of SIRT1 has de-repressed expression of PPAR-y or enhanced podocyte expression of PPAR-y (in the absence of VDR) has contributed to the down regulation of SIRT1. |
| 637 | 28069388 | It appears that either the deficit of SIRT1 has de-repressed expression of PPAR-y or enhanced podocyte expression of PPAR-y (in the absence of VDR) has contributed to the down regulation of SIRT1. |
| 638 | 28069388 | It appears that either the deficit of SIRT1 has de-repressed expression of PPAR-y or enhanced podocyte expression of PPAR-y (in the absence of VDR) has contributed to the down regulation of SIRT1. |
| 639 | 27871084 | Olmesartan Prevents Microalbuminuria in db/db Diabetic Mice Through Inhibition of Angiotensin II/p38/SIRT1-Induced Podocyte Apoptosis. |
| 640 | 27836811 | Here, we report the involvement of the reciprocal interplay between deacetylase SIRT1 and protein kinase AMPK in podocyte high glucose-induced abolition of insulin-dependent glucose uptake, manifesting insulin resistance. |
| 641 | 27836811 | Here, we report the involvement of the reciprocal interplay between deacetylase SIRT1 and protein kinase AMPK in podocyte high glucose-induced abolition of insulin-dependent glucose uptake, manifesting insulin resistance. |
| 642 | 27836811 | Here, we report the involvement of the reciprocal interplay between deacetylase SIRT1 and protein kinase AMPK in podocyte high glucose-induced abolition of insulin-dependent glucose uptake, manifesting insulin resistance. |
| 643 | 27836811 | Here, we report the involvement of the reciprocal interplay between deacetylase SIRT1 and protein kinase AMPK in podocyte high glucose-induced abolition of insulin-dependent glucose uptake, manifesting insulin resistance. |
| 644 | 27836811 | Immunodetection methods were used to determine SIRT1 protein level and AMPK phosphorylation degree. |
| 645 | 27836811 | Immunodetection methods were used to determine SIRT1 protein level and AMPK phosphorylation degree. |
| 646 | 27836811 | Immunodetection methods were used to determine SIRT1 protein level and AMPK phosphorylation degree. |
| 647 | 27836811 | Immunodetection methods were used to determine SIRT1 protein level and AMPK phosphorylation degree. |
| 648 | 27836811 | We have demonstrated that the absence of the stimulating effect of insulin on glucose uptake into primary rat podocytes after long-time exposition to high glucose concentrations, is a result of decreased SIRT1 protein levels and activity, associated with decreased AMPK phosphorylation degree, presumably underlying the induction of insulin resistance. |
| 649 | 27836811 | We have demonstrated that the absence of the stimulating effect of insulin on glucose uptake into primary rat podocytes after long-time exposition to high glucose concentrations, is a result of decreased SIRT1 protein levels and activity, associated with decreased AMPK phosphorylation degree, presumably underlying the induction of insulin resistance. |
| 650 | 27836811 | We have demonstrated that the absence of the stimulating effect of insulin on glucose uptake into primary rat podocytes after long-time exposition to high glucose concentrations, is a result of decreased SIRT1 protein levels and activity, associated with decreased AMPK phosphorylation degree, presumably underlying the induction of insulin resistance. |
| 651 | 27836811 | We have demonstrated that the absence of the stimulating effect of insulin on glucose uptake into primary rat podocytes after long-time exposition to high glucose concentrations, is a result of decreased SIRT1 protein levels and activity, associated with decreased AMPK phosphorylation degree, presumably underlying the induction of insulin resistance. |
| 652 | 27836811 | Our findings suggest that the interplay between SIRT1 and AMPK is involved in the regulation of insulin action in podocytes. |
| 653 | 27836811 | Our findings suggest that the interplay between SIRT1 and AMPK is involved in the regulation of insulin action in podocytes. |
