Ignet

Gene Information

Gene symbol: HSPA1A

Gene name: heat shock 70kDa protein 1A

HGNC ID: 5232

Synonyms: HSP70-1

Related Genes

#	Gene Symbol	Number of hits
1	AGT	1 hits
2	AMMECR1	1 hits
3	CAD	1 hits
4	DNAJA2	1 hits
5	GCLC	1 hits
6	HMOX1	1 hits
7	HSF1	1 hits
8	HSPA4L	1 hits
9	HSPB1	1 hits
10	HSPD1	1 hits
11	MAPK14	1 hits
12	MAPK8	1 hits
13	MKS1	1 hits
14	PIK3CA	1 hits
15	PLK1	1 hits
16	SIRT1	1 hits
17	SLK	1 hits
18	TAOK1	1 hits
19	TXN	1 hits
20	WDR73	1 hits
21	WT1	1 hits

Related Sentences

#	PMID	Sentence
1	34831368	The role of the Hsp70 chaperone on the angiotensin II-induced EMT after angiotensin II type 1 receptor (AT₁R) blockage, as a possible molecular target for therapeutic strategy against hypertensive renal damage is discussed.
2	32604897	High-glucose stress initiated stress response by increasing intracellular heat shock protein 70 (Hsp70), sirtuin-1 (Sirt-1), thioredoxin (Trx), glutamate-cysteine ligase (gamma-glutamyl cysteine synthetase; γ-GCS) and heme oxygenase-1 (HO-1) in podocytes by 30-50% compared to untreated cells.
3	32604897	High-glucose stress initiated stress response by increasing intracellular heat shock protein 70 (Hsp70), sirtuin-1 (Sirt-1), thioredoxin (Trx), glutamate-cysteine ligase (gamma-glutamyl cysteine synthetase; γ-GCS) and heme oxygenase-1 (HO-1) in podocytes by 30-50% compared to untreated cells.
4	32604897	High-glucose stress initiated stress response by increasing intracellular heat shock protein 70 (Hsp70), sirtuin-1 (Sirt-1), thioredoxin (Trx), glutamate-cysteine ligase (gamma-glutamyl cysteine synthetase; γ-GCS) and heme oxygenase-1 (HO-1) in podocytes by 30-50% compared to untreated cells.
5	32604897	High-glucose stress initiated stress response by increasing intracellular heat shock protein 70 (Hsp70), sirtuin-1 (Sirt-1), thioredoxin (Trx), glutamate-cysteine ligase (gamma-glutamyl cysteine synthetase; γ-GCS) and heme oxygenase-1 (HO-1) in podocytes by 30-50% compared to untreated cells.
6	32604897	Carnosine (1 mM) also induced a corresponding upregulation of these intracellular stress markers, which was even more prominent compared to glucose for Hsp70 (21%), γ-GCS and HO-1 (13% and 20%, respectively; all p < 0.001).
7	32604897	Carnosine (1 mM) also induced a corresponding upregulation of these intracellular stress markers, which was even more prominent compared to glucose for Hsp70 (21%), γ-GCS and HO-1 (13% and 20%, respectively; all p < 0.001).
8	32604897	Carnosine (1 mM) also induced a corresponding upregulation of these intracellular stress markers, which was even more prominent compared to glucose for Hsp70 (21%), γ-GCS and HO-1 (13% and 20%, respectively; all p < 0.001).
9	32604897	Carnosine (1 mM) also induced a corresponding upregulation of these intracellular stress markers, which was even more prominent compared to glucose for Hsp70 (21%), γ-GCS and HO-1 (13% and 20%, respectively; all p < 0.001).
10	32604897	Co-incubation of carnosine (1 mM) and glucose (25 mM) induced further upregulation of Hsp70 (84%), Sirt-1 (52%), Trx (35%), γ-GCS (90%) and HO-1 (73%) concentrations compared to untreated cells (all p < 0.001).
11	32604897	Co-incubation of carnosine (1 mM) and glucose (25 mM) induced further upregulation of Hsp70 (84%), Sirt-1 (52%), Trx (35%), γ-GCS (90%) and HO-1 (73%) concentrations compared to untreated cells (all p < 0.001).
12	32604897	Co-incubation of carnosine (1 mM) and glucose (25 mM) induced further upregulation of Hsp70 (84%), Sirt-1 (52%), Trx (35%), γ-GCS (90%) and HO-1 (73%) concentrations compared to untreated cells (all p < 0.001).
13	32604897	Co-incubation of carnosine (1 mM) and glucose (25 mM) induced further upregulation of Hsp70 (84%), Sirt-1 (52%), Trx (35%), γ-GCS (90%) and HO-1 (73%) concentrations compared to untreated cells (all p < 0.001).
