Source:http://linkedlifedata.com/resource/pubmed/id/18485863
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Predicate | Object |
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rdf:type | |
lifeskim:mentions | |
pubmed:issue |
4
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pubmed:dateCreated |
2008-5-19
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pubmed:abstractText |
Regulated protein degradation by the ubiquitin-proteasome pathway ensures the unidirectionality of mitotic progression by removing cell-cycle regulators required at earlier stages. The APC/C ubiquitin-protein ligase targets proteins by appending polyubiquitin degradation signals that are subsequently recognized by the 26S proteasome. Reporting in this issue, Jin et al. (2008) identify a TEK motif in both ubiquitin and substrates of APC/C that mediates assembly of these degradation signals.
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pubmed:commentsCorrections | |
pubmed:language |
eng
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pubmed:journal | |
pubmed:citationSubset |
IM
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pubmed:chemical | |
pubmed:status |
MEDLINE
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pubmed:month |
May
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pubmed:issn |
1097-4172
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pubmed:author | |
pubmed:issnType |
Electronic
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pubmed:day |
16
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pubmed:volume |
133
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pubmed:owner |
NLM
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pubmed:authorsComplete |
Y
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pubmed:pagination |
570-2
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pubmed:meshHeading |
pubmed-meshheading:18485863-Amino Acid Motifs,
pubmed-meshheading:18485863-Animals,
pubmed-meshheading:18485863-Humans,
pubmed-meshheading:18485863-Proteins,
pubmed-meshheading:18485863-Ubiquitin,
pubmed-meshheading:18485863-Ubiquitin-Protein Ligase Complexes,
pubmed-meshheading:18485863-Ubiquitination
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pubmed:year |
2008
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pubmed:articleTitle |
DeTEKting ubiquitination of APC/C substrates.
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pubmed:affiliation |
Department of Biochemistry and Molecular Biology, Louisiana State University School of Medicine, New Orleans, LA 70112, USA.
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pubmed:publicationType |
Journal Article,
Comment
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