Cytotoxicity of the Bacillus cereus Nhe enterotoxin requires specific binding order of its three exoprotein components.
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Structure of the NheA Component of the Nhe Toxin from Bacillus cereus: Implications for FunctionAssembling the puzzle: Oligomerization of α-pore forming proteins in membranesConcerted action of sphingomyelinase and non-hemolytic enterotoxin in pathogenic Bacillus cereus.Complex formation between NheB and NheC is necessary to induce cytotoxic activity by the three-component Bacillus cereus Nhe enterotoxin.The Bacillus cereus Hbl and Nhe tripartite enterotoxin components assemble sequentially on the surface of target cells and are not interchangeable.Massive horizontal gene transfer, strictly vertical inheritance and ancient duplications differentially shape the evolution of Bacillus cereus enterotoxin operons hbl, cytK and nhe.Antibody Binding Studies Reveal Conformational Flexibility of the Bacillus cereus Non-Hemolytic Enterotoxin (Nhe) A-Component.Probiotic Bacillus cereus Strains, a Potential Risk for Public Health in China.Regulation of toxin production by Bacillus cereus and its food safety implications.Monoclonal antibodies neutralize Bacillus cereus Nhe enterotoxin by inhibiting ordered binding of its three exoprotein components.Formation of very large conductance channels by Bacillus cereus Nhe in Vero and GH(4) cells identifies NheA + B as the inherent pore-forming structure.Non-hemolytic enterotoxin of Bacillus cereus induces apoptosis in Vero cells.Evidence for Complex Formation of the Bacillus cereus Haemolysin BL Components in Solution.Crystallization and preliminary crystallographic analysis of the NheA component of the Nhe toxin from Bacillus cereus.Ordered self-assembly of proteins for computation in mammalian cells.Risks for public health related to the presence of Bacillus cereus and other Bacillus spp. including Bacillus thuringiensis in foodstuffsStructural and Mechanistic Features of ClyA-Like α-Pore-Forming ToxinsBacterial Toxins - Structure, Properties and Mode of Action
P2860
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P2860
Cytotoxicity of the Bacillus cereus Nhe enterotoxin requires specific binding order of its three exoprotein components.
description
2010 nî lūn-bûn
@nan
2010年の論文
@ja
2010年論文
@yue
2010年論文
@zh-hant
2010年論文
@zh-hk
2010年論文
@zh-mo
2010年論文
@zh-tw
2010年论文
@wuu
2010年论文
@zh
2010年论文
@zh-cn
name
Cytotoxicity of the Bacillus c ...... s three exoprotein components.
@en
Cytotoxicity of the Bacillus c ...... s three exoprotein components.
@nl
type
label
Cytotoxicity of the Bacillus c ...... s three exoprotein components.
@en
Cytotoxicity of the Bacillus c ...... s three exoprotein components.
@nl
prefLabel
Cytotoxicity of the Bacillus c ...... s three exoprotein components.
@en
Cytotoxicity of the Bacillus c ...... s three exoprotein components.
@nl
P2093
P2860
P356
P1476
Cytotoxicity of the Bacillus c ...... s three exoprotein components.
@en
P2093
Andrea Didier
Annette Fagerlund
Carina Nielsen
Marianne Sødring
Maximilian Casteel
Maximilian Moravek
Per Einar Granum
Richard Dietrich
Simon P Hardy
Stefanie Bock
P2860
P304
P356
10.1128/IAI.00247-10
P407
P577
2010-07-12T00:00:00Z