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rdf:type |
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lifeskim:mentions |
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pubmed:issue |
4
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pubmed:dateCreated |
1978-4-17
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pubmed:abstractText |
A procedure is described for removing most of the GDP bound at the exchangeable GTP binding site (E site) of tubulin. Microtubule protein containing substoichiometric amounts of GDP at the E site is found to polymerize in response to: (a) two nonhydrolyzable ATP analogues, adenylyl imidodiphosphate (AMP-PNP) and adenylyl beta, gamma-methylenediphosphonate (AMP-PCP); and (b) substoichiometric levels of GTP or dGTP. The results are interpreted as suggesting that: (1) when GDP is removed from tubulin, the E site shows broad specificity for nucleoside triphosphates: (2) microtubule assembly can be induced by the binding of substoichiometric amounts of nucleoside triphosphate to the E site.
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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 |
Feb
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pubmed:issn |
0006-2960
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pubmed:author |
|
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pubmed:issnType |
Print
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pubmed:day |
21
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pubmed:volume |
17
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pubmed:owner |
NLM
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pubmed:authorsComplete |
Y
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pubmed:pagination |
734-40
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pubmed:dateRevised |
2006-11-15
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pubmed:meshHeading |
pubmed-meshheading:623742-Adenosine Triphosphate,
pubmed-meshheading:623742-Animals,
pubmed-meshheading:623742-Brain,
pubmed-meshheading:623742-Glycoproteins,
pubmed-meshheading:623742-Guanosine Diphosphate,
pubmed-meshheading:623742-Guanosine Triphosphate,
pubmed-meshheading:623742-Kinetics,
pubmed-meshheading:623742-Microtubules,
pubmed-meshheading:623742-Nerve Tissue Proteins,
pubmed-meshheading:623742-Protein Binding,
pubmed-meshheading:623742-Swine,
pubmed-meshheading:623742-Tubulin
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pubmed:year |
1978
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pubmed:articleTitle |
Nucleotide specificity in microtubule assembly in vitro.
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pubmed:publicationType |
Journal Article,
Research Support, U.S. Gov't, P.H.S.,
Research Support, U.S. Gov't, Non-P.H.S.
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