14	32604897	Although podocytes tolerated high carnosine concentrations (10 mM), high carnosine levels only slightly increased Trx and γ-GCS (10% and 19%, respectively, compared to controls; p < 0.001), but not Hsp70, Sirt-1 and HO-1 proteins (p not significant), and did not modify the glucose-induced oxidative stress response.
15	32604897	Although podocytes tolerated high carnosine concentrations (10 mM), high carnosine levels only slightly increased Trx and γ-GCS (10% and 19%, respectively, compared to controls; p < 0.001), but not Hsp70, Sirt-1 and HO-1 proteins (p not significant), and did not modify the glucose-induced oxidative stress response.
16	32604897	Although podocytes tolerated high carnosine concentrations (10 mM), high carnosine levels only slightly increased Trx and γ-GCS (10% and 19%, respectively, compared to controls; p < 0.001), but not Hsp70, Sirt-1 and HO-1 proteins (p not significant), and did not modify the glucose-induced oxidative stress response.
17	32604897	Although podocytes tolerated high carnosine concentrations (10 mM), high carnosine levels only slightly increased Trx and γ-GCS (10% and 19%, respectively, compared to controls; p < 0.001), but not Hsp70, Sirt-1 and HO-1 proteins (p not significant), and did not modify the glucose-induced oxidative stress response.
18	27216364	Ste20-like kinase, SLK, activates the heat shock factor 1 - Hsp70 pathway.
19	27216364	Ste20-like kinase, SLK, activates the heat shock factor 1 - Hsp70 pathway.
20	27216364	Ste20-like kinase, SLK, activates the heat shock factor 1 - Hsp70 pathway.
21	27216364	Ste20-like kinase, SLK, activates the heat shock factor 1 - Hsp70 pathway.
22	27216364	Ste20-like kinase, SLK, activates the heat shock factor 1 - Hsp70 pathway.
23	27216364	Ste20-like kinase, SLK, activates the heat shock factor 1 - Hsp70 pathway.
24	27216364	Ste20-like kinase, SLK, activates the heat shock factor 1 - Hsp70 pathway.
25	27216364	Ste20-like kinase, SLK, activates the heat shock factor 1 - Hsp70 pathway.
26	27216364	Ste20-like kinase, SLK, activates the heat shock factor 1 - Hsp70 pathway.
27	27216364	Ste20-like kinase, SLK, activates the heat shock factor 1 - Hsp70 pathway.
28	27216364	When highly expressed, SLK signals via c-Jun N-terminal kinase and p38 to induce apoptosis, and it exacerbates apoptosis induced by ischemia-reperfusion injury.
29	27216364	When highly expressed, SLK signals via c-Jun N-terminal kinase and p38 to induce apoptosis, and it exacerbates apoptosis induced by ischemia-reperfusion injury.
30	27216364	When highly expressed, SLK signals via c-Jun N-terminal kinase and p38 to induce apoptosis, and it exacerbates apoptosis induced by ischemia-reperfusion injury.
31	27216364	When highly expressed, SLK signals via c-Jun N-terminal kinase and p38 to induce apoptosis, and it exacerbates apoptosis induced by ischemia-reperfusion injury.
32	27216364	When highly expressed, SLK signals via c-Jun N-terminal kinase and p38 to induce apoptosis, and it exacerbates apoptosis induced by ischemia-reperfusion injury.
33	27216364	When highly expressed, SLK signals via c-Jun N-terminal kinase and p38 to induce apoptosis, and it exacerbates apoptosis induced by ischemia-reperfusion injury.
34	27216364	When highly expressed, SLK signals via c-Jun N-terminal kinase and p38 to induce apoptosis, and it exacerbates apoptosis induced by ischemia-reperfusion injury.
35	27216364	When highly expressed, SLK signals via c-Jun N-terminal kinase and p38 to induce apoptosis, and it exacerbates apoptosis induced by ischemia-reperfusion injury.
36	27216364	When highly expressed, SLK signals via c-Jun N-terminal kinase and p38 to induce apoptosis, and it exacerbates apoptosis induced by ischemia-reperfusion injury.
37	27216364	When highly expressed, SLK signals via c-Jun N-terminal kinase and p38 to induce apoptosis, and it exacerbates apoptosis induced by ischemia-reperfusion injury.
38	27216364	We address the interaction of SLK with the heat shock factor 1 (HSF1)-Hsp70 pathway.
39	27216364	We address the interaction of SLK with the heat shock factor 1 (HSF1)-Hsp70 pathway.
40	27216364	We address the interaction of SLK with the heat shock factor 1 (HSF1)-Hsp70 pathway.
41	27216364	We address the interaction of SLK with the heat shock factor 1 (HSF1)-Hsp70 pathway.
42	27216364	We address the interaction of SLK with the heat shock factor 1 (HSF1)-Hsp70 pathway.
