Pages that link to "Q54397646"

The following pages link to Penicillin-binding proteins in beta-lactam-resistant laboratory mutants of Streptococcus pneumoniae. (Q54397646):

Displaying 33 items.

• Crystal structure of PBP2x from a highly penicillin-resistant Streptococcus pneumoniae clinical isolate: a mosaic framework containing 83 mutations (Q27634800) (← links)
• The structural modifications induced by the M339F substitution in PBP2x from Streptococcus pneumoniae further decreases the susceptibility to beta-lactams of resistant strains (Q27641845) (← links)
• X-ray structure of Streptococcus pneumoniae PBP2x, a primary penicillin target enzyme (Q27732630) (← links)
• Penicillin-binding proteins and beta-lactam resistance (Q28267300) (← links)
• In vitro selection of one-step mutants of Streptococcus pneumoniae resistant to different oral beta-lactam antibiotics is associated with alterations of PBP2x (Q35121849) (← links)
• Profiling of β-lactam selectivity for penicillin-binding proteins in Streptococcus pneumoniae D39 (Q35607798) (← links)
• Consequences of the interaction of beta-lactam antibiotics with penicillin binding proteins from sensitive and resistant Staphylococcus aureus strains (Q35642011) (← links)
• Whole genome sequencing of penicillin-resistant Streptococcus pneumoniae reveals mutations in penicillin-binding proteins and in a putative iron permease. (Q35907639) (← links)
• Gene localization, size, and physical map of the chromosome of Streptococcus pneumoniae (Q36166269) (← links)
• Pneumococcal resistance to antibiotics (Q36636190) (← links)
• The rise and fall of bacterial clones: Streptococcus pneumoniae (Q37299242) (← links)
• Streptococcus pneumoniae PBP2x mid-cell localization requires the C-terminal PASTA domains and is essential for cell shape maintenance (Q37844678) (← links)
• Molecular mechanisms of β-lactam resistance in Streptococcus pneumoniae (Q37990942) (← links)
• Penicillin-binding protein 2b of Streptococcus pneumoniae in piperacillin-resistant laboratory mutants (Q38304657) (← links)
• Genomic analyses of DNA transformation and penicillin resistance in Streptococcus pneumoniae clinical isolates. (Q38324659) (← links)
• Relatedness of penicillin-binding protein 1a genes from different clones of penicillin-resistant Streptococcus pneumoniae isolated in South Africa and Spain (Q38324879) (← links)
• Nucleotide sequences of genes encoding penicillin-binding proteins from Streptococcus pneumoniae and Streptococcus oralis with high homology to Escherichia coli penicillin-binding proteins 1a and 1b (Q38327719) (← links)
• Acquisition of five high-Mr penicillin-binding protein variants during transfer of high-level beta-lactam resistance from Streptococcus mitis to Streptococcus pneumoniae (Q39565315) (← links)
• Penicillin-binding proteins 2b and 2x of Streptococcus pneumoniae are primary resistance determinants for different classes of beta-lactam antibiotics (Q39781766) (← links)
• A mutation in the D,D-carboxypeptidase penicillin-binding protein 3 of Streptococcus pneumoniae contributes to cefotaxime resistance of the laboratory mutant C604. (Q39784064) (← links)
• A novel resistance mechanism against beta-lactams in Streptococcus pneumoniae involves CpoA, a putative glycosyltransferase (Q39845765) (← links)
• Biochemical characterization of penicillin-resistant and -sensitive penicillin-binding protein 2x transpeptidase activities of Streptococcus pneumoniae and mechanistic implications in bacterial resistance to beta-lactam antibiotics (Q39846687) (← links)
• Five independent combinations of mutations can result in low-affinity penicillin-binding protein 2x of Streptococcus pneumoniae (Q39945759) (← links)
• Unusual septum formation in Streptococcus pneumoniae mutants with an alteration in the D,D-carboxypeptidase penicillin-binding protein 3. (Q40341352) (← links)
• Mechanism of β-lactam action in Streptococcus pneumoniae: the piperacillin paradox (Q41817144) (← links)
• Altered lipid composition in Streptococcus pneumoniae cpoA mutants (Q41890973) (← links)
• The CiaRH system of Streptococcus pneumoniae prevents lysis during stress induced by treatment with cell wall inhibitors and by mutations in pbp2x involved in beta-lactam resistance (Q42026100) (← links)
• Choice of an Oral β-Lactam Antibiotic for Infections due to Penicillin-resistant Streptococcus pneumoniae (Q44313307) (← links)
• Genomic analysis and reconstruction of cefotaxime resistance in Streptococcus pneumoniae. (Q51051543) (← links)
• The role of penicillin-binding protein 3 (PBP 3) in cefotaxime resistance in Streptococcus pneumoniae. (Q54240648) (← links)
• Penicillin binding protein 2x as a major contributor to intrinsic beta-lactam resistance of Streptococcus pneumoniae (Q70494368) (← links)
• Molecular Characterization of a Mutation Affecting the Amount ofStreptococcus pneumoniaePenicillin-Binding Protein 3 (Q73625998) (← links)
• Genetic Studies of Cefotaxime Resistance in Streptococcus pneumoniae (Q73791391) (← links)