PUBLICATIONS


Bibliography
(
Full-Length Manuscripts)

1968-1980     1981-1990     1991-1995     1996-present

1. Spector, T. and Johns, D.G. “Oxidation of 4-Hydroxypyrazolo [3,4-d]pyrimidine by Xanthine Oxidase: The Route of Electron Transfer From Substrate to Acceptor Dyes.” Biochem. Biophys. Res. Communs. 32, 1039-1044 (1968).

2. Johns, D.G., Spector, T., and Robins, R.K. “Studies on the Mode of Oxidation of Pyrazolo[3,4-d]pyrimidine by Aldehyde Oxidase and Xanthine Oxidase.” Biochem. Pharm. 18, 2371-2383 (1969).

3. Spector, T. and Johns, D.G. “4- Hydroxypyrazolo[3,4-d]pyrimidine as a Substrate For Xanthine Oxidase: Loss of Conventional Substrate Activity with Catalytic Cycling of the Enzyme.” Biochem. Biophys. Res. Communs. 38, 583-589 (1970).

4. Spector, T. and Johns, D.G. “Stoichiometric Inhibition of Reduced Xanthine Oxidase by Hydroxypyrazolo[3,4-d]pyrimidines.” J. Biol. Chem. 245, 5079-5085 (1970).

5. Spector, T. and Massey, V. “Interactions of Substrate and Non- substrate Effectors with p-Hydroxybenzoate Hydroxylase from Pseudomonas fluorescens.” Biochem. Biophys. Res. Commun. 45, 1219-1226 (1971).

6. Howell, L.G., Spector, T., and Massey, V. “Purification and Properties of p-Hydroxybenzoate from Pseudomonas fluorescens.” J. Biol. Chem. 247, 4340-4350 (1972).

7. Spector, T., and Massey, V. “Studies on The Effector Specificity of p-Hydroxybenzoate Hydroxylase from Pseudomonas fluorescens.” J. Biol. Chem. 247, 4679-4687 (1972).

8. Spector, T. and Massey, V. “p-Hydroxybenzoate Hydroxylase from Pseudomonas fluorescens: Evidence for an Oxygenated Flavin Intermediate.” J. Biol. Chem. 247, 5632-5636 (1972).

9. Spector, T. and Massey, V. “p-Hydroxybenzoate Hydroxylase from Pseudomonas fluorescens: Reactivity with Oxygen.” J. Biol. Chem. 247, 7123-7127 (1972).

10. Spector, T., Miller, R.L., Fyfe, J.A. and Krenitsky, T.A. “GMP Synthetase from E. coli B-96: Interactions with Substrate Analogs.” Biochim. Biophys. Acta, 370, 585-591 (1974).

11. Spector, T. and Beacham, L.M. III “GMP Synthetase from E. coli B-96: Inhibition by Nucleosides.” J. Biol. Chem. 250, 3101-3107 (1975).

12. Spector, T. “Studies with GMP Synthetase from Ehrlich Ascites Cells: Purification, Properties, and Interactions With Nucleotide Analogs.” J. Biol. Chem. 250, 7372-7376 (1975).

13. Spector, T. and Miller, R.L. “Mammalian Adenylosuccinate Synthetase: Nucleotide Monophosphate Substrates and Inhibitors.” Biochim. Biophys. Acta 445, 509-517 (1976).

14. Spector, T., Jones, T.E., Krenitsky, T.A., and Harvey, R.H. “Guanosine Monophosphate Synthetase from Ehrlich Ascites Cells: Multiple Inhibition by Pyrophosphate and Nucleosides.” Biochim. Biophys. Acta 452, 597-607 (1976).

15. Spector, T. “Mammalian Adenylosuccinate Lyase: Participation in the Conversion of 2′-dIMP and ß-D-Arabinosyl-IMP to Adenine Nucleotides.” Biochim. Biophys. Acta 481, 741-745 (1977).

16. Spector, T. “Inhibition of Urate Production by Allopurinol.” (Commentary) Biochem. Pharmacol. 26, 355-358 (1977).

17. Agarwal, R.P., Spector, T., and Parks, R.E., Jr. “Tight Binding Inhibitors: IV. Inhibition of Adenosine Deaminases by Various Inhibitors.” Biochem. Pharmacol. 26, 359-367 (1977).

