about
The pore-forming toxin listeriolysin O mediates a novel entry pathway of L. monocytogenes into human hepatocytesInerolysin, a cholesterol-dependent cytolysin produced by Lactobacillus inersBiological 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 cytolysinsConformational changes during pore formation by the perforin-related protein pleurotolysinListeriolysin O Membrane Damaging Activity Involves Arc Formation and Lineaction -- Implication for Listeria monocytogenes Escape from Phagocytic VacuoleA new model for pore formation by cholesterol-dependent cytolysinsDefining the interaction of perforin with calcium and the phospholipid membraneCrystal structure of listeriolysin O reveals molecular details of oligomerization and pore formationpH dependence of listeriolysin O aggregation and pore-forming abilityPlasticity of listeriolysin O pores and its regulation by pH and unique histidine [corrected].Crucial role of perfringolysin O D1 domain in orchestrating structural transitions leading to membrane-perforating pores: a hydrogen-deuterium exchange study.Monomer-monomer interactions propagate structural transitions necessary for pore formation by the cholesterol-dependent cytolysins.Membrane assembly of the cholesterol-dependent cytolysin pore complex.A Nonpolycationic Fully Proteinaceous Multiagent System for Potent Targeted Delivery of siRNA.Modes of calreticulin recruitment to the major histocompatibility complex class I assembly pathwayThe role of the activated macrophage in clearing Listeria monocytogenes infectionInvasive extravillous trophoblasts restrict intracellular growth and spread of Listeria monocytogenes.Alpha-galactosylceramide promotes killing of Listeria monocytogenes within the macrophage phagosome through invariant NKT-cell activationDendritic cells inhibit the progression of Listeria monocytogenes intracellular infection by retaining bacteria in major histocompatibility complex class II-rich phagosomes and by limiting cytosolic growthDevelopment 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.Membrane damage during Listeria monocytogenes infection triggers a caspase-7 dependent cytoprotective responseListeria monocytogenes exploits cystic fibrosis transmembrane conductance regulator (CFTR) to escape the phagosome.Acidification Activates Toxoplasma gondii Motility and Egress by Enhancing Protein Secretion and Cytolytic ActivityA small molecule deubiquitinase inhibitor increases localization of inducible nitric oxide synthase to the macrophage phagosome and enhances bacterial killingStabilized nanosystem of nanocarriers with an immobilized biological factor for anti-tumor therapy.Listeriolysin O secreted by Listeria monocytogenes into the host cell cytosol is degraded by the N-end rule pathway.RNA Helicase Important for Listeria monocytogenes Hemolytic Activity and Virulence Factor ExpressionPrison break: pathogens' strategies to egress from host cells.Listeriolysin O: a key protein of Listeria monocytogenes with multiple functions.Perforin-2 Protects Host Cells and Mice by Restricting the Vacuole to Cytosol Transitioning of a Bacterial Pathogen.Intracellular pH sensors: design principles and functional significance.Role of pore-forming toxins in neonatal sepsisGranzymes drive a rapid listeriolysin O-induced T cell apoptosisMolecular analysis of the iap gene of Listeria monocytogenes isolated from cheeses in rio grande do Sul, BrazilDevelopment of a mariner-based transposon and identification of Listeria monocytogenes determinants, including the peptidyl-prolyl isomerase PrsA2, that contribute to its hemolytic phenotype.Glycan-dependent and -independent interactions contribute to cellular substrate recruitment by calreticulin.How Bacteria Subvert Animal Cell Structure and Function.Engineering a pH responsive pore forming protein.
P2860
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P2860
description
2005 nî lūn-bûn
@nan
2005 թուականի Օգոստոսին հրատարակուած գիտական յօդուած
@hyw
2005 թվականի օգոստոսին հրատարակված գիտական հոդված
@hy
2005年の論文
@ja
2005年論文
@yue
2005年論文
@zh-hant
2005年論文
@zh-hk
2005年論文
@zh-mo
2005年論文
@zh-tw
2005年论文
@wuu
name
Molecular basis of listeriolysin O pH dependence.
@ast
Molecular basis of listeriolysin O pH dependence.
@en
type
label
Molecular basis of listeriolysin O pH dependence.
@ast
Molecular basis of listeriolysin O pH dependence.
@en
prefLabel
Molecular basis of listeriolysin O pH dependence.
@ast
Molecular basis of listeriolysin O pH dependence.
@en
P2093
P2860
P356
P1476
Molecular basis of listeriolysin O pH dependence.
@en
P2093
Daniel W Schuerch
Elizabeth M Wilson-Kubalek
Rodney K Tweten
P2860
P304
12537-12542
P356
10.1073/PNAS.0500558102
P407
P577
2005-08-16T00:00:00Z