alpha-synuclein has structural and functional similarities to small heat shock proteins
- Authors
- Kim, Thomas Doohun; Choi, E; Rhim, H; Paik, SR; Yang, CH
- Issue Date
- Nov-2004
- Publisher
- ACADEMIC PRESS
- Keywords
- Parkinson's disease; Small heat shock protein; α-Synuclein
- Citation
- BIOCHEMICAL AND BIOPHYSICAL RESEARCH COMMUNICATIONS, v.324, no.4, pp 1352 - 1359
- Pages
- 8
- Journal Title
- BIOCHEMICAL AND BIOPHYSICAL RESEARCH COMMUNICATIONS
- Volume
- 324
- Number
- 4
- Start Page
- 1352
- End Page
- 1359
- URI
- https://scholarworks.sookmyung.ac.kr/handle/2020.sw.sookmyung/159227
- DOI
- 10.1016/j.bbrc.2004.09.208
- ISSN
- 0006-291X
1090-2104
- Abstract
- The aggregation and fibrillization of α-synuclein, a major component of Lewy bodies, is a key event in Parkinson's disease. Although the mechanisms of fibrils formation are largely investigated, physiological function of α-synuclein is not yet clearly elucidated. Here, we showed that C-terminal region of α-synuclein is similar to α-crystalline domain of small heat shock proteins. In our experiments, α-synuclein, like small heat shock proteins, protected cellular proteins from denaturation, and confer Escherichia coli cellular tolerances against thermal- and oxidative-stresses. © 2004 Elsevier Inc. All rights reserved.
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