Regulation of SRC-3 (pCIP/ACTR/AIB-1/RAC-3/TRAM-1) Coactivator Activity by IκB Kinase
By R. Wu, J. Qin, Y. Hashimoto, J. Wong, Jianming Xu, S. Tsai, M. Tsai, B. O’Malley. Molecular and Cellular Biology, 2002
258 citations recorded by the source corpus.
Subfields: Cancer Research, Genetics, Oncology
View Paper: https://www.semanticscholar.org/paper/5f2d29c138e8fdf5bd3723dc1a694c4815007f6d
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Citations in the corpus
- Mechanisms of tamoxifen resistance. (2004, background): “These effects are most likely to be achieved by the phosphorylation of co-regulators, which may in turn effect their nuclear sublocalisation (Hong & Privalsky 2000, Wu et al. 2002).”
- IκB Kinase α-Mediated Derepression of SMRT Potentiates Acetylation of RelA/p65 by p300 (2006, background): “Unlike IKK , IKK has distinct functions as a nuclear kinase capable of phosphorylating SRC-3 (66), CBP (67), histone H3, and the SMRT corepressor (4, 5, 26, 67), events linked to transcriptional activation of both NF- B-regulated and non-NF- B-regulated gene targets (4, 5, 26, 47).”
- Coregulator function: a key to understanding tissue specificity of selective receptor modulators. (2004, background): “Moreover, SRC-3 is found as a complex with I B kinase (IKK), the kinase responsible for phosphorylation and subsequent degradation of I B and consequently the activation of nuclear factor- B (NF- B); IKK complexes can phosphorylate SRC-3 in vitro (222).”