Funding Agency

Agency
National Institute of Health (NIH)
Institute
National Cancer Institute (NCI)
Type
Research Project (R01)
Project #
1R01CA064566-01
Application #
2107125
Study Section
Experimental Therapeutics Subcommittee 1 (ET)
Project Start
1994-07-19
Project End
1997-06-30
Budget Start
1994-07-19
Budget End
1995-06-30
Support Year
1
Fiscal Year
1994
Total Cost
Indirect Cost

  Institution

Name
University of South Carolina at Columbia
Department
Pharmacology
Type
Schools of Pharmacy
DUNS #
111310249
City
Columbia
State
SC
Country
United States
Zip Code
29208

  Publications

Zapf, J W; Zhao, P S; Steadman, D J et al. (1999) Genetic complementation and resistance to 5-fluoro-2'-deoxyuridine in thymidine auxotrophs expressing a highly defective mutant of human thymidylate synthase. Biochem Pharmacol 58:973-81
Steadman, D J; Spencer, H T; Dunlap, R B et al. (1999) Substitution at residue 214 of human thymidylate synthase alters nucleotide binding and isomerization of ligand-protein complexes. Biochemistry 38:5582-7
Williams, A W; Dunlap, R B; Berger, S H (1998) A hydroxyl group at residue 216 is essential for catalysis by human thymidylate synthase. Biochemistry 37:7096-102
Steadman, D J; Zhao, P S; Spencer, H T et al. (1998) A structural role for glutamine 214 in human thymidylate synthase. Biochemistry 37:7089-95