(PDF) Inducible Phosphorylation of NF-κB P65 at Serine 468

Inducible Phosphorylation of NF-κB P65 at Serine 468 by T Cell Costimulation Is Mediated by IKKϵ

Journal of Biological Chemistry - United States

doi 10.1074/jbc.m508045200

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January 3, 2006

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American Society for Biochemistry & Molecular Biology (ASBMB)

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Amanote Research

Inducible Phosphorylation of NF-κB P65 at Serine 468 by T Cell Costimulation Is Mediated by IKKϵ

Journal of Biological Chemistry - United States

doi 10.1074/jbc.m508045200

Full Text

Abstract

Categories

Date

Authors

Publisher

Related search

Transient and Selective NF- B P65 Serine 536 Phosphorylation Induced by T Cell Costimulation Is Mediated by I B Kinase and Controls the Kinetics of P65 Nuclear Import

NF- B Activation Induced by T Cell Receptor/Cd28 Costimulation Is Mediated by Protein Kinase C-

Casein Kinase II-mediated Phosphorylation of NF-κB P65 Subunit Enhances Inducible Nitric-Oxide Synthase Gene Transcriptionin Vivo

Bruton's Tyrosine Kinase Is Involved in P65-Mediated Transactivation and Phosphorylation of P65 on Serine 536 During NFκB Activation by Lipopolysaccharide

AKIP1 Enhances NF-κB-dependent Gene Expression by Promoting the Nuclear Retention and Phosphorylation of P65

P53 Induces NF-κB Activation by an IκB Kinase-Independent Mechanism Involving Phosphorylation of P65 by Ribosomal S6 Kinase 1

Helicobacter Pylori- Induced Cell Death Is Counteracted by NF-κB-mediated Transcription of DARPP-32

TDP-43 Inhibits NF-κB Activity by Blocking P65 Nuclear Translocation

Corrigendum: Regulation of Naive T Cell Function by the NF-κB Pathway