Multiple Lysine Mutations in the C-Terminal Domain of p53 Interfere with MDM2-Dependent Protein Degradation and Ubiquitination

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Veröffentlicht in:	Molecular and Cellular Biology 2000-12, Vol.20 (24), p.9391-9398
Hauptverfasser:	Nakamura, Seiichi, Roth, Jack A., Mukhopadhyay, Tapas
Format:	Artikel
Sprache:	eng
Schlagworte:	Acetylation Amino Acid Sequence Amino Acid Substitution Carcinoma, Non-Small-Cell Lung Cell Fractionation Ecdysone - analogs & derivatives Ecdysone - pharmacology Fatty Acids, Unsaturated - pharmacology Gene Expression Gene Expression Regulation Genes, p53 - genetics Genes, Reporter GTPase-Activating Proteins - metabolism Humans Immunoblotting Immunohistochemistry Lung Neoplasms MDM2 gene MDM2 protein Nuclear Proteins - genetics Nuclear Proteins - metabolism p53 gene Plasmids - genetics Plasmids - metabolism Point Mutation Precipitin Tests Protein Structure, Tertiary Proto-Oncogene Proteins - metabolism Proto-Oncogene Proteins c-mdm2 Transcriptional Activation Transfection Tumor Cells, Cultured Tumor Suppressor Protein p53 - chemistry Tumor Suppressor Protein p53 - genetics Tumor Suppressor Protein p53 - metabolism ubiquitin ubiquitination
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Zusammenfassung:	Article Usage Stats Services MCB Citing Articles Google Scholar PubMed Related Content Social Bookmarking CiteULike Delicious Digg Facebook Google+ Mendeley Reddit StumbleUpon Twitter current issue Spotlights in the Current Issue MCB About MCB Subscribers Authors Reviewers Advertisers Inquiries from the Press Permissions & Commercial Reprints ASM Journals Public Access Policy MCB RSS Feeds 1752 N Street N.W. • Washington DC 20036 202.737.3600 • 202.942.9355 fax • journals@asmusa.org Print ISSN: 0270-7306 Online ISSN: 1098-5549 Copyright © 2014 by the American Society for Microbiology. For an alternate route to MCB .asm.org, visit: MCB
ISSN:	0270-7306 1098-5549 1098-5549
DOI:	10.1128/MCB.20.24.9391-9398.2000