Staphylococcal alpha-toxin: oligomerization of hydrophilic monomers to form amphiphilic hexamers induced through contact with deoxycholate detergent micelles.
about
Alpha-toxin of Staphylococcus aureusStaphylococcus aureus α-toxin: nearly a century of intrigueObstructing toxin pathways by targeted pore blockageDimerization and protein binding specificity of the U2AF homology motif of the splicing factor Puf602-Methyl-2,4-pentanediol induces spontaneous assembly of staphylococcal α-hemolysin into heptameric pore structureMolecular Architecture and Functional Analysis of NetB, a Pore-forming Toxin from Clostridium perfringensCholesterol-dependent interaction of syncollin with the membrane of the pancreatic zymogen granuleOroxylin A inhibits hemolysis via hindering the self-assembly of α-hemolysin heptameric transmembrane poreGrafting synthetic transmembrane units to the engineered low-toxicity α-hemolysin to restore its hemolytic activity.Functional truncated membrane pores.An engineered dimeric protein pore that spans adjacent lipid bilayers.Role of the amino latch of staphylococcal alpha-hemolysin in pore formation: a co-operative interaction between the N terminus and position 217.Partitioning of individual flexible polymers into a nanoscopic protein pore.Prolonged residence time of a noncovalent molecular adapter, beta-cyclodextrin, within the lumen of mutant alpha-hemolysin pores.A functional protein pore with a "retro" transmembrane domain.Aggregation of IgE receptors induces degranulation in rat basophilic leukemia cells permeabilized with alpha-toxin from Staphylococcus aureus.Stochastic sensing of organic analytes by a pore-forming protein containing a molecular adapter.Protonation dynamics of the alpha-toxin ion channel from spectral analysis of pH-dependent current fluctuations.Channel-forming bacterial toxins in biosensing and macromolecule deliveryTemperature-independent porous nanocontainers for single-molecule fluorescence studies.Identification and partial characterization of a cytolytic toxin produced by Gardnerella vaginalisReversal of charge selectivity in transmembrane protein pores by using noncovalent molecular adapters.Subunit stoichiometry of staphylococcal alpha-hemolysin in crystals and on membranes: a heptameric transmembrane pore.Functionally distinct monomers and trimers produced by a viral oncoprotein.Staphylococcal alpha toxin promotes blood coagulation via attack on human platelets.High resolution crystallographic studies of alpha-hemolysin-phospholipid complexes define heptamer-lipid head group interactions: implication for understanding protein-lipid interactions.Transmembrane beta-barrel of staphylococcal alpha-toxin forms in sensitive but not in resistant cells.Pore-forming bacterial protein hemolysins (cytolysins).Analysis of single nucleic acid molecules with protein nanoporesEvolving protocells to prototissues: rational design of a missing link.Small-angle X-ray scattering study on CEL-III, a hemolytic lectin from Holothuroidea Cucumaria echinata, and its oligomer induced by the binding of specific carbohydrate.Suppression of cell membrane permeability by suramin: involvement of its inhibitory actions on connexin 43 hemichannels.Chromatofocusing: a new method for purification of staphylococcal enterotoxins B and C1.Localization and environment of tryptophans in soluble and membrane-bound states of a pore-forming toxin from Staphylococcus aureus.Effect of staphylococcal alpha-toxin on intracellular Ca2+ in polymorphonuclear leukocytes.The cytolytic toxin aerolysin must aggregate to disrupt erythrocytes, and aggregation is stimulated by human glycophorin.Release of interleukin-1 beta associated with potent cytocidal action of staphylococcal alpha-toxin on human monocytes.Quantitation of monomeric and oligomeric forms of membrane-bound staphylococcal alpha-toxin by enzyme-linked immunosorbent assay with a neutralizing monoclonal antibody.Quantitative analysis of the binding and oligomerization of staphylococcal alpha-toxin in target erythrocyte membranes.Use of a monoclonal antibody to determine the mode of transmembrane pore formation by streptolysin O.
P2860
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P2860
Staphylococcal alpha-toxin: oligomerization of hydrophilic monomers to form amphiphilic hexamers induced through contact with deoxycholate detergent micelles.
description
1981 nî lūn-bûn
@nan
1981年の論文
@ja
1981年学术文章
@wuu
1981年学术文章
@zh-cn
1981年学术文章
@zh-hans
1981年学术文章
@zh-my
1981年学术文章
@zh-sg
1981年學術文章
@yue
1981年學術文章
@zh
1981年學術文章
@zh-hant
name
Staphylococcal alpha-toxin: ol ...... oxycholate detergent micelles.
@ast
Staphylococcal alpha-toxin: ol ...... oxycholate detergent micelles.
@en
type
label
Staphylococcal alpha-toxin: ol ...... oxycholate detergent micelles.
@ast
Staphylococcal alpha-toxin: ol ...... oxycholate detergent micelles.
@en
prefLabel
Staphylococcal alpha-toxin: ol ...... oxycholate detergent micelles.
@ast
Staphylococcal alpha-toxin: ol ...... oxycholate detergent micelles.
@en
P2093
P2860
P356
P1476
Staphylococcal alpha-toxin: ol ...... oxycholate detergent micelles.
@en
P2093
Tranum-Jensen J
P2860
P304
P356
10.1073/PNAS.78.9.5475
P407
P577
1981-09-01T00:00:00Z