World's Best Scientists 2026 revealed!

D-Index & Metrics

Biology and Biochemistry

D-Index
54
Citations
12599
World Ranking
15495
National Ranking
6468

Overview

David W. Fry is affiliated with Pfizer in the United States. Their research spans several fields within medicine, with a focus on immunology and microbiology. The subfields in which they have contributed include oncology, immunology, genetics, and pulmonary and respiratory medicine.

Their work covers topics that intersect cancer immunotherapy and biomarker discovery, phagocytosis and immune regulation, immune cell functions and interactions, as well as research on HER2/EGFR in cancer and chronic lymphocytic leukemia. Lung cancer treatments and associated mutations are also among the key subjects addressed in their research portfolio.

David W. Fry has published in notable venues such as Gastroenterology and UNC Libraries. Their recent papers include:

  • Combination of PD-1 Inhibitor and OX40 Agonist Induces Tumor Rejection and Immune Memory in Mouse Models of Pancreatic Cancer, 2020, Gastroenterology
  • Drug-induced ubiquitylation and degradation of ErbB receptor tyrosine kinases: implications for cancer therapy, 2020, UNC Libraries

The frequent co-authors collaborating with David W. Fry are Ying Ma, Jun Li, Huamin Wang, Yulun Chiu, and Charles V. Kingsley.

Best Publications

  • A specific inhibitor of the epidermal growth factor receptor tyrosine kinase

    David W. Fry;Alan J. Kraker;Amy McMichael;Linda A. Ambroso

  • Irreversible inhibitors of tyrosine kinases

    Alexander James Bridges;William Alexander Denny;Ellen Myra Dobrusin;Annette Marian Doherty

  • Induced focal adhesion kinase (FAK) expression in FAK-null cells enhances cell spreading and migration requiring both auto- and activation loop phosphorylation sites and inhibits adhesion-dependent tyrosine phosphorylation of Pyk2.

    James D. Owen;Paul J. Ruest;David W. Fry;Steven K. Hanks

  • Specific, irreversible inactivation of the epidermal growth factor receptor and erbB2, by a new class of tyrosine kinase inhibitor

    David W. Fry;Alexander J. Bridges;William A. Denny;Annette Doherty

  • Tyrosine Kinase Inhibitors. 8. An Unusually Steep Structure−Activity Relationship for Analogues of 4-(3-Bromoanilino)-6,7-dimethoxyquinazoline (PD 153035), a Potent Inhibitor of the Epidermal Growth Factor Receptor

    Alexander J. Bridges;Hairong Zhou;Donna R. Cody;Gordon W. Rewcastle

  • Bicyclic compounds capable of inhibiting tyrosine kinases of the epidermal growth factor receptor family

    Alexander James Bridges;William Alexander Denny;David Fry;Alan Kraker

  • Tyrosine kinase inhibitors. 5. Synthesis and structure-activity relationships for 4-[(phenylmethyl)amino]- and 4-(phenylamino)quinazolines as potent adenosine 5'-triphosphate binding site inhibitors of the tyrosine kinase domain of the epidermal growth factor receptor.

    Gordon W. Rewcastle;William A. Denny;Alexander J. Bridges;Hairong Zhou

  • Antitumor activity and pharmacokinetic properties of PF-00299804, a second-generation irreversible pan-erbB receptor tyrosine kinase inhibitor

    Andrea J. Gonzales;Kenneth E. Hook;Irene W. Althaus;Paul A. Ellis

  • Tyrosine kinase inhibitors. 15. 4-(Phenylamino)quinazoline and 4-(phenylamino)pyrido[d]pyrimidine acrylamides as irreversible inhibitors of the ATP binding site of the epidermal growth factor receptor.

    J. B. Smaill;B. D. Palmer;G. W. Rewcastle;W. A. Denny

  • Pyrido 2,3-d] pyrimidines and 4-aminopyrimidines as inhibitors of cellular proliferation

    Diane Harris Boschelli;Ellen Myra Dobrusin;Annette Marian Doherty;Ali Fattaey

  • Drug‐induced ubiquitylation and degradation of ErbB receptor tyrosine kinases: implications for cancer therapy

    Ami Citri;Iris Alroy;Sara Lavi;Chanan Rubin

  • Structure−Activity Relationships for a Novel Series of Pyrido[2,3-d]pyrimidine Tyrosine Kinase Inhibitors

    James M. Hamby;Cleo J. C. Connolly;Mel C. Schroeder;R. Thomas Winters

  • Pyrido[2,3-d]pyrimidin-7-ones as specific inhibitors of cyclin-dependent kinase 4.

    Scott N. Vanderwel;Patricia J. Harvey;Dennis J. Mcnamara;Joseph T. Repine

  • Tyrosine kinase inhibitors. 9. Synthesis and evaluation of fused tricyclic quinazoline analogues as ATP site inhibitors of the tyrosine kinase activity of the epidermal growth factor receptor

    Gordon W. Rewcastle;Brian D. Palmer;Alexander J. Bridges;H. D. Hollis Showalter

  • Role of tyrosine kinase activity of epidermal growth factor receptor in the lysophosphatidic acid-stimulated mitogen-activated protein kinase pathway.

    Jess M. Cunnick;Jay F. Dorsey;Todd Standley;James Turkson

  • Tyrosine kinase inhibitors. 7. 7-Amino-4-(phenylamino)- and 7-amino-4-[(phenylmethyl)amino]pyrido[4,3-d]pyrimidines: a new class of inhibitors of the tyrosine kinase activity of the epidermal growth factor receptor.

    Andrew M. Thompson;Alexander J. Bridges;David W. Fry;Alan J. Kraker

  • Inhibition of the epidermal growth factor receptor family of tyrosine kinases as an approach to cancer chemotherapy: progression from reversible to irreversible inhibitors.

    David W. Fry

  • Tyrosine kinase inhibitors. 10. Isomeric 4-[(3-bromophenyl)amino]pyrido[d]-pyrimidines are potent ATP binding site inhibitors of the tyrosine kinase function of the epidermal growth factor receptor.

    Gordon W. Rewcastle;Brian D. Palmer;Andrew M. Thompson;Alexander J. Bridges

  • Tyrosine kinase inhibitors. 16. 6,5,6-tricyclic benzothieno[3, 2-d]pyrimidines and pyrimido[5,4-b-] and -[4,5-b]ĭndoles as potent inhibitors of the epidermal growth factor receptor tyrosine kinase.

    H. D. Hollis Showalter;Alexander J. Bridges;Hairong Zhou;Anthony D. Sercel

  • Inhibitors of tyrosine kinase.

    Wayne D. Klohs;David W. Fry;Alan J. Kraker

Frequent Co-Authors

William A. Denny
William A. Denny University of Auckland
Brian D. Palmer
Brian D. Palmer University of Auckland
Richard J. Cote
Richard J. Cote Washington University in St. Louis
James T. Elder
James T. Elder University of Michigan–Ann Arbor
José Baselga
José Baselga Memorial Sloan Kettering Cancer Center
Leonard M. Neckers
Leonard M. Neckers National Institutes of Health
Susan E. Bates
Susan E. Bates Columbia University
Zena Werb
Zena Werb University of California, San Francisco
Edison T. Liu
Edison T. Liu The Jackson Laboratory
Timothy G. Myers
Timothy G. Myers National Institutes of Health

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Best Scientists Citing David W. Fry