S. Vakulenko

发表

Kinetic mechanism of enterococcal aminoglycoside phosphotransferase 2"-Ib.

J. Zajicek, S. Mobashery, M. Tóth, 2007, Biochemistry.

The Importance of a Critical Protonation State and the Fate of the Catalytic Steps in Class A β-Lactamases and Penicillin-binding Proteins*

S. Meroueh, T. Stemmler, D. Golemi-Kotra, 2004, Journal of Biological Chemistry.

An antibiotic-resistance enzyme from a deep-sea bacterium.

S. Mobashery, M. Tóth, Clyde A. Smith, 2010, Journal of the American Chemical Society.

Mechanistic Basis for the Action of New Cephalosporin Antibiotics Effective against Methicillin- and Vancomycin-resistant Staphylococcus aureus*

S. Mobashery, S. Vakulenko, Mijoon Lee, 2006, Journal of Biological Chemistry.

Structure of GES-1 at atomic resolution: insights into the evolution of carbapenamase activity in the class A extended-spectrum beta-lactamases.

K. Kantardjieff, Clyde A. Smith, S. Vakulenko, 2007, Acta crystallographica. Section D, Biological crystallography.

Multiplex PCR for Detection of Aminoglycoside Resistance Genes in Enterococci

M. Zervos, J. Chow, S. Vakulenko, 2003, Antimicrobial Agents and Chemotherapy.

Discovery of a New Class of Non-β-lactam Inhibitors of Penicillin-Binding Proteins with Gram-Positive Antibacterial Activity

M. Suckow, Malika Kumarasiri, Hualiang Pi, 2014, Journal of the American Chemical Society.

The Basis for Resistance to β-Lactam Antibiotics by Penicillin-binding Protein 2a of Methicillin-resistant Staphylococcus aureus*

S. Mobashery, S. Vakulenko, Shahriar Mobashery, 2004, Journal of Biological Chemistry.

Effects of Asp-179 mutations in TEMpUC19 beta-lactamase on susceptibility to beta-lactams

S. Mobashery, M. Tóth, S. Vakulenko, 1995, Antimicrobial agents and chemotherapy.

Structural Analysis of the Role of Pseudomonas aeruginosa Penicillin-Binding Protein 5 in β-Lactam Resistance

Malika Kumarasiri, S. Mobashery, M. Tóth, 2013, Antimicrobial Agents and Chemotherapy.

Evidence for Structural Elasticity of Class A β-Lactamases in the Course of Catalytic Turnover of the Novel Cephalosporin Cefepime

I. Massova, S. Mobashery, S. Vakulenko, 1996 .

The basis for resistance to beta-lactam antibiotics by penicillin-binding protein 2a of methicillin-resistant Staphylococcus aureus.

S. Mobashery, S. Vakulenko, C. Fuda, 2004, The Journal of biological chemistry.

C6 Hydroxymethyl-Substituted Carbapenem MA-1-206 Inhibits the Major Acinetobacter baumannii Carbapenemase OXA-23 by Impeding Deacylation

M. Tóth, Clyde A. Smith, S. Vakulenko, 2022, mBio.

The nucleotide sequence of an aminoglycoside 3'-phosphotransferase gene from E. coli.

S. Vakulenko, A. Simoncsits, M. Kálmán, 1987, Nucleic acids research.

Characterization of fluoroquinolone-resistant mutant strains of Mycobacterium tuberculosis selected in the laboratory and isolated from patients

G. Alangaden, S. Vakulenko, S. Lerner, 1995, Antimicrobial agents and chemotherapy.

New C-3' hydroxamate-substituted and more lipophilic cyclic hydroxamate cephalosporin derivatives as a potential new generation of selective antimicrobial agents.

S. Franzblau, S. Vakulenko, U. Möllmann, 2006, Organic & biomolecular chemistry.

The l,d-Transpeptidase LdtAb from Acinetobacter baumannii Is Poorly Inhibited by Carbapenems and Has a Unique Structural Architecture.

M. Tóth, Clyde A. Smith, S. Vakulenko, 2022, ACS infectious diseases.

Purification, crystallization and preliminary X-ray analysis of the aminoglycoside-6'-acetyltransferase AAC(6')-Im.

