Structural characterization of the N terminus of IpaC from Shigella flexneri - Wikidata - wikimedia - TriplyDB

Structural characterization of the N terminus of IpaC from Shigella flexneri

Structural characterization of the N terminus of IpaC from Shigella flexneri

http://www.wikidata.org/entity/Q39730227

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Combination of Two Separate Binding Domains Defines Stoichiometry between Type III Secretion System Chaperone IpgC and Translocator Protein IpaB Protein 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 cells Cytoplasmic targeting of IpaC to the bacterial pole directs polar type III secretion in Shigella Influence 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.

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Structural characterization of the N terminus of IpaC from Shigella flexneri

http://www.wikidata.org/entity/Q39730227

description

2003 nî lūn-bûn

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2003年の論文

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2003年論文

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2003年論文

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2003年論文

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2003年論文

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2003年论文

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2003年论文

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2003年论文

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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

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IAI.71.3.1255-1264.2003

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Infection and Immunity

P1476

Structural characterization of the N terminus of IpaC from Shigella flexneri

@en

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Amanda T Harrington

http://www.w3.org/2001/XMLSchema#string

Andrew Wessel

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Jeffrey R Barker

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Patricia D Hearn

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Wendy L Picking

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William D Picking

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P2860

Type III protein secretion systems in bacterial pathogens of animals and plants

Three-dimensional secretion signals in chaperone-effector complexes of bacterial pathogens

Structure and composition of the Shigella flexneri "needle complex", a part of its type III secreton

Port of entry--the type III secretion translocon.

Characterization of the interaction partners of secreted proteins and chaperones of Shigella flexneri.

Characterization of invasion plasmid antigen genes (ipaBCD) from Shigella flexneri

Identification of icsA, a plasmid locus of Shigella flexneri that governs bacterial intra- and intercellular spread through interaction with F-actin.

Yersinia enterocolitica type III secretion. On the role of SycE in targeting YopE into HeLa cells.

The tripartite type III secreton of Shigella flexneri inserts IpaB and IpaC into host membranes

From flagellum assembly to virulence: the extended family of type III export chaperones.

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1255-1264

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scholarly article

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10.1128/IAI.71.3.1255-1264.2003

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3

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2003-03-01T00:00:00Z

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12595440

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Shigella flexneri

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148864

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