| pubmed-article:16892050 | rdf:type | pubmed:Citation | lld:pubmed |
| pubmed-article:16892050 | lifeskim:mentions | umls-concept:C0021467 | lld:lifeskim |
| pubmed-article:16892050 | lifeskim:mentions | umls-concept:C1510470 | lld:lifeskim |
| pubmed-article:16892050 | lifeskim:mentions | umls-concept:C0021469 | lld:lifeskim |
| pubmed-article:16892050 | pubmed:issue | 9 | lld:pubmed |
| pubmed-article:16892050 | pubmed:dateCreated | 2006-8-21 | lld:pubmed |
| pubmed-article:16892050 | pubmed:databankReference | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:16892050 | pubmed:databankReference | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:16892050 | pubmed:abstractText | Small-molecule inhibitors of kinesin-5 (refs. 1-3), a protein essential for eukaryotic cell division, represent alternatives to antimitotic agents that target tubulin. While tubulin is needed for multiple intracellular processes, the known functions of kinesin-5 are limited to dividing cells, making it likely that kinesin-5 inhibitors would have fewer side effects than do tubulin-targeting drugs. Kinesin-5 inhibitors, such as monastrol, act through poorly understood allosteric mechanisms, not competing with ATP binding. Moreover, the microscopic mechanism of full-length kinesin-5 motility is not known. Here we characterize the motile properties and allosteric inhibition of Eg5, a vertebrate kinesin-5, using a GFP fusion protein in single-molecule fluorescence assays. We find that Eg5 is a processive kinesin whose motility includes, in addition to ATP-dependent directional motion, a diffusive component not requiring ATP hydrolysis. Monastrol suppresses the directional processive motility of microtubule-bound Eg5. These data on Eg5's allosteric inhibition will impact these inhibitors' use as probes and development as chemotherapeutic agents. | lld:pubmed |
| pubmed-article:16892050 | pubmed:grant | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:16892050 | pubmed:language | eng | lld:pubmed |
| pubmed-article:16892050 | pubmed:journal | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:16892050 | pubmed:citationSubset | IM | lld:pubmed |
| pubmed-article:16892050 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:16892050 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
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| pubmed-article:16892050 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:16892050 | pubmed:status | MEDLINE | lld:pubmed |
| pubmed-article:16892050 | pubmed:month | Sep | lld:pubmed |
| pubmed-article:16892050 | pubmed:issn | 1552-4450 | lld:pubmed |
| pubmed-article:16892050 | pubmed:author | pubmed-author:SchmidtChrist... | lld:pubmed |
| pubmed-article:16892050 | pubmed:author | pubmed-author:KapoorTarun... | lld:pubmed |
| pubmed-article:16892050 | pubmed:author | pubmed-author:PetermanErwin... | lld:pubmed |
| pubmed-article:16892050 | pubmed:author | pubmed-author:KwokBenjamin... | lld:pubmed |
| pubmed-article:16892050 | pubmed:author | pubmed-author:KapiteinLukas... | lld:pubmed |
| pubmed-article:16892050 | pubmed:author | pubmed-author:KimJeffrey... | lld:pubmed |
| pubmed-article:16892050 | pubmed:issnType | Print | lld:pubmed |
| pubmed-article:16892050 | pubmed:volume | 2 | lld:pubmed |
| pubmed-article:16892050 | pubmed:owner | NLM | lld:pubmed |
| pubmed-article:16892050 | pubmed:authorsComplete | Y | lld:pubmed |
| pubmed-article:16892050 | pubmed:pagination | 480-5 | lld:pubmed |
| pubmed-article:16892050 | pubmed:dateRevised | 2007-11-14 | lld:pubmed |
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| pubmed-article:16892050 | pubmed:meshHeading | pubmed-meshheading:16892050... | lld:pubmed |
| pubmed-article:16892050 | pubmed:meshHeading | pubmed-meshheading:16892050... | lld:pubmed |
| pubmed-article:16892050 | pubmed:meshHeading | pubmed-meshheading:16892050... | lld:pubmed |
| pubmed-article:16892050 | pubmed:meshHeading | pubmed-meshheading:16892050... | lld:pubmed |
| pubmed-article:16892050 | pubmed:meshHeading | pubmed-meshheading:16892050... | lld:pubmed |
| pubmed-article:16892050 | pubmed:year | 2006 | lld:pubmed |
| pubmed-article:16892050 | pubmed:articleTitle | Allosteric inhibition of kinesin-5 modulates its processive directional motility. | lld:pubmed |
| pubmed-article:16892050 | pubmed:affiliation | Laboratory of Chemistry and Cell Biology, The Rockefeller University, 1230 York Avenue, New York, New York 10021, USA. | lld:pubmed |
| pubmed-article:16892050 | pubmed:publicationType | Journal Article | lld:pubmed |
| pubmed-article:16892050 | pubmed:publicationType | Research Support, Non-U.S. Gov't | lld:pubmed |
| pubmed-article:16892050 | pubmed:publicationType | Research Support, N.I.H., Extramural | lld:pubmed |
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