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Gene Information
Gene symbol: AKT1
Gene name: v-akt murine thymoma viral oncogene homolog 1
HGNC ID: 391
Synonyms: RAC, PKB, PRKBA, AKT
Related Genes
Related Sentences
| # | PMID | Sentence |
| 1 | 26453750 | Human cells expressing HLA class I ligands for inhibitory receptors KIR2DL1, KIR2DL2/3, or CD94-NKG2A were transfected with IL-15Rα. |
| 2 | 26453750 | Proliferation of primary NK cells in response to transpresented IL-15 was reduced by engagement of either KIR2DL1 or KIR2DL2/3 by cognate HLA-C ligands. |
| 3 | 26453750 | Inhibitory KIR-HLA-C interactions did not reduce the proliferation induced by soluble IL-15. |
| 4 | 26453750 | Therefore, transpresentation of IL-15 is subject to downregulation by MHC class I-specific inhibitory receptors. |
| 5 | 26453750 | Similarly, proliferation of the NKG2A(+) cell line NKL induced by IL-15 transpresentation was inhibited by HLA-E. |
| 6 | 26453750 | Coengagement of inhibitory receptors, either KIR2DL1 or CD94-NKG2A, did not inhibit phosphorylation of Stat5 but inhibited selectively phosphorylation of Akt and S6 ribosomal protein. |
| 7 | 26425723 | Concomitant molecular alterations involving the PI3K/AKT/mTOR and RAF/MEK pathways were also identified and suggest other treatment strategies that deserve investigation. |
| 8 | 26410627 | IL-2-mediated activation of the Akt kinase and mTORc1 signaling was both necessary and sufficient to shift differentiation away from Tfh cells, instead promoting that of Th1 cells. |
| 9 | 26343197 | This review provides an appraisal of some of the key signaling pathways that may contribute to immune suppression in ovarian cancer, with a particular focus on the potential involvement of the c-KIT/PI3K/AKT, wnt/β-catenin, IL-6/STAT3 and AhR signaling pathways in regulation of indoleamine 2,3-dioxygenase expression in tumor-associated macrophages. |
| 10 | 26275051 | The microarray analyses of the CD34+ cells and granulocytes were performed from 20 de novo MPN subjects: JAK2 positive ET, PV, PMF subjects, and JAK2 negative ET/PMF subjects. |
| 11 | 26275051 | The microarray analyses of the CD34+ cells and granulocytes were performed from 20 de novo MPN subjects: JAK2 positive ET, PV, PMF subjects, and JAK2 negative ET/PMF subjects. |
| 12 | 26275051 | The microarray analyses of the CD34+ cells and granulocytes were performed from 20 de novo MPN subjects: JAK2 positive ET, PV, PMF subjects, and JAK2 negative ET/PMF subjects. |
| 13 | 26275051 | Thirty-six genes (including RUNX1, TNFRSF19) were persistently highly expressed, while 42 genes (including FOXD4, PDE4A) were underexpressed both in CD34+ cells and granulocytes. |
| 14 | 26275051 | Thirty-six genes (including RUNX1, TNFRSF19) were persistently highly expressed, while 42 genes (including FOXD4, PDE4A) were underexpressed both in CD34+ cells and granulocytes. |
| 15 | 26275051 | Thirty-six genes (including RUNX1, TNFRSF19) were persistently highly expressed, while 42 genes (including FOXD4, PDE4A) were underexpressed both in CD34+ cells and granulocytes. |
| 16 | 26275051 | Using proteomic studies, significant up-regulation was observed for MAPK and PI3K/AKT signaling regulators that control myeloid cell apoptosis and proliferation: RAC2, MNDA, S100A8/9, CORO1A, and GNAI2. |
| 17 | 26275051 | Using proteomic studies, significant up-regulation was observed for MAPK and PI3K/AKT signaling regulators that control myeloid cell apoptosis and proliferation: RAC2, MNDA, S100A8/9, CORO1A, and GNAI2. |
| 18 | 26275051 | Using proteomic studies, significant up-regulation was observed for MAPK and PI3K/AKT signaling regulators that control myeloid cell apoptosis and proliferation: RAC2, MNDA, S100A8/9, CORO1A, and GNAI2. |
| 19 | 26275051 | When the status of the mTOR signaling pathway related genes was analyzed, PI3K/AKT regulators were preferentially up-regulated in CD34+ cells of MPNs, with down-regulated major components of the protein complex EIF4F. |
| 20 | 26275051 | When the status of the mTOR signaling pathway related genes was analyzed, PI3K/AKT regulators were preferentially up-regulated in CD34+ cells of MPNs, with down-regulated major components of the protein complex EIF4F. |
| 21 | 26275051 | When the status of the mTOR signaling pathway related genes was analyzed, PI3K/AKT regulators were preferentially up-regulated in CD34+ cells of MPNs, with down-regulated major components of the protein complex EIF4F. |
| 22 | 26275051 | Molecular profiling of CD34+ cells and granulocytes of MPN determined gene expression patterns beyond their recognized function in disease pathogenesis that included dominant up-regulation of PI3K/AKT signaling. |
| 23 | 26275051 | Molecular profiling of CD34+ cells and granulocytes of MPN determined gene expression patterns beyond their recognized function in disease pathogenesis that included dominant up-regulation of PI3K/AKT signaling. |
| 24 | 26275051 | Molecular profiling of CD34+ cells and granulocytes of MPN determined gene expression patterns beyond their recognized function in disease pathogenesis that included dominant up-regulation of PI3K/AKT signaling. |
| 25 | 26254061 | Autophagy is involved in oral rAAV/Aβ vaccine-induced Aβ clearance in APP/PS1 transgenic mice. |
| 26 | 26254061 | In this study, we first demonstrated that oral vaccination with rAAV/Aß decreased the p62 level and up-regulated the LC3B-II/LC3B-I ratio in APP/PS1 mouse brain, suggesting enhanced autophagy. |
| 27 | 26254061 | Further, inhibition of the Akt/mTOR pathway may account for autophagy enhancement. |
| 28 | 26254061 | We also found increased anti-Aß antibodies in the sera of APP/PS1 mice with oral vaccination, accompanied by elevation of complement factors C1q and C3 levels in the brain. |
| 29 | 26244501 | Avian Reovirus Protein p17 Functions as a Nucleoporin Tpr Suppressor Leading to Activation of p53, p21 and PTEN and Inactivation of PI3K/AKT/mTOR and ERK Signaling Pathways. |
| 30 | 26244501 | Avian Reovirus Protein p17 Functions as a Nucleoporin Tpr Suppressor Leading to Activation of p53, p21 and PTEN and Inactivation of PI3K/AKT/mTOR and ERK Signaling Pathways. |
| 31 | 26244501 | Avian reovirus (ARV) protein p17 has been shown to regulate cell cycle and autophagy by activation of p53/PTEN pathway; nevertheless, it is still unclear how p53 and PTEN are activated by p17. |
| 32 | 26244501 | Avian reovirus (ARV) protein p17 has been shown to regulate cell cycle and autophagy by activation of p53/PTEN pathway; nevertheless, it is still unclear how p53 and PTEN are activated by p17. |
| 33 | 26244501 | Here, we report for the first time that p17 functions as a nucleoporin Tpr suppressor that leads to p53 nuclear accumulation and consequently activates p53, p21, and PTEN. |
| 34 | 26244501 | Here, we report for the first time that p17 functions as a nucleoporin Tpr suppressor that leads to p53 nuclear accumulation and consequently activates p53, p21, and PTEN. |
| 35 | 26244501 | In addition to upregulation of PTEN by activation of p53 pathway, this study also suggests that ARV protein p17 acts as a positive regulator of PTEN. |
| 36 | 26244501 | In addition to upregulation of PTEN by activation of p53 pathway, this study also suggests that ARV protein p17 acts as a positive regulator of PTEN. |
| 37 | 26244501 | ARV p17 stabilizes PTEN by stimulating phosphorylation of cytoplasmic PTEN and by elevating Rak-PTEN association to prevent it from E3 ligase NEDD4-1 targeting. |
| 38 | 26244501 | ARV p17 stabilizes PTEN by stimulating phosphorylation of cytoplasmic PTEN and by elevating Rak-PTEN association to prevent it from E3 ligase NEDD4-1 targeting. |
| 39 | 26244501 | To activate PTEN, p17 is able to promote β-arrestin-mediated PTEN translocation from the cytoplasm to the plasma membrane via a Rock-1-dependent manner. |
| 40 | 26244501 | To activate PTEN, p17 is able to promote β-arrestin-mediated PTEN translocation from the cytoplasm to the plasma membrane via a Rock-1-dependent manner. |
| 41 | 26244501 | The accumulation of p53 in the nucleus induces the PTEN- and p21-mediated downregulation of cyclin D1 and CDK4. |
| 42 | 26244501 | The accumulation of p53 in the nucleus induces the PTEN- and p21-mediated downregulation of cyclin D1 and CDK4. |
| 43 | 26244501 | Furthermore, Tpr and CDK4 knockdown increased virus production in contrast to depletion of p53, PTEN, and LC3 reducing virus yield. |
| 44 | 26244501 | Furthermore, Tpr and CDK4 knockdown increased virus production in contrast to depletion of p53, PTEN, and LC3 reducing virus yield. |
| 45 | 26244501 | Taken together, our data suggest that p17-mediated Tpr suppression positively regulates p53, PTEN, and p21 and negatively regulates PI3K/AKT/mTOR and ERK signaling pathways, both of which are beneficial for virus replication. |
| 46 | 26244501 | Taken together, our data suggest that p17-mediated Tpr suppression positively regulates p53, PTEN, and p21 and negatively regulates PI3K/AKT/mTOR and ERK signaling pathways, both of which are beneficial for virus replication. |
| 47 | 26221268 | Functional analysis studies revealed that rCRT/39-272 has potent immunostimulatory activities in both activating human monocytes and B cells to secrete cytokines. rCRT/39-272 can drive the activation of bone marrow derived DC in TLR4/CD14 dependent way, as indicated by secretion of cytokines IL-12/IL-23 (p40) and IL-1β. |
| 48 | 26221268 | Functional analysis studies revealed that rCRT/39-272 has potent immunostimulatory activities in both activating human monocytes and B cells to secrete cytokines. rCRT/39-272 can drive the activation of bone marrow derived DC in TLR4/CD14 dependent way, as indicated by secretion of cytokines IL-12/IL-23 (p40) and IL-1β. |
| 49 | 26221268 | Exposure of DC to rCRT/39-272 induces P-Akt, suggesting that rCRT/39-272 induces maturation of DC through PI3K/Akt signaling pathway. |
| 50 | 26221268 | Exposure of DC to rCRT/39-272 induces P-Akt, suggesting that rCRT/39-272 induces maturation of DC through PI3K/Akt signaling pathway. |
| 51 | 26221268 | The results suggest that soluble rCRT/39-272 is a potent stimulatory agent to DC maturation in TLR4/CD14 and PI3K/Akt dependent pathway. |
| 52 | 26221268 | The results suggest that soluble rCRT/39-272 is a potent stimulatory agent to DC maturation in TLR4/CD14 and PI3K/Akt dependent pathway. |
| 53 | 26155399 | Akt1 and -2 inhibition diminishes terminal differentiation and enhances central memory CD8+ T-cell proliferation and survival. |
| 54 | 26155399 | Akt1 and -2 inhibition diminishes terminal differentiation and enhances central memory CD8+ T-cell proliferation and survival. |
| 55 | 26155399 | Akt1 and -2 inhibition diminishes terminal differentiation and enhances central memory CD8+ T-cell proliferation and survival. |
| 56 | 26155399 | Akt1 and -2 inhibition diminishes terminal differentiation and enhances central memory CD8+ T-cell proliferation and survival. |
| 57 | 26155399 | Akt1 and -2 inhibition diminishes terminal differentiation and enhances central memory CD8+ T-cell proliferation and survival. |
| 58 | 26155399 | Akt1 and -2 inhibition diminishes terminal differentiation and enhances central memory CD8+ T-cell proliferation and survival. |
| 59 | 26155399 | Akt1 and -2 inhibition diminishes terminal differentiation and enhances central memory CD8+ T-cell proliferation and survival. |
| 60 | 26155399 | The differentiation of CD8 + memory T cells is thought to be coordinated by the phosphoinositide 3-kinase (PI3K)/Akt pathway. |
| 61 | 26155399 | The differentiation of CD8 + memory T cells is thought to be coordinated by the phosphoinositide 3-kinase (PI3K)/Akt pathway. |
| 62 | 26155399 | The differentiation of CD8 + memory T cells is thought to be coordinated by the phosphoinositide 3-kinase (PI3K)/Akt pathway. |
| 63 | 26155399 | The differentiation of CD8 + memory T cells is thought to be coordinated by the phosphoinositide 3-kinase (PI3K)/Akt pathway. |
| 64 | 26155399 | The differentiation of CD8 + memory T cells is thought to be coordinated by the phosphoinositide 3-kinase (PI3K)/Akt pathway. |
| 65 | 26155399 | The differentiation of CD8 + memory T cells is thought to be coordinated by the phosphoinositide 3-kinase (PI3K)/Akt pathway. |
| 66 | 26155399 | The differentiation of CD8 + memory T cells is thought to be coordinated by the phosphoinositide 3-kinase (PI3K)/Akt pathway. |
| 67 | 26155399 | We, therefore, investigated the role of Akt isoforms in the differentiation and proliferation of memory CD8 + T cells. |
| 68 | 26155399 | We, therefore, investigated the role of Akt isoforms in the differentiation and proliferation of memory CD8 + T cells. |
| 69 | 26155399 | We, therefore, investigated the role of Akt isoforms in the differentiation and proliferation of memory CD8 + T cells. |
| 70 | 26155399 | We, therefore, investigated the role of Akt isoforms in the differentiation and proliferation of memory CD8 + T cells. |
| 71 | 26155399 | We, therefore, investigated the role of Akt isoforms in the differentiation and proliferation of memory CD8 + T cells. |
| 72 | 26155399 | We, therefore, investigated the role of Akt isoforms in the differentiation and proliferation of memory CD8 + T cells. |
| 73 | 26155399 | We, therefore, investigated the role of Akt isoforms in the differentiation and proliferation of memory CD8 + T cells. |
| 74 | 26155399 | We found that Akt1 and Akt2, but not Akt3, drive the terminal differentiation of CD8 + T cells, and their inhibition enhances the therapeutically superior TCM phenotype. |
| 75 | 26155399 | We found that Akt1 and Akt2, but not Akt3, drive the terminal differentiation of CD8 + T cells, and their inhibition enhances the therapeutically superior TCM phenotype. |
| 76 | 26155399 | We found that Akt1 and Akt2, but not Akt3, drive the terminal differentiation of CD8 + T cells, and their inhibition enhances the therapeutically superior TCM phenotype. |
| 77 | 26155399 | We found that Akt1 and Akt2, but not Akt3, drive the terminal differentiation of CD8 + T cells, and their inhibition enhances the therapeutically superior TCM phenotype. |
| 78 | 26155399 | We found that Akt1 and Akt2, but not Akt3, drive the terminal differentiation of CD8 + T cells, and their inhibition enhances the therapeutically superior TCM phenotype. |
