Author
Alfred G. Gilman
Other affiliations: University of Virginia, York University, University of Texas System ...read more
Bio: Alfred G. Gilman is an academic researcher from University of Texas Southwestern Medical Center. The author has contributed to research in topics: G protein & Cyclase. The author has an hindex of 114, co-authored 204 publications receiving 50866 citations. Previous affiliations of Alfred G. Gilman include University of Virginia & York University.
Topics: G protein, Cyclase, Gs alpha subunit, G alpha subunit, Protein subunit
Papers published on a yearly basis
Papers
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TL;DR: 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.
Abstract: PERSPECTIVES AND SUMMARY .............................................................. 615 HISTORY ............................................................................................... 616 INDIVIDUAL G PROTEINS: FUNCTIONS AND MOLECULAR ENTITIES .......... 617 Criteria .for Involvement of a G Protein ..................................................... 618 Functions Regulated by G Proteins ........................................................... 619 Molecular Entities and Structure .............................................................. 622 LIGAND-G PROTEIN TERACTIONS ........................................................ 631 LIGAND-REGULATED PROTEIN-PROTEIN TERACTIONS ........................... 634 Receptor-G Protein Interactions ............................................................... 634 G Protein-Effector Interactions ................................................................ 638 G PROTEII~I-MEMBRANE INTERACTIONS .................................................. 643 COVALENT MODIFICATION F G PROTEINS ............................................ 644
6,160 citations
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TL;DR: A simple and sensitive assay for adenosine 3':5'-cyclic monophosphate (cAMP) has been developed that is based on competition for protein binding of the nucleotide, presumably to a cAMP-dependent protein kinase.
Abstract: A simple and sensitive assay for adenosine 3′:5′-cyclic monophosphate (cAMP) has been developed that is based on competition for protein binding of the nucleotide, presumably to a cAMP-dependent protein kinase. The nucleotide-protein complex is adsorbed on a cellulose ester filter. Assay conditions are such that a binding constant approaching 10-9 M is obtained, and the assay is thus sensitive to 0.05-0.10 pmol of cAMP.
3,048 citations
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TL;DR: It is clear that detailed understanding of the mechanism of regulation of CAMP synthesis will soon be achieved from study of the interactions of purified components that have been reconstituted in lipid bilayers of defined composition.
1,645 citations
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TL;DR: The structure of the G protein heterotrimer Gi alpha 1(GDP)beta 1 gamma 2 (at 2.3 A) reveals two nonoverlapping regions of contact between alpha and beta, an extended interface between beta and nearly all of gamma, and limited interaction of alpha with gamma as mentioned in this paper.
1,071 citations
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TL;DR: G protein beta gamma subunits have been found to have regulatory effects on certain types of adenylyl cyclase, and interactions suggest mechanisms for communication between distinct signal-transducing pathways.
Abstract: Heterotrimeric guanine nucleotide-binding regulatory proteins (G proteins) dissociate into guanosine triphosphate (GTP)-bound alpha subunits and a complex of beta and gamma subunits after interaction with receptors. The GTP-alpha subunit complex activates appropriate effectors, such as adenylyl cyclase, retinal phosphodiesterase, phospholipase C, and ion channels. G protein beta gamma subunits have been found to have regulatory effects on certain types of adenylyl cyclase. In the presence of Gs alpha, the alpha subunit of the G protein that activates adenylyl cyclase, one form of adenylyl cyclase was inhibited by beta gamma, some forms were activated by beta gamma, and some forms were not affected by beta gamma. These interactions suggest mechanisms for communication between distinct signal-transducing pathways.
1,048 citations
Cited by
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TL;DR: Current structural and cell biological data suggest models for how integrins transmit signals between their extracellular ligand binding adhesion sites and their cytoplasmic domains, which link to the cytoskeleton and to signal transduction pathways.
8,275 citations
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TL;DR: Mutation of the active site of caspase-9 attenuated the activation of cazase-3 and cellular apoptotic response in vivo, indicating that casp enzyme-9 is the most upstream member of the apoptotic protease cascade that is triggered by cytochrome c and dATP.
7,231 citations
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TL;DR: A deletion of three base pairs that results in the omission of a phenylalanine residue at the center of the first predicted nucleotide-binding domain was detected in CF patients.
Abstract: Overlapping complementary DNA clones were isolated from epithelial cell libraries with a genomic DNA segment containing a portion of the putative cystic fibrosis (CF) locus, which is on chromosome 7 Transcripts, approximately 6500 nucleotides in size, were detectable in the tissues affected in patients with CF The predicted protein consists of two similar motifs, each with (i) a domain having properties consistent with membrane association and (ii) a domain believed to be involved in ATP (adenosine triphosphate) binding A deletion of three base pairs that results in the omission of a phenylalanine residue at the center of the first predicted nucleotide-binding domain was detected in CF patients
6,731 citations
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TL;DR: Diacylglycerol operates within the plane of the membrane to activate protein kinase C, whereas inositol trisphosphate is released into the cytoplasm to function as a second messenger for mobilizing intracellular calcium.
Abstract: There has recently been rapid progress in understanding receptors that generate intracellular signals from inositol lipids. One of these lipids, phosphatidylinositol 4,5-bisphosphate, is hydrolysed to diacylglycerol and inositol trisphosphate as part of a signal transduction mechanism for controlling a variety of cellular processes including secretion, metabolism, phototransduction and cell proliferation. Diacylglycerol operates within the plane of the membrane to activate protein kinase C, whereas inositol trisphosphate is released into the cytoplasm to function as a second messenger for mobilizing intracellular calcium.
5,712 citations
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TL;DR: Two novel neuropeptides are identified, both derived from the same precursor by proteolytic processing, that bind and activate two closely related (previously) orphan G protein-coupled receptors in the hypothalamus of rats.
5,162 citations