pubmed-article:16797541 | rdf:type | pubmed:Citation | lld:pubmed |
pubmed-article:16797541 | lifeskim:mentions | umls-concept:C0162638 | lld:lifeskim |
pubmed-article:16797541 | lifeskim:mentions | umls-concept:C1257945 | lld:lifeskim |
pubmed-article:16797541 | lifeskim:mentions | umls-concept:C0699900 | lld:lifeskim |
pubmed-article:16797541 | lifeskim:mentions | umls-concept:C1823882 | lld:lifeskim |
pubmed-article:16797541 | lifeskim:mentions | umls-concept:C0243125 | lld:lifeskim |
pubmed-article:16797541 | lifeskim:mentions | umls-concept:C0205263 | lld:lifeskim |
pubmed-article:16797541 | lifeskim:mentions | umls-concept:C1704735 | lld:lifeskim |
pubmed-article:16797541 | lifeskim:mentions | umls-concept:C0127400 | lld:lifeskim |
pubmed-article:16797541 | pubmed:issue | 16 | lld:pubmed |
pubmed-article:16797541 | pubmed:dateCreated | 2006-7-3 | lld:pubmed |
pubmed-article:16797541 | pubmed:abstractText | F-Box proteins (FBPs) are variable adaptor proteins that earmark protein substrates for ubiquination and destruction by the proteasome. Through their N-terminal F-box motif, they couple specific protein substrates to a catalytic machinery known as SCF (Skp-1/Cul1/F-Box) E3-ubiquitin ligase. Typical FBPs bind the specific substrates in a phosphorylation dependent manner via their C-termini using either leucine rich repeats (LRR) or tryptophan-aspartic acid (WD40) domains for substrate recognition. By using a gene trap strategy that selects for genes induced during programmed cell death, we have isolated the mouse homolog of the hypothetical human F-Box protein 33 (FBX33). Here we identify FBX33 as a component of an SCF E3-ubiquitin ligase that targets the multifunctional regulator Y-box binding protein 1 (YB-1)/dbpB/p50 for polyubiquitination and destruction by the proteasome. By targeting YB-1 for proteasomal degradation, FBX33 negatively interferes with YB-1 mediated functions. In contrast to typical FBPs, FBX33 has no C-terminal LRR or WD40 domains and associates with YB-1 via its N-terminus. The present study confirms the existence of a formerly hypothetical F-Box protein in living cells and describes one of its substrates. | lld:pubmed |
pubmed-article:16797541 | pubmed:language | eng | lld:pubmed |
pubmed-article:16797541 | pubmed:journal | http://linkedlifedata.com/r... | lld:pubmed |
pubmed-article:16797541 | pubmed:citationSubset | IM | lld:pubmed |
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pubmed-article:16797541 | pubmed:status | MEDLINE | lld:pubmed |
pubmed-article:16797541 | pubmed:month | Jul | lld:pubmed |
pubmed-article:16797541 | pubmed:issn | 0014-5793 | lld:pubmed |
pubmed-article:16797541 | pubmed:author | pubmed-author:ZopfDieterD | lld:pubmed |
pubmed-article:16797541 | pubmed:author | pubmed-author:WempeFrankF | lld:pubmed |
pubmed-article:16797541 | pubmed:author | pubmed-author:von... | lld:pubmed |
pubmed-article:16797541 | pubmed:author | pubmed-author:LutzMarcusM | lld:pubmed |
pubmed-article:16797541 | pubmed:author | pubmed-author:BahrInkeI | lld:pubmed |
pubmed-article:16797541 | pubmed:issnType | Print | lld:pubmed |
pubmed-article:16797541 | pubmed:day | 10 | lld:pubmed |
pubmed-article:16797541 | pubmed:volume | 580 | lld:pubmed |
pubmed-article:16797541 | pubmed:owner | NLM | lld:pubmed |
pubmed-article:16797541 | pubmed:authorsComplete | Y | lld:pubmed |
pubmed-article:16797541 | pubmed:pagination | 3921-30 | lld:pubmed |
pubmed-article:16797541 | pubmed:dateRevised | 2008-11-21 | lld:pubmed |
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pubmed-article:16797541 | pubmed:year | 2006 | lld:pubmed |
pubmed-article:16797541 | pubmed:articleTitle | Proteasomal degradation of the multifunctional regulator YB-1 is mediated by an F-Box protein induced during programmed cell death. | lld:pubmed |
pubmed-article:16797541 | pubmed:affiliation | Department for Molecular Hematology, University of Frankfurt Medical School, Theodor-Stern-Kai 7, 60590 Frankfurt am Main, Germany. | lld:pubmed |
pubmed-article:16797541 | pubmed:publicationType | Journal Article | lld:pubmed |
pubmed-article:16797541 | pubmed:publicationType | Research Support, Non-U.S. Gov't | lld:pubmed |
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