| 79 | 26155399 | We found that Akt1 and Akt2, but not Akt3, drive the terminal differentiation of CD8 + T cells, and their inhibition enhances the therapeutically superior TCM phenotype. |
| 80 | 26155399 | We found that Akt1 and Akt2, but not Akt3, drive the terminal differentiation of CD8 + T cells, and their inhibition enhances the therapeutically superior TCM phenotype. |
| 81 | 26155399 | Furthermore, the inhibition of Akt1 and Akt2, but not Akt 3, delays CD8 + T-cell exhaustion and preserves naïve and TCM CD8 + T cells, thus enhancing their proliferative ability and survival and prolonging their cytokine and Granzyme B production ability. |
| 82 | 26155399 | Furthermore, the inhibition of Akt1 and Akt2, but not Akt 3, delays CD8 + T-cell exhaustion and preserves naïve and TCM CD8 + T cells, thus enhancing their proliferative ability and survival and prolonging their cytokine and Granzyme B production ability. |
| 83 | 26155399 | Furthermore, the inhibition of Akt1 and Akt2, but not Akt 3, delays CD8 + T-cell exhaustion and preserves naïve and TCM CD8 + T cells, thus enhancing their proliferative ability and survival and prolonging their cytokine and Granzyme B production ability. |
| 84 | 26155399 | Furthermore, the inhibition of Akt1 and Akt2, but not Akt 3, delays CD8 + T-cell exhaustion and preserves naïve and TCM CD8 + T cells, thus enhancing their proliferative ability and survival and prolonging their cytokine and Granzyme B production ability. |
| 85 | 26155399 | Furthermore, the inhibition of Akt1 and Akt2, but not Akt 3, delays CD8 + T-cell exhaustion and preserves naïve and TCM CD8 + T cells, thus enhancing their proliferative ability and survival and prolonging their cytokine and Granzyme B production ability. |
| 86 | 26155399 | Furthermore, the inhibition of Akt1 and Akt2, but not Akt 3, delays CD8 + T-cell exhaustion and preserves naïve and TCM CD8 + T cells, thus enhancing their proliferative ability and survival and prolonging their cytokine and Granzyme B production ability. |
| 87 | 26155399 | Furthermore, the inhibition of Akt1 and Akt2, but not Akt 3, delays CD8 + T-cell exhaustion and preserves naïve and TCM CD8 + T cells, thus enhancing their proliferative ability and survival and prolonging their cytokine and Granzyme B production ability. |
| 88 | 26155399 | Here, we define a mechanism in which proliferative potential, function, and survival of CD8 + T cells are enhanced by maintaining a reservoir of TCM and naïve cells using only Akt1 and Akt2 inhibition. |
| 89 | 26155399 | Here, we define a mechanism in which proliferative potential, function, and survival of CD8 + T cells are enhanced by maintaining a reservoir of TCM and naïve cells using only Akt1 and Akt2 inhibition. |
| 90 | 26155399 | Here, we define a mechanism in which proliferative potential, function, and survival of CD8 + T cells are enhanced by maintaining a reservoir of TCM and naïve cells using only Akt1 and Akt2 inhibition. |
| 91 | 26155399 | Here, we define a mechanism in which proliferative potential, function, and survival of CD8 + T cells are enhanced by maintaining a reservoir of TCM and naïve cells using only Akt1 and Akt2 inhibition. |
| 92 | 26155399 | Here, we define a mechanism in which proliferative potential, function, and survival of CD8 + T cells are enhanced by maintaining a reservoir of TCM and naïve cells using only Akt1 and Akt2 inhibition. |
| 93 | 26155399 | Here, we define a mechanism in which proliferative potential, function, and survival of CD8 + T cells are enhanced by maintaining a reservoir of TCM and naïve cells using only Akt1 and Akt2 inhibition. |
| 94 | 26155399 | Here, we define a mechanism in which proliferative potential, function, and survival of CD8 + T cells are enhanced by maintaining a reservoir of TCM and naïve cells using only Akt1 and Akt2 inhibition. |
| 95 | 26155399 | Therefore, our findings strongly suggest the utility of using Akt1 and Akt2 inhibitors to modulate CD8 + T cells, both for adoptive cell transfer and vaccine-based cancer immune therapies. |
| 96 | 26155399 | Therefore, our findings strongly suggest the utility of using Akt1 and Akt2 inhibitors to modulate CD8 + T cells, both for adoptive cell transfer and vaccine-based cancer immune therapies. |
| 97 | 26155399 | Therefore, our findings strongly suggest the utility of using Akt1 and Akt2 inhibitors to modulate CD8 + T cells, both for adoptive cell transfer and vaccine-based cancer immune therapies. |
| 98 | 26155399 | Therefore, our findings strongly suggest the utility of using Akt1 and Akt2 inhibitors to modulate CD8 + T cells, both for adoptive cell transfer and vaccine-based cancer immune therapies. |
| 99 | 26155399 | Therefore, our findings strongly suggest the utility of using Akt1 and Akt2 inhibitors to modulate CD8 + T cells, both for adoptive cell transfer and vaccine-based cancer immune therapies. |
| 100 | 26155399 | Therefore, our findings strongly suggest the utility of using Akt1 and Akt2 inhibitors to modulate CD8 + T cells, both for adoptive cell transfer and vaccine-based cancer immune therapies. |
| 101 | 26155399 | Therefore, our findings strongly suggest the utility of using Akt1 and Akt2 inhibitors to modulate CD8 + T cells, both for adoptive cell transfer and vaccine-based cancer immune therapies. |
| 102 | 26078940 | Molecular Analysis of AFP and HSA Interactions with PTEN Protein. |
| 103 | 26078940 | The protein sequence of AFP has significant homology to that of human serum albumin (HSA), but its biological characteristics are vastly different from HSA. |
| 104 | 26078940 | The AFP functions as a regulator in the phosphatidylinositol 3-kinase (PI3K)/protein kinase B (AKT) pathway, but HSA plays a key role as a transport protein. |
| 105 | 26078940 | The data from colocalization and co-IP displayed a strong interaction between AFP and PTEN (phosphatase and tensin homolog), demonstrating that AFP did bind to PTEN, but HSA did not. |
| 106 | 26078940 | The molecular docking study further showed that the AFP domains I and III could contact with PTEN. |
| 107 | 26078940 | In silicon substitutions of AFP binding site residues at position 490M/K and 105L/R corresponding to residues K490 and R105 in HSA resulted in steric clashes with PTEN residues R150 and K46, respectively. |
| 108 | 26078940 | Ultimately, the experimental results and the molecular modeling data from the interactions of AFP and HSA with PTEN will help us to identify targets for designing drugs and vaccines against human hepatocellular carcinoma. |
| 109 | 26047480 | EADs is postulated to induce cell cycle arrest that is p53- and p21-dependent based on the upregulated expression of p53 and p21 (P<0.05). |
| 110 | 26047480 | EADs is postulated to induce cell cycle arrest that is p53- and p21-dependent based on the upregulated expression of p53 and p21 (P<0.05). |
| 111 | 26047480 | The expression of Bax was upregulated with downregulation of Bcl-2 following treatment with EADs. |
| 112 | 26047480 | The expression of Bax was upregulated with downregulation of Bcl-2 following treatment with EADs. |
| 113 | 26047480 | The elevated Bax/Bcl-2 ratio and the depolarization of mitochondrial membrane potential suggest that EADs-induced apoptosis is mitochondria-dependent. |
| 114 | 26047480 | The elevated Bax/Bcl-2 ratio and the depolarization of mitochondrial membrane potential suggest that EADs-induced apoptosis is mitochondria-dependent. |
| 115 | 26047480 | The expression of oxidative stress-related AKT, p-AKT, ERK, and p-ERK was downregulated with upregulation of JNK and p-JNK. |
| 116 | 26047480 | The expression of oxidative stress-related AKT, p-AKT, ERK, and p-ERK was downregulated with upregulation of JNK and p-JNK. |
| 117 | 26047480 | The data indicate that induction of oxidative-stress related apoptosis by EADs was mediated by inhibition of AKT and ERK, and activation of JNK. |
| 118 | 26047480 | The data indicate that induction of oxidative-stress related apoptosis by EADs was mediated by inhibition of AKT and ERK, and activation of JNK. |
| 119 | 26039731 | We also exposed human hepatocellular carcinoma HepG2 cells to high levels of palmitate, which enhanced endoplasmic reticulum stress-related gene expression and impaired insulin-stimulated Akt phosphorylation (Ser473). |
| 120 | 26034349 | It includes mainly therapies targeting against kinases, including epidermal growth factor receptor, Ras/Raf/mitogen-activated protein kinase cascade, human epidermal growth factor receptor 2, insulin growth factor-1 receptor, phosphoinositide 3-kinase/Akt/mTOR and hepatocyte growth factor receptor. |
| 121 | 25967534 | In addition, a number of monoclonal antibodies targeting AKT, mTOR and PI3K pathways are under evaluation. |
| 122 | 25949867 | STAT5 activation, Foxp3 expression, and hnRNPE1 activation mediated by PI3K/Akt signaling were required for Dab2 expression during GM-CSF-derived BMDC development regardless of TGF-β signaling. |
| 123 | 25949867 | Dab2-silencing was accompanied by enhanced IL-12 and IL-6 expression, and an improved capacity of DC for antigen uptake, migration and T cell stimulation, which generated strong CTL in vaccinated mice. |
| 124 | 25793397 | Although the phosphatidylinositol 3-kinase (PI3K)/Akt signaling pathway is one of the targets of NS1, the MFPTr virus suppressed the phosphorylation of Akt when compared with the wild-type (WT) virus. |
| 125 | 25793397 | It was suggested that this might lead to the subsequent inhibition of the cleavage of PARP-1 and caspase-3, which is important for the progression of apoptosis. |
| 126 | 25711535 | HER2 and AKT phosphorylation was demonstrated in primary FMC by immunoblot analysis, indicating HER2 as a therapeutic target. |
| 127 | 25711535 | Immune sera to mutant pfeHER2-K bound 3T3/HER2 cells weakly, but they showed better recognition of K12 and K248 cells that also express HER1 and HER3, suggesting distinct HER2 epitopes displayed by FMC that may be simulated by feHER2-K. |
| 128 | 25680514 | The DEX (CRCL-GL261)-DCs were found to promote cell proliferation and cytotoxic T lymphocyte (CTL) activity of CD4(+) and CD8(+) T cells in vitro compared with DEX (GL261)-DCs, which were loaded with DEXs derived from DCs loaded with GL261 tumor cell lysates. |
| 129 | 25680514 | Moreover, depletion of CD4(+) and CD8(+) T cells significantly impaired the anti-tumor effect of DEX (CRCL-GL261)-DCs. |
| 130 | 25680514 | Finally, DEX (CRCL-GL261)-DCs were found to negatively regulate Casitas B cell lineage lymphoma (Cbl)-b and c-Cbl signaling, leading to the activation of phosphatidyl inositol 3-kinase (PI3K)/Akt and extracellular signal-regulated kinase (ERK) signaling in T cells. |
| 131 | 25550785 | Overexpression of GRIM-19, a mitochondrial respiratory chain complex I protein, suppresses hepatocellular carcinoma growth. |
| 132 | 25550785 | Overexpression of GRIM-19, a mitochondrial respiratory chain complex I protein, suppresses hepatocellular carcinoma growth. |
| 133 | 25550785 | Overexpression of GRIM-19, a mitochondrial respiratory chain complex I protein, suppresses hepatocellular carcinoma growth. |
| 134 | 25550785 | AKT1, pAKT1, cyclinD1, CDK4, PCNA, Bax, Bcl-2, cleaved caspase-9, cleaved caspase-3, and cytochrome C were detected by Western blot and immunofluorescence. |
| 135 | 25550785 | AKT1, pAKT1, cyclinD1, CDK4, PCNA, Bax, Bcl-2, cleaved caspase-9, cleaved caspase-3, and cytochrome C were detected by Western blot and immunofluorescence. |
| 136 | 25550785 | AKT1, pAKT1, cyclinD1, CDK4, PCNA, Bax, Bcl-2, cleaved caspase-9, cleaved caspase-3, and cytochrome C were detected by Western blot and immunofluorescence. |
| 137 | 25550785 | We also found that AKT1 expression and phosphorylation were regulated by the expression of GRIM-19. |
| 138 | 25550785 | We also found that AKT1 expression and phosphorylation were regulated by the expression of GRIM-19. |
| 139 | 25550785 | We also found that AKT1 expression and phosphorylation were regulated by the expression of GRIM-19. |
| 140 | 25550785 | Collectively, our study demonstrated that GRIM-19 overexpression suppressed HCC growth and downregulated AKT1 expression, suggesting that GRIM-19 might play a crucial role in hepatocarcinogenesis through negatively regulating the PI3K/AKT signaling pathway. |
| 141 | 25550785 | Collectively, our study demonstrated that GRIM-19 overexpression suppressed HCC growth and downregulated AKT1 expression, suggesting that GRIM-19 might play a crucial role in hepatocarcinogenesis through negatively regulating the PI3K/AKT signaling pathway. |
| 142 | 25550785 | Collectively, our study demonstrated that GRIM-19 overexpression suppressed HCC growth and downregulated AKT1 expression, suggesting that GRIM-19 might play a crucial role in hepatocarcinogenesis through negatively regulating the PI3K/AKT signaling pathway. |
| 143 | 25473100 | Notably, the delay of PCD was mediated by modulation of the antiapoptotic proteins, Mcl-1 and Bfl-1, and impairment of loss of Δψm in macrophages through the neutralization of oxidative and nitrosative stress. |
| 144 | 25473100 | Analysis of the targets of LdDNA identified an early activation of the TLR9-dependent PI3K/Akt and SFK pathways, which were required for the observation of the antiapoptotic effects in macrophages. |
| 145 | 25304692 | The phosphatidylinositol-3-kinase (PI3K)-dependent Akt and the mammalian target of rapamycin (mTOR) (PI3K/Akt/mTOR) are major host cell signalling pathways that regulate protein synthesis, cell growth, proliferation, migration and survival. |
| 146 | 25225677 | PI3K/Akt regulates survival during differentiation of human macrophages by maintaining NF-κB-dependent expression of antiapoptotic Bcl-xL. |
| 147 | 25225677 | PI3K/Akt regulates survival during differentiation of human macrophages by maintaining NF-κB-dependent expression of antiapoptotic Bcl-xL. |
| 148 | 25225677 | PI3K/Akt regulates survival during differentiation of human macrophages by maintaining NF-κB-dependent expression of antiapoptotic Bcl-xL. |
| 149 | 25225677 | PI3K/Akt regulates survival during differentiation of human macrophages by maintaining NF-κB-dependent expression of antiapoptotic Bcl-xL. |
| 150 | 25225677 | PI3K/Akt regulates survival during differentiation of human macrophages by maintaining NF-κB-dependent expression of antiapoptotic Bcl-xL. |
| 151 | 25225677 | Our results indicate that PI3K/Akt distinctively regulates survival of macrophages during and after differentiation. |
