A novel NF-kappaB pathway involving IKKbeta and p65/RelA Ser-536 phosphorylation results in p53 Inhibition in the absence of NF-kappaB transcriptional activity. (Q40478659)

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English	A novel NF-kappaB pathway involving IKKbeta and p65/RelA Ser-536 phosphorylation results in p53 Inhibition in the absence of NF-kappaB transcriptional activity.	scientific article

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scholarly article

1 reference

Europe PubMed Central

20 September 2017

A novel NF-kappaB pathway involving IKKbeta and p65/RelA Ser-536 phosphorylation results in p53 Inhibition in the absence of NF-kappaB transcriptional activity. (English)

1 reference

Europe PubMed Central

20 September 2017

phosphorylation

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author name string

Soo-Jin Jeong

1

1 reference

Europe PubMed Central

20 September 2017

Cynthia A Pise-Masison

2

1 reference

Europe PubMed Central

20 September 2017

Michael F Radonovich

3

1 reference

Europe PubMed Central

20 September 2017

Hyeon Ung Park

4

1 reference

Europe PubMed Central

20 September 2017

John N Brady

5

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Europe PubMed Central

20 September 2017

language of work or name

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publication date

20 December 2004

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Europe PubMed Central

20 September 2017

Journal of Biological Chemistry

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Europe PubMed Central

20 September 2017

280

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Europe PubMed Central

20 September 2017

11

1 reference

Europe PubMed Central

20 September 2017

10326-10332

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Europe PubMed Central

20 September 2017

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Akt suppresses apoptosis by stimulating the transactivation potential of the RelA/p65 subunit of NF-kappaB.

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

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Tumor necrosis factor alpha-induced phosphorylation of RelA/p65 on Ser529 is controlled by casein kinase II

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Inactivation of p53 by human T-cell lymphotropic virus type 1 Tax requires activation of the NF-kappaB pathway and is dependent on p53 phosphorylation.

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The human T-cell leukemia virus type-1 Tax protein regulates the activity of the IkappaB kinase complex

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Human T-cell lymphotropic virus type 1 tax induction of biologically Active NF-kappaB requires IkappaB kinase-1-mediated phosphorylation of RelA/p65.

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Positive and negative regulation of IkappaB kinase activity through IKKbeta subunit phosphorylation

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IKK beta plays an essential role in the phosphorylation of RelA/p65 on serine 536 induced by lipopolysaccharide

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IKK beta and phosphatidylinositol 3-kinase/Akt participate in non-pathogenic Gram-negative enteric bacteria-induced RelA phosphorylation and NF-kappa B activation in both primary and intestinal epithelial cell lines

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Tax-independent constitutive IkappaB kinase activation in adult T-cell leukemia cells

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Tumor necrosis factor-alpha-induced IKK phosphorylation of NF-kappaB p65 on serine 536 is mediated through the TRAF2, TRAF5, and TAK1 signaling pathway

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HTLV-I Tax protein binds to MEKK1 to stimulate IkappaB kinase activity and NF-kappaB activation.

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MAP3K-related kinase involved in NF-kappaB induction by TNF, CD95 and IL-1

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NF-kappaB-inducing kinase activates IKK-alpha by phosphorylation of Ser-176

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Differential regulation of IkappaB kinase alpha and beta by two upstream kinases, NF-kappaB-inducing kinase and mitogen-activated protein kinase/ERK kinase kinase-1

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NF-kappaB activation by tumour necrosis factor requires the Akt serine-threonine kinase

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Acetylation of RelA at discrete sites regulates distinct nuclear functions of NF-kappaB.

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Post-activation turn-off of NF-kappa B-dependent transcription is regulated by acetylation of p65

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10.1074/JBC.M412643200

1 reference

Europe PubMed Central

20 September 2017

1 reference

Europe PubMed Central

20 September 2017

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