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Proceedings of the National Academy of Sciences of the United States of America|August 5, 1997
A natural polymorphism in beta-lactamase is a global suppressorW Huang, T PalzkillAntimicrobial Agents and Chemotherapy|October 31, 1998
Display of functional beta-lactamase inhibitory protein on the surface of M13 bacteriophageW Huang, J Petrosino, T PalzkillGene|July 6, 2000
Use of the arabinose p(bad) promoter for tightly regulated display of proteins on bacteriophageW Huang, M McKevitt, T PalzkillThe Journal of Biological Chemistry|November 20, 1997
Cephalosporin substrate specificity determinants of TEM-1 beta-lactamaseC Cantu, W Huang, T PalzkillThe Journal of Biological Chemistry|April 5, 2000
Design of potent beta-lactamase inhibitors by phage display of beta-lactamase inhibitory proteinW Huang, Z Zhang, T PalzkillThe Journal of Biological Chemistry|September 13, 1996
Selection and characterization of amino acid substitutions at residues 237-240 of TEM-1 beta-lactamase with altered substrate specificity for aztreonam and ceftazidimeC Cantu, W Huang, T PalzkillAntimicrobial Agents and Chemotherapy|November 16, 2001
Binding properties of a peptide derived from beta-lactamase inhibitory proteinG W Rudgers, W Huang, T PalzkillGene|December 16, 1998
Mapping protein-ligand interactions using whole genome phage display librariesT Palzkill, W Huang, G M WeinstockThe Journal of Biological Chemistry|September 23, 1994
Characterization of TEM-1 beta-lactamase mutants from positions 238 to 241 with increased catalytic efficiency for ceftazidimeK V Venkatachalam, W Huang, M LaRocco, et al.Antimicrobial Agents and Chemotherapy|October 1, 1994
Effect of threonine-to-methionine substitution at position 265 on structure and function of TEM-1 beta-lactamaseW Huang, Q Q Le, M LaRocco, et al.Pageof 238