About: Oligomerization is required for p53 to be efficiently ubiquitinated by MDM2

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scientific journal article

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rdf:type	Item
description	artículu científicu espublizáu en 1999 (ast) vědecký článek publikovaný v roce 1999 (cs) наукова стаття, опублікована в червні 1999 (uk) 1999 թուականի Յունիսին հրատարակուած գիտական յօդուած (hyw) 1999 թվականի հունիսին հրատարակված գիտական հոդված (hy) vedecký článok (publikovaný 1999/06/04) (sk) مقالة علمية (نشرت في 4-6-1999) (ar) article publié dans la revue scientifique Journal of Biological Chemistry (fr) wetenschappelijk artikel (gepubliceerd op 1999/06/04) (nl) im Juni 1999 veröffentlichter wissenschaftlicher Artikel (de) scientific journal article (en)
publication date	wds:Q28609844-05D37C54-871B-4EBF-8010-5841FDEB44F0
publication date	1999-06-04 00:00:00Z (xsd:dateTime)
language of work or name	wds:Q28609844-1753B1BE-5B25-4F09-A9E7-645F3CCAA0C1
language of work or name	English
cites work	wds:Q28609844-02A19E57-F32E-479C-B058-C88EB6D2FF85 wds:Q28609844-04ED9CB4-F930-42D9-935B-CD10ED1C7CDF wds:Q28609844-1B24F41F-0ED3-4713-98DD-5AC06ACAEC42 wds:Q28609844-31444F1F-D614-4DBE-914C-CFB57AB72A00 wds:Q28609844-4048F840-F992-4201-80EF-BEF998FA0650 wds:Q28609844-420E949C-3F2B-4F16-B264-76A3032A14FA wds:Q28609844-59325E05-87CD-45E0-AD48-A22F7E852667 wds:Q28609844-5E430DF6-67B2-42B8-965E-4B93C060D0DD wds:Q28609844-64386D61-E00E-49E7-B5DE-26C7D76916B6 wds:Q28609844-6B7A5F7F-3172-4412-9A0A-2A64F3C4842F wds:Q28609844-78393C43-E0C0-4742-8042-6CC801AE3F89 wds:Q28609844-7874BAA6-107A-4BD0-B1B7-00025A3AA9A1 wds:Q28609844-7F09405C-49D3-41EC-BFE4-00C2D93D6410 wds:Q28609844-7F414B06-57BE-455F-9C5A-9308B7AB33F8 wds:Q28609844-8FBCCAB8-5C28-4F34-BD66-5746D9C8E1C6 wds:Q28609844-9182A37F-4CCD-49FA-98FB-FC42BCD21D6F wds:Q28609844-92B0660A-82C7-4D58-A5CD-8B1620816458 wds:Q28609844-95742355-06A7-4C4B-B8E7-56582D86FAFA wds:Q28609844-95DE0112-F448-4975-82B3-A53FB0B18465 wds:Q28609844-981512CA-0E7B-4D06-8C0A-9AC879C1060E wds:Q28609844-AD9F8936-C11D-4008-9338-1426ACF392BC wds:Q28609844-BDB31C44-C945-44D3-8EBB-0801314A940B wds:Q28609844-C1417F61-9366-45EE-A0F3-437005FE1648 wds:Q28609844-E93A6749-9AC3-486F-8DCD-BFD5F77C6148 wds:Q28609844-F475A0DE-4D54-4B65-98B9-C0ABE6658A47 wds:Q28609844-FB25B088-963E-4FD9-80C2-2B0EFBACF190
cites work	Mdm2 promotes the rapid degradation of p53 Regulation of p53 stability by Mdm2 DNA damage-induced phosphorylation of p53 alleviates inhibition by MDM2 Accumulation of p53 in a mutant cell line defective in the ubiquitin pathway Nuclear export is required for degradation of endogenous p53 by MDM2 and human papillomavirus E6 The mdm-2 gene is induced in response to UV light in a p53-dependent manner Oncoprotein MDM2 is a ubiquitin ligase E3 for tumor suppressor p53 Cancer. p53, guardian of the genome The mdm-2 oncogene product forms a complex with the p53 protein and inhibits p53-mediated transactivation Proteolytic cleavage of human p53 by calpain: a potential regulator of protein stability p53, the cellular gatekeeper for growth and division