18. Miller, R.L., Adamczyk, D.L., and Spector, T. “Reassessment of the Interactions of Guanylate Kinase and 6-Thioguanosine 5′-Phosphate.” Biochem. Pharmacol. 26, 1573-1576 (1977).

19. Spector, T. “Refinement of the Coomassie Blue Method of Protein Quantitation: A Simple and Linear Spectrophotometric Assay for 0.5-50 Micrograms of Protein.” Analyt. Biochem. 86, 142-146 (1978).

20. Spector, T. “GMP Synthetase From Ehrlich Ascites Cells.” in “Methods in Enzymology, Purine and Pyrimidine Nucleotide Metabolism.” Vol. LI, pp. 219-224 (eds. P.A. Hofee and M. E. Jones) NY Acad. Press (1978).

21. Spector, T. “Precise Temperature Control of the Gilford Spectrophotometer: A Simple and Inexpensive Modification.” Analyt. Biochem. 93, 171-173 (1979).

22. Spector, T., Jones, T.E., and Miller, R.L. “Reaction Mechanism and Specificity of Human GMP Reductase: Substrates, Inhibitors, Activators and Inactivators.” J. Biol. Chem. 254, 2308-2315 (1979).

23. Spector, T., Jones, T.E., and Elion, G.B. “Specificity of Adenylosuccinate Synthetase and Adenylosuccinate Lyase from Leishmania donovani: Selective Amination of an Antiprotozoal Agent.” J. Biol. Chem. 254, 8422-8426 (1979).

24. Spector, T. “Charcoal-Facilitated Dialysis.” Analyt. Biochem. 103, 313-316 (1980).

25. Spector, T. and Cleland. W.W. “Meanings Of Ki For Conventional and Alternate-Substrate Inhibitors.” Biochem. Pharmacol. 30, 1-7 (1981).

26. Spector, T. and Hajian, G. “Statistical Methods to Distinguish Competitive, Noncompetitive and Uncompetitive Enzyme Inhibitors.” Analytical Biochem. 115, 403-409 (1981).

27. Marr, J.J., Berens, R.L., Nelson, D.J., Krenitsky, T.A., Spector, T., LaFon, S.W., and Elion, G.B. “Antileishmanial Action of 4-Thiopyrazolo[3,4-d]pyrimidine and Its Riboside: Biological Effects and Metabolism.” Biochem. Pharmacol. 31, 143-148 (1982).

28. Spector, T., Berens, R.L., and Marr, J.J. “Adenylosuccinate Synthetase and Adenylosuccinate Lyase from Trypanosoma cruzi: Specificity Studies with Potential Chemotherpeutic Agents.” Biochem. Pharmacol. 31, 225-229 (1982).

29. Spector, T. and Jones, T.E. “GMP Reductase from Leishmania donovani: A Possible Chemotherapeutic Target.” Biochem. Pharmacol. 31, 3891-3897 (1982).

30. Nelson, D.J., LaFon, S.W., Jones, T.E., Spector,, T., Berens, R.L., and Marr, J.J. “The Metabolism of Formycin B in Leishmania donovani.” Biochem. Biophys. Res. Commun. 108, 349-354 (1982).

31. Spector, T., Jones, T.E. and Beacham, L., M. III “Conversion of 2,6-Diamino-9-(2-hydroxyethoxymethyl) purine to Acyclovir as Catalyzed by Adenosine Deaminase.” Biochem. Pharmacol. 32, 2505-2509 (1983).

32. Averett, D.R., Lubbers, C., Elion, G.B., and Spector, T. “Ribonucleotide Reductase Induced by Herpes Simplex Type 1: Characterization of a Distinct Enzyme.” J. Biol. Chem. 258, 9831-9838 (1983).

33. Spector, T. and Averett, D.R. “A Simple Method to Purify Ribonucleotide Reductase.” Analytical Biochem. 134, 467-470 (1983).

