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

Interfacial properties of α-synuclein's Parkinsonian variants.

Biophysical chemistry - 1 Jun 2023

Mohapatra Anshuman, Hans Amrita, Chaudhary Nitin

Abstract excerpt

Human alpha-synuclein (αS) is associated with the occurrence of Parkinson's disease. In the past decade, six autosomally dominant mutations have been identified in αS (SNCA) gene that translate into A30P, E46K, H50Q, G51D, A53E, and A53T mutations in the protein. These mutations alter the electrostatics and hydrophobicity of a cardinal region of the protein. A comprehensive comparison of interfacial properties of...

Read the complete abstract on PubMed

Topics

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

Share to Mutation
Share to alpha-Synuclein
Share to Gene Expression

Methodology Data sources Editorial policy Privacy About Contact Helena Bioinformatics

Share to Lipids

Share to Parkinson Disease

Source

Identifiers

PMID: 37019052
DOI: 10.1016/j.bpc.2023.107006

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

Interfacial properties of α-synuclein's Parkinsonian variants.PMID 37019052Read ↗

Helical alpha-synuclein forms highly conductive ion channels.Semantic proximity Read ↗

Combined Effects of Mutation and Ionic Strength on α-Synuclein Reveal Generic Features of Aggregation-Prone Monomeric States.Semantic proximity Read ↗

Structural Properties of α-Synuclein in Functional and Pathological ContextsSemantic proximity Read ↗

Aggregation and membrane activity of mutant A30P alpha-synuclein on mitochondrial membranes.Semantic proximity Read ↗

Aromaticity at position 39 in α‐synuclein: A modulator of amyloid fibril assembly and membrane‐bound conformationsSemantic proximity Read ↗

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

Alpha-synuclein selectively binds to anionic phospholipids embedded in liquid-disordered domains.Semantic proximity Read ↗

Pathogenic mutations shift the equilibria of alpha-synuclein single molecules towards structured conformers.Semantic proximity Read ↗

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

Direct evidence for upright and helical structure of alpha-synuclein at lipid membranesSemantic proximity Read ↗

Conformational Dynamics of α-Synuclein: A Study of its Intramolecular Forces in the Presence of Selected CompoundsSemantic proximity Read ↗

E46K Parkinson's-linked mutation enhances C-terminal-to-N-terminal contacts in alpha-synuclein.Semantic proximity Read ↗

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