| Literature DB >> 15504363 |
Thomas Doohun Kim1, Eunjin Choi, Hyangshuk Rhim, Seung R Paik, Chul-Hak Yang.
Abstract
The aggregation and fibrillization of alpha-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 alpha-synuclein is not yet clearly elucidated. Here, we showed that C-terminal region of alpha-synuclein is similar to alpha-crystalline domain of small heat shock proteins. In our experiments, alpha-synuclein, like small heat shock proteins, protected cellular proteins from denaturation, and confer Escherichia coli cellular tolerances against thermal- and oxidative-stresses.Entities:
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Year: 2004 PMID： 15504363 DOI： 10.1016/j.bbrc.2004.09.208
Source DB: PubMed Journal: Biochem Biophys Res Commun ISSN： 0006-291X Impact factor: 3.575