The Streptococcus pneumoniae beta-galactosidase is a surface protein
about
Genome of the Bacterium Streptococcus pneumoniae Strain R6RNA-guided editing of bacterial genomes using CRISPR-Cas systemsHost glycan sugar-specific pathways in Streptococcus pneumoniae: galactose as a key sugar in colonisation and infection [corrected]Structural Insights into the Substrate Specificity of Streptococcus pneumoniae β(1,3)-Galactosidase BgaCUnravelling the multiple functions of the architecturally intricate Streptococcus pneumoniae β-galactosidase, BgaAThe Streptococcus pneumoniae pilus-1 displays a biphasic expression patternGenetic Stabilization of the Drug-Resistant PMEN1 Pneumococcus Lineage by Its Distinctive DpnIII Restriction-Modification SystemPromiscuous signaling by a regulatory system unique to the pandemic PMEN1 pneumococcal lineage.ManLMN is a glucose transporter and central metabolic regulator in Streptococcus pneumoniaeCharacterization of novel beta-galactosidase activity that contributes to glycoprotein degradation and virulence in Streptococcus pneumoniae.New adhesin functions of surface-exposed pneumococcal proteins.A novel protein, RafX, is important for common cell wall polysaccharide biosynthesis in Streptococcus pneumoniae: implications for bacterial virulenceStreptococcus suis type 2 SSU0587 protein is a beta-galactosidase that contributes to bacterial adhesion but not to virulence in mice.Characterization of a unique glycosylated anchor endopeptidase that cleaves the LPXTG sequence motif of cell surface proteins of Gram-positive bacteria.A functional genomics approach to establish the complement of carbohydrate transporters in Streptococcus pneumoniae.Catabolite control protein A (CcpA) contributes to virulence and regulation of sugar metabolism in Streptococcus pneumoniae.The role of complex carbohydrate catabolism in the pathogenesis of invasive streptococci.Global transcriptional analysis of clpP mutations of type 2 Streptococcus pneumoniae and their effects on physiology and virulenceVancomycin tolerance induced by erythromycin but not by loss of vncRS, vex3, or pep27 function in Streptococcus pneumoniae.Programmable repression and activation of bacterial gene expression using an engineered CRISPR-Cas system.The Streptococcus pneumoniae cia regulon: CiaR target sites and transcription profile analysis.BgaA acts as an adhesin to mediate attachment of some pneumococcal strains to human epithelial cells.Bacterial glycosidases in pathogenesis and glycoengineering.Chemoenzymatic Synthesis of a Type 2 Blood Group A Tetrasaccharide and Development of High-throughput Assays Enables a Platform for Screening Blood Group Antigen-cleaving Enzymes.CcpA-dependent and -independent control of beta-galactosidase expression in Streptococcus pneumoniae occurs via regulation of an upstream phosphotransferase system-encoding operon.Epigenetic Switch Driven by DNA Inversions Dictates Phase Variation in Streptococcus pneumoniae.Identification of Bacterial Surface Antigens by Screening Peptide Phage Libraries Using Whole Bacteria Cell-Purified AntiseraPositive correlation between tyrosine phosphorylation of CpsD and capsular polysaccharide production in Streptococcus pneumoniae.Cell Surface Glycoside Hydrolases of Streptococcus gordonii Promote Growth in Saliva.Bacterial hydrolysis of host glycoproteins - powerful protein modification and efficient nutrient acquisition.Pneumococcal surface proteins: when the whole is greater than the sum of its parts.Role of Streptococcus pneumoniae Proteins in Evasion of Complement-Mediated Immunity.Characterization of a novel fucose-regulated promoter (PfcsK) suitable for gene essentiality and antibacterial mode-of-action studies in Streptococcus pneumoniae.Inactivation of the srtA gene affects localization of surface proteins and decreases adhesion of Streptococcus pneumoniae to human pharyngeal cells in vitro.Essentiality of clpX, but not clpP, clpL, clpC, or clpE, in Streptococcus pneumoniae R6.Roles of pneumococcal DivIB in cell divisionIdentification of a pneumococcal glycosidase that modifies O-linked glycans.Three surface exoglycosidases from Streptococcus pneumoniae, NanA, BgaA, and StrH, promote resistance to opsonophagocytic killing by human neutrophils.Growth of Streptococcus pneumoniae on human glycoconjugates is dependent upon the sequential activity of bacterial exoglycosidases.LacR is a repressor of lacABCD and LacT is an activator of lacTFEG, constituting the lac gene cluster in Streptococcus pneumoniae.
P2860
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P2860
The Streptococcus pneumoniae beta-galactosidase is a surface protein
description
2000 nî lūn-bûn
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2000年の論文
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2000年学术文章
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2000年学术文章
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2000年学术文章
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name
The Streptococcus pneumoniae beta-galactosidase is a surface protein
@en
The Streptococcus pneumoniae beta-galactosidase is a surface protein.
@nl
type
label
The Streptococcus pneumoniae beta-galactosidase is a surface protein
@en
The Streptococcus pneumoniae beta-galactosidase is a surface protein.
@nl
prefLabel
The Streptococcus pneumoniae beta-galactosidase is a surface protein
@en
The Streptococcus pneumoniae beta-galactosidase is a surface protein.
@nl
P2860
P1476
The Streptococcus pneumoniae beta-galactosidase is a surface protein
@en
P2093
P2860
P304
P356
10.1128/JB.182.20.5919-5921.2000
P407
P577
2000-10-01T00:00:00Z