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John A. Katzenellenbogen

Researcher at University of Illinois at Urbana–Champaign

Publications -  705
Citations -  38548

John A. Katzenellenbogen is an academic researcher from University of Illinois at Urbana–Champaign. The author has contributed to research in topics: Estrogen receptor & Estrogen receptor alpha. The author has an hindex of 95, co-authored 691 publications receiving 36132 citations. Previous affiliations of John A. Katzenellenbogen include Virginia Tech & Harvard University.

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Nongenotropic, sex-nonspecific signaling through the estrogen or androgen receptors: dissociation from transcriptional activity.

TL;DR: A novel paradigm of sex steroid action on osteoblasts, osteocytes, embryonic fibroblasts, and HeLa cells involving activation of a Src/Shc/ERK signaling pathway and attenuating apoptosis is demonstrated, providing proof of principle for the development of function-specific-as opposed to tissue-selective-and gender-neutral pharmacotherapeutics.
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Phenol red in tissue culture media is a weak estrogen: implications concerning the study of estrogen-responsive cells in culture

TL;DR: Phenol red has been found to have significant estrogenic activity at the concentrations (15-45 microM) at which it is found in tissue culture media as mentioned in this paper, which has been shown to stimulate the proliferation of estrogen receptor-positive MCF-7 breast cancer cells in a dose-dependent manner.
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Pyrazole Ligands: Structure−Affinity/Activity Relationships and Estrogen Receptor-α-Selective Agonists

TL;DR: Investigations suggest that the pyrazole triols prefer to bind to ERalpha with their C(3)-phenol in the estradiol A-ring binding pocket and that binding selectivity results from differences in the interaction of thePyrazole core and C(4)-propyl group with portions of the receptor where ERalpha has a smaller residue than ERbeta.
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Estrogen receptor-beta potency-selective ligands: structure-activity relationship studies of diarylpropionitriles and their acetylene and polar analogues.

TL;DR: This study suggests that, in this series of ligands, the nitrile functionality is critical to ERbeta selectivity because it provides the optimal combination of linear geometry and polarity.
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The estradiol pharmacophore: Ligand structure-estrogen receptor binding affinity relationships and a model for the receptor binding site

TL;DR: The various elements in this model for the binding of steroidal estrogens by the estrogen receptor are consistent with evidence emerging from the crystal structures of related nuclear hormone receptor ligand complexes.