Tumor necrosis factor-alpha-induced IKK phosphorylation of NF-kappaB p65 on serine 536 is mediated through the TRAF2, TRAF5, and TAK1 signaling pathway (Q24306909)

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

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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 (English)

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phosphorylation

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1 reference

based on heuristic

inferred from title

Hiroyasu Nakano

object named as

Hiroyasu Nakano

4

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Hiroaki Sakurai

object named as

Hiroaki Sakurai

1

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8

object named as

Ikuo Saiki

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author name string

Shunsuke Suzuki

2

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Noritaka Kawasaki

3

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Tatsuma Okazaki

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Atsushi Chino

6

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Takahiro Doi

7

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language of work or name

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publication date

19 September 2003

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Journal of Biological Chemistry

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278

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38

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36916-23

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Phosphorylation meets ubiquitination: the control of NF-[kappa]B activity

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NF-kappaB signaling pathways in mammalian and insect innate immunity

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Cyclooxygenase-selective inhibition of prostanoid formation: transducing biochemical selectivity into clinical read-outs

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Missing pieces in the NF-kappaB puzzle

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Mapping of the inducible IkappaB phosphorylation sites that signal its ubiquitination and degradation

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Role of IkappaBalpha ubiquitination in signal-induced activation of NFkappaB in vivo

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A cytokine-responsive IkappaB kinase that activates the transcription factor NF-kappaB

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IKK-1 and IKK-2: cytokine-activated IkappaB kinases essential for NF-kappaB activation

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The IkappaB kinase complex (IKK) contains two kinase subunits, IKKalpha and IKKbeta, necessary for IkappaB phosphorylation and NF-kappaB activation

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Control of IkappaBalpha proteolysis by the ubiquitin-proteasome pathway

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A novel family of putative signal transducers associated with the cytoplasmic domain of the 75 kDa tumor necrosis factor receptor

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TRAF5, an activator of NF-kappaB and putative signal transducer for the lymphotoxin-beta receptor

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Critical roles of TRAF2 and TRAF5 in tumor necrosis factor-induced NF-kappa B activation and protection from cell death

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Recruitment of the IKK signalosome to the p55 TNF receptor: RIP and A20 bind to NEMO (IKKgamma) upon receptor stimulation

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The death domain kinase RIP mediates the TNF-induced NF-kappaB signal

1 reference

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Complementation cloning of NEMO, a component of the IkappaB kinase complex essential for NF-kappaB activation

1 reference

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IkappaB kinase (IKK)-associated protein 1, a common component of the heterogeneous IKK complex

1 reference

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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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MEKK1 activates both IkappaB kinase alpha and IkappaB kinase beta

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Mitogen-activated protein kinase/ERK kinase kinases 2 and 3 activate nuclear factor-kappaB through IkappaB kinase-alpha and IkappaB kinase-beta

1 reference

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The essential role of MEKK3 in TNF-induced NF-kappaB activation

1 reference

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The kinase TAK1 can activate the NIK-I kappaB as well as the MAP kinase cascade in the IL-1 signalling pathway

1 reference

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21 January 2018

Functional interactions of transforming growth factor beta-activated kinase 1 with IkappaB kinases to stimulate NF-kappaB activation

1 reference

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Regulation of the transcriptional activity of the nuclear factor-kappaB p65 subunit.

1 reference

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Nf-kappa B, chemokine gene transcription and tumour growth

1 reference

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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

1 reference

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The phosphorylation status of nuclear NF-kappa B determines its association with CBP/p300 or HDAC-1

1 reference

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Akt stimulates the transactivation potential of the RelA/p65 Subunit of NF-kappa B through utilization of the Ikappa B kinase and activation of the mitogen-activated protein kinase p38.

1 reference

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The NF-kappa B activation in lymphotoxin beta receptor signaling depends on the phosphorylation of p65 at serine 536.

1 reference

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Phosphorylation of serine 276 is essential for p65 NF-kappaB subunit-dependent cellular responses

1 reference

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Activation of nuclear factor-kappaB-dependent transcription by tumor necrosis factor-alpha is mediated through phosphorylation of RelA/p65 on serine 529.

