Faculty

Institution

Unit

Venue

Sergei Vakulenko

University of Notre Dame

Affiliations

College of Science

Chemistry and Biochemistry

NoneSergei Vakulenko is currently serving as a Chemistry And Biochemistry faculty at University of Notre Dame.

Honors

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Experiences

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Education

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Sergei Vakulenko

University of Notre Dame

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pharmacology clinical microbiology biochemistry microbiology enzymes molecular biology antimicrobial resistance structural biology protein structure enzyme inhibition applied microbiology protein science drug resistance drug discovery medicinal chemistry biological chemistry antimicrobial agents antibiotic resistance structural molecular biology bacteria bacteriology biomolecular structure protein chemistry crystal structures antimicrobial chemotherapy enzyme catalysis carbapenemase activity structure-function enzyme kinetics x-ray crystallography infection control protein x-ray crystallography antimicrobial susceptibility biocatalysis microbial genetics molecular science biochemical sciences molecular structure structural chemistry medical microbiology pharmaceutical chemistry molecular microbiology biological inorganic chemistry clinical infection structural basis preliminary x-ray analysis chemical sciences redox biology antibacterial agents structural morphology respiratory infections b-lactam antibiotics acinetobacter baumannii potent inhibition escherichia coli diagnostic microbiology molecular catalysis pharmaceutical biotechnology drug targeting cell wall molecular substrates catalytic process mutagenesis structural bioinformatics emerging infectious diseases disease transmission penicillin-binding proteins gram-negative bacteria mechanistic basis ges family ges-type b-lactamases kinetic mechanism molecular diagnostics pathogen detection aminoglycoside resistance genes multiplex pcr methicillin-resistant staphylococcus aureus

Notable Scholarly Works

Notable Federal Grants

Collaborators

Decarboxylation of the Catalytic Lysine Residue by the C5α-Methyl-Substituted Carbapenem Na-1-157 Leads to Potent Inhibition of the Oxa-58 Carbapenemase. ACS Infectious Diseases (2024)

Marta TothNichole K. StewartAiliena O. MaggioloPojun QuanMd Mahbub Kabir KhanJohn D. BuynakClyde A. SmithSergei B. Vakulenko

pathogenic bacteriabiocatalysisbiochemistryprotein scienceclinical microbiologymembrane biologyenzyme catalysismedicinal chemistryinfectious diseasesredox biologyenzymespotent inhibitionprotein chemistrycarbohydrate-protein interactionsenzyme inhibitionfunctional selectivitymolecular biologyantiviral researchdrug metabolismcatalytic lysine residue

Restricted Rotational Flexibility of the C5α-Methyl-Substituted Carbapenem Na-1-157 Leads to Potent Inhibition of the Ges-5 Carbapenemase. ACS Infectious Diseases (2024)

Nichole K. StewartMarta TothPojun QuanMichael BeerJohn D. BuynakClyde A. SmithSergei B. Vakulenko

pharmacologypathogensinfection controlemerging infectious diseasesvirologyinfectious diseasesrotational flexibilityclinical infectionrespiratory infectionsglobal healthclinical infectious diseasedisease transmissionpotent inhibitionclinical microbiology

The C5α-Methyl-Substituted Carbapenem Na-1-157 Exhibits Potent Activity Against Klebsiella Spp. Isolates Producing Oxa-48-Type Carbapenemases. ACS Infectious Diseases (2023)

Clyde A. SmithNichole K. StewartMarta TothPojun QuanJohn D. BuynakSergei B. Vakulenko

pharmacologypathogensinfection controlemerging infectious diseasesmicrobial pathogenesisvirologyinfectious diseasesclinical microbiologyclinical infectionrespiratory infectionsbacteriaklebsiella pneumoniaedisease transmissionepidemiology

C6 Hydroxymethyl-Substituted Carbapenem Ma-1-206 Inhibits the Major Acinetobacter Baumannii Carbapenemase Oxa-23 by Impeding Deacylation. mBio (2022)

Nichole K. StewartMarta TothMaha A. AlqurafiWeirui ChaiThu Q. NguyenPojun QuanMijoon LeeJohn D. BuynakClyde A. SmithSergei B. Vakulenko

pharmacologybacteriologymicrobiologymicrobial pathogenesisantibacterial agentsenzyme inhibitionbacteriaglobal healthclinical microbiology

The L,D -Transpeptidase Ldt Ab From Acinetobacter Baumannii is Poorly Inhibited by Carbapenems and Has a Unique Structural Architecture. ACS Infectious Diseases (2022)

Marta TothNichole K. StewartClyde A. SmithMijoon LeeSergei B. Vakulenko

pharmacologymicrobiologydrug discoveryinfectious diseasesmicrobial pathogenesisprotein structureenzyme inhibitionclinical infectionbacteriaenzymesclinical microbiology

Effects of Inactivation of D, D -Transpeptidases of Acinetobacter Baumannii on Bacterial Growth and Susceptibility to β-Lactam Antibiotics. Antimicrobial Agents and Chemotherapy (2021)

Marta TothMijoon LeeNichole K. StewartSergei B. Vakulenko

pharmacologyb-lactam antibioticsbacteriologymicrobiologyinfectious diseasesapplied microbiologyantimicrobial resistancebacterial growthacinetobacter baumanniiantimicrobial susceptibilityclinical microbiology

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. ACS Infectious Diseases (2021)

Nichole K. StewartMarta TothAnastasiya StasyukSergei B. VakulenkoClyde A. Smith

biocatalysismicrobial geneticsbiochemistrybiomolecular interactionsprotein scienceclinical microbiologygeneticsenzyme catalysisstructure-function enzyme kineticscatalytic mechanismgene expressionstructural biologyprotein structureredox biologycatalysisstructural molecular biologyenzymesenzyme inhibitionmolecular biology

