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Restricted Rotational Flexibility of the C5α-Methyl-Substituted Carbapenem NA-1-157 Leads to Potent Inhibition of the GES‑5 Carbapenemase

ACS infectious diseases, 2024-04, Vol.10 (4), p.1232-1249

2024

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

ACS infectious diseases, 2023-05, Vol.9 (5), p.1123-1136

2023

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

ACS infectious diseases, 2022-09, Vol.8 (9), p.1948-1961

2022

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

ACS infectious diseases, 2022-09, Vol.8 (9), p.1948-1961

2022

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

mBio, 2022-04, Vol.13 (3), p.e0036722-e0036722

2022

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

Antimicrobial agents and chemotherapy, 2022-01, Vol.66 (1), p.e0172921-e0172921

2022

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Structural and mechanistic studies on carbapenem-hydrolysing class D serine β-lactamases leading to improved inhibitor design

Acta crystallographica. Section A, Foundations and advances, 2021-08, Vol.77 (a2), p.C104-C104

2021

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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, 2021-06, Vol.7 (6), p.1765-1776

2021

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Inhibition of the Clostridioides difficile Class D β‑Lactamase CDD‑1 by Avibactam

ACS infectious diseases, 2021-05, Vol.7 (5), p.1164-1176

2021

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A surface loop modulates activity of the Bacillus class D β-lactamases

Journal of structural biology, 2020-08, Vol.211 (2), p.107544-107544, Article 107544

2020

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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

Journal of structural biology, 2019-12, Vol.208 (3), p.107391-107391, Article 107391

2019

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Structural basis for the diversity of the mechanism of nucleotide hydrolysis by the aminoglycoside‐2′′‐phosphotransferases

Acta crystallographica. Section D, Biological crystallography., 2019-12, Vol.75 (12), p.1129-1137

2019

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

Antimicrobial agents and chemotherapy, 2019-10, Vol.63 (10)

2019

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

Antimicrobial agents and chemotherapy, 2019-02, Vol.63 (2)

2019

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Intrinsic Class D β-Lactamases of Clostridium difficile

mBio, 2018-12, Vol.9 (6)

2018

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Intrinsic Class D β-Lactamases of italic toggle="yes">Clostridium difficile /italic

mBio, 2018-12, Vol.9 (6)

2018

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

Journal of medicinal chemistry, 2018-05, Vol.61 (9), p.3845-3854

2018

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

Microbial cell, 2017-11, Vol.4 (12), p.402-410

2017

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The role of conserved surface hydrophobic residues in the carbapenemase activity of the class D [beta]-lactamases

Acta crystallographica. Section D, Biological crystallography., 2017-08, Vol.73 (8), p.692

2017

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

Acta crystallographica. Section D, Structural biology, 2017-08, Vol.73 (8), p.692-701

2017

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Role of the Conserved Disulfide Bridge in Class A Carbapenemases

The Journal of biological chemistry, 2016-10, Vol.291 (42), p.22196-22206

2016

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Role of the Conserved Disulfide Bridge in Class A CarbapenemasesThis work was supported by National Institutes of Health Grant R01AI089726 (to S. B. V.). The SSRL Structural Molecular Biology Program is supported by the Department of Energy Office of Biological and Environmental Research and by the National Institutes of Health, National Institute of General Medical Sciences (including Grant P41GM103393). The authors declare that they have no conflicts of interest with the contents of this artic

The Journal of biological chemistry, 2016-10, Vol.291 (42), p.22196-22206

2016

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

Nature chemical biology, 2016-01, Vol.12 (1), p.9

2016

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

Biochemistry (Easton), 2015-01, Vol.54 (2), p.588-597

2015

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

Acta crystallographica. Section D, Biological crystallography., 2014-10, Vol.70 (10), p.2754-2764

2014

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Restricted Rotational Flexibility of the C5α-Methyl-Substituted Carbapenem NA-1-157 Leads to Potent Inhibition of the GES‑5 Carbapenemase

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

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

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

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

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

Structural and mechanistic studies on carbapenem-hydrolysing class D serine β-lactamases leading to improved inhibitor design

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

Inhibition of the Clostridioides difficile Class D β‑Lactamase CDD‑1 by Avibactam

A surface loop modulates activity of the Bacillus class D β-lactamases

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

Structural basis for the diversity of the mechanism of nucleotide hydrolysis by the aminoglycoside‐2′′‐phosphotransferases

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

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

Intrinsic Class D β-Lactamases of Clostridium difficile

Intrinsic Class D β-Lactamases of italic toggle="yes">Clostridium difficile /italic

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

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

The role of conserved surface hydrophobic residues in the carbapenemase activity of the class D [beta]-lactamases

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

Role of the Conserved Disulfide Bridge in Class A Carbapenemases

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

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

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

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