NF-κB p65 (RelA) homodimer uses distinct mechanisms to recognize DNA targets
- 1 April 2000
- Vol. 8 (4) , 419-428
- https://doi.org/10.1016/s0969-2126(00)00123-4
Abstract
No abstract availableKeywords
This publication has 29 references indexed in Scilit:
- Crystal Structure of a Tyrosine Phosphorylated STAT-1 Dimer Bound to DNAPublished by Elsevier ,1998
- JAKS AND STATS: Biological ImplicationsAnnual Review of Immunology, 1998
- NF-κB AND REL PROTEINS: Evolutionarily Conserved Mediators of Immune ResponsesAnnual Review of Immunology, 1998
- Structure of the DNA-binding domains from NFAT, Fos and Jun bound specifically to DNANature, 1998
- A novel DNA recognition mode by the NF-κB p65 homodimerNature Structural & Molecular Biology, 1998
- Structure of the human NF-kappa B p52 homodimer-DNA complex at 2.1AresolutionThe EMBO Journal, 1997
- TRANSCRIPTION FACTORS OF THE NFAT FAMILY:Regulation and FunctionAnnual Review of Immunology, 1997
- THE NF-κB AND IκB PROTEINS: New Discoveries and InsightsAnnual Review of Immunology, 1996
- Structure of the NF-κB p50 homodimer bound to DNANature, 1995
- Structure of NF-κB p50 homodimer bound to a κB siteNature, 1995