World's Best Scientists 2026 revealed!

D-Index & Metrics

Chemistry

D-Index
66
Citations
16715
World Ranking
7234
National Ranking
2148

Biology and Biochemistry

D-Index
66
Citations
16659
World Ranking
8615
National Ranking
3869

Research.com Recognitions

  • 1973 - Member of the National Academy of Sciences

Overview

Lester J. Reed was affiliated with The University of Texas at Austin in the United States. The academic career of Reed encompassed various research undertakings within their field, although specific research papers and topics are not detailed in available records.

Reed received recognition by being named a Member of the National Academy of Sciences in 1973, indicating a significant standing within the scientific community at that time.

While detailed information on Reed's publications, including individual papers or books, is not available, the scientist's career spanned a variety of scientific inquiries as reflected by their institutional affiliation and membership in a national scientific body.

As Lester J. Reed is deceased, their contributions to science are recorded as part of the historical academic legacy of The University of Texas at Austin.

Best Publications

  • The remarkable structural and functional organization of the eukaryotic pyruvate dehydrogenase complexes.

    Z H Zhou;D B McCarthy;C M O'Connor;L J Reed

  • α-KETO ACID DEHYDROGENASE COMPLEXES, X. REGULATION OF THE ACTIVITY OF THE PYRUVATE DEHYDROGENASE COMPLEX FROM BEEF KIDNEY MITOCHONDRIA BY PHOSPHORYLATION AND DEPHOSPHORYLATION

    Tracy C. Linn;Flora H. Pettit;Lester J. Reed

  • Crystalline α-Lipoic Acid: A Catalytic Agent Associated with Pyruvate Dehydrogenase

    Lester J. Reed;Betty G. DeBusk;I. C. Gunsalus;Carl S. Hornberger

  • [12] α-ketoglutarate dehydrogenase complex from Escherichia coli

    Lester J. Reed;Barid B. Mukherjee

  • α-KETO ACID DEHYDROGENASE COMPLEXES, XI. COMPARATIVE STUDIES OF REGULATORY PROPERTIES OF THE PYRUVATE DEHYDROGENASE COMPLEXES FROM KIDNEY, HEART, AND LIVER MITOCHONDRIA

    Tracy C. Linn;Flora H. Pettit;Ferdinand Hucho;Lester J. Reed

  • Regulation of pyruvate dehydrogenase kinase and phosphatase by acetyl-CoA/CoA and NADH/NAD ratios.

    Flora H. Pettit;John W. Pelley;Lester J. Reed

  • Sites of phosphorylation on pyruvate dehydrogenase from bovine kidney and heart

    Stephen J. Yeaman;Eldridge T. Hutcheson;Thomas E. Roche;Flora H. Pettit

  • α-Keto acid dehydrogenase complexes

    Cecilio R. Barrera;Genshin Namihira;Lynn Hamilton;Petr Munk

  • Keto acid dehydrogenase complexes. XV. Purification and properties of the component enzymes of the pyruvate dehydrogenase complexes from bovine kidney and heart.

    Tracy C. Linn;John W. Pelley;Flora H. Pettit;Ferdinand Hucho

  • A Trail of Research from Lipoic Acid to α-Keto Acid Dehydrogenase Complexes

    Lester J. Reed

  • Structure-function relationships in dihydrolipoamide acyltransferases.

    Unknown

  • Purification and characterization of branched chain α-keto acid dehydrogenase complex of bovine kidney

    Flora H. Pettit;Stephen J. Yeaman;Lester J. Reed

  • Studies on the nature and reactions of protein-bound lipoic acid.

    Lester J. Reed;Masahiko Koike;Mark E. Levitch;Franklin R. Leach

  • alpha-Keto acid dehydrogenation complexes. IV. Resolution and reconstitution of the Escherichia coli pyruvate dehydrogenation complex.

    Masahiko Koike;Masahiko Koike;Lester J. Reed;Lester J. Reed;William R. Carroll;William R. Carroll

  • Keto acid dehydrogenase complexes. XVII. Kinetic and regulatory properties of pyruvate dehydrogenase kinase and pyruvate dehydrogenase phosphatase from bovine kidney and heart

    Ferdinand Hucho;Douglas D. Randall;Thomas E. Roche;Michael W. Burgett

  • alpha-Keto acid dehydrogenation complexes. I. Purification and properties of pyruvate and alpha-ketoglutarate dehydrogenation complexes of Escherichia coli.

    Masahiko Koike;Masahiko Koike;Lester J. Reed;Lester J. Reed;William R. Carroll;William R. Carroll

  • [50] Purification and resolution of the pyruvate dehydrogenase complex (Escherichia coli)

    Lester J. Reed;Charles R. Willms

  • Function of calcium ions in pyruvate dehydrogenase phosphatase activity.

    Flora H. Pettit;Thomas E. Roche;Lester J. Reed

  • Regulation of mammalian pyruvate dehydrogenase complex by a phosphorylation-dephosphorylation cycle.

    Lester J. Reed

  • α-Keto Acid Dehydrogenase Complexes XX. A KINETIC STUDY OF THE PYRUVATE DEHYDROGENASE COMPLEX FROM BOVINE KIDNEY

    C. Stanley Tsai;Michael W. Burgett;Lester J. Reed

  • Regulation of Mammalian Pyruvate and Branched-Chain α-Keto Acid Dehydrogenase Complexes by Phosphorylation — Dephosphorylation

    Lester J. Reed;Zahi Damuni;Margaret L. Merryfield

Frequent Co-Authors

Thomas E. Roche
Thomas E. Roche Kansas State University
Karen S. Browning
Karen S. Browning The University of Texas at Austin
Stephen J. Yeaman
Stephen J. Yeaman Newcastle University
Ferdinand Hucho
Ferdinand Hucho Freie Universität Berlin
Z. Hong Zhou
Z. Hong Zhou University of California, Los Angeles
Timothy S. Baker
Timothy S. Baker University of California, San Diego
Vincent du Vigneaud
Vincent du Vigneaud Cornell University
David J. DeRosier
David J. DeRosier Brandeis University
Mulchand S. Patel
Mulchand S. Patel University at Buffalo, State University of New York
Gordon H. Dixon
Gordon H. Dixon University of Calgary

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