Cytoplasmically "sequestered" wild type p53 protein is resistant to Mdm2-mediated degradation (Q48111113)

8 February 2018

title

Cytoplasmically "sequestered" wild type p53 protein is resistant to Mdm2-mediated degradation (English)

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8 February 2018

author name string

A Zaika

series ordinal

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8 February 2018

N Marchenko

series ordinal

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8 February 2018

U M Moll

series ordinal

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8 February 2018

language of work or name

English

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publication date

1 September 1999

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8 February 2018

Journal of Biological Chemistry

published in

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8 February 2018

volume

274

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issue

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8 February 2018

page(s)

27474-27480

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8 February 2018

Mdm2 promotes the rapid degradation of p53

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The Ink4a tumor suppressor gene product, p19Arf, interacts with MDM2 and neutralizes MDM2's inhibition of p53

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The alternative product from the human CDKN2A locus, p14(ARF), participates in a regulatory feedback loop with p53 and MDM2.

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Oncoprotein MDM2 conceals the activation domain of tumour suppressor p53

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ARF promotes MDM2 degradation and stabilizes p53: ARF-INK4a locus deletion impairs both the Rb and p53 tumor suppression pathways

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Human p53 expressed in baculovirus-infected Sf9 cells displays a two-dimensional isoform pattern identical to wild-type p53 from human cells

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p53 is covalently linked to 5.8S rRNA.

21 January 2018

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Regulation of the sequence-specific DNA binding function of p53 by protein kinase C and protein phosphatases

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Activation of p53 Sequence-Specific DNA Binding by Acetylation of the p53 C-Terminal Domain

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Cytoplasmically sequestered wild-type p53 protein in neuroblastoma is relocated to the nucleus by a C-terminal peptide

21 January 2018

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The human oncoprotein MDM2 arrests the cell cycle: elimination of its cell-cycle-inhibitory function induces tumorigenesis

21 January 2018

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Regulation of p53 function and stability by phosphorylation

21 January 2018

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JNK targets p53 ubiquitination and degradation in nonstressed cells

21 January 2018

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Synergistic activation of p53 by inhibition of MDM2 expression and DNA damage

21 January 2018

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21 January 2018

Identifiers

DOI

10.1074/JBC.274.39.27474

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8 February 2018

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8 February 2018