Discovery of diverse thyroid hormone receptor antagonists by high-throughput docking. - Test2 - elhamkhani - TriplyDB

Discovery of diverse thyroid hormone receptor antagonists by high-throughput docking.

Discovery of diverse thyroid hormone receptor antagonists by high-throughput docking.

http://www.wikidata.org/entity/Q30940049

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The SWISS-MODEL Repository of annotated three-dimensional protein structure homology models Orphan nuclear receptors in drug discovery A rapid cytoplasmic mechanism for PI3 kinase regulation by the nuclear thyroid hormone receptor, TRβ, and genetic evidence for its role in the maturation of mouse hippocampal synapses in vivo Chemogenomics: an emerging strategy for rapid target and drug discovery Rapid signaling at the plasma membrane by a nuclear receptor for thyroid hormone Computational modeling-based discovery of novel classes of anti-inflammatory drugs that target lanthionine synthetase C-like protein 2 Dendritic cell immunoreceptor is a new target for anti-AIDS drug development: identification of DCIR/HIV-1 inhibitors The Quantum Nature of Drug-Receptor Interactions: Deuteration Changes Binding Affinities for Histamine Receptor Ligands Compound activity prediction using models of binding pockets or ligand properties in 3D.Inhibition by stabilization: targeting the Plasmodium falciparum aldolase-TRAP complex Virtual screening of chemical libraries.Discovery of antiandrogen activity of nonsteroidal scaffolds of marketed drugs Improved docking, screening and selectivity prediction for small molecule nuclear receptor modulators using conformational ensembles.Structural determinants of PERK inhibitor potency and selectivity Understanding nuclear receptors using computational methods.SiMMap: a web server for inferring site-moiety map to recognize interaction preferences between protein pockets and compound moieties.Nuclear receptor engineering based on novel structure activity relationships revealed by farnesyl pyrophosphate.Inhibition of thyroid hormone receptor locally in the retina is a therapeutic strategy for retinal degeneration.Discovery of novel ligands for mouse olfactory receptor MOR42-3 using an in silico screening approach and in vitro validation.Making virtual screening a reality.Thyroid hormone response element half-site organization and its effect on thyroid hormone mediated transcription.The immediate and late effects of thyroid hormone (triiodothyronine) on murine coagulation gene transcription.Mining the receptorome.Promotion of the induction of cell pluripotency through metabolic remodeling by thyroid hormone triiodothyronine-activated PI3K/AKT signal pathway Docking and scoring with ICM: the benchmarking results and strategies for improvement.Virtual interactomics of proteins from biochemical standpoint.Potential Broad Spectrum Inhibitors of the Coronavirus 3CLpro: A Virtual Screening and Structure-Based Drug Design Study.Current and potential rodent screens and tests for thyroid toxicants.Screening Outside the Catalytic Site: Inhibition of Macromolecular Inter-actions Through Structure-Based Virtual Ligand Screening Experiments.Structure-based discovery of antagonists of nuclear receptor LRH-1.Dehydrogenation of the indoline-containing drug 4-chloro-N-(2-methyl-1-indolinyl)-3-sulfamoylbenzamide (indapamide) by CYP3A4: correlation with in silico predictions A critical review finds styrene lacks direct endocrine disruptor activity.Bacterial biosensors for screening isoform-selective ligands for human thyroid receptors α-1 and β-1.Discovery of novel inhibitors targeting enoyl-acyl carrier protein reductase in Plasmodium falciparum by structure-based virtual screening.Retrospective molecular docking study of WY-25105 ligand to β-secretase and bias of the three-dimensional structure flexibility.Progress towards development of an amphibian-based thyroid screening assay using Xenopus laevis. Organismal and thyroidal responses to the model compounds 6-propylthiouracil, methimazole, and thyroxine.Editor's Highlight: Structure-Based Investigation on the Binding and Activation of Typical Pesticides With Thyroid Receptor.Dioxin Exposure Alters Molecular and Morphological Responses to Thyroid Hormone in Xenopus laevis Cultured Cells and Prometamorphic Tadpoles.Metformin interacts with AMPK through binding to γ subunit.High-throughput structural characterisation of therapeutic protein targets

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Discovery of diverse thyroid hormone receptor antagonists by high-throughput docking.

http://www.wikidata.org/entity/Q30940049

description

2003 nî lūn-bûn

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2003 թուականի Մայիսին հրատարակուած գիտական յօդուած

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2003 թվականի մայիսին հրատարակված գիտական հոդված

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2003年の論文

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2003年論文

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2003年論文

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2003年論文

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2003年論文

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2003年論文

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2003年论文

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name

Discovery of diverse thyroid hormone receptor antagonists by high-throughput docking.

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Discovery of diverse thyroid hormone receptor antagonists by high-throughput docking.

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type

label

Discovery of diverse thyroid hormone receptor antagonists by high-throughput docking.

@ast

Discovery of diverse thyroid hormone receptor antagonists by high-throughput docking.

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prefLabel

Discovery of diverse thyroid hormone receptor antagonists by high-throughput docking.

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Discovery of diverse thyroid hormone receptor antagonists by high-throughput docking.

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PNAS.1131854100

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

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Discovery of diverse thyroid hormone receptor antagonists by high-throughput docking.

@en

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Bruce M Raaka

http://www.w3.org/2001/XMLSchema#string

Herbert H Samuels

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Li Fan

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Matthieu Schapira

http://www.w3.org/2001/XMLSchema#string

Maxim Totrov

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Sharmistha Das

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Stephen R Wilson

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Zhiguo Zhou

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P2860

NRIF3 is a novel coactivator mediating functional specificity of nuclear hormone receptors

A new family of nuclear receptor coregulators that integrate nuclear receptor signaling through CREB-binding protein

Structure of the ligand-binding domain of oestrogen receptor beta in the presence of a partial agonist and a full antagonist

Crystal structure of a heterodimeric complex of RAR and RXR ligand-binding domains

Structural insights into the mode of action of a pure antiestrogen

Structural basis for antagonist-mediated recruitment of nuclear co-repressors by PPARalpha

Structural characterization of a subtype-selective ligand reveals a novel mode of estrogen receptor antagonism

Crystal structure of the ligand-binding domain of the human nuclear receptor RXR-alpha

Molecular basis of agonism and antagonism in the oestrogen receptor

Structure and specificity of nuclear receptor-coactivator interactions

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