World's Best Scientists 2026 revealed!

D-Index & Metrics

Chemistry

D-Index
49
Citations
8425
World Ranking
14838
National Ranking
3788

Biology and Biochemistry

D-Index
50
Citations
8720
World Ranking
17663
National Ranking
7247

Overview

Gary Cecchini is affiliated with the University of California, San Francisco in the United States. Their research primarily focuses on biochemistry, genetics, and molecular biology, with a strong emphasis on molecular biology as the dominant subfield. Additional areas of study include biochemistry, physiology, genetics, and ecology.

The scientist's work covers diverse topics such as:

  • RNA and protein synthesis mechanisms
  • Mitochondrial function and pathology
  • Eicosanoids and hypertension pharmacology
  • Bacterial genetics and biotechnology
  • Bacteriophages and microbial interactions
  • Protein structure and dynamics
  • Ubiquitin and proteasome pathways

Recent publications demonstrate ongoing contributions to the field, including the following papers:

  • The roles of SDHAF2 and dicarboxylate in covalent flavinylation of SDHA, the human complex II flavoprotein (2020), published in Proceedings of the National Academy of Sciences
  • An evolving view of complex II-noncanonical complexes, megacomplexes, respiration, signaling, and beyond (2023), published in Journal of Biological Chemistry
  • CryoEM structures reveal how the bacterial flagellum rotates and switches direction (2024), published in Nature Microbiology
  • Determination of Flavin Potential in Proteins by Xanthine/Xanthine Oxidase Method (2020), published in BIO-PROTOCOL
  • CryoEM structure of a post-assembly MS-ring reveals plasticity in stoichiometry and conformation (2023), published in PLoS ONE

Frequent co-authors collaborating with Gary Cecchini include T.M. Iverson, Elena Maklashina, Pankaj Sharma, Prashant K. Singh, and Markus Voehler. These collaborations highlight a network of research in related biochemical and molecular biology topics.

The scientist frequently publishes in the Journal of Biological Chemistry, with three publications there, alongside contributions to Proceedings of the National Academy of Sciences, Nature Microbiology, BIO-PROTOCOL, and PLoS ONE. This distribution shows a presence in journals focused on biological chemistry and molecular biology research.

Best Publications

  • Architecture of succinate dehydrogenase and reactive oxygen species generation.

    Victoria Yankovskaya;Rob Horsefield;Susanna Törnroth;César Luna-Chavez;César Luna-Chavez

  • Function and structure of complex II of the respiratory chain

    Gary Cecchini

  • Structure of the Escherichia coli fumarate reductase respiratory complex.

    Tina M. Iverson;César Luna-Chavez;Gary Cecchini;Douglas C. Rees

  • Succinate dehydrogenase and fumarate reductase from Escherichia coli.

    Gary Cecchini;Imke Schröder;Robert P Gunsalus;Elena Maklashina;Elena Maklashina

  • Structural and Computational Analysis of the Quinone-binding Site of Complex II (Succinate-Ubiquinone Oxidoreductase) A MECHANISM OF ELECTRON TRANSFER AND PROTON CONDUCTION DURING UBIQUINONE REDUCTION

    Rob Horsefield;Victoria Yankovskaya;Graham Sexton;William Whittingham

  • Anaerobic Expression of Escherichia coli Succinate Dehydrogenase: Functional Replacement of Fumarate Reductase in the Respiratory Chain during Anaerobic Growth

    Elena Maklashina;Deborah A. Berthold;Gary Cecchini

  • Chemotactic activity of the lipid peroxidation product 4-hydroxynonenal and homologous hydroxyalkenals.

    Curzio M;Esterbauer H;Di Mauro C;Cecchini G

  • Fumarate reductase mutants of Escherichia coli that lack covalently bound flavin.

    M. Blaut;K. Whittaker;A. Valdovinos;B. A. C. Ackrell

  • Electron-transfer mechanisms through biological redox chains in multicenter enzymes.

    Lars J.C. Jeuken;Anne K. Jones;Stephen K. Chapman;Gary Cecchini

  • A novel intracellular isoform of matrix metalloproteinase-2 induced by oxidative stress activates innate immunity.

    David H. Lovett;Rajeev Mahimkar;Robert L. Raffai;Leslie Cape

  • Crystallographic studies of the Escherichia coli quinol-fumarate reductase with inhibitors bound to the quinol-binding site.

    Tina M. Iverson;César Luna-Chavez;César Luna-Chavez;Laura R. Croal;Gary Cecchini;Gary Cecchini

  • Electron transfer and catalytic control by the iron-sulfur clusters in a respiratory enzyme, E. coli fumarate reductase.

    Janette M Hudson;Kerensa Heffron;Violetta Kotlyar;Yelizaveta Sher

  • Regulation of amino acid transport activity and growth rate of animal cells in culture.

    Dale L. Oxender;Mary Lee;Gary Cecchini

  • Structure of Escherichia coli succinate:quinone oxidoreductase with an occupied and empty quinone-binding site.

    Jonathan Ruprecht;Victoria Yankovskaya;Elena Maklashina;Elena Maklashina;So Iwata

  • [3Fe-4S] to [4Fe-4S] cluster conversion in Escherichia coli fumarate reductase by site-directed mutagenesis.

    Annamaria Manodori;Gary Cecchini;Imke Schroder;Robert P. Gunsalus

  • A Structural Model for Binding of the Serine-Rich Repeat Adhesin GspB to Host Carbohydrate Receptors

    Tasia M. Pyburn;Barbara A. Bensing;Yan Q. Xiong;Bruce J. Melancon

  • Escherichia coli fumarate reductase frdC and frdD mutants. Identification of amino acid residues involved in catalytic activity with quinones.

    David J. Westenberg;Robert P. Gunsalus;Brian A. C. Ackrell;Harry J. Sices

  • The quinone-binding and catalytic site of complex II.

    Elena Maklashina;Gary Cecchini;Gary Cecchini

  • Enzyme electrokinetics: energetics of succinate oxidation by fumarate reductase and succinate dehydrogenase.

    Christophe Léger;Kerensa Heffron;Harsh R. Pershad;Elena Maklashina

  • Effect of anoxia/reperfusion on the reversible active/de-active transition of NADH–ubiquinone oxidoreductase (complex I) in rat heart

    Elena Maklashina;Yelizaveta Sher;Hui-Zhong Zhou;Mary O Gray

Frequent Co-Authors

Joel H. Weiner
Joel H. Weiner University of Alberta
Robert P. Gunsalus
Robert P. Gunsalus University of California, Los Angeles
So Iwata
So Iwata Kyoto University
Michael K. Johnson
Michael K. Johnson University of Georgia
Andrei D. Vinogradov
Andrei D. Vinogradov Lomonosov Moscow State University
Fraser A. Armstrong
Fraser A. Armstrong University of Oxford
Michael Eisenbach
Michael Eisenbach Weizmann Institute of Science
David H. Lovett
David H. Lovett University of California, San Francisco
Douglas C. Rees
Douglas C. Rees California Institute of Technology
Thomas P. Singer
Thomas P. Singer University of California, San Francisco

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