The ability of NR LBDs to transfer repression function to a heterologous DNA binding
domain, and the cross-squelching of repression by untethered LBDs, has suggested that
repression is mediated by interactions with putative cellular corepressor proteins. The
yeast-two hybrid screen for protein interactors has proven to be the key to the isolation
and characterization of corepressors. This short review will focus on N-CoR and SMRT.
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