S
Scott A. Hollingsworth
Researcher at Merck & Co.
Publications - 35
Citations - 2376
Scott A. Hollingsworth is an academic researcher from Merck & Co.. The author has contributed to research in topics: G protein-coupled receptor & Chemistry. The author has an hindex of 16, co-authored 31 publications receiving 1305 citations. Previous affiliations of Scott A. Hollingsworth include Oregon State University & Stanford University.
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Journal ArticleDOI
Molecular Dynamics Simulation for All.
TL;DR: The types of information molecular dynamics simulations can provide and the ways in which they typically motivate further experimental work are described.
Journal ArticleDOI
Structure of a Signaling Cannabinoid Receptor 1-G Protein Complex
Kaavya Krishna Kumar,Moran Shalev-Benami,Michael J. Robertson,Hongli Hu,Samuel D. Banister,Scott A. Hollingsworth,Naomi R. Latorraca,Hideaki E. Kato,Daniel Hilger,Shoji Maeda,William I. Weis,William I. Weis,David L. Farrens,Ron O. Dror,Sanjay V. Malhotra,Brian K. Kobilka,Georgios Skiniotis,Georgios Skiniotis +17 more
TL;DR: The structure of the CB1-Gi signaling complex bound to the highly potent agonist MDMB-Fubinaca (FUB) is presented, which compose the structural framework to explain CB1 activation by different classes of ligands and provide insights into the G protein coupling and selectivity mechanisms adopted by the receptor.
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A fresh look at the Ramachandran plot and the occurrence of standard structures in proteins.
TL;DR: High-fidelity conformational information is used to explore novel ways to convey some of the basic aspects of the Ramachandran plot and of protein conformation to highlight the pressing need for a standard nomenclature for peptide conformation.
Journal ArticleDOI
Molecular mechanism of GPCR-mediated arrestin activation
Naomi R. Latorraca,Jason K. Wang,Brian Bauer,Raphael J. L. Townshend,Scott A. Hollingsworth,Julia Eve Olivieri,H. Eric Xu,H. Eric Xu,Martha E. Sommer,Ron O. Dror +9 more
TL;DR: The results, which suggest that diverse receptor binding modes can activate arrestin, provide a structural foundation for the design of functionally selective (‘biased’) GPCR-targeted ligands with desired effects on arrestin signalling.
Journal ArticleDOI
How GPCR Phosphorylation Patterns Orchestrate Arrestin-Mediated Signaling
Naomi R. Latorraca,Matthieu Masureel,Scott A. Hollingsworth,Franziska M. Heydenreich,Franziska M. Heydenreich,Carl-Mikael Suomivuori,Connor Brinton,Raphael J. L. Townshend,Michel Bouvier,Brian K. Kobilka,Ron O. Dror +10 more
TL;DR: The structural basis for the long-standing "barcode" hypothesis is revealed and has important implications for design of functionally selective GPCR-targeted drugs.