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Chemistry

D-Index
57
Citations
12278
World Ranking
11035
National Ranking
3019

Overview

Charles H. Williams is affiliated with the University of Michigan-Ann Arbor in the United States. Their research spans across several fields primarily within Biochemistry, Genetics and Molecular Biology, and Medicine. The main focus areas of their work include Molecular Biology, Pulmonary and Respiratory Medicine, Cancer Research, Genetics, and Sociology and Political Science.

Williams' work addresses a variety of significant scientific topics. Among these are Ferroptosis and cancer prognosis, RNA modifications and cancer, ATP Synthase and ATPases research, Education Systems and Policy, Youth Education and Societal Dynamics, Congenital heart defects research, and Cardiomyopathy and Myosin studies.

The scientist has contributed to multiple publications over the years. Key papers featuring their involvement include:

  • "GPR68-ATF4 signaling is a novel prosurvival pathway in glioblastoma activated by acidic extracellular microenvironment" (2024) in Experimental Hematology and Oncology
  • "The E3 ubiquitin ligase component, Cereblon, is an evolutionarily conserved regulator of Wnt signaling" (2021) in Nature Communications
  • "Should we overcome the resistance to bioelectrical impedance in heart failure?" (2020) in Expert Review of Medical Devices
  • "The USP46 complex deubiquitylates LRP6 to promote Wnt/β-catenin signaling" (2023) in Nature Communications
  • "PEGylated PLGA Nanoparticle Delivery of Eggmanone for T Cell Modulation: Applications in Rheumatic Autoimmunity" (2020) in International Journal of Nanomedicine

Frequent collaborators in Williams' research include:

  • Charles C. Hong
  • Leif R. Neitzel
  • James A. Perry
  • Mark Pendras
  • Alex Gyftopoulos

The publication venues where Williams has frequently contributed include Circulation, Nature Communications, The FASEB Journal, Circulation Research, and After Dinner Conversation.

In addition to journal articles, Williams has also contributed to book publications. Notably, they published a book titled "Current Strategies in Biotechnology and Bioresource Technology Vol. 2" (2020) with Book Publisher International, a part of SCIENCEDOMAIN International.

Best Publications

  • Microsomal triphosphopyridine nucleotide-cytochrome c reductase of liver.

    Charles H. Williams;Henry Kamin

  • [92] The preparation and properties of microsomal TPNH-cytochrome c reductase from pig liver

    Bettie Sue Siler Masters;Charles H. Williams;Henry Kamin

  • On the reaction mechanism of yeast glutathione reductase.

    Vincent Massey;Charles H. Williams

  • Human Placenta Thioredoxin Reductase: ISOLATION OF THE SELENOENZYME, STEADY STATE KINETICS, AND INHIBITION BY THERAPEUTIC GOLD COMPOUNDS *

    Stephan Gromer;L. David Arscott;Charles H. Williams;R. Heiner Schirmer

  • Thioredoxin reductase two modes of catalysis have evolved.

    C H Williams;L D Arscott;S Müller;B W Lennon

  • Twists in Catalysis: Alternating Conformations of Escherichia coli Thioredoxin Reductase

    Brett W. Lennon;Charles H. Williams;Charles H. Williams;Martha L. Ludwig

  • The mechanism of thioredoxin reductase from human placenta is similar to the mechanisms of lipoamide dehydrogenase and glutathione reductase and is distinct from the mechanism of thioredoxin reductase from Escherichia coli

    L. David Arscott;Stephan Gromer;R. Heiner Schirmer;Katja Becker

  • STUDIES ON THE MECHANISM OF MICROSOMAL TRIPHOSPHOPYRIDINE NUCLEOTIDE-CYTOCHROME C REDUCTASE.

    Bettie Sue Siler Masters;Bettie Sue Siler Masters;Bettie Sue Siler Masters;Henry Kamin;Henry Kamin;Henry Kamin;Quentin H. Gibson;Quentin H. Gibson;Quentin H. Gibson;Charles H. Williams;Charles H. Williams;Charles H. Williams

  • Crystal structure of Escherichia coli thioredoxin reductase refined at 2 A resolution. Implications for a large conformational change during catalysis.

