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Annals of the New York Academy of Sciences|November 21, 2012
Metallo-β-lactamase structure and functionTimothy PalzkillFrontiers in Molecular Biosciences|March 13, 2018
Structural and Mechanistic Basis for Extended-Spectrum Drug-Resistance Mutations in Altering the Specificity of TEM, CTX-M, and KPC β-lactamasesTimothy PalzkillMbio|November 16, 2021
Deep Mutational Scanning Reveals the Active-Site Sequence Requirements for the Colistin Antibiotic Resistance Enzyme MCR-1Zhizeng Sun, Timothy PalzkillThe Journal of Biological Chemistry|July 31, 2004
Dissecting the protein-protein interface between beta-lactamase inhibitory protein and class A beta-lactamasesZhen Zhang, Timothy PalzkillThe Journal of Biological Chemistry|August 23, 2003
Determinants of binding affinity and specificity for the interaction of TEM-1 and SME-1 beta-lactamase with beta-lactamase inhibitory proteinZhen Zhang, Timothy PalzkillThe Journal of Biological Chemistry|March 3, 2005
Functional analysis of active site residues of the fosfomycin resistance enzyme FosA from Pseudomonas aeruginosaZanna Beharry, Timothy PalzkillBMC Biochemistry|March 8, 2017
Systematic substitutions at BLIP position 50 result in changes in binding specificity for class A β-lactamasesCarolyn J Adamski, Timothy PalzkillAntimicrobial Agents and Chemotherapy|February 27, 2003
Amino acid sequence requirements at residues 69 and 238 for the SME-1 beta-lactamase to confer resistance to beta-lactam antibioticsFahd K Majiduddin, Timothy PalzkillAntimicrobial Agents and Chemotherapy|July 29, 2005
Amino acid residues that contribute to substrate specificity of class A beta-lactamase SME-1Fahd K Majiduddin, Timothy PalzkillCurrent Opinion in Structural Biology|July 3, 2023
Structural biology of MCR-1-mediated resistance to polymyxin antibioticsIsabel Cristina Materon, Timothy PalzkillPageof 15