43	27216364	We address the interaction of SLK with the heat shock factor 1 (HSF1)-Hsp70 pathway.
44	27216364	We address the interaction of SLK with the heat shock factor 1 (HSF1)-Hsp70 pathway.
45	27216364	We address the interaction of SLK with the heat shock factor 1 (HSF1)-Hsp70 pathway.
46	27216364	We address the interaction of SLK with the heat shock factor 1 (HSF1)-Hsp70 pathway.
47	27216364	We address the interaction of SLK with the heat shock factor 1 (HSF1)-Hsp70 pathway.
48	27216364	Increased expression of SLK in GECs (following transfection) induced HSF1 transcriptional activity.
49	27216364	Increased expression of SLK in GECs (following transfection) induced HSF1 transcriptional activity.
50	27216364	Increased expression of SLK in GECs (following transfection) induced HSF1 transcriptional activity.
51	27216364	Increased expression of SLK in GECs (following transfection) induced HSF1 transcriptional activity.
52	27216364	Increased expression of SLK in GECs (following transfection) induced HSF1 transcriptional activity.
53	27216364	Increased expression of SLK in GECs (following transfection) induced HSF1 transcriptional activity.
54	27216364	Increased expression of SLK in GECs (following transfection) induced HSF1 transcriptional activity.
55	27216364	Increased expression of SLK in GECs (following transfection) induced HSF1 transcriptional activity.
56	27216364	Increased expression of SLK in GECs (following transfection) induced HSF1 transcriptional activity.
57	27216364	Increased expression of SLK in GECs (following transfection) induced HSF1 transcriptional activity.
58	27216364	Moreover, HSF1 transcriptional activity was increased by in vitro ischemia-reperfusion injury (chemical anoxia/recovery) and heat shock, and in both instances was amplified further by SLK overexpression.
59	27216364	Moreover, HSF1 transcriptional activity was increased by in vitro ischemia-reperfusion injury (chemical anoxia/recovery) and heat shock, and in both instances was amplified further by SLK overexpression.
60	27216364	Moreover, HSF1 transcriptional activity was increased by in vitro ischemia-reperfusion injury (chemical anoxia/recovery) and heat shock, and in both instances was amplified further by SLK overexpression.
61	27216364	Moreover, HSF1 transcriptional activity was increased by in vitro ischemia-reperfusion injury (chemical anoxia/recovery) and heat shock, and in both instances was amplified further by SLK overexpression.
62	27216364	Moreover, HSF1 transcriptional activity was increased by in vitro ischemia-reperfusion injury (chemical anoxia/recovery) and heat shock, and in both instances was amplified further by SLK overexpression.
63	27216364	Moreover, HSF1 transcriptional activity was increased by in vitro ischemia-reperfusion injury (chemical anoxia/recovery) and heat shock, and in both instances was amplified further by SLK overexpression.
64	27216364	Moreover, HSF1 transcriptional activity was increased by in vitro ischemia-reperfusion injury (chemical anoxia/recovery) and heat shock, and in both instances was amplified further by SLK overexpression.
65	27216364	Moreover, HSF1 transcriptional activity was increased by in vitro ischemia-reperfusion injury (chemical anoxia/recovery) and heat shock, and in both instances was amplified further by SLK overexpression.
66	27216364	Moreover, HSF1 transcriptional activity was increased by in vitro ischemia-reperfusion injury (chemical anoxia/recovery) and heat shock, and in both instances was amplified further by SLK overexpression.
67	27216364	Moreover, HSF1 transcriptional activity was increased by in vitro ischemia-reperfusion injury (chemical anoxia/recovery) and heat shock, and in both instances was amplified further by SLK overexpression.
68	27216364	HSF1 binds to promoters of target genes, such as Hsp70 and induces their transcription.
69	27216364	HSF1 binds to promoters of target genes, such as Hsp70 and induces their transcription.
70	27216364	HSF1 binds to promoters of target genes, such as Hsp70 and induces their transcription.
71	27216364	HSF1 binds to promoters of target genes, such as Hsp70 and induces their transcription.
72	27216364	HSF1 binds to promoters of target genes, such as Hsp70 and induces their transcription.
73	27216364	HSF1 binds to promoters of target genes, such as Hsp70 and induces their transcription.
74	27216364	HSF1 binds to promoters of target genes, such as Hsp70 and induces their transcription.
75	27216364	HSF1 binds to promoters of target genes, such as Hsp70 and induces their transcription.
76	27216364	HSF1 binds to promoters of target genes, such as Hsp70 and induces their transcription.
77	27216364	HSF1 binds to promoters of target genes, such as Hsp70 and induces their transcription.
78	27216364	By analogy to HSF1, SLK stimulated Hsp70 expression.
79	27216364	By analogy to HSF1, SLK stimulated Hsp70 expression.
