4 research outputs found
Replication of Vesicular Stomatitis Virus in L Cells
No full textTitle: Replication of Vesicular Stomatitis Virus in L Cells, Author: Martin Petric, Location: ThodeA heat resistant strain (HR-LT) of the Indiana serotype of vesicular stomatitis virus was characterized. Virus specific RNA and protein components of the cytoplasmic extract of cells infected with this strain of virus in the presence and absence of interference, were examined.ThesisMaster of Science (MS
ChemInform Abstract: Design, Synthesis and Bioactivity Evaluation of Tribactam β Lactamase Inhibitors (VIII).
No full text4-Substituted Trinems as Broad Spectrum β-Lactamase Inhibitors: Structure-Based Design, Synthesis, and Biological Activity<sup>⊥</sup>
No full textA wide variety of pathogens have acquired antimicrobial resistance as an inevitable evolutionary response to the extensive use of antibacterial agents. In particular, one of the most widely used antibiotic
structural classes is the β-lactams, in which the most common and the most efficient mechanism of bacterial resistance is the synthesis of β-lactamases. Class C β-lactamase enzymes are primarily cephalosporinases,
mostly chromosomally encoded, and are inducible by exposure to some β-lactam agents and resistant to
inhibition by marketed β-lactamase inhibitors. In an ongoing effort to alleviate this problem a series
of novel 4-substituted trinems was designed and synthesized. Significant in vitro inhibitory activity was
measured against the bacterial β-lactamases of class C and additionally against class A. The lead compound
LK-157 was shown to be a potent mechanism-based inactivator. Acylation of the active site Ser 64 of
the class C enzyme β-lactamase was observed in the solved crystal structures of two inhibitors complexes
to AmpC enzyme from E. cloacae. Structure−activity relationships in the series reveal the importance
of the trinem scaffold for inhibitory activity and the interesting potential of the series for further
development
4-Substituted Trinems as Broad Spectrum β-Lactamase Inhibitors: Structure-Based Design, Synthesis, and Biological Activity<sup>⊥</sup>
No full textA wide variety of pathogens have acquired antimicrobial resistance as an inevitable evolutionary response to the extensive use of antibacterial agents. In particular, one of the most widely used antibiotic
structural classes is the β-lactams, in which the most common and the most efficient mechanism of bacterial resistance is the synthesis of β-lactamases. Class C β-lactamase enzymes are primarily cephalosporinases,
mostly chromosomally encoded, and are inducible by exposure to some β-lactam agents and resistant to
inhibition by marketed β-lactamase inhibitors. In an ongoing effort to alleviate this problem a series
of novel 4-substituted trinems was designed and synthesized. Significant in vitro inhibitory activity was
measured against the bacterial β-lactamases of class C and additionally against class A. The lead compound
LK-157 was shown to be a potent mechanism-based inactivator. Acylation of the active site Ser 64 of
the class C enzyme β-lactamase was observed in the solved crystal structures of two inhibitors complexes
to AmpC enzyme from E. cloacae. Structure−activity relationships in the series reveal the importance
of the trinem scaffold for inhibitory activity and the interesting potential of the series for further
development
