Negative regulation of NF-κB p65 activity by serine 536 phosphorylation-Reference-Cited by-同舟云学术

Negative regulation of NF-κB p65 activity by serine 536 phosphorylation

Published:2016-08-23 Issue:442 Volume:9 Page:
ISSN:1945-0877
Container-title:Science Signaling
language:en
Short-container-title:Sci. Signal.

Author:

Pradère Jean-Philippe¹,Hernandez Céline¹,Koppe Christiane²,Friedman Richard A.³,Luedde Tom²,Schwabe Robert F.¹

Affiliation:

1. Department of Medicine, Columbia University, New York, NY 10032, USA.

2. Department of Medicine III, University Hospital RWTH Aachen, 52074 Aachen, Germany.

3. Biomedical Informatics Shared Resource, Herbert Irving Comprehensive Cancer Center and Department of Biomedical Informatics, Columbia University, New York, NY 10032, USA.

Abstract

The kinase IKK fine-tunes inflammation by both activating and inhibiting signaling by the p65 subunit of NF-κB.

Funder

NIH

Fondation pour la Recherche Medicale

Publisher

American Association for the Advancement of Science (AAAS)

Subject

Cell Biology,Molecular Biology,Biochemistry

Reference42 articles.

1. Activators and target genes of Rel/NF-κB transcription factors

2. Phosphorylation Meets Ubiquitination: The Control of NF-κB Activity

3. IKK biology

4. IκB Kinase (IKK)-Associated Protein 1, a Common Component of the Heterogeneous IKK Complex

5. Identification of an oncoprotein- and UV-responsive protein kinase that binds and potentiates the c-Jun activation domain.

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