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Cited by 540

The DOI matches its Crossref record; 1 of the 1 references it cites were found in a registry or an index.

A Broken α-Helix in Folded α-Synuclein

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Chandra, Sreeganga, Chen, Xiaocheng, Rizo, Josep, Jahn, Reinhard, Südhof, Thomas C.·2003·Journal of Biological Chemistry

Abstract

alpha-Synuclein is a small cytosolic protein of presynaptic nerve terminals composed of seven 11-residue repeats and a hydrophilic tail. alpha-Synuclein misfolding and dysfunction may contribute to the pathogenesis of Parkinson's disease and neurodegenerative dementias, but its normal folding and function are unknown. In solution, alpha-synuclein is natively unstructured but assumes an alpha-helical conformation upon binding to phospholipid membranes. We now show that this conformation of alpha-synuclein consists of two alpha-helical regions that are interrupted by a short break. The structural organization of the alpha-helices of alpha-synuclein was not anticipated by sequence analyses and may be important for its pathogenic role.

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Metadata

Authors
Chandra, S., Chen, X., Rizo, J., Jahn, R., & Südhof, T. C.
Venue
Journal of Biological Chemistry
Publisher
Elsevier BV
Published
2003-04
Volume
278
Issue
17
Pages
15313-15318
ISSN
0021-9258 (ISSN-L)
OpenAlex
W1844422703
Cited by
540
References
1
FWCI
13.46
Type
journal article
Language
en
Open access
hybrid

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CoChat. (2026). Citation check: A Broken α-Helix in Folded α-Synuclein. https://app.cochat.ai/papers/10.1074/jbc.m213128200
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Chandra, S., Chen, X., Rizo, J., Jahn, R., & Südhof, T. C. (2003). A Broken α-Helix in Folded α-Synuclein. Journal of Biological Chemistry. https://doi.org/10.1074/jbc.m213128200

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Contains information from the Semantic Scholar Academic Graph Datasets, made available under the ODC Attribution License (ODC-BY 1.0).

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