Abstract
The NF-κB transcription factor complex plays a role in directing the inducible expression of a number of genes involved in the immune response, importantly including c-myc [1]. NF-κB consists of homo- or hetero-dimers drawn from a family of proteins, the members of which share a conserved 300 amino acid sequence, the Rel homology domain, originally identified as the transforming agent of the avian reticuloendotheliosis virus. Mammahan Rel-related proteins include NF-κB 1 (p50), NF-κB2 (p52), c-Rel, RelA (p65), and RelB. NF-κB 1 and NF-κB2 are derived from larger precursor proteins (pl05 and p 100, respectively) that can inhibit NF-κB. c-Rel, RelA and RelB contain transactivation domains at their carboxyl terminal ends that are capable of activating gene transcription. Transcriptionally active dimers are those in which one of the proteins contains a transactivation domain (for review see [2–4]).
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© 1997 Springer-Verlag Berlin Heidelberg
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Francis, D.A., Sen, R., Rothstein, T.L. (1997). Receptor-specific Regulation of NF-κB, c-Myc and Fas-mediated Apoptosis in Primary B Cells. In: Potter, M., Melchers, F. (eds) C-Myc in B-Cell Neoplasia. Current Topics in Microbiology and Immunology, vol 224. Springer, Berlin, Heidelberg. https://doi.org/10.1007/978-3-642-60801-8_8
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DOI: https://doi.org/10.1007/978-3-642-60801-8_8
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