Linked Life Data

16376884

Source:http://linkedlifedata.com/resource/pubmed/id/16376884

Statements in which the resource exists as a subject.
PredicateObject
rdf:type
lifeskim:mentions
pubmed:issue
1
pubmed:dateCreated
2006-1-2
pubmed:abstractText
We have used surface plasmon resonance to quantify the kinetics and stoichiometry of the interaction between p53 and nucleophosmin (NPM). Domains characterising the interface between the two proteins were identified by chemical cross-linking, proteolytic digestion and mass spectrometry based peptide mapping. We show that the C-terminal domain of NPM (residues 242-269) interacts with two regions of p53 (residues 175-196 and residues 343-363) which belong, respectively, to the DNA binding domain and the tetramerisation domain. Potential biological consequences of such interactions are discussed.
pubmed:commentsCorrections
pubmed:language
eng
pubmed:journal
pubmed:citationSubset
IM
pubmed:chemical
pubmed:status
MEDLINE
pubmed:month
Jan
pubmed:issn
0014-5793
pubmed:author
pubmed:issnType
Print
pubmed:day
9
pubmed:volume
580
pubmed:owner
NLM
pubmed:authorsComplete
Y
pubmed:pagination
345-50
pubmed:dateRevised
2009-11-3
pubmed:meshHeading
pubmed:year
2006
pubmed:articleTitle
Characterisation of the interface between nucleophosmin (NPM) and p53: potential role in p53 stabilisation.
pubmed:affiliation
Enzymologie et Cinétique Structurale, LBPA, UMR 8113 CNRS/Ecole Normale Supérieure de Cachan, 61 Avenue du Président Wilson, 94235 Cachan, France. lambert@lbpa.ens-cachan.fr
pubmed:publicationType
Journal Article