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Journal ArticleDOI

Estrogen receptor phosphorylation

Deborah A. Lannigan
- 01 Jan 2003 - 
- Vol. 68, Iss: 1, pp 1-9
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TLDR
This review presents evidence that these phosphorylations occur, and identifies the kinases thought to be responsible, and the functional importance of ERalpha phosphorylation is discussed.
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This article is published in Steroids.The article was published on 2003-01-01. It has received 471 citations till now. The article focuses on the topics: Protein phosphorylation & Phosphorylation cascade.

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Journal ArticleDOI

Estrogen receptor interaction with estrogen response elements.

TL;DR: Review of data from the own laboratory and those in the literature indicate that ERalpha binding affinity does not relate linearly with E(2)-induced transcriptional activation, and it is suggested that the reasons for this discord include cellular amounts of coactivators and adaptor proteins that play roles both in ER binding and transcriptionalactivation; phosphorylation of ER and other proteins involved in transcriptional activated; and sequence-specific and protein-induced alterations in chromatin architecture.
Journal ArticleDOI

Coregulator Function: A Key to Understanding Tissue Specificity of Selective Receptor Modulators

TL;DR: Increased understanding of the effect of cellular environment on nuclear receptors and their coregulators has the potential to open the field of SRM discovery and research to many members of the nuclear receptor superfamily.
Journal ArticleDOI

Estrogen signaling multiple pathways to impact gene transcription.

TL;DR: This review will focus on the recent knowledge about the mechanism by which ERs regulate the expression of target genes and the emerging field of integration of membrane and nuclear receptor signaling, giving examples of the ways by which the genomic and non-genomic actions of ERs on target genes converge.
Journal ArticleDOI

Structure–function relationship of estrogen receptor α and β: Impact on human health

TL;DR: Understanding the structural basis and the molecular mechanisms by which ER transduce E2 signals in target cells will allow to create new pharmacologic therapies aimed at the treatment of a variety of human diseases affecting the cardiovascular system, the reproductive system, and the skeletal system.
Journal ArticleDOI

Genomic targets of nuclear estrogen receptors.

TL;DR: Analysis of estrogen response sequences in mammalian target genes supports the view that specific, hormone-driven gene expression programs can result from the interplay of environmental and cellular cues with the distinct types of estrogen-response sequences.
References
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Journal ArticleDOI

Specificity of receptor tyrosine kinase signaling: Transient versus sustained extracellular signal-regulated kinase activation

Christopher J. Marshall
- 27 Jan 1995 - 
TL;DR: Experiments with PC12 cells suggest that the duration of ERK activation is critical for cell signaling decisions, and the extracellular signal-regulated kinase (ERK-regulated) MAPK pathway may be sufficient for these cellular responses.
Journal ArticleDOI

Specificity and mechanism of action of some commonly used protein kinase inhibitors

TL;DR: The results demonstrate that the specificities of protein kinase inhibitors cannot be assessed simply by studying their effect on kinases that are closely related in primary structure, and proposes guidelines for the use of protein Kinase inhibitors in cell-based assays.
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Interaction of estrogenic chemicals and phytoestrogens with estrogen receptor beta.

TL;DR: The estrogenic activity of environmental chemicals and phytoestrogens in competition binding assays with ERα or ERβ protein, and in a transient gene expression assay using cells in which an acute estrogenic response is created by cotransfecting cultures with recombinant human ERβ complementary DNA (cDNA) in the presence of an estrogen-dependent reporter plasmid are investigated.
Journal ArticleDOI

Molecular basis of agonism and antagonism in the oestrogen receptor.

TL;DR: The crystal structures of the LBD of ER in complex with the endogenous oestrogen, 17β-oestradiol, and the selective antagonist raloxifene provide a molecular basis for the distinctive pharmacophore of the ER and its catholic binding properties.
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