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Biology and Biochemistry

D-Index
84
Citations
38908
World Ranking
3240
National Ranking
1640

Overview

Rodney L. Levine is affiliated with the National Institutes of Health in the United States. Their research primarily spans the field of Biochemistry, Genetics, and Molecular Biology, with a notable focus on Molecular Biology and related subfields. The scientist's work is concentrated on topics such as redox biology and oxidative stress, mitochondrial function and pathology, receptor mechanisms and signaling, glutathione transferases and polymorphisms, ATP synthase and ATPases research, biotin and related studies, and sulfur compounds in biology.

Their recent publications reflect a range of studies in these areas. Notable papers include:

  • MICAL1 constrains cardiac stress responses and protects against disease by oxidizing CaMKII, 2020, Journal of Clinical Investigation
  • Oxidative stress-induced autonomous activation of the calcium/calmodulin-dependent kinase II involves disulfide formation in the regulatory domain, 2022, Journal of Biological Chemistry
  • Metabolic dependency mapping identifies Peroxiredoxin 1 as a driver of resistance to ATM inhibition, 2025, Redox Biology
  • Energy homeostasis is a conserved process: Evidence from Paracoccus denitrificans' response to acute changes in energy demand, 2021, PLoS ONE
  • Ndufaf2, a protein in mitochondrial complex I, interacts in vivo with methionine sulfoxide reductases, 2023, Redox Report

They frequently co-author publications with several researchers, including Geumsoo Kim, Yi He, Lo Lai, Jung Mi Lim, and Elizabeth D. Luczak.

The scientist's work has been published in multiple venues with repeated contributions to journals such as:

  • Journal of Biological Chemistry
  • Archives of Biochemistry and Biophysics
  • Free Radical Biology and Medicine
  • Journal of Clinical Investigation
  • Redox Biology

Best Publications

  • Determination of carbonyl content in oxidatively modified proteins.

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

  • CARBONYL ASSAYS FOR DETERMINATION OF OXIDATIVELY MODIFIED PROTEINS

    Rodney L. Levine;Joy A. Williams;Earl P. Stadtman;Emily Shacter

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

    E. R. Stadtman;R. L. Levine

  • Methionine residues as endogenous antioxidants in proteins

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

  • Carbonyl modified proteins in cellular regulation, aging, and disease,

    Rodney L Levine

  • Oxidative damage during aging targets mitochondrial aconitase

    Liang-Jun Yan;Rodney L. Levine;Rajindar S. Sohal

  • Detection and characterization of the product of hydroethidine and intracellular superoxide by HPLC and limitations of fluorescence

    Hongtao Zhao;Joy Joseph;Henry M. Fales;Edward A. Sokoloski

  • Oxidative modification of proteins during aging.

    Rodney L. Levine;Earl R. Stadtman

  • Conversion of amino acid residues in proteins and amino acid homopolymers to carbonyl derivatives by metal-catalyzed oxidation reactions.

    A Amici;R L Levine;L Tsai;E R Stadtman

  • Differential susceptibility of plasma proteins to oxidative modification: examination by western blot immunoassay.

    Emily Shacter;Joy A. Williams;Michael Lim;Rodney L. Levine

  • Glutamic and aminoadipic semialdehydes are the main carbonyl products of metal-catalyzed oxidation of proteins.

    Jesús R. Requena;Chien-Chung Chao;Rodney L. Levine;Earl R. Stadtman

  • Turnover of bacterial glutamine synthetase: oxidative inactivation precedes proteolysis

    Rodney L. Levine;Cynthia N. Oliver;Richard M. Fulks;Earl R. Stadtman

  • Methionine in proteins defends against oxidative stress

    Shen Luo;Rodney L. Levine

  • Oxidation of Methionine in Proteins: Roles in Antioxidant Defense and Cellular Regulation

    Rodney L. Levine;Jackob Moskovitz;Earl R. Stadtman

  • Methionine oxidation and aging

    Earl R. Stadtman;Holly Van Remmen;Arlan Richardson;Nancy B. Wehr

  • Oxidative modification of glutamine synthetase. I. Inactivation is due to loss of one histidine residue.

    R L Levine

  • Methionine residues may protect proteins from critical oxidative damage.

    Rodney L. Levine;Barbara S. Berlett;Jackob Moskovitz;Laurent Mosoni

  • Oxidation of methionine residues of proteins: biological consequences.

    Earl R. Stadtman;Jackob Moskovitz;Rodney L. Levine

  • Determination of carbonyl groups in oxidatively modified proteins by reduction with tritiated sodium borohydride

    Anke-G. Lenz;Ulrich Costabel;Shmuel Shaltiel;Rodney L. Levine

  • Oxidation of either methionine 351 or Methionine 358 in alpha-1-Antitrypsin causes loss of anti-neutrophil elastase activity

    Clifford Taggart;Daniel Cervantes-Laurean;Geumsoo Kim;Noel G. McElvaney

Frequent Co-Authors

Earl R. Stadtman
Earl R. Stadtman National Institutes of Health
Clifford C. Taggart
Clifford C. Taggart Queen's University Belfast
Joel Moss
Joel Moss National Institutes of Health
Noel G. McElvaney
Noel G. McElvaney Royal College of Surgeons in Ireland
Ad Bax
Ad Bax National Institutes of Health
Tracey A. Rouault
Tracey A. Rouault National Institutes of Health
Arlan Richardson
Arlan Richardson University of Oklahoma Health Sciences Center
Catherine M. Greene
Catherine M. Greene Royal College of Surgeons in Ireland
Rajindar S. Sohal
Rajindar S. Sohal University of Southern California
Anthony Wynshaw-Boris
Anthony Wynshaw-Boris Case Western Reserve University

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