pubmed-article:3909887 | rdf:type | pubmed:Citation | lld:pubmed |
pubmed-article:3909887 | lifeskim:mentions | umls-concept:C0029246 | lld:lifeskim |
pubmed-article:3909887 | lifeskim:mentions | umls-concept:C0008051 | lld:lifeskim |
pubmed-article:3909887 | lifeskim:mentions | umls-concept:C0596997 | lld:lifeskim |
pubmed-article:3909887 | lifeskim:mentions | umls-concept:C1421451 | lld:lifeskim |
pubmed-article:3909887 | lifeskim:mentions | umls-concept:C0040649 | lld:lifeskim |
pubmed-article:3909887 | lifeskim:mentions | umls-concept:C1879746 | lld:lifeskim |
pubmed-article:3909887 | lifeskim:mentions | umls-concept:C1547011 | lld:lifeskim |
pubmed-article:3909887 | pubmed:dateCreated | 1986-2-11 | lld:pubmed |
pubmed-article:3909887 | pubmed:abstractText | The intermediate filament gene vimentin exists in a single copy in the chick haploid genome. However, it exhibits the curious property of producing at least three functional vimentin mRNA transcripts in vivo through the differential utilization of multiple polyadenylylation sites. According to one group in erythroid cells there may be a tissue-specific utilization of one of these poly A addition sites. The chicken and hamster vimentin genes exhibit remarkable nucleotide sequence homology both within coding and 3'-noncoding regions (82%). This nucleotide homology extends both to the size and juxtaposition of exons. With the noted exception of valine, even the frequency of codons utilized is strongly conserved across the widely different species. Of course, this strong homology at the DNA level extends to an amino acid homology of 92% between vimentins and 65% between related proteins in the same species. | lld:pubmed |
pubmed-article:3909887 | pubmed:language | eng | lld:pubmed |
pubmed-article:3909887 | pubmed:journal | http://linkedlifedata.com/r... | lld:pubmed |
pubmed-article:3909887 | pubmed:citationSubset | IM | lld:pubmed |
pubmed-article:3909887 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
pubmed-article:3909887 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
pubmed-article:3909887 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
pubmed-article:3909887 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
pubmed-article:3909887 | pubmed:status | MEDLINE | lld:pubmed |
pubmed-article:3909887 | pubmed:issn | 0077-8923 | lld:pubmed |
pubmed-article:3909887 | pubmed:author | pubmed-author:ZehnerZ EZE | lld:pubmed |
pubmed-article:3909887 | pubmed:author | pubmed-author:PatersonB MBM | lld:pubmed |
pubmed-article:3909887 | pubmed:issnType | Print | lld:pubmed |
pubmed-article:3909887 | pubmed:volume | 455 | lld:pubmed |
pubmed-article:3909887 | pubmed:owner | NLM | lld:pubmed |
pubmed-article:3909887 | pubmed:authorsComplete | Y | lld:pubmed |
pubmed-article:3909887 | pubmed:pagination | 79-94 | lld:pubmed |
pubmed-article:3909887 | pubmed:dateRevised | 2006-11-15 | lld:pubmed |
pubmed-article:3909887 | pubmed:meshHeading | pubmed-meshheading:3909887-... | lld:pubmed |
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pubmed-article:3909887 | pubmed:year | 1985 | lld:pubmed |
pubmed-article:3909887 | pubmed:articleTitle | The chicken vimentin gene: aspects of organization and transcription during myogenesis. | lld:pubmed |
pubmed-article:3909887 | pubmed:publicationType | Journal Article | lld:pubmed |
pubmed-article:3909887 | pubmed:publicationType | Comparative Study | lld:pubmed |
pubmed-article:3909887 | pubmed:publicationType | Review | lld:pubmed |
entrez-gene:420519 | entrezgene:pubmed | pubmed-article:3909887 | lld:entrezgene |
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