Discover Community Create You

Loading publication...

Noodle always counts identifier-free feature events for service operation. With your permission, Google Analytics can also estimate audience and engagement. Search text, publication identifiers, cookies, IP addresses and browser fingerprints are never included in Noodle's first-party event counters.

Privacy details

Article

Massively parallel quantification of mutational impact on IAPP amyloid formation.

Nature communications - 17 Mar 2026

Badia Marta, Batlle Cristina, Bolognesi Benedetta

Abstract excerpt

Amyloid fibrils formed by the islet amyloid polypeptide cause pancreatic beta-cell damage, resulting in reduced insulin secretion and type 2 diabetes. Changes in the amino acid sequence of this peptide can influence its aggregation rate, and animals expressing variants that do not form amyloids do not develop type 2 diabetes. Conversely, specific single amino acid changes can accelerate the aggregation rate of...

Read the complete abstract on PubMed

Topics

Share this publication in a Topic to start or enrich a Post.

Share to Amino Acid Sequence
Share to Amyloid
Share to Amyloid beta-Peptides

Methodology Data sources Editorial policy Privacy About Contact Helena Bioinformatics

Share to Islet Amyloid Polypeptide

Share to Mutation

Source

Open in PubMed Open full text

Identifiers

PMID: 41844597
DOI: 10.1038/s41467-026-70611-z
PMCID: PMC13144336

Genes

IAPP

Provenance

PubMed metadata and Literature Corpus relationships. Corpus snapshot updated 6 Sept 2026.

Related research

Semantic proximity does not establish scientific evidence.

Research trail→

Click a neighbor to travelStep 1 · 12 closest

Massively parallel quantification of mutational impact on IAPP amyloid formation.PMID 41844597Read ↗

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

An atlas of amyloid aggregation: the impact of substitutions, insertions, deletions and truncations on amyloid beta fibril nucleationSemantic proximity Read ↗

An atlas of amyloid aggregation: the impact of substitutions, insertions, deletions and truncations on amyloid beta fibril nucleationSemantic proximity Read ↗

The genetic landscape for amyloid beta fibril nucleation accurately discriminates familial Alzheimer's disease mutations.Semantic proximity Read ↗

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

The genetic landscape for amyloid beta fibril nucleation accurately discriminates familial Alzheimer’s disease mutationsSemantic proximity Read ↗

Massively parallel genetic perturbation suggests the energetic structure of an amyloid-β transition stateSemantic proximity Read ↗

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

Experimental and computational analysis of the basis for accelerated amyloid formation by a disease linked mutant of human islet amyloid polypeptide.Semantic proximity Read ↗

Massively parallel genetic perturbation reveals the energetic architecture of an amyloid beta nucleation reactionSemantic proximity Read ↗

Complete characterization of the mutation landscape reveals the effect on amylin stability and amyloidogenicity.Semantic proximity Read ↗

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

⌁Select a neighboring publication to make it the new centre.