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Carbapenemase-Producing Organisms: A Global Scourge

Clinical infectious diseases, 2018-04, Vol.66 (8), p.1290-1297

2018

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New Delhi Metallo-β-Lactamase-Producing Enterobacterales Bacteria, Switzerland, 2019-2020

Emerging infectious diseases, 2021-10, Vol.27 (10), p.2628-2637

2021

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Principles and current strategies targeting metallo‐β‐lactamase mediated antibacterial resistance

Medicinal research reviews, 2020-09, Vol.40 (5), p.1558-1592

2020

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Global dissemination of extensively drug‐resistant carbapenemase‐producing Enterobacteriaceae: clinical perspectives on detection, treatment and infection control

Journal of internal medicine, 2015-05, Vol.277 (5), p.501-512

2015

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Metallo-β-Lactamases: Structure, Function, Epidemiology, Treatment Options, and the Development Pipeline

Antimicrobial agents and chemotherapy, 2020-09, Vol.64 (10)

2020

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Structure-guided optimization of D-captopril for discovery of potent NDM-1 inhibitors

Bioorganic & medicinal chemistry, 2021-01, Vol.29, p.115902-115902, Article 115902

2021

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Elucidation of critical chemical moieties of metallo-β-lactamase inhibitors and prioritisation of target metallo-β-lactamases

Journal of enzyme inhibition and medicinal chemistry, 2024-12, Vol.39 (1), p.2318830-2318830

2024

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Molecular and computational approaches to understand resistance of New Delhi metallo β-lactamase variants (NDM-1, NDM-4, NDM-5, NDM-6, NDM-7)-producing strains against carbapenems

Journal of biomolecular structure & dynamics, 2019-05, Vol.37 (8), p.2061-2071

2019

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H2depda: An acyclic adjuvant potentiates meropenem activity in vitro against metallo-β-lactamase-producing enterobacterales

European journal of medicinal chemistry, 2019-04, Vol.167, p.367-376

2019

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Exploring Aztreonam in Combination with Ceftazidime-Avibactam or Meropenem-Vaborbactam as Potential Treatments for Metallo- and Serine-β-Lactamase-Producing Enterobacteriaceae

Antimicrobial agents and chemotherapy, 2019-12, Vol.63 (12)

2019

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Occurrence and Transmission of blaNDM-Carrying Enterobacteriaceae from Geese and the Surrounding Environment on a Commercial Goose Farm

Applied and environmental microbiology, 2021-05, Vol.87 (10)

2021

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Crystal structure of NDM‐1 reveals a common β‐lactam hydrolysis mechanism

The FASEB journal, 2011-08, Vol.25 (8), p.2574-2582

2011

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β-Lactamases and β-Lactamase Inhibitors in the 21st Century

Journal of molecular biology, 2019-08, Vol.431 (18), p.3472-3500

2019

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Carbapenem resistance in Acinetobacter baumannii: mechanisms and epidemiology

Clinical microbiology and infection, 2006-09, Vol.12 (9), p.826-836

2006

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Could β-Lactam Antibiotics Block Humoral Immunity?

Frontiers in immunology, 2021-09, Vol.12, p.680146-680146

2021

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Gene Network Analysis of Metallo Beta Lactamase Family Proteins Indicates the Role of Gene Partners in Antibiotic Resistance and Reveals Important Drug Targets

Journal of cellular biochemistry, 2016-06, Vol.117 (6), p.1330-1339

2016

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Zinc-binding metallophores protect Pseudomonas aeruginosa from calprotectin-mediated metal starvation

FEMS microbiology letters, 2022-08, Vol.369 (1)

2022

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Crystal structure of New Delhi metallo‐β‐lactamase reveals molecular basis for antibiotic resistance

Protein science, 2011-09, Vol.20 (9), p.1484-1491

2011

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Approaches for the discovery of metallo‐β‐lactamase inhibitors: A review

Chemical biology & drug design, 2019-08, Vol.94 (2), p.1427-1440

2019

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Changing Genotypic Distribution, Antimicrobial Susceptibilities, and Risk Factors of Urinary Tract Infection Caused by Carbapenemase-Producing Pseudomonas aeruginosa

