Helix Dipole Movement and Conformational Variability Contribute to Allosteric GDP Release in Gαi Subunits,-Reference-Cited by-同舟云学术

Helix Dipole Movement and Conformational Variability Contribute to Allosteric GDP Release in Gαi Subunits,

Published:2009-02-17 Issue:12 Volume:48 Page:2630-2642
ISSN:0006-2960
Container-title:Biochemistry
language:en
Short-container-title:Biochemistry

Author:

Preininger Anita M.¹,Funk Michael A.¹,Oldham William M.¹,Meier Scott M.¹,Johnston Christopher A.¹,Adhikary Suraj¹,Kimple Adam J.¹,Siderovski David P.¹,Hamm Heidi E.¹,Iverson Tina M.¹

Affiliation:

1. Departments of Pharmacology, Biological Sciences, and Biochemistry, Vanderbilt University Medical Center, Nashville, Tennessee 37232-6600, and Department of Pharmacology, University of North Carolina School of Medicine, Chapel Hill, North Carolina 27599-7365

Publisher

American Chemical Society (ACS)

Subject

Biochemistry

Link

https://pubs.acs.org/doi/pdf/10.1021/bi801853a

Reference60 articles.

1. Structural basis of function in heterotrimeric G proteins

2. How receptors talk to trimeric G proteins

3. Heterotrimeric G protein activation by G-protein-coupled receptors

4. Receptor-Mediated Activation of Heterotrimeric G-Proteins: Current Structural Insights

5. The Guanine Nucleotide-Binding Switch in Three Dimensions

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