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

From intrinsically disordered protein to context-dependent folding: The α-synuclein tetramer is teased out of hiding.

Proceedings of the National Academy of Sciences of the United States of America - 4 Aug 2015

Pochapsky Thomas C

Abstract excerpt

No abstract is available from the source.

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 Mutation
Share to Neurons
Share to Protein Multimerization

Methodology Data sources Editorial policy Privacy About Contact Helena Bioinformatics

Share to Repetitive Sequences, Amino Acid

Source

Open in PubMed Open full text

Identifiers

PMID: 26204916
DOI: 10.1073/pnas.1512077112
PMCID: PMC4534271

Provenance

PubMed metadata and Literature Corpus relationships. Corpus snapshot updated 8 Sept 2026.

Related research

Semantic proximity does not establish scientific evidence.

Research trail→

Click a neighbor to travelStep 1 · 12 closest

From intrinsically disordered protein to context-dependent folding: The α-synuclein tetramer is teased out of hiding.PMID 26204916Read ↗

Pathological unfoldomics of uncontrolled chaos: intrinsically disordered proteins and human diseases.Semantic proximity Read ↗

Aggregation prone regions and gatekeeping residues in protein sequences.Semantic proximity Read ↗

The amyloid state of proteins: A boon or bane?Semantic proximity Read ↗

BIOMEDICINE: One Misfolded Protein Allows Others to Sneak By.Semantic proximity Read ↗

Rationally Designed Variants of α-Synuclein Illuminate Its in vivo Structural Properties in Health and DiseaseSemantic proximity Read ↗

Structural biology. Versatility from protein disorder.Semantic proximity Read ↗

Molecular determinants of protein pathogenicity at the single-aggregate levelSemantic proximity Read ↗

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

A targetable N-terminal motif orchestrates α-Synuclein oligomer to fibril conversionSemantic proximity Read ↗

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

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

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