pubmed-article:7787244 | rdf:type | pubmed:Citation | lld:pubmed |
pubmed-article:7787244 | lifeskim:mentions | umls-concept:C0033684 | lld:lifeskim |
pubmed-article:7787244 | lifeskim:mentions | umls-concept:C1519249 | lld:lifeskim |
pubmed-article:7787244 | lifeskim:mentions | umls-concept:C1710082 | lld:lifeskim |
pubmed-article:7787244 | lifeskim:mentions | umls-concept:C0936012 | lld:lifeskim |
pubmed-article:7787244 | lifeskim:mentions | umls-concept:C1880022 | lld:lifeskim |
pubmed-article:7787244 | lifeskim:mentions | umls-concept:C0205225 | lld:lifeskim |
pubmed-article:7787244 | pubmed:issue | 2 | lld:pubmed |
pubmed-article:7787244 | pubmed:dateCreated | 1995-7-24 | lld:pubmed |
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pubmed-article:7787244 | pubmed:databankReference | http://linkedlifedata.com/r... | lld:pubmed |
pubmed-article:7787244 | pubmed:abstractText | Kinectin is a kinesin-binding protein (Toyoshima et al., 1992) that is required for kinesin-based motility (Kumar et al., 1995). A kinectin cDNA clone containing a 4.7-kilobase insert was isolated from an embryonic chick brain cDNA library by immunoscreening with a panel of monoclonal antibodies. The cDNA contained an open reading frame of 1364 amino acids encoding a protein of 156 kDa. A bacterially expressed product of the full length cDNA bound purified kinesin. Transient expression in CV-1 cells gave an endoplasmic reticulum distribution that depended upon the N-terminal domain. Analysis of the predicted amino acid sequence indicated a highly hydrophobic near N-terminal stretch of 28 amino acids and a large portion (326-1248) of predicted alpha helical coiled coils. The 30-kDa fragment containing the N-terminal hydrophobic region was produced by cell-free in vitro translation and found to assemble with canine pancreas rough microsomes. Cleavage of the N terminus was not observed confirming its role as a potential transmembrane domain. Thus, the kinectin cDNA encodes a cytoplasmic-oriented integral membrane protein that binds kinesin and is likely to be a coiled-coil dimer. | lld:pubmed |
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pubmed-article:7787244 | pubmed:language | eng | lld:pubmed |
pubmed-article:7787244 | pubmed:journal | http://linkedlifedata.com/r... | lld:pubmed |
pubmed-article:7787244 | pubmed:citationSubset | IM | lld:pubmed |
pubmed-article:7787244 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
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pubmed-article:7787244 | pubmed:status | MEDLINE | lld:pubmed |
pubmed-article:7787244 | pubmed:month | Feb | lld:pubmed |
pubmed-article:7787244 | pubmed:issn | 1059-1524 | lld:pubmed |
pubmed-article:7787244 | pubmed:author | pubmed-author:BeckerMM | lld:pubmed |
pubmed-article:7787244 | pubmed:author | pubmed-author:YuHH | lld:pubmed |
pubmed-article:7787244 | pubmed:author | pubmed-author:SheetzM PMP | lld:pubmed |
pubmed-article:7787244 | pubmed:author | pubmed-author:KumarJJ | lld:pubmed |
pubmed-article:7787244 | pubmed:author | pubmed-author:NicchittaC... | lld:pubmed |
pubmed-article:7787244 | pubmed:author | pubmed-author:ToyoshimaII | lld:pubmed |
pubmed-article:7787244 | pubmed:issnType | Print | lld:pubmed |
pubmed-article:7787244 | pubmed:volume | 6 | lld:pubmed |
pubmed-article:7787244 | pubmed:owner | NLM | lld:pubmed |
pubmed-article:7787244 | pubmed:authorsComplete | Y | lld:pubmed |
pubmed-article:7787244 | pubmed:pagination | 171-83 | lld:pubmed |
pubmed-article:7787244 | pubmed:dateRevised | 2009-11-18 | lld:pubmed |
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