M. Tóth, Clyde A. Smith, S. Vakulenko, 2012, Acta crystallographica. Section F, Structural biology and crystallization communications.

Purification, crystallization and preliminary X-ray analysis of the beta-lactamase Oih-1 from Oceanobacillus iheyensis.

M. Tóth, Clyde A. Smith, S. Vakulenko, 2009, Acta crystallographica. Section F, Structural biology and crystallization communications.

Purification, crystallization and preliminary X-ray analysis of aminoglycoside-2''-phosphotransferase-Ic [APH(2'')-Ic] from Enterococcus gallinarum.

L. Byrnes, Clyde A. Smith, S. Vakulenko, 2008, Acta crystallographica. Section F, Structural biology and crystallization communications.

Purification, crystallization and preliminary X-ray analysis of Enterococcus faecium aminoglycoside-2''-phosphotransferase-Ib [APH(2'')-Ib].

H. Baker, E. Baker, P. Young, 2005, Acta crystallographica. Section F, Structural biology and crystallization communications.

Source of Phosphate in the Enzymic Reaction as a Point of Distinction among Aminoglycoside 2″-Phosphotransferases*

S. Mobashery, M. Tóth, J. Chow, 2009, Journal of Biological Chemistry.

Class D β-Lactamases: Are They All Carbapenemases?

M. Tóth, S. Vakulenko, N. T. Antunes, 2014, Antimicrobial Agents and Chemotherapy.

[Nucleotide sequence of aacC2 gene from a clinical strain of Escherichia coli].

S. Vakulenko, E. Entina, 1990, Antibiotiki i khimioterapiia = Antibiotics and chemoterapy [sic].

Structure−activity Relationship for the Oxadiazole Class of Antibiotics Scheme 1. Structure of the Lead Oxadiazole 1

M. Suckow, Hualiang Pi, S. Mobashery, 2022 .

Versatility of Aminoglycosides and Prospects for Their Future

S. Mobashery, S. Vakulenko, Shahriar Mobashery, 2003, Clinical Microbiology Reviews.

Discovery of antibiotic (E)-3-(3-carboxyphenyl)-2-(4-cyanostyryl)quinazolin-4(3H)-one.

M. Suckow, J. Hermoso, Malika Kumarasiri, 2015, Journal of the American Chemical Society.

Co-opting the cell wall in fighting methicillin-resistant Staphylococcus aureus: potent inhibition of PBP 2a by two anti-MRSA beta-lactam antibiotics.

S. Mobashery, S. Vakulenko, Mijoon Lee, 2008, Journal of the American Chemical Society.

Effects on Substrate Profile by Mutational Substitutions at Positions 164 and 179 of the Class A TEMpUC19 β-Lactamase from Escherichia coli*

I. Massova, S. Mobashery, M. Tóth, 1999, The Journal of Biological Chemistry.

Zinc(II) Coordination Complexes as Membrane‐Active Fluorescent Probes and Antibiotics

James R. Johnson, W. M. Leevy, Bradley D. Smith, 2008, Chembiochem : a European journal of chemical biology.

Short Alkylated Peptoid Mimics of Antimicrobial Lipopeptides

Sean P. Palecek, Amy J. Karlsson, A. Barron, 2010, Antimicrobial Agents and Chemotherapy.

Selection and Characterization of β-Lactam–β-Lactamase Inactivator-Resistant Mutants following PCR Mutagenesis of the TEM-1 β-Lactamase Gene

Lakshmi P. Kotra, L. Kotra, S. Mobashery, 1998, Antimicrobial Agents and Chemotherapy.

Selection and characterization of beta-lactam-beta-lactamase inactivator-resistant mutants following PCR mutagenesis of the TEM-1 beta-lactamase gene.

L. Kotra, S. Mobashery, S. Vakulenko, 1998, Antimicrobial agents and chemotherapy.

DNA probes for studies of aminoglycoside resistance in enterobacteriaceae clinical strains

S. Vakulenko, S. M. Navashin, 1992, World journal of microbiology & biotechnology.

Resistance -Lactam β Penicillin-Binding Protein 5 in Pseudomonas aeruginosa Structural Analysis of the Role of

Malika Kumarasiri, S. Mobashery, M. Tóth, 2014 .