    Gabriel Waksman;Talluru S.R. Krishna;Charles H. Williams;John Kuriyan

  • Active sites of thioredoxin reductases: Why selenoproteins?

    Stephan Gromer;Linda Johansson;Holger Bauer;L. David Arscott

  • Convergent evolution of similar function in two structurally divergent enzymes.

    John Kuriyan;John Kuriyan;T. S. R. Krishna;T. S. R. Krishna;Lim Wong;Brian Guenther

  • Mechanism and structure of thioredoxin reductase from Escherichia coli.

    Charles H. Williams

  • Acyl-coenzyme A dehydrogenase from pig kidney. Purification and properties.

    Colin Thorpe;Rowena G. Matthews;Charles H. Williams

  • Recombinant Plasmodium falciparum glutathione reductase is inhibited by the antimalarial dye methylene blue.

    P.M Färber;L.D Arscott;C.H Williams;K Becker

  • Lipoamide dehydrogenase, glutathione reductase, thioredoxin reductase, and thioredoxin.

    Charles H. Williams;Giuliana Zanetti;L. David Arscott;Joan K. McAllister

  • High-performance liquid-chromatographic separation and fluorescence measurement of biogenic amines in plasma, urine, and tissue.

    T P Davis;C W Gehrke;T D Cunningham;K C Kuo

  • Crystal structure of reduced thioredoxin reductase from Escherichia coli: structural flexibility in the isoalloxazine ring of the flavin adenine dinucleotide cofactor.

    Brett W. Lennon;Charles H. Williams;Charles H. Williams;Martha L. Ludwig

  • Measurement of the oxidation-reduction potentials for two-electron and four-electron reduction of lipoamide dehydrogenase from pig heart.

    Rowena G. Matthews;Charles H. Williams

  • Role of a hydrophobic polypeptide in the N-terminal region of NADPH-cytochrome P-450 reductase in complex formation with P-450lm

    Shaun D. Black;Shaun D. Black;John S. French;John S. French;Charles H. Williams;Charles H. Williams;Minor J. Coon;Minor J. Coon

  • Reactivity of thioredoxin as a protein thiol-disulfide oxidoreductase

    Zhiyong Cheng;Jinfeng Zhang;David P. Ballou;Charles H. Williams

  • Accelerated Substrate Cycling of Fructose-6-phosphate in the Muscle of Malignant Hyperthermic Pigs

    M. G. Clark;C. H. Williams;W. F. Pfeifer;D. P. Bloxham

  • A method for titrating oxygen-sensitive organic redox systems with reducing agents in solution.

    B.D. Burleigh;G.P. Foust;C.H. Williams

  • Use of a site-directed triple mutant to trap intermediates: demonstration that the flavin C(4a)-thiol adduct and reduced flavin are kinetically competent intermediates in mercuric ion reductase.

    Susan M. Miller;Vincent Massey;David Ballou;Charles H. Williams

  • An anaerobic titration assembly for spectrophotometric use

    G. P. Foust;G. P. Foust;B. D. Burleigh;B. D. Burleigh;Stephen G. Mayhew;Stephen G. Mayhew;C. H. Williams;C. H. Williams

Frequent Co-Authors

Vincent Massey
Vincent Massey University of Michigan–Ann Arbor
David P. Ballou
David P. Ballou University of Michigan–Ann Arbor
Katja Becker
Katja Becker University of Giessen
R. Heiner Schirmer
R. Heiner Schirmer Heidelberg University
Minor J. Coon
Minor J. Coon University of Michigan–Ann Arbor
Rowena G. Matthews
Rowena G. Matthews University of Michigan–Ann Arbor
John Kuriyan
John Kuriyan Vanderbilt University
Christopher T. Walsh
Christopher T. Walsh Stanford University
Mike O'Donnell
Mike O'Donnell Rockefeller University
Martha L. Ludwig
Martha L. Ludwig University of Michigan–Ann Arbor

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