In vivo interaction of beta-lactam antibiotics with the penicillin-binding proteins of Streptococcus pneumoniae.
about
Microscale insights into pneumococcal antibiotic mutant selection windowsClassic reaction kinetics can explain complex patterns of antibiotic action.Genetics of oxacillin resistance in clinical isolates of Streptococcus pneumoniae that are oxacillin resistant and penicillin susceptible.High-level (beta)-lactam resistance and cell wall synthesis catalyzed by the mecA homologue of Staphylococcus sciuri introduced into Staphylococcus aureusMutational analysis of class A and class B penicillin-binding proteins in Streptococcus gordonii.Profiling of β-lactam selectivity for penicillin-binding proteins in Escherichia coli strain DC2.Penicillin-binding proteins of penicillin-susceptible and -resistant pneumococci: immunological relatedness of altered proteins and changes in peptides carrying the beta-lactam binding site.Separation of abnormal cell wall composition from penicillin resistance through genetic transformation of Streptococcus pneumoniae.Profiling of β-lactam selectivity for penicillin-binding proteins in Streptococcus pneumoniae D39Competition of beta-lactam antibiotics for the penicillin-binding proteins of Neisseria gonorrhoeaeRelationship of shape to initiation of new sites of envelope growth in Streptococcus faecium cells treated with beta-lactam antibiotics.Inhibition of beta-lactam antibiotics at two different times in the cell cycle of Streptococcus faecium ATCC 9790Detergent-resistant Streptococcus faecium derivatives that display conditional penicillin lysis.Antimicrobial susceptibility and genetic characteristics of Streptococcus pneumoniae isolates indicating possible nosocomial transmission routes in a community hospital in Japan.Analysis of multiply antimicrobial-resistant isolates of Streptococcus pneumoniae from the United StatesDirect quantitation of the number of individual penicillin-binding proteins per cell in Escherichia coli.Variation in penicillin-binding protein patterns of penicillin-resistant clinical isolates of pneumococci.Streptococcus pneumoniae PBP2x mid-cell localization requires the C-terminal PASTA domains and is essential for cell shape maintenance.The biochemical basis of antimicrobial and bacterial resistance.In vitro activity of sanfetrinem and affinity for the penicillin-binding proteins of Streptococcus pneumoniaeAssociation of a thr-371 substitution in a conserved amino acid motif of penicillin-binding protein 1A with penicillin resistance of Streptococcus pneumoniae.Penicillin-binding proteins 2b and 2x of Streptococcus pneumoniae are primary resistance determinants for different classes of beta-lactam antibioticsA mutation in the D,D-carboxypeptidase penicillin-binding protein 3 of Streptococcus pneumoniae contributes to cefotaxime resistance of the laboratory mutant C604.Possible physiological functions of penicillin-binding proteins in Staphylococcus aureus.A novel resistance mechanism against beta-lactams in Streptococcus pneumoniae involves CpoA, a putative glycosyltransferase.Susceptibility of pneumococci to 14 beta-lactam agents: comparison of strains resistant, intermediate-resistant, and susceptible to penicillin.Affinity of ceftaroline and other beta-lactams for penicillin-binding proteins from Staphylococcus aureus and Streptococcus pneumoniae.Unusual septum formation in Streptococcus pneumoniae mutants with an alteration in the D,D-carboxypeptidase penicillin-binding protein 3.5-Alkyloxytryptamines are membrane-targeting, broad-spectrum antibiotics.Selective penicillin-binding protein imaging probes reveal substructure in bacterial cell division.Mechanism of β-lactam action in Streptococcus pneumoniae: the piperacillin paradox.Cellular aspects of the distinct M protein and SfbI anchoring pathways in Streptococcus pyogenesInhibition of cell wall synthesis and acylation of the penicillin binding proteins during prolonged exposure of growing Streptococcus pneumoniae to benzylpenicillin.Crystal structure of a peptidoglycan synthesis regulatory factor (PBP3) from Streptococcus pneumoniae.Gene expression profiling of the response of Streptococcus pneumoniae to penicillin.Penicillin-degrading activities of peptides from pneumococcal penicillin-binding proteins.Penicillin-binding proteins in beta-lactam-resistant laboratory mutants of Streptococcus pneumoniae.
P2860
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P2860
In vivo interaction of beta-lactam antibiotics with the penicillin-binding proteins of Streptococcus pneumoniae.
description
1980 nî lūn-bûn
@nan
1980 թուականի Հոկտեմբերին հրատարակուած գիտական յօդուած
@hyw
1980 թվականի հոտեմբերին հրատարակված գիտական հոդված
@hy
1980年の論文
@ja
1980年論文
@yue
1980年論文
@zh-hant
1980年論文
@zh-hk
1980年論文
@zh-mo
1980年論文
@zh-tw
1980年论文
@wuu
name
In vivo interaction of beta-la ...... s of Streptococcus pneumoniae.
@ast
In vivo interaction of beta-la ...... s of Streptococcus pneumoniae.
@en
type
label
In vivo interaction of beta-la ...... s of Streptococcus pneumoniae.
@ast
In vivo interaction of beta-la ...... s of Streptococcus pneumoniae.
@en
prefLabel
In vivo interaction of beta-la ...... s of Streptococcus pneumoniae.
@ast
In vivo interaction of beta-la ...... s of Streptococcus pneumoniae.
@en
P2093
P2860
P356
P1476
In vivo interaction of beta-la ...... s of Streptococcus pneumoniae.
@en
P2093
R Hakenbeck
R Williamson
P2860
P304
P356
10.1128/AAC.18.4.629
P407
P577
1980-10-01T00:00:00Z