34. Spector, T., Jones, T.E., Nelson, D.J., Lafon, S.W., Berens, R.L., and Marr, J.J. “Monophosphates of Formycin B and Allopurinol Riboside: Interactions with leishmanial and Mammalian Adenylosuccinate Synthetase and GMP Reductase.” Biochem. Pharmacol. 33, 1611-1617 (1984).

35. Furman, P., St. Clair, M.H., and Spector, T. “Acyclovir Triphosphate is a Suicide Inactivator of Herpes Simplex Virus DNA Polymerase.” J. Biol. Chem. 259, 9575-9579 (1984).

36. Spector, T. “Progress Curve Analysis of Adenosine Deaminase Catalyzed Reactions.” Analyt. Biochem. 138, 242-245 (1984).

37. Averett, D.R. and Spector, T. “Ribonucleotide Reductase of Herpes Simplex Virus Type 2 Resembles That of Herpes Simplex Virus Type I .” J. Virol. 52, 981-983 (1984).

38. Spector, T., and Ferone, R. “Folic Acid does not Inactivate Xanthine Oxidase.” J. Biol. Chem. 259, 10784-10786 (1984).

39. Spector, T., and Jones, T.E. “Herpes Simplex Type I Ribonucleotide Reductase: Mechanism Studies with Inhibitors.” J. Biol. Chem. 260, 8694-8697 (1985).

40. Spector, T., Averett, D.R., Nelson, D.J., Lambe, C.U., St. Clair, M.H., and Furman, P.A. “Potentiation of Acyclovir’s Antiherpetic Activity by Ribonucleotide Reductase Inhibitions.” Proc. Natl. Acad. Sci. 82, 4254-4257 (1985).

41. Spector, T. “Improvement of A Simple Method to Purify Ribonucleotide Reductase.” Prep. Biochem. 51, 183-188 (1985).

42. Ator, M.A., Stubbe, J., and Spector, T. “Mechanism of Ribonucleotide Reductase from Herpes Simplex Virus Type 1: Evidence for 3′-Carbon-Hydrogen Bond Cleavage and Inactivation by Nucleotide Analogs.” J. Biol. Chem. 261, 3595-3599 (1986).

43. Krenitsky, T.A., Spector, T., and Hall, W.W. “Xanthine Oxidase from Human Liver: Purification and Substrate Specificity.” Arch. Biochem. Biophys. 247, 108-119 (1986).

44. Spector, T., Hall, W.W., and Krenitsky, T.K. “Human and Bovine Xanthine Oxidase: Mechanism Studies with Oxipurinol.” Biochem. Pharmacol. 35, 3109-3114 (1986).

45. Furman, P.A., Spector, T., and Fyfe, J.A. “Acyclovir: Mechanism of Action”. in “Human Herpesvirus Infections.” pp. 129-140. (eds. C. Lopez & B. Roizman) Raven Press, New York (1986).

46. Spector, T. “Inhibition of the Ribonucleotide Reductases Encoded by Herpes Simplex Viruses.” Pharmac. Ther. 31, 295-302 (1985) “Copyright 1987”

47. Harrington, J.A., Miller, W.H., and Spector, T. “Effector Studies of 3′-Azidothymidine Nucleotides with Human Ribonucleotide Reductase”. Biochem. Pharmacol. 36, 3757-3761 (1987).

48. Spector, T. Stonehuerner, J.G., Biron, K.K., and Averett, D.R. “Ribonucleotide Reductase Induced by Varicella Zoster Virus: Characterization, and Potentiation of Acyclovir by Its Inhibition.” Biochem. Pharmacol. 36, 4341-4346 (1987).

49. St. Clair, M.H., Richards, C.A., Spector, T., Weinhold, K.J., Miller, W.H., Langlois, A.L., and Furman, P.A. “3′-Azidothymidine Triphosphate as an Inhibitor and Substrate of Purified Human Immunodeficiency Virus Reverse Transcriptase.” Antimicrob. Agents and Chemother. 31, 1972-1977 (1987).

50. Spector, T. “Oxipurinol as an Inhibitor of the Xanthine Oxidase Catalyzed Production of Superoxide Radical.” Biochem. Pharmacol. 37, 349-352 (1988).

