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

Controlling aggregation propensity in A53T mutant of alpha-synuclein causing Parkinson's disease.

Biochemical and biophysical research communications - 18 Sept 2009

Kumar Sonu, Sarkar Anita, Sundar Durai

Abstract excerpt

Understanding alpha-synuclein in terms of fibrillization, aggregation, solubility and stability is fundamental in Parkinson's disease (PD). The three familial mutations, namely, A30P, E46K and A53T cause PD because the hydrophobic regions in alpha-synuclein acquire beta-sheet configuration, and have a propensity to fibrillize and form amyloids that cause cytotoxicity and neurodegeneration. On simulating the...

Read the complete abstract on PubMed

Topics

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

Share to alpha-Synuclein
Share to Amino Acid Substitution
Share to Parkinson Disease

Methodology Data sources Editorial policy Privacy About Contact Helena Bioinformatics

Share to Protein Stability

Share to Protein Structure, Secondary

Share to Solubility

Share to Thermodynamics

Share to Valine

Source

Identifiers

PMID: 19580781
DOI: 10.1016/j.bbrc.2009.07.008

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

Controlling aggregation propensity in A53T mutant of alpha-synuclein causing Parkinson's disease.PMID 19580781Read ↗

Comparison of Kinetics, Toxicity, Oligomer Formation, and Membrane Binding Capacity of α-Synuclein Familial Mutations at the A53 Site, Including the Newly Discovered A53V Mutation.Semantic proximity Read ↗

Computational investigation on the effects of H50Q and G51D mutations on the α-Synuclein aggregation propensity.Semantic proximity Read ↗

Comparison of structure and dynamics of micelle-bound human alpha-synuclein and Parkinson disease variants.Semantic proximity Read ↗

Engineered alpha-synuclein prevents wild type and familial Parkin variant fibril formation.Semantic proximity Read ↗

Familial Parkinson Disease-associated Mutations Alter the Site-specific Microenvironment and Dynamics of α-SynucleinSemantic proximity Read ↗

Alteration of the alpha-synuclein folding landscape by a mutation related to Parkinson's disease.Semantic proximity Read ↗

The α-synuclein hereditary mutation E46K unlocks a more stable, pathogenic fibril structureSemantic proximity Read ↗

E46K Mutation of α-Synuclein Preorganizes the Intramolecular Interactions Crucial for Aggregation.Semantic proximity Read ↗

Site-specific perturbations of alpha-synuclein fibril structure by the Parkinson's disease associated mutations A53T and E46K.Semantic proximity Read ↗

The H50Q mutation induces a 10-fold decrease in the solubility of α-synuclein.Semantic proximity Read ↗

Site-specific fluorescence dynamics of α-synuclein fibrils using time-resolved fluorescence studies: effect of familial Parkinson's disease-associated mutations.Semantic proximity Read ↗

The α-synuclein hereditary mutation E46K unlocks a more stable, pathogenic fibril structureSemantic proximity Read ↗

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