| 152 | 25225677 | Our results indicate that PI3K/Akt distinctively regulates survival of macrophages during and after differentiation. |
| 153 | 25225677 | Our results indicate that PI3K/Akt distinctively regulates survival of macrophages during and after differentiation. |
| 154 | 25225677 | Our results indicate that PI3K/Akt distinctively regulates survival of macrophages during and after differentiation. |
| 155 | 25225677 | Our results indicate that PI3K/Akt distinctively regulates survival of macrophages during and after differentiation. |
| 156 | 25225677 | More specifically, a signaling pathway consisting of PI3K/Akt-NF-κB-Bcl-xL regulates cell survival during the differentiation process. |
| 157 | 25225677 | More specifically, a signaling pathway consisting of PI3K/Akt-NF-κB-Bcl-xL regulates cell survival during the differentiation process. |
| 158 | 25225677 | More specifically, a signaling pathway consisting of PI3K/Akt-NF-κB-Bcl-xL regulates cell survival during the differentiation process. |
| 159 | 25225677 | More specifically, a signaling pathway consisting of PI3K/Akt-NF-κB-Bcl-xL regulates cell survival during the differentiation process. |
| 160 | 25225677 | More specifically, a signaling pathway consisting of PI3K/Akt-NF-κB-Bcl-xL regulates cell survival during the differentiation process. |
| 161 | 25225677 | PI3K/Akt-mediated activation of NF-κB plays a key role in survival of differentiating macrophages by specifically sustaining antiapoptotic Bcl-xL expression. |
| 162 | 25225677 | PI3K/Akt-mediated activation of NF-κB plays a key role in survival of differentiating macrophages by specifically sustaining antiapoptotic Bcl-xL expression. |
| 163 | 25225677 | PI3K/Akt-mediated activation of NF-κB plays a key role in survival of differentiating macrophages by specifically sustaining antiapoptotic Bcl-xL expression. |
| 164 | 25225677 | PI3K/Akt-mediated activation of NF-κB plays a key role in survival of differentiating macrophages by specifically sustaining antiapoptotic Bcl-xL expression. |
| 165 | 25225677 | PI3K/Akt-mediated activation of NF-κB plays a key role in survival of differentiating macrophages by specifically sustaining antiapoptotic Bcl-xL expression. |
| 166 | 25225677 | With the use of pharmacological inhibitors and siRNA for Akt and Bcl-xL, we show that in the absence of Akt-dependent Bcl-xL expression during differentiation, cells undergo caspase-mediated apoptosis. |
| 167 | 25225677 | With the use of pharmacological inhibitors and siRNA for Akt and Bcl-xL, we show that in the absence of Akt-dependent Bcl-xL expression during differentiation, cells undergo caspase-mediated apoptosis. |
| 168 | 25225677 | With the use of pharmacological inhibitors and siRNA for Akt and Bcl-xL, we show that in the absence of Akt-dependent Bcl-xL expression during differentiation, cells undergo caspase-mediated apoptosis. |
| 169 | 25225677 | With the use of pharmacological inhibitors and siRNA for Akt and Bcl-xL, we show that in the absence of Akt-dependent Bcl-xL expression during differentiation, cells undergo caspase-mediated apoptosis. |
| 170 | 25225677 | With the use of pharmacological inhibitors and siRNA for Akt and Bcl-xL, we show that in the absence of Akt-dependent Bcl-xL expression during differentiation, cells undergo caspase-mediated apoptosis. |
| 171 | 25225677 | In contrast, in differentiated macrophages, Bcl-xL expression is independent of PI3K/Akt activation. |
| 172 | 25225677 | In contrast, in differentiated macrophages, Bcl-xL expression is independent of PI3K/Akt activation. |
| 173 | 25225677 | In contrast, in differentiated macrophages, Bcl-xL expression is independent of PI3K/Akt activation. |
| 174 | 25225677 | In contrast, in differentiated macrophages, Bcl-xL expression is independent of PI3K/Akt activation. |
| 175 | 25225677 | In contrast, in differentiated macrophages, Bcl-xL expression is independent of PI3K/Akt activation. |
| 176 | 25201410 | CRM197 is a naturally nontoxic diphtheria toxin mutant that binds and inhibits heparin-binding epidermal growth factor-like growth factor. |
| 177 | 25201410 | CRM197 is a naturally nontoxic diphtheria toxin mutant that binds and inhibits heparin-binding epidermal growth factor-like growth factor. |
| 178 | 25201410 | Activation of cleaved caspase-3, 8, and 9, activity of matrix metalloproteinase-2/9 (MMP-2/9), and expression of phosphorylated Akt (p-Akt) were also checked. |
| 179 | 25201410 | Activation of cleaved caspase-3, 8, and 9, activity of matrix metalloproteinase-2/9 (MMP-2/9), and expression of phosphorylated Akt (p-Akt) were also checked. |
| 180 | 25201410 | The activation of cleaved caspase-3, 8, 9 was promoted, activity of MMP-2 and MMP-9 and expression of p-Akt were inhibited significantly by the treatment of CRM197 and shRNA-VCAM-1 alone or in combination, indicating that the combination of CRM197 with shRNA-VCAM-1 additively inhibited the malignant behavior of human glioblastoma cells via activating caspase-3, 8, 9 as well as inhibiting MMP-2, MMP-9, and Akt pathway. |
| 181 | 25201410 | The activation of cleaved caspase-3, 8, 9 was promoted, activity of MMP-2 and MMP-9 and expression of p-Akt were inhibited significantly by the treatment of CRM197 and shRNA-VCAM-1 alone or in combination, indicating that the combination of CRM197 with shRNA-VCAM-1 additively inhibited the malignant behavior of human glioblastoma cells via activating caspase-3, 8, 9 as well as inhibiting MMP-2, MMP-9, and Akt pathway. |
| 182 | 25187540 | Mitogen-activated protein kinase-interacting kinase regulates mTOR/AKT signaling and controls the serine/arginine-rich protein kinase-responsive type 1 internal ribosome entry site-mediated translation and viral oncolysis. |
| 183 | 25104444 | ErbB-2-directed peptide vaccines have been shown to be effective in prevention of spontaneous tumorigenesis of breast in neu transgenic mouse model, and cellular immunity is proposed as a mechanism for the anti-tumor efficacy. |
| 184 | 25104444 | In addition, immune serum from the mice of ErbB-2 vaccine group had an inhibitory effect on mammosphere-forming capacity and signaling through ErbB-2 and downstream Akt pathway in ErbB-2 overexpressing mouse mammary cancer cells. |
| 185 | 25104444 | We also suggest that a strategy of inducing strong immune responses using multi-epitope ErbB-2-directed helper vaccine might be useful in preventing breast cancer recurrence. |
| 186 | 24821968 | Elmo1 and Elmo2 are highly homologous cytoplasmic adaptor proteins that interact with Dock family guanine nucleotide exchange factors to promote activation of the small GTPase Rac. |
| 187 | 24821968 | Elmo1 and Elmo2 are highly homologous cytoplasmic adaptor proteins that interact with Dock family guanine nucleotide exchange factors to promote activation of the small GTPase Rac. |
| 188 | 24821968 | Elmo1 and Elmo2 are highly homologous cytoplasmic adaptor proteins that interact with Dock family guanine nucleotide exchange factors to promote activation of the small GTPase Rac. |
| 189 | 24821968 | In T lymphocytes, Dock2 is essential for CCR7- and CXCR4-dependent Rac activation and chemotaxis, but the role of Elmo proteins in regulating Dock2 function in primary T cells is not known. |
| 190 | 24821968 | In T lymphocytes, Dock2 is essential for CCR7- and CXCR4-dependent Rac activation and chemotaxis, but the role of Elmo proteins in regulating Dock2 function in primary T cells is not known. |
| 191 | 24821968 | In T lymphocytes, Dock2 is essential for CCR7- and CXCR4-dependent Rac activation and chemotaxis, but the role of Elmo proteins in regulating Dock2 function in primary T cells is not known. |
| 192 | 24821968 | In this article, we show that endogenous Elmo1, but not Elmo2, interacts constitutively with Dock2 in mouse and human primary T cells. |
| 193 | 24821968 | In this article, we show that endogenous Elmo1, but not Elmo2, interacts constitutively with Dock2 in mouse and human primary T cells. |
| 194 | 24821968 | In this article, we show that endogenous Elmo1, but not Elmo2, interacts constitutively with Dock2 in mouse and human primary T cells. |
| 195 | 24821968 | CD4(+) T cells from Elmo1(-/-) mice were profoundly impaired in polarization, Rac activation, and chemotaxis in response to CCR7 and CXCR4 stimulation. |
| 196 | 24821968 | CD4(+) T cells from Elmo1(-/-) mice were profoundly impaired in polarization, Rac activation, and chemotaxis in response to CCR7 and CXCR4 stimulation. |
| 197 | 24821968 | CD4(+) T cells from Elmo1(-/-) mice were profoundly impaired in polarization, Rac activation, and chemotaxis in response to CCR7 and CXCR4 stimulation. |
| 198 | 24821968 | Transfection of full-length Elmo1, but not Elmo2 or a Dock2-binding mutant of Elmo1, rescued defective migration of Elmo1(-/-) T cells. |
| 199 | 24821968 | Transfection of full-length Elmo1, but not Elmo2 or a Dock2-binding mutant of Elmo1, rescued defective migration of Elmo1(-/-) T cells. |
| 200 | 24821968 | Transfection of full-length Elmo1, but not Elmo2 or a Dock2-binding mutant of Elmo1, rescued defective migration of Elmo1(-/-) T cells. |
| 201 | 24821968 | Interestingly, Dock2 protein levels were reduced by 4-fold in Elmo1(-/-) lymphocytes despite normal levels of Dock2 mRNA. |
| 202 | 24821968 | Interestingly, Dock2 protein levels were reduced by 4-fold in Elmo1(-/-) lymphocytes despite normal levels of Dock2 mRNA. |
| 203 | 24821968 | Interestingly, Dock2 protein levels were reduced by 4-fold in Elmo1(-/-) lymphocytes despite normal levels of Dock2 mRNA. |
| 204 | 24821968 | Dock2 polyubiquitination was increased in Elmo1(-/-) T cells, and treatment with proteasome inhibitors partially restored Dock2 levels in Elmo1(-/-) T cells. |
| 205 | 24821968 | Dock2 polyubiquitination was increased in Elmo1(-/-) T cells, and treatment with proteasome inhibitors partially restored Dock2 levels in Elmo1(-/-) T cells. |
| 206 | 24821968 | Dock2 polyubiquitination was increased in Elmo1(-/-) T cells, and treatment with proteasome inhibitors partially restored Dock2 levels in Elmo1(-/-) T cells. |
| 207 | 24821968 | Finally, we show that Dock2 is directly ubiquitinated in CD4(+) T cells and that Elmo1 expression in heterologous cells inhibits ubiquitination of Dock2. |
| 208 | 24821968 | Finally, we show that Dock2 is directly ubiquitinated in CD4(+) T cells and that Elmo1 expression in heterologous cells inhibits ubiquitination of Dock2. |
| 209 | 24821968 | Finally, we show that Dock2 is directly ubiquitinated in CD4(+) T cells and that Elmo1 expression in heterologous cells inhibits ubiquitination of Dock2. |
| 210 | 24821968 | Taken together, these findings reveal a previously unknown, nonredundant role for Elmo1 in controlling Dock2 levels and Dock2-dependent T cell migration in primary lymphocytes. |
| 211 | 24821968 | Taken together, these findings reveal a previously unknown, nonredundant role for Elmo1 in controlling Dock2 levels and Dock2-dependent T cell migration in primary lymphocytes. |
| 212 | 24821968 | Taken together, these findings reveal a previously unknown, nonredundant role for Elmo1 in controlling Dock2 levels and Dock2-dependent T cell migration in primary lymphocytes. |
| 213 | 24821968 | This work provides valuable insights into the molecular regulation of Dock2 by Elmo1 that can be used to design improved inhibitors that target the Elmo-Dock-Rac signaling complex. |
| 214 | 24821968 | This work provides valuable insights into the molecular regulation of Dock2 by Elmo1 that can be used to design improved inhibitors that target the Elmo-Dock-Rac signaling complex. |
| 215 | 24821968 | This work provides valuable insights into the molecular regulation of Dock2 by Elmo1 that can be used to design improved inhibitors that target the Elmo-Dock-Rac signaling complex. |
| 216 | 24767856 | In vitro, hepatocytes co-expressing HBx and a pre-S2 mutant showed enhanced expression of vascular endothelial growth factor-A, phosphorylated Akt 1/2/3, phosphorylated extracellular signal-regulated kinase 1/2, and phosphorylated mammalian target of rapamycin signals. |
| 217 | 24767856 | In vitro, hepatocytes co-expressing HBx and a pre-S2 mutant showed enhanced expression of vascular endothelial growth factor-A, phosphorylated Akt 1/2/3, phosphorylated extracellular signal-regulated kinase 1/2, and phosphorylated mammalian target of rapamycin signals. |
| 218 | 24767856 | The oncogenic signals of vascular endothelial growth factor-A, phosphorylated Akt 1/2/3, phosphorylated extracellular signal-regulated kinase 1/2, and phosphorylated mammalian target of rapamycin were sequentially and differentially activated at different stages in tumorigenesis. |
| 219 | 24767856 | The oncogenic signals of vascular endothelial growth factor-A, phosphorylated Akt 1/2/3, phosphorylated extracellular signal-regulated kinase 1/2, and phosphorylated mammalian target of rapamycin were sequentially and differentially activated at different stages in tumorigenesis. |
| 220 | 24712747 | Then, results show a clear induction of JAK/STAT and MAPK signaling pathways in infected NPTr cells. |
| 221 | 24712747 | Conversely, PI3K/Akt signaling pathways was not activated. |
| 222 | 24712747 | The inhibition of the JAK/STAT pathway clearly reduced interferon type I and III responses and the induction of SOCS1 at the transcript level in infected NPTr cells. |
| 223 | 24712562 | BCG-induced apoptosis was associated with dephosphorylation of the prosurvival activated threonine kinase (Akt) and its target FOXO3. |
| 224 | 24712562 | Finally, real-time quantitative PCR (qRT-PCR) analysis of the expression profile of BCG-infected macrophages showed an upregulation of two pro-apoptotic targets of FOXO3, NOXA and p53 upregulated modulator of apoptosis (PUMA). |
| 225 | 24337749 | KLRG1 impairs CD4+ T cell responses via p16ink4a and p27kip1 pathways: role in hepatitis B vaccine failure in individuals with hepatitis C virus infection. |
| 226 | 24337749 | In this study, we investigated the expression and function of an inhibitory receptor, killer cell lectin-like receptor subfamily G member 1 (KLRG1), in the regulation of CD4(+) T cells and HBV vaccine responses during HCV infection. |
| 227 | 24337749 | We demonstrated that KLRG1 was overexpressed on CD4(+) T cells from HCV-infected, HBV vaccine nonresponders compared with HBV vaccine responders. |
