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Virtual Screening and Experimental Testing of B1 Metallo-β-lactamase Inhibitors

https://doi.org/10.1021/acs.jcim.8b00133
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Outgoing claims: the papers this work cites, builds on, or argues with.

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AIM‐1: An Antibiotic‐Degrading Metallohydrolase That Displays Mechanistic Flexibility
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Diaryl‐Substituted Azolylthioacetamides: Inhibitor Discovery of New Delhi Metallo‐β‐Lactamase‐1 (NDM‐1)
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Discovery of 1‐Hydroxypyridine‐2(1H)‐thione‐6‐carboxylic Acid as a First‐in‐Class Low‐Cytotoxic Nanomolar Metallo β‐Lactamase Inhibitor
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SWISS‐MODEL and the Swiss‐Pdb Viewer: An environment for comparative protein modeling
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The 3‐D structure of a zinc metallo‐beta‐lactamase from Bacillus cereus reveals a new type of protein fold.
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AutoDock4 and AutoDockTools4: Automated docking with selective receptor flexibility
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Understanding the determinants of substrate specificity in IMP family metallo‐β‐lactamases: The importance of residue 262
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Crystal structure of New Delhi metallo‐β‐lactamase reveals molecular basis for antibiotic resistance
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Zinc binding in proteins and solution: A simple but accurate nonbonded representation
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Avalanche for shape and feature-based virtual screening with 3D alignment
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The use of 4-(2-pyridylazo)resorcinol in studies of zinc release from Escherichia coli aspartate transcarbamoylase
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Sequence analysis of the L1 metallo-β-lactamase from Xanthomonas maltophilia
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VMD: Visual molecular dynamics
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The identification of new metallo-β-lactamase inhibitor leads from fragment-based screening
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3-Mercapto-1,2,4-triazoles and N-acylated thiosemicarbazides as metallo-β-lactamase inhibitors
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Captopril analogues as metallo-β-lactamase inhibitors
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Synthesis and kinetic testing of new inhibitors for a metallo-β-lactamase from Klebsiella pneumonia and Pseudomonas aeruginosa
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Design, synthesis, and in vitro and biological evaluation of potent amino acid-derived thiol inhibitors of the metallo-β-lactamase IMP-1
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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
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Novel IMP-1 metallo-β-lactamase inhibitors can reverse meropenem resistance inEscherichia coliexpressing IMP-1
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Whole-genome sequencing enabling the detection of a colistin-resistant hypermutating Citrobacter werkmanii strain harbouring a novel metallo-β-lactamase VIM-48
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Hydroxyl Groups in the ββ Sandwich of Metallo-β-lactamases Favor Enzyme Activity: A Computational Protein Design Study
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The Three-Dimensional Structure of VIM-2, a Zn-β-Lactamase from Pseudomonas aeruginosa in Its Reduced and Oxidised Form
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Insight into stereochemistry of a new IMP allelic variant (IMP-55) metallo-β-lactamase identified in a clinical strain of Acinetobacter baumannii
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Alarming β-lactamase-mediated resistance in multidrug-resistant Enterobacteriaceae
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Antibiotic sensitization using biphenyl tetrazoles as potent inhibitors of Bacteroides fragilis metallo-β-lactamase
inferredcites →https://doi.org/10.1016/s1473-3099(11)70056-1openalex-snapshot
Metallo-β-lactamases: a last frontier for β-lactams?
inferredcites →https://doi.org/10.1021/acs.biochem.5b00106openalex-snapshot
Exploring the Role of Residue 228 in Substrate and Inhibitor Recognition by VIM Metallo-β-lactamases
inferredcites →https://doi.org/10.1021/acs.jmedchem.5b01289openalex-snapshot
Discovery of Novel Inhibitor Scaffolds against the Metallo-β-lactamase VIM-2 by Surface Plasmon Resonance (SPR) Based Fragment Screening
inferredcites →https://doi.org/10.1021/acsmedchemlett.5b00098openalex-snapshot
Amino Acid Thioester Derivatives: A Highly Promising Scaffold for the Development of Metallo-β-lactamase L1 Inhibitors
