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The Journal of Biological Chemistry|March 6, 1999
Identification of residues in beta-lactamase critical for binding beta-lactamase inhibitory proteinG W Rudgers, T PalzkillProtein Engineering|August 28, 2001
Protein minimization by random fragmentation and selectionG W Rudgers, T PalzkillAntimicrobial Agents and Chemotherapy|November 16, 2001
Binding properties of a peptide derived from beta-lactamase inhibitory proteinG W Rudgers, W Huang, T PalzkillProteins|September 1, 1992
Probing beta-lactamase structure and function using random replacement mutagenesisT Palzkill, D BotsteinProceedings 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 PalzkillJournal of Bacteriology|August 1, 1992
Identification of amino acid substitutions that alter the substrate specificity of TEM-1 beta-lactamaseT Palzkill, D BotsteinThe Journal of Biological Chemistry|October 3, 1998
The role of residue 238 of TEM-1 beta-lactamase in the hydrolysis of extended-spectrum antibioticsC Cantu, T PalzkillProtein Science : a Publication of the Protein Society|November 21, 2001
Identification of residues critical for metallo-beta-lactamase function by codon randomization and selectionI C Materon, T PalzkillJournal of Bacteriology|April 1, 1996
Systematic mutagenesis of the active site omega loop of TEM-1 beta-lactamaseJ F Petrosino, T PalzkillProtein Engineering, Design & Selection : PEDS|March 24, 2010
Identification and characterization of beta-lactamase inhibitor protein-II (BLIP-II) interactions with beta-lactamases using phage displayN G Brown, T PalzkillPageof 4