TIMOTHY PALZKILL to Ceftazidime
This is a "connection" page, showing publications TIMOTHY PALZKILL has written about Ceftazidime.
Connection Strength
4.875
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The mechanism of ceftazidime and cefiderocol hydrolysis by D179Y variants of KPC carbapenemases is similar and involves the formation of a long-lived covalent intermediate. Antimicrob Agents Chemother. 2024 03 06; 68(3):e0110823.
Score: 0.863
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Klebsiella pneumoniae carbapenemase variant 44 acquires ceftazidime-avibactam resistance by altering the conformation of active-site loops. J Biol Chem. 2024 01; 300(1):105493.
Score: 0.853
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Mapping the determinants of catalysis and substrate specificity of the antibiotic resistance enzyme CTX-M ?-lactamase. Commun Biol. 2023 01 12; 6(1):35.
Score: 0.803
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The Drug-Resistant Variant P167S Expands the Substrate Profile of CTX-M ?-Lactamases for Oxyimino-Cephalosporin Antibiotics by Enlarging the Active Site upon Acylation. Biochemistry. 2017 07 11; 56(27):3443-3453.
Score: 0.547
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A triple mutant in the O-loop of TEM-1 ?-lactamase changes the substrate profile via a large conformational change and an altered general base for catalysis. J Biol Chem. 2015 Apr 17; 290(16):10382-94.
Score: 0.465
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An analysis of why highly similar enzymes evolve differently. Genetics. 2003 Feb; 163(2):457-66.
Score: 0.202
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Slow Protein Dynamics Elicits New Enzymatic Functions by Means of Epistatic Interactions. Mol Biol Evol. 2022 10 07; 39(10).
Score: 0.197
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Antagonism between substitutions in ?-lactamase explains a path not taken in the evolution of bacterial drug resistance. J Biol Chem. 2020 05 22; 295(21):7376-7390.
Score: 0.166
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Synergistic effects of functionally distinct substitutions in ?-lactamase variants shed light on the evolution of bacterial drug resistance. J Biol Chem. 2018 11 16; 293(46):17971-17984.
Score: 0.149
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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. 1996 Sep 13; 271(37):22538-45.
Score: 0.129
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Characterization of the global stabilizing substitution A77V and its role in the evolution of CTX-M ?-lactamases. Antimicrob Agents Chemother. 2015 Nov; 59(11):6741-8.
Score: 0.120
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Natural Variants of the KPC-2 Carbapenemase have Evolved Increased Catalytic Efficiency for Ceftazidime Hydrolysis at the Cost of Enzyme Stability. PLoS Pathog. 2015 Jun; 11(6):e1004949.
Score: 0.118
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Characterization of TEM-1 beta-lactamase mutants from positions 238 to 241 with increased catalytic efficiency for ceftazidime. J Biol Chem. 1994 Sep 23; 269(38):23444-50.
Score: 0.113
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Roles of amino acids 161 to 179 in the PSE-4 omega loop in substrate specificity and in resistance to ceftazidime. Antimicrob Agents Chemother. 1998 Oct; 42(10):2576-83.
Score: 0.037
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Systematic mutagenesis of the active site omega loop of TEM-1 beta-lactamase. J Bacteriol. 1996 Apr; 178(7):1821-8.
Score: 0.031
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Structural Basis for Different Substrate Profiles of Two Closely Related Class D ?-Lactamases and Their Inhibition by Halogens. Biochemistry. 2015 Jun 02; 54(21):3370-80.
Score: 0.030
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Evolution of antibiotic resistance: several different amino acid substitutions in an active site loop alter the substrate profile of beta-lactamase. Mol Microbiol. 1994 Apr; 12(2):217-29.
Score: 0.027
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Outbreak of ceftazidime resistance due to a novel extended-spectrum beta-lactamase in isolates from cancer patients. Antimicrob Agents Chemother. 1992 Sep; 36(9):1991-6.
Score: 0.024