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rdf:type |
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lifeskim:mentions |
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pubmed:issue |
5124
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pubmed:dateCreated |
1993-9-14
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pubmed:abstractText |
Microtubule polarity arises from the head-to-tail orientation of alpha-beta tubulin heterodimers in the microtubule lattice. The identity of the polypeptide at each end of the microtubule is unknown, but structural models predict that the beta-tubulin end contains an exchangeable guanosine triphosphate (GTP) binding site. When GTP-coated fluorescent beads were incubated with microtubules, they bound specifically to plus ends, suggesting that tubulin is oriented in microtubules with beta-tubulin toward the plus end.
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pubmed:grant |
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pubmed:language |
eng
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pubmed:journal |
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pubmed:citationSubset |
IM
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pubmed:chemical |
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pubmed:status |
MEDLINE
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pubmed:month |
Aug
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pubmed:issn |
0036-8075
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pubmed:author |
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pubmed:issnType |
Print
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pubmed:day |
20
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pubmed:volume |
261
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pubmed:owner |
NLM
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pubmed:authorsComplete |
Y
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pubmed:pagination |
1044-7
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pubmed:dateRevised |
2007-11-14
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pubmed:meshHeading |
pubmed-meshheading:8102497-Adenosine Triphosphate,
pubmed-meshheading:8102497-Animals,
pubmed-meshheading:8102497-Binding, Competitive,
pubmed-meshheading:8102497-Binding Sites,
pubmed-meshheading:8102497-Ethylmaleimide,
pubmed-meshheading:8102497-Guanosine Triphosphate,
pubmed-meshheading:8102497-Microtubules,
pubmed-meshheading:8102497-Paclitaxel,
pubmed-meshheading:8102497-Tetrahymena,
pubmed-meshheading:8102497-Tubulin
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pubmed:year |
1993
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pubmed:articleTitle |
Localization of an exchangeable GTP binding site at the plus end of microtubules.
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pubmed:affiliation |
Department of Pharmacology, University of California, San Francisco 94143-0450.
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pubmed:publicationType |
Journal Article,
Research Support, U.S. Gov't, P.H.S.,
Research Support, Non-U.S. Gov't
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