World's Best Scientists 2026 revealed!

D-Index & Metrics

Chemistry

D-Index
78
Citations
19572
World Ranking
3858
National Ranking
1231

Biology and Biochemistry

D-Index
80
Citations
20286
World Ranking
4143
National Ranking
2031

Research.com Recognitions

  • 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

Overview

Carl Frieden is affiliated with Washington University in St. Louis in the United States. Their research contributions span primarily the fields of Biochemistry, Genetics and Molecular Biology, and Medicine, with significant work in subfields such as Molecular Biology, Physiology, Immunology, Computational Theory and Mathematics, and Biophysics.

The scientific topics frequently addressed by Frieden include Alzheimer's disease research and treatments, Protein Structure and Dynamics, Computational Drug Discovery Methods, Advanced Fluorescence Microscopy Techniques, Neuroinflammation and Neurodegeneration Mechanisms, Inflammation biomarkers and pathways, and Cholesterol and Lipid Metabolism.

Frieden's publication record includes papers in notable journals and venues, with key recent works as follows:

  • APOE3 -Jacksonville (V236E) variant reduces self-aggregation and risk of dementia, 2021, Science Translational Medicine
  • Functional insights from biophysical study of TREM2 interactions with apoE and Aβ 1-42, 2020, Alzheimer s & Dementia
  • Apolipoprotein E4 has extensive conformational heterogeneity in lipid-free and lipid-bound forms, 2023, Proceedings of the National Academy of Sciences
  • Bioorthogonal Chemistry Enables Single-Molecule FRET Measurements of Catalytically Active Protein Disulfide Isomerase, 2020, ChemBioChem
  • Functional insights from biophysical study of TREM2 interactions with ApoE and Aβ1-42, 2020, bioRxiv (Cold Spring Harbor Laboratory)

Frequent publication venues include:

  • Biophysical Journal
  • bioRxiv (Cold Spring Harbor Laboratory)
  • Science Translational Medicine
  • Alzheimer s & Dementia
  • Proceedings of the National Academy of Sciences

The scientist collaborates regularly with several coauthors, including:

  • Melissa D. Stuchell-Brereton
  • Berevan Baban
  • Gregory T. DeKoster
  • Andrea Soranno
  • Maxwell I. Zimmerman

Carl Frieden has been recognized with several distinctions in their career, including election as a Member of the National Academy of Sciences in 1988, as a Fellow of the American Association for the Advancement of Science (AAAS) in 1989, and as a Fellow of the American Academy of Arts and Sciences in 2004.

Best Publications

  • 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

  • Kinetic Aspects of Regulation of Metabolic Processes: THE HYSTERETIC ENZYME CONCEPT

    Carl Frieden

  • ApoE influences amyloid-β (Aβ) clearance despite minimal apoE/Aβ association in physiological conditions

    Philip B. Verghese;Joseph M. Castellano;Kanchan Garai;Yinong Wang

  • L-Glutamate Dehydrogenases*

    Barry R. Goldin;Carl Frieden

  • Amyloid seeds formed by cellular uptake, concentration, and aggregation of the amyloid-beta peptide

    Xiaoyan Hu;Scott L. Crick;Guojun Bu;Carl Frieden

  • Glutamic dehydrogenase. I. The effect of coenzyme on the sedimentation velocity and kinetic behavior.

    Carl Frieden

  • Slow Transitions and Hysteretic Behavior in Enzymes

    Carl Frieden

  • Actin polymerization. The mechanism of action of cytochalasin D.

    D W Goddette;C Frieden

  • Fluorescence correlation spectroscopy shows that monomeric polyglutamine molecules form collapsed structures in aqueous solutions

    Scott L. Crick;Murali Jayaraman;Carl Frieden;Ronald Wetzel

  • Glutamic dehydrogenase. II. The effect of various nucleotides on the association-dissociation and kinetic properties.

    Carl Frieden

  • GLUTAMATE DEHYDROGENASE. V. THE RELATION OF ENZYME STRUCTURE TO THE CATALYTIC FUNCTION

    Carl Frieden

  • Treatment of Enzyme Kinetic Data I. THE EFFECT OF MODIFIERS ON THE KINETIC PARAMETERS OF SINGLE SUBSTRATE ENZYMES

    Carl Frieden

  • Protein-Protein Interaction and Enzymatic Activity

    Carl Frieden

  • Analysis of progress curves by simulations generated by numerical integration.

    C T Zimmerle;C Frieden

  • Myoadenylate deaminase deficiency.

    Jack B. Shumate;Richard Katnik;Martha Ruiz;Kenneth Kaiser

  • Glutamic dehydrogenase. III. The order of substrate addition in the enzymatic reaction.

    Carl Frieden

  • Unmasking the roles of N- and C-terminal flanking sequences from exon 1 of huntingtin as modulators of polyglutamine aggregation

    Scott L. Crick;Kiersten M. Ruff;Kanchan Garai;Carl Frieden

  • Protein aggregation processes: In search of the mechanism.

    Carl Frieden

  • Climate Change and the Integrity of Science

    Jennifer Sills;P. H. Gleick;R. M. Adams;R. M. Amasino

  • PapD-like chaperones provide the missing information for folding of pilin proteins

    Michelle M. Barnhart;Jerome S. Pinkner;Gabriel E. Soto;Frederic G. Sauer

Frequent Co-Authors

Elliot L. Elson
Elliot L. Elson Washington University in St. Louis
Michael L. Gross
Michael L. Gross Washington University in St. Louis
Scott J. Hultgren
Scott J. Hultgren Washington University in St. Louis
Jerome S. Pinkner
Jerome S. Pinkner Washington University in St. Louis
Paul E. Bock
Paul E. Bock Vanderbilt University
David M. Holtzman
David M. Holtzman Washington University in St. Louis
Leonard J. Banaszak
Leonard J. Banaszak University of Minnesota
Jeffrey I. Gordon
Jeffrey I. Gordon Washington University in St. Louis
John A. Cooper
John A. Cooper Washington University in St. Louis
Jin-Moo Lee
Jin-Moo Lee Washington University in St. Louis

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