Isolation and Characterization of a Species-Specific DNA Probe for the Detection of Candida krusei

S. Vakulenko, S. Lerner, E. Manavathu, 1996, Current Microbiology.

Mutational Replacement of Leu-293 in the Class C Enterobacter cloacae P99 β-Lactamase Confers Increased MIC of Cefepime

S. Mobashery, S. Vakulenko, S. Lerner, 2002, Antimicrobial Agents and Chemotherapy.

The Class A β-Lactamase FTU-1 Is Native to Francisella tularensis

M. Tóth, S. Vakulenko, N. T. Antunes, 2011, Antimicrobial Agents and Chemotherapy.

Role of the Conserved Disulfide Bridge in Class A Carbapenemases*

M. Tóth, Clyde A. Smith, S. Vakulenko, 2016, The Journal of Biological Chemistry.

In Crystallo Time-Resolved Interaction of the Clostridioides difficile CDD-1 enzyme with Avibactam Provides New Insights into the Catalytic Mechanism of Class D β-lactamases.

M. Tóth, Clyde A. Smith, S. Vakulenko, 2021, ACS infectious diseases.

Mechanistic Basis for the Emergence of Catalytic Competence against Carbapenem Antibiotics by the GES Family of β-Lactamases

S. Mobashery, S. Vakulenko, Hilary Frase, 2009, The Journal of Biological Chemistry.

Molecular dynamics at the root of expansion of function in the M69L inhibitor-resistant TEM beta-lactamase from Escherichia coli.

Yun Zhang, Laurent Maveyraud, Samy O Meroueh, 2002, Journal of the American Chemical Society.

Class D β-lactamases do exist in Gram-positive bacteria

Sergei Vakulenko, M. Tóth, Clyde A. Smith, 2015, Nature chemical biology.

Structural basis for carbapenemase activity of the OXA-23 β-lactamase from Acinetobacter baumannii.

Malika Kumarasiri, S. Mobashery, M. Tóth, 2013, Chemistry & biology.

Critical involvement of a carbamylated lysine in catalytic function of class D β-lactamases

J. Samama, S. Mobashery, L. Maveyraud, 2001, Proceedings of the National Academy of Sciences of the United States of America.

Effects of Inactivation of d,d-Transpeptidases of Acinetobacter baumannii on Bacterial Growth and Susceptibility to β-Lactam Antibiotics

M. Tóth, S. Vakulenko, Mijoon Lee, 2021, Antimicrobial agents and chemotherapy.

Intrinsic Class D β-Lactamases of Clostridium difficile

M. Tóth, Clyde A. Smith, S. Vakulenko, 2018, mBio.

Design of novel antibiotics that bind to the ribosomal acyltransfer site.

Lakshmi P Kotra, L. Kotra, S. Mobashery, 2002, Journal of the American Chemical Society.

Mutations in the aph(2")-Ic Gene Are Responsible for Increased Levels of Aminoglycoside Resistance

J. Chow, S. Vakulenko, D. Clewell, 2002, Antimicrobial Agents and Chemotherapy.

Novel Aminoglycoside 2″-Phosphotransferase Identified in a Gram-Negative Pathogen

M. Tóth, S. Vakulenko, N. T. Antunes, 2012, Antimicrobial Agents and Chemotherapy.

Revisiting the Nucleotide and Aminoglycoside Substrate Specificity of the Bifunctional Aminoglycoside Acetyltransferase(6′)-Ie/Aminoglycoside Phosphotransferase(2″)-Ia Enzyme*

M. Tóth, S. Vakulenko, Hilary Frase, 2012, The Journal of Biological Chemistry.

Aminoglycoside resistance profile and structural architecture of the aminoglycoside acetyltransferase AAC(6')-Im

M. Tóth, Clyde A. Smith, S. Vakulenko, 2017, Microbial cell.

HYDROLYSIS OF ATP BY AMINOGLYCOSIDE 3’- PHOSPHOTRANSFERASES: AN UNEXPECTED COST TO BACTERIA FOR HARBORING AN ANTIBIOTIC RESISTANCE ENZYME

Honggao Yan, S. Mobashery, Choonkeun Kim, 2005 .

