Site-specific Phosphorylation of the p65 Protein Subunit Mediates Selective Gene Expression by Differential NF-κB and RNA Polymerase II Promoter Recruitment

Monoubiquitination of nuclear RelA negatively regulates NF-κB activity independent of proteasomal degradation

(2012) Karin Hochrainer et al.   CELLULAR AND MOLECULAR LIFE SCIENCES

Phosphorylation of p65(RelA) on Ser547 by ATM Represses NF-κB-Dependent Transcription of Specific Genes after Genotoxic Stress

(2012) Hélène Sabatel et al.   PLoS One

Posttranslational modifications of NF-κB: Another layer of regulation for NF-κB signaling pathway

(2010) Bo Huang et al.   CELLULAR SIGNALLING

Gene-Specific Repression of Proinflammatory Cytokines in Stimulated Human Macrophages by Nuclear I B 

(2010) C. C. Ghosh et al.   JOURNAL OF IMMUNOLOGY

Specification of the NF-κB transcriptional response by p65 phosphorylation and TNF-induced nuclear translocation of IKKε

(2010) Rita Moreno et al.   NUCLEIC ACIDS RESEARCH

Thr435phosphorylation regulates RelA (p65) NF-κB subunit transactivation

(2009) John M. O'Shea et al.   BIOCHEMICAL JOURNAL

Phosphorylation of NF-κB p65 at Ser468 controls its COMMD1-dependent ubiquitination and target gene-specific proteasomal elimination

(2009) Hui Geng et al.   EMBO REPORTS

Repression of gene expression by unphosphorylated NF- B p65 through epigenetic mechanisms

(2008) J. Dong et al.   GENES & DEVELOPMENT

RelA Ser276 Phosphorylation Is Required for Activation of a Subset of NF- B-Dependent Genes by Recruiting Cyclin-Dependent Kinase 9/Cyclin T1 Complexes

(2008) D. E. Nowak et al.   MOLECULAR AND CELLULAR BIOLOGY