| 228 | 24337749 | The capacity of CD4(+) T cells to proliferate and secrete IL-2 cytokine was inversely associated with the level of KLRG1 expression. |
| 229 | 24337749 | Importantly, blocking KLRG1 signaling resulted in a significant improvement in CD4(+) T cell proliferation and IL-2 production in HCV-infected, HBV vaccine nonresponders in response to TCR stimulation. |
| 230 | 24337749 | Moreover, blockade of KLRG1 increased the phosphorylation of Akt (Ser(473)) and decreased the expression of cell cycle inhibitors p16(ink4a) and p27(kip1), which subsequently enhanced the expression of cyclin-dependent kinase 2 and cyclin E. |
| 231 | 24337749 | These results suggest that the KLRG1 pathway impairs CD4(+) T cell responses to neoantigen and induces a state of immune senescence in individuals with HCV infection, raising the possibility that blocking this negative-signaling pathway might improve HBV vaccine responses in the setting of chronic viral infection. |
| 232 | 23833306 | Accelerated tumor growth mediated by sublytic levels of antibody-induced complement activation is associated with activation of the PI3K/AKT survival pathway. |
| 233 | 23536633 | This was associated with higher rates of apoptosis in precursor cells and increased expression of cleaved caspase-3 and BCL-xL and downregulation of cyclin B1. |
| 234 | 23536633 | Further, blockade of fatty-acid synthesis decreased DC expression of MHC class II, ICAM-1, B7-1, and B7-2 but increased their production of selected proinflammatory cytokines including IL-12 and MCP-1. |
| 235 | 23536633 | Accordingly, inhibition of fatty-acid synthesis enhanced DC capacity to activate allogeneic as well as Ag-restricted CD4(+) and CD8(+) T cells and induce CTL responses. |
| 236 | 23536633 | We found that inhibition of fatty-acid synthesis resulted in elevated expression of numerous markers of ER stress in humans and mice and was associated with increased MAPK and Akt signaling. |
| 237 | 23531110 | Overexpression of the human epidermal growth factor receptor 2 (HER2) is identified in approximately 25- 30% of breast cancers and indicates a poor prognosis. |
| 238 | 23531110 | It is believed that aberrant activations of several signaling pathways involving the human epidermal growth factor receptor (EGFR/HER) family, phosphoinositide 3 kinase/Akt (PI3K/Akt) pathway, and vascular endothelial growth factor (VEGF) family, contribute to the development of trastuzumab resistance. |
| 239 | 23378844 | Role of PI3K/Akt signaling in memory CD8 T cell differentiation. |
| 240 | 23378844 | Role of PI3K/Akt signaling in memory CD8 T cell differentiation. |
| 241 | 23378844 | In this review, we will discuss the role of the phosphatidylinositol 3-kinase signaling pathway as a central signaling node, and the function of Akt as a rheostat in orchestrating the differentiation of memory CD8 T cells. |
| 242 | 23378844 | In this review, we will discuss the role of the phosphatidylinositol 3-kinase signaling pathway as a central signaling node, and the function of Akt as a rheostat in orchestrating the differentiation of memory CD8 T cells. |
| 243 | 23303829 | Ran-binding protein 3 (RanBP3) is a Ran-interacting protein that is best known for its role as a cofactor of CRM1-mediated cargo nuclear export. |
| 244 | 23303829 | Moreover, we demonstrated that the function of RanBP3 during vRNP nuclear export is regulated by phosphorylation at Ser58, and that RanBP3 phosphorylation is modulated by both PI3K/Akt and Ras/ERK/RSK pathways in the late phase of viral infection. |
| 245 | 23251389 | Wogonin induced calreticulin/annexin A1 exposure dictates the immunogenicity of cancer cells in a PERK/AKT dependent manner. |
| 246 | 23251389 | Wogonin induced calreticulin/annexin A1 exposure dictates the immunogenicity of cancer cells in a PERK/AKT dependent manner. |
| 247 | 23251389 | Here we demonstrated for the first time that wogonin elicits a potent antitumor immunity effect by inducing the translocation of calreticulin (CRT) and Annexin A1 to cell plasma membrane as well as the release of high-mobility group protein 1 (HMGB1) and ATP. |
| 248 | 23251389 | Here we demonstrated for the first time that wogonin elicits a potent antitumor immunity effect by inducing the translocation of calreticulin (CRT) and Annexin A1 to cell plasma membrane as well as the release of high-mobility group protein 1 (HMGB1) and ATP. |
| 249 | 23251389 | We found that wogonin-induced reactive oxygen species (ROS) production causes an endoplasmic reticulum (ER) stress response, including the phosphorylation of PERK (PKR-like endoplasmic reticulum kinase)/PKR (protein kinase R) and eIF2α (eukaryotic initiation factor 2α), which served as upstream signal for the activation of phosphoinositide 3-kinase (PI3K)/AKT, inducing calreticulin (CRT)/Annexin A1 cell membrane translocation. |
| 250 | 23251389 | We found that wogonin-induced reactive oxygen species (ROS) production causes an endoplasmic reticulum (ER) stress response, including the phosphorylation of PERK (PKR-like endoplasmic reticulum kinase)/PKR (protein kinase R) and eIF2α (eukaryotic initiation factor 2α), which served as upstream signal for the activation of phosphoinositide 3-kinase (PI3K)/AKT, inducing calreticulin (CRT)/Annexin A1 cell membrane translocation. |
| 251 | 23251389 | P22/CHP, a Ca(2+)-binding protein, was associated with CRT and was required for CRT translocation to cell membrane. |
| 252 | 23251389 | P22/CHP, a Ca(2+)-binding protein, was associated with CRT and was required for CRT translocation to cell membrane. |
| 253 | 23251389 | In conclusion, the activation of PI3K pathway elicited by ER stress induced CRT/Annexin A1 translocation ("eat me" signal) and HMGB1 release, mediating wogonin-induced immunity of tumor cell vaccine. |
| 254 | 23251389 | In conclusion, the activation of PI3K pathway elicited by ER stress induced CRT/Annexin A1 translocation ("eat me" signal) and HMGB1 release, mediating wogonin-induced immunity of tumor cell vaccine. |
| 255 | 22922731 | Curcumin inhibits HCV replication by induction of heme oxygenase-1 and suppression of AKT. |
| 256 | 22922731 | Curcumin inhibits HCV replication by induction of heme oxygenase-1 and suppression of AKT. |
| 257 | 22922731 | Curcumin inhibits HCV replication by induction of heme oxygenase-1 and suppression of AKT. |
| 258 | 22922731 | In addition to the heme oxygenase-1 induction, signaling molecule activities of AKT, extracellular signal-regulated kinases (ERK) and nuclear factor-κB (NF-κB) were inhibited by curcumin. |
| 259 | 22922731 | In addition to the heme oxygenase-1 induction, signaling molecule activities of AKT, extracellular signal-regulated kinases (ERK) and nuclear factor-κB (NF-κB) were inhibited by curcumin. |
| 260 | 22922731 | In addition to the heme oxygenase-1 induction, signaling molecule activities of AKT, extracellular signal-regulated kinases (ERK) and nuclear factor-κB (NF-κB) were inhibited by curcumin. |
| 261 | 22922731 | In summary, curcumin inhibited HCV replication by heme oxygenase-1 induction and AKT pathway inhibition. |
| 262 | 22922731 | In summary, curcumin inhibited HCV replication by heme oxygenase-1 induction and AKT pathway inhibition. |
| 263 | 22922731 | In summary, curcumin inhibited HCV replication by heme oxygenase-1 induction and AKT pathway inhibition. |
| 264 | 22491318 | Viral genomes are maintained at an average copy number of 25 per neuron and can be induced to productively replicate by interfering with PI3-Kinase / Akt signaling or the simple withdrawal of nerve growth factor(1). |
| 265 | 22467649 | Signal integration by Akt regulates CD8 T cell effector and memory differentiation. |
| 266 | 22467649 | Signal integration by Akt regulates CD8 T cell effector and memory differentiation. |
| 267 | 22467649 | The strength and nature of TCR signaling, along with signals delivered by cytokines like IL-2 and IL-12, influence differentiation of SLECs and memory precursor effector cells. |
| 268 | 22467649 | The strength and nature of TCR signaling, along with signals delivered by cytokines like IL-2 and IL-12, influence differentiation of SLECs and memory precursor effector cells. |
| 269 | 22467649 | Whereas sustained Akt activation severely impaired CD8 T cell memory and protective immunity, in vivo inhibition of Akt rescued SLECs from deletion and increased the number of memory CD8 T cells. |
| 270 | 22467649 | Whereas sustained Akt activation severely impaired CD8 T cell memory and protective immunity, in vivo inhibition of Akt rescued SLECs from deletion and increased the number of memory CD8 T cells. |
| 271 | 22442494 | In this review, we summarize current findings supporting a model in which leishmania target host regulatory molecules and pathways, such as the PTP SHP-1 and the PI3K/Akt signaling cascade, to prevent effective macrophage activation. |
| 272 | 22359505 | The PI3K/Akt signaling pathway controls cell growth in many cell types by modulating the activity of FOXO transcription factors. |
| 273 | 22359505 | The PI3K/Akt signaling pathway controls cell growth in many cell types by modulating the activity of FOXO transcription factors. |
| 274 | 22359505 | We show that phosphorylation of Akt, FOXO and mTOR in CD8 T cells occurs in a dynamic fashion in vivo during an acute viral infection. |
| 275 | 22359505 | We show that phosphorylation of Akt, FOXO and mTOR in CD8 T cells occurs in a dynamic fashion in vivo during an acute viral infection. |
| 276 | 21835795 | Myxoma virus induces type I interferon production in murine plasmacytoid dendritic cells via a TLR9/MyD88-, IRF5/IRF7-, and IFNAR-dependent pathway. |
| 277 | 21835795 | Using pDCs derived from genetic knockout mice, we show that the myxoma virus-induced innate immune response requires the endosomal DNA sensor TLR9 and its adaptor MyD88, transcription factors IRF5 and IRF7, and the type I IFN positive-feedback loop mediated by IFNAR1. |
| 278 | 21835795 | It is independent of the cytoplasmic RNA sensing pathway mediated by the mitochondrial adaptor molecule MAVS, the TLR3 adaptor TRIF, or the transcription factor IRF3. |
| 279 | 21835795 | Using pharmacological inhibitors, we demonstrate that myxoma virus-induced type I IFN and IL-12p70 production in murine pDCs is also dependent on phosphatidylinositol 3-kinase (PI3K) and Akt. |
| 280 | 21497908 | Regulation of influenza A virus induced CXCL-10 gene expression requires PI3K/Akt pathway and IRF3 transcription factor. |
| 281 | 21497908 | Regulation of influenza A virus induced CXCL-10 gene expression requires PI3K/Akt pathway and IRF3 transcription factor. |
| 282 | 21497908 | Regulation of influenza A virus induced CXCL-10 gene expression requires PI3K/Akt pathway and IRF3 transcription factor. |
| 283 | 21497908 | Regulation of influenza A virus induced CXCL-10 gene expression requires PI3K/Akt pathway and IRF3 transcription factor. |
| 284 | 21497908 | To understand the regulation of CXCL-10, we investigated the role of PI3K/AKT pathway in regulating virus induced CXCL-10 production. |
| 285 | 21497908 | To understand the regulation of CXCL-10, we investigated the role of PI3K/AKT pathway in regulating virus induced CXCL-10 production. |
| 286 | 21497908 | To understand the regulation of CXCL-10, we investigated the role of PI3K/AKT pathway in regulating virus induced CXCL-10 production. |
| 287 | 21497908 | To understand the regulation of CXCL-10, we investigated the role of PI3K/AKT pathway in regulating virus induced CXCL-10 production. |
| 288 | 21497908 | Previously we have shown that wild type (WT) influenza A virus infection activates PI3K/AKT pathway, whereas PR8-SH3-mf-1 mutant virus is unable to activate this pathway. |
| 289 | 21497908 | Previously we have shown that wild type (WT) influenza A virus infection activates PI3K/AKT pathway, whereas PR8-SH3-mf-1 mutant virus is unable to activate this pathway. |
| 290 | 21497908 | Previously we have shown that wild type (WT) influenza A virus infection activates PI3K/AKT pathway, whereas PR8-SH3-mf-1 mutant virus is unable to activate this pathway. |
| 291 | 21497908 | Previously we have shown that wild type (WT) influenza A virus infection activates PI3K/AKT pathway, whereas PR8-SH3-mf-1 mutant virus is unable to activate this pathway. |
| 292 | 21497908 | Our data suggested that PI3K/AKT pathway contributes to influenza A virus induced CXCL-10 production. |
| 293 | 21497908 | Our data suggested that PI3K/AKT pathway contributes to influenza A virus induced CXCL-10 production. |
| 294 | 21497908 | Our data suggested that PI3K/AKT pathway contributes to influenza A virus induced CXCL-10 production. |
| 295 | 21497908 | Our data suggested that PI3K/AKT pathway contributes to influenza A virus induced CXCL-10 production. |
| 296 | 21497908 | This process is involved in binding of IRF3 to the ISRE binding site in CXCL-10 promoter region. |
| 297 | 21497908 | This process is involved in binding of IRF3 to the ISRE binding site in CXCL-10 promoter region. |
| 298 | 21497908 | This process is involved in binding of IRF3 to the ISRE binding site in CXCL-10 promoter region. |
| 299 | 21497908 | This process is involved in binding of IRF3 to the ISRE binding site in CXCL-10 promoter region. |
| 300 | 21098227 | In this study, we demonstrate that the induction of TNF and IL-6 expression by LVS in mouse bone marrow-derived macrophages was markedly enhanced when PI3K activity was inhibited by either of the well-known chemical inhibitors, wortmannin or LY294002. |
| 301 | 21098227 | The enhanced cytokine expression was accompanied by enhanced activation of p38 MAPK and ERK1/2, both of which were critical for LVS-induced expression of TNF and IL-6. |
| 302 | 21098227 | LVS-induced MAPK activation and cytokine production were TLR2- and MyD88- dependent. |
| 303 | 21098227 | PI3K/Akt activation was MyD88-dependent, but was surprisingly TLR2-independent. |
| 304 | 21098227 | LVS infection also rapidly induced MAPK phosphatase-1 (MKP-1) expression; PI3K and TLR2 signaling were required. |
| 305 | 21098227 | Peak levels of MKP-1 correlated closely with the decline in p38 MAPK and ERK1/2 phosphorylation. |
| 306 | 21098227 | These data suggest that infection by LVS restrains the TLR2-triggered proinflammatory response via parallel activation of PI3K, leading to enhanced MKP-1 expression, accelerated deactivation of MAPKs, and suppression of proinflammatory cytokine production. |
