| pubmed-article:9285555 | rdf:type | pubmed:Citation | lld:pubmed |
| pubmed-article:9285555 | lifeskim:mentions | umls-concept:C0007634 | lld:lifeskim |
| pubmed-article:9285555 | lifeskim:mentions | umls-concept:C0812292 | lld:lifeskim |
| pubmed-article:9285555 | lifeskim:mentions | umls-concept:C0031715 | lld:lifeskim |
| pubmed-article:9285555 | lifeskim:mentions | umls-concept:C0007586 | lld:lifeskim |
| pubmed-article:9285555 | lifeskim:mentions | umls-concept:C0441655 | lld:lifeskim |
| pubmed-article:9285555 | lifeskim:mentions | umls-concept:C0851285 | lld:lifeskim |
| pubmed-article:9285555 | pubmed:issue | 9 | lld:pubmed |
| pubmed-article:9285555 | pubmed:dateCreated | 1997-9-22 | lld:pubmed |
| pubmed-article:9285555 | pubmed:abstractText | A-myb, a conserved member of the Myb proto-oncogene family, encodes a sequence-specific DNA binding protein (A-Myb) that binds to and transactivates promoters containing myb-binding sites. Previous work has suggested that the C-terminus of A-Myb functions as a regulatory domain, however, the physiological signals that control the activity of A-Myb have not yet been identified. The presence of potential phosphorylation sites for cyclin-dependent kinases in the C-terminus of A-Myb has prompted us to examine the possibility that the function of A-Myb is controlled by the cell cycle. We here show that the transactivation potential of A-Myb is repressed by the C-terminal domain and that phosphorylation of A-Myb, induced by cyclins A and E, relieves this inhibitory effect. Our work provides the first evidence that the function of A-Myb is regulated by the cell cycle machinery and that the carboxy-terminal domain of A-Myb acts as a cell cycle sensor. In addition, we show that A-myb mRNA expression is also cell cycle regulated and attains maximal levels during the late G1- and early S-phase. Thus, A-Myb appears to be controlled by two different mechanisms resulting in maximal A-Myb activity during the G1/S-transition and the S-phase of the cell cycle. | lld:pubmed |
| pubmed-article:9285555 | pubmed:language | eng | lld:pubmed |
| pubmed-article:9285555 | pubmed:journal | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:9285555 | pubmed:citationSubset | IM | lld:pubmed |
| pubmed-article:9285555 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:9285555 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:9285555 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:9285555 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:9285555 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:9285555 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:9285555 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:9285555 | pubmed:status | MEDLINE | lld:pubmed |
| pubmed-article:9285555 | pubmed:month | Aug | lld:pubmed |
| pubmed-article:9285555 | pubmed:issn | 0950-9232 | lld:pubmed |
| pubmed-article:9285555 | pubmed:author | pubmed-author:KlempnauerK... | lld:pubmed |
| pubmed-article:9285555 | pubmed:author | pubmed-author:ZieboldUU | lld:pubmed |
| pubmed-article:9285555 | pubmed:issnType | Print | lld:pubmed |
| pubmed-article:9285555 | pubmed:day | 28 | lld:pubmed |
| pubmed-article:9285555 | pubmed:volume | 15 | lld:pubmed |
| pubmed-article:9285555 | pubmed:owner | NLM | lld:pubmed |
| pubmed-article:9285555 | pubmed:authorsComplete | Y | lld:pubmed |
| pubmed-article:9285555 | pubmed:pagination | 1011-9 | lld:pubmed |
| pubmed-article:9285555 | pubmed:dateRevised | 2006-11-15 | lld:pubmed |
| pubmed-article:9285555 | pubmed:meshHeading | pubmed-meshheading:9285555-... | lld:pubmed |
| pubmed-article:9285555 | pubmed:meshHeading | pubmed-meshheading:9285555-... | lld:pubmed |
| pubmed-article:9285555 | pubmed:meshHeading | pubmed-meshheading:9285555-... | lld:pubmed |
| pubmed-article:9285555 | pubmed:meshHeading | pubmed-meshheading:9285555-... | lld:pubmed |
| pubmed-article:9285555 | pubmed:meshHeading | pubmed-meshheading:9285555-... | lld:pubmed |
| pubmed-article:9285555 | pubmed:meshHeading | pubmed-meshheading:9285555-... | lld:pubmed |
| pubmed-article:9285555 | pubmed:meshHeading | pubmed-meshheading:9285555-... | lld:pubmed |
| pubmed-article:9285555 | pubmed:meshHeading | pubmed-meshheading:9285555-... | lld:pubmed |
| pubmed-article:9285555 | pubmed:meshHeading | pubmed-meshheading:9285555-... | lld:pubmed |
| pubmed-article:9285555 | pubmed:meshHeading | pubmed-meshheading:9285555-... | lld:pubmed |
| pubmed-article:9285555 | pubmed:meshHeading | pubmed-meshheading:9285555-... | lld:pubmed |
| pubmed-article:9285555 | pubmed:meshHeading | pubmed-meshheading:9285555-... | lld:pubmed |
| pubmed-article:9285555 | pubmed:year | 1997 | lld:pubmed |
| pubmed-article:9285555 | pubmed:articleTitle | Linking Myb to the cell cycle: cyclin-dependent phosphorylation and regulation of A-Myb activity. | lld:pubmed |
| pubmed-article:9285555 | pubmed:affiliation | Hans-Spemann-Laboratory, Max-Planck-Institute for Immunobiology, Freiburg, Germany. | lld:pubmed |
| pubmed-article:9285555 | pubmed:publicationType | Journal Article | lld:pubmed |
| pubmed-article:9285555 | pubmed:publicationType | Research Support, Non-U.S. Gov't | lld:pubmed |
| http://linkedlifedata.com/r... | pubmed:referesTo | pubmed-article:9285555 | lld:pubmed |
| http://linkedlifedata.com/r... | pubmed:referesTo | pubmed-article:9285555 | lld:pubmed |
| http://linkedlifedata.com/r... | pubmed:referesTo | pubmed-article:9285555 | lld:pubmed |
| http://linkedlifedata.com/r... | pubmed:referesTo | pubmed-article:9285555 | lld:pubmed |
