TIMOTHY PALZKILL to Enzyme Stability
This is a "connection" page, showing publications TIMOTHY PALZKILL has written about Enzyme Stability.
Connection Strength
0.855
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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: 0.151
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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: 0.139
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Removal of the Side Chain at the Active-Site Serine by a Glycine Substitution Increases the Stability of a Wide Range of Serine ?-Lactamases by Relieving Steric Strain. Biochemistry. 2016 05 03; 55(17):2479-90.
Score: 0.128
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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: 0.120
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Deep sequencing of systematic combinatorial libraries reveals ?-lactamase sequence constraints at high resolution. J Mol Biol. 2012 Dec 07; 424(3-4):150-67.
Score: 0.100
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Multiple global suppressors of protein stability defects facilitate the evolution of extended-spectrum TEM ?-lactamases. J Mol Biol. 2010 Dec 17; 404(5):832-46.
Score: 0.087
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Genetic and structural characterization of an L201P global suppressor substitution in TEM-1 beta-lactamase. J Mol Biol. 2008 Dec 05; 384(1):151-64.
Score: 0.076
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A natural polymorphism in beta-lactamase is a global suppressor. Proc Natl Acad Sci U S A. 1997 Aug 05; 94(16):8801-6.
Score: 0.035
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A secondary drug resistance mutation of TEM-1 beta-lactamase that suppresses misfolding and aggregation. Proc Natl Acad Sci U S A. 2001 Jan 02; 98(1):283-8.
Score: 0.011
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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