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 Domain
Open Access
- 1 July 2001
- journal article
- Published by Elsevier
- Vol. 276 (29), 26769-26776
- https://doi.org/10.1074/jbc.m102448200
Abstract
No abstract availableKeywords
This publication has 33 references indexed in Scilit:
- Ubiquitin-mediated proteolysis: biological regulation via destructionBioEssays, 2000
- Phosphorylation Meets Ubiquitination: The Control of NF-κB ActivityAnnual Review of Immunology, 2000
- SCF and Cullin/RING H2-Based Ubiquitin LigasesAnnual Review of Cell and Developmental Biology, 1999
- NF-κB to the rescue: RELs, apoptosis and cellular transformationTrends in Genetics, 1999
- The 26S Proteasome: A Molecular Machine Designed for Controlled ProteolysisAnnual Review of Biochemistry, 1999
- Cotranslational Biogenesis of NF-κB p50 by the 26S ProteasomeCell, 1998
- A Glycine-Rich Region in NF-κB p105 Functions as a Processing Signal for the Generation of the p50 SubunitMolecular and Cellular Biology, 1996
- Ubiquitin-mediated Processing of NF-κB Transcriptional Activator Precursor p105Journal of Biological Chemistry, 1995
- The ubiquitinproteasome pathway is required for processing the NF-κB1 precursor protein and the activation of NF-κBCell, 1994
- Generation of p50 subunit of NF-kB by processing of p105 through an ATP-dependent pathwayNature, 1991