| 654 | 27836811 | Our findings suggest that the interplay between SIRT1 and AMPK is involved in the regulation of insulin action in podocytes. |
| 655 | 27836811 | Our findings suggest that the interplay between SIRT1 and AMPK is involved in the regulation of insulin action in podocytes. |
| 656 | 26931474 | Our previous data indicated that the decrease in Sirt1 expression in proximal tubules caused the reduction in glomerular Sirt1 and the subsequent increase in glomerular Claudin-1. |
| 657 | 26931472 | In podocytes, SIRT1 regulates the expression of important genes such as PGC-1α, Foxo4, p65 and STAT3, which act to maintain podocyte function by modulating the levels of histone acetylation. |
| 658 | 26931472 | In podocytes, SIRT1 regulates the expression of important genes such as PGC-1α, Foxo4, p65 and STAT3, which act to maintain podocyte function by modulating the levels of histone acetylation. |
| 659 | 26931472 | In podocytes, SIRT1 regulates the expression of important genes such as PGC-1α, Foxo4, p65 and STAT3, which act to maintain podocyte function by modulating the levels of histone acetylation. |
| 660 | 26931472 | In podocytes, SIRT1 regulates the expression of important genes such as PGC-1α, Foxo4, p65 and STAT3, which act to maintain podocyte function by modulating the levels of histone acetylation. |
| 661 | 26931472 | In podocytes, SIRT1 regulates the expression of important genes such as PGC-1α, Foxo4, p65 and STAT3, which act to maintain podocyte function by modulating the levels of histone acetylation. |
| 662 | 26931472 | Here, we confirmed that SIRT1 protects podocytes by maintaining PGC-1α via its deacetylase-activated transcriptional activity in mitochondria and podocytes. |
| 663 | 26931472 | Here, we confirmed that SIRT1 protects podocytes by maintaining PGC-1α via its deacetylase-activated transcriptional activity in mitochondria and podocytes. |
| 664 | 26931472 | Here, we confirmed that SIRT1 protects podocytes by maintaining PGC-1α via its deacetylase-activated transcriptional activity in mitochondria and podocytes. |
| 665 | 26931472 | Here, we confirmed that SIRT1 protects podocytes by maintaining PGC-1α via its deacetylase-activated transcriptional activity in mitochondria and podocytes. |
| 666 | 26931472 | Here, we confirmed that SIRT1 protects podocytes by maintaining PGC-1α via its deacetylase-activated transcriptional activity in mitochondria and podocytes. |
| 667 | 26931472 | We then showed that the alteration of Foxo4 (forkhead box O4) acetylation and decrease in SIRT1 promote podocyte apoptosis in diabetic nephropathy, resulting in the gradual development of diabetic nephropathy. |
| 668 | 26931472 | We then showed that the alteration of Foxo4 (forkhead box O4) acetylation and decrease in SIRT1 promote podocyte apoptosis in diabetic nephropathy, resulting in the gradual development of diabetic nephropathy. |
| 669 | 26931472 | We then showed that the alteration of Foxo4 (forkhead box O4) acetylation and decrease in SIRT1 promote podocyte apoptosis in diabetic nephropathy, resulting in the gradual development of diabetic nephropathy. |
| 670 | 26931472 | We then showed that the alteration of Foxo4 (forkhead box O4) acetylation and decrease in SIRT1 promote podocyte apoptosis in diabetic nephropathy, resulting in the gradual development of diabetic nephropathy. |
| 671 | 26931472 | We then showed that the alteration of Foxo4 (forkhead box O4) acetylation and decrease in SIRT1 promote podocyte apoptosis in diabetic nephropathy, resulting in the gradual development of diabetic nephropathy. |
| 672 | 26931472 | Next, we showed that advanced glycation end products (AGEs) induced p65 and STAT3 acetylation in human podocytes. |
| 673 | 26931472 | Next, we showed that advanced glycation end products (AGEs) induced p65 and STAT3 acetylation in human podocytes. |
| 674 | 26931472 | Next, we showed that advanced glycation end products (AGEs) induced p65 and STAT3 acetylation in human podocytes. |