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Triazolylthioacetamide: A Valid Scaffold for the Development of New Delhi Metallo-β-Lactmase-1 (NDM-1) Inhibitors
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Carbamylmethyl Mercaptoacetate Thioether: A Novel Scaffold for the Development of L1 Metallo-β-lactamase Inhibitors
inferredcites →https://doi.org/10.1021/acsmedchemlett.7b00548openalex-snapshot
Rhodanine as a Potent Scaffold for the Development of Broad-Spectrum Metallo-β-lactamase Inhibitors
inferredcites →https://doi.org/10.1021/ar0400241openalex-snapshot
Metallo-β-lactamases: Novel Weaponry for Antibiotic Resistance in Bacteria
inferredcites →https://doi.org/10.1021/bi001860vopenalex-snapshot
Familial Mutations and Zinc Stoichiometry Determine the Rate-Limiting Step of Nitrocefin Hydrolysis by Metallo-β-lactamase from Bacteroides fragilis
inferredcites →https://doi.org/10.1021/bi050801kopenalex-snapshot
Virtual Screening against Metalloenzymes for Inhibitors and Substrates
inferredcites →https://doi.org/10.1021/bi100232qopenalex-snapshot
Biochemical and Structural Characterization of Mycobacterium tuberculosis β-Lactamase with the Carbapenems Ertapenem and Doripenem
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Characterization of Purified New Delhi Metallo-β-lactamase-1
inferredcites →https://doi.org/10.1021/bi500916yopenalex-snapshot
Biochemical, Mechanistic, and Spectroscopic Characterization of Metallo-β-lactamase VIM-2
inferredcites →https://doi.org/10.1021/bi9730339openalex-snapshot
Unanticipated Inhibition of the Metallo-β-lactamase from Bacteroides fragilis by 4-Morpholineethanesulfonic Acid (MES): A Crystallographic Study at 1.85-Å Resolution
inferredcites →https://doi.org/10.1021/bi992569mopenalex-snapshot
Crystal Structure of the IMP-1 Metallo β-Lactamase from Pseudomonas aeruginosa and Its Complex with a Mercaptocarboxylate Inhibitor: Binding Determinants of a Potent, Broad-Spectrum Inhibitor,
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Bacterial Resistance to β-Lactam Antibiotics: Compelling Opportunism, Compelling Opportunity
inferredcites →https://doi.org/10.1021/ja0657556openalex-snapshot
Role of Zinc Content on the Catalytic Efficiency of B1 Metallo β-Lactamases
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New Delhi Metallo-β-Lactamase: Structural Insights into β-Lactam Recognition and Inhibition
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Shape Signatures: A New Approach to Computer-Aided Ligand- and Receptor-Based Drug Design
inferredcites →https://doi.org/10.1021/jm701031nopenalex-snapshot
Crystallographic Investigation of the Inhibition Mode of a VIM-2 Metallo-β-lactamase from Pseudomonas aeruginosa by a Mercaptocarboxylate Inhibitor
inferredcites →https://doi.org/10.1021/jm901137jopenalex-snapshot
New Substructure Filters for Removal of Pan Assay Interference Compounds (PAINS) from Screening Libraries and for Their Exclusion in Bioassays
inferredcites →https://doi.org/10.1021/jm9012938openalex-snapshot
Evolving Carbapenemases: Can Medicinal Chemists Advance One Step Ahead of the Coming Storm?
inferredcites →https://doi.org/10.1038/513481aopenalex-snapshot
Chemistry: Chemical con artists foil drug discovery
inferredcites →https://doi.org/10.1038/nature13445openalex-snapshot
Aspergillomarasmine A overcomes metallo-β-lactamase antibiotic resistance
inferredcites →https://doi.org/10.1038/nchem.2110openalex-snapshot
Rhodanine hydrolysis leads to potent thioenolate mediated metallo-β-lactamase inhibition
inferredcites →https://doi.org/10.1038/nchembio.2083openalex-snapshot
Membrane anchoring stabilizes and favors secretion of New Delhi metallo-β-lactamase
inferredcites →https://doi.org/10.1038/s41467-017-00601-9openalex-snapshot
A general reaction mechanism for carbapenem hydrolysis by mononuclear and binuclear metallo-β-lactamases
inferredcites →https://doi.org/10.1039/b802311eopenalex-snapshot
Structural basis for the broad-spectrum inhibition of metallo-β-lactamases by thiols
inferredcites →https://doi.org/10.1039/c3mt00359kopenalex-snapshot
Siderophore-dependent iron uptake systems as gates for antibiotic Trojan horse strategies against Pseudomonas aeruginosa
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Bifunctional antimicrobial conjugates and hybrid antimicrobials
inferredcites →https://doi.org/10.1042/bj20070573openalex-snapshot
The role of OXA-1 β-lactamase Asp66 in the stabilization of the active-site carbamate group and in substrate turnover
inferredcites →https://doi.org/10.1073/pnas.1601368113openalex-snapshot
Cross-class metallo-β-lactamase inhibition by bisthiazolidines reveals multiple binding modes
inferredcites →https://doi.org/10.1074/jbc.m104742200openalex-snapshot
Succinic Acids as Potent Inhibitors of Plasmid-borne IMP-1 Metallo-β-lactamase
inferredcites →https://doi.org/10.1074/jbc.m301062200openalex-snapshot
