2008 - Distinguished Scientist Award, American Heart Association
1992 - Nobel Prize for their discoveries concerning reversible protein phosphorylation as a biological regulatory mechanism
1991 - Welch Award in Chemistry, Robert A. Welch Foundation
1989 - Albert Lasker Award for Basic Medical Research, Lasker Foundation
1978 - Canada Gairdner International Award
1973 - Member of the National Academy of Sciences
1966 - Fellow of John Simon Guggenheim Memorial Foundation
Biochemistry, Protein kinase A, Molecular biology, Kinase and Cell biology are his primary areas of study. His study in Phosphorylase kinase, Glycogen phosphorylase, Mitogen-activated protein kinase kinase, Enzyme and Threonine is done as part of Biochemistry. His research in Phosphorylase kinase intersects with topics in Adenosine triphosphate and Skeletal muscle.
His Protein kinase A research is multidisciplinary, incorporating elements of Protein structure, Glycogen synthase and Adenosine. His Molecular biology study integrates concerns from other disciplines, such as Casein kinase 2, cDNA library, Peptide sequence, Phosphorylation and Serine/threonine-specific protein kinase. In his study, Isozyme is strongly linked to Protein subunit, which falls under the umbrella field of Kinase.
His primary areas of investigation include Biochemistry, Protein kinase A, Molecular biology, Cell biology and Kinase. His biological study deals with issues like Skeletal muscle, which deal with fields such as Phosphorylase b and Adenosine triphosphate. His Protein kinase A research integrates issues from Threonine, Protein subunit and GSK-3.
His Molecular biology study also includes
His main research concerns Cell biology, Protein kinase A, Molecular biology, MAPK/ERK pathway and Biochemistry. In his study, Actin, Chemotaxis and Colforsin is inextricably linked to Platelet-derived growth factor receptor, which falls within the broad field of Cell biology. To a larger extent, Edwin G. Krebs studies Kinase with the aim of understanding Protein kinase A.
His Molecular biology study combines topics from a wide range of disciplines, such as Epidermal growth factor, Kinase activity, Protein tyrosine phosphatase, Phosphorylation and Fibroblast growth factor. His MAPK/ERK pathway research focuses on Apoptosis and how it relates to B-cell receptor. Edwin G. Krebs works mostly in the field of Biochemistry, limiting it down to concerns involving Insulin Receptor Substrate Proteins and, occasionally, IRS2 and Insulin receptor substrate.
Edwin G. Krebs focuses on Cell biology, Protein kinase A, MAPK/ERK pathway, Molecular biology and Signal transduction. Edwin G. Krebs interconnects B-cell receptor and Platelet-derived growth factor receptor in the investigation of issues within Cell biology. His Protein kinase A research includes themes of Eukaryotic Initiation Factor-4E, GSK-3, Forskolin, Platelet-derived growth factor and Type 2 diabetes.
His work carried out in the field of Molecular biology brings together such families of science as Cyclin-dependent kinase 4, Cyclin-dependent kinase 2, Mitogen-activated protein kinase kinase, CDC2 Protein Kinase and Phosphorylation. Phosphorylation is a subfield of Biochemistry that Edwin G. Krebs explores. His Signal transduction research includes elements of Endocrinology and Insulin receptor.
This overview was generated by a machine learning system which analysed the scientist’s body of work. If you have any feedback, you can contact us here.
The MAPK signaling cascade.
Rony Seger;Edwin G. Krebs.
The FASEB Journal (1995)
An Adenosine 3',5'-Monophosphate-dependant Protein Kinase from Rabbit Skeletal Muscle
D. A. Walsh;John P. Perkins;Edwin G. Krebs.
Journal of Biological Chemistry (1968)
Protein Serine/Threonine Kinases
Arthur M. Edelman;Donald K. Blumenthal;Edwin G. Krebs.
Annual Review of Biochemistry (1987)
Purification and Characterization of a Protein Inhibitor of Adenosine 3',5'-Monophosphate-dependent Protein Kinases
Donal A. Walsh;Charles D. Ashby;Carmen Gonzalez;Dianne Calkins.
Journal of Biological Chemistry (1971)
Purification and properties of rabbit skeletal muscle adenosine 3',5'-monophosphate-dependent protein kinases.
Erwin M. Reimann;Donal A. Walsh;Edwin G. Krebs.
Journal of Biological Chemistry (1971)
Role of multiple basic residues in determining the substrate specificity of cyclic AMP-dependent protein kinase.
B E Kemp;D J Graves;E Benjamini;E G Krebs.
Journal of Biological Chemistry (1977)
The isolation and crystallization of rabbit skeletal muscle phosphorylase b.
Edmond H. Fischer;Edwin G. Krebs.
Journal of Biological Chemistry (1958)
PURIFICATION AND PROPERTIES OF RABBIT SKELETAL MUSCLE PHOSPHORYLASE B KINASE.
Edwin G. Krebs;David S. Love;Gloria E. Bratvold;Kenneth A. Trayser.
Biochemistry (1964)
[43] Preparation of homogeneous cyclic AMP-dependent protein kinase(s) and its subunits from rabbit skeletal muscle
J.A. Beavo;P.J. Bechtel;E.G. Krebs.
Methods in Enzymology (1974)
Rapid Membrane Effects of Steroids in Neuroblastoma Cells: Effects of Estrogen on Mitogen Activated Protein Kinase Signalling Cascade and c-fos Immediate Early Gene Transcription
Jyoti J. Watters;Jean S. Campbell;Matthew J. Cunningham;Edwin G. Krebs.
Endocrinology (1997)
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