The Zinc Finger Domain of NEMO Is Selectively Required for NF-κB Activation by UV Radiation and Topoisomerase Inhibitors

No abstract is available for this paper.

• Publication year

  2002

• Venue

  Molecular and Cellular Biology

• Publication date

  2002-08-01

• Fields of study

  Biology, Medicine, Chemistry

• Identifiers
  DOI 10.1128/MCB.22.16.5813-5825.2002PMID 12138192PMCID PMC133970
• External record

  Open on Semantic Scholar

• Source metadata

  Semantic Scholar, PubMed

• No claims are published for this paper.

• No concepts are published for this paper.

• IkappaBbeta, but not IkappaBalpha, functions as a classical cytoplasmic inhibitor of NF-kappaB dimers by masking both NF-kappaB nuclear localization sequences in resting cells.

  2001cited by this paper
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  2001influential reference
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  2001cited by this paper
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• IκB Family Members Function by Different Mechanisms*

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  2001cited by this paper
• The IKK complex: an integrator of all signals that activate NF-κB?

  2000cited by this paper
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  2000cited by this paper
• NEMO/IKK gamma-deficient mice model incontinentia pigmenti.

  2000cited by this paper
• Complete lack of NF-kappaB activity in IKK1 and IKK2 double-deficient mice: additional defect in neurulation.

  2000cited by this paper
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  2000cited by this paper
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  2000influential reference
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  2000cited by this paper
• The IKK complex: an integrator of all signals that activate NF-kappaB?

  2000cited by this paper
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• Selective inhibition of NF-kappaB activation by a peptide that blocks the interaction of NEMO with the IkappaB kinase complex.

  2000cited by this paper
• IκBα and IκBα/NF-κB Complexes Are Retained in the Cytoplasm through Interaction with a Novel Partner, RasGAP SH3-binding Protein 2*

  2000cited by this paper
• A nuclear export signal in the N-terminal regulatory domain of IκBα controls cytoplasmic localization of inactive NF-κB/IκBα complexes

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• Selective inhibition of NF-κB activation by a peptide that blocks the interaction of NEMO with the IκB kinase complex

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  2000cited by this paper
• The SCFbeta-TRCP-ubiquitin ligase complex associates specifically with phosphorylated destruction motifs in IkappaBalpha and beta-catenin and stimulates IkappaBalpha ubiquitination in vitro.

  1999cited by this paper
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  1999cited by this paper
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  1999cited by this paper
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  1999cited by this paper
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  1999cited by this paper
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  1999cited by this paper
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  1999cited by this paper
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  1999cited by this paper
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  1999cited by this paper
• HOS, a human homolog of Slimb, forms an SCF complex with Skp1 and Cullin1 and targets the phosphorylation-dependent degradation of IκB and β-catenin

  1999cited by this paper
• IkappaBalpha ubiquitination is catalyzed by an SCF-like complex containing Skp1, cullin-1, and two F-box/WD40-repeat proteins, betaTrCP1 and betaTrCP2.

  1999cited by this paper
• Ubiquitin-dependent degradation of IkappaBalpha is mediated by a ubiquitin ligase Skp1/Cul 1/F-box protein FWD1.

  1999cited by this paper
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  1999cited by this paper
• Complementation Cloning of NEMO, a Component of the IκB Kinase Complex Essential for NF-κB Activation

  1998cited by this paper
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  1998cited by this paper
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  1998cited by this paper
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  1998cited by this paper
• Ionizing radiation and short wavelength UV activate NF-kappaB through two distinct mechanisms.

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  1998cited by this paper
• IKK-γ is an essential regulatory subunit of the IκB kinase complex

  1998cited by this paper
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  1997cited by this paper
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  1997cited by this paper
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  1994cited by this paper
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  2018influential citation
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