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G proteins: transducers of receptor-generated signals.
  • A. Gilman
  • Biology, Medicine
  • Annual review of biochemistry
  • 1987
This paper presents a meta-analysis of G Protein Interactions and its Foundations, which states that G Proteins are Law-Regulated and G Protein-Effector Interactions are Nonvolatile. Expand
Structure of RGS4 Bound to AlF4 −-Activated Giα1: Stabilization of the Transition State for GTP Hydrolysis
RGS4 appears to catalyze rapid hydrolysis of GTP primarily by stabilizing the switch regions of G(i alpha1), although the conserved Asn-128 from RGS4 could also play a catalytic role by interacting with the hydrolytic water molecule or the side chain of Gln-204. Expand
Complexity and diversity of mammalian adenylyl cyclases.
The discovery of new isoforms of mammalian adenylyl cyclase has revealed unanticipated mechanisms of regulation, including activation or inhibition by the G-protein beta gamma subunit complex, inhibition by G(o) alpha, inhibited by Ca2+, and phosphorylation by protein kinases C and A. Expand
Structures of active conformations of Gi alpha 1 and the mechanism of GTP hydrolysis.
AlF4- complexes formed by the G protein Gi alpha 1 demonstrate specific roles in transition-state stabilization for two highly conserved residues, suggesting a mechanism that may promote release of the beta gamma subunit complex when the alpha subunit is activated by GTP. Expand
Direct stimulation of the guanine nucleotide exchange activity of p115 RhoGEF by Galpha13.
The GTPase activities of two G protein alpha subunits, Galpha12 and Galpha13, are stimulated by the Rho guanine nucleotide exchange factor p115 RhoGEF, which can directly link heterotrimeric G proteinalpha subunits to regulation of Rho. Expand
Mammalian Ric-8A (Synembryn) Is a Heterotrimeric Gα Protein Guanine Nucleotide Exchange Factor*
Purification and biochemical characterization of recombinant Ric-8A revealed that it is a potent guanine nucleotide exchange factor for a subset of Gα proteins including Gαq, Gαi1, and Gαo, but not Gαs. Expand
Crystal structure of the catalytic domains of adenylyl cyclase in a complex with Gsalpha.GTPgammaS.
The crystal structure of a soluble, catalytically active form of adenylyl cyclase in a complex with its stimulatory heterotrimeric G protein alpha subunit (Gsalpha) and forskolin and structural elements important for substrate recognition and catalysis were identified. Expand
The structure of the G protein heterotrimer Giα1 β 1 γ 2
Altering in GDP binding in the heterotrimer (compared with alpha-GDP) explain stabilization of the inactive conformation of alpha by beta gamma, which is a circularized sevenfold beta propeller. Expand
p115 RhoGEF, a GTPase activating protein for Gα12 and Gα13
Members of the regulators of G protein signaling (RGS) family stimulate the intrinsic guanosine triphosphatase (GTPase) activity of the α subunits of certain heterotrimeric guanine nucleotide–bindingExpand
GAIP and RGS4 Are GTPase-Activating Proteins for the Gi Subfamily of G Protein α Subunits
Two RGS family members, GAIP and RGS4, are GTPase-activating proteins (GAPs), accelerating the rate of GTP hydrolysis by Gi alpha 1 at least 40-fold, consistent with their proposed role as negative regulators of G protein-mediated signaling. Expand