Mechanisms of islet amyloidosis toxicity in type 2 diabetes
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On the Environmental Factors Affecting the Structural and Cytotoxic Properties of IAPP PeptidesDynamics of the formation of a hydrogel by a pathogenic amyloid peptide: islet amyloid polypeptide.Role of Cholesterol and Phospholipids in Amylin Misfolding, Aggregation and Etiology of Islet AmyloidosisProtein misfolding and aggregation in Alzheimer's disease and type 2 diabetes mellitusInter-species cross-seeding: stability and assembly of rat-human amylin aggregatesStructural Characterization of Fibrils from Recombinant Human Islet Amyloid Polypeptide by Solid-State NMR: The Central FGAILS Segment Is Part of the β-Sheet CoreAromaticity and amyloid formation: effect of π-electron distribution and aryl substituent geometry on the self-assembly of peptides derived from hIAPP(22-29).Analysis of the Amyloidogenic Potential of Pufferfish (Takifugu rubripes) Islet Amyloid Polypeptide Highlights the Limitations of Thioflavin-T Assays and the Difficulties in Defining AmyloidogenicityIon mobility spectrometry-mass spectrometry defines the oligomeric intermediates in amylin amyloid formation and the mode of action of inhibitorsAmyloid aggregation and deposition of human islet amyloid polypeptide at membrane interfaces.Mutational analysis of preamyloid intermediates: the role of his-tyr interactions in islet amyloid formationStructure-Based Small Molecule Modulation of a Pre-Amyloid State: Pharmacological Enhancement of IAPP Membrane-Binding and Toxicity.Discovery of ethyl urea derivatives as inhibitors of islet amyloid polypeptide fibrillization and cytotoxicity.Protein post-translational modifications and misfolding: new concepts in heart failure.Self-assembled amyloid fibrils with controllable conformational heterogeneity.Islet Amyloid Polypeptide: Structure, Function, and Pathophysiology.Matrix Metalloproteinase-9 Protects Islets from Amyloid-induced ToxicityInhibition of Toxic IAPP Amyloid by Extracts of Common FruitsIdentification of Plant Extracts that Inhibit the Formation of Diabetes-Linked IAPP AmyloidTime-resolved studies define the nature of toxic IAPP intermediates, providing insight for anti-amyloidosis therapeutics.Proteasome regulates turnover of toxic human amylin in pancreatic cells.Unlocking the biology of RAGE in diabetic microvascular complicationsMitochondria in metabolic disease: getting clues from proteomic studies.Mechanistic Contributions of Biological Cofactors in Islet Amyloid Polypeptide Amyloidogenesis.Inhibition of islet amyloid polypeptide aggregation and associated cytotoxicity by nonsteroidal anti-inflammatory drugs.Structural studies and cytotoxicity assays of "aggregation-prone" IAPP(8-16) and its non-amyloidogenic variants suggest its important role in fibrillogenesis and cytotoxicity of human amylin.Selenium-enriched Spirulina protects INS-1E pancreatic beta cells from human islet amyloid polypeptide-induced apoptosis through suppression of ROS-mediated mitochondrial dysfunction and PI3/AKT pathway.Cellular Regulation of Amyloid Formation in Aging and Disease.Biochemical profiling of diabetes disease progression by multivariate vibrational microspectroscopy of the pancreas.Amylin receptor: a common pathophysiological target in Alzheimer's disease and diabetes mellitusCyclic AC253, a novel amylin receptor antagonist, improves cognitive deficits in a mouse model of Alzheimer's diseaseThe many faces of proteins.The Molecular Physiopathogenesis of Islet Amyloidosis.The Physiological and Pathological Implications of the Formation of Hydrogels, with a Specific Focus on Amyloid Polypeptides.Membrane-mediated amyloid deposition of human islet amyloid polypeptide.Islet Amyloid Polypeptide Membrane Interactions: Effects of Membrane Composition.RAGE binds preamyloid IAPP intermediates and mediates pancreatic β cell proteotoxicity.Teaching an old scaffold new recognition tricks: oligopyrrolamide antagonists of IAPP aggregation.Pancreatic Beta Cell Death: Novel Potential Mechanisms in Diabetes Therapy.The 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.
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P2860
Mechanisms of islet amyloidosis toxicity in type 2 diabetes
description
2013 nî lūn-bûn
@nan
2013 թուականի Ապրիլին հրատարակուած գիտական յօդուած
@hyw
2013 թվականի ապրիլին հրատարակված գիտական հոդված
@hy
2013年の論文
@ja
2013年論文
@yue
2013年論文
@zh-hant
2013年論文
@zh-hk
2013年論文
@zh-mo
2013年論文
@zh-tw
2013年论文
@wuu
name
Mechanisms of islet amyloidosis toxicity in type 2 diabetes
@ast
Mechanisms of islet amyloidosis toxicity in type 2 diabetes
@en
Mechanisms of islet amyloidosis toxicity in type 2 diabetes
@nl
type
label
Mechanisms of islet amyloidosis toxicity in type 2 diabetes
@ast
Mechanisms of islet amyloidosis toxicity in type 2 diabetes
@en
Mechanisms of islet amyloidosis toxicity in type 2 diabetes
@nl
prefLabel
Mechanisms of islet amyloidosis toxicity in type 2 diabetes
@ast
Mechanisms of islet amyloidosis toxicity in type 2 diabetes
@en
Mechanisms of islet amyloidosis toxicity in type 2 diabetes
@nl
P2860
P3181
P1433
P1476
Mechanisms of islet amyloidosis toxicity in type 2 diabetes
@en
P2093
Ann Marie Schmidt
P2860
P304
P3181
P356
10.1016/J.FEBSLET.2013.01.017
P407
P577
2013-01-18T00:00:00Z