A
Alissa L. W. Kleinhenz
Researcher at Howard Hughes Medical Institute
Publications - 4
Citations - 509
Alissa L. W. Kleinhenz is an academic researcher from Howard Hughes Medical Institute. The author has contributed to research in topics: G protein-coupled receptor & Arrestin. The author has an hindex of 3, co-authored 4 publications receiving 249 citations. Previous affiliations of Alissa L. W. Kleinhenz include Duke University & University of Michigan.
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Journal ArticleDOI
Structure of the M2 Muscarinic Receptor-β-Arrestin Complex in a Lipid Nanodisc
Dean P. Staus,Dean P. Staus,Hongli Hu,Hongli Hu,Michael J. Robertson,Alissa L. W. Kleinhenz,Alissa L. W. Kleinhenz,Alissa L. W. Kleinhenz,Laura M. Wingler,Laura M. Wingler,William D. Capel,Naomi R. Latorraca,Robert J. Lefkowitz,Robert J. Lefkowitz,Georgios Skiniotis +14 more
TL;DR: A cryo-electron microscopy structure of β-arrestin 1 in complex with M2 muscarinic receptor reconstituted in lipid nanodiscs is presented and it is shown that the C-edge is critical for stable complex formation, βarr1 recruitment, receptor internalization, and desensitization of G-protein activation.
Journal ArticleDOI
Molecular mechanism of biased signaling in a prototypical G protein-coupled receptor.
Carl-Mikael Suomivuori,Naomi R. Latorraca,Laura M. Wingler,Laura M. Wingler,Stephan Eismann,Matthew C. King,Alissa L. W. Kleinhenz,Alissa L. W. Kleinhenz,Alissa L. W. Kleinhenz,Meredith A. Skiba,Dean P. Staus,Dean P. Staus,Andrew C. Kruse,Robert J. Lefkowitz,Robert J. Lefkowitz,Ron O. Dror +15 more
TL;DR: Detailed atomic-level molecular dynamics simulations are used to determine how arrestin bias and G protein bias arise at the angiotensin II type 1 receptor and designed ligands with desired signaling profiles.
Journal ArticleDOI
Angiotensin and biased analogs induce structurally distinct active conformations within a GPCR
Laura M. Wingler,Laura M. Wingler,Meredith A. Skiba,Conor McMahon,Dean P. Staus,Dean P. Staus,Alissa L. W. Kleinhenz,Alissa L. W. Kleinhenz,Alissa L. W. Kleinhenz,Carl-Mikael Suomivuori,Naomi R. Latorraca,Ron O. Dror,Robert J. Lefkowitz,Robert J. Lefkowitz,Andrew C. Kruse +14 more
TL;DR: Crystal structures elucidate how ligands select among signaling conformations of a G protein–coupled receptor and could provide a framework for the rational design of drugs that are more effective and have fewer side effects.
Journal ArticleDOI
Molecular Mechanism of Biased Signaling in a Prototypical G-protein-coupled Receptor
Carl-Mikael Suomivuori,Naomi R. Latorraca,Laura M. Wingler,Laura M. Wingler,Stephan Eismann,Matthew C. King,Alissa L. W. Kleinhenz,Alissa L. W. Kleinhenz,Alissa L. W. Kleinhenz,Meredith A. Skiba,Dean P. Staus,Dean P. Staus,Andrew C. Kruse,Robert J. Lefkowitz,Robert J. Lefkowitz,Ron O. Dror +15 more
TL;DR: In this article, the authors used extensive atomic-level molecular dynamics simulations to determine how arrestin bias and G protein bias arise at the angiotensin II type 1 receptor, which adopts two major signaling conformations, one couples almost exclusively to arrestin, whereas the other also couples effectively to a G protein.