51. Spector, T. “Ribonucleotide Reductases Encoded By Herpes Viruses: Inhibitors and Clinical Considerations.” in “International Encyclopedia of Pharmacol. and Therapeutics” Section 128, Chapter 12, pp. 235-243 (eds. J.G. Cory and A.H. Cory) Pergamon Press, New York (1989).

52. Spector, T., Harrington, J.A., Morrison, R.W., Jr., Lambe, C.U., Nelson, D.J., Averett, D.R., Biron, K., and Furman, P.A. “2-Acetylpyridine-5-[dimethylamino)thiocarbonyl]thiocarbonohydrazone (A1110U), A Potent Inactivator of Ribonucleotide Reductases of Herpes Simplex and Varicella- Zoster Viruses and a Potentiator of Acyclovir.” Proc. Natl. Acad. Sci. 86, 1051-1055 (1989).

53. Resetar, A. and Spector, T. “Glucuronidation of 3′-Azido- 3′-deoxythymidine: Human and Rat Enyzme Specificity.” Biochem. Pharmacol. 38, 1389-1393 (1989).

54. Reardon, J.E., and Spector, T. “Herpes Simplex Virus Type I DNA Polymerase: Mechanism of Inhibition by Acyclovir Triphosphate.” J. Biol Chem. 264, 7405-7411 (1989).

55. Ellis, N.M., Lobe, D.C., and Spector, T. “Synergistic Therapy by Acyclovir and A1110U for Mice Orofacially Infected With Herpes Simplex Virus.” Antimicrob. Agents Chemother. 33, 1691-1696 (1989).

56. Spector, T., Hall, W.E., Porter, D.J.T., Lambe, C.U., Nelson D.J., and Krenitsky, T.A. “Inhibition of Xanthine Oxidase by 4-hydroxy- 6-mercaptopyrazolo[3,4-d]pyrimidine.” Biochem. Pharmacol. 38, 4315-4320 (1989).

57. Baum, K.F., Berens, R.L., Marr, J.J., Harrington, J.A. and Spector, T. “Purine Deoxynucleoside Salvage in Giardia Lamblia.” J. Biol. Chem. 264, 21087-21090 (1989).

58. Spector, T. and Harrington, J.A. “Rapid Sampling of Multiple Enzyme Reactions.” J. Virolog. Methods 26, 237-244(1989).

59. Porter, D.J.T., Harrington, J.A., Spector, T. “Herpes Simplex Type I Ribonucleotide Reductase: Selective Inactivation by A1110U and Its Iron Complex.” Biochem. Pharmacol. 39, 639-46 (1990).

60. Spector, T., and Fyfe, J.A. “Synergy and Antagonism in Polymerase- targeted Antiviral Therapy: Effects of Deoxynucleoside Triphosphate Pool Modulation on Prodrug Activation.” in Synergy and Antagonism in Chemotherapy (eds. T.-C. Chou and D. Rideout), pp. 285-310. Academic Press, San Diego (1991).

61. Lobe, D.C., Spector, T., and Ellis, N.M., “Synergistic Topical Therapy by Acyclovir and A1110U for Herpes Simplex Virus Induced Zosteriform Rash In Mice.” Antiviral Research 15, 87-100 (1991).

62. Spector, T., Harrington, J.A., and Porter, D.J. “Human and Herpes Ribonucleotide Reductases: Inhibition by 2-acetylpyridine 5-[(2-chloroanalino)thiocarbonyl]-thiocarbonohydrozone (348U87)” Biochem. Pharmacol. 42, 91-96 (1991).

63. Resetar, A. Minick, D., and Spector, T. “Glucuronidation of 3′-Azido- 3′-deoxythymidine Catalyzed by Human Liver UDP-Glucuronosyltransferase: Significance of Nucleoside Hydrophobicity and Inhibition by Xenobiotics.” Biochem. Pharmacol. 42, 559-568 (1991).

64. Koszalka, G.W, Averett, D.R., Fyfe, J.A., Roberts, G.B., Spector, T., Biron, K., and Krenitsky, T.A., “6-N-substituted Derivatives of Adenine Arabinoside as Selective Inhibitors of Varicella-Zoster Virus.” Antimicrob. Agents Chemother. 35,1437-1443 (1991).

