Linked Life Data

16338354

Source:http://linkedlifedata.com/resource/pubmed/id/16338354

Statements in which the resource exists as a subject.
PredicateObject
rdf:type
lifeskim:mentions
pubmed:dateCreated
2005-12-12
pubmed:abstractText
Ubiquitin (Ub) regulates important cellular processes through covalent attachment to its substrates. Distinct fates are bestowed on multi-Ub chains linked through different lysine residues. Ub contains seven conserved lysines, all of which could be used for multi-Ub chain formation. K29 and K48 are the signals for proteasome-mediated proteolysis. Multi-Ub chains linked through K63 have nonproteolytic functions. Studies of Ub-binding factors are likely the key to understanding diverse functions of the Ub molecule. Yeast two-hybrid assay can be a powerful approach to dissect the interaction between Ub and its binding proteins and also the function of these Ub-chain binding proteins in vivo.
pubmed:language
eng
pubmed:journal
pubmed:citationSubset
IM
pubmed:chemical
pubmed:status
MEDLINE
pubmed:issn
0076-6879
pubmed:author
pubmed:issnType
Print
pubmed:volume
399
pubmed:owner
NLM
pubmed:authorsComplete
Y
pubmed:pagination
157-64
pubmed:meshHeading
pubmed:year
2005
pubmed:articleTitle
Analysis of ubiquitin chain-binding proteins by two-hybrid methods.
pubmed:affiliation
Institute of Biotechnology, Department of Molecular Medicine, University of Texas Health Science Center, San Antonio, Texas, USA.
pubmed:publicationType
Journal Article, Research Support, Non-U.S. Gov't