Annals of Laboratory Medicine, 2024, 44(1), , pp.38-46

2024

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Genetic Features Leading to Reduced Susceptibility to Aztreonam-Avibactam among Metallo-β-Lactamase-Producing Escherichia coli Isolates

Antimicrobial agents and chemotherapy, 2020-11, Vol.64 (12)

2020

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A multiscale approach to predict the binding mode of metallo beta‐lactamase inhibitors

Proteins, structure, function, and bioinformatics, 2022-02, Vol.90 (2), p.372-384

2022

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Worldwide trend discovery of structural and functional relationship of metallo-β-lactamase for structure-based drug design: A bibliometric evaluation and patent analysis

International journal of biological macromolecules, 2024-01, Vol.256 (Pt 2), p.128230-128230, Article 128230

2024

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A close look onto structural models and primary ligands of metallo-β-lactamases

Drug resistance updates, 2018-09, Vol.40 (9), p.1-12

2018

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Benchmark studies of hydrogen bond governing reactivity of cephalosporins in L1 metallo‐β‐lactamase: Efficient and reliable QSPR equations

International journal of quantum chemistry, 2021-02, Vol.121 (4), p.n/a

2021

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Carbapenemase-Producing Organisms: A Global Scourge

New Delhi Metallo-β-Lactamase-Producing Enterobacterales Bacteria, Switzerland, 2019-2020

Principles and current strategies targeting metallo‐β‐lactamase mediated antibacterial resistance

Global dissemination of extensively drug‐resistant carbapenemase‐producing Enterobacteriaceae: clinical perspectives on detection, treatment and infection control

Metallo-β-Lactamases: Structure, Function, Epidemiology, Treatment Options, and the Development Pipeline

Structure-guided optimization of D-captopril for discovery of potent NDM-1 inhibitors

Elucidation of critical chemical moieties of metallo-β-lactamase inhibitors and prioritisation of target metallo-β-lactamases

Molecular and computational approaches to understand resistance of New Delhi metallo β-lactamase variants (NDM-1, NDM-4, NDM-5, NDM-6, NDM-7)-producing strains against carbapenems

H2depda: An acyclic adjuvant potentiates meropenem activity in vitro against metallo-β-lactamase-producing enterobacterales

Exploring Aztreonam in Combination with Ceftazidime-Avibactam or Meropenem-Vaborbactam as Potential Treatments for Metallo- and Serine-β-Lactamase-Producing Enterobacteriaceae

Occurrence and Transmission of blaNDM-Carrying Enterobacteriaceae from Geese and the Surrounding Environment on a Commercial Goose Farm

Crystal structure of NDM‐1 reveals a common β‐lactam hydrolysis mechanism

β-Lactamases and β-Lactamase Inhibitors in the 21st Century

Carbapenem resistance in Acinetobacter baumannii: mechanisms and epidemiology

Could β-Lactam Antibiotics Block Humoral Immunity?

Gene Network Analysis of Metallo Beta Lactamase Family Proteins Indicates the Role of Gene Partners in Antibiotic Resistance and Reveals Important Drug Targets

Zinc-binding metallophores protect Pseudomonas aeruginosa from calprotectin-mediated metal starvation

Crystal structure of New Delhi metallo‐β‐lactamase reveals molecular basis for antibiotic resistance

Approaches for the discovery of metallo‐β‐lactamase inhibitors: A review

Changing Genotypic Distribution, Antimicrobial Susceptibilities, and Risk Factors of Urinary Tract Infection Caused by Carbapenemase-Producing Pseudomonas aeruginosa

Genetic Features Leading to Reduced Susceptibility to Aztreonam-Avibactam among Metallo-β-Lactamase-Producing Escherichia coli Isolates

A multiscale approach to predict the binding mode of metallo beta‐lactamase inhibitors

Worldwide trend discovery of structural and functional relationship of metallo-β-lactamase for structure-based drug design: A bibliometric evaluation and patent analysis

A close look onto structural models and primary ligands of metallo-β-lactamases

Benchmark studies of hydrogen bond governing reactivity of cephalosporins in L1 metallo‐β‐lactamase: Efficient and reliable QSPR equations

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