65. Harrington, J.A., and Spector, T. “Human Ribonucleotide Reductase: Activation and Inhibition by Analogs Of ATP”. Biochem. Pharmacol. 42, 759-763 (1991).

66. Reardon, J.E., and Spector, T. “Acyclovir: Mechanism of Antiviral Action and Potentiation by Ribonucleotide Reductase Inhibitors.” in Advances in Pharmacology vol. 22 (ed. T. August ) Academic Press, NY pp. 1-27 (1991).

67. Porter, D.J.T., Chesnut, W.G., Taylor, L.C.E., Merrill, B.M., and Spector, T, “Inactivation of Dihydropyrimidine Dehydrogenase by 5-Iodouracil” J. Biol. Chem. 266 19988-19994 (1991).

68. Lambe, C.U., Resetar, A.M., Spector, T., Koszalka, G.W, and Nelson, D.N. ‘Metabolism and Pharmacokinetics of the Anti-V aricella Zoster Virus Agent 6-Dimethylaminopurine Arabinoside.” Antimicrob. Agents Chemother. 36 353-360 (1992).

69. Porter, D.J.T., Chestnut, W.G., Taylor, L.C.E., Merrill, B.M., and Spector, T, “Mechanism-Based Inactivation of Dihydropyrimidine Dehydrogenase by 5-Ethynyluracil” J. Biol. Chem. 267 5236-5242 (1992).

70. Spector, T, Lobe, D.C., Ellis, M.N., Blumenkopf,T., and Szczech, G. M. “Inactivators of Herpes Simplex Virus Ribonucleotide Reductase: Hematological Profiles andIn Vivo Potentiation of the Antiviral Activity of Acyclovir” Antimicrob. Agents Chemother. 36, 934-937 (1992).

71. Averett, D.R., Steinberg, H., Koszalka, G.W, Spector, and Krenitsky, T.A., “Purine Arabinosides as Inhibitors of Hematopoietic Progenitor Cells.” Antiviral Chem. Chemother. 3, 179-182 (1992).

72. Blumenkopf, T.A., Harrington, J.A., Koble, C.S., Bankstron, D.S., Morrison, R.W. Jr., Bigham, E. C., Styles, V.L., and Spector, T, “2-Acetylpyridine Thiocarbonohydrazones: Potent Inactivators of Herpes Simplex Virus Ribonucleotide Reductase” J. Med. Chem. 35, 2306-2314 (1992).

73. Furfine, ES, D’Souza, E, Ingold, K, Leban, JJ, Spector, T, and Porter, DJT, “Two-step binding mechanism for HIV Protease inhibitors” Biochemistry 31, 7886-7891 (1992).

74. Porter, DJT, and Spector, T, “Alternative substrates for calf intestinal adenosine deaminase: Pre-steady-state kinetic analysis.” J. Biol. Chem. 268, 2480-2485 (1993).

75. Burns, C.L., St. Clair, M.H., Frick, L.W., Spector, T., Averett, D.R., English, M.L., Holmes, T.J., Krenitsky, T.A., and Koszalka, G.W. “Novel 6-alkoxypurine-2′, 3′-dideoxynucleosides os inhibitors of the cytopathic effect of human immunodeficiency virus (HIV)” J. Med. Chem. 36, 378-384 (1993).

76. Hamzeh, F. M., Spector, T., and Leitman, P.S.”2-Acetylpyridine-5-[dimethylamino)thiocarbonyl]thiocarbonohydrazone (1110U81) Potently inhibits human cytomegalovirus and potentiates the antiviral effects of ganciclovir” Antimicrob. Agents Chemother. 37, 602-604 (1993).

77. Harringinton, J.A., Reardon, J.E., and Spector, T. “AZT monophosphate: an inhibitor of exonucleolytic repair of AZT-terminated DNA” Antimicrob. Agents Chemother. 37, 918-920 (1993).

78. Spector, T, “348U87: An Inactivator of Herpes Virus Ribonucleotide Reductase That Potentiates the Antiviral Activity of Acyclovir” Drugs of The Future 18, 25-28 (1993).

