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Karen E. Chapman

Researcher at University of Edinburgh

Publications -  161
Citations -  9896

Karen E. Chapman is an academic researcher from University of Edinburgh. The author has contributed to research in topics: Glucocorticoid & Glucocorticoid receptor. The author has an hindex of 51, co-authored 158 publications receiving 8992 citations. Previous affiliations of Karen E. Chapman include Royal Edinburgh Hospital & University of Newcastle.

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The anti-inflammatory and immunosuppressive effects of glucocorticoids, recent developments and mechanistic insights

TL;DR: A greater understanding is required of the mechanisms by which glucocorticoids exert their anti-inflammatory and immunosuppressive actions, and recent research is shedding new light on some of these mechanisms and has produced some surprising new findings.
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11β-Hydroxysteroid Dehydrogenases: Intracellular Gate-Keepers of Tissue Glucocorticoid Action

TL;DR: The 11β-HSDDs illuminate the emerging biology of intracrine control, afford important insights into human pathogenesis, and offer new tissue-restricted therapeutic avenues.
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Identification of new susceptibility loci for osteoarthritis (arcOGEN): A genome-wide association study

TL;DR: One of the signals close to genome-wide significance was within the FTO gene, which is involved in regulation of bodyweight—a strong risk factor for osteoarthritis.
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11 beta-hydroxysteroid dehydrogenase is an exclusive 11 beta- reductase in primary cultures of rat hepatocytes: effect of physicochemical and hormonal manipulations

TL;DR: Conditions for primary culture of adult rat hepatocytes that maintain high 11 beta HSR-1 messenger RNA expression are defined, which will allow investigation of the control of 11 beta-reductase activity and its implications for glucocorticoid-regulated hepatic functions.
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Human placental 11 beta-hydroxysteroid dehydrogenase: evidence for and partial purification of a distinct NAD-dependent isoform

TL;DR: The NAD-dependent human placental 11 beta HSD is distinct from the previously characterized rat liver isoform and may be the product of a separate gene.