Catalytic mechanism of penicillin-binding protein 5 of Escherichia coli.

S. Meroueh, S. Mobashery, S. Vakulenko, 2007, Biochemistry.

Crystal Structure of Carbapenemase OXA-58 from Acinetobacter baumannii

M. Tóth, Clyde A. Smith, S. Vakulenko, 2014, Antimicrobial Agents and Chemotherapy.

The Crystal Structures of Substrate and Nucleotide Complexes of Enterococcus faecium Aminoglycoside-2′′-Phosphotransferase-IIa [APH(2′′)-IIa] Provide Insights into Substrate Selectivity in the APH(2′′) Subfamily

E. Baker, L. Byrnes, P. Young, 2009, Journal of bacteriology.

The Crystal Structures of Substrate and Nucleotide Complexes of Enterococcus faecium Aminoglycoside-2 (cid:2)(cid:2) -Phosphotransferase-IIa [APH(2 (cid:2)(cid:2) )-IIa] Provide Insights into Substrate Selectivity in the APH(2 (cid:2)(cid:2) ) Subfamily (cid:1) ‡

E. Baker, L. Byrnes, P. Young, 2009 .

Structural consequences of the inhibitor-resistant Ser130Gly substitution in TEM beta-lactamase.

Brian K Shoichet, B. Shoichet, D. Golemi-Kotra, 2005, Biochemistry.

A Novel Extended-Spectrum β-Lactamase, SGM-1, from an Environmental Isolate of Sphingobium sp

M. Tóth, S. Vakulenko, Hilary Frase, 2013, Antimicrobial Agents and Chemotherapy.

Class A Carbapenemase FPH-1 from Francisella philomiragia

M. Tóth, S. Vakulenko, N. T. Antunes, 2012, Antimicrobial Agents and Chemotherapy.

A Synthetic Dual Drug Sideromycin Induces Gram-Negative Bacteria To Commit Suicide with a Gram-Positive Antibiotic.

W. Boggess, S. Vakulenko, Marvin J. Miller, 2018, Journal of medicinal chemistry.

Structure of the extended-spectrum class C β-lactamase ADC-1 from Acinetobacter baumannii.

M. Tóth, Clyde A. Smith, S. Vakulenko, 2014, Acta crystallographica. Section D, Biological crystallography.

Resistance to the third-generation cephalosporin ceftazidime by a deacylation-deficient mutant of the TEM β-lactamase by the uncommon covalent-trapping mechanism.

S. Mobashery, M. Tóth, S. Vakulenko, 2011, Biochemistry.

Kinetic and Structural Requirements for Carbapenemase Activity in GES-Type β-Lactamases

Clyde A. Smith, S. Vakulenko, Hilary Frase, 2014, Biochemistry.

Importance of Position 170 in the Inhibition of GES-Type β-Lactamases by Clavulanic Acid

M. Tóth, S. Vakulenko, N. T. Antunes, 2011, Antimicrobial Agents and Chemotherapy.

Mutant TEM β-Lactamase Producing Resistance to Ceftazidime, Ampicillins, and β-Lactamase Inhibitors

Sergei Vakulenko, S. Vakulenko, Dasantila Golemi, 2002, Antimicrobial Agents and Chemotherapy.

Mutant TEM (cid:2) -Lactamase Producing Resistance to Ceftazidime, Ampicillins, and (cid:2) -Lactamase Inhibitors

S. Vakulenko, D. Golemi, 2002 .

Selection and Characterization of b-Lactam – b-Lactamase Inactivator-Resistant Mutants following PCR Mutagenesis of the TEM-1 b-Lactamase Gene

L. Kotra, S. Mobashery, S. Vakulenko, 1998 .

Insights into class D beta-lactamases are revealed by the crystal structure of the OXA10 enzyme from Pseudomonas aeruginosa.

