The penicillin-binding proteins: structure and role in peptidoglycan biosynthesis.
By E. Sauvage, F. Kerff, M. Terrak, J. Ayala, P. Charlier. FEMS Microbiology Reviews, 2008
1,327 citations recorded by the source corpus.
Subfields: Ecology, Genetics, Molecular Biology
View Paper: https://www.semanticscholar.org/paper/68ce3998cbd2a92538c5635b874eb1043441321f
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Citations in the corpus
- Peptidoglycan Hydrolases of Escherichia coli (2011, background): “Penicillin-binding proteins (PBPs) are a family of bacterial acyl-serine transferases of common evolutionary origin specifically inhibited by the covalent binding of -lactam antibiotics to their active sites (77, 156, 229, 312).”
- Stress Physiology of Lactic Acid Bacteria (2016, background): “-Lactam antibiotics, such as penicillin and its analogs, block PG biosynthesis through inhibition of the activity of a group of penicillin-binding protein (PBP) transpeptidases that catalyze the polymerization of the glycan strand or the cross-linking between glycan chains (362, 363).”
- The bacterial cell envelope. (2010, background): “Transpeptidases that couple branched stem peptides are mechanistically similar to those that couple unbranched stem peptides; however, their substrate specificity is sufficiently different that they only recognize unbranched stem peptides, and some of them are resistant to beta lactams (Rohrer and B”
- Beta-lactam antibiotics induce a lethal malfunctioning of the bacterial cell wall synthesis machinery (2014, background): “Bacteria encode a variety of PBPs that participate in PG assembly (Sauvage et al., 2008).”
- Cytoplasmic steps of peptidoglycan biosynthesis. (2008, background): “The present review deals with the cytoplasmic steps of peptidoglycan synthesis; the subsequent steps are reviewed by Bouhss et al. (2008) and Sauvage et al. (2008) in this issue.”
- Three Decades of β-Lactamase Inhibitors (2010, background): “A pentapeptide is attached to each NAM unit, and the cross-linking of two D-alanine–D-alanine NAM pentapeptides is catalyzed by PBPs, which act as transpeptidases (142, 377).”
- Penicillin-binding proteins and beta-lactam resistance. (2008, background): “The penicillin-binding domains of PBPs are transpeptidases or carboxypeptidases involved in peptidoglycan metabolism (Goffin & Ghuysen, 2002; Sauvage et al., 2008).”