80	27216364	By analogy to HSF1, SLK stimulated Hsp70 expression.
81	27216364	By analogy to HSF1, SLK stimulated Hsp70 expression.
82	27216364	By analogy to HSF1, SLK stimulated Hsp70 expression.
83	27216364	By analogy to HSF1, SLK stimulated Hsp70 expression.
84	27216364	By analogy to HSF1, SLK stimulated Hsp70 expression.
85	27216364	By analogy to HSF1, SLK stimulated Hsp70 expression.
86	27216364	By analogy to HSF1, SLK stimulated Hsp70 expression.
87	27216364	By analogy to HSF1, SLK stimulated Hsp70 expression.
88	27216364	Hsp70 was also enhanced by anoxia/recovery and was further amplified by SLK overexpression.
89	27216364	Hsp70 was also enhanced by anoxia/recovery and was further amplified by SLK overexpression.
90	27216364	Hsp70 was also enhanced by anoxia/recovery and was further amplified by SLK overexpression.
91	27216364	Hsp70 was also enhanced by anoxia/recovery and was further amplified by SLK overexpression.
92	27216364	Hsp70 was also enhanced by anoxia/recovery and was further amplified by SLK overexpression.
93	27216364	Hsp70 was also enhanced by anoxia/recovery and was further amplified by SLK overexpression.
94	27216364	Hsp70 was also enhanced by anoxia/recovery and was further amplified by SLK overexpression.
95	27216364	Hsp70 was also enhanced by anoxia/recovery and was further amplified by SLK overexpression.
96	27216364	Hsp70 was also enhanced by anoxia/recovery and was further amplified by SLK overexpression.
97	27216364	Hsp70 was also enhanced by anoxia/recovery and was further amplified by SLK overexpression.
98	27216364	Induction of HSF1 and Hsp70 was dependent on the kinase activity of SLK, and was mediated via polo-like kinase-1.
99	27216364	Induction of HSF1 and Hsp70 was dependent on the kinase activity of SLK, and was mediated via polo-like kinase-1.
100	27216364	Induction of HSF1 and Hsp70 was dependent on the kinase activity of SLK, and was mediated via polo-like kinase-1.
101	27216364	Induction of HSF1 and Hsp70 was dependent on the kinase activity of SLK, and was mediated via polo-like kinase-1.
102	27216364	Induction of HSF1 and Hsp70 was dependent on the kinase activity of SLK, and was mediated via polo-like kinase-1.
103	27216364	Induction of HSF1 and Hsp70 was dependent on the kinase activity of SLK, and was mediated via polo-like kinase-1.
104	27216364	Induction of HSF1 and Hsp70 was dependent on the kinase activity of SLK, and was mediated via polo-like kinase-1.
105	27216364	Induction of HSF1 and Hsp70 was dependent on the kinase activity of SLK, and was mediated via polo-like kinase-1.
106	27216364	Induction of HSF1 and Hsp70 was dependent on the kinase activity of SLK, and was mediated via polo-like kinase-1.
107	27216364	Induction of HSF1 and Hsp70 was dependent on the kinase activity of SLK, and was mediated via polo-like kinase-1.
108	27216364	Transfection of constitutively active HSF1 enhanced Hsp70 expression and inhibited SLK-induced apoptosis.
109	27216364	Transfection of constitutively active HSF1 enhanced Hsp70 expression and inhibited SLK-induced apoptosis.
110	27216364	Transfection of constitutively active HSF1 enhanced Hsp70 expression and inhibited SLK-induced apoptosis.
111	27216364	Transfection of constitutively active HSF1 enhanced Hsp70 expression and inhibited SLK-induced apoptosis.
112	27216364	Transfection of constitutively active HSF1 enhanced Hsp70 expression and inhibited SLK-induced apoptosis.
113	27216364	Transfection of constitutively active HSF1 enhanced Hsp70 expression and inhibited SLK-induced apoptosis.
114	27216364	Transfection of constitutively active HSF1 enhanced Hsp70 expression and inhibited SLK-induced apoptosis.
115	27216364	Transfection of constitutively active HSF1 enhanced Hsp70 expression and inhibited SLK-induced apoptosis.
116	27216364	Transfection of constitutively active HSF1 enhanced Hsp70 expression and inhibited SLK-induced apoptosis.
117	27216364	Transfection of constitutively active HSF1 enhanced Hsp70 expression and inhibited SLK-induced apoptosis.
118	27216364	Conversely, the proapoptotic action of SLK was augmented by HSF1 shRNA, or the Hsp70 inhibitor, pifithrin-μ.
119	27216364	Conversely, the proapoptotic action of SLK was augmented by HSF1 shRNA, or the Hsp70 inhibitor, pifithrin-μ.
120	27216364	Conversely, the proapoptotic action of SLK was augmented by HSF1 shRNA, or the Hsp70 inhibitor, pifithrin-μ.
