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Chemistry

D-Index
43
Citations
7046
World Ranking
17206
National Ranking
4228

Overview

Mark S. Hargrove is affiliated with Iowa State University in the United States. Their research spans multiple disciplines including biochemistry, genetics, molecular biology, medicine, and agricultural and biological sciences.

The scientist's main fields of study comprise:

  • Biochemistry, Genetics and Molecular Biology
  • Medicine
  • Agricultural and Biological Sciences

Within these fields, their work covers several specialized subfields:

  • Cell Biology
  • Plant Science
  • Hematology
  • Molecular Biology
  • Inorganic Chemistry

The key topics explored in their publications include:

  • Hemoglobin structure and function
  • Heme Oxygenase-1 and Carbon Monoxide
  • Metal-Organic Frameworks: Synthesis and Applications
  • Plant responses to water stress
  • Legume Nitrogen Fixing Symbiosis
  • Platelet Disorders and Treatments
  • Blood groups and transfusion

Recent scientific papers authored or coauthored by Mark S. Hargrove include:

  • Plant hemoglobins: a journey from unicellular green algae to vascular plants, 2020, New Phytologist
  • Oxygen Generation via Water Splitting by a Novel Biogenic Metal Ion-Binding Compound, 2021, Applied and Environmental Microbiology
  • Refractory severe idiopathic thrombocytopenia and treatment challenges, 2023, Annals of Medicine and Surgery

The frequent coauthors associated with their research are:

  • Philip Dershwitz
  • Nathan Bandow
  • Jun-Won Yang
  • Jeremy D. Semrau
  • Marcus T. McEllistrem

Mark S. Hargrove's publications appear in venues such as:

  • Applied and Environmental Microbiology
  • New Phytologist
  • Annals of Medicine and Surgery

Best Publications

  • A Ubiquitously Expressed Human Hexacoordinate Hemoglobin

    James T. Trent;Mark S. Hargrove

  • Two hemoglobin genes in Arabidopsis thaliana: the evolutionary origins of leghemoglobins.

    B Trevaskis;R A Watts;C R Andersson;D J Llewellyn

  • Human neuroglobin, a hexacoordinate hemoglobin that reversibly binds oxygen

    James T. Trent;Richard A. Watts;Mark S. Hargrove

  • The Association Rate Constant for Heme Binding to Globin Is Independent of Protein Structure

    Mark S. Hargrove;Doug Barrick;John S. Olson

  • His64(E7)→Tyr apomyoglobin as a reagent for measuring rates of hemin dissociation

    M S Hargrove;E W Singleton;M L Quillin;L A Ortiz

  • The Stability of Holomyoglobin Is Determined by Heme Affinity

    Mark S. Hargrove;John S. Olson

  • Rice Hemoglobins (Gene Cloning, Analysis, and O2-Binding Kinetics of a Recombinant Protein Synthesized in Escherichia coli)

    R Arredondo-Peter;M S Hargrove;G Sarath;J F Moran

  • Crystal structure of a nonsymbiotic plant hemoglobin.

    Mark S Hargrove;Eric Allen Brucker;Boguslaw Stec;Gautam Sarath

  • Plants, humans and hemoglobins.

    Suman Kundu;James T Trent;Mark S Hargrove

  • His64(E7)–>Tyr apomyoglobin as a reagent for measuring rates of hemin dissociation.

    Unknown

  • NO Dioxygenase Activity in Hemoglobins Is Ubiquitous In Vitro, but Limited by Reduction In Vivo

    Benoit J. Smagghe;James T. Trent;Mark S. Hargrove

  • Stability of myoglobin: a model for the folding of heme proteins.

    Mark S. Hargrove;Szymon Krzywda;Anthony J. Wilkinson;Yi Dou

  • Quaternary structure regulates hemin dissociation from human hemoglobin.

    Mark S. Hargrove;Timothy Whitaker;John S. Olson;Rita J. Vali

  • STRUCTURAL FACTORS GOVERNING HEMIN DISSOCIATION FROM METMYOGLOBIN

    Mark S. Hargrove;and Anthony J. Wilkinson;John S. Olson

  • Structure and reactivity of hexacoordinate hemoglobins

    Smita Kakar;Federico G. Hoffman;Jay F. Storz;Marian Fabian

  • Review: Correlations between oxygen affinity and sequence classifications of plant hemoglobins

    Benoit J. Smagghe;Julie A. Hoy;Ryan Percifield;Suman Kundu

  • Spectral, Kinetic, and Thermodynamic Properties of Cu(I) and Cu(II) Binding by Methanobactin from Methylosinus trichosporium OB3b†

    Dong W. Choi;Corbin J. Zea;Young S. Do;Jeremy D. Semrau

  • Characterization of recombinant soybean leghemoglobin a and apolar distal histidine mutants.

    Mark S Hargrove;Jennifer K Barry;Eric Allen Brucker;Michael B Berry

  • The structure and function of plant hemoglobins.

    Julie A. Hoy;Mark S. Hargrove

  • Plant and cyanobacterial hemoglobins reduce nitrite to nitric oxide under anoxic conditions.

    Ryan Sturms;Alan A DiSpirito;Mark S Hargrove

  • A Flash Photolysis Method to Characterize Hexacoordinate Hemoglobin Kinetics

    Mark S. Hargrove

Frequent Co-Authors

John S. Olson
John S. Olson Rice University
Herbert J. Fromm
Herbert J. Fromm Iowa State University
Gautam Sarath
Gautam Sarath Agricultural Research Service
Jacob W. Petrich
Jacob W. Petrich Iowa State University
Randy H. Kardon
Randy H. Kardon University of Iowa
Alan A. DiSpirito
Alan A. DiSpirito Iowa State University
George N. Phillips
George N. Phillips Rice University
Elizabeth S. Dennis
Elizabeth S. Dennis Commonwealth Scientific and Industrial Research Organisation
Kiyoshi Nagai
Kiyoshi Nagai MRC Laboratory of Molecular Biology
William James Peacock
William James Peacock University of Technology Sydney

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