Listeriolysin O: cholesterol inhibits cytolysis but not binding to cellular membranes.
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Cholesterol-dependent cytolysins, a family of versatile pore-forming toxinsRedefining cholesterol's role in the mechanism of the cholesterol-dependent cytolysinsHistone modifications induced by a family of bacterial toxinsBiological effects of listeriolysin O: implications for vaccinationMultifaceted activity of listeriolysin O, the cholesterol-dependent cytolysin of Listeria monocytogenesMore than a pore: the cellular response to cholesterol-dependent cytolysinsListeriolysin O Membrane Damaging Activity Involves Arc Formation and Lineaction -- Implication for Listeria monocytogenes Escape from Phagocytic VacuolePlasticity of listeriolysin O pores and its regulation by pH and unique histidine [corrected].Membrane assembly of the cholesterol-dependent cytolysin pore complex.Listeriolysin O as cytotoxic component of an immunotoxinListeria pathogenesis and molecular virulence determinantsMouse, but not human, ApoB-100 lipoprotein cholesterol is a potent innate inhibitor of Streptococcus pneumoniae pneumolysin.Differential interaction of the two cholesterol-dependent, membrane-damaging toxins, streptolysin O and Vibrio cholerae cytolysin, with enantiomeric cholesterol.Conformational changes that effect oligomerization and initiate pore formation are triggered throughout perfringolysin O upon binding to cholesterol.The cholesterol-dependent cytolysins pneumolysin and streptolysin O require binding to red blood cell glycans for hemolytic activityPlasma membrane microdomains act as concentration platforms to facilitate intoxication by aerolysin.Role of pore-forming toxins in neonatal sepsisBiotechnological applications of Listeria's sophisticated infection strategies.Mechanisms of cytolysin-induced cell damage -- a role for auto- and paracrine signalling.K+ efflux is required for histone H3 dephosphorylation by Listeria monocytogenes listeriolysin O and other pore-forming toxins.Human lymphocytic B-leukemia cell line treatment with the bacterial toxin listeriolysin O and rituximab (anti-CD20 antibody): Effects of similar localization of their receptors.Activation of the unfolded protein response by Listeria monocytogenes.Cholesterol Promotes Interaction of the Protein CLIC1 with Phospholipid Monolayers at the Air-Water Interface.Dissociated linkage of cytokine-inducing activity and cytotoxicity to different domains of listeriolysin O from Listeria monocytogenes.Listeriolysin O enhances cytoplasmic delivery by Her-2 targeting liposomes.Contribution of cysteine residue to the properties of Listeria monocytogenes listeriolysin O.Evaluation of the safety and adjuvant effect of a detoxified listeriolysin O mutant on the humoral response to dengue virus antigens.The multiple mechanisms of Ca2+ signalling by listeriolysin O, the cholesterol-dependent cytolysin of Listeria monocytogenes.The role of cholesterol in the activity of pneumolysin, a bacterial protein toxin.Endoplasmic reticulum chaperone Gp96 controls actomyosin dynamics and protects against pore-forming toxins.Listeriolysin O secreted by Listeria monocytogenes induces NF-kappaB signalling by activating the IkappaB kinase complex.Eukaryotic expression plasmid transfer from the intracellular bacterium Listeria monocytogenes to host cells.Listeriolysin O-induced stimulation of mucin exocytosis in polarized intestinal mucin-secreting cells: evidence for toxin recognition of membrane-associated lipids and subsequent toxin internalization through caveolae.Molecular analysis of the cytolytic protein ClyA (SheA) from Escherichia coli.Molecular docking based screening of Listeriolysin-O for improved inhibitors.Fisetin inhibits Listeria monocytogenes virulence by interfering with the oligomerization of listeriolysin O.Listeriolysin O-induced membrane permeation mediates persistent interleukin-6 production in Caco-2 cells during Listeria monocytogenes infection in vitro.Heliothis virescens and Manduca sexta lipid rafts are involved in Cry1A toxin binding to the midgut epithelium and subsequent pore formation.The conserved undecapeptide shared by thiol-activated cytolysins is involved in membrane binding.A bacterial big-MAC attack.
P2860
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P2860
Listeriolysin O: cholesterol inhibits cytolysis but not binding to cellular membranes.
description
1998 nî lūn-bûn
@nan
1998年の論文
@ja
1998年学术文章
@wuu
1998年学术文章
@zh
1998年学术文章
@zh-cn
1998年学术文章
@zh-hans
1998年学术文章
@zh-my
1998年学术文章
@zh-sg
1998年學術文章
@yue
1998年學術文章
@zh-hant
name
Listeriolysin O: cholesterol inhibits cytolysis but not binding to cellular membranes.
@en
Listeriolysin O: cholesterol inhibits cytolysis but not binding to cellular membranes.
@nl
type
label
Listeriolysin O: cholesterol inhibits cytolysis but not binding to cellular membranes.
@en
Listeriolysin O: cholesterol inhibits cytolysis but not binding to cellular membranes.
@nl
prefLabel
Listeriolysin O: cholesterol inhibits cytolysis but not binding to cellular membranes.
@en
Listeriolysin O: cholesterol inhibits cytolysis but not binding to cellular membranes.
@nl
P2093
P2860
P1476
Listeriolysin O: cholesterol inhibits cytolysis but not binding to cellular membranes.
@en
P2093
Chakraborty T
P2860
P304
P356
10.1046/J.1365-2958.1998.00858.X
P407
P577
1998-06-01T00:00:00Z