Ligand-specific interactions modulate kinetic, energetic, and mechanical properties of the human β2 adrenergic receptor.
about
Structural approaches to understanding retinal proteins needed for visionSubstrate-induced changes in the structural properties of LacYDynamic single-molecule force spectroscopy of rhodopsin in native membranesAtomic force microscopy: a multifaceted tool to study membrane proteins and their interactions with ligands.Simulations of biased agonists in the β(2) adrenergic receptor with accelerated molecular dynamics.Divergent label-free cell phenotypic pharmacology of ligands at the overexpressed β₂-adrenergic receptors.Development and characterization of pepducins as Gs-biased allosteric agonists.Single-molecule force spectroscopy of G-protein-coupled receptors.Peptide transporter DtpA has two alternate conformations, one of which is promoted by inhibitor binding.Agonist binding by the β2-adrenergic receptor: an effect of receptor conformation on ligand association-dissociation characteristicsObserving a lipid-dependent alteration in single lactose permeasesIdentifying and quantifying two ligand-binding sites while imaging native human membrane receptors by AFM.Advances in receptor conformation research: the quest for functionally selective conformations focusing on the β2-adrenoceptorCholesterol increases kinetic, energetic, and mechanical stability of the human β2-adrenergic receptor.Identification of a Novel Gnao-Mediated Alternate Olfactory Signaling Pathway in Murine OSNs.Conformational flexibility and structural dynamics in GPCR-mediated G protein activation: a perspective.Ligands raise the constraint that limits constitutive activation in G protein-coupled opioid receptors.Kinetic, energetic, and mechanical differences between dark-state rhodopsin and opsin.Imaging G protein-coupled receptors while quantifying their ligand-binding free-energy landscape.The Allostery Landscape: Quantifying Thermodynamic Couplings in Biomolecular Systems.Minireview: More than just a hammer: ligand "bias" and pharmaceutical discovery.P23H opsin knock-in mice reveal a novel step in retinal rod disc morphogenesis.Grand opening of structure-guided design for novel opioids.Watching cellular machinery in action, one molecule at a time.Detailed analysis of biased histamine H₄ receptor signalling by JNJ 7777120 analogues.Applications of Single-Molecule Methods to Membrane Protein Folding Studies.Retinal Conformation Changes Rhodopsin's Dynamic Ensemble.Effect of material flexibility on the thermodynamics and kinetics of hydrophobically induced evaporation of water.Olfactory Receptors Modulate Physiological Processes in Human Airway Smooth Muscle Cells.Ligand-selective activation of heterologously-expressed mammalian olfactory receptor.Molecular modeling studies give hint for the existence of a symmetric hβ₂R-Gαβγ-homodimer.Construction of Structural Mimetics of the Thyrotropin Receptor Intracellular Domain.Evolutionary action and structural basis of the allosteric switch controlling β2AR functional selectivity.Molecular Basis of Oxytocin Receptor Signalling in the Brain: What We Know and What We Need to Know.G Protein-Coupled Receptors Contain Two Conserved Packing Clusters.Bioluminescence resonance energy transfer-based biosensors allow monitoring of ligand- and transducer-mediated GPCR conformational changes
P2860
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P2860
Ligand-specific interactions modulate kinetic, energetic, and mechanical properties of the human β2 adrenergic receptor.
description
2012 nî lūn-bûn
@nan
2012年の論文
@ja
2012年論文
@yue
2012年論文
@zh-hant
2012年論文
@zh-hk
2012年論文
@zh-mo
2012年論文
@zh-tw
2012年论文
@wuu
2012年论文
@zh
2012年论文
@zh-cn
name
Ligand-specific interactions m ...... human β2 adrenergic receptor.
@ast
Ligand-specific interactions m ...... human β2 adrenergic receptor.
@en
type
label
Ligand-specific interactions m ...... human β2 adrenergic receptor.
@ast
Ligand-specific interactions m ...... human β2 adrenergic receptor.
@en
prefLabel
Ligand-specific interactions m ...... human β2 adrenergic receptor.
@ast
Ligand-specific interactions m ...... human β2 adrenergic receptor.
@en
P2093
P2860
P1433
P1476
Ligand-specific interactions m ...... human β2 adrenergic receptor.
@en
P2093
Daniel J Müller
Juan J Fung
Michael Zocher
P2860
P304
P356
10.1016/J.STR.2012.05.010
P577
2012-06-28T00:00:00Z