A surface on the androgen receptor that allosterically regulates coactivator binding - Test2 - elhamkhani - TriplyDB

A surface on the androgen receptor that allosterically regulates coactivator binding

A surface on the androgen receptor that allosterically regulates coactivator binding

http://www.wikidata.org/entity/Q27648698

about

Identification of a new androgen receptor (AR) co-regulator BUD31 and related peptides to suppress wild-type and mutated AR-mediated prostate cancer growth via peptide screening and X-ray structure analysis Steroid Receptor-Associated Immunophilins: A Gateway to Steroid Signalling Targeting the androgen receptor with steroid conjugates Molecular basis for dimer formation of TRβ variant D355R Targeting the binding function 3 (BF3) site of the human androgen receptor through virtual screening.Identification of a new hormone-binding site on the surface of thyroid hormone receptor A natural-product switch for a dynamic protein interface Fragment Screening of RORγt Using Cocktail Crystallography: Identification of Simultaneous Binding of Multiple Fragments PA1 protein, a new competitive decelerator acting at more than one step to impede glucocorticoid receptor-mediated transactivation The oncoprotein BCL11A binds to orphan nuclear receptor TLX and potentiates its transrepressive function Characterizing protein domain associations by Small-molecule ligand binding The helix 1-3 loop in the glucocorticoid receptor LBD is a regulatory element for FKBP cochaperones.Minoxidil may suppress androgen receptor-related functions Minireview: Not picking pockets: nuclear receptor alternate-site modulators (NRAMs)Small molecule inhibitors targeting the "achilles' heel" of androgen receptor activity Research resource: modulators of glucocorticoid receptor activity identified by a new high-throughput screening assay.Severe forms of partial androgen insensitivity syndrome due to p.L830F novel mutation in androgen receptor gene in a Brazilian family.Targeting the regulation of androgen receptor signaling by the heat shock protein 90 cochaperone FKBP52 in prostate cancer cells.Intrinsic disorder in the androgen receptor: identification, characterisation and drugability.Advances in small molecule inhibitors of androgen receptor for the treatment of advanced prostate cancer.Selectively targeting the DNA-binding domain of the androgen receptor as a prospective therapy for prostate cancer.Glucocorticoid receptor cofactors as therapeutic targets.A noncompetitive small molecule inhibitor of estrogen-regulated gene expression and breast cancer cell growth that enhances proteasome-dependent degradation of estrogen receptor {alpha}.Recent advances in allosteric androgen receptor inhibitors for the potential treatment of castration-resistant prostate cancer.Helix 11 dynamics is critical for constitutive androstane receptor activity.Analysis of agonist and antagonist effects on thyroid hormone receptor conformation by hydrogen/deuterium exchange.Small molecule inhibitors as probes for estrogen and androgen receptor action Constitutive activity of the androgen receptor.Quantification of a New Anti-Cancer Molecule MJC13 Using a Rapid, Sensitive, and Reliable Liquid Chromatography-Tandem Mass Spectrometry Method Detection of persistent organic pollutants binding modes with androgen receptor ligand binding domain by docking and molecular dynamics.Regulation of steroid hormone receptor function by the 52-kDa FK506-binding protein (FKBP52).The road less traveled: new views of steroid receptor action from the path of dose-response curves.Solution formulation development and efficacy of MJC13 in a preclinical model of castration-resistant prostate cancer The FKBP52 Cochaperone Acts in Synergy with β-Catenin to Potentiate Androgen Receptor Signaling.Similarities and Distinctions in Actions of Surface-Directed and Classic Androgen Receptor Antagonists.Drug Repurposing from an Academic Perspective.Separate regions of glucocorticoid receptor, coactivator TIF2, and comodulator STAMP modify different parameters of glucocorticoid-mediated gene induction.Corepressor effect on androgen receptor activity varies with the length of the CAG encoded polyglutamine repeat and is dependent on receptor/corepressor ratio in prostate cancer cells.Androgen receptor: structure, role in prostate cancer and drug discovery.A competitive inhibitor that reduces recruitment of androgen receptor to androgen-responsive genes

P2860

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P2860

A surface on the androgen receptor that allosterically regulates coactivator binding

http://www.wikidata.org/entity/Q27648698

description

2007 nî lūn-bûn

@nan

2007 թուականի Հոկտեմբերին հրատարակուած գիտական յօդուած

@hyw

2007 թվականի հոտեմբերին հրատարակված գիտական հոդված

@hy

2007年の論文

@ja

2007年論文

@yue

2007年論文

@zh-hant

2007年論文

@zh-hk

2007年論文

@zh-mo

2007年論文

@zh-tw

2007年论文

@wuu

name

A surface on the androgen receptor that allosterically regulates coactivator binding

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A surface on the androgen receptor that allosterically regulates coactivator binding

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A surface on the androgen receptor that allosterically regulates coactivator binding

@nl

type

label

A surface on the androgen receptor that allosterically regulates coactivator binding

@ast

A surface on the androgen receptor that allosterically regulates coactivator binding

@en

A surface on the androgen receptor that allosterically regulates coactivator binding

@nl

prefLabel

A surface on the androgen receptor that allosterically regulates coactivator binding

@ast

A surface on the androgen receptor that allosterically regulates coactivator binding

@en

A surface on the androgen receptor that allosterically regulates coactivator binding

@nl

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PNAS.0708036104

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Proceedings of the National Academy of Sciences of the United States of America

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A surface on the androgen receptor that allosterically regulates coactivator binding

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Edson Delgado Rodrigues

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Ellena Mar

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John D Baxter

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Kevan M Shokat

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Raynard Bateman

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Robert J Fletterick

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P2860

The molecular mechanisms of coactivator utilization in ligand-dependent transactivation by the androgen receptor

Recognition and accommodation at the androgen receptor coactivator binding interface

Ligand selectivity by seeking hydrophobicity in thyroid hormone receptor

In vivo activation of the p53 pathway by small-molecule antagonists of MDM2

Crystallographic comparison of the estrogen and progesterone receptor's ligand binding domains

Nuclear-receptor ligands and ligand-binding domains

Androgen receptor-cofactor interactions as targets for new drug discovery

Androgen receptor in prostate cancer

Sensors and signals: a coactivator/corepressor/epigenetic code for integrating signal-dependent programs of transcriptional response

Small-molecule inhibitors of protein-protein interactions: progressing towards the dream

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16074-16079

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10.1073/PNAS.0708036104

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41

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104

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Eva Estébanez-Perpiñá

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2007-10-02T00:00:00Z

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5934310

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17911242

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1999396

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