L. Kotra, J. Samama, S. Tranier, 2000, Structure.

Characterization of the bifunctional aminoglycoside-modifying enzyme ANT(3'')-Ii/AAC(6')-IId from Serratia marcescens.

J. Zajicek, S. Mobashery, Choonkeun Kim, 2006, Biochemistry.

Aminoglycoside 2″-Phosphotransferase Type IIIa from Enterococcus*

J. Zajicek, S. Mobashery, J. Chow, 2008, Journal of Biological Chemistry.

Mutations in mmpL and in the Cell Wall Stress Stimulon Contribute to Resistance to Oxadiazole Antibiotics in Methicillin-Resistant Staphylococcus aureus

S. Mobashery, S. Vakulenko, Mayland Chang, 2014, Antimicrobial Agents and Chemotherapy.

aureusstant Staphylococcus to Oxadiazole Antibiotics in Stress Stimulon Contribute to Resistance and in the Cell Wall mmpL Mutations in

S. Mobashery, S. Vakulenko, Mayland Chang, 2014 .

Crystal structure and kinetic mechanism of aminoglycoside phosphotransferase‐2″‐IVa

M. Tóth, Clyde A. Smith, S. Vakulenko, 2010, Protein science : a publication of the Protein Society.

Structural Basis for Enhancement of Carbapenemase Activity in the OXA-51 Family of Class D β-Lactamases.

K. Kantardjieff, M. Tóth, Clyde A. Smith, 2015, ACS chemical biology.

Role of the Hydrophobic Bridge in the Carbapenemase Activity of Class D β-Lactamases

M. Tóth, Clyde A. Smith, S. Vakulenko, 2018, Antimicrobial Agents and Chemotherapy.

The First Structural and Mechanistic Insights for Class D beta-Lactamases: Evidence for a Novel Catalytic Process for Turnover of beta-Lactam Antibiotics

L. Kotra, J. Samama, S. Tranier, 2000 .

Structure of the phosphotransferase domain of the bifunctional aminoglycoside-resistance enzyme AAC(6')-Ie-APH(2'')-Ia.

M. Tóth, Clyde A. Smith, S. Vakulenko, 2014, Acta crystallographica. Section D, Biological crystallography.

A Surface Loop Modulates Activity of the Bacillus Class D β-Lactamases.

M. Tóth, Clyde A. Smith, S. Vakulenko, 2020, Journal of structural biology.

The Crystal Structures of CDD-1, the Intrinsic Class D β-Lactamase from the Pathogenic Gram-Positive Bacterium Clostridioides difficile, and its Complex with Cefotaxime.

M. Tóth, Clyde A. Smith, S. Vakulenko, 2019, Journal of structural biology.

Structural Insights into the Mechanism of Carbapenemase Activity of the OXA-48 β-Lactamase

M. Tóth, Clyde A. Smith, S. Vakulenko, 2019, Antimicrobial Agents and Chemotherapy.

Structural basis for progression toward the carbapenemase activity in the GES family of β-lactamases.

Malika Kumarasiri, S. Mobashery, M. Tóth, 2012, Journal of the American Chemical Society.

A Novel Extended-Spectrum (cid:1) -Lactamase, SGM-1, from an Environmental Isolate of Sphingobium sp.

M. Tóth, S. Vakulenko, Hilary Frase, 2013 .

Cytoplasmic-Membrane Anchoring of a Class A β-Lactamase and Its Capacity in Manifesting Antibiotic Resistance

S. Mobashery, S. Vakulenko, M. Suvorov, 2007, Antimicrobial Agents and Chemotherapy.

Antibiotic Resistance and Substrate Profiles of the Class A Carbapenemase KPC-6

S. Vakulenko, N. T. Antunes, Hilary Frase, 2012, Antimicrobial Agents and Chemotherapy.

Identification of Products of Inhibition of GES-2 β-Lactamase by Tazobactam by X-ray Crystallography and Spectrometry*

S. Mobashery, M. Tóth, Clyde A. Smith, 2011, The Journal of Biological Chemistry.

Synthetic peptidoglycan substrates for penicillin-binding protein 5 of Gram-negative bacteria.

