pubmed-article:8867735 | rdf:type | pubmed:Citation | lld:pubmed |
pubmed-article:8867735 | lifeskim:mentions | umls-concept:C0033684 | lld:lifeskim |
pubmed-article:8867735 | lifeskim:mentions | umls-concept:C0085139 | lld:lifeskim |
pubmed-article:8867735 | lifeskim:mentions | umls-concept:C1510470 | lld:lifeskim |
pubmed-article:8867735 | lifeskim:mentions | umls-concept:C1705994 | lld:lifeskim |
pubmed-article:8867735 | lifeskim:mentions | umls-concept:C1513492 | lld:lifeskim |
pubmed-article:8867735 | lifeskim:mentions | umls-concept:C1709533 | lld:lifeskim |
pubmed-article:8867735 | pubmed:issue | 3 | lld:pubmed |
pubmed-article:8867735 | pubmed:dateCreated | 1996-12-10 | lld:pubmed |
pubmed-article:8867735 | pubmed:abstractText | The cellular processes of transport, division and, possibly, early development all involve microtubule-based motors. Recent work shows that, unexpectedly, many of these cellular functions are carried out by different types of kinesin and kinesin-related motor proteins. The kinesin proteins are a large and rapidly growing family of microtubule-motor proteins that share a 340-amino-acid motor domain. Phylogenetic analysis of the conserved motor domains groups the kinesin proteins into a number of subfamilies, the members of which exhibit a common molecular organization and related functions. The kinesin proteins that belong to different subfamilies differ in their rates and polarity of movement along microtubules, and probably in the particles/organelles that they transport. The kinesins arose early in eukaryotic evolution and gene duplication has allowed functional specialization to occur, resulting in a surprisingly large number of different classes of these proteins adapted for intracellular transport of vesicles and organelles, and for assembly and force generation in the meiotic and mitotic spindles. | lld:pubmed |
pubmed-article:8867735 | pubmed:language | eng | lld:pubmed |
pubmed-article:8867735 | pubmed:journal | http://linkedlifedata.com/r... | lld:pubmed |
pubmed-article:8867735 | pubmed:citationSubset | IM | lld:pubmed |
pubmed-article:8867735 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
pubmed-article:8867735 | pubmed:status | MEDLINE | lld:pubmed |
pubmed-article:8867735 | pubmed:month | Mar | lld:pubmed |
pubmed-article:8867735 | pubmed:issn | 0265-9247 | lld:pubmed |
pubmed-article:8867735 | pubmed:author | pubmed-author:MooreJ DJD | lld:pubmed |
pubmed-article:8867735 | pubmed:author | pubmed-author:EndowS ASA | lld:pubmed |
pubmed-article:8867735 | pubmed:issnType | Print | lld:pubmed |
pubmed-article:8867735 | pubmed:volume | 18 | lld:pubmed |
pubmed-article:8867735 | pubmed:owner | NLM | lld:pubmed |
pubmed-article:8867735 | pubmed:authorsComplete | Y | lld:pubmed |
pubmed-article:8867735 | pubmed:pagination | 207-19 | lld:pubmed |
pubmed-article:8867735 | pubmed:dateRevised | 2006-11-15 | lld:pubmed |
pubmed-article:8867735 | pubmed:meshHeading | pubmed-meshheading:8867735-... | lld:pubmed |
pubmed-article:8867735 | pubmed:meshHeading | pubmed-meshheading:8867735-... | lld:pubmed |
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pubmed-article:8867735 | pubmed:meshHeading | pubmed-meshheading:8867735-... | lld:pubmed |
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pubmed-article:8867735 | pubmed:meshHeading | pubmed-meshheading:8867735-... | lld:pubmed |
pubmed-article:8867735 | pubmed:year | 1996 | lld:pubmed |
pubmed-article:8867735 | pubmed:articleTitle | Kinesin proteins: a phylum of motors for microtubule-based motility. | lld:pubmed |
pubmed-article:8867735 | pubmed:affiliation | Department of Microbiology, Duke University Medical Center, Durham, NC 27710, USA. moore@abacus.mc.duke.edu | lld:pubmed |
pubmed-article:8867735 | pubmed:publicationType | Journal Article | lld:pubmed |
pubmed-article:8867735 | pubmed:publicationType | Research Support, U.S. Gov't, P.H.S. | lld:pubmed |
pubmed-article:8867735 | pubmed:publicationType | Review | lld:pubmed |
pubmed-article:8867735 | pubmed:publicationType | Research Support, Non-U.S. Gov't | lld:pubmed |
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