1 reference

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

1 reference

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Transcriptional activation of the NF-kappaB p65 subunit by mitogen- and stress-activated protein kinase-1 (MSK1)

1 reference

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Activation of phosphatidylinositol 3-kinase in response to interleukin-1 leads to phosphorylation and activation of the NF-kappaB p65/RelA subunit

1 reference

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

1 reference

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Distinct roles of the Ikappa B kinase alpha and beta subunits in liberating nuclear factor kappa B (NF-kappa B) from Ikappa B and in phosphorylating the p65 subunit of NF-kappa B.

1 reference

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PTEN blocks tumor necrosis factor-induced NF-kappa B-dependent transcription by inhibiting the transactivation potential of the p65 subunit

1 reference

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Requirement for glycogen synthase kinase-3beta in cell survival and NF-kappaB activation

1 reference

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Multiple signaling pathways mediate LIF-induced skeletal muscle satellite cell proliferation

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NF-kappa B RelA-deficient lymphocytes: normal development of T cells and B cells, impaired production of IgA and IgG1 and reduced proliferative responses

1 reference

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TAK1 is critical for IkappaB kinase-mediated activation of the NF-kappaB pathway

1 reference

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Duplexes of 21-nucleotide RNAs mediate RNA interference in cultured mammalian cells

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Phosphorylation-dependent activation of TAK1 mitogen-activated protein kinase kinase kinase by TAB1

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TGF-beta-activated kinase 1 stimulates NF-kappa B activation by an NF-kappa B-inducing kinase-independent mechanism

1 reference

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TAB2, a novel adaptor protein, mediates activation of TAK1 MAPKKK by linking TAK1 to TRAF6 in the IL-1 signal transduction pathway

1 reference

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Interleukin-1 (IL-1) receptor-associated kinase leads to activation of TAK1 by inducing TAB2 translocation in the IL-1 signaling pathway

1 reference

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IRAK-mediated translocation of TRAF6 and TAB2 in the interleukin-1-induced activation of NFkappa B

1 reference

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Receptor activator of NF-kappaB ligand (RANKL) activates TAK1 mitogen-activated protein kinase kinase kinase through a signaling complex containing RANK, TAB2, and TRAF6

1 reference

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Essential role of nuclear factor (NF)-kappaB-inducing kinase and inhibitor of kappaB (IkappaB) kinase alpha in NF-kappaB activation through lymphotoxin beta receptor, but not through tumor necrosis factor receptor I

1 reference

https://api.crossref.org/works/10.1074%2FJBC.M301598200

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The lymphotoxin-beta receptor induces different patterns of gene expression via two NF-kappaB pathways

1 reference

https://api.crossref.org/works/10.1074%2FJBC.M301598200

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Protein phosphatase 2A interacts with and directly dephosphorylates RelA

1 reference

https://api.crossref.org/works/10.1074%2FJBC.M301598200

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The tumor suppressor protein menin interacts with NF-kappaB proteins and inhibits NF-kappaB-mediated transactivation

1 reference

https://api.crossref.org/works/10.1074%2FJBC.M301598200

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The nuclear import of p53 is determined by the presence of a basic domain and its relative position to the nuclear localization signal

1 reference

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based on heuristic

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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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https://api.crossref.org/works/10.1074%2FJBC.M301598200

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based on heuristic

inferred from DOI database lookup

Activation of NF-kappa B by phosphatase inhibitors involves the phosphorylation of I kappa B alpha at phosphatase 2A-sensitive sites

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Novel inhibitors of cytokine-induced IkappaBalpha phosphorylation and endothelial cell adhesion molecule expression show anti-inflammatory effects in vivo

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Identifiers

10.1074/JBC.M301598200

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Consolidated OpenCitations Corpus – April 2017

OpenCitations bibliographic resource ID

OpenCitations bibliographic resource ID

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Consolidated OpenCitations Corpus – April 2017

OpenCitations bibliographic resource ID

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Consolidated OpenCitations Corpus – April 2017

OpenCitations bibliographic resource ID

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