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Differential inhibition of Staphylococcus aureus PBP2 by glycopeptide antibiotics.
Lipoprotein cofactors located in the outer membrane activate bacterial cell wall polymerases.
Vancomycin analogues active against vanA-resistant strains inhibit bacterial transglycosylase without binding substrate.
Forming cross-linked peptidoglycan from synthetic gram-negative Lipid II.
Lipoprotein activators stimulate Escherichia coli penicillin-binding proteins by different mechanisms.
Reconstitution of peptidoglycan cross-linking leads to improved fluorescent probes of cell wall synthesis.
Detection of lipid-linked peptidoglycan precursors by exploiting an unexpected transpeptidase reaction.
Cofactor bypass variants reveal a conformational control mechanism governing cell wall polymerase activity.
SEDS proteins are a widespread family of bacterial cell wall polymerases.
Lipid II overproduction allows direct assay of transpeptidase inhibition by ß-lactams.
Peptidoglycan Cross-Linking Preferences of Staphylococcus aureus Penicillin-Binding Proteins Have Implications for Treating MRSA Infections.
Identification of a Functionally Unique Family of Penicillin-Binding Proteins.
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.
FtsW is a peptidoglycan polymerase that is functional only in complex with its cognate penicillin-binding protein.
Chemical tools to characterize peptidoglycan synthases.