期刊
MOLECULAR NEUROBIOLOGY
卷 47, 期 2, 页码 622-631出版社
HUMANA PRESS INC
DOI: 10.1007/s12035-012-8338-x
关键词
Single-molecule fluorescence; Aggregation; Amyloid; Oligomers; Parkinson's disease
资金
- NIA NIH HHS [F31 AG038110] Funding Source: Medline
- NIGMS NIH HHS [T32 GM007223] Funding Source: Medline
The aggregation and deposition of the neuronal protein alpha-synuclein in the substantia nigra region of the brain is a key pathological feature of Parkinson's disease. alpha-Synuclein assembles from a monomeric state in solution, which lacks stable secondary and tertiary contacts, into highly structured fibrillar aggregates through a pathway which involves the population of multiple oligomeric species over a range of time scales. These features make alpha-synuclein well suited for study with single-molecule techniques, which are particularly useful for characterizing dynamic, heterogeneous samples. Here, we review the current literature featuring single-molecule fluorescence studies of alpha-synuclein and discuss how these studies have contributed to our understanding of both its function and its role in disease.
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