Statements in which the resource exists as a subject.
PredicateObject
rdf:type
lifeskim:mentions
pubmed:issue
10
pubmed:dateCreated
2006-9-28
pubmed:abstractText
iASPP is one of the most evolutionarily conserved inhibitors of p53, whereas ASPP1 and ASPP2 are activators of p53. We show here that, in addition to the DNA-binding domain, the ASPP family members also bind to the proline-rich region of p53, which contains the most common p53 polymorphism at codon 72. Furthermore, the ASPP family members, particularly iASPP, bind to and regulate the activity of p53Pro72 more efficiently than that of p53Arg72. Hence, escape from negative regulation by iASPP is a newly identified mechanism by which p53Arg72 activates apoptosis more efficiently than p53Pro72.
pubmed:language
eng
pubmed:journal
pubmed:citationSubset
IM
pubmed:chemical
pubmed:status
MEDLINE
pubmed:month
Oct
pubmed:issn
1061-4036
pubmed:author
pubmed:issnType
Print
pubmed:volume
38
pubmed:owner
NLM
pubmed:authorsComplete
Y
pubmed:pagination
1133-41
pubmed:dateRevised
2009-11-19
pubmed:meshHeading
pubmed-meshheading:16964264-Amino Acid Sequence, pubmed-meshheading:16964264-Apoptosis, pubmed-meshheading:16964264-Arginine, pubmed-meshheading:16964264-Binding Sites, pubmed-meshheading:16964264-Breast Neoplasms, pubmed-meshheading:16964264-Carcinoma, pubmed-meshheading:16964264-Cells, Cultured, pubmed-meshheading:16964264-Codon, pubmed-meshheading:16964264-Conserved Sequence, pubmed-meshheading:16964264-Female, pubmed-meshheading:16964264-Gene Expression Regulation, pubmed-meshheading:16964264-Homozygote, pubmed-meshheading:16964264-Humans, pubmed-meshheading:16964264-Intracellular Signaling Peptides and Proteins, pubmed-meshheading:16964264-Molecular Sequence Data, pubmed-meshheading:16964264-Polymorphism, Genetic, pubmed-meshheading:16964264-Proline, pubmed-meshheading:16964264-Repressor Proteins, pubmed-meshheading:16964264-Tumor Suppressor Protein p53, pubmed-meshheading:16964264-Tyrosine
pubmed:year
2006
pubmed:articleTitle
iASPP preferentially binds p53 proline-rich region and modulates apoptotic function of codon 72-polymorphic p53.
pubmed:affiliation
Ludwig Institute for Cancer Research, University College London, 91 Riding House Street, London W1W 7BS, UK.
pubmed:publicationType
Journal Article, Research Support, Non-U.S. Gov't