Recent insights in islet amyloid polypeptide-induced membrane disruption and its role in beta-cell death in type 2 diabetes mellitus
about
A single mutation in the nonamyloidogenic region of islet amyloid polypeptide greatly reduces toxicityCytoplasmic penetration and persistent infection of mammalian cells by polyglutamine aggregatesMolecular Structure, Membrane Interactions, and Toxicity of the Islet Amyloid Polypeptide in Type 2 Diabetes MellitusOn the Environmental Factors Affecting the Structural and Cytotoxic Properties of IAPP PeptidesThree-Dimensional Structure and Orientation of Rat Islet Amyloid Polypeptide Protein in a Membrane Environment by Solution NMR SpectroscopyInfluence of Bisphenol A on Type 2 Diabetes MellitusA brief history of prionsRole of Cholesterol and Phospholipids in Amylin Misfolding, Aggregation and Etiology of Islet AmyloidosisMultiple β-sheet molecular dynamics of amyloid formation from two ABl-SH3 domain peptides.Calcium-activated calpain-2 is a mediator of beta cell dysfunction and apoptosis in type 2 diabetes.Human antimicrobial peptides and proteinsThe effect of Aβ on IAPP aggregation in the presence of an isolated β-cell membrane.The Mitochondrial Peptidase Pitrilysin Degrades Islet Amyloid Polypeptide in Beta-Cells.Biphasic effects of insulin on islet amyloid polypeptide membrane disruption.Macromolecular crowding as a suppressor of human IAPP fibril formation and cytotoxicity.Distinct internalization pathways of human amylin monomers and its cytotoxic oligomers in pancreatic cellsExendin-4 increases islet amyloid deposition but offsets the resultant beta cell toxicity in human islet amyloid polypeptide transgenic mouse islets.Insights into the consequences of co-polymerisation in the early stages of IAPP and Aβ peptide assembly from mass spectrometry.Probing ion channel activity of human islet amyloid polypeptide (amylin).Binding Orientations and Lipid Interactions of Human Amylin at Zwitterionic and Anionic Lipid BilayersInduction of negative curvature as a mechanism of cell toxicity by amyloidogenic peptides: the case of islet amyloid polypeptide.Islet amyloid polypeptide toxicity and membrane interactionsAmyloid deposition in transplanted human pancreatic islets: a conceivable cause of their long-term failure.Aggregation of islet amyloid polypeptide: from physical chemistry to cell biology.Toxic oligomers and islet beta cell death: guilty by association or convicted by circumstantial evidence?Unique features of human cathelicidin LL-37.Mechanistic Contributions of Biological Cofactors in Islet Amyloid Polypeptide Amyloidogenesis.Inhibition of islet amyloid polypeptide aggregation and associated cytotoxicity by nonsteroidal anti-inflammatory drugs.Dewetting transition assisted clearance of (NFGAILS) amyloid fibrils from cell membranes by graphene.Activation of innate immunity by lysozyme fibrils is critically dependent on cross-β sheet structure.Implications of peptide assemblies in amyloid diseases.Amylin uncovered: a review on the polypeptide responsible for type II diabetes.Islet amyloid polypeptide acts on glucose- stimulated beta cells to reduce voltage-gated calcium channel activation, intracellular Ca(2+) concentration, and insulin secretion.Inhibitory effects of choline-O-sulfate on amyloid formation of human islet amyloid polypeptide.Wildlife sequences of islet amyloid polypeptide (IAPP) identify critical species variants for fibrillization.Interfacial interaction and lateral association of cross-seeding assemblies between hIAPP and rIAPP oligomers.Further evidence for amyloid deposition in clinical pancreatic islet grafts.Cholesterol modulates the interaction of the islet amyloid polypeptide with membranes.The role of the disulfide bond in the interaction of islet amyloid polypeptide with membranes.The Molecular Physiopathogenesis of Islet Amyloidosis.