Inhibition of the Clostridioides Difficile Class D β-Lactamase Cdd-1 by Avibactam. ACS Infectious Diseases (2021)

Nichole K. StewartMarta TothAnastasiya StasyukMijoon LeeClyde A. SmithSergei B. Vakulenko

pharmacologyinfection controlmicrobiologyvirologyinfectious diseasesclinical infectionenzyme inhibitionmicrobial geneticsrespiratory infectionsbacteriadiagnostic microbiologytropical medicineclinical microbiology

Structural and Mechanistic Studies on Carbapenem-Hydrolysing Class D Serine β-Lactamases Leading to Improved Inhibitor Design. Acta Crystallographica Section A Foundations and Advances (2021)

Clyde A. SmithNichole K. StewartMarta TothSergei B. Vakulenko

biomolecular structurebiophysicsstructural biologycrystal structuresmechanistic studiesstructural chemistryprotein structurebiochemistrystructural molecular biologybiomolecular engineeringcrystallographyx-ray crystallographyenzymesinhibitor design

A Surface Loop Modulates Activity of the Bacillus Class D β-Lactamases. Journal of Structural Biology (2020)

Nichole K. StewartMonolekha BhattacharyaMarta TothClyde A. SmithSergei B. Vakulenko

pharmacologybiomolecular structurestructural biologyprotein structuremolecular biologystructural molecular biologyimmunologysurface loopenzymes

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Sergei Vakulenko

University of Notre Dame

Affiliations

College of Science

Chemistry and Biochemistry

NoneSergei Vakulenko is currently serving as a Chemistry And Biochemistry faculty at University of Notre Dame.

Honors

Create free account to unlock more features

Experiences

Create free account to unlock more features

Education

Create free account to unlock more features

Sergei Vakulenko

University of Notre Dame

You can click a keyword to filter the displayed items

Notable Scholarly Works

Notable Federal Grants

Collaborators

Decarboxylation of the Catalytic Lysine Residue by the C5α-Methyl-Substituted Carbapenem Na-1-157 Leads to Potent Inhibition of the Oxa-58 Carbapenemase. ACS Infectious Diseases (2024)

Marta TothNichole K. StewartAiliena O. MaggioloPojun QuanMd Mahbub Kabir KhanJohn D. BuynakClyde A. SmithSergei B. Vakulenko

Restricted Rotational Flexibility of the C5α-Methyl-Substituted Carbapenem Na-1-157 Leads to Potent Inhibition of the Ges-5 Carbapenemase. ACS Infectious Diseases (2024)

Nichole K. StewartMarta TothPojun QuanMichael BeerJohn D. BuynakClyde A. SmithSergei B. Vakulenko

The C5α-Methyl-Substituted Carbapenem Na-1-157 Exhibits Potent Activity Against Klebsiella Spp. Isolates Producing Oxa-48-Type Carbapenemases. ACS Infectious Diseases (2023)

Clyde A. SmithNichole K. StewartMarta TothPojun QuanJohn D. BuynakSergei B. Vakulenko

C6 Hydroxymethyl-Substituted Carbapenem Ma-1-206 Inhibits the Major Acinetobacter Baumannii Carbapenemase Oxa-23 by Impeding Deacylation. mBio (2022)

Nichole K. StewartMarta TothMaha A. AlqurafiWeirui ChaiThu Q. NguyenPojun QuanMijoon LeeJohn D. BuynakClyde A. SmithSergei B. Vakulenko

pharmacologybacteriologymicrobiologymicrobial pathogenesisantibacterial agentsenzyme inhibitionbacteriaglobal healthclinical microbiology

The L,D -Transpeptidase Ldt Ab From Acinetobacter Baumannii is Poorly Inhibited by Carbapenems and Has a Unique Structural Architecture. ACS Infectious Diseases (2022)

Marta TothNichole K. StewartClyde A. SmithMijoon LeeSergei B. Vakulenko

pharmacologymicrobiologydrug discoveryinfectious diseasesmicrobial pathogenesisprotein structureenzyme inhibitionclinical infectionbacteriaenzymesclinical microbiology

Effects of Inactivation of D, D -Transpeptidases of Acinetobacter Baumannii on Bacterial Growth and Susceptibility to β-Lactam Antibiotics. Antimicrobial Agents and Chemotherapy (2021)

Marta TothMijoon LeeNichole K. StewartSergei B. Vakulenko

Nichole K. StewartMarta TothAnastasiya StasyukSergei B. VakulenkoClyde A. Smith

Inhibition of the Clostridioides Difficile Class D β-Lactamase Cdd-1 by Avibactam. ACS Infectious Diseases (2021)

Nichole K. StewartMarta TothAnastasiya StasyukMijoon LeeClyde A. SmithSergei B. Vakulenko

Structural and Mechanistic Studies on Carbapenem-Hydrolysing Class D Serine β-Lactamases Leading to Improved Inhibitor Design. Acta Crystallographica Section A Foundations and Advances (2021)

Clyde A. SmithNichole K. StewartMarta TothSergei B. Vakulenko

A Surface Loop Modulates Activity of the Bacillus Class D β-Lactamases. Journal of Structural Biology (2020)

Nichole K. StewartMonolekha BhattacharyaMarta TothClyde A. SmithSergei B. Vakulenko

pharmacologybiomolecular structurestructural biologyprotein structuremolecular biologystructural molecular biologyimmunologysurface loopenzymes

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