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Predicate | Object |
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rdf:type | |
lifeskim:mentions | |
pubmed:issue |
1
|
pubmed:dateCreated |
1997-2-27
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pubmed:abstractText |
New images, calculated from electron micrographs, show the three-dimensional structures of microtubules and tubulin sheets decorated stoichiometrically with globular motor protein domains (heads). Single heads of kinesin and ncd, the kinesin-related protein that moves in the reverse direction to kinesin, bind in the same way to the same site on tubulin. Dimeric kinesin and dimeric ncd show an interesting difference in the positions of their second heads.
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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 |
Feb
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pubmed:issn |
0955-0674
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pubmed:author | |
pubmed:issnType |
Print
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pubmed:volume |
9
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pubmed:owner |
NLM
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pubmed:authorsComplete |
Y
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pubmed:pagination |
4-11
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pubmed:dateRevised |
2005-11-16
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pubmed:meshHeading | |
pubmed:year |
1997
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pubmed:articleTitle |
The structure of microtubule-motor complexes.
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pubmed:affiliation |
Medical Research Council Laboratory of Molecular Biology, Medical Research Council, Centre Hills Road, Cambridge CB2 2QH, UK. laa@mrc-lmb.cam.ac.uk
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pubmed:publicationType |
Journal Article,
Review
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