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Featured researches published by Joseph A. Dunn.


Annals of the New York Academy of Sciences | 1983

PHORBOL ESTER RECEPTORS AND THE IN VITRO EFFECTS OF TUMOR PROMOTERS

Peter M. Blumberg; K. Barry Delclos; Joseph A. Dunn; Susan Jaken; Karen L. Leach; Emily Yeh

The evidence for the multistage nature of tumor promotion in vivo and for multiple subclasses of phorbol ester receptors in vitro argues that multiple mechanisms of tumor promotion exist. The existence of multiple mechanisms suggests that brute force assay for tumor promoters in vivo may be inadequate and that understanding of mechanisms may be essential. The interest in the phorbol esters is not primarily that they are environmental hazards for man, but rather that they provide a probe for phorbol ester receptors. These receptors are found in people, and modulation of their activity may play a role in tumor promotion in man.


Biochemical Pharmacology | 1996

In vitro characterization of a novel series of platelet-derived growth factor receptor tyrosine kinase inhibitors

David G. Sawutz; Donald C. Bode; G.Maurice Briggs; John Reid; Paul C. Canniff; Lisa Caldwell; Connie R. Faltynek; Deborah Miller; Joseph A. Dunn; Lawrence de Garavilla; Joseph Guiles; Carolyn Weigelt; William F. Michne; Adi Treasurywala; Paul J. Silver

In this report, we describe the discovery and characterization of a novel biarylhydrazone series of platelet-derived growth factor (PDGF) receptor tyrosine kinase inhibitors typified by the prototype WIN 41662 (3-phenyl-N1-[1-(4-pytidyl)pyrimidine]hydrazone). WIN 41662 inhibited PDGF-stimulated autophosphorylation of PDGF receptors from human vascular smooth muscle cells (hVSMC) with an IC50 value of 60 nM. The inhibitor appeared to be competitive with respect to substrate (Mn(2+)-ATP), having a calculated Ki of 15 +/- 5 nM. WIN 41662 was approximately 500-fold more potent in inhibiting the PDGF receptor tyrosine kinase than the p56lck tyrosine kinase. It was inactive against other serine/threonine and tyrosine kinases tested. WIN 41662 produced concentration-dependent inhibition of PDGF-stimulated receptor autophosphorylation in intact hVSMC with an IC50 < 100 nM. Intracellular Ca2+ mobilization and cell proliferation were events that occurred in hVSMC subsequent to PDGF receptor activation. WIN 41662 inhibited PDGF-stimulated Ca2+ mobilization and cell proliferation ([3H]TdR incorporation) with IC50 values of 430 nM and 2.3 microM, respectively. These effects appeared to be specifically related to PDGF receptor tyrosine kinase inhibition since WIN 41662 was not cytotoxic (in vitro) and since WIN 72039, a close structural analog that does not inhibit PDGF receptor tyrosine kinase, also did not inhibit PDGF-stimulated receptor autophosphorylation, Ca2+ mobilization, or hVSMC proliferation. Thus, WIN 41662 is representative of a novel class of selective PDGF receptor tyrosine kinase inhibitors that inhibit PDGF-regulated secondary events in intact cells.


International Journal of Radiation Oncology Biology Physics | 1979

Chemical mechanism of the radiation potentiating effects of 2,2-Dimethylaziridine-type antitumor agents☆

Thomas J. Bardos; Joseph A. Dunn; Michael E. Perlman

Abstract Three 2,2-dimethyl phosphoraziridines, bis(2,2-dimethylaziridinyl)phosphinyl urethane (AB-132, NSC 51325), ethyl bis(2,2-dimethylaziridinyi)phosphinate (AB-163 NSC 108878) and bis(2,2-dimethylaziridinyl)-N-hydroxyurethane (AB-182, NSC 200724) which have shown synergistic antitumor effects in conjunction with X-irradiation, are characterized by their rapid hydrolysis via S N 1-mechanism and via the formation of transient 5-membered cyclic intermediates exhibiting phosphorylating activities. It was shown that the formation of the latter correlates with the observed maxima in the cholinesterase inhibitory effects of these compounds. It is proposed that the same intermediate hydrolysis products may block the repair of X-irradiation induced breaks in the DNA strands by phosphorylating their free YOH end groups. Additional mechanisms of the radiation potentiating effects of these compounds (not shown by their C-unsubstituted analogs), involving free radical-ion formation, are currently under investigation.


Journal of Medicinal Chemistry | 1994

5,7-Dimethoxy-3-(4-pyridinyl)quinoline is a potent and selective inhibitor of human vascular beta-type platelet-derived growth factor receptor tyrosine kinase.

Roland E. Dolle; Joseph A. Dunn; Mark A. Bobko; Baldev Singh; Joan E. Kuster; Eugene R. Baizman; Alex L. Harris; David G. Sawutz; Deborah Miller; Su Wang; Connie R. Faltynek; Wen Xie; Jay Sarup; D. Christopher Bode; Edward D. Pagani; Paul J. Silver


Cancer Research | 1983

Specific Binding of [20-3H]12-Deoxyphorbol 13-Isobutyrate to Phorbol Ester Receptor Subclasses in Mouse Skin Particulate Preparations

Joseph A. Dunn; Peter M. Blumberg


Cancer Research | 1985

Heterogeneity of [3H]Phorbol 12,13-Dibutyrate Binding in Primary Mouse Keratinocytes at Different Stages of Maturation

Joseph A. Dunn; Arco Y. Jeng; Stuart H. Yuspa; Peter M. Blumberg


Virology | 2005

Potent inhibition of HIV-1 entry by (s4dU)35

András Horváth; Szilvia Tokés; Tracy L. Hartman; Karen Watson; Jim A. Turpin; Robert W. Buckheit; Zsolt Sebestyén; János Szöllosi; Ilona Benko; Thomas J. Bardos; Joseph A. Dunn; László Fésüs; Ferenc Tóth; János Aradi


Cancer Research | 1992

Aflatoxin-transformed C3H/10T1/2 Cells Overexpress Protein Kinase C and Have an Altered Response to Phorbol Ester Treatments

Joseph A. Dunn; Michael B. Faletto; Steven J. Kasper; Hira L. Gurtoo


Journal of Medicinal Chemistry | 1991

Synthesis of potential dual-acting radiation sensitizer antineoplastic agents : 2,2-dimethylphosphoraziridines containing 2-nitroimidazoles or other electron-affinic moieties

Michael E. Perlman; Joseph A. Dunn; Thomas A. Piscitelli; Julie Earle; William C. Rose; Galen L. Wampler; Joan E. MacDiarmid; Thomas J. Bardos


Journal of Medicinal Chemistry | 1990

Synthesis of new nucleoside phosphoraziridines as potential site-directed antineoplastic agents.

Robert G. Breiner; William C. Rose; Joseph A. Dunn; Joan E. MacDiarmid; Thomas J. Bardos

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Peter M. Blumberg

National Institutes of Health

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David G. Sawutz

University of Cincinnati Academic Health Center

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Joan E. MacDiarmid

State University of New York System

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Paul J. Silver

University of Texas System

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