| 307 | 20709527 | CA9 is not expressed in healthy renal tissue but is expressed in most clear cell renal cell carcinomas (CCRCC) through HIF-1α accumulation driven by hypoxia and inactivation of the VHL gene. |
| 308 | 20709527 | In metastatic disease, high CA9 expression by IHC was reported to be a powerful prognostic marker with better survival and sensitivity to IL-2, but this is still debated. |
| 309 | 20709527 | The prognostic value of CA9 in CCRCC could be explained by the frequent VHL gene inactivation driving an early activation of the HIF pathway. |
| 310 | 20709527 | The poorer prognosis associated with low CA9 expressing tumours could be due to the simultaneous overexpression of EGFR contributing to the activation of AkT and mTOR pathways. |
| 311 | 20696947 | Emerging reports reveal that activating Toll-like receptor-2 (TLR2)-MyD88 signals in CD8 T lymphocytes enhances cytokine production and cytotoxicity; however, the signaling pathway remains undefined. |
| 312 | 20696947 | We found that TLR2 engagement on T-cell receptor transgenic CD8 OT-1 T cells increased T-bet transcription factor levels consequently, augmenting effector transcript and protein levels both in vivo and in vitro. |
| 313 | 20696947 | In contrast, TLR2 agonist did not costimulate TLR2(-/-)OT-1 or MyD88(-/-)OT-1 T cells. |
| 314 | 20696947 | Inhibiting mTOR, Akt, or protein kinase C in T cells abolished the costimulatory effects of the TLR2 agonist. |
| 315 | 20664824 | [¹¹C]RAC; (18)F-Fluoromisonidazole; 89-12; 9-[¹⁸F]Fluoropropyl-(+)-dihydrotetrabenazine; Adalimumab, Adecatumumab, ADMVA, ADXS-11-001, Aflibercept, Agatolimod sodium, AGS-004, Alglucosidase alfa, Aliskiren fumarate, Alvocidib hydrochloride, AMG-108, AMG-853, Apixaban, Aripiprazole, Armodafinil, Atazanavir sulfate, Atomoxetine hydrochloride; Bevacizumab, BioMatrix Flex drug eluting stent, Biphasic insulin aspart, Bortezomib, Bosentan; Caspofungin acetate, Cediranib, Cetuximab, ChimeriVax-Dengue, Choriogonadotropin alfa, Cinacalcet hydrochloride, Cizolirtine citrate, Clofarabine, Cocaine conjugate vaccine, CX-717; Darbepoetin alfa, Dasatinib, Decitabine, Denosumab, Desvenlafaxine succinate, Dexamethasone sodium phosphate, Dienogest, Diphencyprone, Doripenem, DTaP-HepB-IPV, Dutasteride; E-7010, Ecallantide, Ecstasy, Eicosapentaenoic acid/docosahexaenoic acid, Emtricitabine, Enfuvirtide, Erlotinib hydrochloride, Eszopiclone, Etonogestrel/ethinyl estradiol, Etoricoxib, Everolimus, Everolimus-eluting coronary stent EVT-201, Ezetimibe, Ezetimibe/simvastatin; Ferumoxytol, Fesoterodine fumavate, Figitumumab, Filgrastim, Fingolimod hydrochloride, Fluticasone furoate, Fluval P, Fluzone, Fondaparinux sodium, Fulvestrant, Fungichromin; Gamma-hydroxybutyrate sodium, Gefitinib, GHB-01L1, GLY-230, GSK-1349572; Hib-MenCY-TT, Hib-TT, HPV-6/11/16/18, Hydrocodone bitartrate; IC-51, Icatibant acetate, Imatinib mesylate, Immunoglobulin intravenous (human), Indetanib, Influenza A (H1N1) 2009 Monovalent Vaccine, Inhalable human insulin, Insulin glargine, Insulin glulisine, Interferon-beta, Ispinesib mesylate, Ixabepilone; Laromustine, Latanoprost/timolol maleate, L-Citrulline, Lenalidomide, Lexatumumab, Linezolid, Lopinavir/ritonavir, Lutropin alfa; Mapatumumab, MDX-066, MDX-1388, Mepolizumab, Methoxy polyethylene glycol-epoetin-beta, Metreleptin, Micafungin sodium, Mometasone furoate/oxymetazoline hydrochloride, Mx-dnG1, Mycophenolic acid sodium salt; Nabiximols, Natalizumab, Nemonoxacin, Norelgestromin/ethinyl estradiol; Oblimersen sodium, Ocriplasmin, Olmesartan medoxomil, Omacetaxine mepesuccinate; Paclitaxel-eluting stent, Pagoclone, Paliperidone, Panitumumab, Pazopanib hydrochloride, PCV7, Pegaptanib octasodium, Peginterferon alfa-2a, Peginterferon alfa-2b/ ribavirin, Pegvisomant, Pemetrexed disodium, Perifosine, Pimecrolimus, Pitavastatin calcium, Plerixafor hydrochloride, Plitidepsin, Posaconazole, Pregabalin, Progesterone capriate; Raltegravir potassium, Ramucirumab, Ranelic acid distrontium salt, Rasburicase, Recombinant Bet V1, Recombinant human insulin, rhFSH, Rolofylline, Romidepsin, Romiplostim, Rosuvastatin calcium; Sapacitabine, Sevelamer carbonate, Sinecatechins, Sirolimus-eluting stent, Sitagliptin phosphate monohydrate, SN-29244, Sorafenib, Sugammadex sodium, Sunitinib malate; Tadalafil, Tafenoquine, Talnetant, Tanezumab, Tapentadol hydrochloride, Tasocitinib citrate, Technosphere/Insulin, Telcagepant, Tenofovir disoproxil fumarate, Teriparatide, Ticagrelor, Tigecycline, Tiotropium bromide, Tipifarnib, Tocilizumab, TS-041; Ulipristal acetate, Urtoxazumab, Ustekinumab; Vandetanib, Varenicline tartrate, Vicriviroc, Voriconazole, Vorinostat, VRC-HIVADV014-00-VP, VRC-HIVDNA016-00-VP; Zoledronic acid monohydrate. |
| 316 | 20558723 | SchuS4 infection also blocked signals required for macrophage cytokine production, including Akt phosphorylation, IkappaB alpha degradation, and NF-kappaB nuclear localization and activation. |
| 317 | 20558723 | SchuS4 infection also blocked signals required for macrophage cytokine production, including Akt phosphorylation, IkappaB alpha degradation, and NF-kappaB nuclear localization and activation. |
| 318 | 20558723 | Mutation of catalase (katG) sensitized F. tularensis to H(2)O(2) and enhanced PTEN oxidation, Akt phosphorylation, NF-kappaB activation, and inflammatory cytokine production. |
| 319 | 20558723 | Mutation of catalase (katG) sensitized F. tularensis to H(2)O(2) and enhanced PTEN oxidation, Akt phosphorylation, NF-kappaB activation, and inflammatory cytokine production. |
| 320 | 20220087 | Attenuation of PI3K/Akt-mediated tumorigenic signals through PTEN activation by DNA vaccine-induced anti-ErbB2 antibodies. |
| 321 | 20220087 | Attenuation of PI3K/Akt-mediated tumorigenic signals through PTEN activation by DNA vaccine-induced anti-ErbB2 antibodies. |
| 322 | 20220087 | Attenuation of PI3K/Akt-mediated tumorigenic signals through PTEN activation by DNA vaccine-induced anti-ErbB2 antibodies. |
| 323 | 20220087 | To correlate intrinsic mechanisms of Ab action with their tumor-inhibitory potential, first we showed that TUBO cells constitutively express phosphorylated transgenic ErbB2/autochthonous ErbB3 heterodimers and exhibit a basal level of Akt phosphorylation, suggesting a constitutive activation of the PI3K/Akt pathway. |
| 324 | 20220087 | To correlate intrinsic mechanisms of Ab action with their tumor-inhibitory potential, first we showed that TUBO cells constitutively express phosphorylated transgenic ErbB2/autochthonous ErbB3 heterodimers and exhibit a basal level of Akt phosphorylation, suggesting a constitutive activation of the PI3K/Akt pathway. |
| 325 | 20220087 | To correlate intrinsic mechanisms of Ab action with their tumor-inhibitory potential, first we showed that TUBO cells constitutively express phosphorylated transgenic ErbB2/autochthonous ErbB3 heterodimers and exhibit a basal level of Akt phosphorylation, suggesting a constitutive activation of the PI3K/Akt pathway. |
| 326 | 20220087 | Treatment with anti-ErbB2 Abs caused a drastic reduction in the basal level of Akt phosphorylation in the absence of an impairment of PI3K enzymatic activity. |
| 327 | 20220087 | Treatment with anti-ErbB2 Abs caused a drastic reduction in the basal level of Akt phosphorylation in the absence of an impairment of PI3K enzymatic activity. |
| 328 | 20220087 | Treatment with anti-ErbB2 Abs caused a drastic reduction in the basal level of Akt phosphorylation in the absence of an impairment of PI3K enzymatic activity. |
| 329 | 20220087 | In conclusion, vaccine-induced anti-ErbB2 Abs directly affected the transformed phenotype of rat ErbB2(+) tumors by impairing ErbB2-mediated PI3K/Akt signaling. |
| 330 | 20220087 | In conclusion, vaccine-induced anti-ErbB2 Abs directly affected the transformed phenotype of rat ErbB2(+) tumors by impairing ErbB2-mediated PI3K/Akt signaling. |
| 331 | 20220087 | In conclusion, vaccine-induced anti-ErbB2 Abs directly affected the transformed phenotype of rat ErbB2(+) tumors by impairing ErbB2-mediated PI3K/Akt signaling. |
| 332 | 20219876 | To begin to understand the surprising survival of macrophage-specific lipopolysaccharide-induced tumor necrosis factor alpha factor-deficient (macLITAF(-/-)) animals after a lethal dose of lipopolysaccharide (LPS), as reported earlier, the present follow-up study focuses on the role of LITAF in the regulation of inflammatory cytokines secreted in response to lethal or sublethal doses of LPS administered to wild-type (WT) and macLITAF(-/-) mice. |
| 333 | 20219876 | A time course study of kinase expression in peritoneal macrophages revealed increased phosphorylation of prosurvival kinases Akt, Erk1/2, and ribosomal S6 kinase (RSK) in macLITAF(-/-) mice compared to that in WT mice (n = 8), confirming their role in LPS-mediated diseases. macLITAF(-/-) mice (n = 8) survived a lethal dose of LPS plus d-galactosamine (d-GalN), expressing lower serum levels of pro- and anti-inflammatory cytokines than the WT levels. |
| 334 | 20219876 | Our results demonstrate that LITAF deficiency in vivo affects cytokines other than TNF-alpha and influences the balance between the pro- and anti-inflammatory cytokines, which protects the animals from the deleterious effects of an LPS-induced inflammatory response, resulting in a beneficial host regulation of inflammatory cytokines and in enhanced survival. |
| 335 | 20130137 | The PI3K/Akt pathway inhibits influenza A virus-induced Bax-mediated apoptosis by negatively regulating the JNK pathway via ASK1. |
| 336 | 20130137 | The PI3K/Akt pathway inhibits influenza A virus-induced Bax-mediated apoptosis by negatively regulating the JNK pathway via ASK1. |
| 337 | 20130137 | The PI3K/Akt pathway inhibits influenza A virus-induced Bax-mediated apoptosis by negatively regulating the JNK pathway via ASK1. |
| 338 | 20130137 | The PI3K/Akt pathway inhibits influenza A virus-induced Bax-mediated apoptosis by negatively regulating the JNK pathway via ASK1. |
| 339 | 20130137 | It has previously been reported that influenza A virus infection activates the phosphatidylinositol 3-kinase (PI3K)/Akt pathway. |
| 340 | 20130137 | It has previously been reported that influenza A virus infection activates the phosphatidylinositol 3-kinase (PI3K)/Akt pathway. |
| 341 | 20130137 | It has previously been reported that influenza A virus infection activates the phosphatidylinositol 3-kinase (PI3K)/Akt pathway. |
| 342 | 20130137 | It has previously been reported that influenza A virus infection activates the phosphatidylinositol 3-kinase (PI3K)/Akt pathway. |
| 343 | 20130137 | In addition, it has been shown that the mutant influenza A virus PR8-SH3-mf-1, which is unable to activate the PI3K/Akt pathway, is more pro-apoptotic than the wild-type (WT) virus. |
| 344 | 20130137 | In addition, it has been shown that the mutant influenza A virus PR8-SH3-mf-1, which is unable to activate the PI3K/Akt pathway, is more pro-apoptotic than the wild-type (WT) virus. |
| 345 | 20130137 | In addition, it has been shown that the mutant influenza A virus PR8-SH3-mf-1, which is unable to activate the PI3K/Akt pathway, is more pro-apoptotic than the wild-type (WT) virus. |
| 346 | 20130137 | In addition, it has been shown that the mutant influenza A virus PR8-SH3-mf-1, which is unable to activate the PI3K/Akt pathway, is more pro-apoptotic than the wild-type (WT) virus. |
| 347 | 20130137 | Here, it is reported that, although both WT and PR8-SH3-mf-1 viruses induced apoptosis, the PR8-SH3-mf-1 virus consistently showed greater potential to induce mitochondrial membrane disruption, cytochrome c release, and translocation and conformational change of Bax than the WT virus. |
| 348 | 20130137 | Here, it is reported that, although both WT and PR8-SH3-mf-1 viruses induced apoptosis, the PR8-SH3-mf-1 virus consistently showed greater potential to induce mitochondrial membrane disruption, cytochrome c release, and translocation and conformational change of Bax than the WT virus. |
| 349 | 20130137 | Here, it is reported that, although both WT and PR8-SH3-mf-1 viruses induced apoptosis, the PR8-SH3-mf-1 virus consistently showed greater potential to induce mitochondrial membrane disruption, cytochrome c release, and translocation and conformational change of Bax than the WT virus. |
| 350 | 20130137 | Here, it is reported that, although both WT and PR8-SH3-mf-1 viruses induced apoptosis, the PR8-SH3-mf-1 virus consistently showed greater potential to induce mitochondrial membrane disruption, cytochrome c release, and translocation and conformational change of Bax than the WT virus. |
| 351 | 20130137 | Furthermore, the PR8-SH3-mf-1 virus was unable to phosphorylate apoptosis signal-regulating kinase 1 (ASK1) but induced higher levels of c-jun N-terminal kinase (JNK) phosphorylation than the WT virus. |
| 352 | 20130137 | Furthermore, the PR8-SH3-mf-1 virus was unable to phosphorylate apoptosis signal-regulating kinase 1 (ASK1) but induced higher levels of c-jun N-terminal kinase (JNK) phosphorylation than the WT virus. |
| 353 | 20130137 | Furthermore, the PR8-SH3-mf-1 virus was unable to phosphorylate apoptosis signal-regulating kinase 1 (ASK1) but induced higher levels of c-jun N-terminal kinase (JNK) phosphorylation than the WT virus. |
| 354 | 20130137 | Furthermore, the PR8-SH3-mf-1 virus was unable to phosphorylate apoptosis signal-regulating kinase 1 (ASK1) but induced higher levels of c-jun N-terminal kinase (JNK) phosphorylation than the WT virus. |
| 355 | 20130137 | Blocking JNK activity could inhibit virus-induced Bax activation and apoptosis. |
| 356 | 20130137 | Blocking JNK activity could inhibit virus-induced Bax activation and apoptosis. |
| 357 | 20130137 | Blocking JNK activity could inhibit virus-induced Bax activation and apoptosis. |
| 358 | 20130137 | Blocking JNK activity could inhibit virus-induced Bax activation and apoptosis. |
| 359 | 20130137 | These results reveal that, during influenza A virus infection, the PI3K/Akt pathway negatively regulates the JNK pathway via ASK1, thereby inhibiting JNK-dependent, Bax-mediated apoptosis. |
| 360 | 20130137 | These results reveal that, during influenza A virus infection, the PI3K/Akt pathway negatively regulates the JNK pathway via ASK1, thereby inhibiting JNK-dependent, Bax-mediated apoptosis. |
