World's Best Scientists 2026 revealed!

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Chemistry

D-Index
129
Citations
73524
World Ranking
340
National Ranking
155

Biology and Biochemistry

D-Index
141
Citations
79229
World Ranking
259
National Ranking
176

Research.com Recognitions

  • 1994 - Nobel Prize for their discovery of G-proteins and the role of these proteins in signal transduction in cells
  • 1989 - Fellow of the American Association for the Advancement of Science (AAAS)
  • 1985 - Member of the National Academy of Sciences
  • 1964 - Fellow of the American Association for the Advancement of Science (AAAS)

Overview

Alfred G. Gilman was affiliated with The University of Texas Southwestern Medical Center in the United States. Throughout their career, Gilman contributed to the scientific understanding of cellular signaling mechanisms and related topics.

Gilman was awarded several recognitions, including the Nobel Prize in 1994 for their discovery of G-proteins and the role of these proteins in signal transduction in cells. Additionally, they were a Fellow of the American Association for the Advancement of Science (AAAS) twice, first in 1964 and later in 1989. Gilman was also a Member of the National Academy of Sciences, elected in 1985.

Further details about their research publications, frequent co-authors, specific fields and subfields of study, as well as book publications, were not available.

Best Publications

  • G PROTEINS: TRANSDUCERS OF RECEPTOR-GENERATED SIGNALS

    Alfred G. Gilman

  • A Protein Binding Assay for Adenosine 3′:5′-Cyclic Monophosphate

    Alfred G. Gilman

  • G proteins and dual control of adenylate cyclase

    Alfred G. Gilman

  • Type-Specific Regulation of Adenylyl Cyclase by G Protein βγ Subunits

    Wei Jen Tang;Alfred G. Gilman

  • The structure of the G protein heterotrimer Giα1β1γ2

    Mark A. Wall;David E. Coleman;Ethan Lee;Jorge A. Iñiguez-Lluhi

  • Biochemical properties of hormone-sensitive adenylate cyclase.

    E. M. Ross;A. G. Gilman

  • Crystal Structure of the Catalytic Domains of Adenylyl Cyclase in a Complex with Gsα·GTPγS

    John J. G. Tesmer;Roger K. Sunahara;Alfred G. Gilman;Stephen R. Sprang

  • Complexity and Diversity of Mammalian Adenylyl Cyclases

    Roger K. Sunahara;Carmen W. Dessauer;Alfred G. Gilman

  • Structures of active conformations of Gi alpha 1 and the mechanism of GTP hydrolysis.

    David E. Coleman;Albert M. Berghuis;Ethan Lee;Maurine E. Linder

  • GAIP and RGS4 Are GTPase-Activating Proteins for the Gi Subfamily of G Protein α Subunits

    David M Berman;Thomas M Wilkie;Alfred G Gilman

  • p115 RhoGEF, a GTPase activating protein for Gα12 and Gα13

    Tohru Kozasa;Xuejun Jiang;Matthew J. Hart;Pamela M. Sternweis

  • Direct Stimulation of the Guanine Nucleotide Exchange Activity of p115 RhoGEF by Gα13

    Matthew J. Hart;Xuejun Jiang;Tohru Kozasa;William Roscoe

  • MAMMALIAN MEMBRANE-BOUND ADENYLYL CYCLASES

    Ronald Taussig;Alfred G. Gilman

  • Structure of RGS4 Bound to AlF4−-Activated Giα1: Stabilization of the Transition State for GTP Hydrolysis

    John J.G. Tesmer;David M. Berman;Alfred G. Gilman;Stephen R. Sprang

  • Protein kinase C phosphorylates the inhibitory guanine-nucleotide-binding regulatory component and apparently suppresses its function in hormonal inhibition of adenylate cyclase.

    Toshiaki Katada;Alfred G. Gilman;Yasuhiro Watanabe;Silvia Bauer

  • Adenylyl cyclase amino acid sequence: possible channel- or transporter-like structure.

    John Krupinski;Françoise Coussen;Françoise Coussen;Heather A. Bakalyar;Wei Jen Tang

  • G proteins

    Unknown

  • Aluminum: a requirement for activation of the regulatory component of adenylate cyclase by fluoride.

    Paul C. Sternweis;Alfred G. Gilman

  • Cyclic Adenosine Monophosphate and Alteration of Chinese Hamster Ovary Cell Morphology: a Rapid, Sensitive In Vitro Assay for the Enterotoxins of Vibrio cholerae and Escherichia coli

    Richard L. Guerrant;Laurence L. Brunton;Terry C. Schnaitman;Lionel I. Rebhun

  • G protein involvement in receptor-effector coupling.

    P J Casey;A G Gilman

  • Identification of the predominant substrate for ADP-ribosylation by islet activating protein.

    G M Bokoch;T Katada;J K Northup;E L Hewlett

Frequent Co-Authors

Paul C. Sternweis
Paul C. Sternweis The University of Texas Southwestern Medical Center
Stephen R. Sprang
Stephen R. Sprang University of Montana
John K. Northup
John K. Northup National Institutes of Health
Elliott M. Ross
Elliott M. Ross The University of Texas Southwestern Medical Center
Patrick J. Casey
Patrick J. Casey National University of Singapore
John J. G. Tesmer
John J. G. Tesmer Purdue University West Lafayette
Allyn C. Howlett
Allyn C. Howlett Wake Forest University
John R. Hepler
John R. Hepler Emory University
Roger K. Sunahara
Roger K. Sunahara University of California, San Diego
Michael Freissmuth
Michael Freissmuth Medical University of Vienna

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