Mdm2 binding to a conformationally sensitive domain on p53 can be modulated by RNA (Q73713259)

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6 November 2019

title

Mdm2 binding to a conformationally sensitive domain on p53 can be modulated by RNA (English)

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6 November 2019

4

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6 November 2019

author name string

L R Burch

1

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6 November 2019

C A Midgley

2

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6 November 2019

R A Currie

3

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6 November 2019

T R Hupp

5

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6 November 2019

publication date

1 April 2000

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6 November 2019

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6 November 2019

volume

472

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6 November 2019

issue

1

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6 November 2019

page(s)

93-98

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Oncoprotein MDM2 is a ubiquitin ligase E3 for tumor suppressor p53

6 November 2019

cites work

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The proliferation of normal human fibroblasts is dependent upon negative regulation of p53 function by mdm2.

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Restoration of the growth suppression function of mutant p53 by a synthetic peptide derived from the p53 C-terminal domain

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Restoration of transcriptional activity of p53 mutants in human tumour cells by intracellular expression of anti-p53 single chain Fv fragments

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DNA damage triggers DRB-resistant phosphorylation of human p53 at the CK2 site

7 January 2021

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DNA damage-induced phosphorylation of p53 alleviates inhibition by MDM2

7 January 2021

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Phosphorylation of p53 serine 15 increases interaction with CBP

7 January 2021

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Two distinct signaling pathways activate the latent DNA binding function of p53 in a casein kinase II-independent manner.

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Mapping of the p53 and mdm-2 interaction domains

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Structure of the MDM2 oncoprotein bound to the p53 tumor suppressor transactivation domain

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Critical role for Ser20 of human p53 in the negative regulation of p53 by Mdm2.

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The tumor suppressor p53 and the oncoprotein simian virus 40 T antigen bind to overlapping domains on the MDM2 protein

7 January 2021

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Regulation of Mdm2-directed degradation by the C terminus of p53.

7 January 2021

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The MDM2 oncoprotein binds specifically to RNA through its RING finger domain

7 January 2021

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The RING finger. A novel protein sequence motif related to the zinc finger.

7 January 2021

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Allosteric regulation of the thermostability and DNA binding activity of human p53 by specific interacting proteins. CRC Cell Transformation Group

7 January 2021

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Characterisation of epitopes on human p53 using phage-displayed peptide libraries: insights into antibody-peptide interactions.

7 January 2021

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Regulation of p53 protein function through alterations in protein-folding pathways

7 January 2021

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Crystal structure of the tetramerization domain of the p53 tumor suppressor at 1.7 angstroms

7 January 2021

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Drosophila homologs of baculovirus inhibitor of apoptosis proteins function to block cell death

7 January 2021

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Conservation of structural domains and biochemical activities of the MDM2 protein from Xenopus laevis.

7 January 2021

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The promyelocytic leukemia protein PML has a pro-apoptotic activity mediated through its RING domain

7 January 2021

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An arenavirus RING (zinc-binding) protein binds the oncoprotein promyelocyte leukemia protein (PML) and relocates PML nuclear bodies to the cytoplasm.

7 January 2021

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inferred from DOI database lookup

7 January 2021

based on heuristic

Identifiers

DOI

10.1016/S0014-5793(00)01427-7

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6 November 2019

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