79. Porter, DJT, and Spector, T, “Dihydropyrimidine dehydrogenase: kinetic Mechanism for reduction of uracil by NADPH.” J. Biol. Chem. 268, 19321-19327 (1993).

80. Baccanari, D.P., Davis, S.T., Knick, V.C., and Spector, T., 5-Ethynyluracil (776C85): A potent modulator of the pharmacokinetics and antitumor activity of 5-fluorouracil” Proc. Natl. Acad. Sci. 90, 11064-11068 (1993).

81. Spector, T., Harrington, J.A., and Porter, D.J. “5-Ethynyluracil (776C85): inactivation of dihydropyrimidine dehydrogenase in vivo ” Biochem. Pharmacol. 46, 2243-2248 (1993).

82. Spector, T., “5-Ethynyluracil (776C85): An Inactivator of Uracil Reductase That Potentiates the Antitumor Activity of 5-Fluorouracil” Current Opinions in Therapeutic Patents. 3, 1751-1754 (1993)

83. Cao, S., Rustum, Y. M., and Spector, T. “5-Ethynyluracil (776C85): Modulation of 5-Fluorouracil Efficacy and Therapeutic Index in Rats Bearing Advanced Colorectal Carcinoma” Cancer Res. 54, 1507-1510 (1994).

84. Spector, T, “Writing a Scientific Manuscript: Highlights For Success” J. Chem. Education 71, 47-50 (1994).

85. Porter, D.J., Harrington, J.A., Almond, M.R., Lowen, G.T., Zimmerman, T.P., and Spector, T., “5-Ethynyl-2(1H)-pyrimidinone: aldehyde oxidase-activation to 5-ethynyluracil (776C85), a mechanism-based inactivator of dihydropyrimidine dehydrogenase” Biochem. Pharmacol. 47, 1165-1171 (1994).

86. Porter, D. J. T., Harrington, J. A., Almond, M. R., Lowen, G. T. and Spector, T., “(R)-5-Fluoro-5,6-dihydrouracil: kinetics of oxidation by dihydropyrimidine dehydrogenase and hydrolysis by dihydropyrimidine aminohydrolase” Biochem. Pharmacol. 48, 775-779 (1994).

87. Spector, T., Porter, D. J. T., Nelson, D. J., Baccanari, D. P., Davis, S. T., Almond, M. R., Khor, S. P., Amyx, H., Cao, S., and Rustum, Y. M., “5-Ethynyluracil (776C85), A Modulator Of The Therapeutic Activity Of 5-Fluorouracil” Drugs of The Future 19, 565-571 (1994).

88. Davis, S. T., Joyner, S.S., Baccanari, D. P., and Spector, T., “5-Ethynyluracil (776C85): protection from 5-fluorouracil-induced neurotoxicity in dogs” Biochem. Pharmacol. 48, 233-236 (1994).

89. Spector, T., Cao, S., Rustum, Y.M., Harrington, J A., and Porter, D. J. T. “Attenuation of The Antitumor Activity of 5-Fluorouracil By (R)-5-Fluoro-5,6-dihydrouracil” Cancer Res. 55, 1239-1241 (1995).

90. Fischel, J. L., Etinne, M. C., Spector, T., Formento, P., Renee, N., and Milano, G., “Dihydropyrimidine dehydrogenase: A tumoral target for fluorouracil modulation” Clin. Cancer Res. 1, 991-996 (1995).

91. Porter, D.J.T., Harrington, J. A., Almond, M, Chestnut, W.G., Tanoury, G., and Spector, T, “Enzymatic Elimination of Fluoride From a-Fluoro-b-alanine” Biochem. Pharmacol. 50, 1475-1484 (1995).

92. Cao, S., Baccanari, D. P., Joyner, S. S., Davis, S. T., Rustum, Y. M., and Spector, T., “5-Ethynyluracil (776C85): Effects on the Antitumor Activity and Pharmacokinetics of Tegafur, a Prodrug of 5-Fluorouracil” Cancer Res. 55, 6227-6230 (1995).

