Statements in which the resource exists as a subject.
PredicateObject
rdf:type
lifeskim:mentions
pubmed:issue
10
pubmed:dateCreated
2008-9-23
pubmed:abstractText
p53 binds to some members of the S100 family (S100B, S100A4, S100A2, and S100A1). We previously showed that both S100B and S100A4 bind to the p53 tetramerization domain, and consequently control its oligomerization state, but only S100B binds to the C-terminal negative regulatory domain (NRD). Here, we investigate other binding partners for p53 within the S100 family (S100A6 and S100A11), and show that binding to the p53 tetramerization domain seems to be a general feature of the S100 family, while binding to the NRD is a characteristic of a subset of the family.
pubmed:grant
pubmed:commentsCorrections
http://linkedlifedata.com/resource/pubmed/commentcorrection/18694925-10187847, http://linkedlifedata.com/resource/pubmed/commentcorrection/18694925-10395934, http://linkedlifedata.com/resource/pubmed/commentcorrection/18694925-10490652, http://linkedlifedata.com/resource/pubmed/commentcorrection/18694925-10876243, http://linkedlifedata.com/resource/pubmed/commentcorrection/18694925-11114324, http://linkedlifedata.com/resource/pubmed/commentcorrection/18694925-11278647, http://linkedlifedata.com/resource/pubmed/commentcorrection/18694925-11390274, http://linkedlifedata.com/resource/pubmed/commentcorrection/18694925-11454863, http://linkedlifedata.com/resource/pubmed/commentcorrection/18694925-11527429, http://linkedlifedata.com/resource/pubmed/commentcorrection/18694925-1454855, http://linkedlifedata.com/resource/pubmed/commentcorrection/18694925-14759526, http://linkedlifedata.com/resource/pubmed/commentcorrection/18694925-15781852, http://linkedlifedata.com/resource/pubmed/commentcorrection/18694925-15941720, http://linkedlifedata.com/resource/pubmed/commentcorrection/18694925-17010455, http://linkedlifedata.com/resource/pubmed/commentcorrection/18694925-8341667, http://linkedlifedata.com/resource/pubmed/commentcorrection/18694925-8520220, http://linkedlifedata.com/resource/pubmed/commentcorrection/18694925-8701470, http://linkedlifedata.com/resource/pubmed/commentcorrection/18694925-8757792, http://linkedlifedata.com/resource/pubmed/commentcorrection/18694925-9039259, http://linkedlifedata.com/resource/pubmed/commentcorrection/18694925-9379433, http://linkedlifedata.com/resource/pubmed/commentcorrection/18694925-9485322, http://linkedlifedata.com/resource/pubmed/commentcorrection/18694925-9582268, http://linkedlifedata.com/resource/pubmed/commentcorrection/18694925-9632811, http://linkedlifedata.com/resource/pubmed/commentcorrection/18694925-9836589, http://linkedlifedata.com/resource/pubmed/commentcorrection/18694925-9886297, http://linkedlifedata.com/resource/pubmed/commentcorrection/18694925-9920729
pubmed:language
eng
pubmed:journal
pubmed:citationSubset
IM
pubmed:chemical
pubmed:status
MEDLINE
pubmed:month
Oct
pubmed:issn
1469-896X
pubmed:author
pubmed:issnType
Electronic
pubmed:volume
17
pubmed:owner
NLM
pubmed:authorsComplete
Y
pubmed:pagination
1663-70
pubmed:dateRevised
2009-11-18
pubmed:meshHeading
pubmed:year
2008
pubmed:articleTitle
Members of the S100 family bind p53 in two distinct ways.
pubmed:affiliation
Centre for Protein Engineering, Medical Research Council, Cambridge University, Cambridge CB2 0QH, United Kingdom.
pubmed:publicationType
Journal Article, Research Support, Non-U.S. Gov't