Allosteric nanobodies reveal the dynamic range and diverse mechanisms of G-protein-coupled receptor activation

Structural Insights into the Dynamic Process of β 2 -Adrenergic Receptor Signaling

(2015) Aashish Manglik et al.   CELL

Divergent Transducer-specific Molecular Efficacies Generate Biased Agonism at a G Protein-coupled Receptor (GPCR)

(2014) Ryan T. Strachan et al.   JOURNAL OF BIOLOGICAL CHEMISTRY

Tracing an allosteric pathway regulating the activity of the HslV protease

(2014) Lichi Shi et al.   PROCEEDINGS OF THE NATIONAL ACADEMY OF SCIENCES OF THE UNITED STATES OF AMERICA

What is biased efficacy? Defining the relationship between intrinsic efficacy and free energy coupling

(2014) H. Ongun Onaran et al.   TRENDS IN PHARMACOLOGICAL SCIENCES

The Dynamic Process of β2-Adrenergic Receptor Activation

(2013) Rie Nygaard et al.   CELL

Ligands Raise the Constraint That Limits Constitutive Activation in G Protein-coupled Opioid Receptors

(2013) Vanessa Vezzi et al.   JOURNAL OF BIOLOGICAL CHEMISTRY

Adrenaline-activated structure of β2-adrenoceptor stabilized by an engineered nanobody

(2013) Aaron M. Ring et al.   NATURE

A three-stage biophysical screening cascade for fragment-based drug discovery

(2013) Ellene H Mashalidis et al.   Nature Protocols

Biased Signaling Pathways in  2-Adrenergic Receptor Characterized by 19F-NMR

(2012) J. J. Liu et al.   SCIENCE

Efficacy of the β2-adrenergic receptor is determined by conformational equilibrium in the transmembrane region

(2012) Yutaka Kofuku et al.   Nature Communications

Quantifying Ligand Bias at Seven-Transmembrane Receptors

(2011) S. Rajagopal et al.   MOLECULAR PHARMACOLOGY

Structure of a nanobody-stabilized active state of the β2 adrenoceptor

(2011) Søren G. F. Rasmussen et al.   NATURE

Crystal structure of the β2 adrenergic receptor–Gs protein complex

(2011) Søren G. F. Rasmussen et al.   NATURE

Multiple ligand-specific conformations of the β2-adrenergic receptor

(2011) Alem W Kahsai et al.   Nature Chemical Biology

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

(2011) R. Moukhametzianov et al.   PROCEEDINGS OF THE NATIONAL ACADEMY OF SCIENCES OF THE UNITED STATES OF AMERICA

PHENIX: a comprehensive Python-based system for macromolecular structure solution

(2010) Paul D. Adams et al.   ACTA CRYSTALLOGRAPHICA SECTION D-BIOLOGICAL CRYSTALLOGRAPHY

MolProbity: all-atom structure validation for macromolecular crystallography

(2009) Vincent B. Chen et al.   ACTA CRYSTALLOGRAPHICA SECTION D-BIOLOGICAL CRYSTALLOGRAPHY

Allosteric Coupling and Conformational Fluctuations in Proteins

(2009) H. Onaran et al.   CURRENT PROTEIN & PEPTIDE SCIENCE

Identification of two distinct inactive conformations of the  2-adrenergic receptor reconciles structural and biochemical observations

(2009) R. O. Dror et al.   PROCEEDINGS OF THE NATIONAL ACADEMY OF SCIENCES OF THE UNITED STATES OF AMERICA