Compounds > beta-lactams
Page last updated: 2024-09-04

beta-lactams and asparagine

beta-lactams has been researched along with asparagine in 6 studies

Compound Research Comparison

Studies
(beta-lactams)		Trials
(beta-lactams)		Recent Studies (post-2010)
(beta-lactams)		Studies
(asparagine)		Trials
(asparagine)		Recent Studies (post-2010) (asparagine)
7,5791793,3956,819411,398

Research

Studies (6)

TimeframeStudies, this research(%)All Research%
pre-19901 (16.67)18.7374
1990's3 (50.00)18.2507
2000's1 (16.67)29.6817
2010's1 (16.67)24.3611
2020's0 (0.00)2.80

Authors

AuthorsStudies
Demain, AL; Heim, J; Shen, YQ; Solomon, NA; Wolfe, S1
Dubus, A; Kania, M; Normark, S; Page, MG1
Giakkoupi, P; Legakis, NJ; Tzelepi, E; Tzouvelekis, LS1
Chen, CC; Herzberg, O1
Eriguchi, Y; Haruta, S; Sawai, T; Yamamoto, ET1
Brown, NG; Horton, LB; Huang, W; Palzkill, T; Vongpunsawad, S1

Other Studies

6 other study(ies) available for beta-lactams and asparagine

ArticleYear
Repression of beta-lactam production in Cephalosporium acremonium by nitrogen sources.
    The Journal of antibiotics, 1984, Volume: 37, Issue:5

    Topics: Acremonium; Ammonium Sulfate; Anti-Bacterial Agents; Asparagine; beta-Lactams; Fermentation; Magnesium; Magnesium Compounds; Nitrogen; Phosphates

1984
Role of asparagine 152 in catalysis of beta-lactam hydrolysis by Escherichia coli AmpC beta-lactamase studied by site-directed mutagenesis.
    Biochemistry, 1995, Jun-13, Volume: 34, Issue:23

    Topics: Anti-Bacterial Agents; Asparagine; beta-Lactamase Inhibitors; beta-Lactamases; beta-Lactams; Catalysis; Escherichia coli; Hydrogen-Ion Concentration; Kinetics; Mutagenesis, Site-Directed; Spectrophotometry, Ultraviolet; Structure-Activity Relationship

1995
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
Relocation of the catalytic carboxylate group in class A beta-lactamase: the structure and function of the mutant enzyme Glu166-->Gln:Asn170-->Asp.
    Protein engineering, 1999, Volume: 12, Issue:7

    Topics: Acylation; Anti-Bacterial Agents; Asparagine; Aspartic Acid; beta-Lactamases; beta-Lactams; Catalytic Domain; Crystallography, X-Ray; Glutamic Acid; Glutamine; Kinetics; Models, Molecular; Mutation; Protein Conformation; Staphylococcus aureus; Structure-Activity Relationship

1999
Characterization of the active-site residues asparagine 167 and lysine 161 of the IMP-1 metallo beta-lactamase.
    FEMS microbiology letters, 2001, Apr-01, Volume: 197, Issue:1

    Topics: Asparagine; beta-Lactamases; beta-Lactams; Binding Sites; Escherichia coli; Humans; Kinetics; Lysine; Mutagenesis, Site-Directed; Zinc

2001
Analysis of the functional contributions of Asn233 in metallo-β-lactamase IMP-1.
    Antimicrobial agents and chemotherapy, 2011, Volume: 55, Issue:12

    Topics: Amino Acid Sequence; Amino Acid Substitution; Anti-Bacterial Agents; Asparagine; beta-Lactam Resistance; beta-Lactamases; beta-Lactams; Escherichia coli; Kinetics; Microbial Sensitivity Tests; Models, Molecular; Molecular Sequence Data; Mutagenesis, Site-Directed

2011