2004 - Fellow of the American Academy of Arts and Sciences
1989 - Fellow of the American Association for the Advancement of Science (AAAS)
1988 - Member of the National Academy of Sciences
Biochemistry, Enzyme, Actin, Biophysics and Substrate are his primary areas of study. Biochemistry is closely attributed to Amyloid in his work. His work on Enzyme assay, Allosteric regulation and Enzyme catalysis as part of general Enzyme research is often related to Kinetic energy, thus linking different fields of science.
His work on Gelsolin is typically connected to Cytochalasin D and Cytochalasin as part of general Actin study, connecting several disciplines of science. While the research belongs to areas of Biophysics, Carl Frieden spends his time largely on the problem of Protein folding, intersecting his research to questions surrounding Fluorescence, Fluorescence correlation spectroscopy and Crystallography. Within one scientific family, Carl Frieden focuses on topics pertaining to Ligand under Substrate, and may sometimes address concerns connected to Substrate concentration, Isomerization and Metabolic regulation.
Carl Frieden focuses on Biochemistry, Stereochemistry, Enzyme, Biophysics and Crystallography. He regularly ties together related areas like Apolipoprotein E in his Biochemistry studies. Carl Frieden combines subjects such as Ligand, Mutant, Binding site and Active site with his study of Stereochemistry.
His work on Substrate and Cofactor as part of general Enzyme research is frequently linked to Phosphofructokinase and Kinetic energy, bridging the gap between disciplines. His work is dedicated to discovering how Biophysics, Actin are connected with Polymerization, Skeletal muscle and Saccharomyces cerevisiae and other disciplines. The concepts of his Crystallography study are interwoven with issues in Fluorine-19 NMR, Nuclear magnetic resonance spectroscopy, Protein secondary structure and Protein folding.
His primary scientific interests are in Biochemistry, Apolipoprotein E, Biophysics, Gene isoform and Protein structure. His Biochemistry research is multidisciplinary, incorporating perspectives in Hydrogen–deuterium exchange and Amyloid. His Apolipoprotein E study combines topics from a wide range of disciplines, such as Receptor, Cysteine and Mutant.
His Biophysics study combines topics in areas such as Protein folding, Folding, Reaction rate constant, Tetramer and Monomer. The various areas that Carl Frieden examines in his Protein structure study include Protein subunit and Circular dichroism. His Dissociation study incorporates themes from Lability, Isomerization and Enzyme.
His scientific interests lie mostly in Biochemistry, Biophysics, Fibril, Protein structure and Amyloid. His studies deal with areas such as Apolipoprotein E and Amyloid precursor protein as well as Biochemistry. The Biophysics study combines topics in areas such as Equilibrium constant, Circular dichroism, Protein folding, Reaction rate constant and Dimer.
Carl Frieden interconnects Crystallography, Chemical physics and Folding in the investigation of issues within Protein folding. His research in Fibril intersects with topics in Adhesion, Molecular biology, Huntingtin, Polyglutamine tract and Exon. His work carried out in the field of Amyloid brings together such families of science as P3 peptide, Plasma protein binding, Protein subunit, Protein filament and Beta sheet.
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Analysis of numerical methods for computer simulation of kinetic processes: development of KINSIM--a flexible, portable system.
Bruce A. Barshop;Richard F. Wrenn;Carl Frieden.
Analytical Biochemistry (1983)
Kinetic Aspects of Regulation of Metabolic Processes: THE HYSTERETIC ENZYME CONCEPT
Journal of Biological Chemistry (1970)
Barry R. Goldin;Carl Frieden.
Current Topics in Cellular Regulation (1971)
ApoE influences amyloid-β (Aβ) clearance despite minimal apoE/Aβ association in physiological conditions
Philip B. Verghese;Joseph M. Castellano;Kanchan Garai;Yinong Wang.
Proceedings of the National Academy of Sciences of the United States of America (2013)
Amyloid seeds formed by cellular uptake, concentration, and aggregation of the amyloid-beta peptide
Xiaoyan Hu;Scott L. Crick;Guojun Bu;Carl Frieden.
Proceedings of the National Academy of Sciences of the United States of America (2009)
Glutamic dehydrogenase. I. The effect of coenzyme on the sedimentation velocity and kinetic behavior.
Journal of Biological Chemistry (1959)
Slow Transitions and Hysteretic Behavior in Enzymes
Annual Review of Biochemistry (1979)
Glutamic dehydrogenase. II. The effect of various nucleotides on the association-dissociation and kinetic properties.
Journal of Biological Chemistry (1959)
Actin polymerization. The mechanism of action of cytochalasin D.
D W Goddette;C Frieden.
Journal of Biological Chemistry (1986)
GLUTAMATE DEHYDROGENASE. V. THE RELATION OF ENZYME STRUCTURE TO THE CATALYTIC FUNCTION
Journal of Biological Chemistry (1963)
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