Phosphorylation of serine 212 confers novel activity to human estrogen receptor α
Abstract
Estrogen receptor α (ERα) can be phosphorylated at various residues, one of which is serine 212 in the DNA binding domain. The majority of human nuclear receptors conserves, as a motif, this serine residue within their DNA binding domain. Among these nuclear receptors, phosphorylation of the corresponding threonine 38 in the nuclear receptor CAR is essential for determining its activity [9]. Here, we have investigated the role of phosphorylated...
Paper Details
Title
Phosphorylation of serine 212 confers novel activity to human estrogen receptor α
Published Date
Apr 1, 2012
Journal
Volume
77
Issue
5
Pages
448 - 453
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