Islet amyloid: from fundamental biophysics to mechanisms of cytotoxicity.
about
On the Environmental Factors Affecting the Structural and Cytotoxic Properties of IAPP PeptidesRole of Cholesterol and Phospholipids in Amylin Misfolding, Aggregation and Etiology of Islet AmyloidosisInter-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 CoreDigested disorder: Quarterly intrinsic disorder digest (April-May-June, 2013).Aromaticity 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 AmyloidogenicityDefining the molecular basis of amyloid inhibitors: human islet amyloid polypeptide-insulin interactions.Ion 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 formationComputational re-engineering of Amylin sequence with reduced amyloidogenic potential.Structure-Based Small Molecule Modulation of a Pre-Amyloid State: Pharmacological Enhancement of IAPP Membrane-Binding and Toxicity.Detection of Helical Intermediates During Amyloid Formation by Intrinsically Disordered Polypeptides and Proteins.In Vitro Studies of Membrane Permeability Induced by Amyloidogenic Polypeptides Using Large Unilamellar Vesicles.Islet Amyloid Polypeptide: Structure, Function, and Pathophysiology.Matrix Metalloproteinase-9 Protects Islets from Amyloid-induced ToxicityStress-impaired transcription factor expression and insulin secretion in transplanted human islets.Crystal Structures of IAPP Amyloidogenic Segments Reveal a Novel Packing Motif of Out-of-Register Beta Sheets.Time-resolved studies define the nature of toxic IAPP intermediates, providing insight for anti-amyloidosis therapeutics.Islet amyloid polypeptide toxicity and membrane interactionsMechanism of IAPP amyloid fibril formation involves an intermediate with a transient β-sheet.Cross-talk between amyloidogenic proteins in type-2 diabetes and Parkinson's disease.Mutations and seeding of amylin fibril-like oligomers.Quantification of transthyretin kinetic stability in human plasma using subunit exchange.Genetically engineered pig models for diabetes research.Mitochondria in metabolic disease: getting clues from proteomic studies.The regulatory roles of NADPH oxidase, intra- and extra-cellular HSP70 in pancreatic islet function, dysfunction and diabetes.Mechanistic Contributions of Biological Cofactors in Islet Amyloid Polypeptide Amyloidogenesis.Inhibitory Mechanism of Epigallocatechin Gallate on Fibrillation and Aggregation of Amidated Human Islet Amyloid Polypeptide.An Account of Amyloid Oligomers: Facts and Figures Obtained from Experiments and Simulations.Cross-interactions between the Alzheimer Disease Amyloid-β Peptide and Other Amyloid Proteins: A Further Aspect of the Amyloid Cascade Hypothesis.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.Modulation of amyloid assembly by glycosaminoglycans: from mechanism to biological significance.β-Hairpin of Islet Amyloid Polypeptide Bound to an Aggregation InhibitorComplete characterization of the mutation landscape reveals the effect on amylin stability and amyloidogenicity.The dynamic plasticity of insulin production in β-cells.Cholesterol modulates the interaction of the islet amyloid polypeptide with membranes.Understanding co-polymerization in amyloid formation by direct observation of mixed oligomers.Extracellular vesicles from human pancreatic islets suppress human islet amyloid polypeptide amyloid formation.
