clavulanic acid has been researched along with asparagine in 5 studies
Timeframe | Studies, this research(%) | All Research% |
---|---|---|
pre-1990 | 0 (0.00) | 18.7374 |
1990's | 2 (40.00) | 18.2507 |
2000's | 2 (40.00) | 29.6817 |
2010's | 1 (20.00) | 24.3611 |
2020's | 0 (0.00) | 2.80 |
Authors | Studies |
---|---|
Giakkoupi, P; Legakis, NJ; Tzelepi, E; Tzouvelekis, LS | 1 |
Bulychev, A; Cabantous, S; Golemi, D; Maveyraud, L; Mobashery, S; Samama, JP; Swarén, P | 1 |
Bachmann, BO; Miller, MT; Rosenzweig, AC; Townsend, CA | 1 |
Bethel, CR; Bonomo, RA; Caselli, E; Distler, AM; Drawz, SM; Hujer, KM; Hurless, KN; Prati, F | 1 |
Antunes, NT; Champion, MM; Frase, H; Toth, M; Vakulenko, SB | 1 |
5 other study(ies) available for clavulanic acid and asparagine
Article | Year |
---|---|
Aspartic acid for asparagine substitution at position 276 reduces susceptibility to mechanism-based inhibitors in SHV-1 and SHV-5 beta-lactamases.
Topics: Amino Acid Substitution; Anti-Bacterial Agents; Asparagine; Aspartic Acid; beta-Lactam Resistance; beta-Lactamase Inhibitors; beta-Lactamases; beta-Lactams; Clavulanic Acid; Enzyme Inhibitors; Escherichia coli; Inhibitory Concentration 50; Microbial Sensitivity Tests; Penicillanic Acid; Sulbactam; Tazobactam | 1999 |
X-ray structure of the Asn276Asp variant of the Escherichia coli TEM-1 beta-lactamase: direct observation of electrostatic modulation in resistance to inactivation by clavulanic acid.
Topics: Asparagine; Aspartic Acid; beta-Lactam Resistance; beta-Lactamase Inhibitors; beta-Lactamases; Clavulanic Acid; Crystallography, X-Ray; Enzyme Activation; Enzyme Inhibitors; Escherichia coli; Kinetics; Models, Molecular; Mutagenesis, Site-Directed; Recombinant Proteins; Static Electricity | 1999 |
Structure of beta-lactam synthetase reveals how to synthesize antibiotics instead of asparagine.
Topics: Adenosine Triphosphate; Amidohydrolases; Amino Acid Sequence; Anti-Bacterial Agents; Asparagine; Aspartate-Ammonia Ligase; Binding Sites; Clavulanic Acid; Crystallography, X-Ray; Escherichia coli; Evolution, Molecular; Magnesium; Models, Molecular; Molecular Sequence Data; Protein Structure, Secondary; Protein Structure, Tertiary; Sequence Alignment; Streptomyces; Structure-Activity Relationship | 2001 |
The role of a second-shell residue in modifying substrate and inhibitor interactions in the SHV beta-lactamase: a study of ambler position Asn276.
Topics: Anti-Infective Agents; Asparagine; beta-Lactamase Inhibitors; beta-Lactamases; Catalytic Domain; Clavulanic Acid; Enzyme Inhibitors; Escherichia coli; Humans; Immunoblotting; Kinetics; Mutagenesis; Protein Binding; Spectrometry, Mass, Electrospray Ionization | 2009 |
Importance of position 170 in the inhibition of GES-type β-lactamases by clavulanic acid.
Topics: Anti-Bacterial Agents; Asparagine; beta-Lactamase Inhibitors; beta-Lactamases; Chromatography, Liquid; Clavulanic Acid; Enzyme Inhibitors; Glycine; Microbial Sensitivity Tests; Serine; Spectrometry, Mass, Electrospray Ionization; Structure-Activity Relationship | 2011 |