Antibody Mapping of the Linear Epitopes of CMY-2 and SHV-1 β-Lactamases

Por Hujer, Andrea M., Bethel, Christopher R., Bonomo, Robert A.
Publicado em 2004

Use of Novel Boronic Acid Transition State Inhibitors To Probe Substrate Affinity in SHV-Type Extended-Spectrum β-Lactamases

Por Thomson, Jodi M., Prati, Fabio, Bethel, Christopher R., Bonomo, Robert A.
Publicado em 2007

Why the Extended-Spectrum β-Lactamases (ESBLs) SHV-2 and SHV-5 are “Hyper-Susceptible” to Mechanism-Based Inhibitors

Por Kalp, Matthew, Bethel, Christopher R., Bonomo, Robert A., Carey, Paul R.
Publicado em 2009

The Different Inhibition Mechanisms of OXA-1 and OXA-24 β-Lactamases Are Determined by the Stability of Active Site Carboxylated Lysine

Por Che, Tao, Bethel, Christopher R., Pusztai-Carey, Marianne, Bonomo, Robert A., Carey, Paul R.
Publicado em 2014

Crystal structure of KPC-2: insights into carbapenemase activity in Class A β-lactamases

Por Ke, Wei, Bethel, Christopher R., Thomson, Jodi M., Bonomo, Robert A., van den Akker, Focco
Publicado em 2007

Detection of SHV β-lactamases in Gram-negative bacilli using fluorescein-labeled antibodies

Por Hujer, Andrea M, Keslar, Karen S, Dietenberger, Nicole J, Bethel, Christopher R, Endimiani, Andrea, Bonomo, Robert A
Publicado em 2009

Inhibitor Resistance in the KPC-2 β-Lactamase, a Preeminent Property of This Class A β-Lactamase

Por Papp-Wallace, Krisztina M., Bethel, Christopher R., Distler, Anne M., Kasuboski, Courtney, Taracila, Magdalena, Bonomo, Robert A.
Publicado em 2010

Clinical Evolution of New Delhi Metallo-β-Lactamase (NDM) Optimizes Resistance under Zn(II) Deprivation

Por Bahr, Guillermo, Vitor-Horen, Luisina, Bethel, Christopher R., Bonomo, Robert A., González, Lisandro J., Vila, Alejandro J.
Publicado no Antimicrob Agents Chemother (2017)

MUTATION OF THE ACTIVE SITE CARBOXY-LYSINE (K70) OF OXA-1 β-LACTAMASE RESULTS IN A DEACYLATION-DEFICIENT ENZYME

Por Schneider, Kyle D., Bethel, Christopher R., Distler, Anne M., Hujer, Andrea M., Bonomo, Robert A., Leonard, David A.
Publicado em 2009

Carboxylation and Decarboxylation of Active Site Lys 84 Controls the Activity of OXA-24 β-Lactamase of Acinetobacter baumannii: Raman Crystallographic and Solution Evidence

Por Che, Tao, Bonomo, Robert A., Shanmugam, Sivaprakash, Bethel, Christopher R., Pusztai-Carey, Marianne, Buynak, John D., Carey, Paul R.
Publicado em 2012

Structures of SHV-1 β-Lactamase with Penem and Penam Sulfone Inhibitors That Form Cyclic Intermediates Stabilized by Carbonyl Conjugation

Por Ke, Wei, Pattanaik, Priyaranjan, Bethel, Christopher R., Sheri, Anjaneyulu, Buynak, John D., Bonomo, Robert A., van den Akker, Focco
Publicado em 2012

Crystal Structure of a Preacylation Complex of the β-Lactamase Inhibitor Sulbactam Bound to a Sulfenamide Bond-Containing Thiol-β-lactamase

Por Rodkey, Elizabeth A., Drawz, Sarah M., Sampson, Jared M., Bethel, Christopher R., Bonomo, Robert A., van den Akker, Focco
Publicado em 2012

In Vivo Evolution of CMY-2 to CMY-33 β-Lactamase in Escherichia coli Sequence Type 131: Characterization of an Acquired Extended-Spectrum AmpC Conferring Resistance to Cefepime

Por Pires, João, Taracila, Magdalena, Bethel, Christopher R., Doi, Yohei, Kasraian, Sara, Tinguely, Regula, Sendi, Parham, Bonomo, Robert A., Endimiani, Andrea
Publicado no Antimicrob Agents Chemother (2015)

The Novel β-Lactamase Inhibitor, ETX-2514, in Combination with Sulbactam Effectively Inhibits Acinetobacter baumannii

Por Barnes, Melissa D, Bethel, Christopher R, Rutter, Joseph D, Akker, Focco Van Den, Papp-Wallace, Krisztina M, Bonomo, Robert A
Publicado no Open Forum Infect Dis (2017)

Elucidating the role of Trp105 in the KPC-2 β-lactamase

Por Papp-Wallace, Krisztina M, Taracila, Magdalena, Wallace, Christopher J, Hujer, Kristine M, Bethel, Christopher R, Hornick, John M, Bonomo, Robert A
Publicado em 2010

Following Drug Uptake and Reactions inside Escherichia coli Cells by Raman Microspectroscopy

Por Heidari Torkabadi, Hossein, Bethel, Christopher R., Papp-Wallace, Krisztina M., de Boer, Piet A. J., Bonomo, Robert A., Carey, Paul R.
Publicado em 2014

Understanding the determinants of substrate specificity in IMP family metallo-β-lactamases: The importance of residue 262

Por Pegg, Kevin M, Liu, Eleanor M, George, Alex C, LaCuran, Alecander E, Bethel, Christopher R, Bonomo, Robert A, Oelschlaeger, Peter
Publicado no Protein Sci (2014)

Inactivation of the Pseudomonas-Derived Cephalosporinase-3 (PDC-3) by Relebactam

Por Barnes, Melissa D., Bethel, Christopher R., Alsop, Jim, Becka, Scott A., Rutter, Joseph D., Papp-Wallace, Krisztina M., Bonomo, Robert A.
Publicado no Antimicrob Agents Chemother (2018)

Molecular Analysis of the Simultaneous Production of Two SHV-Type Extended-Spectrum Beta-Lactamases in a Clinical Isolate of Enterobacter cloacae by Using Single-Nucleotide Polymor...

Por Szabó, Dóra, Melan, Melissa A., Hujer, Andrea M., Bonomo, Robert A., Hujer, Kristine M., Bethel, Christopher R., Kristóf, Katalin, Paterson, David L.
Publicado em 2005

Inhibition of the Class C β-Lactamase from Acinetobacter spp: Insights into Effective Inhibitor Design

Por Drawz, Sarah M., Babic, Maja, Bethel, Christopher R., Taracila, Magda, Distler, Anne M., Ori, Claudia, Caselli, Emilia, Prati, Fabio, Bonomo, Robert A.
Publicado em 2010