The molecular characterization of the first autolytic lysozyme of Streptococcus pneumoniae reveals evolutionary mobile domains.
about
The PECACE domain: a new family of enzymes with potential peptidoglycan cleavage activity in Gram-positive bacteriaCholine Binding Proteins from Streptococcus pneumoniae: A Dual Role as Enzybiotics and Targets for the Design of New AntimicrobialsCrystal structure of CbpF, a bifunctional choline-binding protein and autolysis regulator from Streptococcus pneumoniaeInsights into pneumococcal fratricide from the crystal structures of the modular killing factor LytCCpl-7, a lysozyme encoded by a pneumococcal bacteriophage with a novel cell wall-binding motifOfloxacin-like antibiotics inhibit pneumococcal cell wall-degrading virulence factors.Role of novel choline binding proteins in virulence of Streptococcus pneumoniae.New adhesin functions of surface-exposed pneumococcal proteins.Identification and characterization of an autolysin-encoding gene of Streptococcus mutansMM1, a temperate bacteriophage of the type 23F Spanish/USA multiresistant epidemic clone of Streptococcus pneumoniae: structural analysis of the site-specific integration system.Competence-programmed predation of noncompetent cells in the human pathogen Streptococcus pneumoniae: genetic requirementsMolecular peculiarities of the lytA gene isolated from clinical pneumococcal strains that are bile insolubleThe autolytic enzyme LytA of Streptococcus pneumoniae is not responsible for releasing pneumolysinUse of a whole genome approach to identify vaccine molecules affording protection against Streptococcus pneumoniae infection.Nasopharyngeal colonization and invasive disease are enhanced by the cell wall hydrolases LytB and LytC of Streptococcus pneumoniae.Induction of natural competence in Streptococcus pneumoniae triggers lysis and DNA release from a subfraction of the cell populationStructure of pneumococcal peptidoglycan hydrolase LytB reveals insights into the bacterial cell wall remodeling and pathogenesis.Purification and polar localization of pneumococcal LytB, a putative endo-beta-N-acetylglucosaminidase: the chain-dispersing murein hydrolase.Insight into the composition of the intercellular matrix of Streptococcus pneumoniae biofilms.Thermal stability of Cpl-7 endolysin from the streptococcus pneumoniae bacteriophage Cp-7; cell wall-targeting of its CW_7 motifs.Expression of Streptococcus pneumoniae Virulence-Related Genes in the Nasopharynx of Healthy ChildrenGlucan-binding proteins of the oral streptococci.Essential PcsB putative peptidoglycan hydrolase interacts with the essential FtsXSpn cell division protein in Streptococcus pneumoniae D39.Recent trends on the molecular biology of pneumococcal capsules, lytic enzymes, and bacteriophage.The essential tacF gene is responsible for the choline-dependent growth phenotype of Streptococcus pneumoniae.Characterization of Afb, a novel bifunctional protein in Streptococcus agalactiae.Different pathways of choline metabolism in two choline-independent strains of Streptococcus pneumoniae and their impact on virulence.Bacterial peptidoglycan (murein) hydrolases.Antibodies to pneumococcal proteins PhtD, CbpA, and LytC in Filipino pregnant women and their infants in relation to pneumococcal carriageStreptococcus pneumoniae autolysis prevents phagocytosis and production of phagocyte-activating cytokines.Cannibalism: a social behavior in sporulating Bacillus subtilis.Pneumococcal surface proteins: when the whole is greater than the sum of its parts.In vitro destruction of Streptococcus pneumoniae biofilms with bacterial and phage peptidoglycan hydrolases.Crystallization and preliminary X-ray diffraction studies of choline-binding protein F from Streptococcus pneumoniae.Biochemical characterization of the major N-acetylmuramidase from Lactobacillus buchneri.The pneumococcal cell envelope stress-sensing system LiaFSR is activated by murein hydrolases and lipid II-interacting antibiotics.Crystallization of the pneumococcal autolysin LytC: in-house phasing using novel lanthanide complexes.Drastic reduction in the virulence of Streptococcus pneumoniae expressing type 2 capsular polysaccharide but lacking choline residues in the cell wall.Competence-induced cells of Streptococcus pneumoniae lyse competence-deficient cells of the same strain during cocultivation.Fine-tuning of choline metabolism is important for pneumococcal colonization.
P2860
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P2860
The molecular characterization of the first autolytic lysozyme of Streptococcus pneumoniae reveals evolutionary mobile domains.
description
1999 nî lūn-bûn
@nan
1999年の論文
@ja
1999年学术文章
@wuu
1999年学术文章
@zh
1999年学术文章
@zh-cn
1999年学术文章
@zh-hans
1999年学术文章
@zh-my
1999年学术文章
@zh-sg
1999年學術文章
@yue
1999年學術文章
@zh-hant
name
The molecular characterization ...... s evolutionary mobile domains.
@en
The molecular characterization ...... s evolutionary mobile domains.
@nl
type
label
The molecular characterization ...... s evolutionary mobile domains.
@en
The molecular characterization ...... s evolutionary mobile domains.
@nl
prefLabel
The molecular characterization ...... s evolutionary mobile domains.
@en
The molecular characterization ...... s evolutionary mobile domains.
@nl
P2093
P2860
P1476
The molecular characterization ...... s evolutionary mobile domains.
@en
P2093
P2860
P304
P356
10.1046/J.1365-2958.1999.01455.X
P407
P577
1999-07-01T00:00:00Z