| 361 | 20130137 | These results reveal that, during influenza A virus infection, the PI3K/Akt pathway negatively regulates the JNK pathway via ASK1, thereby inhibiting JNK-dependent, Bax-mediated apoptosis. |
| 362 | 20130137 | These results reveal that, during influenza A virus infection, the PI3K/Akt pathway negatively regulates the JNK pathway via ASK1, thereby inhibiting JNK-dependent, Bax-mediated apoptosis. |
| 363 | 19880213 | Activation of both cell types is associated with the induction of the MAP kinase pathway, the phosphorylation of STAT1, STAT5 and AKT and with transcription factor NF-kappaB activation in vitro and in vivo. |
| 364 | 19346299 | The human epidermal growth factor receptor (HER-2) oncogene encodes a transmembrane tyrosine kinase receptor that has evolved as a major classifier of invasive breast cancer and target of therapy for the disease. |
| 365 | 19346299 | A series of biomarkers potentially associated with resistance to trastuzumab is discussed with emphasis on the phosphatase and tensin homologue deleted on chromosome ten/Akt and insulin-like growth factor receptor pathways. |
| 366 | 19346299 | The efficacy results for the more recently approved small molecule HER-1/HER-2 kinase inhibitor lapatinib are also presented along with a more limited review of markers of resistance for this agent. |
| 367 | 19344189 | Standard treatments and current development of new therapies for malignant gliomas are reviewed, focusing specifically on growth factors and their receptors (e.g. epidermal growth factor receptor, vascular endothelial growth factor receptor, and platelet-derived growth factor receptor), as well as the intracellular effector molecules that are downstream of these growth factors (e.g. |
| 368 | 19344189 | Ras/Raf/mitogen-activated protein kinase, phosphatidylinositol 3-kinase/AKT/mammalian target of rapamycin, and protein kinase C). |
| 369 | 19129452 | E4orf1 has been reported to signal through the phosphatidylinositol 3'-kinase pathway leading to the activation of Akt, mTOR, and p70 S6K. |
| 370 | 19129452 | E4orf1 has been reported to signal through the phosphatidylinositol 3'-kinase pathway leading to the activation of Akt, mTOR, and p70 S6K. |
| 371 | 19129452 | Evidence presented here shows that E4orf1 may also induce the phosphorylation of Akt and p70 S6K in a manner that depends on Rac1 and its guanine nucleotide exchange factor Tiam1. |
| 372 | 19129452 | Evidence presented here shows that E4orf1 may also induce the phosphorylation of Akt and p70 S6K in a manner that depends on Rac1 and its guanine nucleotide exchange factor Tiam1. |
| 373 | 19107122 | Retroviral transfer of a constitutively active form of Akt into the parental tumor significantly increased its resistance against E7-specific CD8(+) T-cell mediated apoptosis. |
| 374 | 19107122 | Retroviral transfer of a constitutively active form of Akt into the parental tumor significantly increased its resistance against E7-specific CD8(+) T-cell mediated apoptosis. |
| 375 | 19107122 | Retroviral transfer of a constitutively active form of Akt into the parental tumor significantly increased its resistance against E7-specific CD8(+) T-cell mediated apoptosis. |
| 376 | 19107122 | We also observed that intratumoral injection of an Akt inhibitor enhanced the therapeutic efficacy of E7-specific vaccine or E7-specific CD8(+) T-cell adoptive transfer against the immune-resistant tumors. |
| 377 | 19107122 | We also observed that intratumoral injection of an Akt inhibitor enhanced the therapeutic efficacy of E7-specific vaccine or E7-specific CD8(+) T-cell adoptive transfer against the immune-resistant tumors. |
| 378 | 19107122 | We also observed that intratumoral injection of an Akt inhibitor enhanced the therapeutic efficacy of E7-specific vaccine or E7-specific CD8(+) T-cell adoptive transfer against the immune-resistant tumors. |
| 379 | 19107122 | Thus, our data indicate that the activation of PI3K/Akt pathway represents a new mechanism of immune escape and has important implications for the development of a novel strategy in cancer immunotherapy against immune-resistant tumor cells. |
| 380 | 19107122 | Thus, our data indicate that the activation of PI3K/Akt pathway represents a new mechanism of immune escape and has important implications for the development of a novel strategy in cancer immunotherapy against immune-resistant tumor cells. |
| 381 | 19107122 | Thus, our data indicate that the activation of PI3K/Akt pathway represents a new mechanism of immune escape and has important implications for the development of a novel strategy in cancer immunotherapy against immune-resistant tumor cells. |
| 382 | 19072345 | Targeted agents against important mitogenic pathways, including MEK/ERK, Src, PI3K/Akt, mTOR, Hedgehog and NF-kappaB, as well as agents targeting histone deacetylase, poly(ADP-ribose) polymerase, heat shock protein 90 and other agents such as beta-lapachone, hold considerable interest for further development. |
| 383 | 18974133 | In human melanoma cells, MFG-E8 knockdown attenuated Akt and Twist signaling and thereby compromised tumor cell survival, EMT, and invasive ability. |
| 384 | 18974133 | MFG-E8-deficient human melanoma cells also showed increased sensitivity to small molecule inhibitors of insulin-like growth factor I receptor and c-Met. |
| 385 | 18948575 | In this study, we showed that direct TLR2-myeloid differentiating factor 88 (MyD88) signaling in CD8 T cells was also required for their efficient clonal expansion by promoting the survival of activated T cells on vaccinia viral infection in vivo. |
| 386 | 18948575 | Furthermore, we observed that direct TLR2 ligation on CD8 T cells promoted CD8 T-cell proliferation and survival in vitro in a manner dependent on the phosphatidylinositol 3-kinase (PI3K)-Akt pathway activation and that activation of Akt controlled memory cell formation in vivo. |
| 387 | 18940265 | Of the 42 HPCF fractions of SEA or SWAP, 26 (61.9%) or 15 (35.7%) showed positive dot blot reaction with RAC vaccinated serum respectively. |
| 388 | 18579606 | Combining confocal microscopy with biochemical analysis and studies of infection requirements using pharmacological inhibitors and small interfering RNAs, we show here that engagement of CD81 activates the Rho GTPase family members Rac, Rho, and Cdc42 and that the block of these signaling pathways drastically reduces HCV infectivity. |
| 389 | 18579606 | Activation of Rho GTPases mediates actin-dependent relocalization of the HCV E2/CD81 complex to cell-cell contact areas where CD81 comes into contact with the tight-junction proteins occludin, ZO-1, and claudin-1, which was recently described as an HCV coreceptor. |
| 390 | 18534979 | Mechanism of influenza A virus NS1 protein interaction with the p85beta, but not the p85alpha, subunit of phosphatidylinositol 3-kinase (PI3K) and up-regulation of PI3K activity. |
| 391 | 18534979 | Influenza A virus infection activates the phosphatidylinositol 3-kinase (PI3K)/Akt pathway by binding influenza A virus NS1 protein to the p85beta regulatory subunit of PI3K. |
| 392 | 18534979 | In this study, we report that NS1 binds to the inter-SH2 (iSH2) domain of p85beta. |
| 393 | 18534979 | Mutational analyses on p85beta iSH2 domain defined that Val-573 is the critical amino acid (AA) that mediates NS1 and p85beta interaction. |
| 394 | 18534979 | In reciprocal gain of function experiments with p85alpha, we demonstrated that mutation to Val at Met-582 leads to NS1 binding and increased PI3K activity. |
| 395 | 18534979 | Molecular modeling based on our experimental results suggested that, in addition to the interaction interface between the NS1 SH3 binding motif 1 (AA 164-167) and p85beta Val-573, AA 137-142 in NS1 might interact with p85beta. |
| 396 | 18534979 | Indeed, mutations of AA 141 and 142 in NS1 disrupted the interaction between NS1 and p85beta. |
| 397 | 18534979 | In contrast, in the mutant virus-infected cells containing mutant NS1 unable to interact with p85beta, the p85beta-associated PI3K activity up-regulation was not seen, suggesting that PI3K up-regulation is dependent upon the interaction between NS1 and p85beta. |
| 398 | 18534979 | Competition experiments and the immunoprecipitation studies demonstrated that NS1, p85beta, and p110 form a complex in cells. |
| 399 | 18534979 | Finally, the mechanism by which binding of NS1 to p85beta regulates PI3K activity was discussed based on a predicted structural model of NS1-p85-p110 complex. |
| 400 | 18463535 | Our results demonstrate that different classes of chemotherapeutic drugs at low nontoxic concentrations regulate activity of Rac, RhoA, and RhoE in murine DC, suggesting that small Rho GTPases might serve as new targets for modulating functional activity of DC vaccines or endogenous DCs in various immunotherapeutic or chemoimmunotherapeutic strategies. |
| 401 | 18177634 | Sphingosine kinase, phosphatidylinositol 3-kinase, Akt, NF-kappaB, and p300 are required for CCL5 production in Mycobacterium bovis Bacillus Calmette-Guérin (BCG)-infected epithelial cells. |
| 402 | 18177634 | Sphingosine kinase, phosphatidylinositol 3-kinase, Akt, NF-kappaB, and p300 are required for CCL5 production in Mycobacterium bovis Bacillus Calmette-Guérin (BCG)-infected epithelial cells. |
| 403 | 18177634 | Sphingosine kinase, phosphatidylinositol 3-kinase, Akt, NF-kappaB, and p300 are required for CCL5 production in Mycobacterium bovis Bacillus Calmette-Guérin (BCG)-infected epithelial cells. |
| 404 | 18177634 | Although NF-kappaB has been implicated, signaling cascades involved in CCL5 production by epithelial cells following infection with Mycobacterium bovis BCG are still not defined. |
| 405 | 18177634 | Although NF-kappaB has been implicated, signaling cascades involved in CCL5 production by epithelial cells following infection with Mycobacterium bovis BCG are still not defined. |
| 406 | 18177634 | Although NF-kappaB has been implicated, signaling cascades involved in CCL5 production by epithelial cells following infection with Mycobacterium bovis BCG are still not defined. |
| 407 | 18177634 | Here we show that using pharmacological inhibition of sphingosine kinase (SPK), striking inhibition of M. bovis BCG-induced CCL5 protein was observed. |
| 408 | 18177634 | Here we show that using pharmacological inhibition of sphingosine kinase (SPK), striking inhibition of M. bovis BCG-induced CCL5 protein was observed. |
| 409 | 18177634 | Here we show that using pharmacological inhibition of sphingosine kinase (SPK), striking inhibition of M. bovis BCG-induced CCL5 protein was observed. |
| 410 | 18177634 | Phosphatidylinositol 3-kinase (PI3K) and Akt were also important for CCL5 production by epithelial cells infected with M. bovis BCG. |
| 411 | 18177634 | Phosphatidylinositol 3-kinase (PI3K) and Akt were also important for CCL5 production by epithelial cells infected with M. bovis BCG. |
| 412 | 18177634 | Phosphatidylinositol 3-kinase (PI3K) and Akt were also important for CCL5 production by epithelial cells infected with M. bovis BCG. |
| 413 | 18177634 | Moreover, there was increased activation of PI3K, IKK/alphabeta and NF-kappaB in A549 cells infected with M. bovis BCG. |
| 414 | 18177634 | Moreover, there was increased activation of PI3K, IKK/alphabeta and NF-kappaB in A549 cells infected with M. bovis BCG. |
| 415 | 18177634 | Moreover, there was increased activation of PI3K, IKK/alphabeta and NF-kappaB in A549 cells infected with M. bovis BCG. |
| 416 | 18177634 | Importantly, the PI3K activation was dependent on SPK. |
| 417 | 18177634 | Importantly, the PI3K activation was dependent on SPK. |
| 418 | 18177634 | Importantly, the PI3K activation was dependent on SPK. |
| 419 | 18177634 | Together, these studies are the first to show that M. bovis BCG-induced CCL5 secretion is dependent on the SPK/PI3K/Akt/NF-kappaB and p300 signaling pathway. |
| 420 | 18177634 | Together, these studies are the first to show that M. bovis BCG-induced CCL5 secretion is dependent on the SPK/PI3K/Akt/NF-kappaB and p300 signaling pathway. |
| 421 | 18177634 | Together, these studies are the first to show that M. bovis BCG-induced CCL5 secretion is dependent on the SPK/PI3K/Akt/NF-kappaB and p300 signaling pathway. |
| 422 | 18160431 | Hepatitis C virus core protein upregulates serine phosphorylation of insulin receptor substrate-1 and impairs the downstream akt/protein kinase B signaling pathway for insulin resistance. |
| 423 | 18160431 | Since we and others have previously observed that HCV core protein activates c-Jun N-terminal kinase (JNK) and mitogen-activated protein kinase, we examined the contribution of these pathways to insulin resistance in hepatocytes. |
| 424 | 18160431 | HCV core protein-mediated Ser(312) phosphorylation of IRS-1 was inhibited by JNK (SP600125) and phosphatidylinositol-3 kinase (LY294002) inhibitors. |
| 425 | 18160431 | Taken together, our results demonstrated that HCV core protein increases IRS-1 phosphorylation at Ser(312) which may contribute in part to the mechanism of insulin resistance. |
| 426 | 17947649 | We further demonstrated that the extent of stimulation, which included both the duration and the levels of antigenic stimulation/costimulation, during priming determined the formation of memory CD8 T cells via controlling the extent of Akt activation, and functional suppression of Akt led to defective CD8 memory formation in vivo. |
| 427 | 17947649 | We further demonstrated that the extent of stimulation, which included both the duration and the levels of antigenic stimulation/costimulation, during priming determined the formation of memory CD8 T cells via controlling the extent of Akt activation, and functional suppression of Akt led to defective CD8 memory formation in vivo. |
| 428 | 17947649 | Collectively, our data suggest that the extent of stimulation controls CD8 memory formation via activation of Akt and may provide important insights into the design of effective vaccines. |
| 429 | 17947649 | Collectively, our data suggest that the extent of stimulation controls CD8 memory formation via activation of Akt and may provide important insights into the design of effective vaccines. |
| 430 | 17881440 | SH3 binding motif 1 in influenza A virus NS1 protein is essential for PI3K/Akt signaling pathway activation. |
