| pubmed-article:2148208 | rdf:type | pubmed:Citation | lld:pubmed |
| pubmed-article:2148208 | lifeskim:mentions | umls-concept:C0330390 | lld:lifeskim |
| pubmed-article:2148208 | lifeskim:mentions | umls-concept:C0026046 | lld:lifeskim |
| pubmed-article:2148208 | lifeskim:mentions | umls-concept:C0001443 | lld:lifeskim |
| pubmed-article:2148208 | lifeskim:mentions | umls-concept:C0021467 | lld:lifeskim |
| pubmed-article:2148208 | lifeskim:mentions | umls-concept:C0021469 | lld:lifeskim |
| pubmed-article:2148208 | lifeskim:mentions | umls-concept:C0205421 | lld:lifeskim |
| pubmed-article:2148208 | lifeskim:mentions | umls-concept:C0146894 | lld:lifeskim |
| pubmed-article:2148208 | pubmed:issue | 24 | lld:pubmed |
| pubmed-article:2148208 | pubmed:dateCreated | 1991-2-7 | lld:pubmed |
| pubmed-article:2148208 | pubmed:abstractText | Kinesin is a microtubule-activated ATPase that moves objects toward the plus end of microtubules and makes microtubules glide along a glass surface. Here we investigate a remarkable effect of the nonhydrolyzable analogue of ATP, adenosine 5'-[beta,gamma-imido]triphosphate (p[NH]ppA), on kinesin-driven microtubule gliding. Microtubule gliding that has been blocked by rapid replacement of ATP with p[NH]ppA requires 1-2 min of exposure to ATP before microtubule gliding resumes. This latency is not shortened by prolonged washing of p[NH]ppA-blocked microtubules in nucleotide-free buffer for up to 15 min, suggesting that ATP binding to a second nucleotide binding site on kinesin triggers the release of bound p[NH]ppA. To test this hypothesis, the release of [3H]p[NH]ppA from kinesin-microtubule complexes was followed in parallel biochemical assays. In nucleotide-free buffer, the bound p[NH]ppA was released over several hours from the complexes. However, addition of ATP caused the release of p[NH]ppA from the kinesin-microtubule complexes within 2 min, which was similar to the latent period for start-up of microtubule gliding after p[NH]ppA inhibition. The stoichiometry of p[NH]ppA bound per kinesin heavy chain at saturation was estimated to be approximately 1:2. These results suggest a model in which each molecule of kinesin has at least two nucleotide binding sites that alternately bind nucleotide. | lld:pubmed |
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| pubmed-article:2148208 | pubmed:language | eng | lld:pubmed |
| pubmed-article:2148208 | pubmed:journal | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:2148208 | pubmed:citationSubset | IM | lld:pubmed |
| pubmed-article:2148208 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
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| pubmed-article:2148208 | pubmed:status | MEDLINE | lld:pubmed |
| pubmed-article:2148208 | pubmed:month | Dec | lld:pubmed |
| pubmed-article:2148208 | pubmed:issn | 0027-8424 | lld:pubmed |
| pubmed-article:2148208 | pubmed:author | pubmed-author:ReeseT STS | lld:pubmed |
| pubmed-article:2148208 | pubmed:author | pubmed-author:KhanSS | lld:pubmed |
| pubmed-article:2148208 | pubmed:author | pubmed-author:SheetzM PMP | lld:pubmed |
| pubmed-article:2148208 | pubmed:author | pubmed-author:CriseBB | lld:pubmed |
| pubmed-article:2148208 | pubmed:author | pubmed-author:SchnappB JBJ | lld:pubmed |
| pubmed-article:2148208 | pubmed:issnType | Print | lld:pubmed |
| pubmed-article:2148208 | pubmed:volume | 87 | lld:pubmed |
| pubmed-article:2148208 | pubmed:owner | NLM | lld:pubmed |
| pubmed-article:2148208 | pubmed:authorsComplete | Y | lld:pubmed |
| pubmed-article:2148208 | pubmed:pagination | 10053-7 | lld:pubmed |
| pubmed-article:2148208 | pubmed:dateRevised | 2009-11-18 | lld:pubmed |
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| pubmed-article:2148208 | pubmed:meshHeading | pubmed-meshheading:2148208-... | lld:pubmed |
| pubmed-article:2148208 | pubmed:year | 1990 | lld:pubmed |
| pubmed-article:2148208 | pubmed:articleTitle | Delayed start-up of kinesin-driven microtubule gliding following inhibition by adenosine 5'-[beta,gamma-imido]triphosphate. | lld:pubmed |
| pubmed-article:2148208 | pubmed:affiliation | Department of Physiology, Boston University Medical Campus, MA 02118. | lld:pubmed |
| pubmed-article:2148208 | pubmed:publicationType | Journal Article | lld:pubmed |
| pubmed-article:2148208 | pubmed:publicationType | Research Support, U.S. Gov't, P.H.S. | lld:pubmed |
| pubmed-article:2148208 | pubmed:publicationType | Research Support, Non-U.S. Gov't | lld:pubmed |
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