Metallo-β-Lactamases: A Major Threat to Human Health

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American Journal of Molecular Biology

ISSN Print: 2161-6620
ISSN Online: 2161-6663
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"Metallo-β-Lactamases: A Major Threat to Human Health"
written by Emer K. Phelan, Manfredi Miraula, Christopher Selleck, David L. Ollis, Gerhard Schenk, Nataša Mitić,
published by American Journal of Molecular Biology, Vol.4 No.3, 2014

has been cited by the following article(s):

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[1]	Microbiological and molecular characterization of clinical carbapenem-resistant Pseudomonas aeruginosa isolates


[2]	Engineering of a bacterial outer membrane vesicle to a nano-scale reactor for the biodegradation of β-lactam antibiotics
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[3]	LAM-1 from Lysobacter antibioticus: A potent zinc-dependent activity that inactivates β-lactam antibiotics
	Journal of Inorganic …, 2022

[4]	Current challenges and advancements towards discovery and resistance of antibiotics
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[5]	Kinetic and Structural Characterization of the First B3 Metallo-β-Lactamase with an Active-Site Glutamic Acid
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[6]	Rational Design of Potent Inhibitors of a Metallohydrolase Using a Fragment‐Based Approach
	…, 2021

[7]	A novel cooperative MBL fold metallohydrolase from pathogen Vibrio vulnificus exhibits β-lactam antibiotic-degrading activities
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[8]	Design and Characterisation of Inhibitory Peptides against Bleg1_2478, an Evolutionary Divergent B3 Metallo-β-lactamase
	2020

[9]	Understanding the Structural Dynamics of Metallo-β-lactamase, Cystatin Related Epididymal Spermatogenic (CRES) protein, and Bacterial Inwardly Rectifying …
	2020

[10]	Structure and mechanism of potent bifunctional β-lactam-and homoserine lactone-degrading enzymes from marine microorganisms
	2020

[11]	Flexible loops of New Delhi metallo-β-lactamase modulate its activity towards different substrates
	2020

[12]	Synthesis and Biological Evaluation of Imidazole derivatives against the Metallo-Β-Lactamase IMP-1
	2020

[13]	Insights into the Mn2+ Binding Site in the Agmatinase-Like Protein (ALP): A Critical Enzyme for the Regulation of Agmatine Levels in Mammals
	2020

[14]	Synthesis and enzyme-based evaluation of analogues L-tyrosine thiol carboxylic acid inhibitor of metallo-β-lactamase IMP-1
	2019

[15]	3D-QSAR and molecular recognition of Klebsiella pneumoniae NDM-1 inhibitors
	2019

[16]	Synthesis and investigation of inhibitory activities of imidazole derivatives against the metallo-β-lactamase IMP-1
	2019

[17]	Inhibitors of Selected Bacterial Metalloenzymes
	2019

[18]	Preparation of Carbon-14 Labeled 2-(2-mercaptoacetamido)-3-phenylpropanoic Acid as Metallo-beta-lactamases Inhibitor (MBLI), for Coadministration with Beta …
	2019

[19]	Design, synthesis and evaluation of monocyclic β-lactams as inhibitors of penicillin-binding proteins of resistant bacteria
	2019

[20]	The Development of New Small-Molecule Inhibitors Targeting Bacterial Metallo-β-lactamases
	Current Topics in Medicinal Chemistry, 2018

[21]	Antibacterial and β‐Lactamase Inhibitory Activity of Monocyclic β‐Lactams
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[22]	Metal‐coordinated Hydroxide as a Nucleophile: a Brief History
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[23]	Biochemical and genetic characterization of a novel metallo-β-lactamase from marine bacterium Erythrobacter litoralis HTCC 2594
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[24]	Kinetic, mechanistic, structural and spectroscopic investigations of Bimetallic Metallohydrolases
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[25]	Identification and lead-in characterization of novel B3 metallo-β-lactamases.
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[26]	Characterization and metal coordination studies of novel metallo-B-lactamase
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[27]	Clinical Implementation of Volumetric Modulated Arc Therapy (VMAT) and Image Guided Radiotherapy (IGRT) Techniques
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[28]	Characterization of a highly efficient antibiotic-degrading metallo-β-lactamase obtained from an uncultured member of a permafrost community
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[29]	Reaction mechanism of the metallohydrolase CpsB from Streptococcus pneumoniae, a promising target for novel antimicrobial agents
	Dalton Transactions, 2017

