| pubmed-article:9822636 | rdf:type | pubmed:Citation | lld:pubmed |
| pubmed-article:9822636 | lifeskim:mentions | umls-concept:C0205474 | lld:lifeskim |
| pubmed-article:9822636 | lifeskim:mentions | umls-concept:C0376315 | lld:lifeskim |
| pubmed-article:9822636 | lifeskim:mentions | umls-concept:C0871161 | lld:lifeskim |
| pubmed-article:9822636 | pubmed:issue | 48 | lld:pubmed |
| pubmed-article:9822636 | pubmed:dateCreated | 1998-12-23 | lld:pubmed |
| pubmed-article:9822636 | pubmed:databankReference | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:9822636 | pubmed:abstractText | Kinectin, an integral membrane protein (160 kDa), was identified as a kinesin-binding protein. Analysis of the predicted amino acid sequence of kinectin cDNA indicated an alpha-helical coiled-coil structure from amino acid 320 to 1310. A 120-kDa kinectin has been observed consistently, and N-terminal sequencing showed that 232 amino acids were missing from the N terminus of full-length kinectin. 120-kDa kinectin was distributed in the supernatant and a low density fraction of vesicles, whereas both forms were in the high density fraction of vesicles. In the electron microscope, the 120-kDa form appeared as a linear molecule of 133 nm in length. In hydrodynamic studies, the cytosolic 120-kDa kinectin was a dimer. Monoclonal antibody molecules (anti-kinectin KR160.9) bound asymmetrically to kinectin often with two antibodies/kinectin, indicative of a parallel coiled-coil. Metabolic labeling with [3H]myristic acid showed that both the 120- and 160-kDa kinectin are myristoylated in chick embryo fibroblasts. The myristoylation of 120-kDa kinectin may provide a mechanism for linking it to a low density fraction of vesicles. Immunoprecipitation with a 160-kDa kinectin-specific antibody brought down the 120-kDa kinectin. Thus, we suggest that kinectin is an extended parallel coiled-coil dimer, often a heterodimer. | lld:pubmed |
| pubmed-article:9822636 | pubmed:grant | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:9822636 | pubmed:language | eng | lld:pubmed |
| pubmed-article:9822636 | pubmed:journal | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:9822636 | pubmed:citationSubset | IM | lld:pubmed |
| pubmed-article:9822636 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:9822636 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
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| pubmed-article:9822636 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:9822636 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:9822636 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:9822636 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:9822636 | pubmed:status | MEDLINE | lld:pubmed |
| pubmed-article:9822636 | pubmed:month | Nov | lld:pubmed |
| pubmed-article:9822636 | pubmed:issn | 0021-9258 | lld:pubmed |
| pubmed-article:9822636 | pubmed:author | pubmed-author:SheetzM PMP | lld:pubmed |
| pubmed-article:9822636 | pubmed:author | pubmed-author:EricksonH PHP | lld:pubmed |
| pubmed-article:9822636 | pubmed:author | pubmed-author:KumarJJ | lld:pubmed |
| pubmed-article:9822636 | pubmed:issnType | Print | lld:pubmed |
| pubmed-article:9822636 | pubmed:day | 27 | lld:pubmed |
| pubmed-article:9822636 | pubmed:volume | 273 | lld:pubmed |
| pubmed-article:9822636 | pubmed:owner | NLM | lld:pubmed |
| pubmed-article:9822636 | pubmed:authorsComplete | Y | lld:pubmed |
| pubmed-article:9822636 | pubmed:pagination | 31738-43 | lld:pubmed |
| pubmed-article:9822636 | pubmed:dateRevised | 2011-11-17 | lld:pubmed |
| pubmed-article:9822636 | pubmed:meshHeading | pubmed-meshheading:9822636-... | lld:pubmed |
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| pubmed-article:9822636 | pubmed:meshHeading | pubmed-meshheading:9822636-... | lld:pubmed |
| pubmed-article:9822636 | pubmed:meshHeading | pubmed-meshheading:9822636-... | lld:pubmed |
| pubmed-article:9822636 | pubmed:meshHeading | pubmed-meshheading:9822636-... | lld:pubmed |
| pubmed-article:9822636 | pubmed:meshHeading | pubmed-meshheading:9822636-... | lld:pubmed |
| pubmed-article:9822636 | pubmed:year | 1998 | lld:pubmed |
| pubmed-article:9822636 | pubmed:articleTitle | Ultrastructural and biochemical properties of the 120-kDa form of chick kinectin. | lld:pubmed |
| pubmed-article:9822636 | pubmed:affiliation | Department of Cell Biology, Duke University Medical Center, Durham, North Carolina 27710, USA. | lld:pubmed |
| pubmed-article:9822636 | pubmed:publicationType | Journal Article | lld:pubmed |
| pubmed-article:9822636 | pubmed:publicationType | Research Support, U.S. Gov't, P.H.S. | lld:pubmed |
| entrez-gene:396335 | entrezgene:pubmed | pubmed-article:9822636 | lld:entrezgene |
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| http://linkedlifedata.com/r... | pubmed:referesTo | pubmed-article:9822636 | lld:pubmed |
