Physiological and pathological properties of alpha-synuclein
alpha-Synuclein belongs to a small group of natively unfolded proteins that can transiently bind to lipid membranes and acquire a partial alpha-helical conformation. Under certain pathogenic conditions, alpha-synuclein aggregates to form oligomers and insoluble fibrils with increased ss-sheet config...
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Published in | Cellular and molecular life sciences : CMLS Vol. 64; no. 17; pp. 2194 - 2201 |
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Main Authors | , |
Format | Journal Article |
Language | English |
Published |
Switzerland
Birkhäuser-Verlag
01.09.2007
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Subjects | |
Online Access | Get full text |
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Summary: | alpha-Synuclein belongs to a small group of natively unfolded proteins that can transiently bind to lipid membranes and acquire a partial alpha-helical conformation. Under certain pathogenic conditions, alpha-synuclein aggregates to form oligomers and insoluble fibrils with increased ss-sheet configuration. Although genetic mutations and multiplications of the gene have been found in familial cases, the mechanism by which this protein aggregates in sporadic cases of Parkinson's disease, dementia with Lewy bodies and multisystem atrophy is not fully understood. Here we review the function of alpha-synuclein and recent insight into the mechanisms by which it aggregates. |
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Bibliography: | ObjectType-Article-2 SourceType-Scholarly Journals-1 ObjectType-Feature-3 content type line 23 ObjectType-Review-1 |
ISSN: | 1420-682X 1420-9071 |
DOI: | 10.1007/s00018-007-7217-5 |