On the mechanism of membrane damage by Staphylococcus aureus alpha-toxin.
about
Alpha-toxin of Staphylococcus aureusStaphylococcus aureus α-toxin: nearly a century of intrigueDecreasing Transmembrane Segment Length Greatly Decreases Perfringolysin O Pore Size.An engineered dimeric protein pore that spans adjacent lipid bilayers.Elimination of a bacterial pore-forming toxin by sequential endocytosis and exocytosis.Annular protofibrils are a structurally and functionally distinct type of amyloid oligomer.Pore-forming Staphylococcus aureus alpha-toxin triggers epidermal growth factor receptor-dependent proliferation.Ion channels and bacterial infection: the case of beta-barrel pore-forming protein toxins of Staphylococcus aureus.Prolonged residence time of a noncovalent molecular adapter, beta-cyclodextrin, within the lumen of mutant alpha-hemolysin pores.Membrane insertion of the heptameric staphylococcal alpha-toxin pore. A domino-like structural transition that is allosterically modulated by the target cell membrane.A functional protein pore with a "retro" transmembrane domain.Cytotoxic activities of Leptospira interrogans hemolysin SphH as a pore-forming protein on mammalian cells.Assembly mechanism of the oligomeric streptolysin O pore: the early membrane lesion is lined by a free edge of the lipid membrane and is extended gradually during oligomerization.Nanopore Detector based analysis of single-molecule conformational kinetics and binding interactions.Aggregation of IgE receptors induces degranulation in rat basophilic leukemia cells permeabilized with alpha-toxin from Staphylococcus aureus.Synthetic protocells to mimic and test cell function.Inhibition of beta-adrenergic receptor kinase prevents rapid homologous desensitization of beta 2-adrenergic receptors.Protonation dynamics of the alpha-toxin ion channel from spectral analysis of pH-dependent current fluctuations.Channel-forming bacterial toxins in biosensing and macromolecule deliveryConductance and ion selectivity of a mesoscopic protein nanopore probed with cysteine scanning mutagenesis.Temperature-independent porous nanocontainers for single-molecule fluorescence studies.Rho-kinase inhibition attenuates calcium-induced contraction in β-escin but not Triton X-100 permeabilized rabbit femoral arteryLocalization of cystic fibrosis transmembrane conductance regulator in chloride secretory epitheliaReversal of charge selectivity in transmembrane protein pores by using noncovalent molecular adapters.Site-directed mutagenesis of the alpha-toxin gene of Staphylococcus aureus: role of histidines in toxin activity in vitro and in a murine modelSubunit stoichiometry of staphylococcal alpha-hemolysin in crystals and on membranes: a heptameric transmembrane pore.Binding and aggregation of the 25-kilodalton toxin of Bacillus thuringiensis subsp. israelensis to cell membranes and alteration by monoclonal antibodies and amino acid modifiers.Permeabilization of rat hepatocytes with Staphylococcus aureus alpha-toxin.Inhibition of OCTN2-mediated transport of carnitine by etoposide.Cytolytic activity of purified cytoplasmic granules from cytotoxic rat large granular lymphocyte tumorsInflammatory lipid mediator generation elicited by viable hemolysin-forming Escherichia coli in lung vasculatureActivation of the hole-forming toxin aerolysin by extracellular processing.Location of a constriction in the lumen of a transmembrane pore by targeted covalent attachment of polymer molecules.Combination Therapy of LysGH15 and Apigenin as a New Strategy for Treating Pneumonia Caused by Staphylococcus aureus.Staphylococcal alpha toxin promotes blood coagulation via attack on human platelets.Distribution of 3H-labeled staphylococcal alpha-toxin and a toxin fragment in micePulmonary microvascular injury induced by Pseudomonas aeruginosa cytotoxin in isolated rabbit lungs.Effect of calcium ions on staphylococcal alpha-toxin-induced hemolysis of rabbit erythrocytes.Susceptibility to staphylococcal alpha-toxin of Friend virus-infected murine erythroblasts during differentiation.Mechanisms of cytolysin-induced cell damage -- a role for auto- and paracrine signalling.
P2860
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P2860
On the mechanism of membrane damage by Staphylococcus aureus alpha-toxin.
description
1981 nî lūn-bûn
@nan
1981年の論文
@ja
1981年論文
@yue
1981年論文
@zh-hant
1981年論文
@zh-hk
1981年論文
@zh-mo
1981年論文
@zh-tw
1981年论文
@wuu
1981年论文
@zh
1981年论文
@zh-cn
name
On the mechanism of membrane damage by Staphylococcus aureus alpha-toxin.
@ast
On the mechanism of membrane damage by Staphylococcus aureus alpha-toxin.
@en
type
label
On the mechanism of membrane damage by Staphylococcus aureus alpha-toxin.
@ast
On the mechanism of membrane damage by Staphylococcus aureus alpha-toxin.
@en
prefLabel
On the mechanism of membrane damage by Staphylococcus aureus alpha-toxin.
@ast
On the mechanism of membrane damage by Staphylococcus aureus alpha-toxin.
@en
P2093
P2860
P356
P1476
On the mechanism of membrane damage by Staphylococcus aureus alpha-toxin.
@en
P2093
Sziegoleit A
Tranum-Jensen J
Wellensiek HJ
P2860
P356
10.1083/JCB.91.1.83
P407
P577
1981-10-01T00:00:00Z