An islet amyloid peptide is derived from an 89-amino acid precursor by proteolytic processing
about
Sequence and functional expression in Xenopus oocytes of a human insulinoma and islet potassium channelMolecular and functional characterization of amylin, a peptide associated with type 2 diabetes mellitusIslet amyloid in type 2 diabetes, and the toxic oligomer hypothesisNeuroendocrine hormone amylin in diabetesCommon mechanisms involved in Alzheimer's disease and type 2 diabetes: a key role of chronic bacterial infection and inflammationMolecular Structure, Membrane Interactions, and Toxicity of the Islet Amyloid Polypeptide in Type 2 Diabetes MellitusCausative factors for formation of toxic islet amyloid polypeptide oligomer in type 2 diabetes mellitusMechanisms of islet amyloidosis toxicity in type 2 diabetesThe Effects of Lipid Membranes, Crowding and Osmolytes on the Aggregation, and Fibrillation Propensity of Human IAPPEndoplasmic reticulum stress and type 2 diabetesOn the Environmental Factors Affecting the Structural and Cytotoxic Properties of IAPP PeptidesConservation of the sequence of islet amyloid polypeptide in five mammals is consistent with its putative role as an islet hormoneIslet amyloid polypeptide: pinpointing amino acid residues linked to amyloid fibril formationProgressive deterioration of insulin secretion in Japanese type 2 diabetic patients in comparison with those who carry the S20G mutation of the islet amyloid polypeptide gene: A long-term follow-up studyProtective role of human insulin against the cytotoxicity associated with human mutant S20G islet amyloid polypeptide.Rat amylin: cloning and tissue-specific expression in pancreatic islets.Beta amyloid and hyperphosphorylated tau deposits in the pancreas in type 2 diabetes.Amylin secretion from the rat pancreas and its selective loss after streptozotocin treatment.The Mitochondrial Peptidase Pitrilysin Degrades Islet Amyloid Polypeptide in Beta-Cells.How type II diabetes-related islet amyloid polypeptide damages lipid bilayers.Impaired glucose tolerance is associated with increased islet amyloid polypeptide (IAPP) immunoreactivity in pancreatic beta cells.S20G mutant amylin exhibits increased in vitro amyloidogenicity and increased intracellular cytotoxicity compared to wild-type amylin.Immunoreactivity and expression of amylin in gastroenteropancreatic endocrine tumorsIslet Amyloid Polypeptide: Structure, Function, and Pathophysiology.Amyloid formation in response to beta cell stress occurs in vitro, but not in vivo, in islets of transgenic mice expressing human islet amyloid polypeptideDegradation of islet amyloid polypeptide by neprilysin.Islet amyloid: from fundamental biophysics to mechanisms of cytotoxicity.The age related amyloids: a growing family of unique biochemical substances.Identification of a cDNA encoding a second putative prohormone convertase related to PC2 in AtT20 cells and islets of LangerhansAggregation of islet amyloid polypeptide: from physical chemistry to cell biology.Current and future treatment of amyloid diseases.Real-time monitoring of apoptosis by caspase-3-like protease induced FRET reduction triggered by amyloid aggregation.Autophagy protects against human islet amyloid polypeptide-associated apoptosisThe ability of insulin to inhibit the formation of amyloid by pro-islet amyloid polypeptide processing intermediates is significantly reduced in the presence of sulfated glycosaminoglycans.The ability of rodent islet amyloid polypeptide to inhibit amyloid formation by human islet amyloid polypeptide has important implications for the mechanism of amyloid formation and the design of inhibitors.Sequence-Dependent Self-Assembly and Structural Diversity of Islet Amyloid Polypeptide-Derived β-Sheet Fibrils.Can Bayliss and Starling gut hormones cure a worldwide pandemic?Amyloid precursor proteins form ordered fibrilsThe Receptor for Advanced Glycation Endproducts is a mediator of toxicity by IAPP and other proteotoxic aggregates: Establishing and Exploiting Common Ground for Novel Amyloidosis Therapies.
P2860
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P2860
An islet amyloid peptide is derived from an 89-amino acid precursor by proteolytic processing
description
1988 թուականի Նոյեմբերին հրատարակուած գիտական յօդուած
@hyw
1988 թվականի նոյեմբերին հրատարակված գիտական հոդված
@hy
article publié dans la revue scientifique Journal of Biological Chemistry
@fr
artículu científicu espublizáu en 1988
@ast
im November 1988 veröffentlichter wissenschaftlicher Artikel
@de
scientific journal article
@en
vedecký článok (publikovaný 1988/11/25)
@sk
vědecký článek publikovaný v roce 1988
@cs
wetenschappelijk artikel (gepubliceerd op 1988/11/25)
@nl
наукова стаття, опублікована в листопаді 1988
@uk
name
An islet amyloid peptide is de ...... rsor by proteolytic processing
@ast
An islet amyloid peptide is de ...... rsor by proteolytic processing
@en
An islet amyloid peptide is de ...... rsor by proteolytic processing
@nl
type
label
An islet amyloid peptide is de ...... rsor by proteolytic processing
@ast
An islet amyloid peptide is de ...... rsor by proteolytic processing
@en
An islet amyloid peptide is de ...... rsor by proteolytic processing
@nl
prefLabel
An islet amyloid peptide is de ...... rsor by proteolytic processing
@ast
An islet amyloid peptide is de ...... rsor by proteolytic processing
@en
An islet amyloid peptide is de ...... rsor by proteolytic processing
@nl
P2093
P1476
An islet amyloid peptide is de ...... rsor by proteolytic processing
@en
P2093
A. H. Rubenstein
D. F. Steiner
G. I. Bell
P304
17243–17246
P407
P577
1988-11-25T00:00:00Z