pubmed-article:12150928 | rdf:type | pubmed:Citation | lld:pubmed |
pubmed-article:12150928 | lifeskim:mentions | umls-concept:C0597357 | lld:lifeskim |
pubmed-article:12150928 | lifeskim:mentions | umls-concept:C0037083 | lld:lifeskim |
pubmed-article:12150928 | lifeskim:mentions | umls-concept:C0031727 | lld:lifeskim |
pubmed-article:12150928 | lifeskim:mentions | umls-concept:C1332379 | lld:lifeskim |
pubmed-article:12150928 | lifeskim:mentions | umls-concept:C1710082 | lld:lifeskim |
pubmed-article:12150928 | lifeskim:mentions | umls-concept:C0086597 | lld:lifeskim |
pubmed-article:12150928 | lifeskim:mentions | umls-concept:C1709450 | lld:lifeskim |
pubmed-article:12150928 | pubmed:issue | 2 | lld:pubmed |
pubmed-article:12150928 | pubmed:dateCreated | 2002-8-1 | lld:pubmed |
pubmed-article:12150928 | pubmed:abstractText | The Arabidopsis BAK1 (BRI1 Associated receptor Kinase 1) was identified by a yeast two-hybrid screen as a specific interactor for BRI1, a critical component of a membrane brassinosteroid (BR) receptor. In yeast, BAK1/BRI1 interaction activates their kinase activities through transphosphorylation. BAK1 and BRI1 share similar gene expression and subcellular localization patterns and physically associate with each other in plants. Overexpression of the BAK1 gene leads to a phenotype reminiscent of BRI1-overexpression transgenic plants and rescues a weak bri1 mutant. In contrast, a bak1 knockout mutation gives rise to a weak bri1-like phenotype and enhances a weak bri1 mutation. We propose that BAK1 and BRI1 function together to mediate plant steroid signaling. | lld:pubmed |
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pubmed-article:12150928 | pubmed:language | eng | lld:pubmed |
pubmed-article:12150928 | pubmed:journal | http://linkedlifedata.com/r... | lld:pubmed |
pubmed-article:12150928 | pubmed:citationSubset | IM | lld:pubmed |
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pubmed-article:12150928 | pubmed:status | MEDLINE | lld:pubmed |
pubmed-article:12150928 | pubmed:month | Jul | lld:pubmed |
pubmed-article:12150928 | pubmed:issn | 0092-8674 | lld:pubmed |
pubmed-article:12150928 | pubmed:author | pubmed-author:LiJianmingJ | lld:pubmed |
pubmed-article:12150928 | pubmed:author | pubmed-author:NamKyoung... | lld:pubmed |
pubmed-article:12150928 | pubmed:issnType | Print | lld:pubmed |
pubmed-article:12150928 | pubmed:day | 26 | lld:pubmed |
pubmed-article:12150928 | pubmed:volume | 110 | lld:pubmed |
pubmed-article:12150928 | pubmed:owner | NLM | lld:pubmed |
pubmed-article:12150928 | pubmed:authorsComplete | Y | lld:pubmed |
pubmed-article:12150928 | pubmed:pagination | 203-12 | lld:pubmed |
pubmed-article:12150928 | pubmed:dateRevised | 2011-9-22 | lld:pubmed |
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pubmed-article:12150928 | pubmed:meshHeading | pubmed-meshheading:12150928... | lld:pubmed |
pubmed-article:12150928 | pubmed:year | 2002 | lld:pubmed |
pubmed-article:12150928 | pubmed:articleTitle | BRI1/BAK1, a receptor kinase pair mediating brassinosteroid signaling. | lld:pubmed |
pubmed-article:12150928 | pubmed:affiliation | Department of Molecular, Cellular, and Developmental Biology, University of Michigan, Ann Arbor, MI 48109, USA. | lld:pubmed |
pubmed-article:12150928 | pubmed:publicationType | Journal Article | lld:pubmed |
pubmed-article:12150928 | pubmed:publicationType | Research Support, U.S. Gov't, P.H.S. | lld:pubmed |
pubmed-article:12150928 | pubmed:publicationType | Research Support, Non-U.S. Gov't | lld:pubmed |
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