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New aryl hydrocarbon receptor homology model targeted to improve docking reliability.

New aryl hydrocarbon receptor homology model targeted to improve docking reliability.

http://www.wikidata.org/entity/Q35686667

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Deciphering Dimerization Modes of PAS Domains: Computational and Experimental Analyses of the AhR:ARNT Complex Reveal New Insights Into the Mechanisms of AhR Transformation Access Path to the Ligand Binding Pocket May Play a Role in Xenobiotics Selection by AhR Bis-aryloxadiazoles as effective activators of the aryl hydrocarbon receptor.In silico identification of an aryl hydrocarbon receptor antagonist with biological activity in vitro and in vivo.Ginsenosides are novel naturally-occurring aryl hydrocarbon receptor ligands A Structural Switch between Agonist and Antagonist Bound Conformations for a Ligand-Optimized Model of the Human Aryl Hydrocarbon Receptor Ligand Binding Domain Naturally occurring marine brominated indoles are aryl hydrocarbon receptor ligands/agonists Chemical genetic screen reveals a role for desmosomal adhesion in mammary branching morphogenesis.Comparative analysis of homology models of the AH receptor ligand binding domain: verification of structure-function predictions by site-directed mutagenesis of a nonfunctional receptor.Specific ligand binding domain residues confer low dioxin responsiveness to AHR1β of Xenopus laevis Ligand promiscuity of aryl hydrocarbon receptor agonists and antagonists revealed by site-directed mutagenesis.Latest developments in molecular docking: 2010-2011 in review.Macromolecular structure and interaction studies of SigF and Usfx in Mycobacterium tuberculosis.Editor's Highlight: Microbial-Derived 1,4-Dihydroxy-2-naphthoic Acid and Related Compounds as Aryl Hydrocarbon Receptor Agonists/Antagonists: Structure-Activity Relationships and Receptor Modeling.Identification of potential aryl hydrocarbon receptor ligands by virtual screening of industrial chemicals.AhR sensing of bacterial pigments regulates antibacterial defence.Comparative In Vitro and In Silico Analysis of the Selectivity of Indirubin as a Human Ah Receptor Agonist

P2860

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P2860

New aryl hydrocarbon receptor homology model targeted to improve docking reliability.

http://www.wikidata.org/entity/Q35686667

description

2011 nî lūn-bûn

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name

New aryl hydrocarbon receptor homology model targeted to improve docking reliability.

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New aryl hydrocarbon receptor homology model targeted to improve docking reliability.

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type

label

New aryl hydrocarbon receptor homology model targeted to improve docking reliability.

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New aryl hydrocarbon receptor homology model targeted to improve docking reliability.

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prefLabel

New aryl hydrocarbon receptor homology model targeted to improve docking reliability.

@ast

New aryl hydrocarbon receptor homology model targeted to improve docking reliability.

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P1433

Journal of Chemical Information and Modeling

P1476

New aryl hydrocarbon receptor homology model targeted to improve docking reliability.

@en

P2093

Anatoly A Soshilov

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

Annalisa Bordogna

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

Ilaria Motto

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

Laura Bonati

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

Michael S Denison

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P2860

Dioxin binding activities of polymorphic forms of mouse and human arylhydrocarbon receptors

Induction of CYP1A1. The AhR/DRE paradigm: transcription, receptor regulation, and expanding biological roles

Structure and interactions of PAS kinase N-terminal PAS domain: model for intramolecular kinase regulation

Structural basis for PAS domain heterodimerization in the basic helix-loop-helix-PAS transcription factor hypoxia-inducible factor

Rescoring Docking Hit Lists for Model Cavity Sites: Predictions and Experimental Testing

Artificial ligand binding within the HIF2 PAS-B domain of the HIF2 transcription factor

Principles of Ligand Binding within a Completely Buried Cavity in HIF2α PAS-B

Comparative protein structure modeling of genes and genomes

CASTp: computed atlas of surface topography of proteins with structural and topographical mapping of functionally annotated residues

Comparative protein modelling by satisfaction of spatial restraints

P304

2868-2881

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scholarly article

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10.1021/CI2001617

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11

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51

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2011-11-02T00:00:00Z

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51701185

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21981577

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3263330

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