Structural characterization of the N terminus of IpaC from Shigella flexneri
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Combination of Two Separate Binding Domains Defines Stoichiometry between Type III Secretion System Chaperone IpgC and Translocator Protein IpaBProtein export according to schedule: architecture, assembly, and regulation of type III secretion systems from plant- and animal-pathogenic bacteria.The C-terminus of IpaC is required for effector activities related to Shigella invasion of host cellsCytoplasmic targeting of IpaC to the bacterial pole directs polar type III secretion in ShigellaInfluence of oligomerization state on the structural properties of invasion plasmid antigen B from Shigella flexneri in the presence and absence of phospholipid membranes.Shigella flexneri infection: pathogenesis and vaccine development.Expression, limited proteolysis and preliminary crystallographic analysis of IpaD, a component of the Shigella flexneri type III secretion system.Conformational stability and differential structural analysis of LcrV, PcrV, BipD, and SipD from type III secretion systems.Molecular pathogenesis of Shigella spp.: controlling host cell signaling, invasion, and death by type III secretion.A translocator-specific export signal establishes the translocator-effector secretion hierarchy that is important for type III secretion system function.Mapping of the chaperone AcrH binding regions of translocators AopB and AopD and characterization of oligomeric and metastable AcrH-AopB-AopD complexes in the type III secretion system of Aeromonas hydrophila.The Bordetella type III secretion system effector BteA contains a conserved N-terminal motif that guides bacterial virulence factors to lipid rafts.Membrane targeting and pore formation by the type III secretion system translocon.Functional relatedness in the Inv/Mxi-Spa type III secretion system family.Impact of the N-terminal secretor domain on YopD translocator function in Yersinia pseudotuberculosis type III secretion.Deoxycholate interacts with IpaD of Shigella flexneri in inducing the recruitment of IpaB to the type III secretion apparatus needle tip.IpaD of Shigella flexneri is independently required for regulation of Ipa protein secretion and efficient insertion of IpaB and IpaC into host membranes.N-terminus of IpaB provides a potential anchor to the Shigella type III secretion system tip complex protein IpaD.Liposomes recruit IpaC to the Shigella flexneri type III secretion apparatus needle as a final step in secretion induction.Identification of the MxiH needle protein residues responsible for anchoring invasion plasmid antigen D to the type III secretion needle tip.
P2860
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P2860
Structural characterization of the N terminus of IpaC from Shigella flexneri
description
2003 nî lūn-bûn
@nan
2003年の論文
@ja
2003年論文
@yue
2003年論文
@zh-hant
2003年論文
@zh-hk
2003年論文
@zh-mo
2003年論文
@zh-tw
2003年论文
@wuu
2003年论文
@zh
2003年论文
@zh-cn
name
Structural characterization of the N terminus of IpaC from Shigella flexneri
@en
Structural characterization of the N terminus of IpaC from Shigella flexneri.
@nl
type
label
Structural characterization of the N terminus of IpaC from Shigella flexneri
@en
Structural characterization of the N terminus of IpaC from Shigella flexneri.
@nl
prefLabel
Structural characterization of the N terminus of IpaC from Shigella flexneri
@en
Structural characterization of the N terminus of IpaC from Shigella flexneri.
@nl
P2093
P2860
P1476
Structural characterization of the N terminus of IpaC from Shigella flexneri
@en
P2093
Amanda T Harrington
Andrew Wessel
Jeffrey R Barker
Patricia D Hearn
Wendy L Picking
William D Picking
P2860
P304
P356
10.1128/IAI.71.3.1255-1264.2003
P407
P577
2003-03-01T00:00:00Z