P2860
Q24650320-CE69E66B-ED7B-4414-B68F-31F43BC84325Q24657543-C0D110EE-8EDA-4EF6-B0B0-323EA4683D65Q26774381-0AC8C957-2A14-4BA6-B5F6-A6CF221A4042Q27022467-F2F8E7E4-A313-480F-993D-294BCE80FD46Q27655538-EE714456-F43F-4C8B-B58B-0958FBE5B7BAQ28075627-7127ABD6-9C32-40EF-A678-1264F9D58158Q28085285-7F3DCE18-12D5-47F8-92A2-43A03F21FCECQ28088416-CC0511E1-385B-40B1-90F9-A9A84B7D1B93Q30009967-D7D9E73D-ABC4-4485-BFF1-A1CA2D5D80F7Q33581290-9F0CE989-1A83-4E80-A0E0-159E18242918Q33673156-E72ED367-5E49-41A9-8D97-BA15F0FD04E5Q33822270-3E785655-C79C-4303-A028-04B8E556D545Q34485889-EE0C5590-7917-4200-AC9B-58D611D92CACQ34536499-D2B342FC-5C64-4527-840E-45F820678C0EQ34903445-12DC8614-3A1C-493D-B097-2777BDD8C0BFQ34982786-C1D836B2-85F3-4081-8111-F402C7E40D4DQ35563969-F3EFCD4A-C55E-4D25-A83E-1EBBB4626247Q36224635-7E28A937-4BA6-4471-A038-5538BE076D83Q36269079-66E01FFB-0EE0-4370-9710-0CB7E0CE634DQ36329000-E1E7F6A8-1A1E-42AE-8DDF-563B09635557Q37151260-0D2F59D2-3C4C-46E3-B0DA-5E3BB65A764EQ37353189-E5A38677-74D5-49BF-9ABA-A10FE6F221B9Q37412301-D3096C4B-4E54-4988-94CB-C57D64159C7FQ37672295-78C1971C-5A92-4B57-8A24-F29BC6B817A6Q37698330-5654FE00-CD84-4248-95BF-7AF2F31864CAQ38598753-23E801FD-D154-4666-B6C1-7EDF3F142A56Q38635739-4FC8D76C-1F37-4847-8463-2C911C6333D1Q38822940-AF34493A-1033-4C09-804A-B6D6A24A6530Q39078176-4166AA4A-43C0-42E8-98A9-1E70B82568EEQ39207798-BAB3685F-7218-4638-B3DB-D4358DFD3CA6Q39431937-9202CBF5-1963-4DAF-9496-6DB3D869AAF4Q39846208-6E479217-ECC6-4914-AF3F-34FB71917E17Q39965850-15A90F0E-E52A-4167-9BD1-FA9303AB0E8EQ40316555-6DE01CB4-B76E-411C-8753-D8CA05A5E449Q40614933-135CD4E0-F498-4C9D-8A28-1909BFB081FEQ41367406-E1EFF0FB-48DB-4020-A2A0-AD3220D2AC66Q41623363-169B4E43-FC9E-477E-BE9D-EDD66300CCC3Q41704295-1447117C-E03B-4D73-88DE-BACDDDF041D2Q42733549-F6DF0157-2AE2-436F-A42B-9ED25585C0A3Q46282033-3491D0C0-4747-41E1-A114-BEA9610E7321
P2860
Recent insights in islet amyloid polypeptide-induced membrane disruption and its role in beta-cell death in type 2 diabetes mellitus
description
article científic
@ca
article scientifique
@fr
articolo scientifico
@it
artigo científico
@pt
bilimsel makale
@tr
scientific article published on January 2008
@en
vedecký článok
@sk
vetenskaplig artikel
@sv
videnskabelig artikel
@da
vědecký článek
@cs
name
Recent insights in islet amylo ...... th in type 2 diabetes mellitus
@en
Recent insights in islet amylo ...... h in type 2 diabetes mellitus.
@nl
type
label
Recent insights in islet amylo ...... th in type 2 diabetes mellitus
@en
Recent insights in islet amylo ...... h in type 2 diabetes mellitus.
@nl
prefLabel
Recent insights in islet amylo ...... th in type 2 diabetes mellitus
@en
Recent insights in islet amylo ...... h in type 2 diabetes mellitus.
@nl
P2860
P921
P356
P1476
Recent insights in islet amylo ...... th in type 2 diabetes mellitus
@en
P2093
J Antoinette Killian
Jo W M Höppener
P2860
P304
P356
10.1155/2008/421287
P5008
P577
2008-01-01T00:00:00Z