| A new function for p53 ubiquitination. | |
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MedLine Citation:
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PMID: 17110328 Owner: NLM Status: MEDLINE |
Abstract/OtherAbstract:
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The amount of p53 protein in a cell is normally limited by ubiquitin-dependent degradation. In this issue of Cell, Le Cam et al. (2006) reveal that p53 ubiquitination contributes to transcriptional activation rather than protein stability. These results may provide insight into how p53 can modulate diverse cellular processes such as growth arrest and apoptosis. |
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Authors:
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Yuko Hirano; Ze'ev Ronai |
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Publication Detail:
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Type: Comment; Journal Article |
Journal Detail:
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Title: Cell Volume: 127 ISSN: 0092-8674 ISO Abbreviation: Cell Publication Date: 2006 Nov |
Date Detail:
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Created Date: 2006-11-19 Completed Date: 2006-12-22 Revised Date: 2007-11-15 |
Medline Journal Info:
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Nlm Unique ID: 0413066 Medline TA: Cell Country: United States |
Other Details:
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Languages: eng Pagination: 675-7 Citation Subset: IM |
Affiliation:
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Burnham Institute for Medical Research, La Jolla, CA 92130, USA. |
Export Citation:
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APA/MLA Format Download EndNote Download BibTex |
| MeSH Terms | |
Descriptor/Qualifier:
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Cell Cycle Proteins
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metabolism Histone Acetyltransferases / metabolism Humans Lysine / metabolism Proto-Oncogene Proteins c-mdm2 / metabolism Repressor Proteins / chemistry, metabolism Transcription Factors / metabolism Tumor Suppressor Protein p53 / metabolism* Ubiquitin-Protein Ligases / metabolism* p300-CBP Transcription Factors |
| Chemical | |
Reg. No./Substance:
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0/Cell Cycle Proteins; 0/E4F1 protein, human; 0/Repressor Proteins; 0/Transcription Factors; 0/Tumor Suppressor Protein p53; 56-87-1/Lysine; EC 2.3.1.48/Histone Acetyltransferases; EC 2.3.1.48/p300-CBP Transcription Factors; EC 2.3.1.48/p300-CBP-associated factor; EC 6.3.2.19/MDM2 protein, human; EC 6.3.2.19/Proto-Oncogene Proteins c-mdm2; EC 6.3.2.19/Ubiquitin-Protein Ligases |
| Comments/Corrections | |
Comment On:
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Cell. 2006 Nov 17;127(4):775-88
[PMID:
17110336
]
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From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine
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