Control of NF-kappa B activity by the I kappa B beta inhibitor (Q41069858)

26 September 2017

title

Control of NF-kappa B activity by the I kappa B beta inhibitor (English)

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26 September 2017

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R Weil

1

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26 September 2017

S T Whiteside

series ordinal

2

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26 September 2017

A Israël

series ordinal

3

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26 September 2017

publication date

1 December 1997

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26 September 2017

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26 September 2017

volume

198

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26 September 2017

issue

1-3

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26 September 2017

page(s)

14-23

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

26 September 2017

cites work

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N- and C-terminal sequences control degradation of MAD3/I kappa B alpha in response to inducers of NF-kappa B activity

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

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A role for phosphorylation and degradation in the control of NF-κB activity

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The precursor of NF-κB p50 has IκB-like functions

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p105 and p98 precursor proteins play an active role in NF-kappa B-mediated signal transduction

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NF-kappa B p100 (Lyt-10) is a component of H2TF1 and can function as an I kappa B-like molecule

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NF-kappa B p100 is one of the high-molecular-weight proteins complexed with the v-Rel oncoprotein in transformed chicken spleen cells.

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IκBγ, a 70 kd protein identical to the C-terminal half of p110 NF-κB: A new member of the IκB family

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

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NF-kappa B: a family of inducible and differentially expressed enhancer-binding proteins in human T cells

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

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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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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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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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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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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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A proteasome inhibitor prevents activation of NF-kappa B and stabilizes a newly phosphorylated form of I kappa B-alpha that is still bound to NF-kappa B

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

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

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Inducible degradation of I kappa B alpha in vitro and in vivo requires the acidic C-terminal domain of the protein

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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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7 January 2021

Both amino- and carboxyl-terminal sequences within I kappa B alpha regulate its inducible degradation

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7 January 2021

Signal-induced site-specific phosphorylation targets I kappa B alpha to the ubiquitin-proteasome pathway

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Critical role for lysines 21 and 22 in signal-induced, ubiquitin-mediated proteolysis of I kappa B-alpha

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Signal-induced degradation of I(kappa)B(alpha): association with NF-kappaB and the PEST sequence in I(kappa)B(alpha) are not required

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7 January 2021

Role of unphosphorylated, newly synthesized I kappa B beta in persistent activation of NF-kappa B

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Mutual regulation of the transcriptional activator NF-kappa B and its inhibitor, I kappa B-alpha

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Tumor necrosis factor and interleukin-1 lead to phosphorylation and loss of I kappa B alpha: a mechanism for NF-kappa B activation

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

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Inactivation of IkappaBbeta by the tax protein of human T-cell leukemia virus type 1: a potential mechanism for constitutive induction of NF-kappaB

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7 January 2021

The HPV-16 E6 and E6-AP complex functions as a ubiquitin-protein ligase in the ubiquitination of p53

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The E6 oncoprotein encoded by human papillomavirus types 16 and 18 promotes the degradation of p53

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Primary structures of two homologous subunits of PA28, a gamma-interferon-inducible protein activator of the 20S proteasome

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7 January 2021

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Identifiers

DOI

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