Log in to save to my catalogue

Small molecule-mediated stabilization of vesicle-associated helical α-synuclein inhibits pathogenic...

Small molecule-mediated stabilization of vesicle-associated helical α-synuclein inhibits pathogenic...

https://devfeature-collection.sl.nsw.gov.au/record/TN_cdi_crossref_primary_10_1038_ncomms6857

Small molecule-mediated stabilization of vesicle-associated helical α-synuclein inhibits pathogenic misfolding and aggregation

About this item

Full title

Small molecule-mediated stabilization of vesicle-associated helical α-synuclein inhibits pathogenic misfolding and aggregation

Publisher

London: Nature Publishing Group UK

Journal title

Nature communications, 2014-12, Vol.5 (1), p.5857, Article 5857

Language

English

Formats

Publication information

Publisher

London: Nature Publishing Group UK

More information

Scope and Contents

Contents

α-synuclein is an abundant presynaptic protein that is important for regulation of synaptic vesicle trafficking, and whose misfolding plays a key role in Parkinson’s disease. While α-synuclein is disordered in solution, it folds into a helical conformation when bound to synaptic vesicles. Stabilization of helical, folded α-synuclein might therefore...

Alternative Titles

Full title

Small molecule-mediated stabilization of vesicle-associated helical α-synuclein inhibits pathogenic misfolding and aggregation

Identifiers

Primary Identifiers

Record Identifier

TN_cdi_crossref_primary_10_1038_ncomms6857

Permalink

https://devfeature-collection.sl.nsw.gov.au/record/TN_cdi_crossref_primary_10_1038_ncomms6857

Other Identifiers

ISSN

2041-1723

E-ISSN

2041-1723

DOI

10.1038/ncomms6857

How to access this item