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1. Full Text Epidemiological Expansion, Structural Studies, and Clinical Challenges of New β-Lactamases from Gram-Negative Bacteria
by Bush, Karen and Fisher, Jed F
Annual review of microbiology, ISSN 0066-4227, 10/2011, Volume 65, Issue 1, pp. 455 - 478
carbapenemase | β-lactam | cephalosporinase | cephalosporin | resistance | Resistance | Carbapenemase | Cephalosporinase | Cephalosporin | Bacterial Proteins - antagonists & inhibitors | Humans | Bacterial Proteins - chemistry | Bacterial Proteins - genetics | Enzyme Inhibitors - pharmacology | Gram-Negative Bacterial Infections - drug therapy | Gram-Negative Bacteria - enzymology | Gram-Negative Bacterial Infections - microbiology | Anti-Bacterial Agents - therapeutic use | Gram-Negative Bacteria - drug effects | beta-Lactamases - chemistry | Animals | beta-Lactamases - genetics | Gram-Negative Bacteria - chemistry | Drug Resistance, Multiple, Bacterial | Gram-Negative Bacterial Infections - epidemiology | Bacterial Proteins - metabolism | Anti-Bacterial Agents - pharmacology | Gram-Negative Bacteria - genetics | beta-Lactamase Inhibitors | beta-Lactamases - metabolism | Physiological aspects | Beta lactamases | Research | Gram-negative bacteria | Epidemiology | Index Medicus | Enzymes | Pathogens | Serine | Inosine monophosphate | Drug resistance | Hydrolysis | Infection | beta -Lactamase | Infectious diseases | Reviews | Inactivators | Evolution | Metallo- beta -lactamase | beta -Lactam antibiotics | Structure-function relationships
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2. Full Text A Standard Numbering Scheme for Class C beta-Lactamases
by Mack, Andrew R and Barnes, Melissa D and Taracila, Magdalena A and Hujer, Andrea M and Hujer, Kristine M and Cabot, Gabriel and Feldgarden, Michael and Haft, Daniel H and Klimke, William and van den Akker, Focco and Vila, Alejandro J and Smania, Andrea and Haider, Shozeb and Papp-Wallace, Krisztina M and Bradford, Patricia A and Rossolini, Gian Maria and Docquier, Jean-Denis and Frere, Jean-Marie and Galleni, Moreno and Hanson, Nancy D and Oliver, Antonio and Plesiat, Patrick and Poirel, Laurent and Nordmann, Patrice and Palzkill, Timothy G and Jacoby, George A and Bush, Karen and Bonomo, Robert A
Antimicrobial agents and chemotherapy, ISSN 0066-4804, 03/2020, Volume 64, Issue 3
Pharmacology & Pharmacy | Life Sciences & Biomedicine | Microbiology | Science & Technology | Gram-Positive Bacteria - drug effects | Gram-Positive Bacteria - enzymology | Gram-Positive Bacteria - genetics | beta-Lactamases - genetics | Anti-Bacterial Agents - chemistry | Gram-Negative Bacteria - genetics | beta-Lactamases - metabolism | Amino Acid Sequence | Bacterial Proteins - antagonists & inhibitors | Gene Expression | Protein Structure, Secondary | Bacterial Proteins - genetics | Terminology as Topic | International Cooperation | beta-Lactamase Inhibitors - pharmacology | beta-Lactams - chemistry | Gram-Negative Bacteria - enzymology | Sequence Homology, Amino Acid | Gram-Negative Bacteria - drug effects | Sequence Alignment | beta-Lactams - pharmacology | beta-Lactamases - classification | Bacterial Proteins - metabolism | Anti-Bacterial Agents - pharmacology | Bacterial Proteins - classification | beta-Lactam Resistance - genetics | Mutation | beta-Lactamase Inhibitors - chemistry | Index Medicus
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3. Full Text Cyclic boronates inhibit all classes of β-lactamases
by Cahill, Samuel T and Cain, Ricky and Wang, David Y and Lohans, Christopher T and Wareham, David W and Oswin, Henry P and Mohammed, Jabril and Spencer, James and Fishwick, Colin W.G and McDonough, Michael A and Schofield, Christopher J and Brema, Jürgen
Antimicrobial agents and chemotherapy, ISSN 0066-4804, 04/2017, Volume 61, Issue 4