| 675 | 26931472 | Next, we showed that advanced glycation end products (AGEs) induced p65 and STAT3 acetylation in human podocytes. |
| 676 | 26931472 | Next, we showed that advanced glycation end products (AGEs) induced p65 and STAT3 acetylation in human podocytes. |
| 677 | 26931472 | Decreased Sirt1 activity in podocytes results in the development of proteinuria and kidney injury via the acetylation of p65 and STAT3. |
| 678 | 26931472 | Decreased Sirt1 activity in podocytes results in the development of proteinuria and kidney injury via the acetylation of p65 and STAT3. |
| 679 | 26931472 | Decreased Sirt1 activity in podocytes results in the development of proteinuria and kidney injury via the acetylation of p65 and STAT3. |
| 680 | 26931472 | Decreased Sirt1 activity in podocytes results in the development of proteinuria and kidney injury via the acetylation of p65 and STAT3. |
| 681 | 26931472 | Decreased Sirt1 activity in podocytes results in the development of proteinuria and kidney injury via the acetylation of p65 and STAT3. |
| 682 | 26931472 | SIRT1 protects podocytes and prevents glomerular injury by deacetylating cortactin and changing cortactin localization, thereby maintaining the integrity of the actin cytoskeleton. |
| 683 | 26931472 | SIRT1 protects podocytes and prevents glomerular injury by deacetylating cortactin and changing cortactin localization, thereby maintaining the integrity of the actin cytoskeleton. |
| 684 | 26931472 | SIRT1 protects podocytes and prevents glomerular injury by deacetylating cortactin and changing cortactin localization, thereby maintaining the integrity of the actin cytoskeleton. |
| 685 | 26931472 | SIRT1 protects podocytes and prevents glomerular injury by deacetylating cortactin and changing cortactin localization, thereby maintaining the integrity of the actin cytoskeleton. |
| 686 | 26931472 | SIRT1 protects podocytes and prevents glomerular injury by deacetylating cortactin and changing cortactin localization, thereby maintaining the integrity of the actin cytoskeleton. |
| 687 | 26424786 | Treatment of diabetic db/db mice with the selective TGR5 agonist INT-777 decreased proteinuria, podocyte injury, mesangial expansion, fibrosis, and CD68 macrophage infiltration in the kidney. |
| 688 | 26424786 | INT-777 also induced renal expression of master regulators of mitochondrial biogenesis, inhibitors of oxidative stress, and inducers of fatty acid β-oxidation, including sirtuin 1 (SIRT1), sirtuin 3 (SIRT3), and Nrf-1. |
| 689 | 26424786 | Increased activity of SIRT3 was evidenced by normalization of the increased acetylation of mitochondrial superoxide dismutase 2 (SOD2) and isocitrate dehydrogenase 2 (IDH2) observed in untreated db/db mice. |
| 690 | 26083654 | This further decreases expression of Sirt1 in glomerular podocytes and increases expression of a tight junction protein, claudin-1, which results in albuminuria. |
| 691 | 25724269 | Independent role of PP2A and mTORc1 in palmitate induced podocyte death. |
| 692 | 25724269 | Independent role of PP2A and mTORc1 in palmitate induced podocyte death. |
| 693 | 25724269 | This impairment in insulin signalling prevents insulin induced SIRT 1 expression and deacetylation of p53. |
| 694 | 25724269 | This impairment in insulin signalling prevents insulin induced SIRT 1 expression and deacetylation of p53. |
| 695 | 25724269 | Further, palmitate treatment prevents insulin induced phosphorylation of PP2A and FOXO1 but it potentiates the phosphorylation of mTOR at Ser 2448. |
| 696 | 25724269 | Further, palmitate treatment prevents insulin induced phosphorylation of PP2A and FOXO1 but it potentiates the phosphorylation of mTOR at Ser 2448. |
| 697 | 25724269 | Interestingly, selective inhibition of PP2A, by Okadaic acid at 5 nM, restored insulin induced phosphorylation of AKT, FOXO1, SIRT1 activity and p53 degradation. |