| 431 | 17881440 | SH3 binding motif 1 in influenza A virus NS1 protein is essential for PI3K/Akt signaling pathway activation. |
| 432 | 17881440 | SH3 binding motif 1 in influenza A virus NS1 protein is essential for PI3K/Akt signaling pathway activation. |
| 433 | 17881440 | SH3 binding motif 1 in influenza A virus NS1 protein is essential for PI3K/Akt signaling pathway activation. |
| 434 | 17881440 | SH3 binding motif 1 in influenza A virus NS1 protein is essential for PI3K/Akt signaling pathway activation. |
| 435 | 17881440 | Recent studies have demonstrated that influenza A virus infection activates the phosphatidylinositol 3-kinase (PI3K)/Akt signaling pathway by binding of influenza NS1 protein to the p85 regulatory subunit of PI3K. |
| 436 | 17881440 | Recent studies have demonstrated that influenza A virus infection activates the phosphatidylinositol 3-kinase (PI3K)/Akt signaling pathway by binding of influenza NS1 protein to the p85 regulatory subunit of PI3K. |
| 437 | 17881440 | Recent studies have demonstrated that influenza A virus infection activates the phosphatidylinositol 3-kinase (PI3K)/Akt signaling pathway by binding of influenza NS1 protein to the p85 regulatory subunit of PI3K. |
| 438 | 17881440 | Recent studies have demonstrated that influenza A virus infection activates the phosphatidylinositol 3-kinase (PI3K)/Akt signaling pathway by binding of influenza NS1 protein to the p85 regulatory subunit of PI3K. |
| 439 | 17881440 | Recent studies have demonstrated that influenza A virus infection activates the phosphatidylinositol 3-kinase (PI3K)/Akt signaling pathway by binding of influenza NS1 protein to the p85 regulatory subunit of PI3K. |
| 440 | 17881440 | Our previous study proposed that two polyproline motifs in NS1 (amino acids 164 to 167 [PXXP], SH3 binding motif 1, and amino acids 213 to 216 [PPXXP], SH3 binding motif 2) may mediate binding to the p85 subunit of PI3K. |
| 441 | 17881440 | Our previous study proposed that two polyproline motifs in NS1 (amino acids 164 to 167 [PXXP], SH3 binding motif 1, and amino acids 213 to 216 [PPXXP], SH3 binding motif 2) may mediate binding to the p85 subunit of PI3K. |
| 442 | 17881440 | Our previous study proposed that two polyproline motifs in NS1 (amino acids 164 to 167 [PXXP], SH3 binding motif 1, and amino acids 213 to 216 [PPXXP], SH3 binding motif 2) may mediate binding to the p85 subunit of PI3K. |
| 443 | 17881440 | Our previous study proposed that two polyproline motifs in NS1 (amino acids 164 to 167 [PXXP], SH3 binding motif 1, and amino acids 213 to 216 [PPXXP], SH3 binding motif 2) may mediate binding to the p85 subunit of PI3K. |
| 444 | 17881440 | Our previous study proposed that two polyproline motifs in NS1 (amino acids 164 to 167 [PXXP], SH3 binding motif 1, and amino acids 213 to 216 [PPXXP], SH3 binding motif 2) may mediate binding to the p85 subunit of PI3K. |
| 445 | 17881440 | Here we performed individual mutational analyses on these two motifs and demonstrated that SH3 binding motif 1 contributes to the interactions of NS1 with p85beta, whereas SH3 binding motif 2 is not required for this process. |
| 446 | 17881440 | Here we performed individual mutational analyses on these two motifs and demonstrated that SH3 binding motif 1 contributes to the interactions of NS1 with p85beta, whereas SH3 binding motif 2 is not required for this process. |
| 447 | 17881440 | Here we performed individual mutational analyses on these two motifs and demonstrated that SH3 binding motif 1 contributes to the interactions of NS1 with p85beta, whereas SH3 binding motif 2 is not required for this process. |
| 448 | 17881440 | Here we performed individual mutational analyses on these two motifs and demonstrated that SH3 binding motif 1 contributes to the interactions of NS1 with p85beta, whereas SH3 binding motif 2 is not required for this process. |
| 449 | 17881440 | Here we performed individual mutational analyses on these two motifs and demonstrated that SH3 binding motif 1 contributes to the interactions of NS1 with p85beta, whereas SH3 binding motif 2 is not required for this process. |
| 450 | 17881440 | Mutant viruses carrying NS1 with mutations in SH3 binding motif 1 failed to interact with p85beta and induce the subsequent activation of PI3K/Akt pathway. |
| 451 | 17881440 | Mutant viruses carrying NS1 with mutations in SH3 binding motif 1 failed to interact with p85beta and induce the subsequent activation of PI3K/Akt pathway. |
| 452 | 17881440 | Mutant viruses carrying NS1 with mutations in SH3 binding motif 1 failed to interact with p85beta and induce the subsequent activation of PI3K/Akt pathway. |
| 453 | 17881440 | Mutant viruses carrying NS1 with mutations in SH3 binding motif 1 failed to interact with p85beta and induce the subsequent activation of PI3K/Akt pathway. |
| 454 | 17881440 | Mutant viruses carrying NS1 with mutations in SH3 binding motif 1 failed to interact with p85beta and induce the subsequent activation of PI3K/Akt pathway. |
| 455 | 17881440 | Our data suggest that SH3 binding motif 1 in NS1 protein is required for NS1-p85beta interaction and PI3K/Akt activation. |
| 456 | 17881440 | Our data suggest that SH3 binding motif 1 in NS1 protein is required for NS1-p85beta interaction and PI3K/Akt activation. |
| 457 | 17881440 | Our data suggest that SH3 binding motif 1 in NS1 protein is required for NS1-p85beta interaction and PI3K/Akt activation. |
| 458 | 17881440 | Our data suggest that SH3 binding motif 1 in NS1 protein is required for NS1-p85beta interaction and PI3K/Akt activation. |
| 459 | 17881440 | Our data suggest that SH3 binding motif 1 in NS1 protein is required for NS1-p85beta interaction and PI3K/Akt activation. |
| 460 | 17881440 | Activation of PI3K/Akt pathway is beneficial for virus replication by inhibiting virus induced apoptosis through phosphorylation of caspase-9. |
| 461 | 17881440 | Activation of PI3K/Akt pathway is beneficial for virus replication by inhibiting virus induced apoptosis through phosphorylation of caspase-9. |
| 462 | 17881440 | Activation of PI3K/Akt pathway is beneficial for virus replication by inhibiting virus induced apoptosis through phosphorylation of caspase-9. |
| 463 | 17881440 | Activation of PI3K/Akt pathway is beneficial for virus replication by inhibiting virus induced apoptosis through phosphorylation of caspase-9. |
| 464 | 17881440 | Activation of PI3K/Akt pathway is beneficial for virus replication by inhibiting virus induced apoptosis through phosphorylation of caspase-9. |
| 465 | 17325368 | Effect of the phosphatidylinositol 3-kinase/Akt pathway on influenza A virus propagation. |
| 466 | 17325368 | Effect of the phosphatidylinositol 3-kinase/Akt pathway on influenza A virus propagation. |
| 467 | 17325368 | Effect of the phosphatidylinositol 3-kinase/Akt pathway on influenza A virus propagation. |
| 468 | 17325368 | Effect of the phosphatidylinositol 3-kinase/Akt pathway on influenza A virus propagation. |
| 469 | 17325368 | Effect of the phosphatidylinositol 3-kinase/Akt pathway on influenza A virus propagation. |
| 470 | 17325368 | Effect of the phosphatidylinositol 3-kinase/Akt pathway on influenza A virus propagation. |
| 471 | 17325368 | Effect of the phosphatidylinositol 3-kinase/Akt pathway on influenza A virus propagation. |
| 472 | 17325368 | Effect of the phosphatidylinositol 3-kinase/Akt pathway on influenza A virus propagation. |
| 473 | 17325368 | The phosphatidylinositol 3-kinase (PI3K)/Akt signalling pathway has attracted much recent interest due to its central role in modulating diverse downstream signalling pathways associated with cell survival, proliferation, differentiation, morphology and apoptosis. |
| 474 | 17325368 | The phosphatidylinositol 3-kinase (PI3K)/Akt signalling pathway has attracted much recent interest due to its central role in modulating diverse downstream signalling pathways associated with cell survival, proliferation, differentiation, morphology and apoptosis. |
| 475 | 17325368 | The phosphatidylinositol 3-kinase (PI3K)/Akt signalling pathway has attracted much recent interest due to its central role in modulating diverse downstream signalling pathways associated with cell survival, proliferation, differentiation, morphology and apoptosis. |
| 476 | 17325368 | The phosphatidylinositol 3-kinase (PI3K)/Akt signalling pathway has attracted much recent interest due to its central role in modulating diverse downstream signalling pathways associated with cell survival, proliferation, differentiation, morphology and apoptosis. |
| 477 | 17325368 | The phosphatidylinositol 3-kinase (PI3K)/Akt signalling pathway has attracted much recent interest due to its central role in modulating diverse downstream signalling pathways associated with cell survival, proliferation, differentiation, morphology and apoptosis. |
| 478 | 17325368 | The phosphatidylinositol 3-kinase (PI3K)/Akt signalling pathway has attracted much recent interest due to its central role in modulating diverse downstream signalling pathways associated with cell survival, proliferation, differentiation, morphology and apoptosis. |
| 479 | 17325368 | The phosphatidylinositol 3-kinase (PI3K)/Akt signalling pathway has attracted much recent interest due to its central role in modulating diverse downstream signalling pathways associated with cell survival, proliferation, differentiation, morphology and apoptosis. |
| 480 | 17325368 | The phosphatidylinositol 3-kinase (PI3K)/Akt signalling pathway has attracted much recent interest due to its central role in modulating diverse downstream signalling pathways associated with cell survival, proliferation, differentiation, morphology and apoptosis. |
| 481 | 17325368 | An increasing amount of information has demonstrated that many viruses activate the PI3K/Akt pathway to augment their efficient replication. |
| 482 | 17325368 | An increasing amount of information has demonstrated that many viruses activate the PI3K/Akt pathway to augment their efficient replication. |
| 483 | 17325368 | An increasing amount of information has demonstrated that many viruses activate the PI3K/Akt pathway to augment their efficient replication. |
| 484 | 17325368 | An increasing amount of information has demonstrated that many viruses activate the PI3K/Akt pathway to augment their efficient replication. |
| 485 | 17325368 | An increasing amount of information has demonstrated that many viruses activate the PI3K/Akt pathway to augment their efficient replication. |
| 486 | 17325368 | An increasing amount of information has demonstrated that many viruses activate the PI3K/Akt pathway to augment their efficient replication. |
| 487 | 17325368 | An increasing amount of information has demonstrated that many viruses activate the PI3K/Akt pathway to augment their efficient replication. |
| 488 | 17325368 | An increasing amount of information has demonstrated that many viruses activate the PI3K/Akt pathway to augment their efficient replication. |
| 489 | 17325368 | In this study, the effect of the PI3K/Akt signalling pathway on influenza virus propagation was investigated. |
| 490 | 17325368 | In this study, the effect of the PI3K/Akt signalling pathway on influenza virus propagation was investigated. |
| 491 | 17325368 | In this study, the effect of the PI3K/Akt signalling pathway on influenza virus propagation was investigated. |
| 492 | 17325368 | In this study, the effect of the PI3K/Akt signalling pathway on influenza virus propagation was investigated. |
| 493 | 17325368 | In this study, the effect of the PI3K/Akt signalling pathway on influenza virus propagation was investigated. |
| 494 | 17325368 | In this study, the effect of the PI3K/Akt signalling pathway on influenza virus propagation was investigated. |
| 495 | 17325368 | In this study, the effect of the PI3K/Akt signalling pathway on influenza virus propagation was investigated. |
| 496 | 17325368 | In this study, the effect of the PI3K/Akt signalling pathway on influenza virus propagation was investigated. |
| 497 | 17325368 | The PI3K-specific inhibitor LY294002 could suppress Akt phosphorylation, suggesting that influenza A virus-induced Akt phosphorylation is PI3K-dependent. |
| 498 | 17325368 | The PI3K-specific inhibitor LY294002 could suppress Akt phosphorylation, suggesting that influenza A virus-induced Akt phosphorylation is PI3K-dependent. |
| 499 | 17325368 | The PI3K-specific inhibitor LY294002 could suppress Akt phosphorylation, suggesting that influenza A virus-induced Akt phosphorylation is PI3K-dependent. |
| 500 | 17325368 | The PI3K-specific inhibitor LY294002 could suppress Akt phosphorylation, suggesting that influenza A virus-induced Akt phosphorylation is PI3K-dependent. |
| 501 | 17325368 | The PI3K-specific inhibitor LY294002 could suppress Akt phosphorylation, suggesting that influenza A virus-induced Akt phosphorylation is PI3K-dependent. |
| 502 | 17325368 | The PI3K-specific inhibitor LY294002 could suppress Akt phosphorylation, suggesting that influenza A virus-induced Akt phosphorylation is PI3K-dependent. |
| 503 | 17325368 | The PI3K-specific inhibitor LY294002 could suppress Akt phosphorylation, suggesting that influenza A virus-induced Akt phosphorylation is PI3K-dependent. |
| 504 | 17325368 | The PI3K-specific inhibitor LY294002 could suppress Akt phosphorylation, suggesting that influenza A virus-induced Akt phosphorylation is PI3K-dependent. |
| 505 | 17325368 | UV-irradiated influenza virus failed to induce Akt phosphorylation, indicating that viral attachment and entry were not sufficient to trigger PI3K/Akt pathway activation. |
| 506 | 17325368 | UV-irradiated influenza virus failed to induce Akt phosphorylation, indicating that viral attachment and entry were not sufficient to trigger PI3K/Akt pathway activation. |
| 507 | 17325368 | UV-irradiated influenza virus failed to induce Akt phosphorylation, indicating that viral attachment and entry were not sufficient to trigger PI3K/Akt pathway activation. |
| 508 | 17325368 | UV-irradiated influenza virus failed to induce Akt phosphorylation, indicating that viral attachment and entry were not sufficient to trigger PI3K/Akt pathway activation. |
| 509 | 17325368 | UV-irradiated influenza virus failed to induce Akt phosphorylation, indicating that viral attachment and entry were not sufficient to trigger PI3K/Akt pathway activation. |
