(Q44664679)

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Site-specific fluorescent labeling of estrogen receptors and structure-activity relationships of ligands in terms of receptor dimer stability

scientific article published in January 2003

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scholarly article

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Europe PubMed Central

PubMed publication ID

5 December 2017

Site-specific fluorescent labeling of estrogen receptors and structure-activity relationships of ligands in terms of receptor dimer stability (English)

1 reference

Europe PubMed Central

PubMed publication ID

5 December 2017

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Anobel Tamrazi

1

1 reference

Europe PubMed Central

PubMed publication ID

5 December 2017

John A Katzenellenbogen

2

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Europe PubMed Central

PubMed publication ID

5 December 2017

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publication date

1 January 2003

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Europe PubMed Central

PubMed publication ID

5 December 2017

Methods in Enzymology

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Europe PubMed Central

PubMed publication ID

5 December 2017

364

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Europe PubMed Central

PubMed publication ID

5 December 2017

37-53

1 reference

Europe PubMed Central

PubMed publication ID

5 December 2017

Connections and regulation of the human estrogen receptor

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Estrogens in the causation of breast, endometrial and ovarian cancers - evidence and hypotheses from epidemiological findings

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Selective estrogen receptor modulators: clinical spectrum

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Molecular determinants for the tissue specificity of SERMs

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The green fluorescent protein

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Use of homogeneous time-resolved fluorescence energy transfer in the measurement of nuclear receptor activation

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Mutational analysis of cysteine residues within the hormone-binding domain of the human estrogen receptor identifies mutants that are defective in both DNA-binding and subcellular distribution

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Estrogen receptor dimerization: ligand binding regulates dimer affinity and dimer dissociation rate

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Altered Ligand Binding Properties and Enhanced Stability of a Constitutively Active Estrogen Receptor: Evidence That an Open Pocket Conformation Is Required for Ligand Interaction

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Fluorescence resonance energy transfer

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The renaissance of fluorescence resonance energy transfer

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The nuclear receptor superfamily: the second decade

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Nuclear receptor minireview series

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The human estrogen receptor hormone binding domain dimerizes independently of ligand activation

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Yeast two-hybrid system demonstrates that estrogen receptor dimerization is ligand-dependent in vivo.

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11 beta-chloromethyl-[3H]estradiol-17 beta: a very high affinity, reversible ligand for the estrogen receptor

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Identifiers

10.1016/S0076-6879(03)64003-6

1 reference

Europe PubMed Central

PubMed publication ID

5 December 2017

PubMed publication ID

1 reference

Europe PubMed Central

PubMed publication ID

5 December 2017

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