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Serdar E. Bulun

Researcher at Northwestern University

Publications -  269
Citations -  21374

Serdar E. Bulun is an academic researcher from Northwestern University. The author has contributed to research in topics: Aromatase & Estrogen. The author has an hindex of 81, co-authored 249 publications receiving 19379 citations. Previous affiliations of Serdar E. Bulun include University of Texas Southwestern Medical Center & Peking University.

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Aromatase Cytochrome P450, The Enzyme Responsible for Estrogen Biosynthesis*

TL;DR: The biosynthesis of estrogens appears to occur throughout the entire vertebrate phylum including mammals, birds, reptiles, amphibians, teleost and elasmobranch fish, and Agnatha, and in the protochordate Amphioxus.
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Estrogen production and action

TL;DR: There can be complex mechanisms that regulate the extraglandular production of estrogen in a tissue-specific and state-specific fashion, and local estrogen biosynthesis by aromatase activity in the brain may be important in the regulation of various cognitive and hypothalamic functions.
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Aromatase expression in endometriosis.

TL;DR: The presence of aromatase expression in eutopic endometrial tissues from patients with endometriosis may be related to the capability of implantation of these tissues on peritoneal surfaces and the possibility of estrogen production in these implants may serve to promote their growth.
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Regulation of Aromatase Expression in Estrogen-Responsive Breast and Uterine Disease: From Bench to Treatment

TL;DR: A single gene encodes the key enzyme for estrogen biosynthesis termed aromatase, inhibition of which effectively eliminates estrogen production, and its roles in breast cancer and endometriosis, whereas their roles in endometrial cancer, uterine fibroids, and aromatases excess syndrome are less clear.
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Progesterone Receptor Isoform A But Not B Is Expressed in Endometriosis

TL;DR: It is concluded that progesterone resistance in endometriotic tissue from laboratory and clinical observations may be accounted for by the presence of the inhibitory PR isoform PR-A and the absence of the stimulatory isoforms PR-B.