serine and cefotaxime

serine has been researched along with cefotaxime in 6 studies

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
Barthélémy, M; Ben Yaghlane, H; Labia, R; Péduzzi, J1
Kelly, JA; Knox, JR; Kuzin, AP; Liu, H1
Huletsky, A; Knox, JR; Levesque, RC1
Gazouli, M; Sidorenko, SV; Tzelepi, E; Tzouvelekis, LS1
Champelovier, D; Chesnel, L; Croizé, J; Dideberg, O; Lemaire, D; Pernot, L; Vernet, T; Zapun, A1
Hakenbeck, R; Maurer, P; Sauerbier, J; Todorova, K1

Other Studies

6 other study(ies) available for serine and cefotaxime

ArticleYear
Single amino acid substitution between SHV-1 beta-lactamase and cefotaxime-hydrolyzing SHV-2 enzyme.
    FEBS letters, 1988, Apr-11, Volume: 231, Issue:1

    Topics: Amino Acid Sequence; beta-Lactamases; Cefotaxime; Escherichia coli; Glycine; Isoenzymes; Molecular Sequence Data; Serine

1988
Binding of cephalothin and cefotaxime to D-ala-D-ala-peptidase reveals a functional basis of a natural mutation in a low-affinity penicillin-binding protein and in extended-spectrum beta-lactamases.
    Biochemistry, 1995, Jul-25, Volume: 34, Issue:29

    Topics: Amino Acid Sequence; Bacterial Proteins; beta-Lactamases; Binding Sites; Carboxypeptidases; Carrier Proteins; Cefotaxime; Cephalothin; Crystallography, X-Ray; Half-Life; Hexosyltransferases; Hydrogen Bonding; Kinetics; Models, Molecular; Muramoylpentapeptide Carboxypeptidase; Penicillin-Binding Proteins; Peptidyl Transferases; Point Mutation; Protein Binding; Protein Structure, Secondary; Serine; Serine-Type D-Ala-D-Ala Carboxypeptidase; Streptomyces; Substrate Specificity

1995
Role of Ser-238 and Lys-240 in the hydrolysis of third-generation cephalosporins by SHV-type beta-lactamases probed by site-directed mutagenesis and three-dimensional modeling.
    The Journal of biological chemistry, 1993, Feb-15, Volume: 268, Issue:5

    Topics: Amino Acid Sequence; Bacillus; Base Sequence; beta-Lactamases; Binding Sites; Cefotaxime; Ceftazidime; Cephalosporins; Citrobacter freundii; Hydrolysis; Lysine; Models, Molecular; Molecular Sequence Data; Molecular Structure; Mutagenesis, Site-Directed; Oligodeoxyribonucleotides; Protein Structure, Secondary; Recombinant Proteins; Serine; Streptomyces

1993
Sequence of the gene encoding a plasmid-mediated cefotaxime-hydrolyzing class A beta-lactamase (CTX-M-4): involvement of serine 237 in cephalosporin hydrolysis.
    Antimicrobial agents and chemotherapy, 1998, Volume: 42, Issue:5

    Topics: Amino Acid Sequence; Bacterial Proteins; Base Sequence; beta-Lactam Resistance; beta-Lactamases; Cefotaxime; Cephalosporins; Genes, Bacterial; Hydrolysis; Molecular Sequence Data; Plasmids; Salmonella typhimurium; Serine

1998
The structural modifications induced by the M339F substitution in PBP2x from Streptococcus pneumoniae further decreases the susceptibility to beta-lactams of resistant strains.
    The Journal of biological chemistry, 2003, Nov-07, Volume: 278, Issue:45

    Topics: Acylation; beta-Lactam Resistance; beta-Lactams; Binding Sites; Carrier Proteins; Cefotaxime; Crystallization; Hydrogen-Ion Concentration; Kinetics; Models, Molecular; Molecular Sequence Data; Molecular Structure; Mutagenesis, Site-Directed; Penicillin G; Penicillin-Binding Proteins; Phenotype; Point Mutation; Serine; Streptococcus pneumoniae

2003
Mutations in Streptococcus pneumoniae penicillin-binding protein 2x: importance of the C-terminal penicillin-binding protein and serine/threonine kinase-associated domains for beta-lactam binding.
    Microbial drug resistance (Larchmont, N.Y.), 2012, Volume: 18, Issue:3

    Topics: Anti-Bacterial Agents; Binding Sites; Boron Compounds; Cefotaxime; Cefuroxime; Computer Simulation; Crystallography, X-Ray; Drug Resistance, Microbial; Models, Molecular; Penicillin-Binding Proteins; Penicillins; Point Mutation; Protein Binding; Protein Serine-Threonine Kinases; Protein Structure, Tertiary; Recombinant Proteins; Serine; Streptococcus pneumoniae; Structure-Activity Relationship

2012