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Lipoprotein cofactors located in the outer membrane activate bacterial cell wall polymerases.
Lipoprotein activators stimulate Escherichia coli penicillin-binding proteins by different mechanisms.
Beta-lactam antibiotics induce a lethal malfunctioning of the bacterial cell wall synthesis machinery.
Identification of MltG as a potential terminase for peptidoglycan polymerization in bacteria.
Cofactor bypass variants reveal a conformational control mechanism governing cell wall polymerase activity.
Suppression of a deletion mutation in the gene encoding essential PBP2b reveals a new lytic transglycosylase involved in peripheral peptidoglycan synthesis in Streptococcus pneumoniae D39.
Peptidoglycan Biogenesis in Escherichia Coli
SEDS proteins are a widespread family of bacterial cell wall polymerases.
The mecillinam resistome reveals a role for peptidoglycan endopeptidases in stimulating cell wall synthesis in Escherichia coli.
Phosphorylation-dependent activation of the cell wall synthase PBP2a in Streptococcus pneumoniae by MacP.
Conserved mechanism of cell-wall synthase regulation revealed by the identification of a new PBP activator in Pseudomonas aeruginosa.
A central role for PBP2 in the activation of peptidoglycan polymerization by the bacterial cell elongation machinery.
Pathway-Directed Screen for Inhibitors of the Bacterial Cell Elongation Machinery.
Maturing Mycobacterium smegmatis peptidoglycan requires non-canonical crosslinks to maintain shape.
FtsW is a peptidoglycan polymerase that is functional only in complex with its cognate penicillin-binding protein.