Pregna-D'-pentarane structure influences progesterone receptor affinity for DNA. (Q38290107)

1 September 2017

title

Pregna-D'-pentarane structure influences progesterone receptor affinity for DNA. (English)

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1 September 2017

Shchelkunova TA

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1 September 2017

Rubtsov PM

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1 September 2017

Levina IS

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1 September 2017

Kamerntsky AV

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1 September 2017

Smirnov AN

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1 September 2017

publication date

1 April 2002

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1 September 2017

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1 September 2017

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1 September 2017

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1 September 2017

page(s)

323-332

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Steroid hormone receptors: an update

1 September 2017

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The antagonists RU486 and ZK98299 stimulate progesterone receptor binding to deoxyribonucleic acid in vitro and in vivo, but have distinct effects on receptor conformation

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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

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Human progesterone receptor complexed with the antagonist RU 486 binds to hormone response elements in a structurally altered form

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Estrogen receptor ligands modulate its interaction with DNA

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Agonist and antagonists induce homodimerization and mixed ligand heterodimerization of human progesterone receptors in vivo by a mammalian two-hybrid assay.

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Two distinct estrogen-regulated promoters generate transcripts encoding the two functionally different human progesterone receptor forms A and B

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7 January 2021

Atomic structure of progesterone complexed with its receptor

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7 January 2021

10.1016/S0039-128X(01)00188-X

Identifiers

DOI

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1 September 2017

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