Source:http://linkedlifedata.com/resource/pubmed/id/20714568
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Predicate | Object |
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rdf:type | |
lifeskim:mentions | |
pubmed:issue |
36
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pubmed:dateCreated |
2010-9-2
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pubmed:abstractText |
Alpha-synuclein, a natively unstructured protein important in the neuropathology of Parkinson's disease, was found to form a Langmuir monolayer in an alpha-helical conformation with its helical axis parallel to the air-water interface. This study sheds light on the role of vesicles in neuronal cells in the accumulation/aggregation of alpha-synuclein.
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pubmed:grant | |
pubmed:language |
eng
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pubmed:journal | |
pubmed:citationSubset |
IM
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pubmed:chemical | |
pubmed:status |
MEDLINE
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pubmed:month |
Sep
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pubmed:issn |
1364-548X
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pubmed:author | |
pubmed:issnType |
Electronic
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pubmed:day |
28
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pubmed:volume |
46
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pubmed:owner |
NLM
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pubmed:authorsComplete |
Y
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pubmed:pagination |
6702-4
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pubmed:dateRevised |
2011-10-4
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pubmed:meshHeading |
pubmed-meshheading:20714568-Air,
pubmed-meshheading:20714568-Humans,
pubmed-meshheading:20714568-Parkinson Disease,
pubmed-meshheading:20714568-Protein Structure, Secondary,
pubmed-meshheading:20714568-Spectrophotometry, Infrared,
pubmed-meshheading:20714568-Water,
pubmed-meshheading:20714568-alpha-Synuclein
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pubmed:year |
2010
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pubmed:articleTitle |
Alpha-synuclein in alpha-helical conformation at air-water interface: implication of conformation and orientation changes during its accumulation/aggregation.
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pubmed:affiliation |
California State University, Los Angeles, 5151 State University Drive, Los Angeles, CA 90032, USA.
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pubmed:publicationType |
Journal Article,
Research Support, U.S. Gov't, Non-P.H.S.,
Research Support, N.I.H., Extramural
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