121	27216364	Conversely, the proapoptotic action of SLK was augmented by HSF1 shRNA, or the Hsp70 inhibitor, pifithrin-μ.
122	27216364	Conversely, the proapoptotic action of SLK was augmented by HSF1 shRNA, or the Hsp70 inhibitor, pifithrin-μ.
123	27216364	Conversely, the proapoptotic action of SLK was augmented by HSF1 shRNA, or the Hsp70 inhibitor, pifithrin-μ.
124	27216364	Conversely, the proapoptotic action of SLK was augmented by HSF1 shRNA, or the Hsp70 inhibitor, pifithrin-μ.
125	27216364	Conversely, the proapoptotic action of SLK was augmented by HSF1 shRNA, or the Hsp70 inhibitor, pifithrin-μ.
126	27216364	Conversely, the proapoptotic action of SLK was augmented by HSF1 shRNA, or the Hsp70 inhibitor, pifithrin-μ.
127	27216364	Conversely, the proapoptotic action of SLK was augmented by HSF1 shRNA, or the Hsp70 inhibitor, pifithrin-μ.
128	27216364	In conclusion, increased expression/activity of SLK activates the HSF1-Hsp70 pathway.
129	27216364	In conclusion, increased expression/activity of SLK activates the HSF1-Hsp70 pathway.
130	27216364	In conclusion, increased expression/activity of SLK activates the HSF1-Hsp70 pathway.
131	27216364	In conclusion, increased expression/activity of SLK activates the HSF1-Hsp70 pathway.
132	27216364	In conclusion, increased expression/activity of SLK activates the HSF1-Hsp70 pathway.
133	27216364	In conclusion, increased expression/activity of SLK activates the HSF1-Hsp70 pathway.
134	27216364	In conclusion, increased expression/activity of SLK activates the HSF1-Hsp70 pathway.
135	27216364	In conclusion, increased expression/activity of SLK activates the HSF1-Hsp70 pathway.
136	27216364	In conclusion, increased expression/activity of SLK activates the HSF1-Hsp70 pathway.
137	27216364	In conclusion, increased expression/activity of SLK activates the HSF1-Hsp70 pathway.
138	27216364	Hsp70 attenuates the primary proapoptotic effect of SLK.
139	27216364	Hsp70 attenuates the primary proapoptotic effect of SLK.
140	27216364	Hsp70 attenuates the primary proapoptotic effect of SLK.
141	27216364	Hsp70 attenuates the primary proapoptotic effect of SLK.
142	27216364	Hsp70 attenuates the primary proapoptotic effect of SLK.
143	27216364	Hsp70 attenuates the primary proapoptotic effect of SLK.
144	27216364	Hsp70 attenuates the primary proapoptotic effect of SLK.
145	27216364	Hsp70 attenuates the primary proapoptotic effect of SLK.
146	27216364	Hsp70 attenuates the primary proapoptotic effect of SLK.
147	27216364	Hsp70 attenuates the primary proapoptotic effect of SLK.
148	26070982	It is concentrated at mitotic microtubules and interacts with α-, β-, and γ-tubulin, heat shock proteins 70 and 90 (HSP-70; HSP-90), and the carbamoyl phosphate synthetase 2/aspartate transcarbamylase/dihydroorotase multi-enzyme complex.
149	26070982	It is concentrated at mitotic microtubules and interacts with α-, β-, and γ-tubulin, heat shock proteins 70 and 90 (HSP-70; HSP-90), and the carbamoyl phosphate synthetase 2/aspartate transcarbamylase/dihydroorotase multi-enzyme complex.
150	26070982	Recombinant WDR73 p.Phe296Leufs26 and p.Arg256Profs18 proteins are truncated, unstable, and show increased interaction with α- and β-tubulin and HSP-70/HSP-90.
151	26070982	Recombinant WDR73 p.Phe296Leufs26 and p.Arg256Profs18 proteins are truncated, unstable, and show increased interaction with α- and β-tubulin and HSP-70/HSP-90.
152	22937108	Alport syndrome is a hereditary glomerulopathy with proteinuria and nephritis caused by defects in genes encoding type IV collagen in the glomerular basement membrane.
153	22937108	Alport syndrome is a hereditary glomerulopathy with proteinuria and nephritis caused by defects in genes encoding type IV collagen in the glomerular basement membrane.
154	22937108	Here we showed that combination treatment of mild electrical stress (MES) and heat stress (HS) ameliorated progressive proteinuria and renal injury in mouse model of Alport syndrome.
155	22937108	Here we showed that combination treatment of mild electrical stress (MES) and heat stress (HS) ameliorated progressive proteinuria and renal injury in mouse model of Alport syndrome.
