about
Alpha-toxin of Staphylococcus aureusStaphylococcus aureus α-toxin: nearly a century of intrigueThe Protective Antigen Component of Anthrax Toxin Forms Functional Octameric ComplexesThe hemolysins of Staphylococcus aureus.Channel-forming bacterial toxins in biosensing and macromolecule deliveryCellular streptolysin S-related hemolysins of group A Streptococcus C203S.Cellular location of alpha-hemolysin in Staphylococcus aureusTemperature-dependent inactivating factor of Pseudomonas aeruginosa exotoxin A.Factors affecting interaction of staphylococcal alpha toxin with membranesSubunit stoichiometry of staphylococcal alpha-hemolysin in crystals and on membranes: a heptameric transmembrane pore.Permeabilization of rat hepatocytes with Staphylococcus aureus alpha-toxin.Nonenteric toxins of Staphylococcus aureus.Biological effects of the interaction of staphylococcal alpha-toxin with human serumStaphylococcal alpha-toxin: oligomerization of hydrophilic monomers to form amphiphilic hexamers induced through contact with deoxycholate detergent micelles.On the mechanism of membrane damage by Staphylococcus aureus alpha-toxin.Inhibiting bacterial toxins by channel blockage.Ultracentrifugal analysis of staphylococcal alpha toxinInteraction of staphylococcal alpha-toxin with artificial and natural membranesLytic effects of staphylococcal alpha-toxin and delta-hemolysin.Some properties of staphylococcal alpha-toxoidDistribution of 3H-labeled staphylococcal alpha-toxin and a toxin fragment in miceQuantitation 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.Mechanism of membrane damage by streptolysin-O.Correlation between toxin binding and hemolytic activity in membrane damage by staphylococcal alpha-toxin.Botulinal toxins and the problem of nomenclature of simple toxins.Demonstration of a temperature-dependent inactivating factor of the thermostable direct hemolysin in Vibrio parahaemolyticusCharacterization of the temperature-dependent inactivating factor of the thermostable direct hemolysin in Vibrio parahaemolyticusCholesteryl de-esterifying enzyme from Staphylococcus aureus: separation from alpha toxin, purification, and some propertiesInhibition of staphylococcal alpha-toxin. A kinetic evaluation of aromatic polysulphonic acids as inhibitors of haemolysis.
P2860
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P2860
description
1967 nî lūn-bûn
@nan
1967年の論文
@ja
1967年論文
@yue
1967年論文
@zh-hant
1967年論文
@zh-hk
1967年論文
@zh-mo
1967年論文
@zh-tw
1967年论文
@wuu
1967年论文
@zh
1967年论文
@zh-cn
name
Physical states of staphylococcal alpha-toxin.
@ast
Physical states of staphylococcal alpha-toxin.
@en
type
label
Physical states of staphylococcal alpha-toxin.
@ast
Physical states of staphylococcal alpha-toxin.
@en
prefLabel
Physical states of staphylococcal alpha-toxin.
@ast
Physical states of staphylococcal alpha-toxin.
@en
P2093
P2860
P1476
Physical states of staphylococcal alpha-toxin.
@en
P2093
Arbuthnott JP
Bernheimer AW
P2860
P304
P407
P577
1967-10-01T00:00:00Z