About: Activation of the DNA-binding ability of latent p53 protein by protein kinase C is abolished by protein kinase CK2.

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About: Activation of the DNA-binding ability of latent p53 protein by protein kinase C is abolished by protein kinase CK2. Goto Sponge NotDistinct Permalink

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	p53 is one of the most important regulators of cell proliferation and differentiation and of programmed cell death, triggering growth arrest and/or apoptosis in response to different cellular stress signals. The sequence-specific DNA-binding function of p53 protein can be activated by several different stimuli that modulate the C-terminal domain of this protein. The predominant mechanism of activation of p53 sequence-specific DNA binding is phosphorylation at specific sites. For example, phosphorylation of p53 by PKC (protein kinase C) occurs in undamaged cells, resulting in masking of the epitope recognized by monoclonal antibody PAb421, and presumably promotes steady-state levels of p53 activity in cycling cells. In contrast, phosphorylation by cdk2 (cyclin-dependent kinase 2)/cyclin A and by the protein kinase CK2 are both enhanced in DNA-damaged cells. p53 is one of the most important regulators of cell proliferation and differentiation and of programmed cell death, triggering growth arrest and/or apoptosis in response to different cellular stress signals. The sequence-specific DNA-binding function of p53 protein can be activated by several different stimuli that modulate the C-terminal domain of this protein. The predominant mechanism of activation of p53 sequence-specific DNA binding is phosphorylation at specific sites. For example, phosphorylation of p53 by PKC (protein kinase C) occurs in undamaged cells, resulting in masking of the epitope recognized by monoclonal antibody PAb421, and presumably promotes steady-state levels of p53 activity in cycling cells. In contrast, phosphorylation by cdk2 (cyclin-dependent kinase 2)/cyclin A and by the protein kinase CK2 are both enhanced in DNA-damaged cells. (en) p53 is one of the most important regulators of cell proliferation and differentiation and of programmed cell death, triggering growth arrest and/or apoptosis in response to different cellular stress signals. The sequence-specific DNA-binding function of p53 protein can be activated by several different stimuli that modulate the C-terminal domain of this protein. The predominant mechanism of activation of p53 sequence-specific DNA binding is phosphorylation at specific sites. For example, phosphorylation of p53 by PKC (protein kinase C) occurs in undamaged cells, resulting in masking of the epitope recognized by monoclonal antibody PAb421, and presumably promotes steady-state levels of p53 activity in cycling cells. In contrast, phosphorylation by cdk2 (cyclin-dependent kinase 2)/cyclin A and by the protein kinase CK2 are both enhanced in DNA-damaged cells. (cs)
Title	Activation of the DNA-binding ability of latent p53 protein by protein kinase C is abolished by protein kinase CK2. Activation of the DNA-binding ability of latent p53 protein by protein kinase C is abolished by protein kinase CK2. (en) Activation of the DNA-binding ability of latent p53 protein by protein kinase C is abolished by protein kinase CK2. (cs)
skos:prefLabel	Activation of the DNA-binding ability of latent p53 protein by protein kinase C is abolished by protein kinase CK2. Activation of the DNA-binding ability of latent p53 protein by protein kinase C is abolished by protein kinase CK2. (en) Activation of the DNA-binding ability of latent p53 protein by protein kinase C is abolished by protein kinase CK2. (cs)
skos:notation	RIV/65269705:_____/07:#0000390!RIV09-MZ0-65269705
http://linked.open...avai/riv/aktivita	V
http://linked.open...avai/riv/aktivity	V
http://linked.open...iv/cisloPeriodika	Pt3
http://linked.open...vai/riv/dodaniDat	2009
http://linked.open...aciTvurceVysledku	Pospíšilová, Šárka
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	Fakultní nemocnice Brno / (nerozlišená součást)
http://linked.open...dnocenehoVysledku	408459
http://linked.open...ai/riv/idVysledku	RIV/65269705:_____/07:#0000390
http://linked.open...riv/jazykVysledku	eng - angličtina
http://linked.open.../riv/klicovaSlova	protein p53 (en)
http://linked.open.../riv/klicoveSlovo	protein p53
http://linked.open...odStatuVydavatele	GB - Spojené království Velké Británie a Severního Irska
http://linked.open...ontrolniKodProRIV	[F896B89F4D2C]
http://linked.open...i/riv/nazevZdroje	Biochemical Journal
http://linked.open...in/vavai/riv/obor	FD
http://linked.open...ichTvurcuVysledku	1 (xsd:int)
http://linked.open...cetTvurcuVysledku	8 (xsd:int)
http://linked.open...UplatneniVysledku	2007
http://linked.open...v/svazekPeriodika	378
http://linked.open...iv/tvurceVysledku	Pospíšilová, Šárka
issn	1214-0287
number of pages	9 (xsd:int)

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