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rdf:type |
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lifeskim:mentions |
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pubmed:issue |
1
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pubmed:dateCreated |
2011-1-7
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pubmed:abstractText |
The p53 tumor suppressor is recognized as a promising target for anti-cancer therapies. We previously reported that protoporphyrin IX (PpIX) disrupts the p53/murine double minute 2 (MDM2) complex and leads to p53 accumulation and activation of apoptosis in HCT 116 cells. Here we show the direct binding of PpIX to the N-terminal domain of p53. Furthermore, we addressed the induction of apoptosis in HCT 116 p53-null cells by PpIX and revealed interactions between PpIX and p73. We propose that PpIX disrupts the p53/MDM2 or MDMX and p73/MDM2 complexes and thereby activates the p53- or p73-dependent cancer cell death.
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pubmed:language |
eng
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pubmed:journal |
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pubmed:citationSubset |
IM
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pubmed:chemical |
http://linkedlifedata.com/resource/pubmed/chemical/DNA-Binding Proteins,
http://linkedlifedata.com/resource/pubmed/chemical/Glutathione Transferase,
http://linkedlifedata.com/resource/pubmed/chemical/MDM2 protein, human,
http://linkedlifedata.com/resource/pubmed/chemical/MDM4 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/Protoporphyrins,
http://linkedlifedata.com/resource/pubmed/chemical/Recombinant Fusion Proteins,
http://linkedlifedata.com/resource/pubmed/chemical/Tumor Suppressor Protein p53,
http://linkedlifedata.com/resource/pubmed/chemical/Tumor Suppressor Proteins,
http://linkedlifedata.com/resource/pubmed/chemical/protoporphyrin IX,
http://linkedlifedata.com/resource/pubmed/chemical/tumor suppressor protein p73
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pubmed:status |
MEDLINE
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pubmed:month |
Jan
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pubmed:issn |
1873-3468
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pubmed:author |
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pubmed:copyrightInfo |
Copyright © 2010 Federation of European Biochemical Societies. Published by Elsevier B.V. All rights reserved.
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pubmed:issnType |
Electronic
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pubmed:day |
3
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pubmed:volume |
585
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pubmed:owner |
NLM
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pubmed:authorsComplete |
Y
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pubmed:pagination |
255-60
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pubmed:meshHeading |
pubmed-meshheading:21146529-Apoptosis,
pubmed-meshheading:21146529-Binding Sites,
pubmed-meshheading:21146529-DNA-Binding Proteins,
pubmed-meshheading:21146529-Electrophoresis, Polyacrylamide Gel,
pubmed-meshheading:21146529-Fluorescence Polarization,
pubmed-meshheading:21146529-Glutathione Transferase,
pubmed-meshheading:21146529-HCT116 Cells,
pubmed-meshheading:21146529-Humans,
pubmed-meshheading:21146529-Mutation,
pubmed-meshheading:21146529-Nuclear Proteins,
pubmed-meshheading:21146529-Protein Binding,
pubmed-meshheading:21146529-Proto-Oncogene Proteins,
pubmed-meshheading:21146529-Proto-Oncogene Proteins c-mdm2,
pubmed-meshheading:21146529-Protoporphyrins,
pubmed-meshheading:21146529-Recombinant Fusion Proteins,
pubmed-meshheading:21146529-Tumor Suppressor Protein p53,
pubmed-meshheading:21146529-Tumor Suppressor Proteins
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pubmed:year |
2011
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pubmed:articleTitle |
Targeting of p53 and its homolog p73 by protoporphyrin IX.
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pubmed:affiliation |
Department of Biotechnology, Intercollegiate Faculty of Biotechnology, University of Gdansk & Medical University of Gdansk, Gdansk, Poland.
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pubmed:publicationType |
Journal Article,
Research Support, Non-U.S. Gov't
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