p105·IκBγ and Prototypical IκBs Use a Similar Mechanism to Bind but a Different Mechanism to Regulate the Subcellular Localization of NF-κB
Open Access
- 1 January 2003
- journal article
- Published by Elsevier
- Vol. 278 (1) , 556-566
- https://doi.org/10.1074/jbc.m207515200
Abstract
No abstract availableKeywords
This publication has 50 references indexed in Scilit:
- Processing of p105 Is Inhibited by Docking of p50 Active Subunits to the Ankyrin Repeat Domain, and Inhibition Is Alleviated by Signaling via the Carboxyl-terminal Phosphorylation/ Ubiquitin-Ligase Binding DomainPublished by Elsevier ,2001
- IκB Family Members Function by Different MechanismsJournal of Biological Chemistry, 2001
- Shared Pathways of IκB Kinase-Induced SCFβTrCP-Mediated Ubiquitination and Degradation for the NF-κB Precursor p105 and IκBαMolecular and Cellular Biology, 2001
- MAIL, a novel nuclear IκB protein that potentiates LPS‐induced IL‐6 productionFEBS Letters, 2000
- Mechanism of IκBα Binding to NF-κB DimersJournal of Biological Chemistry, 2000
- NF-κB AND REL PROTEINS: Evolutionarily Conserved Mediators of Immune ResponsesAnnual Review of Immunology, 1998
- I kappa B epsilon, a novel member of the Ikappa B family, controls RelA and cRel NF-kappa B activityThe EMBO Journal, 1997
- THE NF-κB AND IκB PROTEINS: New Discoveries and InsightsAnnual Review of Immunology, 1996
- p105 and p98 precursor proteins play an active role in NF-kappa B-mediated signal transduction.Genes & Development, 1993
- Related subunits of NF-κB map to two distinct loci associated with translocations in leukemia, NFKB1 and NFKB2Genomics, 1992