Pneumococcal LytR, a protein from the LytR-CpsA-Psr family, is essential for normal septum formation in Streptococcus pneumoniae.
about
Structural basis of PcsB-mediated cell separation in Streptococcus pneumoniaeCharacterization of Acp, a peptidoglycan hydrolase of Clostridium perfringens with N-acetylglucosaminidase activity that is implicated in cell separation and stress-induced autolysisThe Leaderless Bacteriocin Enterocin K1 Is Highly Potent against Enterococcus faecium: A Study on Structure, Target Spectrum and Receptor.Divergence of the SigB regulon and pathogenesis of the Bacillus cereus sensu lato group.Deficiency of BrpB causes major defects in cell division, stress responses and biofilm formation by Streptococcus mutans.Phylogenetic relationship and virulence inference of Streptococcus Anginosus Group: curated annotation and whole-genome comparative analysis support distinct species designationModification of the CpsA protein reveals a role in alteration of the Streptococcus agalactiae cell envelopeCoordinate regulation of Gram-positive cell surface components.Staphylococcus aureus mutants lacking the LytR-CpsA-Psr family of enzymes release cell wall teichoic acids into the extracellular mediumPeptide-regulated gene depletion system developed for use in Streptococcus pneumoniae.BrpA is involved in regulation of cell envelope stress responses in Streptococcus mutans.Functional analysis of the CpsA protein of Streptococcus agalactiae.Psr is involved in regulation of glucan production, and double deficiency of BrpA and Psr is lethal in Streptococcus mutans.Effects of low PBP2b levels on cell morphology and peptidoglycan composition in Streptococcus pneumoniae R6.A programmed cell division delay preserves genome integrity during natural genetic transformation in Streptococcus pneumoniae.Identification of pneumococcal proteins that are functionally linked to penicillin-binding protein 2b (PBP2b).In vivo virulence of Mycobacterium tuberculosis depends on a single homologue of the LytR-CpsA-Psr proteins.Pneumococcal LytR Protein Is Required for the Surface Attachment of Both Capsular Polysaccharide and Teichoic Acids: Essential for Pneumococcal Virulence.
P2860
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P2860
Pneumococcal LytR, a protein from the LytR-CpsA-Psr family, is essential for normal septum formation in Streptococcus pneumoniae.
description
2009 nî lūn-bûn
@nan
2009年の論文
@ja
2009年論文
@yue
2009年論文
@zh-hant
2009年論文
@zh-hk
2009年論文
@zh-mo
2009年論文
@zh-tw
2009年论文
@wuu
2009年论文
@zh
2009年论文
@zh-cn
name
Pneumococcal LytR, a protein f ...... n in Streptococcus pneumoniae.
@en
Pneumococcal LytR, a protein f ...... n in Streptococcus pneumoniae.
@nl
type
label
Pneumococcal LytR, a protein f ...... n in Streptococcus pneumoniae.
@en
Pneumococcal LytR, a protein f ...... n in Streptococcus pneumoniae.
@nl
prefLabel
Pneumococcal LytR, a protein f ...... n in Streptococcus pneumoniae.
@en
Pneumococcal LytR, a protein f ...... n in Streptococcus pneumoniae.
@nl
P2860
P356
P1476
Pneumococcal LytR, a protein f ...... n in Streptococcus pneumoniae.
@en
P2093
Ola Johnsborg
P2860
P304
P356
10.1128/JB.00724-09
P577
2009-07-06T00:00:00Z