S. Mobashery, S. Vakulenko, Mijoon Lee, 2004, The Journal of organic chemistry.

Antibacterials as wonder drugs and how their effectiveness is being compromised

L. Kotra, L. Mourey, J. Samama, 2002 .

Hydrolysis of ATP by Aminoglycoside 3′-Phosphotransferases

Honggao Yan, S. Mobashery, Choonkeun Kim, 2006, Journal of Biological Chemistry.

The C5α-Methyl-Substituted Carbapenem NA-1-157 Exhibits Potent Activity against Klebsiella spp. Isolates Producing OXA-48-Type Carbapenemases.

M. Tóth, Clyde A. Smith, S. Vakulenko, 2023, ACS infectious diseases.

The role of conserved surface hydrophobic residues in the carbapenemase activity of the class D β-lactamases.

M. Tóth, Clyde A. Smith, S. Vakulenko, 2017, Acta crystallographica. Section D, Structural biology.

Resistance to β-Lactam Antibiotics and Its Mediation by the Sensor Domain of the Transmembrane BlaR Signaling Pathway in Staphylococcus aureus * 210

S. Meroueh, D. Golemi-Kotra, S. Mobashery, 2003, The Journal of Biological Chemistry.

Structural basis for the diversity of the mechanism of nucleotide hydrolysis by the aminoglycoside-2''-phosphotransferases.

M. Tóth, Clyde A. Smith, S. Vakulenko, 2019, Acta crystallographica. Section D, Structural biology.

Mutant APH(2″)-IIa Enzymes with Increased Activity against Amikacin and Isepamicin

M. Tóth, J. Chow, Clyde A. Smith, 2010, Antimicrobial Agents and Chemotherapy.

Bulky “Gatekeeper” Residue Changes the Cosubstrate Specificity of Aminoglycoside 2″-Phosphotransferase IIa

M. Tóth, Clyde A. Smith, S. Vakulenko, 2013, Antimicrobial Agents and Chemotherapy.

Aminoglycoside 2′′-Phosphotransferase IIIa (APH(2′′)-IIIa) Prefers GTP over ATP

L. Byrnes, M. Tóth, Clyde A. Smith, 2012, The Journal of Biological Chemistry.

A mechanism-based inhibitor targeting the DD-transpeptidase activity of bacterial penicillin-binding proteins.

Sergei Vakulenko, S. Mobashery, S. Vakulenko, 2003, Journal of the American Chemical Society.

Structure of the bifunctional aminoglycoside-resistance enzyme AAC(6')-Ie-APH(2'')-Ia revealed by crystallographic and small-angle X-ray scattering analysis.

T. Weiss, M. Tóth, Clyde A. Smith, 2014, Acta crystallographica. Section D, Biological crystallography.

Structure of the phosphotransferase domain of the bifunctional aminoglycoside-resistance enzyme AAC(6')-Ie-APH(2'')-Ia.

M. Tóth, S. Vakulenko, Hilary Frase, 2014, Acta crystallographica. Section D, Biological crystallography.

A light-inactivated antibiotic.

Z. H. Li, S. Vakulenko, S. Mobashery, 2000, Journal of medicinal chemistry.

Co-opting the cell wall in fighting methicillin-resistant Staphylococcus aureus: potent inhibition of PBP 2a by two anti-MRSA beta-lactam antibiotics.

S. Mobashery, S. Vakulenko, Mijoon Lee, 2008, Journal of the American Chemical Society.

Characterization of the β-Lactam Antibiotic Sensor Domain of the MecR1 Signal Sensor/Transducer Protein from Methicillin-Resistant Staphylococcus aureus†

S. Mobashery, S. Vakulenko, J. Cha, 2007 .

The Basis for Resistance to b -Lactam Antibiotics by Penicillin-Binding Protein 2a (PBP2a) of Methicillin-Resistant Staphylococcus aureus

S. Mobashery, S. Vakulenko, M. Suvorov, 2004 .

Structure-activity relationship for the oxadiazole class of antibiotics.

M. Suckow, S. Mobashery, S. Vakulenko, 2015, Journal of medicinal chemistry.