Search Results - "Mehta, Shrenik C"

Natural Variants of the KPC-2 Carbapenemase have Evolved Increased Catalytic Efficiency for Ceftazidime Hydrolysis at the Cost of Enzyme Stability by Mehta, Shrenik C, Rice, Kacie, Palzkill, Timothy

“…The spread of β-lactamases that hydrolyze penicillins, cephalosporins and carbapenems among Gram-negative bacteria has limited options for treating bacterial…”
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PBP2a mutations causing high-level Ceftaroline resistance in clinical methicillin-resistant Staphylococcus aureus isolates by Long, S Wesley, Olsen, Randall J, Mehta, Shrenik C, Palzkill, Timothy, Cernoch, Patricia L, Perez, Katherine K, Musick, William L, Rosato, Adriana E, Musser, James M

“…Ceftaroline is the first member of a novel class of cephalosporins approved for use in the United States. Although prior studies have identified eight…”
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KPC-2 β-lactamase enables carbapenem antibiotic resistance through fast deacylation of the covalent intermediate by Mehta, Shrenik C., Furey, Ian M., Pemberton, Orville A., Boragine, David M., Chen, Yu, Palzkill, Timothy

“…Serine active-site β-lactamases hydrolyze β-lactam antibiotics through the formation of a covalent acyl-enzyme intermediate followed by deacylation via an…”
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Protein conjugates and fusion proteins as ocular therapeutics by Mehta, Shrenik C., Kelley, Robert F., Tesar, Devin B.

“…•Current treatments for AMD and the need for LAD are summarized.•Key considerations for development of LAD technologies are detailed.•Currently marketed…”
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Local interactions with the Glu166 base and the conformation of an active site loop play key roles in carbapenem hydrolysis by the KPC-2 β-lactamase by Furey, Ian M., Mehta, Shrenik C., Sankaran, Banumathi, Hu, Liya, Prasad, B.V. Venkataram, Palzkill, Timothy

“…The Klebsiella pneumoniae carbapenemase-2 (KPC-2) is a common source of antibiotic resistance in Gram-negative bacterial infections. KPC-2 is a class A…”
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Lead Optimization Yields High Affinity Frizzled 7‑Targeting Peptides That Modulate Clostridium difficile Toxin B Pathogenicity in Epithelial Cells by Hansen, Simon, Nile, Aaron H, Mehta, Shrenik C, Fuhrmann, Jakob, Hannoush, Rami N

“…Frizzled 7 (FZD7) receptors have been shown to play a central role in intestinal stem cell regeneration and, more recently, in Clostridium difficile…”
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Discovery of Allosteric Modulators of Factor XIa by Targeting Hydrophobic Domains Adjacent to Its Heparin-Binding Site by Karuturi, Rajesh, Al-Horani, Rami A, Mehta, Shrenik C, Gailani, David, Desai, Umesh R

“…To discover promising sulfated allosteric modulators (SAMs) of glycosaminoglycan-binding proteins (GBPs), such as human factor XIa (FXIa), we screened a…”
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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 β‑Lactamases by Relieving Steric Strain by Stojanoski, Vlatko, Adamski, Carolyn J, Hu, Liya, Mehta, Shrenik C, Sankaran, Banumathi, Zwart, Peter, Prasad, B. V. Venkataram, Palzkill, Timothy

“…Serine β-lactamases are bacterial enzymes that hydrolyze β-lactam antibiotics. They utilize an active-site serine residue as a nucleophile, forming an…”
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Deep Sequencing of Random Mutant Libraries Reveals the Active Site of the Narrow Specificity CphA Metallo-β-Lactamase is Fragile to Mutations by Sun, Zhizeng, Mehta, Shrenik C., Adamski, Carolyn J., Gibbs, Richard A., Palzkill, Timothy

“…CphA is a Zn 2+ -dependent metallo-β-lactamase that efficiently hydrolyzes only carbapenem antibiotics. To understand the sequence requirements for CphA…”
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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: e1004949 by Mehta, Shrenik C, Rice, Kacie, Palzkill, Timothy

“…The spread of β-lactamases that hydrolyze penicillins, cephalosporins and carbapenems among Gram-negative bacteria has limited options for treating bacterial…”
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Avoiding the Carbapenem Trap: KPC‐2 β‐lactamase Sequence Requirements for Carbapenem Hydrolysis by Mehta, Shrenik C, Samanta, Moumita, Chow, Dar‐Chone, Palzkill, Timothy

“…Abstract only β‐lactamases are bacterial enzymes that mediate antibiotic resistance through hydrolysis and inactivation of β‐lactam antibiotics. The hydrolysis…”
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KPC-2 β-lactamase enables carbapenem antibiotic resistance through fast deacylation of the covalent intermediate by Mehta, Shrenik C, Furey, Ian M, Pemberton, Orville A, Boragine, David M, Chen, Yu, Palzkill, Timothy

“…Serine active-site β-lactamases hydrolyze β-lactam antibiotics through the formation of a covalent acyl-enzyme intermediate followed by deacylation via an…”
Get full text

Deep Sequencing of Random Mutant Libraries Reveals the Active Site of the Narrow Specificity CphA Metallo-[beta]-Lactamase is Fragile to Mutations by Sun, Zhizeng, Mehta, Shrenik C, Adamski, Carolyn J, Gibbs, Richard A, Palzkill, Timothy

“…CphA is a Zn2+ -dependent metallo-β-lactamase that efficiently hydrolyzes only carbapenem antibiotics. To understand the sequence requirements for CphA…”
Get full text