moxalactam has been researched along with nitrocefin in 4 studies
| Timeframe | Studies, this research(%) | All Research% |
|---|---|---|
| pre-1990 | 1 (25.00) | 18.7374 |
| 1990's | 0 (0.00) | 18.2507 |
| 2000's | 3 (75.00) | 29.6817 |
| 2010's | 0 (0.00) | 24.3611 |
| 2020's | 0 (0.00) | 2.80 |
| Authors | Studies |
|---|---|
| Amicosante, G; Caporale, B; Celenza, G; Docquier, JD; Mezzatesta, M; Pellegrini, C; Perilli, M; Rossolini, GM; Stefani, S | 1 |
| Castanheira, M; Samuelsen, Ø; Spencer, J; Walsh, TR | 1 |
| Eley, A; Greenwood, D | 1 |
| Dideberg, O; Garau, G; Hernandez, JF; Kahn, R; Nauton, L | 1 |
4 other study(ies) available for moxalactam and nitrocefin
| Article | Year |
|---|---|
Identification and characterization of a new metallo-beta-lactamase, IND-5, from a clinical isolate of Chryseobacterium indologenes.
Topics: Amino Acid Sequence; Anti-Bacterial Agents; beta-Lactam Resistance; beta-Lactamases; Carbapenems; Cephalosporins; Chryseobacterium; Flavobacteriaceae Infections; Humans; Kinetics; Microbial Sensitivity Tests; Molecular Sequence Data; Penicillins; Sequence Analysis, DNA | 2007 |
Kinetic characterization of VIM-7, a divergent member of the VIM metallo-beta-lactamase family.
Topics: Acremonium; Bacterial Proteins; beta-Lactamases; Catalysis; Catalytic Domain; Cefepime; Ceftazidime; Cephalosporins; Kinetics; Models, Molecular; Mutation; Penicillinase; Protein Structure, Tertiary; Recombinant Proteins; Structure-Activity Relationship; Substrate Specificity | 2008 |
Beta-lactamases of type culture strains of the Bacteroides fragilis group and of strains that hydrolyse cefoxitin, latamoxef and imipenem.
Topics: Bacteroides fragilis; beta-Lactamase Inhibitors; beta-Lactamases; Cefoxitin; Cephalosporins; Drug Resistance, Microbial; Imipenem; Isoelectric Point; Kinetics; Microbial Sensitivity Tests; Moxalactam; Nephelometry and Turbidimetry; Thienamycins | 1986 |
Structural insights into the design of inhibitors for the L1 metallo-beta-lactamase from Stenotrophomonas maltophilia.
Topics: Anti-Bacterial Agents; Apoenzymes; beta-Lactamase Inhibitors; beta-Lactamases; Binding Sites; Captopril; Cephalosporins; Enzyme Inhibitors; Escherichia coli; Hydrogen Bonding; Hydrogen-Ion Concentration; Indicators and Reagents; Inhibitory Concentration 50; Ligands; Models, Molecular; Molecular Structure; Moxalactam; Protein Binding; Protein Structure, Secondary; Stenotrophomonas maltophilia; Stereoisomerism; Substrate Specificity; Sulfates; Water; X-Ray Diffraction; Zinc | 2008 |