Streptococcus pyogenes cytolysin-mediated translocation does not require pore formation by streptolysin O.
about
The pore-forming toxin listeriolysin O mediates a novel entry pathway of L. monocytogenes into human hepatocytesMore than a pore: the cellular response to cholesterol-dependent cytolysinsBacterial Secretion Systems: An OverviewThe Cholesterol-dependent Cytolysin Membrane-binding Interface Discriminates Lipid Environments of Cholesterol to Support β-Barrel Pore Insertion.Streptolysin O clearance through sequestration into blebs that bud passively from the plasma membraneInhibition of Inflammasome-Dependent Interleukin 1β Production by Streptococcal NAD+-Glycohydrolase: Evidence for Extracellular Activity.Development of a single-gene, signature-tag-based approach in combination with alanine mutagenesis to identify listeriolysin O residues critical for the in vivo survival of Listeria monocytogenes.Streptolysin O and NAD-glycohydrolase prevent phagolysosome acidification and promote group A Streptococcus survival in macrophages.Role of pore-forming toxins in bacterial infectious diseases.A novel cholesterol-insensitive mode of membrane binding promotes cytolysin-mediated translocation by Streptolysin OStreptolysin O and its co-toxin NAD-glycohydrolase protect group A Streptococcus from Xenophagic killing.Structural studies of Streptococcus pyogenes streptolysin O provide insights into the early steps of membrane penetration.Counteractive balancing of transcriptome expression involving CodY and CovRS in Streptococcus pyogenes.Packing a punch: the mechanism of pore formation by cholesterol dependent cytolysins and membrane attack complex/perforin-like proteins.The Streptococcus pyogenes NAD(+) glycohydrolase modulates epithelial cell PARylation and HMGB1 releaseStreptolysin O Rapidly Impairs Neutrophil Oxidative Burst and Antibacterial Responses to Group A Streptococcus.Dual modes of membrane binding direct pore formation by Streptolysin O.The NADase-Negative Variant of the Streptococcus pyogenes Toxin NAD⁺ Glycohydrolase Induces JNK1-Mediated Programmed Cellular Necrosis.Analysis of polymorphic residues reveals distinct enzymatic and cytotoxic activities of the Streptococcus pyogenes NAD+ glycohydrolase.Reduction of streptolysin O (SLO) pore-forming activity enhances inflammasome activation.Intrinsic repair protects cells from pore-forming toxins by microvesicle shedding.Binding of NAD+-Glycohydrolase to Streptolysin O Stabilizes Both Toxins and Promotes Virulence of Group A Streptococcus.Visualization of bacterial toxin induced responses using live cell fluorescence microscopy.Cholesterol-dependent cytolysins impair pro-inflammatory macrophage responses.
P2860
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P2860
Streptococcus pyogenes cytolysin-mediated translocation does not require pore formation by streptolysin O.
description
2010 nî lūn-bûn
@nan
2010 թուականի Մարտին հրատարակուած գիտական յօդուած
@hyw
2010 թվականի մարտին հրատարակված գիտական հոդված
@hy
2010年の論文
@ja
2010年論文
@yue
2010年論文
@zh-hant
2010年論文
@zh-hk
2010年論文
@zh-mo
2010年論文
@zh-tw
2010年论文
@wuu
name
Streptococcus pyogenes cytolys ...... e formation by streptolysin O.
@ast
Streptococcus pyogenes cytolys ...... e formation by streptolysin O.
@en
type
label
Streptococcus pyogenes cytolys ...... e formation by streptolysin O.
@ast
Streptococcus pyogenes cytolys ...... e formation by streptolysin O.
@en
prefLabel
Streptococcus pyogenes cytolys ...... e formation by streptolysin O.
@ast
Streptococcus pyogenes cytolys ...... e formation by streptolysin O.
@en
P2093
P2860
P356
P1433
P1476
Streptococcus pyogenes cytolys ...... e formation by streptolysin O.
@en
P2093
Michael G Caparon
N'Goundo Magassa
Sukantha Chandrasekaran
P2860
P304
P356
10.1038/EMBOR.2010.37
P577
2010-03-26T00:00:00Z