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Clinical Microbiology and Infection, ISSN 1198-743X, 01/2010, Volume 16, Issue 1, pp. 33 - 38
Journal Article
Journal Article
Antimicrobial Agents and Chemotherapy, ISSN 0066-4804, 08/2018, Volume 62, Issue 8
Journal Article
Synlett, ISSN 0936-5214, 10/2016, Volume 27, Issue 17, pp. 2447 - 2450
Abstract 7-β-Thien-2-yl-acetamido-3-[(4-nitro-3-carboxyphenyl)thiomethyl]-3-cephem-4-carboxylic acid (CENTA) is a yellow chromogenic β-lactamases (BL)... 
letter | synthesis | CENTA | β-lactamase kinetics | chromogenic substrate | β-lactamase detection
Journal Article
Expert Review of Anti-infective Therapy, ISSN 1478-7210, 03/2018, Volume 16, Issue 3, pp. 205 - 218
Introduction: The spread of extended-spectrum β-lactamase (ESBL)-producing Enterobacteriaceae has become a major public health threat worldwide. Area covered:... 
β-lactam/β-lactamase inhibitor combinations | extended-spectrum β-lactamase-producing Enterobacteriaceae | treatment outcomes | β-lactamase | Antibiotic resistance | extended-spectrum β–lactamase-producing Enterobacteriaceae
Journal Article
Journal of Antimicrobial Chemotherapy, ISSN 0305-7453, 01/2011, Volume 66, Issue 1, pp. 48 - 53
Journal Article
Evaluation of methods for AmpC β-lactamase in gram negative clinical isolates form tertiary care hospitals, 12/2005
The purpose of this study was to simultaneously screen for Extended-spectrum β-lactamases (ESBL) and AmpC β-lactamases in gram negative clinical isolates from... 
ESBL, AmpC β -lactamases, Disk test
Journal
Comparison of double disc and three dimensional methods to screen for ESBL producers in a tertiary care hospital, 12/2006
Extended spectrum β lactamases (ESBLs) continue to be a major problem in clinical setups world over, conferring resistance to the expanded spectrum... 
Extended spectrum β lactamases, multidrug resistance, enterobacteriaceae
Journal
Journal of Inorganic Biochemistry, ISSN 0162-0134, 10/2016, Volume 163, pp. 185 - 193
Metallo-β-lactamases (MBLs) catalyse the hydrolysis of almost all β-lactam antibacterials including the latest generation carbapenems and are a growing... 
Metallo-β-lactamase | Carbapenem | β-Lactam antibiotics | Metalloenzyme | Antibiotic resistance | Zinc hydrolase | beta-Lactamases - chemistry | Metalloproteins - chemistry | Bacillus cereus - enzymology | Iron - chemistry | Bacterial Proteins - chemistry | CRYSTAL-STRUCTURE | BIOCHEMISTRY & MOLECULAR BIOLOGY | beta-Lactam antibiotics | CHEMISTRY, INORGANIC & NUCLEAR | 3-DIMENSIONAL STRUCTURE | STENOTROPHOMONAS-MALTOPHILIA | STREPTOCOCCUS-PNEUMONIAE | STRUCTURAL BASIS | BROAD-SPECTRUM INHIBITOR | THIOMANDELIC ACID | ACTIVE-SITE LOOP | BACILLUS-CEREUS | Metallo-beta-lactamase | PHOSPHORYLCHOLINE ESTERASE | MBL, metallo-β-lactamase | ROO, rubredoxin:oxygen reductase | SBL, serine-β-lactamase | Pce, phosphorylcholine esterase | EDTA, ethylenediaminetetraacetic acid | ETHE1, ethylmalonic encephalopathy 1 | IC50, half maximal inhibitory concentration | CPSF, cleavage | TCEP·HCl, tris(2-carboxyethyl)phosphine hydrochloride salt | NDM-1, New Delhi metallo-β-lactamase 1 | PMSF, phenylmethylsulfonyl fluoride | IPTG, isopropyl β-D-1-thiogalactopyranoside | VIM-2, Verona integron-encoded metallo-β-lactamase 2 | SNM, sensitivity to nitrogen mustard | polyadenylation specificity factor | SDS-PAGE, sodium dodecyl sulfate polyacrylamide gel electrophoresis | ESI MS, electrospray ionisation mass spectrometry | BcII, metallo-β-lactamase II from Bacillus cereus
Journal Article
Journal of Antimicrobial Chemotherapy, ISSN 0305-7453, 2013, Volume 68, Issue 7, pp. 1681 - 1682
Journal Article
Current Protein and Peptide Science, ISSN 1389-2037, 2018, Volume 19, Issue 2, pp. 130 - 144
Antibiotic resistance in gram-negative bacteria has emerged as a major health threat that occurs because these bacteria actively produce beta-lactamases... 
β-lactam antibiotics | Metallo-β-lactamase | Inhibitors of β-lactamases | Acylation reaction | Structure of β-lactamases | Serine-β-lactamase | Catalytic mechanism of β-lactamases | Deacylation reaction | ACTIVE-SITE | CRYSTAL-STRUCTURE | BIOCHEMISTRY & MOLECULAR BIOLOGY | ANTIBIOTIC-RESISTANCE | deacylation reaction | SIDEROPHORE MONOSULFACTAM BAL30072 | SITE-DIRECTED MUTAGENESIS | Serine-beta-lactamase | structure of beta-lactamases | inhibitors of beta-lactamases | SUBSTRATE-SPECIFICITY | beta-lactam antibiotics | ZINC-BINDING SITES | metallo-beta-lactamase | PSEUDOMONAS-AERUGINOSA | acylation reaction | catalytic mechanism of beta-lactamases | IN-VITRO ACTIVITY | STANDARD NUMBERING SCHEME | Catalytic Domain | Humans | Bacterial Proteins - chemistry | beta-Lactamase Inhibitors - pharmacology | Serine - chemistry | Zinc - chemistry | Serine - metabolism | Hydrolysis | beta-Lactamases - chemistry | Protein Binding | Bacterial Proteins - metabolism | Protein Conformation | Anti-Bacterial Agents - pharmacology | Molecular Structure | Catalysis | beta-Lactamases - metabolism | Acylation | Residues | Deactivation | β-Lactam antibiotics | Serine | Health risks | Amino acids | Amides | Metallography | Helices | Inactivation | Zinc | Inhibitors | Antibiotics | E coli | Antibiotic resistance | Penicillin | Bacteria | Deacylation | Gram-negative bacteria | Structure-function relationships
Journal Article