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Timothy Palzkill Lab

Publications

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Most Recent Publications from the Palzkill Lab

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Patel MP, Hu L, Stojanoski V, Sankaran B, Prasad BVV, Palzkill T. The Drug-Resistant Variant P167S Expands the Substrate Profile of CTX-M β-Lactamases for Oxyimino-Cephalosporin Antibiotics by Enlarging the Active Site upon Acylation. Biochemistry. In Press.

Adamski CJ, Palzkill T. Systematic substitutions at BLIP position 50 result in changes in binding specificity for class A β-lactamases. BMC Biochem. 2017 Mar 6;18(1):2.

Adamski CJ, Palzkill T. BLIP-II Employs Differential Hotspot Residues To Bind Structurally Similar Staphylococcus aureus PBP2a and Class A β-Lactamases. Biochemistry. 2017 Feb 28;56(8):1075-1084.

Hurwitz AM, Huang W, Kou B, Estes MK, Atmar RL, Palzkill T. Identification and Characterization of Single-Chain Antibodies that Specifically Bind GI Noroviruses. PLoS One. 2017 Jan 17;12(1)

Hurwitz AM, Huang W, Estes MK, Atmar RL, Palzkill T. Deep sequencing of phage-displayed peptide libraries reveals sequence motif that detects norovirus. Protein Eng Des Sel. 2017 Feb;30(2):129-139.

Chow DC, Rice K, Huang W, Atmar RL, Palzkill T. Engineering Specificity from Broad to Narrow: Design of a β-Lactamase Inhibitory Protein (BLIP) Variant That Exclusively Binds and Detects KPC β-Lactamase. ACS Infect Dis. 2016 Dec 9;2(12):969-979.

Stojanoski V, Sankaran B, Prasad BV, Poirel L, Nordmann P, Palzkill T. Structure of the catalytic domain of the colistin resistance enzyme MCR-1. BMC Biol. 2016 Sep 21;14(1):81.

Sun Z, Mehta SC, Adamski CJ, Gibbs RA, Palzkill T. Deep Sequencing of Random Mutant Libraries Reveals the Active Site of the Narrow Specificity CphA Metallo-β-Lactamase is Fragile to Mutations. Scientific Reports. 2016 Sep 12;6.

Stojanoski V, Adamski CJ, Hu L, Mehta SC, Sankaran B, Zwart P, Prasad BV, Palzkill T. Removal of the Side Chain at the Active-Site Serine by a Glycine Substitution Increases the Stability of a Wide Range of Serine β-Lactamases by Relieving Steric Strain. Biochemistry. 2016 May 3;55(17):2479-90.

Patel MP, Fryszczyn BG, Palzkill T. Characterization of the global stabilizing substitution A77V and its role in the evolution of CTX-M β-lactamases. Antimicrob Agents Chemother. 2015 Nov;59(11):6741-8.

Mehta SC, Rice K, Palzkill T. 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 1;11(6):e1004949.

Stojanoski V, Chow DC, Fryszczyn B, Hu L, Nordmann P, Poirel L, Sankaran B, Prasad BV, Palzkill T. Structural Basis for Different Substrate Profiles of Two Closely Related Class D β-Lactamases and Their Inhibition by Halogens. Biochemistry. 2015 Jun 2;54(21):3370-80.

Stojanoski V, Chow DC, Hu L, Sankaran B, Gilbert HF, Prasad BV, Palzkill T. A triple mutant in the Ω-loop of TEM-1 β-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.

Adamski CJ, Cardenas AM, Brown NG, Horton LB, Sankaran B, Prasad BV, Gilbert HF, Palzkill T. Molecular basis for the catalytic specificity of the CTX-M extended-spectrum β-lactamases. Biochemistry. 2015 Jan 20;54(2):447-57.

Fryszczyn BG, Adamski CJ, Brown NG, Rice K, Huang W, Palzkill T. Role of β-lactamase residues in a common interface for binding the structurally unrelated inhibitory proteins BLIP and BLIP-II. Protein Sci. 2014 Sep;23(9):1235-46.

Huang W, Samanta M, Crawford SE, Estes MK, Neill FH, Atmar RL, Palzkill T. Identification of human single-chain antibodies with broad reactivity for noroviruses. Protein Eng Des Sel. 2014 Oct;27(10):339-49.

Brown NG, Chow DC, Ruprecht KE, Palzkill T. Identification of the β-lactamase inhibitor protein-II (BLIP-II) interface residues essential for binding affinity and specificity for class A β-lactamases. J Biol Chem. 2013 Jun 14;288(24):17156-66.

Brown NG, Chow DC, Palzkill T. BLIP-II is a highly potent inhibitor of Klebsiella pneumoniae carbapenemase (KPC-2). Antimicrob Agents Chemother. 2013 Jul;57(7):3398-401.

Rogers JD, Ajami NJ, Fryszczyn BG, Estes MK, Atmar RL, Palzkill T. Identification and characterization of a peptide affinity reagent for detection of noroviruses in clinical samples. J Clin Microbiol. 2013 Jun;51(6):1803-8.

Palzkill T. Metallo-β-lactamase structure and function. Ann N Y Acad Sci. 2013 Jan;1277:91-104.

Deng Z, Huang W, Bakkalbasi E, Brown NG, Adamski CJ, Rice K, Muzny D, Gibbs RA, Palzkill T. Deep sequencing of systematic combinatorial libraries reveals β-lactamase sequence constraints at high resolution. J Mol Biol. 2012 Dec 7;424(3-4):150-67.

Fryszczyn BG, Brown NG, Huang W, Balderas MA, Palzkill T. Use of periplasmic target protein capture for phage display engineering of tight-binding protein-protein interactions. Protein Eng Des Sel. 2011 Nov;24(11):819-28.

Yuan J, Cardenas AM, Gilbert HF, Palzkill T. Determination of the amino acid sequence requirements for catalysis by the highly proficient orotidine monophosphate decarboxylase. Protein Sci. 2011 Nov;20(11):1891-906.

Brown NG, Horton LB, Huang W, Vongpunsawad S, Palzkill T. Analysis of the functional contributions of Asn233 in metallo-β-lactamase IMP-1. Antimicrob Agents Chemother. 2011 Dec;55(12):5696-702.

Brown NG, Chow DC, Sankaran B, Zwart P, Prasad BV, Palzkill T. Analysis of the binding forces driving the tight interactions between beta-lactamase inhibitory protein-II (BLIP-II) and class A beta-lactamases. J Biol Chem. 2011 Sep 16;286(37):32723-35.

Yuan J, Chow DC, Huang W, Palzkill T. Identification of a β-lactamase inhibitory protein variant that is a potent inhibitor of Staphylococcus PC1 β-lactamase. J Mol Biol. 2011 Mar 11;406(5):730-44.

Brown NG, Pennington JM, Huang W, Ayvaz T, Palzkill T. Multiple global suppressors of protein stability defects facilitate the evolution of extended-spectrum TEM β-lactamases. J Mol Biol. 2010 Dec 17;404(5):832-46.