156	22937108	The expressions of kidney injury marker neutrophil gelatinase-associated lipocalin and pro-inflammatory cytokines interleukin-6, tumor necrosis factor-α and interleukin-1β were suppressed by MES+HS treatment.
157	22937108	The expressions of kidney injury marker neutrophil gelatinase-associated lipocalin and pro-inflammatory cytokines interleukin-6, tumor necrosis factor-α and interleukin-1β were suppressed by MES+HS treatment.
158	22937108	The anti-proteinuric effect of MES+HS treatment is mediated by podocytic activation of phosphatidylinositol 3-OH kinase (PI3K)-Akt and heat shock protein 72 (Hsp72)-dependent pathways in vitro and in vivo.
159	22937108	The anti-proteinuric effect of MES+HS treatment is mediated by podocytic activation of phosphatidylinositol 3-OH kinase (PI3K)-Akt and heat shock protein 72 (Hsp72)-dependent pathways in vitro and in vivo.
160	22937108	The anti-inflammatory effect of MES+HS was mediated by glomerular activation of c-jun NH(2)-terminal kinase 1/2 (JNK1/2) and p38-dependent pathways ex vivo.
161	22937108	The anti-inflammatory effect of MES+HS was mediated by glomerular activation of c-jun NH(2)-terminal kinase 1/2 (JNK1/2) and p38-dependent pathways ex vivo.
162	22937108	Collectively, our studies show that combination treatment of MES and HS confers anti-proteinuric and anti-inflammatory effects on Alport mice likely through the activation of multiple signaling pathways including PI3K-Akt, Hsp72, JNK1/2, and p38 pathways, providing a novel candidate therapeutic strategy to decelerate the progression of patho-phenotypes in Alport syndrome.
163	22937108	Collectively, our studies show that combination treatment of MES and HS confers anti-proteinuric and anti-inflammatory effects on Alport mice likely through the activation of multiple signaling pathways including PI3K-Akt, Hsp72, JNK1/2, and p38 pathways, providing a novel candidate therapeutic strategy to decelerate the progression of patho-phenotypes in Alport syndrome.
164	18922888	Heat shock protein (HSP) HSP27, HSP60, HSP70, and HSP90 are induced by cellular stresses and play a key role in cytoprotection.
165	18922888	Heat shock protein (HSP) HSP27, HSP60, HSP70, and HSP90 are induced by cellular stresses and play a key role in cytoprotection.
166	18922888	Heat shock protein (HSP) HSP27, HSP60, HSP70, and HSP90 are induced by cellular stresses and play a key role in cytoprotection.
167	18922888	Heat shock protein (HSP) HSP27, HSP60, HSP70, and HSP90 are induced by cellular stresses and play a key role in cytoprotection.
168	18922888	We studied both the expression and the phosphorylation state of HSP27, HSP60, HSP70, and HSP90 in vivo in rats made diabetic with streptozotocin and in vitro in mesangial cells and podocytes exposed to either high glucose or mechanical stretch.
169	18922888	We studied both the expression and the phosphorylation state of HSP27, HSP60, HSP70, and HSP90 in vivo in rats made diabetic with streptozotocin and in vitro in mesangial cells and podocytes exposed to either high glucose or mechanical stretch.
170	18922888	We studied both the expression and the phosphorylation state of HSP27, HSP60, HSP70, and HSP90 in vivo in rats made diabetic with streptozotocin and in vitro in mesangial cells and podocytes exposed to either high glucose or mechanical stretch.
171	18922888	We studied both the expression and the phosphorylation state of HSP27, HSP60, HSP70, and HSP90 in vivo in rats made diabetic with streptozotocin and in vitro in mesangial cells and podocytes exposed to either high glucose or mechanical stretch.
172	18922888	Immunohistochemical analysis revealed an overexpression of HSP25, HSP60, and HSP72 in the diabetic outer medulla, whereas no differences were seen in the glomeruli.
173	18922888	Immunohistochemical analysis revealed an overexpression of HSP25, HSP60, and HSP72 in the diabetic outer medulla, whereas no differences were seen in the glomeruli.
174	18922888	Immunohistochemical analysis revealed an overexpression of HSP25, HSP60, and HSP72 in the diabetic outer medulla, whereas no differences were seen in the glomeruli.
175	18922888	Immunohistochemical analysis revealed an overexpression of HSP25, HSP60, and HSP72 in the diabetic outer medulla, whereas no differences were seen in the glomeruli.
176	18922888	In conclusion, diabetes and diabetes-related insults differentially modulate HSP27, HSP60, and HSP70 expression/phosphorylation in the glomeruli and in the medulla, and this may affect the ability of renal cells to mount an effective cytoprotective response.
177	18922888	In conclusion, diabetes and diabetes-related insults differentially modulate HSP27, HSP60, and HSP70 expression/phosphorylation in the glomeruli and in the medulla, and this may affect the ability of renal cells to mount an effective cytoprotective response.
