TIMOTHY PALZKILL to beta-Lactams
This is a "connection" page, showing publications TIMOTHY PALZKILL has written about beta-Lactams.
Connection Strength
1.758
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Mutagenesis of zinc ligand residue Cys221 reveals plasticity in the IMP-1 metallo-?-lactamase active site. Antimicrob Agents Chemother. 2012 Nov; 56(11):5667-77.
Score: 0.399
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Amino acid residues that contribute to substrate specificity of class A beta-lactamase SME-1. Antimicrob Agents Chemother. 2005 Aug; 49(8):3421-7.
Score: 0.245
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Exploiting the Carboxylate-Binding Pocket of ?-Lactamase Enzymes Using a Focused DNA-Encoded Chemical Library. J Med Chem. 2024 01 11; 67(1):620-642.
Score: 0.219
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Mutagenesis and structural analysis reveal the CTX-M ?-lactamase active site is optimized for cephalosporin catalysis and drug resistance. J Biol Chem. 2023 05; 299(5):104630.
Score: 0.208
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Reduced In Vitro Susceptibility of Streptococcus pyogenes to ?-Lactam Antibiotics Associated with Mutations in the pbp2x Gene Is Geographically Widespread. J Clin Microbiol. 2020 03 25; 58(4).
Score: 0.169
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Development and Evaluation of a Novel Protein-Based Assay for Specific Detection of KPC ?-Lactamases from Klebsiella pneumoniae Clinical Isolates. mSphere. 2020 01 08; 5(1).
Score: 0.166
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Analysis of the functional contributions of Asn233 in metallo-?-lactamase IMP-1. Antimicrob Agents Chemother. 2011 Dec; 55(12):5696-702.
Score: 0.093
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Biochemical characterization of beta-lactamases Bla1 and Bla2 from Bacillus anthracis. Antimicrob Agents Chemother. 2003 Jun; 47(6):2040-2.
Score: 0.053
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Molecular analysis of beta-lactamase structure and function. Int J Med Microbiol. 2002 Jul; 292(2):127-37.
Score: 0.049
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A Standard Numbering Scheme for Class C ?-Lactamases. Antimicrob Agents Chemother. 2020 02 21; 64(3).
Score: 0.042
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Susceptibility of beta-lactamase to core amino acid substitutions. Protein Eng. 1999 Sep; 12(9):761-9.
Score: 0.041
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The role of residue 238 of TEM-1 beta-lactamase in the hydrolysis of extended-spectrum antibiotics. J Biol Chem. 1998 Oct 09; 273(41):26603-9.
Score: 0.038
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Effect of threonine-to-methionine substitution at position 265 on structure and function of TEM-1 beta-lactamase. Antimicrob Agents Chemother. 1994 Oct; 38(10):2266-9.
Score: 0.029
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The rate-limiting step in the folding of the cis-Pro167Thr mutant of TEM-1 beta-lactamase is the trans to cis isomerization of a non-proline peptide bond. Proteins. 1996 May; 25(1):104-11.
Score: 0.008