Allosteric activation of latent p53 tetramers (Q28623087)

3 February 2017

title

Allosteric activation of latent p53 tetramers (English)

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3 February 2017

T. R. Hupp

1

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3 February 2017

D. P. Lane

series ordinal

2

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3 February 2017

language of work or name

English

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publication date

1 October 1994

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3 February 2017

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3 February 2017

volume

4

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3 February 2017

issue

10

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3 February 2017

page(s)

865–875

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UV Irradiation Stimulates Levels of p53 Cellular Tumor Antigen in Nontransformed Mouse Cells

3 February 2017

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The p21 Cdk-interacting protein Cip1 is a potent inhibitor of G1 cyclin-dependent kinases

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Characterization of the human p53 gene

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Regulation of the specific DNA binding function of p53

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Mutation of the casein kinase II phosphorylation site abolishes the anti-proliferative activity of p53.

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The p53 protein is an unusually shaped tetramer that binds directly to DNA.

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7 January 2021

The p53 tumour suppressor protein is phosphorylated at serine 389 by casein kinase II.

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Human DNA-activated protein kinase phosphorylates serines 15 and 37 in the amino-terminal transactivation domain of human p53.

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Human p53 is phosphorylated by p60-cdc2 and cyclin B-cdc2

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Characterization of the tumor suppressor protein p53 as a protein kinase C substrate and a S100b-binding protein

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Definition of a consensus binding site for p53

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Site-specific binding of wild-type p53 to cellular DNA is inhibited by SV40 T antigen and mutant p53

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Enhanced binding activity observed between anti-carcinoembryonic monoclonal antibodies

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Activation of the cryptic DNA binding function of mutant forms of p53.

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7 January 2021

Conformational shifts propagate from the oligomerization domain of p53 to its tetrameric DNA binding domain and restore DNA binding to select p53 mutants.

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7 January 2021

Allosteric proteins and cellular control systems

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7 January 2021

10.1016/S0960-9822(00)00195-0

Identifiers

DOI

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