Control of IκB-α Proteolysis by Site-Specific, Signal-Induced Phosphorylation
Author:
Affiliation:
1. Laboratory of Immunoregulation, National Institute of Allergy and Infectious Diseases, National Institutes of Health, Bethesda, MD 20892-1876.
Publisher
American Association for the Advancement of Science (AAAS)
Subject
Multidisciplinary
Reference19 articles.
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2. BOURS, V, THE ONCOPROTEIN BCL-3 DIRECTLY TRANSACTIVATES THROUGH KAPPA-B MOTIFS VIA ASSOCIATION WITH DNA-BINDING P50B HOMODIMERS, CELL 72: 729 (1993).
3. BOURS, V, A NOVEL MITOGEN-INDUCIBLE GENE-PRODUCT RELATED TO P50/P105-NF-KAPPA-B PARTICIPATES IN TRANSACTIVATION THROUGH A KAPPA-B SITE, MOLECULAR AND CELLULAR BIOLOGY 12: 685 (1992).
4. BRESSLER, P, MUTATIONAL ANALYSIS OF THE P50-SUBUNIT OF NF-KAPPA-B AND INHIBITION OF NF-KAPPA-B ACTIVITY BY TRANSDOMINANT P50 MUTANTS, JOURNAL OF VIROLOGY 67: 288 (1993).
5. BROWN, K, MUTUAL REGULATION OF THE TRANSCRIPTIONAL ACTIVATOR NF-KAPPA-B AND ITS INHIBITOR, I-KAPPA-B-ALPHA, PROCEEDINGS OF THE NATIONAL ACADEMY OF SCIENCES OF THE UNITED STATES OF AMERICA 90: 2532 (1993).
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