Phosphorylation of NF-kappa B p65 by PKA stimulates transcriptional activity by promoting a novel bivalent interaction with the coactivator CBP/p300 (Q28619230)

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English	Phosphorylation of NF-kappa B p65 by PKA stimulates transcriptional activity by promoting a novel bivalent interaction with the coactivator CBP/p300	scientific journal article

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scholarly article

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PubMed publication ID

3 February 2017

Phosphorylation of NF-kappa B p65 by PKA stimulates transcriptional activity by promoting a novel bivalent interaction with the coactivator CBP/p300 (English)

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PubMed publication ID

3 February 2017

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phosphorylation

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author name string

H. Zhong

1

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PubMed publication ID

3 February 2017

R. E. Voll

2

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PubMed publication ID

3 February 2017

S. Ghosh

3

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PubMed publication ID

3 February 2017

publication date

1 April 1998

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PubMed publication ID

3 February 2017

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PubMed publication ID

3 February 2017

1

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PubMed publication ID

3 February 2017

5

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PubMed publication ID

3 February 2017

661–671

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PubMed publication ID

3 February 2017

Recruitment of p300/CBP in p53-dependent signal pathways

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The NF-kappa B and I kappa B proteins: new discoveries and insights

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The CBP co-activator is a histone acetyltransferase

1 reference

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CBP as a transcriptional coactivator of c-Myb

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The EVES motif mediates both intermolecular and intramolecular regulation of c-Myb

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Interaction and functional collaboration of p300/CBP and bHLH proteins in muscle and B-cell differentiation

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CREB-binding protein/p300 are transcriptional coactivators of p65

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Activation of p53 sequence-specific DNA binding by acetylation of the p53 C-terminal domain

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A growing coactivator network

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Versatile molecular glue. Transcriptional control

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Association between proto-oncoprotein Rel and TATA-binding protein mediates transcriptional activation by NF-kappa B.

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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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Interaction of the co-activator CBP with Myb proteins: effects on Myb-specific transactivation and on the cooperativity with NF-M

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Phosphorylation of CREB at Ser-133 induces complex formation with CREB-binding protein via a direct mechanism

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Transactivation domain 2 (TA2) of p65 NF-kappa B. Similarity to TA1 and phorbol ester-stimulated activity and phosphorylation in intact cells

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