X-ray crystal structure of the B component of Hemolysin BL fromBacillus cereus
about
Structure of the NheA Component of the Nhe Toxin from Bacillus cereus: Implications for FunctionAdaptation in Bacillus cereus: From Stress to DiseaseThe pesticidal Cry6Aa toxin from Bacillus thuringiensis is structurally similar to HlyE-family alpha pore-forming toxinsAssembling the puzzle: Oligomerization of α-pore forming proteins in membranesExpanding the known repertoire of virulence factors produced by Bacillus cereus through early secretome profiling in three redox conditions.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.Antibody Binding Studies Reveal Conformational Flexibility of the Bacillus cereus Non-Hemolytic Enterotoxin (Nhe) A-Component.YaxAB, a Yersinia enterocolitica pore-forming toxin regulated by RovA.Production, secretion and biological activity of Bacillus cereus enterotoxinsCry6Aa1, a Bacillus thuringiensis nematocidal and insecticidal toxin, forms pores in planar lipid bilayers at extremely low concentrations and without the need of proteolytic processing.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.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.Screening of Cytotoxic B. cereus on Differentiated Caco-2 Cells and in Co-Culture with Mucus-Secreting (HT29-MTX) Cells.Cytotoxicity of the Bacillus cereus Nhe enterotoxin requires specific binding order of its three exoprotein components.Disruption of the open conductance in the β-tongue mutants of Cytolysin A.Structure and mechanism of the two-component α-helical pore-forming toxin YaxAB.Membrane insertion of α-xenorhabdolysin in near-atomic detailFlagella-mediated secretion of a novel cytotoxin affecting both vertebrate and invertebrate hostsStructural and Mechanistic Features of ClyA-Like α-Pore-Forming ToxinsBacterial Toxins - Structure, Properties and Mode of Action
P2860
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P2860
X-ray crystal structure of the B component of Hemolysin BL fromBacillus cereus
description
2008 nî lūn-bûn
@nan
2008 թուականի Մայիսին հրատարակուած գիտական յօդուած
@hyw
2008 թվականի մայիսին հրատարակված գիտական հոդված
@hy
2008年の論文
@ja
2008年論文
@yue
2008年論文
@zh-hant
2008年論文
@zh-hk
2008年論文
@zh-mo
2008年論文
@zh-tw
2008年论文
@wuu
name
X-ray crystal structure of the B component of Hemolysin BL fromBacillus cereus
@ast
X-ray crystal structure of the B component of Hemolysin BL fromBacillus cereus
@en
X-ray crystal structure of the B component of Hemolysin BL fromBacillus cereus
@nl
type
label
X-ray crystal structure of the B component of Hemolysin BL fromBacillus cereus
@ast
X-ray crystal structure of the B component of Hemolysin BL fromBacillus cereus
@en
X-ray crystal structure of the B component of Hemolysin BL fromBacillus cereus
@nl
prefLabel
X-ray crystal structure of the B component of Hemolysin BL fromBacillus cereus
@ast
X-ray crystal structure of the B component of Hemolysin BL fromBacillus cereus
@en
X-ray crystal structure of the B component of Hemolysin BL fromBacillus cereus
@nl
P2093
P2860
P3181
P356
P1433
P1476
X-ray crystal structure of the B component of Hemolysin BL from Bacillus cereus
@en
P2093
Mahendra Madegowda
Subramaniam Eswaramoorthy
Subramanyam Swaminathan
P2860
P304
P3181
P356
10.1002/PROT.21888
P407
P577
2008-05-01T00:00:00Z