| 698 | 25724269 | Interestingly, selective inhibition of PP2A, by Okadaic acid at 5 nM, restored insulin induced phosphorylation of AKT, FOXO1, SIRT1 activity and p53 degradation. |
| 699 | 25724269 | On the other hand, partial inhibition of mTORc1, by low dose of Rapamycin (1 nM) also restored phosphorylation of AKT and SIRT1 activity, whereas no significant changes were observed in insulin induced phosphorylation of PP2A after mTORc1 inhibition. |
| 700 | 25724269 | On the other hand, partial inhibition of mTORc1, by low dose of Rapamycin (1 nM) also restored phosphorylation of AKT and SIRT1 activity, whereas no significant changes were observed in insulin induced phosphorylation of PP2A after mTORc1 inhibition. |
| 701 | 25724269 | To the best of our knowledge this is the first report suggesting independent role of PP2A and mTORc1 in palmitate induced IR and associated podocyte death. |
| 702 | 25724269 | To the best of our knowledge this is the first report suggesting independent role of PP2A and mTORc1 in palmitate induced IR and associated podocyte death. |
| 703 | 25724269 | Therefore, the best therapeutic approach for treatment of diabetic kidney disease should involve manipulating phosphorylation of both PP2A and mTORc1. |
| 704 | 25724269 | Therefore, the best therapeutic approach for treatment of diabetic kidney disease should involve manipulating phosphorylation of both PP2A and mTORc1. |
| 705 | 25424328 | Sirtuin1 Maintains Actin Cytoskeleton by Deacetylation of Cortactin in Injured Podocytes. |
| 706 | 25424328 | Sirtuin1 Maintains Actin Cytoskeleton by Deacetylation of Cortactin in Injured Podocytes. |
| 707 | 25424328 | Sirtuin1 Maintains Actin Cytoskeleton by Deacetylation of Cortactin in Injured Podocytes. |
| 708 | 25424328 | Sirtuin1 Maintains Actin Cytoskeleton by Deacetylation of Cortactin in Injured Podocytes. |
| 709 | 25424328 | The increase in urinary albumin excretion and BUN and the severity of glomerular injury were all significantly greater in SIRT1(pod-/-) mice than in wild-type mice. |
| 710 | 25424328 | The increase in urinary albumin excretion and BUN and the severity of glomerular injury were all significantly greater in SIRT1(pod-/-) mice than in wild-type mice. |
| 711 | 25424328 | The increase in urinary albumin excretion and BUN and the severity of glomerular injury were all significantly greater in SIRT1(pod-/-) mice than in wild-type mice. |
| 712 | 25424328 | The increase in urinary albumin excretion and BUN and the severity of glomerular injury were all significantly greater in SIRT1(pod-/-) mice than in wild-type mice. |
| 713 | 25424328 | Furthermore, SIRT1 activation deacetylated the actin-binding and -polymerizing protein cortactin in the nucleus and facilitated deacetylated cortactin localization in the cytoplasm. |
| 714 | 25424328 | Furthermore, SIRT1 activation deacetylated the actin-binding and -polymerizing protein cortactin in the nucleus and facilitated deacetylated cortactin localization in the cytoplasm. |
| 715 | 25424328 | Furthermore, SIRT1 activation deacetylated the actin-binding and -polymerizing protein cortactin in the nucleus and facilitated deacetylated cortactin localization in the cytoplasm. |
| 716 | 25424328 | Furthermore, SIRT1 activation deacetylated the actin-binding and -polymerizing protein cortactin in the nucleus and facilitated deacetylated cortactin localization in the cytoplasm. |
| 717 | 25424328 | Taken together, these findings indicate that SIRT1 protects podocytes and prevents glomerular injury by deacetylating cortactin and thereby, maintaining actin cytoskeleton integrity. |
| 718 | 25424328 | Taken together, these findings indicate that SIRT1 protects podocytes and prevents glomerular injury by deacetylating cortactin and thereby, maintaining actin cytoskeleton integrity. |
| 719 | 25424328 | Taken together, these findings indicate that SIRT1 protects podocytes and prevents glomerular injury by deacetylating cortactin and thereby, maintaining actin cytoskeleton integrity. |
