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References from Discovery of Symmetrical o ‐Methylpyridine Substituted Tertiary Amines and Dy(III) Complexes as Metallo‐β‐Lactamase Inhibitor and Antimicrobial. Local targets link to admitted publications; unresolved targets remain external evidence.
Global Burden of Bacterial Antimicrobial Resistance in 2019: A Systematic Analysis
10.1016/s0140-6736(21)02724-0 · 2022 · External reference
Global Burden of Bacterial Antimicrobial Resistance 1990‐2021: A Systematic Analysis with Forecasts to 2022‐2050
10.1016/s0140-6736(24)01867-1 · 2024 · External reference
Potential Economic Burden of Carbapenem‐Resistant Enterobacteriaceae (CRE) in the United States
10.1016/j.cmi.2016.09.003 · 2017 · External reference
Revised Ambler Classiffcation of Beta‐Lactamases
10.1093/jac/dki130 · 2005 · External reference
β‐Lactamases: A Focus on Current Challenges
10.1101/cshperspect.a025239 · 2016 · External reference
Molecular Analysis of Beta‐Lactamase Structure and Function
10.1078/1438-4221-00198 · 2002 · External reference
Metallo‐β‐Lactamases: A Major Threat to Human Health
10.4236/ajmb.2014.43011 · 2014 · External reference
An Updated Phylogeny of the Metallo‐β‐Lactamases
10.1093/jac/dkaa392 · 2021 · External reference
How Clavulanic Acid Inhibits Serine β‐Lactamase
10.1002/cbic.202400280 · 2024 · External reference
Ceftolozane/Tazobactam:Place in Therapy
10.1080/14787210.2018.1447381 · 2018 · External reference
Sulbactam/Durlobactam:First Approval
10.1007/s40265-023-01920-6 · 2023 · External reference
Metallo‐β‐Lactamases in the Age of Multidrug Resistance: From Structure and Mechanism to Evolution, Dissemination, and Inhibitor Design
10.1021/acs.chemrev.1c00138 · 2021 · External reference
Nitroxoline and Its Derivatives Are Potent Inhibitors of Metallo‐β‐Lactamases
10.1016/j.ejmech.2021.113975 · 2022 · External reference
Discovery of 3‐Aryl Substituted Benzoxaboroles as Broad‐Spectrum Inhibitors of Serine‐ and Metallo‐β‐Lactamases
10.1016/j.bmcl.2021.127956 · 2021 · External reference
A Modified Vancomycin Molecule Confers Potent Inhibitory Efficacy Against Resistant Bacteria Mediated by Metallo‐β‐Lactamases
10.3390/molecules27227685 · 2022 · External reference
Aurones and Derivatives as Promising New Delhi Metallo‐β‐Lactamase (NDM‐1) Inhibitors
10.1016/j.bmc.2023.117559 · 2024 · External reference
Discovery of Hydroxamate as a Promising Scaffold Dually Inhibiting Metallo‐ and Serine‐β‐Lactamases
10.1016/j.ejmech.2023.116055 · 2024 · External reference
((S)‐3‐Mercapto‐2‐Methylpropanamido) Acetic Acid Derivatives as Metallo‐β‐Lactamase Inhibitors: Synthesis, Kinetic and Crystallographic Studies
10.1016/j.ejmech.2018.01.032 · 2018 · External reference
N‐Aryl Mercaptopropionamides as Broad‐Spectrum Inhibitors of Metallo‐β‐Lactamases
10.1021/acs.jmedchem.1c01755 · 2022 · External reference
Dithiocarbamates Combined with Copper for Revitalizing Meropenem Efficacy Against NDM‐1‐Producing Carbapenem‐Resistant Enterobacteriaceae
10.1016/j.bioorg.2021.105474 · 2022 · External reference
Triazolylthioacetamide: A Valid Scaffold for the Development of New Delhi Metallo β‐Lactmase‐1 (NDM‐1) Inhibitors
10.1021/acsmedchemlett.5b00495 · 2016 · External reference
Triazolylthioacetamides Confer Inhibitory Efficacy against Metallo‐β‐Lactamases IMP‐1
10.2174/1570180817999200831094019 · 2021 · External reference
