Diverse effects of BCL3 phosphorylation on its modulation of NF-kappaB p52 homodimer binding to DNA (Q24315762)

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8 November 2019

title

Diverse effects of BCL3 phosphorylation on its modulation of NF-kappaB p52 homodimer binding to DNA (English)

1 reference

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8 November 2019

0 references

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I-kappaB/NF-kappaB complex

1 reference

Gene Ontology release 2020-05-02

Gene Ontology ID

GO:0033256

Bcl3/NF-kappaB2 complex

1 reference

Gene Ontology release 2020-05-02

Gene Ontology ID

GO:0033257

Nuclear factor kappa B subunit 2

1 reference

BCL3 transcription coactivator

GOA release 2020-03-11

1 reference

GOA release 2020-03-11

author

Timothy W McKeithan

series ordinal

2

1 reference

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8 November 2019

author name string

D L Bundy

series ordinal

1

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8 November 2019

language of work or name

English

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publication date

1 December 1997

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Journal of Biological Chemistry

8 November 2019

published in

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8 November 2019

volume

272

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8 November 2019

issue

52

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8 November 2019

page(s)

33132-33139

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Common structural constituents confer I kappa B activity to NF-kappa B p105 and I kappa B/MAD-3.

8 November 2019

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The DNA binding subunit of NF-kappa B is identical to factor KBF1 and homologous to the rel oncogene product

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The candidate proto-oncogene bcl-3 is related to genes implicated in cell lineage determination and cell cycle control

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Purified human I kappa B can rapidly dissociate the complex of the NF-kappa B transcription factor with its cognate DNA.

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Characterization of an immediate-early gene induced in adherent monocytes that encodes IκB-like activity

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DNA binding and I kappa B inhibition of the cloned p65 subunit of NF-kappa B, a rel-related polypeptide

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The oncoprotein Bcl-3 directly transactivates through kappa B motifs via association with DNA-binding p50B homodimers

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I kappa B-beta regulates the persistent response in a biphasic activation of NF-kappa B

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Cloning of an NF-kappa B subunit which stimulates HIV transcription in synergy with p65

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Characterization of cDNA for the large subunit of the transcription initiation factor TFIIF

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Candidate proto-oncogene bcl-3 encodes a subunit-specific inhibitor of transcription factor NF-kappa B

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7 January 2021

The candidate oncoprotein Bcl-3 is an antagonist of p50/NF-kappa B-mediated inhibition

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Structure of NF-kappa B p50 homodimer bound to a kappa B site

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7 January 2021

Structure of the NF-kappa B p50 homodimer bound to DNA

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Cloning of the DNA-binding subunit of human nuclear factor kappa B: the level of its mRNA is strongly regulated by phorbol ester or tumor necrosis factor alpha

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Distinct combinations of NF-kappa B subunits determine the specificity of transcriptional activation

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The ankyrin repeat domains of the NF-kappa B precursor p105 and the protooncogene bcl-3 act as specific inhibitors of NF-kappa B DNA binding

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Disulfide cross-linking in crude embryonic lysates reveals three complexes of the Drosophila morphogen dorsal and its inhibitor cactus

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Regulation of the human P-selectin promoter by Bcl-3 and specific homodimeric members of the NF-kappa B/Rel family

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7 January 2021

Regulation of NFKB1 proteins by the candidate oncoprotein BCL-3: generation of NF-kappaB homodimers from the cytoplasmic pool of p50-p105 and nuclear translocation

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7 January 2021

I kappa B epsilon, a novel member of the I kappa B family, controls RelA and cRel NF-kappa B activity

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The candidate proto-oncogene bcl-3 encodes a transcriptional coactivator that activates through NF-kappa B p50 homodimers

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7 January 2021

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7 January 2021

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7 January 2021

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7 January 2021

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Identifiers

DOI

10.1074/JBC.272.52.33132

2 references

Consolidated OpenCitations Corpus – April 2017

3672886

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8 November 2019

3672886

1 reference

Consolidated OpenCitations Corpus – April 2017

Consolidated OpenCitations Corpus – April 2017

2 references

3672886