| 510 | 17325368 | UV-irradiated influenza virus failed to induce Akt phosphorylation, indicating that viral attachment and entry were not sufficient to trigger PI3K/Akt pathway activation. |
| 511 | 17325368 | UV-irradiated influenza virus failed to induce Akt phosphorylation, indicating that viral attachment and entry were not sufficient to trigger PI3K/Akt pathway activation. |
| 512 | 17325368 | UV-irradiated influenza virus failed to induce Akt phosphorylation, indicating that viral attachment and entry were not sufficient to trigger PI3K/Akt pathway activation. |
| 513 | 17325368 | Blockage of PI3K/Akt activation by LY294002 and overexpression of the general receptor for phosphoinositides-1 PH domain (Grp1-PH) led to a reduction in virus yield. |
| 514 | 17325368 | Blockage of PI3K/Akt activation by LY294002 and overexpression of the general receptor for phosphoinositides-1 PH domain (Grp1-PH) led to a reduction in virus yield. |
| 515 | 17325368 | Blockage of PI3K/Akt activation by LY294002 and overexpression of the general receptor for phosphoinositides-1 PH domain (Grp1-PH) led to a reduction in virus yield. |
| 516 | 17325368 | Blockage of PI3K/Akt activation by LY294002 and overexpression of the general receptor for phosphoinositides-1 PH domain (Grp1-PH) led to a reduction in virus yield. |
| 517 | 17325368 | Blockage of PI3K/Akt activation by LY294002 and overexpression of the general receptor for phosphoinositides-1 PH domain (Grp1-PH) led to a reduction in virus yield. |
| 518 | 17325368 | Blockage of PI3K/Akt activation by LY294002 and overexpression of the general receptor for phosphoinositides-1 PH domain (Grp1-PH) led to a reduction in virus yield. |
| 519 | 17325368 | Blockage of PI3K/Akt activation by LY294002 and overexpression of the general receptor for phosphoinositides-1 PH domain (Grp1-PH) led to a reduction in virus yield. |
| 520 | 17325368 | Blockage of PI3K/Akt activation by LY294002 and overexpression of the general receptor for phosphoinositides-1 PH domain (Grp1-PH) led to a reduction in virus yield. |
| 521 | 17325368 | These data suggest that the PI3K/Akt signalling pathway plays a role in influenza virus propagation. |
| 522 | 17325368 | These data suggest that the PI3K/Akt signalling pathway plays a role in influenza virus propagation. |
| 523 | 17325368 | These data suggest that the PI3K/Akt signalling pathway plays a role in influenza virus propagation. |
| 524 | 17325368 | These data suggest that the PI3K/Akt signalling pathway plays a role in influenza virus propagation. |
| 525 | 17325368 | These data suggest that the PI3K/Akt signalling pathway plays a role in influenza virus propagation. |
| 526 | 17325368 | These data suggest that the PI3K/Akt signalling pathway plays a role in influenza virus propagation. |
| 527 | 17325368 | These data suggest that the PI3K/Akt signalling pathway plays a role in influenza virus propagation. |
| 528 | 17325368 | These data suggest that the PI3K/Akt signalling pathway plays a role in influenza virus propagation. |
| 529 | 17170431 | Influenza A virus NS1 protein activates the phosphatidylinositol 3-kinase (PI3K)/Akt pathway by direct interaction with the p85 subunit of PI3K. |
| 530 | 17170431 | Influenza A virus NS1 protein activates the phosphatidylinositol 3-kinase (PI3K)/Akt pathway by direct interaction with the p85 subunit of PI3K. |
| 531 | 17170431 | Influenza A virus NS1 protein activates the phosphatidylinositol 3-kinase (PI3K)/Akt pathway by direct interaction with the p85 subunit of PI3K. |
| 532 | 17170431 | Influenza A virus NS1 protein activates the phosphatidylinositol 3-kinase (PI3K)/Akt pathway by direct interaction with the p85 subunit of PI3K. |
| 533 | 17170431 | Influenza A virus NS1 protein activates the phosphatidylinositol 3-kinase (PI3K)/Akt pathway by direct interaction with the p85 subunit of PI3K. |
| 534 | 17170431 | Influenza A virus infection activates the phosphatidylinositol 3-kinase (PI3K)/Akt pathway, but the mechanism is not clear. |
| 535 | 17170431 | Influenza A virus infection activates the phosphatidylinositol 3-kinase (PI3K)/Akt pathway, but the mechanism is not clear. |
| 536 | 17170431 | Influenza A virus infection activates the phosphatidylinositol 3-kinase (PI3K)/Akt pathway, but the mechanism is not clear. |
| 537 | 17170431 | Influenza A virus infection activates the phosphatidylinositol 3-kinase (PI3K)/Akt pathway, but the mechanism is not clear. |
| 538 | 17170431 | Influenza A virus infection activates the phosphatidylinositol 3-kinase (PI3K)/Akt pathway, but the mechanism is not clear. |
| 539 | 17170431 | Here, it is reported that influenza A virus NS1 protein is responsible for PI3K/Akt pathway activation. |
| 540 | 17170431 | Here, it is reported that influenza A virus NS1 protein is responsible for PI3K/Akt pathway activation. |
| 541 | 17170431 | Here, it is reported that influenza A virus NS1 protein is responsible for PI3K/Akt pathway activation. |
| 542 | 17170431 | Here, it is reported that influenza A virus NS1 protein is responsible for PI3K/Akt pathway activation. |
| 543 | 17170431 | Here, it is reported that influenza A virus NS1 protein is responsible for PI3K/Akt pathway activation. |
| 544 | 17170431 | It was demonstrated that the NS1 protein interacts with the p85 regulatory subunit of PI3K via direct binding to the SH3 and C-terminal SH2 domains of p85. |
| 545 | 17170431 | It was demonstrated that the NS1 protein interacts with the p85 regulatory subunit of PI3K via direct binding to the SH3 and C-terminal SH2 domains of p85. |
| 546 | 17170431 | It was demonstrated that the NS1 protein interacts with the p85 regulatory subunit of PI3K via direct binding to the SH3 and C-terminal SH2 domains of p85. |
| 547 | 17170431 | It was demonstrated that the NS1 protein interacts with the p85 regulatory subunit of PI3K via direct binding to the SH3 and C-terminal SH2 domains of p85. |
| 548 | 17170431 | It was demonstrated that the NS1 protein interacts with the p85 regulatory subunit of PI3K via direct binding to the SH3 and C-terminal SH2 domains of p85. |
| 549 | 17170431 | Mutant virus encoding NS1 protein with mutations in the SH-binding motifs failed to interact with SH domains of p85 and did not activate the PI3K/Akt pathway. |
| 550 | 17170431 | Mutant virus encoding NS1 protein with mutations in the SH-binding motifs failed to interact with SH domains of p85 and did not activate the PI3K/Akt pathway. |
| 551 | 17170431 | Mutant virus encoding NS1 protein with mutations in the SH-binding motifs failed to interact with SH domains of p85 and did not activate the PI3K/Akt pathway. |
| 552 | 17170431 | Mutant virus encoding NS1 protein with mutations in the SH-binding motifs failed to interact with SH domains of p85 and did not activate the PI3K/Akt pathway. |
| 553 | 17170431 | Mutant virus encoding NS1 protein with mutations in the SH-binding motifs failed to interact with SH domains of p85 and did not activate the PI3K/Akt pathway. |
| 554 | 17170431 | Our study has established a novel function of NS1: by interacting with p85 via the SH-binding motifs, NS1 can activate the PI3K/Akt pathway. |
| 555 | 17170431 | Our study has established a novel function of NS1: by interacting with p85 via the SH-binding motifs, NS1 can activate the PI3K/Akt pathway. |
| 556 | 17170431 | Our study has established a novel function of NS1: by interacting with p85 via the SH-binding motifs, NS1 can activate the PI3K/Akt pathway. |
| 557 | 17170431 | Our study has established a novel function of NS1: by interacting with p85 via the SH-binding motifs, NS1 can activate the PI3K/Akt pathway. |
| 558 | 17170431 | Our study has established a novel function of NS1: by interacting with p85 via the SH-binding motifs, NS1 can activate the PI3K/Akt pathway. |
| 559 | 17143278 | Lipopolysaccharide or CD40 signaling stabilizes Akt1, promoting both activation and Bcl-2-dependent survival of DCs. |
| 560 | 17018635 | After screening 3 x 10(6) clones from 3 different cDNA libraries, 15 tumor antigens were identified, including cytokeratin 2-8, glutamyl-prolyl-tRNA synthetase, complement C3, galectin 8, and serine/threonine-rich protein kinase 1. |
| 561 | 17018635 | Multiple proteins involved in the Rho/Rho-associated, coiled coil-containing protein kinase (Rock) signal transduction pathway were found to be immunogenic, including Rock1, Rho/Rac guanine nucleotide exchange factor 2, and schistosoma mansoni adult worm antigen preparation 70. |
| 562 | 16807769 | We employed RNA interference to determine the role of tissue transglutaminase II (TGase II) in motility of cancer cells. |
| 563 | 16807769 | Down-regulation of TGase II by small interfering RNA against TGase II impaired adhesion and motility of HeLa cells by decreasing phosphorylation of the protein kinase, Akt, and reactive oxygen species (ROS). |
| 564 | 16641451 | Herein, we show that SAG induces extracellular signal-regulated kinase 1 (ERK-1) and ERK-2 phosphorylation through phosphoinositide 3-kinase (PI3K), protein kinase C, and Ras activation and p38 mitogen-activated protein kinase (MAPK) phosphorylation through PI3K and Akt activation. |
| 565 | 16641451 | ERK-1 and ERK-2 activation results in an increase in the production of reactive oxygen species (ROS) 3 to 6 h after SAG treatment, while p38 MAPK activation and subsequent tumor necrosis factor alpha release result in the production of nitric oxide (NO) 24 h after SAG treatment. |
| 566 | 16153533 | The hyaluronan-binding protease upregulates ERK1/2 and PI3K/Akt signalling pathways in fibroblasts and stimulates cell proliferation and migration. |
| 567 | 16153533 | The hyaluronan-binding protease upregulates ERK1/2 and PI3K/Akt signalling pathways in fibroblasts and stimulates cell proliferation and migration. |
| 568 | 16153533 | The hyaluronan-binding protease (HABP) is a serine protease in human plasma which is structurally related to plasminogen activators, coagulation factor XII and hepathocyte growth factor activator. |
| 569 | 16153533 | The hyaluronan-binding protease (HABP) is a serine protease in human plasma which is structurally related to plasminogen activators, coagulation factor XII and hepathocyte growth factor activator. |
| 570 | 16153533 | It can in vitro activate the coagulation factor FVII, kininogen and plasminogen activators. |
| 571 | 16153533 | It can in vitro activate the coagulation factor FVII, kininogen and plasminogen activators. |
| 572 | 16153533 | Treatment of lung fibroblasts with HABP lead to a rapid activation of signalling pathways, including the mitogen-activated protein kinase (MAPK) pathway with c-Raf, MEK and ERK1/2. |
| 573 | 16153533 | Treatment of lung fibroblasts with HABP lead to a rapid activation of signalling pathways, including the mitogen-activated protein kinase (MAPK) pathway with c-Raf, MEK and ERK1/2. |
| 574 | 16153533 | Additionally the activation of the PI3K/Akt pathway and of several translation-related proteins was found. |
| 575 | 16153533 | Additionally the activation of the PI3K/Akt pathway and of several translation-related proteins was found. |
| 576 | 16153533 | Stimulation of signalling and proliferation by HABP involved the fibroblast growth factor receptor 1 (FGFR-1). |
| 577 | 16153533 | Stimulation of signalling and proliferation by HABP involved the fibroblast growth factor receptor 1 (FGFR-1). |
| 578 | 16153533 | HABP-stimulated proliferation of lung fibroblasts MRC-5 was accompanied by a significant intracellular increase in basic fibroblast growth factor (bFGF), the major ligand of FGFR-1; bFGF could however not be identified in the supernatant of HABP-treated cells. |
| 579 | 16153533 | HABP-stimulated proliferation of lung fibroblasts MRC-5 was accompanied by a significant intracellular increase in basic fibroblast growth factor (bFGF), the major ligand of FGFR-1; bFGF could however not be identified in the supernatant of HABP-treated cells. |
| 580 | 15879099 | Tat-induced TGF-beta mRNA synthesis is also blocked by the ERK1 inhibitor PD98059, suggesting that ERK1 is needed for TGF-beta production. |
| 581 | 15879099 | Moreover, Tat strongly activates the c-Jun component of the multimolecular complex AP-1, whereas TGF-beta triggers c-Fos and c-Jun. |
| 582 | 15879099 | Of note, treatment of NK cells with PTX-B or PT9K/129G inhibits Tat- and TGF-beta-induced activation of AP-1. |
| 583 | 15879099 | TGF-beta enhances starvation-induced NK cell apoptosis, significantly reduces transcription of the antiapoptotic protein Bcl-2, and inhibits Akt phosphorylation induced by oligomerization of the triggering NK cell receptor NKG2D. |
| 584 | 15879099 | It is of note that in NK cells from patients with early HIV-1 infection, mRNA expression of Bcl-2 and Bcl-x(L) was consistently lower than that in healthy donors; interestingly, TGF-beta and Tat were detected in the sera of these patients. |
| 585 | 15277580 | Immunosuppressive factors, such as vascular endothelial growth factor, transforming growth factor-beta, prostaglandin E2, interleukin (IL)-10, and IL-6, are made frequently by cancer cells. |
| 586 | 15277580 | However, a number of factors appear to be made directly in response to signaling molecules, such as RAS, AKT, and signal transducer and activator of transcription 3, which are activated as a result of genetic events that occur during oncogenesis. |
| 587 | 14680449 | Promising therapeutic targets for cancer metastasis have been identified, including Src, focal adhesion kinase, the integrin receptor, the vascular endothelial growth factor receptor, the epidermal growth factor receptor, Her-2/neu, c-Met, Ras/Rac GTPases, Raf kinase, farnesyl diphosphate synthase (i.e., amino-bisphosphonate therapeutic target) and matrix metalloproteases within the context of their implicated functional roles in cancer growth, invasion, angiogenesis and survival at secondary sites. |
| 588 | 11907644 | This surface contact mediated signal essentially interferes with the propagation of the interleukin 2 receptor signal by blocking the activation of the protein kinase B, also called Akt kinase, both in vitro and after experimental infection. |
| 589 | 11434724 | In vitro tissue culture studies showed that finely ground clinoptilolite inhibits protein kinase B (c-Akt), induces expression of p21WAF1/CIP1 and p27KIP1 tumor suppressor proteins, and blocks cell growth in several cancer cell lines. |