| 720 | 25424328 | Taken together, these findings indicate that SIRT1 protects podocytes and prevents glomerular injury by deacetylating cortactin and thereby, maintaining actin cytoskeleton integrity. |
| 721 | 25126552 | Recent studies have suggested that the activity of three nutrient-sensing signals, mTORC1, AMPK, and Sirt1, is altered in the diabetic kidney. |
| 722 | 24952428 | The silent mating type information regulation 2 homolog 1 gene (Sirt1) encodes an NAD-dependent deacetylase that modifies the activity of well-known transcriptional regulators affected in kidney diseases. |
| 723 | 24941909 | Further, GSPE significantly decreased 24 h albumin levels and increased the expression of nephrin and podocalyxin. |
| 724 | 24941909 | Finally, GSPE activated the expression of PGC-1α, silent mating type information regulation 2 homolog 1 (SIRT1) and AMP-activated protein kinase (AMPK). |
| 725 | 24608443 | Here, we determined the roles of Sirt1 and the effect of NF-κB (p65) and STAT3 acetylation in DN. |
| 726 | 24608443 | Here, we determined the roles of Sirt1 and the effect of NF-κB (p65) and STAT3 acetylation in DN. |
| 727 | 24608443 | Here, we determined the roles of Sirt1 and the effect of NF-κB (p65) and STAT3 acetylation in DN. |
| 728 | 24608443 | We found that acetylation of p65 and STAT3 was increased in both mouse and human diabetic kidneys. |
| 729 | 24608443 | We found that acetylation of p65 and STAT3 was increased in both mouse and human diabetic kidneys. |
| 730 | 24608443 | We found that acetylation of p65 and STAT3 was increased in both mouse and human diabetic kidneys. |
| 731 | 24608443 | In human podocytes, advanced glycation end products (AGEs) induced p65 and STAT3 acetylation and overexpression of acetylation-incompetent mutants of p65 and STAT3 abrogated AGE-induced expression of NF-κB and STAT3 target genes. |
| 732 | 24608443 | In human podocytes, advanced glycation end products (AGEs) induced p65 and STAT3 acetylation and overexpression of acetylation-incompetent mutants of p65 and STAT3 abrogated AGE-induced expression of NF-κB and STAT3 target genes. |
| 733 | 24608443 | In human podocytes, advanced glycation end products (AGEs) induced p65 and STAT3 acetylation and overexpression of acetylation-incompetent mutants of p65 and STAT3 abrogated AGE-induced expression of NF-κB and STAT3 target genes. |
| 734 | 24608443 | Inhibition of AGE formation in db/db mice by pyridoxamine treatment attenuated proteinuria and podocyte injury, restored SIRT1 expression, and reduced p65 and STAT3 acetylation. |
| 735 | 24608443 | Inhibition of AGE formation in db/db mice by pyridoxamine treatment attenuated proteinuria and podocyte injury, restored SIRT1 expression, and reduced p65 and STAT3 acetylation. |
| 736 | 24608443 | Inhibition of AGE formation in db/db mice by pyridoxamine treatment attenuated proteinuria and podocyte injury, restored SIRT1 expression, and reduced p65 and STAT3 acetylation. |
| 737 | 24608443 | Diabetic db/db mice with conditional deletion of SIRT1 in podocytes developed more proteinuria, kidney injury, and acetylation of p65 and STAT3 compared with db/db mice without SIRT1 deletion. |
| 738 | 24608443 | Diabetic db/db mice with conditional deletion of SIRT1 in podocytes developed more proteinuria, kidney injury, and acetylation of p65 and STAT3 compared with db/db mice without SIRT1 deletion. |
| 739 | 24608443 | Diabetic db/db mice with conditional deletion of SIRT1 in podocytes developed more proteinuria, kidney injury, and acetylation of p65 and STAT3 compared with db/db mice without SIRT1 deletion. |
| 740 | 24608443 | Treatment of db/db mice with a bromodomain and extraterminal (BET)-specific bromodomain inhibitor (MS417) which blocks acetylation-mediated association of p65 and STAT3 with BET proteins, attenuated proteinuria, and kidney injury. |
