Full-length rat amylin forms fibrils following substitution of single residues from human amylin.
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Porcine islet amyloid polypeptide fragments are refractory to amyloid formationA single mutation in the nonamyloidogenic region of islet amyloid polypeptide greatly reduces toxicityPrediction of "hot spots" of aggregation in disease-linked polypeptidesMolecular Structure, Membrane Interactions, and Toxicity of the Islet Amyloid Polypeptide in Type 2 Diabetes MellitusAtomic structure of the cross-β spine of islet amyloid polypeptide (amylin)Three-Dimensional Structure and Orientation of Rat Islet Amyloid Polypeptide Protein in a Membrane Environment by Solution NMR SpectroscopyMolecular mechanisms for protein-encoded inheritanceInter-species cross-seeding: stability and assembly of rat-human amylin aggregatesDirect detection of transient alpha-helical states in islet amyloid polypeptideHuman islet amyloid polypeptide monomers form ordered beta-hairpins: a possible direct amyloidogenic precursor.AGGRESCAN: a server for the prediction and evaluation of "hot spots" of aggregation in polypeptides.Solution state structures of human pancreatic amylin and pramlintide.Solution structures of rat amylin peptide: simulation, theory, and experiment.Role of small oligomers on the amyloidogenic aggregation free-energy landscapeIslet amyloid deposition limits the viability of human islet grafts but not porcine islet grafts.Analysis of the Amyloidogenic Potential of Pufferfish (Takifugu rubripes) Islet Amyloid Polypeptide Highlights the Limitations of Thioflavin-T Assays and the Difficulties in Defining AmyloidogenicityStable and metastable states of human amylin in solution.Misfolded proteins in Alzheimer's disease and type II diabetes.Beta structure motifs of islet amyloid polypeptides identified through surface-mediated assembliesStructure-Based Small Molecule Modulation of a Pre-Amyloid State: Pharmacological Enhancement of IAPP Membrane-Binding and Toxicity.Identification of Human Islet Amyloid Polypeptide as a BACE2 Substrate.The dye SYPRO orange binds to amylin amyloid fibrils but not pre-fibrillar intermediates.Analysis of the ability of pramlintide to inhibit amyloid formation by human islet amyloid polypeptide reveals a balance between optimal recognition and reduced amyloidogenicity.Islet Amyloid Polypeptide: Structure, Function, and Pathophysiology.α-helix to β-hairpin transition of human amylin monomer.Peptide conformation and supramolecular organization in amylin fibrils: constraints from solid-state NMR.Islet amyloid: from fundamental biophysics to mechanisms of cytotoxicity.Effect of proline mutations on the monomer conformations of amylin.Sequence and crowding effects in the aggregation of a 10-residue fragment derived from islet amyloid polypeptideExploring amyloid formation by a de novo design.AFM of biological complexes: what can we learn?Aggregation of islet amyloid polypeptide: from physical chemistry to cell biology.Islet inflammation in type 2 diabetes and physiology.The role of the 14-20 domain of the islet amyloid polypeptide in amyloid formationStudy reanalysis using a mechanism-based pharmacokinetic/pharmacodynamic model of pramlintide in subjects with type 1 diabetes.Peptide Inhibitors of the amyloidogenesis of IAPP: verification of the hairpin-binding geometry hypothesis.Idealized models of protofilaments of human islet amyloid polypeptideHelix stabilization precedes aqueous and bilayer-catalyzed fiber formation in islet amyloid polypeptideAmylin proprotein processing generates progressively more amyloidogenic peptides that initially sample the helical state.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.
P2860
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P2860
Full-length rat amylin forms fibrils following substitution of single residues from human amylin.
description
2003 nî lūn-bûn
@nan
2003 թուականի Փետրուարին հրատարակուած գիտական յօդուած
@hyw
2003 թվականի փետրվարին հրատարակված գիտական հոդված
@hy
2003年の論文
@ja
2003年論文
@yue
2003年論文
@zh-hant
2003年論文
@zh-hk
2003年論文
@zh-mo
2003年論文
@zh-tw
2003年论文
@wuu
name
Full-length rat amylin forms f ...... le residues from human amylin.
@ast
Full-length rat amylin forms f ...... le residues from human amylin.
@en
type
label
Full-length rat amylin forms f ...... le residues from human amylin.
@ast
Full-length rat amylin forms f ...... le residues from human amylin.
@en
prefLabel
Full-length rat amylin forms f ...... le residues from human amylin.
@ast
Full-length rat amylin forms f ...... le residues from human amylin.
@en
P2093
P1476
Full-length rat amylin forms f ...... le residues from human amylin.
@en
P2093
Claire Goldsbury
Garth Cooper
Janelle Green
Joerg Kistler
Peter Frey
Shabir Sunderji
Thierry Mini
P304
P356
10.1016/S0022-2836(02)01377-3
P407
P50
P577
2003-02-01T00:00:00Z