The chaperone proteins HSP70, HSP40/DnaJ and GRP78/BiP suppress misfolding and formation of β-sheet-containing aggregates by human amylin: a potential role for defective chaperone biology in Type 2 diabetes.
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Neuroendocrine hormone amylin in diabetesHsp72 (HSPA1A) Prevents Human Islet Amyloid Polypeptide Aggregation and Toxicity: A New Approach for Type 2 Diabetes TreatmentChaperones ameliorate beta cell dysfunction associated with human islet amyloid polypeptide overexpressionNetwork-based regularization for high dimensional SNP data in the case-control study of Type 2 diabetesThe NRF2-KEAP1 pathway is an early responsive gene network in arsenic exposed lymphoblastoid cells.Gender-dimorphic regulation of DJ1 and its interactions with metabolic proteins in streptozotocin-induced diabetic rats.KU-32, a novel drug for diabetic neuropathy, is safe for human islets and improves in vitro insulin secretion and viability.β-Cell failure in type 2 diabetes: a case of asking too much of too few?Association between promoter polymorphisms of the GRP78 gene and risk of type 2 diabetes in a Chinese Han populationStress and the inflammatory process: a major cause of pancreatic cell death in type 2 diabetes.The redox environment triggers conformational changes and aggregation of hIAPP in Type II Diabetes.Role of proteomics in understanding prion infection.Impaired proteostasis: role in the pathogenesis of diabetes mellitus.The regulatory roles of NADPH oxidase, intra- and extra-cellular HSP70 in pancreatic islet function, dysfunction and diabetes.The role of copper(II) in the aggregation of human amylin.A two-site mechanism for the inhibition of IAPP amyloidogenesis by zinc.The role of copper(II) and zinc(II) in the degradation of human and murine IAPP by insulin-degrading enzyme.Physiologic Doses of Bilirubin Contribute to Tolerance of Islet Transplants by Suppressing the Innate Immune Response.A Rationally Designed Hsp70 Variant Rescues the Aggregation-Associated Toxicity of Human IAPP in Cultured Pancreatic Islet β-Cells.
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P2860
The chaperone proteins HSP70, HSP40/DnaJ and GRP78/BiP suppress misfolding and formation of β-sheet-containing aggregates by human amylin: a potential role for defective chaperone biology in Type 2 diabetes.
description
2010 nî lūn-bûn
@nan
2010年の論文
@ja
2010年論文
@yue
2010年論文
@zh-hant
2010年論文
@zh-hk
2010年論文
@zh-mo
2010年論文
@zh-tw
2010年论文
@wuu
2010年论文
@zh
2010年论文
@zh-cn
name
The chaperone proteins HSP70, ...... ne biology in Type 2 diabetes.
@en
The chaperone proteins HSP70, ...... ne biology in Type 2 diabetes.
@nl
type
label
The chaperone proteins HSP70, ...... ne biology in Type 2 diabetes.
@en
The chaperone proteins HSP70, ...... ne biology in Type 2 diabetes.
@nl
prefLabel
The chaperone proteins HSP70, ...... ne biology in Type 2 diabetes.
@en
The chaperone proteins HSP70, ...... ne biology in Type 2 diabetes.
@nl
P2093
P2860
P356
P1433
P1476
The chaperone proteins HSP70, ...... ne biology in Type 2 diabetes.
@en
P2093
Anthony Hickey
Christina M Buchanan
Jacqueline F Aitken
Kerry M Loomes
Thomas Brittain
Vita Chien
P2860
P304
P356
10.1042/BJ20100434
P407
P577
2010-11-01T00:00:00Z