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Article

Selection for nonamyloidogenic mutants of islet amyloid polypeptide (IAPP) identifies an extended region for amyloidogenicity.

Biochemistry - 14 Sept 2010

Fox Ayano, Snollaerts Thibaut, Errecart Casanova Camille, Calciano Anastasia, Nogaj Luiza A, Moffet David A

Abstract excerpt

The aggregation of the 37-residue protein, islet amyloid polypeptide (IAPP), as either insoluble amyloid or as small oligomers, appears to play a direct role in the death of pancreatic beta-islet cells in type II diabetes. While IAPP has been known to be the primary component of type II diabetes amyloid, the molecular interactions responsible for this aggregation have not been identified. To identify the...

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Share to Amino Acid Sequence
Share to Amyloid

Methodology Data sources Editorial policy Privacy About Contact Helena Bioinformatics

Share to Green Fluorescent Proteins

Share to Islet Amyloid Polypeptide

Share to Microscopy, Atomic Force

Share to Molecular Sequence Data

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Share to Protein Structure, Secondary

Source

Open in PubMed Open full text

Identifiers

PMID: 20698575
DOI: 10.1021/bi100337p
PMCID: PMC2963167

Genes

IAPP

Provenance

PubMed metadata and Literature Corpus relationships. Corpus snapshot updated 6 Sept 2026. Manifest publication-graph-cohort-2026-09-06.1.

Source receipt: pubmed, retrieved 6 Sept 2026.

Related research

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Selection for nonamyloidogenic mutants of islet amyloid polypeptide (IAPP) identifies an extended region for amyloidogenicity.PMID 20698575Read ↗

Destabilization of human IAPP amyloid fibrils by proline mutations outside of the putative amyloidogenic domain: is there a critical amyloidogenic domain in human IAPP?Semantic proximity Read ↗

Analysis of Proline Substitutions Reveals the Plasticity and Sequence Sensitivity of Human IAPP Amyloidogenicity and Toxicity.Semantic proximity Read ↗

Mutational analysis of preamyloid intermediates: the role of his-tyr interactions in islet amyloid formation.Semantic proximity Read ↗

Massively parallel quantification of mutational impact on IAPP amyloid formationSemantic proximity Read ↗

Tracking the amyloidogenic core of IAPP amyloid fibrils: Insights from micro-Raman spectroscopy.Semantic proximity Read ↗

Elucidating conformational alteration of human islet amyloid polypeptide by nonsynonymous substitutionSemantic proximity Read ↗

Mutations that reduce aggregation of the Alzheimer's Abeta42 peptide: an unbiased search for the sequence determinants of Abeta amyloidogenesis.Semantic proximity Read ↗

Massively parallel quantification of mutational impact on IAPP amyloid formation.Semantic proximity Read ↗

Residue specific effects of human islet polypeptide amyloid on self-assembly and on cell toxicity.Semantic proximity Read ↗

The S20G substitution in hIAPP is more amyloidogenic and cytotoxic than wild-type hIAPP in mouse islets.Semantic proximity Read ↗

Mutations enhance the aggregation propensity of the Alzheimer's A beta peptide.Semantic proximity Read ↗

Rationally designed, nontoxic, nonamyloidogenic analogues of human islet amyloid polypeptide with improved solubility.Semantic proximity Read ↗

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