93. Khor, S-P, Amyx, H., Davis, S., Nelson, D. J., Baccanari, D. P., and Spector, T., “Dihydropyrimidine Dehydrogenase Inactivation and 5-Fluorouracil Pharmacokinetics: Allometric Scaling of Animal Data, Pharmacokinetics and Toxicodynamics of 5-Fluorouracil in Humans” Cancer Chemother. Pharmacokinetics. 39, 233-238 (1997).

94. Baker, S. D., Khor, S. P., Adjei, A. A., Doucette, M., Spector, T., Amin, J. M., Jersey, J., Donehower, R.C., Grochow, L. B., Sartorius, S. E., Noe, D. A., Hohneker, J. A., and Rowinsky, E. K., “Pharmacokinetic, Oral Bioavailability, and Safety Study of 5-Fluorouracil in Patients Treated with 776C85, and Inactivator of Dihydropyrimidine Dehydrogenase”. J. Clin. Oncology 14, 3085-3096 (1996).

95. Fischel, J. L., Formento, P., Etinne, M. C., Spector, T., Renee, N., and Milano, G., “Dual modulation of 5-fluorouracil cytotoxicity using folinic acid with a dihydropyrimidine dehydrogenase inhibitor.” Biochem. Pharmacol. 53, 1703-1709 (1997).

96. Arellano, M., Malet-Martino, M., Martino, R. and Spector, T., “5-Ethynyluracil (GW776): Effects on the Formation of the Toxic Catabolites of 5-Fluorouracil, Fluoroacetate and Fluorohydroxypropionic Acid, in the Isolated Perfused Rat Liver Model.” British J. Cancer 76, 1170-1180 (1997).

97. Adams, E.R., Leffert, J.J., Craig, D.J., Spector, T., Pizzorno,G., “In Vivo Effect of 5-Ethynyluracil on 5-Fluorouracil Metabolism Determined by 19F-NMR Spectroscopy”. Cancer Res. 59, 122-7 (1999).

98. Baker SD, Diasio RB, O’Reilly S, Lucas VS, Khor SP, Sartorius SE, Donehower RC, Grochow LB, Spector T, Hohneker JA, Rowinsky EK, “Phase I and Pharmacologic Study of Oral Fluorouracil on a Chronic Daily Schedule in Combination With the Dihydropyrimidine Dehydrogenase Inactivator Eniluracil”. J Clin Oncol 18, 915- 926 (2000).

99. Bading JR, Alauddin MM, Fissekis JD, Shahinian AH, Joung J, Spector T, Conti PS. “Blocking catabolism with eniluracil enhances PET studies of 5-[18F]fluorouracil pharmacokinetics.” J Nucl Med 41, 1714-1724 (2000).

100. Cao, S., Baccanari, D. P., Rustum, Y. M., Davis,S.T., Tansik, R., Porter, D..J. T., and Spector, T., “(R)a-Fluoro-b-Alanine: Effects on the Antitumor Activity and Toxicity of 5-Fluorouracil”. Biochem. Pharmacol. 59, 953-960 (2000).

101. Paff MT Baccanari DP Davis ST Cao SS Tansik RL Rustum YM Spector T., ” Preclinical development of eniluracil: Enhancing the therapeutic index and dosing convenience of 5-fluorouracil.” Invest. New Drugs. 18, 365-371 (2000).

102. Galbusera C, Orth P, Fedida D, and Spector T. Superoxide Radical Production By Allopurinol and Xanthine Oxidase. Biochem. Pharmacol. 71:1747-52. (2006).

103. Spector, T., Cao, S., A possible cause and remedy for the clinical failure of 5-fluorouracil plus eniluracil. Clinical Colorectal Cancer. 9: 52-54 (2010).

104. Stephenson, CM, Levin, RD, Spector, T, Lis, CG. Phase I clinical trial to evaluate the safety, tolerability, and pharmacokinetics of high-dose intravenous ascorbic acid in patients with advanced cancer. Cancer Chemotherapy and Pharmacology, 72:139-146: (2013).

105. Rivera E, Chang JC, Semiglazov V, Burdaeva O, Kirby MG, Spector T. Eniluracil Plus 5-Fluorouracil and Leucovorin: Treatment for Metastatic Breast Cancer Patients in Whom Capecitabine Treatment Rapidly Failed. Clinical Breast Cancer, 14: 26-30 (2014).

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