About: Recognition of DNA modified by antitumor cisplatin by

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An Entity of Type : http://linked.opendata.cz/ontology/domain/vavai/Vysledek, within Data Space : linked.opendata.cz associated with source document(s)

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rdf:type	skos:Concept http://linked.opendata.cz/ontology/domain/vavai/Vysledek
Description	Binding of active, latent, and in vitro-activated p53 protein to DNA fragments modified by antitumor cisplatin was studied using electrophoretic mobility shift assay in agarose gels and immunoblotting analysis. We found that both latent and active p53 forms bound to random sequences of DNA globally modified by cisplatin with a higher affinity than to unmodified DNA. Interestingly, the latent form exhibited a more pronounced selectivity for platinated DNA than the active p53. Consistently with this observation, the preference of the latent form for platinated DNA decreased as a consequence of the activation of latent p53 by phosphorylation at the protein kinase C site within its C-terminus or by binding of the monoclonal antibody Bp53-10.1. Competition experiments involving a 20-bp consensus sequence of p53 suggested that the p53 core domain was a primary binding site of the active p53 when it bound to DNA fragments lacking consensus sequence, but modified by cisplatin. In addition, the latent protein Binding of active, latent, and in vitro-activated p53 protein to DNA fragments modified by antitumor cisplatin was studied using electrophoretic mobility shift assay in agarose gels and immunoblotting analysis. We found that both latent and active p53 forms bound to random sequences of DNA globally modified by cisplatin with a higher affinity than to unmodified DNA. Interestingly, the latent form exhibited a more pronounced selectivity for platinated DNA than the active p53. Consistently with this observation, the preference of the latent form for platinated DNA decreased as a consequence of the activation of latent p53 by phosphorylation at the protein kinase C site within its C-terminus or by binding of the monoclonal antibody Bp53-10.1. Competition experiments involving a 20-bp consensus sequence of p53 suggested that the p53 core domain was a primary binding site of the active p53 when it bound to DNA fragments lacking consensus sequence, but modified by cisplatin. In addition, the latent protein (en)
Title	Recognition of DNA modified by antitumor cisplatin by Recognition of DNA modified by antitumor cisplatin by (en)
skos:prefLabel	Recognition of DNA modified by antitumor cisplatin by Recognition of DNA modified by antitumor cisplatin by (en)
skos:notation	RIV/00209805:_____/03:00008208!RIV/2004/GA0/L26004/N
http://linked.open.../vavai/riv/strany	1305; 1316
http://linked.open...avai/riv/aktivita	P
http://linked.open...avai/riv/aktivity	P(GA301/02/0831), P(NC7131)
http://linked.open...iv/cisloPeriodika	8
http://linked.open...vai/riv/dodaniDat	2004
http://linked.open...aciTvurceVysledku	Vojtěšek, Bořivoj
http://linked.open.../riv/druhVysledku	J - Článek v odborném periodiku
http://linked.open...iv/duvernostUdaju	S - Úplné a pravdivé údaje nepodléhající ochraně podle zvláštních právních předpisů
http://linked.open...titaPredkladatele	Masarykův onkologický ústav
http://linked.open...dnocenehoVysledku	624817
http://linked.open...ai/riv/idVysledku	RIV/00209805:_____/03:00008208
http://linked.open...riv/jazykVysledku	eng - angličtina
http://linked.open.../riv/klicovaSlova	Latent p53;Antitumour drugs;Cisplatin;DNA damage;Protein-DNA interaction (en)
http://linked.open.../riv/klicoveSlovo	Cisplatin DNA damage Protein-DNA interaction Antitumour drugs Latent p53
http://linked.open...odStatuVydavatele	GB - Spojené království Velké Británie a Severního Irska
http://linked.open...ontrolniKodProRIV	[A2DFA856F3E6]
http://linked.open...i/riv/nazevZdroje	Biochemical Pharmacology
http://linked.open...in/vavai/riv/obor	FD
http://linked.open...ichTvurcuVysledku	2 (xsd:int)
http://linked.open...cetTvurcuVysledku	9 (xsd:int)
http://linked.open...vavai/riv/projekt	Interactions of p53 protein and its homologues with DNA and their role in malignant transformation Analysis of functional alterations of mutant forms of p53 protein in human cancers.
http://linked.open...UplatneniVysledku	2003
http://linked.open...v/svazekPeriodika	65
http://linked.open...iv/tvurceVysledku	Vojtěšek, Bořivoj
issn	0006-2952
number of pages	12 (xsd:int)

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