Source:http://linkedlifedata.com/resource/pubmed/id/11960904
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Predicate | Object |
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rdf:type | |
lifeskim:mentions | |
pubmed:issue |
4
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pubmed:dateCreated |
2002-4-18
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pubmed:abstractText |
The p53-Mdm2 paradigm represents the best-studied relationship between a tumor suppressor gene which functions as a transcription factor and an oncogene, which functions primarily as an E3 protein ligase. The intimate relationship between these two partners has expanded to include almost every cellular biological system - from development, to growth control and programmed cell death. The affair between Mdm2 and p53 is closely controlled by a complex array of post-translational modifications, which in turn dictates the stability and activity of p53 and Mdm2. Functional diversity depends on the association with a large subset of partner proteins, which dictates the type of activity and corresponding selectivity. Here we summarize the current understanding of post-translational modifications and their effect on conformation-based functional relationship between Mdm2 and p53, as it pertains to their diverse cellular biological functions.
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pubmed:grant | |
pubmed:language |
eng
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pubmed:journal | |
pubmed:citationSubset |
IM
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pubmed:chemical |
http://linkedlifedata.com/resource/pubmed/chemical/MDM2 protein, human,
http://linkedlifedata.com/resource/pubmed/chemical/Nuclear Proteins,
http://linkedlifedata.com/resource/pubmed/chemical/Proto-Oncogene Proteins,
http://linkedlifedata.com/resource/pubmed/chemical/Proto-Oncogene Proteins c-mdm2,
http://linkedlifedata.com/resource/pubmed/chemical/Tumor Suppressor Protein p53
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pubmed:status |
MEDLINE
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pubmed:month |
Apr
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pubmed:issn |
0143-3334
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pubmed:author | |
pubmed:issnType |
Print
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pubmed:volume |
23
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pubmed:owner |
NLM
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pubmed:authorsComplete |
Y
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pubmed:pagination |
541-7
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pubmed:dateRevised |
2007-11-14
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pubmed:meshHeading |
pubmed-meshheading:11960904-Humans,
pubmed-meshheading:11960904-Neoplasms,
pubmed-meshheading:11960904-Nuclear Proteins,
pubmed-meshheading:11960904-Phosphorylation,
pubmed-meshheading:11960904-Protein Conformation,
pubmed-meshheading:11960904-Protein Processing, Post-Translational,
pubmed-meshheading:11960904-Proto-Oncogene Proteins,
pubmed-meshheading:11960904-Proto-Oncogene Proteins c-mdm2,
pubmed-meshheading:11960904-Tumor Suppressor Protein p53
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pubmed:year |
2002
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pubmed:articleTitle |
p53-Mdm2--the affair that never ends.
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pubmed:affiliation |
Ruttenberg Cancer Center Mount Sinai School of Medicine, New York, NY 10029, USA.
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pubmed:publicationType |
Journal Article,
Research Support, U.S. Gov't, P.H.S.,
Review
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