(Q30521288)

English

Comparison of dynamics of extracellular accesses to the β(1) and β(2) adrenoceptors binding sites uncovers the potential of kinetic basis of antagonist selectivity

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scholarly article

1 reference

Europe PubMed Central

PMC publication ID

12 August 2017

Comparison of dynamics of extracellular accesses to the β(1) and β(2) adrenoceptors binding sites uncovers the potential of kinetic basis of antagonist selectivity (English)

1 reference

Europe PubMed Central

PMC publication ID

12 August 2017

author name string

Balaji Selvam

1

1 reference

Europe PubMed Central

PMC publication ID

12 August 2017

Jeff Wereszczynski

2

1 reference

Europe PubMed Central

PMC publication ID

12 August 2017

Irina G Tikhonova

3

1 reference

Europe PubMed Central

PMC publication ID

12 August 2017

language of work or name

1 reference

based on heuristic

inferred from title

publication date

2 May 2012

1 reference

Europe PubMed Central

PMC publication ID

12 August 2017

Chemical Biology and Drug Design

1 reference

Europe PubMed Central

PMC publication ID

12 August 2017

80

1 reference

Europe PubMed Central

PMC publication ID

12 August 2017

2

1 reference

Europe PubMed Central

PMC publication ID

12 August 2017

215-226

1 reference

Europe PubMed Central

PMC publication ID

12 August 2017

Activation mechanism of the β2-adrenergic receptor

1 reference

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Ligand-induced modulation of the free-energy landscape of G protein-coupled receptors explored by adaptive biasing techniques

1 reference

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Molecular basis of ligand dissociation in β-adrenergic receptors

1 reference

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Crystal structure of the β2 adrenergic receptor-Gs protein complex

1 reference

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Two distinct conformations of helix 6 observed in antagonist-bound structures of a 1-adrenergic receptor

1 reference

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1 reference

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1 reference

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Ligand-specific regulation of the extracellular surface of a G-protein-coupled receptor

1 reference

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Structure of a beta1-adrenergic G-protein-coupled receptor

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High-resolution crystal structure of an engineered human beta2-adrenergic G protein-coupled receptor

1 reference

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Crystal structure of the human beta2 adrenergic G-protein-coupled receptor

1 reference

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The selectivity of beta-adrenoceptor antagonists at the human beta1, beta2 and beta3 adrenoceptors

1 reference

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A primate-dominant third glycosylation site of the beta2-adrenergic receptor routes receptors to degradation during agonist regulation

1 reference

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Sequential binding of agonists to the beta2 adrenoceptor. Kinetic evidence for intermediate conformational states

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Glycosylation of beta(1)-adrenergic receptors regulates receptor surface expression and dimerization

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Steered molecular dynamics and mechanical functions of proteins

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Binding pockets of the beta(1)- and beta(2)-adrenergic receptors for subtype-selective agonists

1 reference

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1 reference

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Beta 1-adrenoceptor subtype selective antagonism of esmolol and its major metabolite in vitro and in man. Investigations using tricresylphosphate as red blood cell carboxylesterase inhibitor

1 reference

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12 December 2020

based on heuristic

inferred from PubMed ID database lookup

Identifiers

10.1111/J.1747-0285.2012.01390.X

1 reference

Europe PubMed Central

PMC publication ID

12 August 2017

PMC publication ID

1 reference

Europe PubMed Central

PMC publication ID

12 August 2017

PubMed publication ID

1 reference

Europe PubMed Central

PMC publication ID

12 August 2017

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