Incorporation of glycine into the cell wall glycopeptide in Staphylococcus aureus: role of sRNA and lipid intermediates
about
Activities and regulation of peptidoglycan synthasesStructure of sortase, the transpeptidase that anchors proteins to the cell wall of Staphylococcus aureustRNA as an active chemical scaffold for diverse chemical transformationsSignal peptides direct surface proteins to two distinct envelope locations of Staphylococcus aureus.Anchor structure of staphylococcal surface proteins. V. Anchor structure of the sortase B substrate IsdC.Anchor structure of staphylococcal surface proteins. III. Role of the FemA, FemB, and FemX factors in anchoring surface proteins to the bacterial cell wall.Anchor structure of staphylococcal surface proteins. II. Cooh-terminal structure of muramidase and amidase-solubilized surface protein.Mycobacterial lipid II is composed of a complex mixture of modified muramyl and peptide moieties linked to decaprenyl phosphateAnalysis of outgrowth of Bacillus subtilis spores lacking penicillin-binding protein 2a.Derepression of beta-lactamase (penicillinase in Bacillus cereus by peptidoglycans.Sortase-catalysed anchoring of surface proteins to the cell wall of Staphylococcus aureus.Mycobacterium.FemABX peptidyl transferases: a link between branched-chain cell wall peptide formation and beta-lactam resistance in gram-positive cocci.Mechanism of action of penicillin: triggering of the pneumococcal autolytic enzyme by inhibitors of cell wall synthesis.Mode of action of novobiocin in Escherichia coli.Presence of UDP-N-acetylmuramyl-hexapeptides and -heptapeptides in enterococci and staphylococci after treatment with ramoplanin, tunicamycin, or vancomycin.Protein secretion and surface display in Gram-positive bacteria.Determinants of murein hydrolase targeting to cross-wall of Staphylococcus aureus peptidoglycanCorrelation between the structure of the bacterial peptidoglycan monomer unit, the specificity of transpeptidation, and susceptibility to beta-lactamsStaphylococcus aureus has clustered tRNA genesLipid intermediates in the biosynthesis of bacterial peptidoglycanMechanism of action of penicillins: a proposal based on their structural similarity to acyl-D-alanyl-D-alanine.The participation of sRNA in the enzymatic synthesis of O-L-lysyl phosphatidylgylcerol in Staphylococcus aureusOritavancin exhibits dual mode of action to inhibit cell-wall biosynthesis in Staphylococcus aureusMycobacteriophage Ms6 LysA: a peptidoglycan amidase and a useful analytical tool.Evolution of peptidoglycan biosynthesis under the selective pressure of antibiotics in Gram-positive bacteria.Immunochemistry of O and R antigens of Salmonella and related Enterobacteriaceae.Role of lipids in the biosynthesis of the bacterial cell envelope.Vancomycin and oritavancin have different modes of action in Enterococcus faeciumKatanosin B and plusbacin A(3), inhibitors of peptidoglycan synthesis in methicillin-resistant Staphylococcus aureus.Identification of the UDP-MurNAc-pentapeptide:L-alanine ligase for synthesis of branched peptidoglycan precursors in Enterococcus faecalis.Interaction of penicillin with the bacterial cell: penicillin-binding proteins and penicillin-sensitive enzymes.Kinetic characterization of lipid II-Ala:alanyl-tRNA ligase (MurN) from Streptococcus pneumoniae using semisynthetic aminoacyl-lipid II substrates.Anchor structure of staphylococcal surface proteins. IV. Inhibitors of the cell wall sorting reaction.Structure-based site-directed mutagenesis of the UDP-MurNAc-pentapeptide-binding cavity of the FemX alanyl transferase from Weissella viridescensLipid intermediates in the biosynthesis of the wall teichoic acid in Staphylococcus lactis 13.Polysaccharide biosynthesis.Lipid II overproduction allows direct assay of transpeptidase inhibition by β-lactams.Anchoring of surface proteins to the cell wall of Staphylococcus aureus. III. Lipid II is an in vivo peptidoglycan substrate for sortase-catalyzed surface protein anchoring.Substrate recognition by the leucyl/phenylalanyl-tRNA-protein transferase. Conservation within the enzyme family and localization to the trypsin-resistant domain.
P2860
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P2860
Incorporation of glycine into the cell wall glycopeptide in Staphylococcus aureus: role of sRNA and lipid intermediates
description
1965 nî lūn-bûn
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1965年の論文
@ja
1965年学术文章
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1965年学术文章
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1965年学术文章
@zh-hans
1965年学术文章
@zh-my
1965年学术文章
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1965年學術文章
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1965年學術文章
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name
Incorporation of glycine into ...... f sRNA and lipid intermediates
@ast
Incorporation of glycine into ...... f sRNA and lipid intermediates
@en
type
label
Incorporation of glycine into ...... f sRNA and lipid intermediates
@ast
Incorporation of glycine into ...... f sRNA and lipid intermediates
@en
prefLabel
Incorporation of glycine into ...... f sRNA and lipid intermediates
@ast
Incorporation of glycine into ...... f sRNA and lipid intermediates
@en
P2860
P356
P1476
Incorporation of glycine into ...... f sRNA and lipid intermediates
@en
P2093
Dietrich CP
Matsuhashi M
P2860
P304
P356
10.1073/PNAS.54.2.587
P407
P577
1965-08-01T00:00:00Z