[30]	Structure-activity relationship study and optimisation of 2-aminopyrrole-1-benzyl-4, 5-diphenyl-1H-pyrrole-3-carbonitrile as a broad spectrum metallo-β-lactamase …
	European Journal of Medicinal Chemistry, 2017

[31]	Identification and lead-in characterization of novel B3 metallo-β-lactamases
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[32]	Insights into an evolutionary strategy leading to antibiotic resistance
	Scientific Reports, 2017

[33]	Dinuclear copper (II) patellamide complexes: Studies on their potential hydrolase-like activities and in vivo stabilities
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[34]	Structure-activity relationship study and optimisation of 2-aminopyrrole-1-benzyl-4, 5-diphenyl-1H-pyrrole-3-carbonitrile as a broad spectrum metallo-β-lactamase …
	European Journal of Medicinal Chemistry, 2017

[35]	Progress toward inhibitors of metallo-β-lactamases
	2017

[36]	1, 2, 4‐Triazole‐3‐thione compounds as inhibitors of di‐zinc metallo‐β‐lactamases
	ChemMedChem, 2017

[37]	1, 2, 4‐Triazole‐3‐thione Compounds as Inhibitors of Dizinc Metallo‐β‐lactamases
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[38]	Property-Guided Synthesis of Tricyclic Indolines to Confront Antibiotic Resistance in Methicillin Resistant Staphylococcus aureus
	2016

[39]	Design, synthesis, and in vitro and biological evaluation of potent amino acid-derived thiol inhibitors of the metallo-β-lactamase IMP-1
	European Journal of Medicinal Chemistry, 2016

[40]	Captopril analogues as metallo-β-lactamase inhibitors
	Bioorganic & medicinal chemistry letters, 2016

[41]	Enhancement of antibiotic-activity through complexation with metal ions-Combined ITC, NMR, enzymatic and biological studies
	Journal of Inorganic Biochemistry, 2016

[42]	AIM‐1: An Antibiotic‐Degrading Metallohydrolase That Displays Mechanistic Flexibility
	Chemistry-A European Journal, 2016

[43]	Microbiological and molecular characterization of clinical carbapenem-resistant Pseudomonas aeruginosa isolates: doctoral dissertation: biomedical sciences …
	2016

[44]	Metallo-β-lactamase-like enzymes from non-pathogenic organisms: an illustration of functional promiscuity
	2016

[45]	Microbiological and molecular characterization of clinical carbapenem-resistant Pseudomonas aeruginosa isolates: doctoral dissertation: biomedical …
	2016

[46]	β-Lactam antibiotic-degrading enzymes from non-pathogenic marine organisms: a potential threat to human health
	JBIC Journal of Biological Inorganic Chemistry, 2015

[47]	Insight on the interaction of an agmatinase-like protein with Mn 2+ activator ions
	Journal of Inorganic Biochemistry, 2015

[48]	Synthesis, characterization and metal coordination of a potential β-lactamase inhibitor: 5-Methyl-2-phenoxymethyl-3-H-imidazole-4-carboxylic acid (PIMA)
	Arabian Journal of Chemistry, 2015

[49]	Promiscuous metallo-β-lactamases: MIM-1 and MIM-2 may play an essential role in quorum sensing networks
	Journal of Inorganic Biochemistry, 2015

[50]	Insight on the interaction of an agmatinase-like protein with Mn2+ activator ions
	Journal of Inorganic Biochemistry, 2015

[51]	Catalytic mechanisms of metallohydrolases containing two metal ions
	Advances in Protein Chemistry and Structural Biology, 2014

[52]	Chapter Three-Catalytic Mechanisms of Metallohydrolases Containing Two Metal Ions
	Advances in protein chemistry and structural biology, 2014

[53]	Metallo‐β‐lactamases and Their Biomimetic Complexes (Eur. J. Inorg. Chem. 18/2014)
	2014

[54]	Metallo‐β‐lactamases and Their Biomimetic Complexes
	European Journal of …, 2014

[1]	Current challenges and advancements towards discovery and resistance of antibiotics Journal of Molecular Structure, 2022 DOI:10.1016/j.molstruc.2021.131380

[2]	LAM-1 from Lysobacter antibioticus: A potent zinc-dependent activity that inactivates β-lactam antibiotics Journal of Inorganic Biochemistry, 2022 DOI:10.1016/j.jinorgbio.2021.111637