P2860
Q27022467-D702CD50-B164-41F2-A28C-610C176D754FQ28088416-A444245A-CB98-4B0E-96B7-B64F1B5E7A9EQ28538620-F4A0A3E6-52B6-4544-928A-744B5F6C00A8Q28553950-354E4CE9-2B91-4481-B70B-2D83FF6731B5Q30402101-46431F21-21AC-48B9-A96B-22CFA0B0D71EQ33852711-78A8F45E-B9F0-42AF-809B-65F4B3941AD7Q33886359-27E9AF6B-21EE-42AE-BE45-AE9172F64FD8Q34282725-E897A819-52E1-4F3C-8A6F-548E5674285BQ35076599-880B36DD-FF01-4A64-ACD1-B8F9D262A7AAQ35139664-6929CFC9-411B-404B-B60D-3D43307128D0Q35139765-E19784AC-9478-44FB-96C0-C3EF2672B1E5Q35612061-307E80FC-9344-4A11-801A-F2BA7CB796B9Q35628125-635101CE-2713-4481-9DE1-27C063D67AF2Q35802280-537D51BC-2915-4F8C-ACA3-368577DFB377Q35802290-C7EB3448-0801-4251-8F2D-F3E961EEF734Q36327915-B80954C8-926D-49BD-9A5D-CFDEDDCE845FQ36381947-B4D74CE9-0F34-454F-97BD-9BBA3DC178DAQ36867289-74271E86-6E08-468D-8F01-D5422F81B2FBQ37075263-D5A0638C-9A4D-4A5E-B95B-0F27E1E6A8B4Q37083241-BF74ABBB-DFE9-44A3-B0FA-E5EA7C9F01FAQ37353189-38C86AC3-70FB-4231-8502-5EF65E0D9AC0Q37353196-3E0D67B4-67C6-441F-9AEE-C91A9A1543F9Q37398112-4D16DE92-A7A5-4167-BACE-598725A18906Q37483335-2D78C38A-DCC6-41C4-AF92-7DF9B34B9491Q37688196-BAF9C706-D626-4A92-B389-1AF14D1E4332Q38142738-DC8D523D-5C80-4B65-B7D3-C08678406228Q38171425-AA531DBE-DD06-4042-B0C0-7556C90E0785Q38424338-08A5E360-7F29-40F2-AD29-4FE6F56C305AQ38635739-DF8F51B5-FDD9-4009-899F-89DCBC50159DQ38744651-1DB6D8A9-8760-4B31-B93A-931D5674D4F9Q38748337-1B3607CF-1927-4508-9358-BCF75A7FDC7BQ38871578-647A7581-C1E2-4A6D-A305-4944EB977B2BQ38967080-13E45808-F4F4-49CF-B129-8F6A4D65FCD2Q39126169-428CD2CB-96C0-4841-9A9E-30BEBD5C611BQ41117781-D50D4D92-8DCD-49EE-B21B-0A2930BB46D3Q41158742-6A2D2B54-0074-4FE9-BDF6-0E72504B008CQ41689708-0CC6E30E-A469-4BB3-B19E-0A9FA82E39E4Q41704295-375BFBC7-BF54-4195-9E4E-69B3EC608623Q41774231-E8EC7545-FDDB-488B-B1DB-F671AC1FCCFDQ42653482-6014C627-28B2-4304-BFE5-37A9E4B29A96
P2860
Islet amyloid: from fundamental biophysics to mechanisms of cytotoxicity.
description
article científic
@ca
article scientifique
@fr
articolo scientifico
@it
artigo científico
@pt
bilimsel makale
@tr
scientific article published on February 2013
@en
vedecký článok
@sk
vetenskaplig artikel
@sv
videnskabelig artikel
@da
vědecký článek
@cs
name
Islet amyloid: from fundamental biophysics to mechanisms of cytotoxicity.
@en
Islet amyloid: from fundamental biophysics to mechanisms of cytotoxicity.
@nl
type
label
Islet amyloid: from fundamental biophysics to mechanisms of cytotoxicity.
@en
Islet amyloid: from fundamental biophysics to mechanisms of cytotoxicity.
@nl
prefLabel
Islet amyloid: from fundamental biophysics to mechanisms of cytotoxicity.
@en
Islet amyloid: from fundamental biophysics to mechanisms of cytotoxicity.
@nl
P2093
P2860
P50
P1433
P1476
Islet amyloid: from fundamental biophysics to mechanisms of cytotoxicity.
@en
P2093
P2860
P304
P356
10.1016/J.FEBSLET.2013.01.046
P407
P577
2013-02-01T00:00:00Z