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

Insights into the origin of the tendency of the PI3-SH3 domain to form amyloid fibrils.

Journal of molecular biology - 4 Oct 2002

Ventura Salvador, Lacroix Emmanuel, Serrano Luis

Abstract excerpt

The SH3 domain of the p85alpha subunit of phosphatidylinositol 3 kinase has been found to form amyloid fibrils in vitro under acidic conditions. PI3-SH3 is peculiar due to a large insertion of 15 amino acid residues in the n-Src loop when compared with more canonical members of the family. Spectrin-SH3 (SPC-SH3) with a shorter loop does not form fibrils under any of our conditions tested. Thus, it could be that...

Read the complete abstract on PubMed

Topics

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

Share to Amyloid
Share to Circular Dichroism
Share to Microscopy, Phase-Contrast

Methodology Data sources Editorial policy Privacy About Contact Helena Bioinformatics

Share to Phosphatidylinositol 3-Kinases

Share to Protein Subunits

Share to Spectrin

Share to src Homology Domains

Share to Thermodynamics

Source

Identifiers

PMID: 12367534
DOI: 10.1016/s0022-2836(02)00783-0

Provenance

PubMed metadata and Literature Corpus relationships. Corpus snapshot updated 7 Sept 2026. Manifest publication-graph-cohort-2026-09-07.1.

Source receipt: pubmed, retrieved 7 Sept 2026.

Related research

Semantic proximity does not establish scientific evidence.

Research trail→

Click a neighbor to travelStep 1 · 12 closest

Insights into the origin of the tendency of the PI3-SH3 domain to form amyloid fibrils.PMID 12367534Read ↗

A single mutation induces amyloid aggregation in the alpha-spectrin SH3 domain: analysis of the early stages of fibril formation.Semantic proximity Read ↗

Probing the mechanism of amyloidogenesis through a tandem repeat of the PI3-SH3 domain suggests a generic model for protein aggregation and fibril formation.Semantic proximity Read ↗

A single mutation in an SH3 domain increases amyloid aggregation by accelerating nucleation, but not by destabilizing thermodynamically the native state.Semantic proximity Read ↗

Atomic resolution structure of a mutant of the spectrin SH3 domain.Semantic proximity Read ↗

Characterization of oligomers of heterogeneous size as precursors of amyloid fibril nucleation of an SH3 domain: an experimental kinetics study.Semantic proximity Read ↗

The folding transition state between SH3 domains is conformationally restricted and evolutionarily conserved.Semantic proximity Read ↗

Hydrogen-exchange stability analysis of Bergerac-Src homology 3 variants allows the characterization of a folding intermediate in equilibrium.Semantic proximity Read ↗

The effect of a proline residue on the rate of growth and the space group of alpha-spectrin SH3-domain crystals.Semantic proximity Read ↗

Mapping the structure of amyloid nucleation precursors by protein engineering kinetic analysis.Semantic proximity Read ↗

A stable alpha-helix-rich intermediate is formed by a single mutation of the beta-sheet protein, src SH3, at pH 3.Semantic proximity Read ↗

Role of native topology investigated by multiple unfolding simulations of four SH3 domains.Semantic proximity Read ↗

High-resolution structure of an alpha-spectrin SH3-domain mutant with a redesigned hydrophobic core.Semantic proximity Read ↗

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