178	18922888	In conclusion, diabetes and diabetes-related insults differentially modulate HSP27, HSP60, and HSP70 expression/phosphorylation in the glomeruli and in the medulla, and this may affect the ability of renal cells to mount an effective cytoprotective response.
179	18922888	In conclusion, diabetes and diabetes-related insults differentially modulate HSP27, HSP60, and HSP70 expression/phosphorylation in the glomeruli and in the medulla, and this may affect the ability of renal cells to mount an effective cytoprotective response.
180	10919839	HSP72 and the osmotic stress protein 94 (Osp94) appear to participate in the adaptation of medullary cells to high extracellular salt and urea concentrations; the small HSPs (HSP25/27 and crystallins) may be involved in the function of mesangial cells and podocytes and contribute to the volume-regulatory remodeling of the cytoskeleton in medullary cells during changes in extracellular tonicity.
181	9553041	Inhibition of cellular proliferation by the Wilms tumor suppressor WT1 requires association with the inducible chaperone Hsp70.
182	9553041	Inhibition of cellular proliferation by the Wilms tumor suppressor WT1 requires association with the inducible chaperone Hsp70.
183	9553041	Inhibition of cellular proliferation by the Wilms tumor suppressor WT1 requires association with the inducible chaperone Hsp70.
184	9553041	Inhibition of cellular proliferation by the Wilms tumor suppressor WT1 requires association with the inducible chaperone Hsp70.
185	9553041	Inhibition of cellular proliferation by the Wilms tumor suppressor WT1 requires association with the inducible chaperone Hsp70.
186	9553041	Inhibition of cellular proliferation by the Wilms tumor suppressor WT1 requires association with the inducible chaperone Hsp70.
187	9553041	Inhibition of cellular proliferation by the Wilms tumor suppressor WT1 requires association with the inducible chaperone Hsp70.
188	9553041	By immunoprecipitation and protein microsequencing analysis, we have identified a major cellular protein associated with endogenous WT1 to be the inducible chaperone Hsp70.
189	9553041	By immunoprecipitation and protein microsequencing analysis, we have identified a major cellular protein associated with endogenous WT1 to be the inducible chaperone Hsp70.
190	9553041	By immunoprecipitation and protein microsequencing analysis, we have identified a major cellular protein associated with endogenous WT1 to be the inducible chaperone Hsp70.
191	9553041	By immunoprecipitation and protein microsequencing analysis, we have identified a major cellular protein associated with endogenous WT1 to be the inducible chaperone Hsp70.
192	9553041	By immunoprecipitation and protein microsequencing analysis, we have identified a major cellular protein associated with endogenous WT1 to be the inducible chaperone Hsp70.
193	9553041	By immunoprecipitation and protein microsequencing analysis, we have identified a major cellular protein associated with endogenous WT1 to be the inducible chaperone Hsp70.
194	9553041	By immunoprecipitation and protein microsequencing analysis, we have identified a major cellular protein associated with endogenous WT1 to be the inducible chaperone Hsp70.
195	9553041	WT1 and Hsp70 are physically associated in embryonic rat kidney cells, in primary Wilms tumor specimens and in cultured cells with inducible expression of WT1.
196	9553041	WT1 and Hsp70 are physically associated in embryonic rat kidney cells, in primary Wilms tumor specimens and in cultured cells with inducible expression of WT1.
197	9553041	WT1 and Hsp70 are physically associated in embryonic rat kidney cells, in primary Wilms tumor specimens and in cultured cells with inducible expression of WT1.
198	9553041	WT1 and Hsp70 are physically associated in embryonic rat kidney cells, in primary Wilms tumor specimens and in cultured cells with inducible expression of WT1.
199	9553041	WT1 and Hsp70 are physically associated in embryonic rat kidney cells, in primary Wilms tumor specimens and in cultured cells with inducible expression of WT1.
200	9553041	WT1 and Hsp70 are physically associated in embryonic rat kidney cells, in primary Wilms tumor specimens and in cultured cells with inducible expression of WT1.
201	9553041	WT1 and Hsp70 are physically associated in embryonic rat kidney cells, in primary Wilms tumor specimens and in cultured cells with inducible expression of WT1.
202	9553041	Colocalization of WT1 and Hsp70 is evident within podocytes of the developing kidney, and Hsp70 is recruited to the characteristic subnuclear clusters that contain WT1.
203	9553041	Colocalization of WT1 and Hsp70 is evident within podocytes of the developing kidney, and Hsp70 is recruited to the characteristic subnuclear clusters that contain WT1.
204	9553041	Colocalization of WT1 and Hsp70 is evident within podocytes of the developing kidney, and Hsp70 is recruited to the characteristic subnuclear clusters that contain WT1.