Ubiquitin-dependent protein degradation p53: puzzle and paradigm Sequence-specific transcriptional activation is essential for growth suppression by p53. Human papillomavirus 16 E6 expression disrupts the p53-mediated cellular response to DNA damage Amplification of a gene encoding a p53-associated protein in human sarcomas Mapping of the p53 and mdm-2 interaction domains Ubiquitination of p53 and p21 is differentially affected by ionizing and UV radiation Proteolysis by calpains: a possible contribution to degradation of p53. A transcriptionally active DNA-binding site for human p53 protein complexes Regulation of Mdm2-directed degradation by the C terminus of p53. Design of a synthetic Mdm2-binding mini protein that activates the p53 response in vivo. UV Irradiation Stimulates Levels of p53 Cellular Tumor Antigen in Nontransformed Mouse Cells Protein ubiquitination involving an E1-E2-E3 enzyme ubiquitin thioester cascade Nuclear accumulation of p53 protein is mediated by several nuclear localization signals and plays a role in tumorigenesis Cellular localization and cell cycle regulation by a temperature-sensitive p53 protein
author name string	wds:Q28609844-2F02B91C-D98A-4C30-A8DE-71E5E4B31CD1
OpenCitations bibliographic resource ID	wds:Q28609844-C55B31B2-2904-4779-89B1-3D274A2D5C6B
OpenCitations bibliographic resource ID	https://w3id.org/oc/corpus/br/3467555
author name string	C. G. Maki
OpenCitations bibliographic resource ID	3467555
rdfs:label	Oligomerization is required for p53 to be efficiently ubiquitinated by MDM2 (en) Oligomerization is required for p53 to be efficiently ubiquitinated by MDM2 (nl) Oligomerization is required for p53 to be efficiently ubiquitinated by MDM2 (ast)
skos:prefLabel	Oligomerization is required for p53 to be efficiently ubiquitinated by MDM2 (en) Oligomerization is required for p53 to be efficiently ubiquitinated by MDM2 (nl) Oligomerization is required for p53 to be efficiently ubiquitinated by MDM2 (ast)
name	Oligomerization is required for p53 to be efficiently ubiquitinated by MDM2 (en) Oligomerization is required for p53 to be efficiently ubiquitinated by MDM2 (nl) Oligomerization is required for p53 to be efficiently ubiquitinated by MDM2 (ast)
title	wds:Q28609844-8A6475BD-FA5A-4350-9963-30B02F3077C6
title	Oligomerization is required for p53 to be efficiently ubiquitinated by MDM2 (en)
page(s)	wds:Q28609844-9B543AFB-E650-4C2B-92AD-DB6843FB8796
page(s)	16531–16535
instance of	wds:Q28609844-44675071-43DA-41C8-AC1D-FDC8B0385A6F
instance of	scholarly article
main subject	wds:Q28609844-98BC3B68-6322-40B9-A817-A0F0C8408EDD
main subject	protein ubiquitination
PubMed ID	wds:Q28609844-AC510FBB-8949-40B5-86E7-B72F9E9FCCCD
PubMed ID	http://rdf.ncbi.nlm.nih.gov/pubchem/reference/10347217
PubMed ID	10347217
published in	wds:Q28609844-E90ED81A-CAC2-4E85-885E-52BBAA5646EB
published in	Journal of Biological Chemistry
issue	wds:Q28609844-4D6C975A-1BEF-463C-AA97-CAEC89AC2E8A
volume	wds:Q28609844-78195A1B-41C2-40FB-9614-6B20837386A8
issue	23
volume	274
DOI	wds:Q28609844-9073DCC3-2400-4E45-9603-940A27F4AE05

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