The 1.5-Å Structure of Chryseobacterium meningosepticum Zinc β-Lactamase in Complex with the Inhibitor, D-Captopril
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Evolution of New Delhi metallo-β-lactamase (NDM) in the clinic: Effects of NDM mutations on stability, zinc affinity, and mono-zinc activity
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On functional and structural heterogeneity of VIM-type metallo-beta-lactamases
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Biochemical characterization of New Delhi metallo-β-lactamase variants reveals differences in protein stability
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The structure of β-lactamases
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Prediction of lipoprotein signal peptides in Gram‐negative bacteria
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Impact of remote mutations on metallo‐β‐lactamase substrate specificity: Implications for the evolution of antibiotic resistance
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Synthesis and Kinetic Testing of Tetrahydropyrimidine‐2‐thione and Pyrrole Derivatives as Inhibitors of the Metallo‐β‐lactamase from Klebsiella pneumonia and Pseudomonas aeruginosa
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Metallo‐β‐lactamase structure and function
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High-Resolution Crystal Structure of the Subclass B3 Metallo-β-Lactamase BJP-1: Rational Basis for Substrate Specificity and Interaction with Sulfonamides
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Activities of NXL104 Combinations with Ceftazidime and Aztreonam against Carbapenemase-Producing Enterobacteriaceae
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Characterization of a New Metallo-β-Lactamase Gene, bla NDM-1 , and a Novel Erythromycin Esterase Gene Carried on a Unique Genetic Structure in Klebsiella pneumoniae Sequence Type 14 from India
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Structural Basis of Metallo-β-Lactamase Inhibition by Captopril Stereoisomers
inferredcites →https://doi.org/10.1128/aac.01336-09openalex-snapshot
Mutational Analysis of VIM-2 Reveals an Essential Determinant for Metallo-β-Lactamase Stability and Folding
inferredcites →https://doi.org/10.1128/aac.01440-12openalex-snapshot
The Sequence-Activity Relationship between Metallo-β-Lactamases IMP-1, IMP-6, and IMP-25 Suggests an Evolutionary Adaptation to Meropenem Exposure
inferredcites →https://doi.org/10.1128/aac.01651-15openalex-snapshot
Elucidating the Role of Residue 67 in IMP-Type Metallo-β-Lactamase Evolution
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Cyclic Boronates Inhibit All Classes of β-Lactamases
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Dissemination of NDM Metallo-β-Lactamase Genes among Clinical Isolates of Enterobacteriaceae Collected during the SMART Global Surveillance Study from 2008 to 2012
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Genetic and Biochemical Characterization of an Acquired Subgroup B3 Metallo-β-Lactamase Gene, bla AIM-1 , and Its Unique Genetic Context in Pseudomonas aeruginosa from Australia
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Biochemical Characterization of the Pseudomonas aeruginosa 101/1477 Metallo-β-Lactamase IMP-1 Produced by Escherichia coli
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Standard Numbering Scheme for Class B β-Lactamases
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N-Arylsulfonyl Hydrazones as Inhibitors of IMP-1 Metallo-β-Lactamase
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Sfh-I, a Subclass B2 Metallo-β-Lactamase from a Serratia fonticola Environmental Isolate
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Update of the Standard Numbering Scheme for Class B β-Lactamases
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Metallo-β-Lactamases: the Quiet before the Storm?
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The Aeromonas hydrophila cphA gene: molecular heterogeneity among class B metallo-beta-lactamases
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Probing substrate binding to Metallo-β-Lactamase L1 from Stenotrophomonas maltophilia by using site-directed mutagenesis
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Structure of Apo- and Monometalated Forms of NDM-1—A Highly Potent Carbapenem-Hydrolyzing Metallo-β-Lactamase
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Discovery of Novel New Delhi Metallo-β-Lactamases-1 Inhibitors by Multistep Virtual Screening
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Metallo beta lactamases inPseudomonas aeruginosaand Acinetobacter species
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Targeting Metallo-β-Lactamase Enzymes in Antibiotic Resistance

What points at this work

Incoming claims: where this work appears in other papers’ reference lists and arguments.

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