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William Atkins

William Atkins

· Professor, Medicinal Chemistry

University of Washington · Medicinal Chemistry Graduate Program

Active 1958–2023

h-index37
Citations4.9k
Papers1279 last 5y
Funding$73.7M

Academic metrics are sourced from OpenAlex and public funding records; values may differ from Google Scholar.

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About

Dr. William M. Atkins earned a Masters Degree in Pharmacology from Harvard University in 1983 and a Ph.D. in Biochemistry from the University of Illinois at Urbana-Champaign in 1988. He performed postdoctoral research in the Department of Chemistry at The Pennsylvania State University as an NIH Kirschstein Postdoctoral Fellow from 1988 to 1991. Dr. Atkins has been a faculty member at the University of Washington since 1991 and served as the Sidney D. Nelson Professor and Chair of Medicinal Chemistry from 2016 to 2025. His research focuses on the enzymology of detoxification enzymes and drug metabolism, with particular emphasis on biophysical mechanisms. He has been awarded NIH grants for research on enzyme systems including Cytochrome P450s, Glutathione S-transferases, and the P-glycoprotein efflux transporter. Recent research efforts include the characterization of nanoparticles for drug delivery and therapeutic antibody drug conjugates. Dr. Atkins serves on international conference committees and review panels, and is a member of editorial boards for scientific journals.

Research topics

  • Chemistry
  • Biochemistry
  • Biology
  • Computer Science
  • Biophysics
  • Computational biology
  • Computational chemistry
  • Stereochemistry

Selected publications

  • Considerations for the Design of Antibody-Based Therapeutics

    Journal of Pharmaceutical Sciences · 2019-06-04 · 288 citations

    reviewOpen accessSenior author

    Antibody-based proteins have become an important class of biologic therapeutics, due in large part to the stability, specificity, and adaptability of the antibody framework. Indeed, antibodies not only have the inherent ability to bind both antigens and endogenous immune receptors but also have proven extremely amenable to protein engineering. Thus, several derivatives of the monoclonal antibody format, including bispecific antibodies, antibody-drug conjugates, and antibody fragments, have demon…

    PublisherOA PDFDOI

  • Heme Binding Biguanides Target Cytochrome P450-Dependent Cancer Cell Mitochondria

    Cell chemical biology · 2017-09-14 · 52 citations

    articleOpen access
    PublisherOA PDFDOI

  • Conformational dynamics of P-glycoprotein in lipid nanodiscs and detergent micelles reveal complex motions on a wide time scale

    Journal of Biological Chemistry · 2018-03-06 · 45 citations

    articleOpen accessSenior authorCorresponding

    P-glycoprotein (P-gp) is a highly substrate-promiscuous efflux transporter that plays a critical role in drug disposition. P-gp utilizes ATP hydrolysis by nucleotide-binding domains (NBDs) to drive transitions between inward-facing (IF) conformations that bind drugs and outward-facing (OF) conformations that release them to the extracellular solution. However, the details of the protein dynamics within either macroscopic IF or OF conformation remain uncharacterized, and the functional role of lo…

    PublisherOA PDFDOI

  • Mechanisms of promiscuity among drug metabolizing enzymes and drug transporters

    FEBS Journal · 2019-10-30 · 43 citations

    reviewOpen access1st authorCorresponding

    Detoxication, or ‘drug‐metabolizing’, enzymes and drug transporters exhibit remarkable substrate promiscuity and catalytic promiscuity. In contrast to substrate‐specific enzymes that participate in defined metabolic pathways, individual detoxication enzymes must cope with substrates of vast structural diversity, including previously unencountered environmental toxins. Presumably, evolution selects for a balance of ‘adequate’ k cat / K M values for a wide range of substrates, rather than optimizi…

    PublisherOA PDFDOI

  • Dynamics and Location of the Allosteric Midazolam Site in Cytochrome P4503A4 in Lipid Nanodiscs

    Biochemistry · 2020 · 37 citations

    Senior authorCorresponding

    Promiscuous and allosteric drug interactions with cytochrome P450 3A4 (CYP3A4) are ubiquitous but incompletely understood at the molecular level. A classic allosteric CYP3A4 drug interaction includes the benzodiazepine midazolam (MDZ). MDZ exhibits homotropic and heterotropic allostery when metabolized to 1'-hydroxy and 4-hydroxy metabolites in varying ratios. The combination of hydrogen-deuterium exchange mass spectrometry (HDX-MS) and Gaussian accelerated molecular dynamics (GaMD) simulations…

    PublisherOA PDFDOI

Recent grants

Frequent coauthors

  • Michael J. Dabrowski

    University of Washington

    19 shared

  • Arthur G. Roberts

    University of Liverpool

    18 shared

  • Sidney D. Nelson

    13 shared

  • Eric C. Dietze

    City of Hope

    12 shared

  • Larissa M. Balogh

    Pfizer (United States)

    10 shared

  • Brenda S. Nieslanik

    University of Washington

    9 shared

  • Catalin E. Doneanu

    Waters (United States)

    9 shared

  • Catherine Ibarra

    Duke Medical Center

    9 shared

Education

  • Ph.D., Biochemistry

    Harvard University

  • M.A., Pharmacology

    The College of William and Mary

  • B.S.

    The University of Illinois

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