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

Modification of C Terminus Provides New Insights into the Mechanism of α-Synuclein Aggregation.

Biophysical journal - 21 Nov 2017

Afitska Kseniia, Fucikova Anna, Shvadchak Volodymyr V, Yushchenko Dmytro A

Abstract excerpt

Aggregation of neuronal protein α-synuclein leads to the formation of amyloid fibrils, which are associated with the development of Parkinson's disease. The mechanism of α-synuclein pathology is not fully understood and is a subject of active research in the field. To tackle this problem, the fusions of fluorescent proteins to α-synuclein C-terminus are often used in cellular and animal studies. The effects...

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 Dose-Response Relationship, Drug

Methodology Data sources Editorial policy Privacy About Contact Helena Bioinformatics

Share to Kinetics

Share to Mutation

Share to Protein Aggregates

Source

Open in PubMed Open full text

Identifiers

PMID: 28939194
DOI: 10.1016/j.bpj.2017.08.027
PMCID: PMC5700244

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

Modification of C Terminus Provides New Insights into the Mechanism of α-Synuclein Aggregation.PMID 28939194Read ↗

A Facile Method to Produce N-Terminally Truncated α-SynucleinSemantic proximity Read ↗

The status of the terminal regions of α-synuclein in different forms of aggregates during fibrillization.Semantic proximity Read ↗

Genetic Code Expansion, Enzymatic Modification, and C-Terminal Labeling Enable Facile Production of Highly Modified α-SynucleinSemantic proximity Read ↗

Effects of N-terminal Acetylation on the Aggregation of Disease-related α-synuclein VariantsSemantic proximity Read ↗

Role of α-Synuclein Regions in Nucleation and Elongation of Amyloid Fiber Assembly.Semantic proximity Read ↗

N-terminal acetylation reduces α-synuclein pathology in models of Parkinson’s diseaseSemantic proximity Read ↗

Acceleration of alpha-synuclein aggregation by homologous peptides.Semantic proximity Read ↗

Mechanisms of enhanced aggregation and fibril formation of Parkinson's disease-related variants of α-synuclein.Semantic proximity Read ↗

Carboxyl truncation of α-synuclein occurs early and is influenced by human APOE genotype in transgenic mouse models of α-synuclein pathogenesisSemantic proximity Read ↗

Residue-specific fluorescent probes of α-synuclein: detection of early events at the N- and C-termini during fibril assembly.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 ↗

Carboxy‐terminal truncations of mouse α‐synuclein alter aggregation and prion‐like seedingSemantic proximity Read ↗

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