M
Michael L. Bernard
Researcher at Ochsner Medical Center
Publications - 39
Citations - 1236
Michael L. Bernard is an academic researcher from Ochsner Medical Center. The author has contributed to research in topics: Atrial fibrillation & Heterotrimeric G protein. The author has an hindex of 12, co-authored 35 publications receiving 1120 citations. Previous affiliations of Michael L. Bernard include Medical University of South Carolina & University of Queensland.
Papers
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Journal ArticleDOI
Receptor-independent activators of heterotrimeric g-protein signaling pathways
Aya Takesono,Mary J. Cismowski,Catalina Ribas,Michael L. Bernard,Peter Chung,Starr Hazard,Emir Duzic,Stephen M. Lanier +7 more
TL;DR: AGS proteins provide unexpected mechanisms for input to heterotrimeric G-protein signaling pathways and may also serve as novel binding partners for Gα and Gβγ that allow the subunits to subserve functions that do not require initialheterotrimer formation.
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The State of the Art: Atrial Fibrillation Epidemiology, Prevention, and Treatment.
Daniel P. Morin,Daniel P. Morin,Michael L. Bernard,Christopher Madias,Paul A. Rogers,Sudarone Thihalolipavan,N.A. Mark Estes +6 more
TL;DR: This "state-of-the-art" review provides a comprehensive update on the understanding of AF in the world today, contemporary therapeutic options, and directions of ongoing and future study.
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Selective Interaction of AGS3 with G-proteins and the Influence of AGS3 on the Activation State of G-proteins
TL;DR: AGS3 and related proteins provide unexpected mechanisms for coordination of G-protein signaling pathways and provide an initial approach to define the role of AGS3 in mammalian signal processing.
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Stabilization of the GDP-bound conformation of Gialpha by a peptide derived from the G-protein regulatory motif of AGS3.
Yuri K. Peterson,Michael L. Bernard,Hongzheng Ma,Starr Hazard,Stephen G. Graber,Stephen M. Lanier +5 more
TL;DR: The AGS3-GPR motif presents an opportunity for selective control of Giα- and Gβγ−regulated effector systems, and the GPR motif allows for alternative modes of signal input to G-protein signaling systems.
Journal ArticleDOI
AGS3 Inhibits GDP Dissociation from Gα Subunits of the Gi Family and Rhodopsin-dependent Activation of Transducin *
Michael Natochin,Brad Lester,Yuri K. Peterson,Michael L. Bernard,Stephen M. Lanier,Nikolai O. Artemyev +5 more
TL;DR: The results suggest that proteins containing GPR motifs, in addition to their potential role as G protein-coupled receptor-independent activators of Gβγ signaling pathways, act as GDP dissociation inhibitors and negatively regulate the activation of a G protein by a Gprotein-cOUpled receptor.