pubmed-article:14520886 | rdf:type | pubmed:Citation | lld:pubmed |
pubmed-article:14520886 | lifeskim:mentions | umls-concept:C0007634 | lld:lifeskim |
pubmed-article:14520886 | lifeskim:mentions | umls-concept:C0043343 | lld:lifeskim |
pubmed-article:14520886 | lifeskim:mentions | umls-concept:C0033684 | lld:lifeskim |
pubmed-article:14520886 | lifeskim:mentions | umls-concept:C0021467 | lld:lifeskim |
pubmed-article:14520886 | lifeskim:mentions | umls-concept:C0205307 | lld:lifeskim |
pubmed-article:14520886 | lifeskim:mentions | umls-concept:C0040649 | lld:lifeskim |
pubmed-article:14520886 | lifeskim:mentions | umls-concept:C0021469 | lld:lifeskim |
pubmed-article:14520886 | lifeskim:mentions | umls-concept:C1660749 | lld:lifeskim |
pubmed-article:14520886 | lifeskim:mentions | umls-concept:C1709694 | lld:lifeskim |
pubmed-article:14520886 | lifeskim:mentions | umls-concept:C0348080 | lld:lifeskim |
pubmed-article:14520886 | pubmed:issue | 3 | lld:pubmed |
pubmed-article:14520886 | pubmed:dateCreated | 2003-10-2 | lld:pubmed |
pubmed-article:14520886 | pubmed:abstractText | The interaction of condensin subunit XCAP-E with various nucleolar subcompartments in XL2 cells was studied. In the interphase cells, XCAP-E was associated with a granular component of nucleoli (as shown by double staining with antibodies against B23) and with small nucleolus-like structures in the nucleoplasm. Inhibition of transcription by actinomycin D does not disrupt interaction of XCAP-E with the granular compartment of segregated nucleoli. Treatment with DRB 5,6-dichloro-1 beta-ribofuranozide-benzimidazole causes disintegration of nucleolar fibrillar complexes, but does not affect nucleolar localization of XCAP-E. The data suggest that nucleolar association of XCAP-E is independent on the functional state of the nucleolus, and imply a possible role of this protein in rRNA processing and pre-fibosome assembly. | lld:pubmed |
pubmed-article:14520886 | pubmed:language | rus | lld:pubmed |
pubmed-article:14520886 | pubmed:journal | http://linkedlifedata.com/r... | lld:pubmed |
pubmed-article:14520886 | pubmed:citationSubset | IM | lld:pubmed |
pubmed-article:14520886 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
pubmed-article:14520886 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
pubmed-article:14520886 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
pubmed-article:14520886 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
pubmed-article:14520886 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
pubmed-article:14520886 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
pubmed-article:14520886 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
pubmed-article:14520886 | pubmed:status | MEDLINE | lld:pubmed |
pubmed-article:14520886 | pubmed:issn | 0041-3771 | lld:pubmed |
pubmed-article:14520886 | pubmed:author | pubmed-author:PoliakovV... | lld:pubmed |
pubmed-article:14520886 | pubmed:author | pubmed-author:GulakP VPV | lld:pubmed |
pubmed-article:14520886 | pubmed:author | pubmed-author:KireevI III | lld:pubmed |
pubmed-article:14520886 | pubmed:author | pubmed-author:UzbekovR ERE | lld:pubmed |
pubmed-article:14520886 | pubmed:author | pubmed-author:Timirbulatova... | lld:pubmed |
pubmed-article:14520886 | pubmed:author | pubmed-author:KartavenkoT... | lld:pubmed |
pubmed-article:14520886 | pubmed:author | pubmed-author:GuellecK LKL | lld:pubmed |
pubmed-article:14520886 | pubmed:issnType | Print | lld:pubmed |
pubmed-article:14520886 | pubmed:volume | 45 | lld:pubmed |
pubmed-article:14520886 | pubmed:owner | NLM | lld:pubmed |
pubmed-article:14520886 | pubmed:authorsComplete | Y | lld:pubmed |
pubmed-article:14520886 | pubmed:pagination | 290-7 | lld:pubmed |
pubmed-article:14520886 | pubmed:dateRevised | 2006-11-15 | lld:pubmed |
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pubmed-article:14520886 | pubmed:year | 2003 | lld:pubmed |
pubmed-article:14520886 | pubmed:articleTitle | [Intracellular localization of XCAP-E protein in XL2 (Xenopus laevis) cells under normal conditions and during inhibition of pRNA transcription and processing]. | lld:pubmed |
pubmed-article:14520886 | pubmed:affiliation | Research Institute of Physico-Chemical Biology, Moscow State University, Institute of Gene Biology RAS, Moscow. al_mira@rambler.ru | lld:pubmed |
pubmed-article:14520886 | pubmed:publicationType | Journal Article | lld:pubmed |
pubmed-article:14520886 | pubmed:publicationType | English Abstract | lld:pubmed |