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

Early sodium dodecyl sulfate induced collapse of α-synuclein correlates with its amyloid formation.

ACS chemical neuroscience - 18 Feb 2015

Basak Sujit, Prasad G V R Krishna, Varkey Jobin, Chattopadhyay Krishnananda

Abstract excerpt

The aggregation of α-synuclein (A-syn) has been implicated strongly in Parkinson's disease (PD). In vitro studies established A-syn to be a member of the intrinsically disordered protein (IDP) family. This protein undergoes structural interconversion between an extended and a compact state, and this equilibrium influences the mechanism of its aggregation. A combination of fluorescence resonance energy transfer...

Read the complete abstract on PubMed

Topics

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

Share to Benzothiazoles
Share to Entropy
Share to Fluorescence Resonance Energy Transfer

Methodology Data sources Editorial policy Privacy About Contact Helena Bioinformatics

Share to Glycerol

Share to Sodium Dodecyl Sulfate

Share to Solutions

Share to Solvents

Source

Identifiers

PMID: 25369246
DOI: 10.1021/cn500168x

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

Early sodium dodecyl sulfate induced collapse of α-synuclein correlates with its amyloid formation.PMID 25369246Read ↗

Reconstitution of Helical Soluble α-Synuclein through Transient Interaction with Lipid InterfacesSemantic proximity Read ↗

Alteration of Structure and Aggregation of α-Synuclein by Familial Parkinson's Disease Associated Mutations.Semantic proximity Read ↗

Unfolding Sequence-Specific Enigma in Monomeric α-Synuclein: Implications for Parkinson's Disease.Semantic proximity Read ↗

High stability and cooperative unfolding of α-synuclein oligomers.Semantic proximity Read ↗

Alpha-synuclein and familial variants affect the chain order and the thermotropic phase behavior of anionic lipid vesicles.Semantic proximity Read ↗

Structural conversion of α-synuclein at the mitochondria induces neuronal toxicitySemantic proximity Read ↗

The structural heterogeneity of α-synuclein is governed by several distinct subpopulations with interconversion times slower than millisecondsSemantic proximity Read ↗

Alpha-synuclein has a high affinity for packing defects in a bilayer membrane: a thermodynamics study.Semantic proximity Read ↗

Effects of impaired membrane interactions on α-synuclein aggregation and neurotoxicity.Semantic proximity Read ↗

The lipid-binding domain of wild type and mutant alpha-synuclein: compactness and interconversion between the broken and extended helix forms.Semantic proximity Read ↗

Parkinson's disease-specific α-Synuclein variants potentially drive Lewy body formation by engaging in promiscuous and non-functional interactions.Semantic proximity Read ↗

Biophysical approaches to characterising protein-protein interactions and intermediate species in protein aggregationSemantic proximity Read ↗

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