The size and/or configuration of the cycloalkane D′ ring in pentacyclic progesterone derivatives are crucial for their high-affinity binding to a protein in addition to progesterone receptor in rat uterine cytosol☆-Reference-Cited by-同舟云学术

The size and/or configuration of the cycloalkane D′ ring in pentacyclic progesterone derivatives are crucial for their high-affinity binding to a protein in addition to progesterone receptor in rat uterine cytosol☆

Published:2000-03 Issue:3 Volume:65 Page:163-170
ISSN:0039-128X
Container-title:Steroids
language:en
Short-container-title:Steroids

Author:

Smirnov Alexander N,Pokrovskaya Elena V,Kogteva Galina S,Shevchenko Valery P,Levina Inna S,Kulikova Lidiya E,Kamernitzky Alexey V

Publisher

Elsevier BV

Subject

Organic Chemistry,Clinical Biochemistry,Pharmacology,Endocrinology,Molecular Biology,Biochemistry

Reference18 articles.

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2. Raynaud JP, Bissery V, Gaboriaud C, Ojasoo T, Teutsch G, Mornon JP. An analysis of the steroid binding domain of receptors and of ligand structure and binding affinity. In: Carlstedt–Duke J, Eriksson H, Gustafsson J-A, editors. The Steroid/Thyroid Hormone Receptor Family and Gene Regulation. Basel: Birkhäuser Verlag, 1989. pp. 337–66.

3. Atomic structure of progesterone complexed with its receptor;Williams;Nature,1988

4. 16 α-substituted analogs of the antiprogestin RU486 induce a unique conformation in the human progesterone receptor resulting in mixed agonist activity;Wagner;Proc Natl Acad Sci USA,1996

5. The antagonists RU486 and ZK98299 stimulate progesterone receptor binding to deoxyribonucleic acid in vitro and in vivo, but have distinct effects on receptor conformation;Gass;Endocrinology,1998

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5. 3- and 19-Oximes of 16α,17α-cyclohexanoprogesterone derivatives: Synthesis and interactions with progesterone receptor and other proteins;Steroids;2008-09