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Chemistry

D-Index
124
Citations
75850
World Ranking
410
National Ranking
177

Biology and Biochemistry

D-Index
124
Citations
74759
World Ranking
521
National Ranking
325

Research.com Recognitions

  • 1991 - Welch Award in Chemistry, Robert A. Welch Foundation
  • 1979 - US President's National Medal of Science "For seminal contributions to understanding of the energy metabolism of anaerobic bacteria and for elucidation of major mechanisms whereby the rates of metabolic processes are finely matched to the requirements of the living cell.", Presented by President Carter at a White House Ceremony on January 14, 1980.
  • 1969 - Member of the National Academy of Sciences

Overview

Earl R. Stadtman was affiliated with the National Institutes of Health in the United States. Their research career encompassed significant contributions to biochemistry, particularly focusing on the energy metabolism of anaerobic bacteria. This work involved clarifying major mechanisms that regulate the rates of metabolic processes according to the requirements of living cells.

Throughout their career, Stadtman earned recognition through several awards. These included the Welch Award in Chemistry from the Robert A. Welch Foundation in 1991. In 1979, they received the US President's National Medal of Science, with a citation highlighting their work "for seminal contributions to understanding of the energy metabolism of anaerobic bacteria and for elucidation of major mechanisms whereby the rates of metabolic processes are finely matched to the requirements of the living cell." This award was presented by President Carter at a White House ceremony on January 14, 1980. Additionally, Stadtman was made a member of the National Academy of Sciences in 1969.

Details on specific papers, co-authors, publication venues, and book publications have not been documented in the available data.

Stadtman's research would have had an impact in fields related to metabolism and enzymology, contributing foundational knowledge to how biochemical processes are regulated in anaerobic organisms.

Best Publications

  • Determination of carbonyl content in oxidatively modified proteins.

    Rodney L. Levine;Donita Garland;Cynthia N. Oliver;Adolfo Amici

  • Protein oxidation and aging

    Earl R Stadtman

  • Protein Oxidation in Aging, Disease, and Oxidative Stress

    Barbara S. Berlett;Earl R. Stadtman

  • Free radical-mediated oxidation of free amino acids and amino acid residues in proteins.

    E. R. Stadtman;R. L. Levine

  • Reactive oxygen-mediated protein oxidation in aging and disease.

    Earl R. Stadtman;Barbara S. Berlett

  • Excess brain protein oxidation and enzyme dysfunction in normal aging and in Alzheimer disease.

    C D Smith;J M Carney;P E Starke-Reed;C N Oliver

  • Metal ion-catalyzed oxidation of proteins: Biochemical mechanism and biological consequences

    Earl R. Stadtman

  • Immunohistochemical detection of 4-hydroxynonenal protein adducts in Parkinson disease.

    Asako Yoritaka;Nobutaka Hattori;Koji Uchida;Masashi Tanaka

  • Oxidation of free amino acids and amino acid residues in proteins by radiolysis and by metal-catalyzed reactions.

    Unknown

  • Age-related changes in oxidized proteins.

    Unknown

  • Methionine residues as endogenous antioxidants in proteins

    Rodney L. Levine;Laurent Mosoni;Barbara S. Berlett;Earl R. Stadtman

  • Metal-catalyzed oxidation of proteins. Physiological consequences.

    E R Stadtman;C N Oliver

  • Oxidative damage to brain proteins, loss of glutamine synthetase activity, and production of free radicals during ischemia/reperfusion-induced injury to gerbil brain.

    C N Oliver;P E Starke-Reed;E R Stadtman;G J Liu

  • Protein oxidation in aging and age-related diseases.

    Earl R. Stadtman

  • Reversible oxidation and inactivation of the tumor suppressor PTEN in cells stimulated with peptide growth factors

    Jaeyul Kwon;Seung-Rock Lee;Kap-Seok Yang;Younghee Ahn

  • Regulation of glutamine synthetase. I. Purification and properties of glutamine synthetase from Escherichia coli.

    C.A. Woolfolk;B. Shapiro;E.R. Stadtman

  • Methionine sulfoxide reductase (MsrA) is a regulator of antioxidant defense and lifespan in mammals.

    Jackob Moskovitz;Shoshana Bar-Noy;Wesley M. Williams;Jesus Requena

  • Regulation of glutamine synthetase. XII. Electron microscopy of the enzyme from Escherichia coli.

    Unknown

  • Covalent attachment of 4-hydroxynonenal to glyceraldehyde-3-phosphate dehydrogenase. A possible involvement of intra- and intermolecular cross-linking reaction.

    K Uchida;E R Stadtman

  • Modification of histidine residues in proteins by reaction with 4-hydroxynonenal.

    Koji Uchida;E. R. Stadtman

  • A gain-of-function of an amyotrophic lateral sclerosis-associated Cu,Zn-superoxide dismutase mutant: An enhancement of free radical formation due to a decrease in Km for hydrogen peroxide

    M B Yim;J H Kang;H S Yim;H S Kwak

  • Inactivation of key metabolic enzymes by mixed-function oxidation reactions: Possible implication in protein turnover and ageing

    Laura Fucci;Cynthia N. Oliver;Minor J. Coon;Earl R. Stadtman

  • Oxidative modification of proteins during aging.

    Rodney L. Levine;Earl R. Stadtman

Frequent Co-Authors

Rodney L. Levine
Rodney L. Levine National Institutes of Health
Sue Goo Rhee
Sue Goo Rhee Ewha Womans University
Koji Uchida
Koji Uchida University of Tokyo
Stanley B. Prusiner
Stanley B. Prusiner University of California, San Francisco
Robert A. Floyd
Robert A. Floyd Oklahoma Medical Research Foundation
Wayne B. Anderson
Wayne B. Anderson National Center for Biotechnology Information
Bertrand Friguet
Bertrand Friguet Sorbonne University
Thressa C. Stadtman
Thressa C. Stadtman National Institutes of Health
Shinya Toyokuni
Shinya Toyokuni Nagoya University
Hiroshi Hiai
Hiroshi Hiai Kyoto University

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