(Q46970010)

27 December 2017

title

Multienzyme assembly of a p53 transcription complex (English)

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27 December 2017

author

Malcolm Walkinshaw

series ordinal

2

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27 December 2017

author name string

Ted R Hupp

series ordinal

1

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27 December 2017

publication date

1 October 2007

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27 December 2017

Nature Structural & Molecular Biology

published in

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27 December 2017

volume

14

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27 December 2017

issue

10

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27 December 2017

page(s)

885-887

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27 December 2017

https://scigraph.springernature.com/pub.10.1038/nsmb1007-885

exact match

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cites work

The P53 pathway: what questions remain to be explored?

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The prolyl isomerase Pin1 orchestrates p53 acetylation and dissociation from the apoptosis inhibitor iASPP

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A mouse p53 mutant lacking the proline-rich domain rescues Mdm4 deficiency and provides insight into the Mdm2-Mdm4-p53 regulatory network

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Small peptides activate the latent sequence-specific DNA binding function of p53.

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Inhibition of p53-dependent transcription by BOX-I phospho-peptide mimetics that bind to p300.

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1 reference

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Four domains of p300 each bind tightly to a sequence spanning both transactivation subdomains of p53

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Mutations in proline 82 of p53 impair its activation by Pin1 and Chk2 in response to DNA damage

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Acetylation of p53 activates transcription through recruitment of coactivators/histone acetyltransferases

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p53 Functions through Stress- and Promoter-Specific Recruitment of Transcription Initiation Components before and after DNA Damage

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p53 must be competent for transcriptional regulation to suppress tumor formation

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Defective apoptosis and B-cell lymphomas in mice with p53 point mutation at Ser 23.

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Lack of p53 Ser389 phosphorylation predisposes mice to develop 2-acetylaminofluorene-induced bladder tumors but not ionizing radiation-induced lymphomas

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Functional analysis of the roles of posttranslational modifications at the p53 C terminus in regulating p53 stability and activity

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Quaternary structures of tumor suppressor p53 and a specific p53 DNA complex

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The Proline Repeat Domain of p53 Binds Directly to the Transcriptional Coactivator p300 and Allosterically Controls DNA-Dependent Acetylation of p53

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Recognition of DNA by p53 Core Domain and Location of Intermolecular Contacts of Cooperative Binding

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A proline repeat domain in the Notch co-activator MAML1 is important for the p300-mediated acetylation of MAML1.

31 March 2020

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Pin1-dependent prolyl isomerization regulates dephosphorylation of Cdc25C and tau proteins

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Structural Basis for High-Affinity Peptide Inhibition of Human Pin1

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Structural basis for phosphoserine-proline recognition by group IV WW domains

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The prolyl isomerase Pin1 is a regulator of p53 in genotoxic response.

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Allosteric effects mediate CHK2 phosphorylation of the p53 transactivation domain.

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ATM and ATR substrate analysis reveals extensive protein networks responsive to DNA damage

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Structural insights into the catalytic mechanism of cyclophilin A

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31 March 2020

Identifiers

DOI

10.1038/NSMB1007-885

1 reference

27 December 2017

Dimensions Publication ID

1008356044

0 references

1 reference

27 December 2017