| 741 | 24608443 | Treatment of db/db mice with a bromodomain and extraterminal (BET)-specific bromodomain inhibitor (MS417) which blocks acetylation-mediated association of p65 and STAT3 with BET proteins, attenuated proteinuria, and kidney injury. |
| 742 | 24608443 | Treatment of db/db mice with a bromodomain and extraterminal (BET)-specific bromodomain inhibitor (MS417) which blocks acetylation-mediated association of p65 and STAT3 with BET proteins, attenuated proteinuria, and kidney injury. |
| 743 | 24608443 | Our findings strongly support a critical role for p65 and STAT3 acetylation in DN. |
| 744 | 24608443 | Our findings strongly support a critical role for p65 and STAT3 acetylation in DN. |
| 745 | 24608443 | Our findings strongly support a critical role for p65 and STAT3 acetylation in DN. |
| 746 | 24202384 | Sirt1-Claudin-1 crosstalk regulates renal function. |
| 747 | 24141423 | Renal tubular Sirt1 attenuates diabetic albuminuria by epigenetically suppressing Claudin-1 overexpression in podocytes. |
| 748 | 24141423 | Renal tubular Sirt1 attenuates diabetic albuminuria by epigenetically suppressing Claudin-1 overexpression in podocytes. |
| 749 | 24141423 | Renal tubular Sirt1 attenuates diabetic albuminuria by epigenetically suppressing Claudin-1 overexpression in podocytes. |
| 750 | 24141423 | Downregulation of Sirt1 and upregulation of the tight junction protein Claudin-1 by SIRT1-mediated epigenetic regulation in podocytes contributed to albuminuria. |
| 751 | 24141423 | Downregulation of Sirt1 and upregulation of the tight junction protein Claudin-1 by SIRT1-mediated epigenetic regulation in podocytes contributed to albuminuria. |
| 752 | 24141423 | Downregulation of Sirt1 and upregulation of the tight junction protein Claudin-1 by SIRT1-mediated epigenetic regulation in podocytes contributed to albuminuria. |
| 753 | 24141423 | In human subjects with diabetes, the levels of SIRT1 and Claudin-1 were correlated with proteinuria levels. |
| 754 | 24141423 | In human subjects with diabetes, the levels of SIRT1 and Claudin-1 were correlated with proteinuria levels. |
| 755 | 24141423 | In human subjects with diabetes, the levels of SIRT1 and Claudin-1 were correlated with proteinuria levels. |
| 756 | 22648295 | Overexpression of the silent mating type information regulation 2 homolog 1, a gene upstream of PGC-1α, prevented aldosterone-induced mitochondrial damage and podocyte injury by upregulating PGC-1α at both the transcriptional and post-translational levels. |
| 757 | 22648295 | Activators of SIRT1, such as resveratol, may be therapeutically useful in glomerular diseases to promote and maintain PGC-1α expression and, consequently, podocyte integrity. |
| 758 | 21858169 | Advanced glycation end products (AGEs) accumulate in patients with diabetes and promote the apoptosis of podocyte by activating the forkhead box O4 (Foxo4) transcription factor to increase the expression of a pro-apoptosis gene, Bcl2l11. |
| 759 | 21858169 | Advanced glycation end products (AGEs) accumulate in patients with diabetes and promote the apoptosis of podocyte by activating the forkhead box O4 (Foxo4) transcription factor to increase the expression of a pro-apoptosis gene, Bcl2l11. |
| 760 | 21858169 | Advanced glycation end products (AGEs) accumulate in patients with diabetes and promote the apoptosis of podocyte by activating the forkhead box O4 (Foxo4) transcription factor to increase the expression of a pro-apoptosis gene, Bcl2l11. |
| 761 | 21858169 | Advanced glycation end products (AGEs) accumulate in patients with diabetes and promote the apoptosis of podocyte by activating the forkhead box O4 (Foxo4) transcription factor to increase the expression of a pro-apoptosis gene, Bcl2l11. |
| 762 | 21858169 | Using chromatin immunoprecipitation we demonstrate that AGE-modified bovine serum albumin (AGE-BSA) enhances Foxo4 binding to a forkhead binding element in the promoter of Bcl2lll. |
| 763 | 21858169 | Using chromatin immunoprecipitation we demonstrate that AGE-modified bovine serum albumin (AGE-BSA) enhances Foxo4 binding to a forkhead binding element in the promoter of Bcl2lll. |
