The mechanism of RU486 antagonism is dependent on the conformation of the carboxy-terminal tail of the human progesterone receptor.
about
Yeast RSP5 and its human homolog hRPF1 potentiate hormone-dependent activation of transcription by human progesterone and glucocorticoid receptorsThe human glucocorticoid receptor beta isoform. Expression, biochemical properties, and putative functionGenetic and biochemical analysis of p23 and ansamycin antibiotics in the function of Hsp90-dependent signaling proteinsThe Angelman syndrome-associated protein, E6-AP, is a coactivator for the nuclear hormone receptor superfamilyJun dimerization protein 2 functions as a progesterone receptor N-terminal domain coactivator.Genetic variation in the progesterone receptor gene and ovarian cancer risk.Steroid receptor induction of gene transcription: a two-step modelSteroid receptor coactivators: servants and masters for control of systems metabolismTranscriptional coregulators: emerging roles of SRC family of coactivators in disease pathologyThe X-ray Structure of RU486 Bound to the Progesterone Receptor in a Destabilized Agonistic ConformationX-ray Structures of Progesterone Receptor Ligand Binding Domain in Its Agonist State Reveal Differing Mechanisms for Mixed Profiles of 11 -Substituted SteroidsAtomic structure of progesterone complexed with its receptorCoactivator/corepressor ratios modulate PR-mediated transcription by the selective receptor modulator RU486The nuclear corepressors NCoR and SMRT are key regulators of both ligand- and 8-bromo-cyclic AMP-dependent transcriptional activity of the human progesterone receptor.16 alpha-substituted analogs of the antiprogestin RU486 induce a unique conformation in the human progesterone receptor resulting in mixed agonist activitySmoothelin-like 1 protein is a bifunctional regulator of the progesterone receptor during pregnancyRegulation of retinal function but nonrescue of vision in RPE65-deficient dogs treated with doxycycline-regulatable AAV vectorsThe classical progesterone receptor mediates Xenopus oocyte maturation through a nongenomic mechanism.Characterization of a molecular switch system that regulates gene expression in mammalian cells through a small molecule.Partial agonist activity of the progesterone receptor antagonist RU486 mediated by an amino-terminal domain coactivator and phosphorylation of serine400Activation of progestin receptors in female reproductive behavior: Interactions with neurotransmittersConditional site-specific integration into human chromosome 19 by using a ligand-dependent chimeric adeno-associated virus/Rep protein.Distinct mechanisms of TGF-beta1-mediated epithelial-to-mesenchymal transition and metastasis during skin carcinogenesis.Expression of endogenous betaretroviruses in the ovine uterus: effects of neonatal age, estrous cycle, pregnancy, and progesterone.A critical role of helix 3-helix 5 interaction in steroid hormone receptor functionDifferent positioning of the ligand-binding domain helix 12 and the F domain of the estrogen receptor accounts for functional differences between agonists and antagonists.Regulation of endogenous human gene expression by ligand-inducible TALE transcription factors.HSV-1-based vectors for gene therapy of neurological diseases and brain tumors: part II. Vector systems and applicationsLEM1, an ATP-binding-cassette transporter, selectively modulates the biological potency of steroid hormones.Regulated gene expression in gene therapy.Role of nonhuman primate models in the discovery and clinical development of selective progesterone receptor modulators (SPRMs).Molecular determinants of nuclear receptor-corepressor interaction.Progesterone antagonists and progesterone receptor modulators.Structural and functional analysis of domains of the progesterone receptor.A regulatory system for use in gene transfer.Antiprogestins prevent progesterone receptor binding to hormone responsive elements in vivoConserved steroid hormone homology converges on nuclear factor κB to modulate inflammation in asthma.Exploring Flexibility of Progesterone Receptor Ligand Binding Domain Using Molecular Dynamics.Minireview: nuclear receptor and coregulator proteomics--2012 and beyond.Thermosensitive mutants of the MPTP and hPTP1B protein tyrosine phosphatases: isolation and structural analysis.
P2860
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P2860
The mechanism of RU486 antagonism is dependent on the conformation of the carboxy-terminal tail of the human progesterone receptor.
description
1992 nî lūn-bûn
@nan
1992 թուականի Մայիսին հրատարակուած գիտական յօդուած
@hyw
1992 թվականի մայիսին հրատարակված գիտական հոդված
@hy
1992年の論文
@ja
1992年論文
@yue
1992年論文
@zh-hant
1992年論文
@zh-hk
1992年論文
@zh-mo
1992年論文
@zh-tw
1992年论文
@wuu
name
The mechanism of RU486 antagon ...... e human progesterone receptor.
@ast
The mechanism of RU486 antagon ...... e human progesterone receptor.
@en
type
label
The mechanism of RU486 antagon ...... e human progesterone receptor.
@ast
The mechanism of RU486 antagon ...... e human progesterone receptor.
@en
prefLabel
The mechanism of RU486 antagon ...... e human progesterone receptor.
@ast
The mechanism of RU486 antagon ...... e human progesterone receptor.
@en
P2093
P1433
P1476
The mechanism of RU486 antagon ...... e human progesterone receptor.
@en
P2093
B W O'Malley
D P McDonnell
W T Schrader
P304
P356
10.1016/0092-8674(92)90234-4
P407
P577
1992-05-01T00:00:00Z