| pubmed-article:9571203 | rdf:type | pubmed:Citation | lld:pubmed |
| pubmed-article:9571203 | lifeskim:mentions | umls-concept:C0680022 | lld:lifeskim |
| pubmed-article:9571203 | lifeskim:mentions | umls-concept:C1519316 | lld:lifeskim |
| pubmed-article:9571203 | lifeskim:mentions | umls-concept:C0019646 | lld:lifeskim |
| pubmed-article:9571203 | lifeskim:mentions | umls-concept:C1519249 | lld:lifeskim |
| pubmed-article:9571203 | lifeskim:mentions | umls-concept:C2700395 | lld:lifeskim |
| pubmed-article:9571203 | lifeskim:mentions | umls-concept:C1711207 | lld:lifeskim |
| pubmed-article:9571203 | pubmed:issue | 2 | lld:pubmed |
| pubmed-article:9571203 | pubmed:dateCreated | 1998-6-2 | lld:pubmed |
| pubmed-article:9571203 | pubmed:databankReference | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:9571203 | pubmed:abstractText | The nucleotide sequence of a 700 basepair cDNA obtained from rabbit bladder was determined. It encodes a 123 amino acid protein, which is the smallest member of histone H2A.F/Z subfamily. The known H2A.F/Z variants are highly conserved in their central core regions of about 100 amino acids but more divergent in their N- and C-terminal ends. In addition to the seven amino acid signature sequence previously known for the H2A proteins, all the cloned H2A.F/Z variants contain an identical peptide sequence, L-E-Y-L-T-A-E-V-L-E-L-A-G-N-A. This 15 amino acid motif is proposed here as the signature sequence to identify new members of the H2A.F/Z subfamily. | lld:pubmed |
| pubmed-article:9571203 | pubmed:grant | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:9571203 | pubmed:language | eng | lld:pubmed |
| pubmed-article:9571203 | pubmed:journal | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:9571203 | pubmed:citationSubset | IM | lld:pubmed |
| pubmed-article:9571203 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:9571203 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:9571203 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:9571203 | pubmed:status | MEDLINE | lld:pubmed |
| pubmed-article:9571203 | pubmed:month | Apr | lld:pubmed |
| pubmed-article:9571203 | pubmed:issn | 0006-291X | lld:pubmed |
| pubmed-article:9571203 | pubmed:author | pubmed-author:BhavanandanV... | lld:pubmed |
| pubmed-article:9571203 | pubmed:author | pubmed-author:GuyRR | lld:pubmed |
| pubmed-article:9571203 | pubmed:author | pubmed-author:JiangWW | lld:pubmed |
| pubmed-article:9571203 | pubmed:issnType | Print | lld:pubmed |
| pubmed-article:9571203 | pubmed:day | 17 | lld:pubmed |
| pubmed-article:9571203 | pubmed:volume | 245 | lld:pubmed |
| pubmed-article:9571203 | pubmed:owner | NLM | lld:pubmed |
| pubmed-article:9571203 | pubmed:authorsComplete | Y | lld:pubmed |
| pubmed-article:9571203 | pubmed:pagination | 613-7 | lld:pubmed |
| pubmed-article:9571203 | pubmed:dateRevised | 2007-11-14 | lld:pubmed |
| pubmed-article:9571203 | pubmed:meshHeading | pubmed-meshheading:9571203-... | lld:pubmed |
| pubmed-article:9571203 | pubmed:meshHeading | pubmed-meshheading:9571203-... | lld:pubmed |
| pubmed-article:9571203 | pubmed:meshHeading | pubmed-meshheading:9571203-... | lld:pubmed |
| pubmed-article:9571203 | pubmed:meshHeading | pubmed-meshheading:9571203-... | lld:pubmed |
| pubmed-article:9571203 | pubmed:meshHeading | pubmed-meshheading:9571203-... | lld:pubmed |
| pubmed-article:9571203 | pubmed:meshHeading | pubmed-meshheading:9571203-... | lld:pubmed |
| pubmed-article:9571203 | pubmed:meshHeading | pubmed-meshheading:9571203-... | lld:pubmed |
| pubmed-article:9571203 | pubmed:meshHeading | pubmed-meshheading:9571203-... | lld:pubmed |
| pubmed-article:9571203 | pubmed:meshHeading | pubmed-meshheading:9571203-... | lld:pubmed |
| pubmed-article:9571203 | pubmed:meshHeading | pubmed-meshheading:9571203-... | lld:pubmed |
| pubmed-article:9571203 | pubmed:meshHeading | pubmed-meshheading:9571203-... | lld:pubmed |
| pubmed-article:9571203 | pubmed:meshHeading | pubmed-meshheading:9571203-... | lld:pubmed |
| pubmed-article:9571203 | pubmed:meshHeading | pubmed-meshheading:9571203-... | lld:pubmed |
| pubmed-article:9571203 | pubmed:meshHeading | pubmed-meshheading:9571203-... | lld:pubmed |
| pubmed-article:9571203 | pubmed:meshHeading | pubmed-meshheading:9571203-... | lld:pubmed |
| pubmed-article:9571203 | pubmed:year | 1998 | lld:pubmed |
| pubmed-article:9571203 | pubmed:articleTitle | Histone H2A.F/Z subfamily: the smallest member and the signature sequence. | lld:pubmed |
| pubmed-article:9571203 | pubmed:affiliation | Department of Biochemistry and Molecular Biology, Pennsylvania State University College of Medicine, Hershey 17033, USA. wjiang@psu.edu | lld:pubmed |
| pubmed-article:9571203 | pubmed:publicationType | Journal Article | lld:pubmed |
| pubmed-article:9571203 | pubmed:publicationType | Research Support, U.S. Gov't, P.H.S. | lld:pubmed |
| entrez-gene:100328558 | entrezgene:pubmed | pubmed-article:9571203 | lld:entrezgene |
| http://linkedlifedata.com/r... | pubmed:referesTo | pubmed-article:9571203 | lld:pubmed |