Inhibitors | Beta-lactams | Antibiotic resistance | Beta-lactamases | Boronate | Carbapenemase | Metalloenzymes | Pharmacology & Pharmacy | Life Sciences & Biomedicine | Microbiology | Science & Technology | Enterobacteriaceae - enzymology | Bacterial Proteins - chemistry | Substrate Specificity | Crystallography, X-Ray | Thermodynamics | beta-Lactamases - genetics | Cloning, Molecular | Escherichia coli - metabolism | Protein Interaction Domains and Motifs | beta-Lactamases - metabolism | Binding Sites | Boronic Acids - chemical synthesis | Enterobacteriaceae - growth & development | Recombinant Proteins - metabolism | Bacterial Proteins - antagonists & inhibitors | Gene Expression | Protein Structure, Secondary | Bacterial Proteins - genetics | Enterobacteriaceae - genetics | Models, Molecular | Recombinant Proteins - chemistry | Recombinant Proteins - genetics | beta-Lactamase Inhibitors - pharmacology | Amino Acid Motifs | Anti-Bacterial Agents - chemical synthesis | beta-Lactamases - chemistry | beta-Lactams - pharmacology | Cyclization | Escherichia coli - genetics | Enterobacteriaceae - drug effects | beta-Lactamase Inhibitors - chemical synthesis | Protein Binding | Bacterial Proteins - metabolism | Anti-Bacterial Agents - pharmacology | beta-Lactam Resistance - genetics | Kinetics | Boronic Acids - pharmacology | beta-Lactam Resistance - drug effects | Index Medicus
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4. Full Text Structure, Genetics and Worldwide Spread of New Delhi Metallo-β-lactamase (NDM): a threat to public health
by Khan, Asad U and Maryam, Lubna and Zarrilli, Raffaele
BMC microbiology, ISSN 1471-2180, 04/2017, Volume 17, Issue 1, pp. 101 - 101
New Delhi-Metallo-Beta-Lactamases | Antibiotic resistance | Carbapenemases | Enterobacteriaceae | Life Sciences & Biomedicine | Microbiology | Science & Technology | Enterobacteriaceae - enzymology | Public Health | Enterobacteriaceae - pathogenicity | Enterobacteriaceae Infections - microbiology | Humans | Bacteria - drug effects | Bacterial Proteins - genetics | Enterobacteriaceae - genetics | Bacteria - genetics | beta-Lactamases - chemistry | Carbapenems - pharmacology | beta-Lactamases - genetics | Enterobacteriaceae - drug effects | Bacteria - enzymology | Anti-Bacterial Agents - pharmacology | beta-Lactamases - metabolism | Drug Resistance, Multiple, Bacterial - genetics | Drug Resistance, Multiple, Bacterial - drug effects | Multiplexing | Aluminum | Biological evolution | Carbapenemase | Phylogeny | Drug resistance | Antiinfectives and antibacterials | Incidence | Proteins | Microorganisms | Enzymatic activity | Phylogenetics | Gram-negative bacteria | Nosocomial infections | Catalysis | Public health | Enzymes | Environmental stress | Polymerase chain reaction | DNA microarrays | Infectious diseases | Hospitals | Inhibitors | Mutation | Carbapenems | Protein structure | Residues | Pneumonia | Oxidoreductase | Genes | Membrane permeability | Amides | Metallography | Risk | E coli | Intestine | Bacteria | β-Lactam antibiotics | Multidrug resistance | Staphylococcus infections | Exploration | Permeability | Hydrolysis | Metallo-b-lactamase | Antibiotics | Pumps | Combinatorial analysis | Acquisitions & mergers | Fitness | Index Medicus
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5. Full Text A Ugi Straightforward Access to Bis-[beta]-lactam Derivatives
by Cheibas, Cristina and Cordier, Marie and Li, Yanyan and El Kaim, Laurent
European journal of organic chemistry, ISSN 1434-193X, 07/2019, Volume 2019, Issue 27, p. 4457
Beta lactamases
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6. Full Text Evolution of New Delhi metallo-β-lactamase (NDM) in the clinic: Effects of NDM mutations on stability, zinc affinity, and mono-zinc activity
by Cheng, Zishuo and Thomas, Pei W and Ju, Lincheng and Bergstrom, Alexander and Mason, Kelly and Clayton, Delaney and Miller, Callie and Bethel, Christopher R and VanPelt, Jamie and Tierney, David L and Page, Richard C and Bonomo, Robert A and Fast, Walter and Crowder, Michael W
The Journal of biological chemistry, ISSN 0021-9258, 2018, Volume 293, Issue 32, pp. 12606 - 12618
Life Sciences & Biomedicine | Biochemistry & Molecular Biology | Science & Technology | Humans | Enzyme Stability | Models, Molecular | Anti-Bacterial Agents - metabolism | Crystallography, X-Ray | Microbial Sensitivity Tests | beta-Lactamases - chemistry | beta-Lactamases - genetics | Protein Conformation | beta-Lactamases - isolation & purification | Mutation | Zinc - pharmacology | beta-Lactamases - metabolism | beta-Lactamase Inhibitors - metabolism | Index Medicus | Editors' Picks | NDM-1 | protein evolution | antibiotic resistance | antibiotics | metalloenzyme | metallo-β-lactamase | enzyme kinetics | Co(II)-substituted enzyme | enzyme mutation
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