| 764 | 21858169 | Using chromatin immunoprecipitation we demonstrate that AGE-modified bovine serum albumin (AGE-BSA) enhances Foxo4 binding to a forkhead binding element in the promoter of Bcl2lll. |
| 765 | 21858169 | Using chromatin immunoprecipitation we demonstrate that AGE-modified bovine serum albumin (AGE-BSA) enhances Foxo4 binding to a forkhead binding element in the promoter of Bcl2lll. |
| 766 | 21858169 | Lysine acetylation of Foxo4 is required for Foxo4 binding and transcription of Bcl2l11 in podocytes treated with AGE-BSA. |
| 767 | 21858169 | Lysine acetylation of Foxo4 is required for Foxo4 binding and transcription of Bcl2l11 in podocytes treated with AGE-BSA. |
| 768 | 21858169 | Lysine acetylation of Foxo4 is required for Foxo4 binding and transcription of Bcl2l11 in podocytes treated with AGE-BSA. |
| 769 | 21858169 | Lysine acetylation of Foxo4 is required for Foxo4 binding and transcription of Bcl2l11 in podocytes treated with AGE-BSA. |
| 770 | 21858169 | The expression of a protein deacetylase that targets Foxo4 for deacetylation, sirtuin (Sirt1), is down regulated in cultured podocytes by AGE-BSA treatment and in glomeruli of diabetic patients. |
| 771 | 21858169 | The expression of a protein deacetylase that targets Foxo4 for deacetylation, sirtuin (Sirt1), is down regulated in cultured podocytes by AGE-BSA treatment and in glomeruli of diabetic patients. |
| 772 | 21858169 | The expression of a protein deacetylase that targets Foxo4 for deacetylation, sirtuin (Sirt1), is down regulated in cultured podocytes by AGE-BSA treatment and in glomeruli of diabetic patients. |
| 773 | 21858169 | The expression of a protein deacetylase that targets Foxo4 for deacetylation, sirtuin (Sirt1), is down regulated in cultured podocytes by AGE-BSA treatment and in glomeruli of diabetic patients. |
| 774 | 21858169 | Glomeruli isolated from diabetic db/db mice have increased acetylation of Foxo4, suppressed expression of Sirt1, and increased expression of Bcl2l11 compared to non-diabetic littermates. |
| 775 | 21858169 | Glomeruli isolated from diabetic db/db mice have increased acetylation of Foxo4, suppressed expression of Sirt1, and increased expression of Bcl2l11 compared to non-diabetic littermates. |
| 776 | 21858169 | Glomeruli isolated from diabetic db/db mice have increased acetylation of Foxo4, suppressed expression of Sirt1, and increased expression of Bcl2l11 compared to non-diabetic littermates. |
| 777 | 21858169 | Glomeruli isolated from diabetic db/db mice have increased acetylation of Foxo4, suppressed expression of Sirt1, and increased expression of Bcl2l11 compared to non-diabetic littermates. |
| 778 | 21858169 | Together, our data provide evidence that alteration of Foxo4 acetylation and down regulation of Sirt1 expression in diabetes promote podocyte apoptosis. |
| 779 | 21858169 | Together, our data provide evidence that alteration of Foxo4 acetylation and down regulation of Sirt1 expression in diabetes promote podocyte apoptosis. |
| 780 | 21858169 | Together, our data provide evidence that alteration of Foxo4 acetylation and down regulation of Sirt1 expression in diabetes promote podocyte apoptosis. |
| 781 | 21858169 | Together, our data provide evidence that alteration of Foxo4 acetylation and down regulation of Sirt1 expression in diabetes promote podocyte apoptosis. |
| 782 | 21858169 | Strategies to preserve Sirt1 expression or reduce Foxo4 acetylation could be used to prevent podocyte loss in diabetes. |
| 783 | 21858169 | Strategies to preserve Sirt1 expression or reduce Foxo4 acetylation could be used to prevent podocyte loss in diabetes. |
| 784 | 21858169 | Strategies to preserve Sirt1 expression or reduce Foxo4 acetylation could be used to prevent podocyte loss in diabetes. |
| 785 | 21858169 | Strategies to preserve Sirt1 expression or reduce Foxo4 acetylation could be used to prevent podocyte loss in diabetes. |