alanine has been researched along with penicillanic acid in 4 studies
Timeframe | Studies, this research(%) | All Research% |
---|---|---|
pre-1990 | 2 (50.00) | 18.7374 |
1990's | 0 (0.00) | 18.2507 |
2000's | 2 (50.00) | 29.6817 |
2010's | 0 (0.00) | 24.3611 |
2020's | 0 (0.00) | 2.80 |
Authors | Studies |
---|---|
Blumberg, PM; Strominger, JL | 2 |
Bonomo, RA; Carey, MP; Carey, PR; Helfand, MS; Hujer, AM; Padayatti, PS; Totir, MA; van den Akker, F | 1 |
Bethel, CR; Bonomo, RA; Knox, JR; Sun, T | 1 |
4 other study(ies) available for alanine and penicillanic acid
Article | Year |
---|---|
Inactivation of D-alanine carboxypeptidase by penicillins and cephalosporins is not lethal in Bacillus subtilis.
Topics: Alanine; Bacillus subtilis; Carboxypeptidases; Cephalosporins; Cephalothin; Cloxacillin; Factor Analysis, Statistical; Hydrogen-Ion Concentration; Microbial Sensitivity Tests; Mutation; Penicillanic Acid; Penicillins; Peptidoglycan; Structure-Activity Relationship; Time Factors | 1971 |
Five penicillin-binding components occur in Bacillus subtilis membranes.
Topics: Alanine; Amino Acids; Bacillus subtilis; Bacterial Proteins; Binding Sites; Binding, Competitive; Carbon Isotopes; Carboxypeptidases; Cell Membrane; Cephalosporins; Electrophoresis, Polyacrylamide Gel; Fluorine; Kinetics; Penicillanic Acid; Penicillin G; Penicillins; Protein Binding; Sodium Dodecyl Sulfate; Stereoisomerism; Sulfonic Acids | 1972 |
Tazobactam forms a stoichiometric trans-enamine intermediate in the E166A variant of SHV-1 beta-lactamase: 1.63 A crystal structure.
Topics: Acylation; Alanine; beta-Lactamase Inhibitors; beta-Lactamases; Binding Sites; Crystallography, X-Ray; Glutamic Acid; Models, Molecular; Molecular Conformation; Penicillanic Acid; Recombinant Proteins; Spectrum Analysis, Raman; Tazobactam | 2004 |
Inhibitor-resistant class A beta-lactamases: consequences of the Ser130-to-Gly mutation seen in Apo and tazobactam structures of the SHV-1 variant.
Topics: Alanine; Amino Acid Substitution; Apoenzymes; beta-Lactam Resistance; beta-Lactamase Inhibitors; beta-Lactamases; Binding Sites; Catalysis; Crystallography, X-Ray; Enzyme Inhibitors; Escherichia coli Proteins; Genetic Variation; Glutamic Acid; Glycine; Hydrolysis; Models, Molecular; Mutagenesis, Site-Directed; Penicillanic Acid; Serine; Tazobactam | 2004 |