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Stimulation-dependent I kappa B alpha phosphorylation marks the NF-kappa B inhibitor for degradation via the ubiquitin-proteasome pathway
scientific journal article
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scholarly article
1 reference
stated in
PubMed
PubMed ID
7479848
retrieved
3 February 2017
title
Stimulation-dependent I kappa B alpha phosphorylation marks the NF-kappa B inhibitor for degradation via the ubiquitin-proteasome pathway
(English)
1 reference
stated in
PubMed
PubMed ID
7479848
retrieved
3 February 2017
main subject
ubiquitin-proteasome system
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NF-κB
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phosphorylation
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author name string
I. Alkalay
series ordinal
1
1 reference
stated in
PubMed
PubMed ID
7479848
retrieved
3 February 2017
A. Yaron
series ordinal
2
1 reference
stated in
PubMed
PubMed ID
7479848
retrieved
3 February 2017
A. Hatzubai
series ordinal
3
1 reference
stated in
PubMed
PubMed ID
7479848
retrieved
3 February 2017
A. Orian
series ordinal
4
1 reference
stated in
PubMed
PubMed ID
7479848
retrieved
3 February 2017
A. Ciechanover
series ordinal
5
1 reference
stated in
PubMed
PubMed ID
7479848
retrieved
3 February 2017
Y. Ben-Neriah
series ordinal
6
1 reference
stated in
PubMed
PubMed ID
7479848
retrieved
3 February 2017
language of work or name
English
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publication date
7 November 1995
1 reference
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PubMed
PubMed ID
7479848
retrieved
3 February 2017
published in
Proceedings of the National Academy of Sciences of the United States of America
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stated in
PubMed
PubMed ID
7479848
retrieved
3 February 2017
volume
92
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stated in
PubMed
PubMed ID
7479848
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3 February 2017
page(s)
10599–10603
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PubMed
PubMed ID
7479848
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3 February 2017
issue
23
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stated in
PubMed
PubMed ID
7479848
retrieved
3 February 2017
cites work
The HPV-16 E6 and E6-AP complex functions as a ubiquitin-protein ligase in the ubiquitination of p53
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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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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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Phosphorylation of I kappa B alpha precedes but is not sufficient for its dissociation from NF-kappa B
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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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Coupling of a signal response domain in I kappa B alpha to multiple pathways for NF-kappa B activation
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I kappa B: a specific inhibitor of the NF-kappa B transcription factor
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In vivo degradation of a transcriptional regulator: the yeast alpha 2 repressor
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Cyclin is degraded by the ubiquitin pathway
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Control of I kappa B-alpha proteolysis by site-specific, signal-induced phosphorylation
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Rapid proteolysis of I kappa B-alpha is necessary for activation of transcription factor 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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The ubiquitin-proteasome proteolytic pathway
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Structure, regulation and function of NF-kappa B
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7 April 2017
NF-kappa B: a lesson in family values
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7 April 2017
Inducibility of kappa immunoglobulin enhancer-binding protein Nf-kappa B by a posttranslational mechanism
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Characterization of an immediate-early gene induced in adherent monocytes that encodes IκB-like activity
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Cell surface control of the multiubiquitination and deubiquitination of high-affinity immunoglobulin E receptors
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Human T-cell leukemia virus type I Tax activation of NF-kappa B/Rel involves phosphorylation and degradation of I kappa B alpha and RelA (p65)-mediated induction of the c-rel gene
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Ligand-dependent polyubiquitination of c-kit gene product: a possible mechanism of receptor down modulation in M07e cells
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A Chinese hamster cell cycle mutant arrested at G2 phase has a temperature-sensitive ubiquitin-activating enzyme, E1.
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Both cyclin A delta 60 and B delta 97 are stable and arrest cells in M-phase, but only cyclin B delta 97 turns on cyclin destruction
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Methylated ubiquitin inhibits cyclin degradation in clam embryo extracts
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NF-kappa B and related proteins: Rel/dorsal homologies meet ankyrin-like repeats
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The N-end rule
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Comparison of the effect of calpain inhibitors on two extralysosomal proteinases: the multicatalytic proteinase complex and m-calpain.
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Ligand-induced polyubiquitination of the platelet-derived growth factor beta-receptor
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Activation-dependent ubiquitination of a T cell antigen receptor subunit on multiple intracellular lysines
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Immunochemical analysis of the turnover of ubiquitin-protein conjugates in intact cells. Relationship to the breakdown of abnormal proteins
1 reference
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reference URL
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based on heuristic
inferred from PubMed ID database lookup
Identifiers
DOI
10.1073/PNAS.92.23.10599
1 reference
stated in
Consolidated OpenCitations Corpus – April 2017
OpenCitations bibliographic resource ID
1677967
ADS bibcode
1995PNAS...9210599A
0 references
OpenCitations bibliographic resource ID
1677967
1 reference
stated in
Consolidated OpenCitations Corpus – April 2017
OpenCitations bibliographic resource ID
1677967
PMCID
40659
1 reference
stated in
Consolidated OpenCitations Corpus – April 2017
OpenCitations bibliographic resource ID
1677967
PubMed ID
7479848
1 reference
stated in
Consolidated OpenCitations Corpus – April 2017
OpenCitations bibliographic resource ID
1677967
ResearchGate publication ID
15718949
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