Compounds > clavulanic acid
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clavulanic acid and asparagine

clavulanic acid has been researched along with asparagine in 5 studies

Research

Studies (5)

TimeframeStudies, this research(%)All Research%
pre-19900 (0.00)18.7374
1990's2 (40.00)18.2507
2000's2 (40.00)29.6817
2010's1 (20.00)24.3611
2020's0 (0.00)2.80

Authors

AuthorsStudies
Giakkoupi, P; Legakis, NJ; Tzelepi, E; Tzouvelekis, LS1
Bulychev, A; Cabantous, S; Golemi, D; Maveyraud, L; Mobashery, S; Samama, JP; Swarén, P1
Bachmann, BO; Miller, MT; Rosenzweig, AC; Townsend, CA1
Bethel, CR; Bonomo, RA; Caselli, E; Distler, AM; Drawz, SM; Hujer, KM; Hurless, KN; Prati, F1
Antunes, NT; Champion, MM; Frase, H; Toth, M; Vakulenko, SB1

Other Studies

5 other study(ies) available for clavulanic acid and asparagine

ArticleYear
Aspartic acid for asparagine substitution at position 276 reduces susceptibility to mechanism-based inhibitors in SHV-1 and SHV-5 beta-lactamases.
    The Journal of antimicrobial chemotherapy, 1999, Volume: 43, Issue:1

    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.
    Biochemistry, 1999, Jul-27, Volume: 38, Issue:30

    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.
    Nature structural biology, 2001, Volume: 8, Issue:8

    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.
    Biochemistry, 2009, Jun-02, Volume: 48, Issue:21

    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.
    Antimicrobial agents and chemotherapy, 2011, Volume: 55, Issue:4

    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