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Emma T van der Westhuizen
Researcher at Monash University
Publications - 35
Citations - 992
Emma T van der Westhuizen is an academic researcher from Monash University. The author has contributed to research in topics: Allosteric regulation & Muscarinic acetylcholine receptor. The author has an hindex of 12, co-authored 27 publications receiving 805 citations. Previous affiliations of Emma T van der Westhuizen include Monash University, Clayton campus & Université de Montréal.
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Quantification of ligand bias for clinically relevant β2-adrenergic receptor ligands: implications for drug taxonomy.
TL;DR: A higher level of ligand texture is demonstrated than previously anticipated, opening perspectives for the establishment of pluridimensional correlations between signaling profiles, drug classification, therapeutic efficacy, and safety.
Journal ArticleDOI
Structural insights into binding specificity, efficacy and bias of a beta2AR partial agonist.
Matthieu Masureel,Yaozhong Zou,Louis Picard,Emma T van der Westhuizen,Emma T van der Westhuizen,Jacob P. Mahoney,João P. G. L. M. Rodrigues,Thomas J. Mildorf,Ron O. Dror,David E. Shaw,Michel Bouvier,Els Pardon,Jan Steyaert,Roger K. Sunahara,William I. Weis,Cheng Zhang,Brian K. Kobilka +16 more
TL;DR: The active-state structure of a GPCR occupied by a partial agonist, β2AR with salmeterol, together with mutagenesis and biophysical studies, explains this ligand's unusual pharmacological profile.
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Endogenous Allosteric Modulators of G Protein–Coupled Receptors
TL;DR: The increasing identification of allosteric modulator lipids, inflammatory peptides, and G PCR-targeted autoantibodies indicates that disease context plays an important role in the generation of putative endogenous GPCR modulators.
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Impedance Responses Reveal β2-Adrenergic Receptor Signaling Pluridimensionality and Allow Classification of Ligands with Distinct Signaling Profiles
TL;DR: It is demonstrated that a single label-free assay based on cellular impedance provides a real-time integration of multiple signaling events engaged upon GPCR activation, indicating that the pluridimensionality of G PCR signaling can be captured using integrative approaches to provide a comprehensive readout of drug activity.
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The Relaxin Family Peptide Receptor 3 Activates Extracellular Signal-Regulated Kinase 1/2 through a Protein Kinase C-Dependent Mechanism
TL;DR: It is identified that RXFP3 stably expressed in Chinese hamster ovary (CHO)-K1 and human embryonic kidney (HEK-RXFP3) cells activates extracellular signal-regulated kinase (ERK) 1/2 when stimulated with H3 relaxin and an H3 Relaxin B-chain (dimer) peptide.