Protein expression pattern of human MIER1 alpha, a novel estrogen receptor binding protein

Expression and Distribution of Calcium-Binding Protein S100P in Human Placenta during Pregnancy

Ethanol and Cancer Induce Similar Changes on Protein Expression Pattern of Human Fibroblast Cell

Abstract Ethanol has a vast consumption around the world. Many researches confirmed some adverse effect of this component on human health. In addition, recent studies showed significant alteration in both cellular population, and protein profile of human foreskin fibroblast cell line (HFFF2) in the specific dosage of ethanol. Here, the role and interaction of some proteins (characterized by sig...

Ethanol and Cancer Induce Similar Changes on Protein Expression Pattern of Human Fibroblast Cell

Abstract Ethanol has a vast consumption around the world. Many researches confirmed some adverse effect of this component on human health. In addition, recent studies showed significant alteration in both cellular population, and protein profile of human foreskin fibroblast cell line (HFFF2) in the specific dosage of ethanol. Here, the role and interaction of some proteins (characterized by sig...

MICoA, a Novel MTA 1 Interacting Protein Coactivator, Regulates Estrogen Receptor-alpha Transactivation Functions*

The transcriptional activity of estrogen receptor-alpha (ER) is modified by coactivators, corepressors and chromatin remodeling complexes. We have previously shown that the metastasis-associated protein-1 (MTA1), a component of histone deacetylase and nucleosome remodeling complexes, represses ER-driven transcription by recruiting histone deacetylases (HDACs) to the estrogen receptor element (E...

Phosphorylation of human estrogen receptor alpha by protein kinase A regulates dimerization.

Phosphorylation provides an important mechanism by which transcription factor activity is regulated. Estrogen receptor alpha (ERalpha) is phosphorylated on multiple sites, and stimulation of a number of growth factor receptors and/or protein kinases leads to ligand-independent and/or synergistic increase in transcriptional activation by ERalpha in the presence of estrogen. Here we show that ERa...