205	9553041	Colocalization of WT1 and Hsp70 is evident within podocytes of the developing kidney, and Hsp70 is recruited to the characteristic subnuclear clusters that contain WT1.
206	9553041	Colocalization of WT1 and Hsp70 is evident within podocytes of the developing kidney, and Hsp70 is recruited to the characteristic subnuclear clusters that contain WT1.
207	9553041	Colocalization of WT1 and Hsp70 is evident within podocytes of the developing kidney, and Hsp70 is recruited to the characteristic subnuclear clusters that contain WT1.
208	9553041	Colocalization of WT1 and Hsp70 is evident within podocytes of the developing kidney, and Hsp70 is recruited to the characteristic subnuclear clusters that contain WT1.
209	9553041	The amino-terminal transactivation domain of WT1 is required for binding to Hsp70, and expression of that domain itself is sufficient to induce expression of Hsp70 through the heat shock element (HSE).
210	9553041	The amino-terminal transactivation domain of WT1 is required for binding to Hsp70, and expression of that domain itself is sufficient to induce expression of Hsp70 through the heat shock element (HSE).
211	9553041	The amino-terminal transactivation domain of WT1 is required for binding to Hsp70, and expression of that domain itself is sufficient to induce expression of Hsp70 through the heat shock element (HSE).
212	9553041	The amino-terminal transactivation domain of WT1 is required for binding to Hsp70, and expression of that domain itself is sufficient to induce expression of Hsp70 through the heat shock element (HSE).
213	9553041	The amino-terminal transactivation domain of WT1 is required for binding to Hsp70, and expression of that domain itself is sufficient to induce expression of Hsp70 through the heat shock element (HSE).
214	9553041	The amino-terminal transactivation domain of WT1 is required for binding to Hsp70, and expression of that domain itself is sufficient to induce expression of Hsp70 through the heat shock element (HSE).
215	9553041	The amino-terminal transactivation domain of WT1 is required for binding to Hsp70, and expression of that domain itself is sufficient to induce expression of Hsp70 through the heat shock element (HSE).
216	9553041	Substitution of a heterologous Hsp70-binding domain derived from human DNAJ is sufficient to restore the functional properties of a WT1 protein with an amino-terminal deletion, an effect that is abrogated by a point mutation in DNAJ that reduces binding to Hsp70.
217	9553041	Substitution of a heterologous Hsp70-binding domain derived from human DNAJ is sufficient to restore the functional properties of a WT1 protein with an amino-terminal deletion, an effect that is abrogated by a point mutation in DNAJ that reduces binding to Hsp70.
218	9553041	Substitution of a heterologous Hsp70-binding domain derived from human DNAJ is sufficient to restore the functional properties of a WT1 protein with an amino-terminal deletion, an effect that is abrogated by a point mutation in DNAJ that reduces binding to Hsp70.
219	9553041	Substitution of a heterologous Hsp70-binding domain derived from human DNAJ is sufficient to restore the functional properties of a WT1 protein with an amino-terminal deletion, an effect that is abrogated by a point mutation in DNAJ that reduces binding to Hsp70.
220	9553041	Substitution of a heterologous Hsp70-binding domain derived from human DNAJ is sufficient to restore the functional properties of a WT1 protein with an amino-terminal deletion, an effect that is abrogated by a point mutation in DNAJ that reduces binding to Hsp70.
221	9553041	Substitution of a heterologous Hsp70-binding domain derived from human DNAJ is sufficient to restore the functional properties of a WT1 protein with an amino-terminal deletion, an effect that is abrogated by a point mutation in DNAJ that reduces binding to Hsp70.
222	9553041	Substitution of a heterologous Hsp70-binding domain derived from human DNAJ is sufficient to restore the functional properties of a WT1 protein with an amino-terminal deletion, an effect that is abrogated by a point mutation in DNAJ that reduces binding to Hsp70.
223	9553041	These observations indicate that Hsp70 is an important cofactor for the function of WT1, and suggest a potential role for this chaperone during kidney differentiation.
224	9553041	These observations indicate that Hsp70 is an important cofactor for the function of WT1, and suggest a potential role for this chaperone during kidney differentiation.
225	9553041	These observations indicate that Hsp70 is an important cofactor for the function of WT1, and suggest a potential role for this chaperone during kidney differentiation.
226	9553041	These observations indicate that Hsp70 is an important cofactor for the function of WT1, and suggest a potential role for this chaperone during kidney differentiation.
227	9553041	These observations indicate that Hsp70 is an important cofactor for the function of WT1, and suggest a potential role for this chaperone during kidney differentiation.
228	9553041	These observations indicate that Hsp70 is an important cofactor for the function of WT1, and suggest a potential role for this chaperone during kidney differentiation.
229	9553041	These observations indicate that Hsp70 is an important cofactor for the function of WT1, and suggest a potential role for this chaperone during kidney differentiation.