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Chemistry

D-Index
54
Citations
8056
World Ranking
12842
National Ranking
3398

Research.com Recognitions

  • 1997 - Fellow of the American Association for the Advancement of Science (AAAS)
  • 1991 - Fellow of the American Society of Mechanical Engineers
  • Member of the Association of American Physicians
  • Member of the Association of American Physicians
  • Member of the Association of American Physicians
  • Member of the Association of American Physicians
  • Member of the Association of American Physicians
  • Member of the Association of American Physicians

Overview

Michael F. Dunn is affiliated with the University of California, Riverside in the United States. Their research spans multiple areas within Agricultural and Biological Sciences and Biochemistry, Genetics, and Molecular Biology. The scientist's work predominantly focuses on subfields such as Plant Science, Molecular Biology, Materials Chemistry, Pollution, and Ecology.

The central themes in Michael F. Dunn's research include Legume Nitrogen Fixing Symbiosis, Enzyme Structure and Function, Biochemical and Molecular Research, Polyamine Metabolism and Applications, Protein Structure and Dynamics, Pesticide and Herbicide Environmental Studies, and Weed Control and Herbicide Applications.

Recent publications authored or co-authored by Michael F. Dunn include:

  • The Biosynthesis and Functions of Polyamines in the Interaction of Plant Growth-Promoting Rhizobacteria with Plants, 2023, Plants
  • Imaging active site chemistry and protonation states: NMR crystallography of the tryptophan synthase α-aminoacrylate intermediate, 2022, Proceedings of the National Academy of Sciences
  • Diversity, properties and functions of bacterial arginases, 2021, FEMS Microbiology Reviews
  • Glyphosate-remediation potential of selected plant species in artificial wetlands, 2021, The Science of The Total Environment
  • Polyamines produced by Sinorhizobium meliloti Rm8530 contribute to symbiotically relevant phenotypes ex planta and to nodulation efficiency on alfalfa, 2020, Microbiology

Michael F. Dunn has collaborated frequently with several researchers, including Leonard J. Mueller, E. Hilario, Rittik K. Ghosh, Víctor A. Becerra-Rivera, and Jacob B. Holmes.

The scientist's work has appeared repeatedly in certain academic journals, with multiple publications in Microbiology, The Science of The Total Environment, Preprints.org, Journal of Visualized Experiments, and FEMS Microbiology Reviews.

Throughout their career, Michael F. Dunn has received several recognitions, including being named a Fellow of the American Association for the Advancement of Science (AAAS) in 1997 and a Fellow of the American Society of Mechanical Engineers in 1991. They also hold membership in the Association of American Physicians.

Best Publications

  • Zinc–Ligand Interactions Modulate Assembly and Stability of the Insulin Hexamer – A Review

    Michael F. Dunn

  • Major roles of isocitrate lyase and malate synthase in bacterial and fungal pathogenesis.

    Unknown

  • The tryptophan synthase bienzyme complex transfers indole between the alpha- and beta-sites via a 25-30 A long tunnel.

    Michael F. Dunn;Valentin Aguilar;Peter Brzovic;William F. Drewe

  • Comparison of solution structural flexibility and zinc binding domains for insulin, proinsulin, and miniproinsulin.

    Niels C. Kaarsholm;Hui Chong Ko;Michael F. Dunn

  • Tryptophan synthase: the workings of a channeling nanomachine.

    Michael F. Dunn;Dimitri Niks;Huu Ngo;Thomas R.M. Barends

  • Mechanistic studies on equine liver alcohol dehydrogenase. I. The stoichiometry relationship of the coenzyme binding sites to the catalytic sites active in the reduction of aromatic aldehydes in the transient state.

    Sidney A. Bernhard;Michael F. Dunn;Pier L. Luisi;Poul Schack

  • Allosteric regulation of substrate channeling and catalysis in the tryptophan synthase bienzyme complex.

    Michael F. Dunn

  • Protein architecture, dynamics and allostery in tryptophan synthase channeling

    Peng Pan;Eilika Woehl;Michael F. Dunn

  • Detection and identification of intermediates in the reaction of L-serine with Escherichia coli tryptophan synthase via rapid-scanning ultraviolet-visible spectroscopy.

    William Frederick Drewe;Michael F. Dunn

  • On the relationship of zinc ion to the structure and function of the 7S nerve growth factor protein.

    Scott E. Pattison;Michael F. Dunn

  • Role of the proximal ligand in peroxidase catalysis. Crystallographic, kinetic, and spectral studies of cytochrome c peroxidase proximal ligand mutants.

    Kalidip Choudhury;Munirathiram Sundaramoorthy;A. Hickman;T. Yonetani

  • Characterization of precrystallization aggregation of canavalin by dynamic light scattering

    W. Kadima;A. McPherson;M.F. Dunn;F.A. Jurnak

  • Insulin-metal ion interactions: the binding of divalent cations to insulin hexamers and tetramers and the assembly of insulin hexamers.

    Frederick D. Coffman;Michael F. Dunn

  • Mechanisms of Stabilization of the Insulin Hexamer through Allosteric Ligand Interactions

    S Rahuel-Clermont;C A French;N C Kaarsholm;M F Dunn

  • Allosteric interactions coordinate catalytic activity between successive metabolic enzymes in the tryptophan synthase bienzyme complex.

    Peter S. Brzović;Khiet Ngo;Michael F. Dunn

  • Reaction mechanism of Escherichia coli cystathionine gamma-synthase: direct evidence for a pyridoxamine derivative of vinylglyoxylate as a key intermediate in pyridoxal phosphate dependent gamma-elimination and gamma-replacement reactions.

    Peter Brzovic;Elizabeth Litzenberger Holbrook;Ronald C. Greene;Michael F. Dunn

  • Characterization of the reaction of L-serine and indole with Escherichia coli tryptophan synthase via rapid-scanning ultraviolet-visible spectroscopy

    William Frederick Drewe;Michael F. Dunn

  • Spectroscopic signatures of the T to R conformational transition in the insulin hexamer.

    M. Roy;M. Roy;M. L. Brader;R. W.-K. Lee;N. C. Kaarsholm

  • Evidence that mutations in a loop region of the alpha-subunit inhibit the transition from an open to a closed conformation in the tryptophan synthase bienzyme complex.

    Peter S. Brzovic;Yoshihiro Sawa;C. Craig Hyde;Edith W. Miles

  • X-ray structure of an unusual Ca2+ site and the roles of Zn2+ and Ca2+ in the assembly, stability, and storage of the insulin hexamer.

    Christopher P. Hill;Zbigniew Dauter;Zbigniew Dauter;Eleanor J. Dodson;Guy G. Dodson

  • Rapid kinetic evidence for adduct formation between the substrate analog p-nitroso-N,N-dimethylaniline and reduced nicotinamide-adenine dinucleotide during enzymic reduction.

    M. F. Dunn;Sidney A. Bernhard

Frequent Co-Authors

Edith Wilson Miles
Edith Wilson Miles National Institutes of Health
Ilme Schlichting
Ilme Schlichting Max Planck Society
Robert S. Phillips
Robert S. Phillips University of Georgia
Paul F. Cook
Paul F. Cook University of Oklahoma
Guy Dodson
Guy Dodson University of York
Christopher P. Hill
Christopher P. Hill University of Utah
Alexander McPherson
Alexander McPherson University of California, Irvine
Edward N. Baker
Edward N. Baker University of Auckland
Wolfgang Baumeister
Wolfgang Baumeister Max Planck Society
Thomas M. Laue
Thomas M. Laue University of New Hampshire

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