cobalt has been researched along with nitrocefin in 5 studies
Timeframe | Studies, this research(%) | All Research% |
---|---|---|
pre-1990 | 0 (0.00) | 18.7374 |
1990's | 0 (0.00) | 18.2507 |
2000's | 4 (80.00) | 29.6817 |
2010's | 1 (20.00) | 24.3611 |
2020's | 0 (0.00) | 2.80 |
Authors | Studies |
---|---|
Benkovic, SJ; Fast, W; Wang, Z | 1 |
Ceolín, M; Rasia, RM; Vila, AJ | 1 |
Bouillenne, F; Charlier, P; Duez, C; Frère, JM; Herman, R; Petrella, S; Sauvage, E | 1 |
Bennett, B; Crowder, MW; Hu, Z; Periyannan, G | 1 |
Bilyj, J; Gahan, LR; Harmer, JR; Larrabee, JA; Mitić, N; Monteiro Pedroso, M; Schenk, G; Selleck, C; Standish, AJ; Tierney, DL | 1 |
5 other study(ies) available for cobalt and nitrocefin
Article | Year |
---|---|
Familial mutations and zinc stoichiometry determine the rate-limiting step of nitrocefin hydrolysis by metallo-beta-lactamase from Bacteroides fragilis.
Topics: Amino Acid Substitution; Arginine; Bacillus cereus; Bacteroides fragilis; beta-Lactamases; Catalysis; Cephalosporins; Cobalt; Cysteine; Dialysis; Hydrolysis; Indicators and Reagents; Kinetics; Metalloproteins; Multigene Family; Mutagenesis, Site-Directed; Recombinant Proteins; Resorcinols; Spectrophotometry, Atomic; Zinc | 2001 |
Grafting a new metal ligand in the cocatalytic site of B. cereus metallo-beta-lactamase: structural flexibility without loss of activity.
Topics: Bacillus cereus; beta-Lactamases; Binding Sites; Catalytic Domain; Cephalosporins; Cobalt; Ligands; Magnetic Resonance Spectroscopy; Metals; Models, Molecular; Molecular Sequence Data; Penicillin G; Pliability; Sequence Alignment; Spectrophotometry; Zinc | 2003 |
Crystal structure of the Actinomadura R39 DD-peptidase reveals new domains in penicillin-binding proteins.
Topics: Actinomycetales; Bacterial Proteins; Cephalosporins; Cobalt; Crystallography, X-Ray; Indicators and Reagents; Models, Molecular; Penicillins; Protein Structure, Tertiary; Serine-Type D-Ala-D-Ala Carboxypeptidase | 2005 |
Role of the Zn1 and Zn2 sites in metallo-beta-lactamase L1.
Topics: beta-Lactamases; Binding Sites; Cephalosporins; Cobalt; Electron Spin Resonance Spectroscopy; Histidine; Iron; Kinetics; Magnetic Resonance Spectroscopy; Mutagenesis, Site-Directed; Organometallic Compounds; Reference Standards; Time Factors; Zinc | 2008 |
Reaction mechanism of the metallohydrolase CpsB from Streptococcus pneumoniae, a promising target for novel antimicrobial agents.
Topics: Anti-Infective Agents; Bacterial Proteins; Binding Sites; Biocatalysis; Calorimetry; Catalytic Domain; Cephalosporins; Circular Dichroism; Cobalt; Crystallography, X-Ray; Electron Spin Resonance Spectroscopy; Hydrolysis; Kinetics; Manganese; Protein Tyrosine Phosphatases; Streptococcus pneumoniae | 2017 |