Agency
National Institute of Health (NIH)
Institute
National Institute of General Medical Sciences (NIGMS)
Type
Predoctoral Individual National Research Service Award (F31)
Project #
5F31GM017581-02
Application #
2172595
Study Section
Minority Programs Review Committee (MPRC)
Project Start
1996-08-01
Project End
Budget Start
1996-08-01
Budget End
1997-07-31
Support Year
2
Fiscal Year
1996
Total Cost
Indirect Cost
Name
Baylor College of Medicine
Department
Microbiology/Immun/Virology
Type
Schools of Medicine
DUNS #
074615394
City
Houston
State
TX
Country
United States
Zip Code
77030
Petrosino, J; Cantu 3rd, C; Palzkill, T (1998) beta-Lactamases: protein evolution in real time. Trends Microbiol 6:323-7
Cantu 3rd, C; Palzkill, T (1998) The role of residue 238 of TEM-1 beta-lactamase in the hydrolysis of extended-spectrum antibiotics. J Biol Chem 273:26603-9
Cantu 3rd, C; Huang, W; Palzkill, T (1997) Cephalosporin substrate specificity determinants of TEM-1 beta-lactamase. J Biol Chem 272:29144-50
Cantu III, C; Huang, W; Palzkill, T (1996) Selection and characterization of amino acid substitutions at residues 237-240 of TEM-1 beta-lactamase with altered substrate specificity for aztreonam and ceftazidime. J Biol Chem 271:22538-45