Degradation of transcription factor IRF-1 by the ubiquitin-proteasome pathway. The C-terminal region governs the protein stability (Q42804594)

7 November 2017

title

Degradation of transcription factor IRF-1 by the ubiquitin-proteasome pathway. The C-terminal region governs the protein stability (English)

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ubiquitin-proteasome system

7 November 2017

main subject

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author name string

K Nakagawa

series ordinal

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7 November 2017

H Yokosawa

series ordinal

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7 November 2017

language of work or name

English

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publication date

1 March 2000

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7 November 2017

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7 November 2017

volume

267

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7 November 2017

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7 November 2017

page(s)

1680-1686

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Regulated expression of a gene encoding a nuclear factor, IRF-1, that specifically binds to IFN-β gene regulatory elements

7 November 2017

cites work

1 reference

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Induction of endogenous IFN-alpha and IFN-beta genes by a regulatory transcription factor, IRF-1.

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Induction of the transcription factor IRF-1 and interferon-beta mRNAs by cytokines and activators of second-messenger pathways

21 January 2018

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Activation of IFN-beta element by IRF-1 requires a posttranslational event in addition to IRF-1 synthesis

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Anti-oncogenic and oncogenic potentials of interferon regulatory factors-1 and -2

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Cellular commitment to oncogene-induced transformation or apoptosis is dependent on the transcription factor IRF-1.

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Absence of the type I IFN system in EC cells: transcriptional activator (IRF-1) and repressor (IRF-2) genes are developmentally regulated

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Ubiquitin-dependent c-Jun degradation in vivo is mediated by the delta domain

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Degradation of the proto-oncogene product c-Fos by the ubiquitin proteolytic system in vivo and in vitro: identification and characterization of the conjugating enzymes

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Interaction between ubiquitin-protein ligase SCFSKP2 and E2F-1 underlies the regulation of E2F-1 degradation

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Purification and cloning of interferon-stimulated gene factor 2 (ISGF2): ISGF2 (IRF-1) can bind to the promoters of both beta interferon- and interferon-stimulated genes but is not a primary transcriptional activator of either

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Cyclin is degraded by the ubiquitin pathway

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Degradation signal masking by heterodimerization of MATalpha2 and MATa1 blocks their mutual destruction by the ubiquitin-proteasome pathway

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Degradation signals for ubiquitin system proteolysis in Saccharomyces cerevisiae

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Oncoprotein MDM2 is a ubiquitin ligase E3 for tumor suppressor p53

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Oligomerization is required for p53 to be efficiently ubiquitinated by MDM2

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Mammalian Sug1 and c-Fos in the nuclear 26S proteasome

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Virus-dependent phosphorylation of the IRF-3 transcription factor regulates nuclear translocation, transactivation potential, and proteasome-mediated degradation

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An IRF-1-dependent pathway of DNA damage-induced apoptosis in mitogen-activated T lymphocytes

21 January 2018

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Cooperation of the tumour suppressors IRF-1 and p53 in response to DNA damage

21 January 2018

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10.1046/J.1432-1327.2000.01163.X

21 January 2018

Identifiers

DOI

1 reference

7 November 2017

1 reference