Discovery of 1‐Hydroxypyridine‐2(1H)‐Thione‐6‐Carboxylic Acid as a First‐in‐Class Low‐Cytotoxic Nanomolar Metallo β‐Lactamase Inhibitor
10.1002/cmdc.201700182 · 2017 · External reference
Dipyridyl‐substituted Thiosemicarbazone as a Potent Broad‐Spectrum Inhibitor of Metallo‐β‐Lactamases
10.1016/j.bmc.2021.116128 · 2021 · External reference
Thiosemicarbazones Exhibit Inhibitory Efficacy against New Delhi Metallo‐β‐Lactamases (NDM‐1)
10.1038/s41429-021-00440-3 · 2021 · External reference
Dihydroxyphenyl‐Substituted Thiosemicarbazone: A Potent Scaffold for the Development of Metallo‐β‐Lactamases Inhibitors and Antimicrobial
10.1016/j.bioorg.2022.105928 · 2022 · External reference
Aromatic Schiff Bases Confer Inhibitory Efficacy against New Delhi Metallo‐β‐Lactamase‐1 (NDM‐1)
10.1016/j.bioorg.2022.105910 · 2022 · External reference
Synthesis and Inhibitory Activity of Acetamidophosphonic Acids against Metallo‐β‐Lactamases
10.1080/10426507.2016.1225741 · 2016 · External reference
NOTA Analogue: A First Dithiocarbamate Inhibitor of Metallo‐β‐Lactamases
10.1016/j.bmcl.2017.10.074 · 2018 · External reference
Synthesis and Preclinical Evaluation of TPA‐Based Zinc Chelators as Metallo‐β‐Lactamase Inhibitors
10.1021/acsinfecdis.8b00137 · 2018 · External reference
Synergistic Antimicrobial Properties of Active Molecular Chitosan with EDTA‐Divalent Metal Ion Compounds
10.1111/jph.12603 · 2017 · External reference
Iminodiacetic Acid as a Novel Metal‐Binding Pharmacophore for New Delhi Metallo‐β‐Lactamase Inhibitor Development
10.1002/cmdc.202000123 · 2020 · External reference
H2depda: An Acyclic Adjuvant Potentiates Meropenem Activity In Vitro against Metallo‐β‐Lactamase Producing Enterobacterales
10.1016/j.ejmech.2019.01.083 · 2019 · External reference
Bismuth Antimicrobial Drugs Serve as Broad‐Spectrum Metallo‐β‐Lactamase Inhibitors
10.1038/s41467-018-02828-6 · 2018 · External reference
Ruthenium Complexes as Prospective Inhibitors of Metallo‐β‐Lactamases to Reverse Carbapenem Resistance
10.1039/d0dt02430a · 2020 · External reference
Total Synthesis and Structural Reassignment of Aspergillomarasmine A
10.1002/anie.201509960 · 2016 · External reference
The Triple Combination of Meropenem, Avibactam, and a Metallo‐β‐Lactamase Inhibitor Optimizes Antibacterial Coverage Against Different β‐Lactamase Producers
10.1016/j.eng.2024.02.010 · 2024 · External reference
Imitation of β‐Lactam Binding Enables Broad‐Spectrum Metallo‐β‐Lactamase Inhibitors
10.1038/s41557-021-00831-x · 2022 · External reference
Zinc‐Chelating Compounds as Inhibitors of Human and Bacterial Zinc Metalloproteases
10.3390/molecules27010056 · 2022 · External reference
Theoretical and Experimental Studies of the Magnetostructural Correlations in Mononuclear DyIII Compounds Evidenced by Quantum Tunneling of Magnetization Time, Crystal Field Parameters, and Point Charge Electrostatic Mode
10.1021/acs.cgd.2c00550 · 2022 · External reference
In Situ Ligand Formations in the Synthetic Processes from Mononuclear Dy (III) Compounds to Binuclear Dy (III) Compounds: Synthesis, Structure, Magnetic Behavior and Theoretical Analysis
10.1021/acs.inorgchem.0c02863 · 2021 · External reference
A New Ligand H4Lox and Its Iron(III) Complex as a Platform for the Development of Heterotrimetallic Complexes
10.1016/j.poly.2016.06.022 · 2016 · External reference
Binuclear Molybdenum Schiff‐Base Complex: An Efficient Catalyst for the Epoxidation of Alkenes
10.1016/j.mcat.2019.110498 · 2019 · External reference