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

Stability of an aggregation-prone partially folded state of human profilin-1 correlates with aggregation propensity.

The Journal of biological chemistry - 29 Jun 2018

Del Poggetto Edoardo, Toto Angelo, Aloise Chiara, Di Piro Francesco, Gori Ludovica, Malatesta Francesco, Gianni Stefano, Chiti Fabrizio, Bemporad Francesco

Abstract excerpt

A set of missense mutations in the gene encoding profilin-1 has been linked to the onset of familial forms of ALS (fALS), also known as Lou Gehrig's disease. The pathogenic potential of these mutations is linked to the formation of intracellular inclusions of the mutant proteins and correlates with the mutation-induced destabilization of its native, fully folded state. However, the mechanism by which these...

Read the complete abstract on PubMed

Topics

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

Share to Amyotrophic Lateral Sclerosis
Share to Hydrogen-Ion Concentration

Methodology Data sources Editorial policy Privacy About Contact Helena Bioinformatics

Share to Mutation

Share to Profilins

Share to Protein Aggregates

Share to Protein Folding

Share to Protein Stability

Source

Open in PubMed Open full text

Identifiers

PMID: 29760185
DOI: 10.1074/jbc.RA118.002087
PMCID: PMC6028969

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

Stability of an aggregation-prone partially folded state of human profilin-1 correlates with aggregation propensity.PMID 29760185Read ↗

Mutations of Profilin-1 Associated with Amyotrophic Lateral Sclerosis Promote Aggregation Due to Structural Changes of Its Native State.Semantic proximity Read ↗

Biophysical analysis of three novel profilin-1 variants associated with amyotrophic lateral sclerosis indicates a correlation between their aggregation propensity and the structural features of their globular state.Semantic proximity Read ↗

Structural basis for mutation-induced destabilization of profilin 1 in ALS.Semantic proximity Read ↗

Histidine tautomerism dependent conformational transitions driven aggregation of profilin-1: Implications in amyotrophic lateral sclerosis.Semantic proximity Read ↗

Mechanistic insights into the conformational switch in profilin-1 subject to collective effects of mutation and histidine tautomerism.Semantic proximity Read ↗

Unlocked capacity of proteins to attack membranes characteristic of aggregation: the evil for diseases and aging from Pandora’s boxSemantic proximity Read ↗

ALS mutations in the TIA-1 prion-like domain trigger highly condensed pathogenic structures.Semantic proximity Read ↗

Resolving the paradox for protein aggregation diseases: NMR structure and dynamics of the membrane-embedded P56S-MSP causing ALS imply a common mechanism for aggregation-prone proteins to attack membranesSemantic proximity Read ↗

A Zn-dependent structural transition of SOD1 modulates its ability to undergo phase separation.Semantic proximity Read ↗

The effect of disease-associated mutations on the folding pathway of human prion protein.Semantic proximity Read ↗

ALS-causing mutations in profilin-1 alter its conformational dynamics: A computational approach to explain propensity for aggregation.Semantic proximity Read ↗

Slow Misfolding of a Molten Globule form of a Mutant Prion Protein Variant into a β-rich Dimer.Semantic proximity Read ↗

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