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Chemistry

D-Index
67
Citations
13416
World Ranking
7063
National Ranking
2100

Research.com Recognitions

  • 1966 - Fellow of the American Association for the Advancement of Science (AAAS)

Overview

Winslow S. Caughey was affiliated with Colorado State University in the United States. Their career included contributions that earned recognition from the scientific community, notably being named a Fellow of the American Association for the Advancement of Science (AAAS) in 1966.

No data is available regarding specific research papers authored by Winslow S. Caughey or any frequent co-authors associated with their work.

The available information does not include details on frequent publication venues, book publications, main fields or subfields of study, or specific topics covered by their research. As such, no listing can be provided for these categories.

Winslow S. Caughey is deceased. The profile is based solely on the documented affiliation and the honor received during their career, reflecting a historical overview of their professional recognition.

Best Publications

  • Protein secondary structures in water from second-derivative amide I infrared spectra.

    Unknown

  • Secondary structure analysis of the scrapie-associated protein PrP 27-30 in water by infrared spectroscopy

    Byron W. Caughey;Aichun Dong;Kolari S. Bhat;Darwin Ernst

  • Mechanism of autooxidation for hemoglobins and myoglobins. Promotion of superoxide production by protons and anions.

    W J Wallace;R A Houtchens;J C Maxwell;W S Caughey

  • An infrared study of CO binding to heart cytochrome c oxidase and hemoglobin A. Implications re O2 reactions.

    S Yoshikawa;M G Choc;M C O'Toole;W S Caughey

  • An infrared study of bound carbon monoxide in the human red blood cell, isolated hemoglobin, and heme carbonyls.

    James O. Alben;Winslow S. Caughey

  • An infrared study of nitric oxide bonding to heme B and hemoglobin A. Evidence for inositol hexaphosphate induced cleavage of proximal histidine to iron bonds

    Unknown

  • Heme A of cytochrome c oxicase. Structure and properties: comparisons with hemes B, C, and S and derivatives.

    WS Caughey;GA Smythe;DH O'Keeffe;JE Maskasky

  • Substituted Deuteroporphyrins. I. Reactions at the Periphery of the Porphyrin Ring1

    Winslow S. Caughey;James O. Alben;Wilfred Y. Fujimoto;J. Lyndal York

  • Infrared methods for study of hemoglobin reactions and structures.

    Unknown

  • Mechanism for the autoxidation of hemoglobin by phenols, nitrite and "oxidant" drugs. Peroxide formation by one electron donation to bound dioxygen.

    William J. Wallace;Winslow S. Caughey

  • The mechanisms of hemoglobin autoxidation. Evidence for proton-assisted nucleophilic displacement of superoxide by anions.

    W.J. Wallace;J.C. Maxwell;W.S. Caughey

  • Redox-dependent changes in beta-extended chain and turn structures of cytochrome c in water solution determined by second derivative amide I infrared spectra.

    Unknown

  • Elucidation of the mode of binding of oxygen to iron in oxyhemoglobin by infrared spectroscopy

    C.H. Barlow;J.C. Maxwell;W.J. Wallace;W.S. Caughey

  • Investigations of cyanide as an infrared probe of hemeprotein ligand binding sites.

    S Yoshikawa;D H O'Keeffe;W S Caughey

  • NMR studies of low-spin ferric complexes of natural porphyrin derivatives. 1. Effect of peripheral substituents on the .pi. electronic asymmetry in biscyano complexes

    Gerd N. La Mar;David B. Viscio;Kevin M. Smith;W. S. Caughey

  • Far‐Infrared Magnetic Resonance in Fe(III) and Mn(III) Porphyrins, Myoglobin, Hemoglobin, Ferrichrome A, and Fe(III) Dithiocarbamates

    Unknown

  • Porphyrins. XIX. Tripdoublet and Quartet Luminescence in Cu and VO Complexes

    Martin Gouterman;Richard A. Mathies;Barry E. Smith;Winslow S. Caughey

  • Substituted deuteroporphyrins. III. Iron(II) derivatives. Reactions with oxygen and preparations from chloro- and methoxohemins

    James O. Alben;William H. Fuchsman;Charles A. Beaudreau;Winslow S. Caughey

  • Dynamic protein structures: infrared evidence for four discrete rapidly interconverting conformers at the carbon monoxide binding site of bovine heart myoglobin.

    Winslow S. Caughey;Hideo Shimada;Miles G. Choc;Melvin P. Tucker

  • Destabilizing Effects of Replacing a Surface Lysine of Cytochrome c with Aromatic Amino Acids: Implications for the Denatured State?

    Bruce E. Bowler;Kevin May;Tony Zaragoza;Peter York

  • Infrared evidence for the mode of binding of oxygen to iron of myoglobin from heart muscle.

    J.C. Maxwell;J.A. Volpe;C.H. Barlow;W.S. Caughey

  • The Crystal Structure and Molecular Stereochemistry of Methoxyiron (III) Mesoporphyrin-IX Dimethyl Ester1

    Unknown

  • Isoforms of yeast cytochrome c oxidase subunit V affect the binuclear reaction center and alter the kinetics of interaction with the isoforms of yeast cytochrome c.

    Larry A. Allen;Xiao-Jian Zhao;Winslow Caughey;Robert O. Poyton

  • Bovine heart cytochrome c oxidase preparations contain high affinity binding sites for magnesium as well as for zinc, copper, and heme iron.

    Ólőf Einarsdóttir;Winslow S. Caughey

  • Substituted Deuteroporphyrins. II. Substituent Effects on Electronic Spectra, Nitrogen Basicities, and Ligand Affinities*

    Winslow S. Caughey;Wilfred Y. Fujimoto;Barbara P. Johnson

  • Cytochrome c oxidase catalysis of the reduction of nitric oxide to nitrous oxide.

    Xiao-Jian Zhao;Vijaya Sampath;W. S. Caughey

  • Structure of carboxymyoglobin in crystals and in solution.

    Unknown

Frequent Co-Authors

Shinya Yoshikawa
Shinya Yoshikawa University of Hyogo
Masao Ikeda-Saito
Masao Ikeda-Saito Tohoku University
Gerd N. La Mar
Gerd N. La Mar University of California, Davis
Mark C. Manning
Mark C. Manning Colorado State University
Tomitake Tsukihara
Tomitake Tsukihara University of Hyogo
Robert W. Woody
Robert W. Woody Colorado State University
Jack L. Strominger
Jack L. Strominger Harvard University
Robert O. Poyton
Robert O. Poyton University of Colorado Boulder
Yuzuru Ishimura
Yuzuru Ishimura Keio University
Stanley F. Hayes
Stanley F. Hayes National Institutes of Health

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