[3]	Engineering of a bacterial outer membrane vesicle to a nano-scale reactor for the biodegradation of β-lactam antibiotics Journal of Biotechnology, 2022 DOI:10.1016/j.jbiotec.2022.07.003

[4]	Current challenges and advancements towards discovery and resistance of antibiotics Journal of Molecular Structure, 2022 DOI:10.1016/j.molstruc.2021.131380

[5]	Engineering of a bacterial outer membrane vesicle to a nano-scale reactor for the biodegradation of β-lactam antibiotics Journal of Biotechnology, 2022 DOI:10.1016/j.jbiotec.2022.07.003

[6]	LAM-1 from Lysobacter antibioticus: A potent zinc-dependent activity that inactivates β-lactam antibiotics Journal of Inorganic Biochemistry, 2022 DOI:10.1016/j.jinorgbio.2021.111637

[7]	LAM-1 from Lysobacter antibioticus: A potent zinc-dependent activity that inactivates β-lactam antibiotics Journal of Inorganic Biochemistry, 2022 DOI:10.1016/j.jinorgbio.2021.111637

[8]	Engineering of a bacterial outer membrane vesicle to a nano-scale reactor for the biodegradation of β-lactam antibiotics Journal of Biotechnology, 2022 DOI:10.1016/j.jbiotec.2022.07.003

[9]	Rational Design of Potent Inhibitors of a Metallohydrolase Using a Fragment‐Based Approach ChemMedChem, 2021 DOI:10.1002/cmdc.202100486

[10]	A Novel Cooperative Metallo-β-Lactamase Fold Metallohydrolase from Pathogen Vibrio vulnificus Exhibits β-Lactam Antibiotic-Degrading Activities Antimicrobial Agents and Chemotherapy, 2021 DOI:10.1128/AAC.00326-21

[11]	Kinetic and Structural Characterization of the First B3 Metallo-β-Lactamase with an Active-Site Glutamic Acid Antimicrobial Agents and Chemotherapy, 2021 DOI:10.1128/AAC.00936-21

[12]	Flexible loops of New Delhi metallo-β-lactamase modulate its activity towards different substrates International Journal of Biological Macromolecules, 2020 DOI:10.1016/j.ijbiomac.2020.04.219

[13]	Structure and mechanism of potent bifunctional β-lactam- and homoserine lactone-degrading enzymes from marine microorganisms Scientific Reports, 2020 DOI:10.1038/s41598-020-68612-z

[14]	Insights into the Mn2+ Binding Site in the Agmatinase-Like Protein (ALP): A Critical Enzyme for the Regulation of Agmatine Levels in Mammals International Journal of Molecular Sciences, 2020 DOI:10.3390/ijms21114132

[15]	Structure and mechanism of potent bifunctional β-lactam- and homoserine lactone-degrading enzymes from marine microorganisms Scientific Reports, 2020 DOI:10.1038/s41598-020-68612-z

[16]	Design and Characterisation of Inhibitory Peptides against Bleg1_2478, an Evolutionary Divergent B3 Metallo-β-lactamase Molecules, 2020 DOI:10.3390/molecules25245797

[17]	3D-QSAR and molecular recognition of Klebsiella pneumoniae NDM-1 inhibitors Molecular Simulation, 2019 DOI:10.1080/08927022.2019.1579327

[18]	Inhibitors of Selected Bacterial Metalloenzymes Current Medicinal Chemistry, 2019 DOI:10.2174/0929867325666180403154018

[19]	Preparation of Carbon-14 Labeled 2-(2-mercaptoacetamido)-3-phenylpropanoic Acid as Metallo-beta-lactamases Inhibitor (MBLI), for Coadministration with Beta-lactam Antibiotics Current Organic Synthesis, 2019 DOI:10.2174/1570179416666190423114704

[20]	Biochemical and genetic characterization of a novel metallo-β-lactamase from marine bacterium Erythrobacter litoralis HTCC 2594 Scientific Reports, 2018 DOI:10.1038/s41598-018-19279-0

[21]	Metal-coordinated Hydroxide as a Nucleophile: a Brief History Zeitschrift für anorganische und allgemeine Chemie, 2018 DOI:10.1002/zaac.201800045

[22]	Biochemical and genetic characterization of a novel metallo-β-lactamase from marine bacterium Erythrobacter litoralis HTCC 2594 Scientific Reports, 2018 DOI:10.1038/s41598-018-19279-0

