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Cited by 507

The DOI matches its Crossref record; 11 of the 11 references it cites were found in a registry or an index.

Mutant and Wild Type Human α-Synucleins Assemble into Elongated Filaments with Distinct Morphologies in Vitro

Open access
Giasson, Benoit I., Uryu, Kunihiro, Trojanowski, John Q., Lee, Virginia M.-Y·1999·Journal of Biological Chemistry

Abstract

alpha-Synuclein is a soluble presynaptic protein which is pathologically redistributed within intracellular lesions characteristic of several neurodegenerative diseases. Here we demonstrate that wild type and two mutant forms of alpha-synuclein linked to familial Parkinson's disease (Ala30 --> Pro and Ala53 --> Thr) self-aggregate and assemble into 10-19-nm-wide filaments with distinct morphologies under defined in vitro conditions. Immunogold labeling demonstrates that the central region of all these filaments are more robustly labeled than the N-terminal or C-terminal regions, suggesting that the latter regions are buried within the filaments. Since in vitro generated alpha-synuclein filaments resemble the major ultrastructural elements of authentic Lewy bodies that are hallmark lesions of Parkinson's disease, we propose that self-aggregating alpha-synuclein is the major subunit protein of these filamentous lesions.

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Metadata

Authors
Giasson, B. I., Uryu, K., Trojanowski, J. Q., & Lee, V. M.-Y.
Venue
Journal of Biological Chemistry
Publisher
Elsevier BV
Published
1999-03
Volume
274
Issue
12
Pages
7619-7622
ISSN
0021-9258 (ISSN-L)
OpenAlex
W2001407922
Cited by
507
References
11
FWCI
28.53
Type
journal article
Language
en
Open access
hybrid

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CoChat. (2026). Citation check: Mutant and Wild Type Human α-Synucleins Assemble into Elongated Filaments with Distinct Morphologies in Vitro. https://app.cochat.ai/papers/10.1074/jbc.274.12.7619
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Giasson, B. I., Uryu, K., Trojanowski, J. Q., & Lee, V. M.-Y. (1999). Mutant and Wild Type Human α-Synucleins Assemble into Elongated Filaments with Distinct Morphologies in Vitro. Journal of Biological Chemistry. https://doi.org/10.1074/jbc.274.12.7619

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