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Cited by 258

The DOI matches its Crossref record; 5 of the 5 references it cites were found in a registry or an index.

Effects of the mutations Ala30 to Pro and Ala53 to Thr on the physical and morphological properties of α‐synuclein protein implicated in Parkinson's disease

Open access
El-Agnaf, Omar M.A, Jakes, Ross, Curran, Martin D, Wallace, Andrew·1998·FEBS Letters

Abstract

α‐Synuclein (α‐syn) protein has been found in association with the pathological lesions of a number of neurodegenerative diseases. Recently, mutations in the α‐syn gene have been reported in families susceptible to an inherited form of Parkinson's disease. We report here that human wild‐type α‐syn, PD‐linked mutant α‐syn(Ala30Pro) and mutant α‐syn(Ala53Thr) proteins can self‐aggregate and form amyloid‐like filaments. The mutant α‐syn forms more β‐sheet and mature filaments than the wild‐type protein. These findings suggest that accumulation of α‐syn as insoluble deposits of amyloid may play a major role in the pathogenesis of these neurodegenerative diseases.

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Metadata

Authors
El-Agnaf, O. M. A., Jakes, R., Curran, M. D., & Wallace, A.
Venue
FEBS Letters
Publisher
Wiley
Published
1998-11-27
Volume
440
Issue
1-2
Pages
67-70
ISSN
  • 0014-5793 (ISSN-L)
  • 1873-3468
OpenAlex
W1972646996
Cited by
258
References
5
FWCI
15.67
Type
journal article
Language
en
Open access
bronze

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CoChat. (2026). Citation check: Effects of the mutations Ala30 to Pro and Ala53 to Thr on the physical and morphological properties of α‐synuclein protein implicated in Parkinson's disease. https://app.cochat.ai/papers/10.1016/s0014-5793(98)01419-7
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El-Agnaf, O. M. A., Jakes, R., Curran, M. D., & Wallace, A. (1998). Effects of the mutations Ala30 to Pro and Ala53 to Thr on the physical and morphological properties of α‐synuclein protein implicated in Parkinson's disease. FEBS Letters. https://doi.org/10.1016/s0014-5793(98)01419-7

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