Binding of p53 to the central domain of Mdm2 is regulated by phosphorylation (Q40251109)

18 September 2017

Binding of p53 to the central domain of Mdm2 is regulated by phosphorylation (English)

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18 September 2017

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Roman Kulikov

1

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18 September 2017

Markus Winter

series ordinal

2

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18 September 2017

Christine Blattner

series ordinal

3

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18 September 2017

language of work or name

English

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publication date

26 July 2006

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Journal of Biological Chemistry

18 September 2017

9

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based on heuristic

inferred from page(s)

published in

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18 September 2017

281

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18 September 2017

39

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18 September 2017

28575-28583

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Mdm2 promotes the rapid degradation of p53

18 September 2017

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https://api.crossref.org/works/10.1074%2FJBC.M513311200

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

21 January 2018

1 reference

https://api.crossref.org/works/10.1074%2FJBC.M513311200

Rescue of embryonic lethality in Mdm2-deficient mice by absence of p53

21 January 2018

1 reference

https://api.crossref.org/works/10.1074%2FJBC.M513311200

Rescue of early embryonic lethality in mdm2-deficient mice by deletion of p53

21 January 2018

1 reference

https://api.crossref.org/works/10.1074%2FJBC.M513311200

Nuclear export is required for degradation of endogenous p53 by MDM2 and human papillomavirus E6

21 January 2018

1 reference

https://api.crossref.org/works/10.1074%2FJBC.M513311200

Identification of a cryptic nucleolar-localization signal in MDM2

21 January 2018

1 reference

https://api.crossref.org/works/10.1074%2FJBC.M513311200

Nucleo-cytoplasmic shuttling of the hdm2 oncoprotein regulates the levels of the p53 protein via a pathway used by the human immunodeficiency virus rev protein.

21 January 2018

1 reference

https://api.crossref.org/works/10.1074%2FJBC.M513311200

Hypophosphorylation of Mdm2 augments p53 stability

21 January 2018

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https://api.crossref.org/works/10.1074%2FJBC.M513311200

DNA damage induced p53 stabilization: no indication for an involvement of p53 phosphorylation

21 January 2018

1 reference

https://api.crossref.org/works/10.1074%2FJBC.M513311200

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

21 January 2018

1 reference

https://api.crossref.org/works/10.1074%2FJBC.M513311200

The role of tetramerization in p53 function

21 January 2018

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https://api.crossref.org/works/10.1074%2FJBC.M513311200

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

21 January 2018

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https://api.crossref.org/works/10.1074%2FJBC.M513311200

Oligomerization is required for p53 to be efficiently ubiquitinated by MDM2

21 January 2018

1 reference

https://api.crossref.org/works/10.1074%2FJBC.M513311200

The conformationally flexible S9-S10 linker region in the core domain of p53 contains a novel MDM2 binding site whose mutation increases ubiquitination of p53 in vivo

21 January 2018

1 reference

https://api.crossref.org/works/10.1074%2FJBC.M513311200

Protein kinase CK1delta phosphorylates key sites in the acidic domain of murine double-minute clone 2 protein (MDM2) that regulate p53 turnover

21 January 2018

1 reference

https://api.crossref.org/works/10.1074%2FJBC.M513311200

In vivo activation of the p53 pathway by small-molecule antagonists of MDM2

21 January 2018

1 reference

https://api.crossref.org/works/10.1074%2FJBC.M513311200

Biogenesis of p53 involves cotranslational dimerization of monomers and posttranslational dimerization of dimers. Implications on the dominant negative effect

21 January 2018

1 reference

https://api.crossref.org/works/10.1074%2FJBC.M513311200

Characterization of p53 oligomerization domain mutations isolated from Li-Fraumeni and Li-Fraumeni like family members.

21 January 2018

1 reference

https://api.crossref.org/works/10.1074%2FJBC.M513311200

Critical contribution of the MDM2 acidic domain to p53 ubiquitination

21 January 2018

1 reference

https://api.crossref.org/works/10.1074%2FJBC.M513311200

Critical role for a central part of Mdm2 in the ubiquitylation of p53.

21 January 2018

1 reference

https://api.crossref.org/works/10.1074%2FJBC.M513311200

Association of p19(ARF) with Mdm2 inhibits ubiquitin ligase activity of Mdm2 for tumor suppressor p53.

21 January 2018

1 reference

https://api.crossref.org/works/10.1074%2FJBC.M513311200

Acetylation of p53 inhibits its ubiquitination by Mdm2.

21 January 2018

1 reference

https://api.crossref.org/works/10.1074%2FJBC.M513311200

MDM2-HDAC1-mediated deacetylation of p53 is required for its degradation

21 January 2018

1 reference

https://api.crossref.org/works/10.1074%2FJBC.M513311200

Molecular interaction map of the p53 and Mdm2 logic elements, which control the Off-On switch of p53 in response to DNA damage

21 January 2018

1 reference

https://api.crossref.org/works/10.1074%2FJBC.M513311200

Polyubiquitination of p53 by a ubiquitin ligase activity of p300.

21 January 2018

1 reference

https://api.crossref.org/works/10.1074%2FJBC.M513311200

The central region of HDM2 provides a second binding site for p53.

21 January 2018

1 reference

https://api.crossref.org/works/10.1074%2FJBC.M513311200

21 January 2018

Identifiers

DOI

10.1074/JBC.M513311200

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18 September 2017

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