[23]	Biochemical and genetic characterization of a novel metallo-β-lactamase from marine bacterium Erythrobacter litoralis HTCC 2594 Scientific Reports, 2018 DOI:10.1038/s41598-018-19279-0

[24]	Metal‐coordinated Hydroxide as a Nucleophile: a Brief History Zeitschrift für anorganische und allgemeine Chemie, 2018 DOI:10.1002/zaac.201800045

[25]	Antibacterial and β‐Lactamase Inhibitory Activity of Monocyclic β‐Lactams Medicinal Research Reviews, 2018 DOI:10.1002/med.21443

[26]	1,2,4‐Triazole‐3‐thione Compounds as Inhibitors of Dizinc Metallo‐β‐lactamases ChemMedChem, 2017 DOI:10.1002/cmdc.201700186

[27]	Insights into an evolutionary strategy leading to antibiotic resistance Scientific Reports, 2017 DOI:10.1038/srep40357

[28]	Enhancement of antibiotic-activity through complexation with metal ions - Combined ITC, NMR, enzymatic and biological studies Journal of Inorganic Biochemistry, 2017 DOI:10.1016/j.jinorgbio.2016.11.028

[29]	Insights into an evolutionary strategy leading to antibiotic resistance Scientific Reports, 2017 DOI:10.1038/srep40357

[30]	Reaction mechanism of the metallohydrolase CpsB from Streptococcus pneumoniae, a promising target for novel antimicrobial agents Dalton Trans., 2017 DOI:10.1039/C7DT01350G

[31]	Structure-activity relationship study and optimisation of 2-aminopyrrole-1-benzyl-4,5-diphenyl-1 H -pyrrole-3-carbonitrile as a broad spectrum metallo-β-lactamase inhibitor European Journal of Medicinal Chemistry, 2017 DOI:10.1016/j.ejmech.2017.05.061

[32]	1,2,4-Triazole-3-thione Compounds as Inhibitors of Dizinc Metallo-β-lactamases ChemMedChem, 2017 DOI:10.1002/cmdc.201700186

[33]	Characterization of a highly efficient antibiotic-degrading metallo-β-lactamase obtained from an uncultured member of a permafrost community Metallomics, 2017 DOI:10.1039/C7MT00195A

[34]	Antibacterial and β-Lactamase Inhibitory Activity of Monocyclic β-Lactams Medicinal Research Reviews, 2017 DOI:10.1002/med.21443

[35]	Promiscuous metallo-β-lactamases: MIM-1 and MIM-2 may play an essential role in quorum sensing networks Journal of Inorganic Biochemistry, 2016 DOI:10.1016/j.jinorgbio.2015.12.014

[36]	Captopril analogues as metallo-β-lactamase inhibitors Bioorganic & Medicinal Chemistry Letters, 2016 DOI:10.1016/j.bmcl.2016.02.007

[37]	Design, synthesis, and in vitro and biological evaluation of potent amino acid-derived thiol inhibitors of the metallo-β-lactamase IMP-1 European Journal of Medicinal Chemistry, 2016 DOI:10.1016/j.ejmech.2016.03.017

[38]	AIM-1: An Antibiotic-Degrading Metallohydrolase That Displays Mechanistic Flexibility Chemistry - A European Journal, 2016 DOI:10.1002/chem.201602762

[39]	AIM‐1: An Antibiotic‐Degrading Metallohydrolase That Displays Mechanistic Flexibility Chemistry – A European Journal, 2016 DOI:10.1002/chem.201602762

[40]	Insight on the interaction of an agmatinase-like protein with Mn2+ activator ions Journal of Inorganic Biochemistry, 2015 DOI:10.1016/j.jinorgbio.2015.01.008

[41]	β-Lactam antibiotic-degrading enzymes from non-pathogenic marine organisms: a potential threat to human health JBIC Journal of Biological Inorganic Chemistry, 2015 DOI:10.1007/s00775-015-1250-x

[42]	Synthesis, characterization and metal coordination of a potential β-lactamase inhibitor: 5-Methyl-2-phenoxymethyl-3-H-imidazole-4-carboxylic acid (PIMA) Arabian Journal of Chemistry, 2015 DOI:10.1016/j.arabjc.2015.11.007

[43]	Metal-Containing Enzymes Advances in Protein Chemistry and Structural Biology, 2014 DOI:10.1016/bs.apcsb.2014.07.002

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