pubmed-article:15047893 | rdf:type | pubmed:Citation | lld:pubmed |
pubmed-article:15047893 | lifeskim:mentions | umls-concept:C0007634 | lld:lifeskim |
pubmed-article:15047893 | lifeskim:mentions | umls-concept:C0008546 | lld:lifeskim |
pubmed-article:15047893 | lifeskim:mentions | umls-concept:C0007586 | lld:lifeskim |
pubmed-article:15047893 | lifeskim:mentions | umls-concept:C1150423 | lld:lifeskim |
pubmed-article:15047893 | lifeskim:mentions | umls-concept:C0182953 | lld:lifeskim |
pubmed-article:15047893 | pubmed:issue | 4 | lld:pubmed |
pubmed-article:15047893 | pubmed:dateCreated | 2004-4-15 | lld:pubmed |
pubmed-article:15047893 | pubmed:databankReference | http://linkedlifedata.com/r... | lld:pubmed |
pubmed-article:15047893 | pubmed:abstractText | The TOUSLED (TSL)-like nuclear protein kinase family is highly conserved in plants and animals. tsl loss of function mutations cause pleiotropic defects in both leaf and flower development, and growth and initiation of floral organ primordia is abnormal, suggesting that basic cellular processes are affected. TSL is more highly expressed in exponentially growing Arabidopsis culture cells than in stationary, nondividing cells. While its expression remains constant throughout the cell cycle in dividing cells, TSL kinase activity is higher in enriched late G2/M-phase and G1-phase populations of Arabidopsis suspension culture cells compared to those in S-phase. tsl mutants also display an aberrant pattern and increased expression levels of the mitotic cyclin gene CycB1;1, suggesting that TSL represses CycB1;1 expression at certain times during development or that cells are delayed in mitosis. TSL interacts with and phosphorylates one of two Arabidopsis homologs of the nucleosome assembly/silencing protein Asf1 and histone H3, as in humans, and a novel plant SANT/myb-domain protein, TKI1, suggesting that TSL plays a role in chromatin metabolism. | lld:pubmed |
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pubmed-article:15047893 | pubmed:language | eng | lld:pubmed |
pubmed-article:15047893 | pubmed:journal | http://linkedlifedata.com/r... | lld:pubmed |
pubmed-article:15047893 | pubmed:citationSubset | IM | lld:pubmed |
pubmed-article:15047893 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
pubmed-article:15047893 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
pubmed-article:15047893 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
pubmed-article:15047893 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
pubmed-article:15047893 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
pubmed-article:15047893 | pubmed:status | MEDLINE | lld:pubmed |
pubmed-article:15047893 | pubmed:month | Apr | lld:pubmed |
pubmed-article:15047893 | pubmed:issn | 0032-0889 | lld:pubmed |
pubmed-article:15047893 | pubmed:author | pubmed-author:DurfeeTimT | lld:pubmed |
pubmed-article:15047893 | pubmed:author | pubmed-author:RoeJudith LJL | lld:pubmed |
pubmed-article:15047893 | pubmed:author | pubmed-author:ReichheldJean... | lld:pubmed |
pubmed-article:15047893 | pubmed:author | pubmed-author:EhsanHashimul... | lld:pubmed |
pubmed-article:15047893 | pubmed:issnType | Print | lld:pubmed |
pubmed-article:15047893 | pubmed:volume | 134 | lld:pubmed |
pubmed-article:15047893 | pubmed:owner | NLM | lld:pubmed |
pubmed-article:15047893 | pubmed:authorsComplete | Y | lld:pubmed |
pubmed-article:15047893 | pubmed:pagination | 1488-99 | lld:pubmed |
pubmed-article:15047893 | pubmed:dateRevised | 2009-11-18 | lld:pubmed |
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