[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
|
|
|