Tyrosine phosphorylation of I kappa B-alpha activates NF-kappa B without proteolytic degradation of I kappa B-alpha (Q71513462)

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19 October 2019

title

Tyrosine phosphorylation of I kappa B-alpha activates NF-kappa B without proteolytic degradation of I kappa B-alpha (English)

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19 October 2019

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1

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19 October 2019

Patrick Auberger

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19 October 2019

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P A Baeuerle

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19 October 2019

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H L Pahl

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19 October 2019

author name string

R A Rupec

2

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19 October 2019

A Livolsi

3

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19 October 2019

E B Traenckner

5

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19 October 2019

C Mueller-Dieckmann

6

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19 October 2019

D Farahifar

7

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19 October 2019

B Rossi

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19 October 2019

J F Peyron

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19 October 2019

language of work or name

English

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publication date

1 September 1996

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19 October 2019

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19 October 2019

volume

86

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19 October 2019

issue

5

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19 October 2019

page(s)

787-798

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In vivo stimulation of I kappa B phosphorylation is not sufficient to activate NF-kappa B

19 October 2019

cites work

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7 January 2021

I kappa B: a specific inhibitor of the NF-kappa B transcription factor

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7 January 2021

Function and activation of NF-kappa B in the immune system

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Constitutive phosphorylation of I kappa B alpha by casein kinase II

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The I kappa B proteins: multifunctional regulators of Rel/NF-kappa B transcription factors

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I kappa B interacts with the nuclear localization sequences of the subunits of NF-kappa B: a mechanism for cytoplasmic retention

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7 January 2021

Coupling of a signal response domain in I kappa B alpha to multiple pathways for NF-kappa B activation

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7 January 2021

Control of I kappa B-alpha proteolysis by site-specific, signal-induced phosphorylation

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Oncogenes and signal transduction

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Jak-STAT pathways and transcriptional activation in response to IFNs and other extracellular signaling proteins

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Rel-associated pp40: an inhibitor of the rel family of transcription factors

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Phosphorylation of I kappa B alpha precedes but is not sufficient for its dissociation from NF-kappa B

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7 January 2021

Inducible phosphorylation of I kappa B alpha is not sufficient for its dissociation from NF-kappa B and is inhibited by protease inhibitors

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7 January 2021

Activation in vitro of NF-kappa B by phosphorylation of its inhibitor I kappa B

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The inducible transcription factor NF-kappa B: structure-function relationship of its protein subunits

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

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The insulinomimetic agents H2O2 and vanadate stimulate tyrosine phosphorylation of potential target proteins for the insulin receptor kinase in intact cells

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7 January 2021

Rapid proteolysis of I kappa B-alpha is necessary for activation of transcription factor NF-kappa B

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7 January 2021

Transcriptional regulation by extracellular signals: mechanisms and specificity

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Induction of tyrosine phosphorylation and T-cell activation by vanadate peroxide, an inhibitor of protein tyrosine phosphatases

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Signal transduction from the cell surface to the nucleus through the phosphorylation of transcription factors

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The rel-associated pp40 protein prevents DNA binding of Rel and NF-kappa B: relationship with I kappa B beta and regulation by phosphorylation

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The v-abl tyrosine kinase negatively regulates NF-kappa B/Rel factors and blocks kappa gene transcription in pre-B lymphocytes

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7 January 2021

Activation of NF-kappa B requires proteolysis of the inhibitor I kappa B-alpha: signal-induced phosphorylation of I kappa B-alpha alone does not release active NF-kappa B

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7 January 2021

Regulation of the NF-kappa B/rel transcription factor and I kappa B inhibitor system

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7 January 2021

Tumor necrosis factor alpha-induced phosphorylation of I kappa B alpha is a signal for its degradation but not dissociation from NF-kappa B

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7 January 2021

The ubiquitin-proteasome pathway is required for processing the NF-kappa B1 precursor protein and the activation of NF-kappa B

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Phosphorylation of human I kappa B-alpha on serines 32 and 36 controls I kappa B-alpha proteolysis and NF-kappa B activation in response to diverse stimuli

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Identifiers

DOI

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19 October 2019

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