Interactions of the type III secretion pathway proteins LcrV and LcrG from Yersinia pestis are mediated by coiled-coil domains.
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The HaloTag: Improving Soluble Expression and Applications in Protein Functional AnalysisType III secretion proteins PcrV and PcrG from Pseudomonas aeruginosa form a 1:1 complex through high affinity interactionsThe crystal structures of theSalmonellatype III secretion system tip protein SipD in complex with deoxycholate and chenodeoxycholateStructure of theYersinia pestistip protein LcrV refined to 1.65 Å resolutionNovel protein-protein interactions of the Yersinia pestis type III secretion system elucidated with a matrix analysis by surface plasmon resonance and mass spectrometry.LcrG secretion is not required for blocking of Yops secretion in Yersinia pestis.Amino acid and structural variability of Yersinia pestis LcrV protein.Biophysical characterization of Chlamydia trachomatis CT584 supports its potential role as a type III secretion needle tip protein.Control of effector export by the Pseudomonas aeruginosa type III secretion proteins PcrG and PcrV.The use of live attenuated bacteria as a delivery system for heterologous antigens.Self-chaperoning of the type III secretion system needle tip proteins IpaD and BipD.Diminished LcrV secretion attenuates Yersinia pseudotuberculosis virulence.Conformational stability and differential structural analysis of LcrV, PcrV, BipD, and SipD from type III secretion systems.Interaction between Yersinia pestis and the host immune systemRoles of YopN, LcrG and LcrV in controlling Yops secretion by Yersinia pestis.Structure and biophysics of type III secretion in bacteriaType III secretion translocon assemblies that attenuate Yersinia virulence.SUMO modification of the neuroprotective protein TDP1 facilitates chromosomal single-strand break repair.Structural analysis of inter-genus complexes of V-antigen and its regulator and their stabilization by divalent metal ions.Nuclear Magnetic Resonance Characterization of the Type III Secretion System Tip Chaperone Protein PcrG of Pseudomonas aeruginosa.Oligomerization of PcrV and LcrV, protective antigens of Pseudomonas aeruginosa and Yersinia pestis.The LcrG Tip Chaperone Protein of the Yersinia pestis Type III Secretion System Is Partially Folded.In Vivo Photo-Cross-Linking to Study T3S Interactions Demonstrated Using the Yersinia pestis T3S System.Structure-function analysis of the C-terminal domain of LcrV from Yersinia pestis.PcrG protects the two long helical oligomerization domains of PcrV, by an interaction mediated by the intramolecular coiled-coil region of PcrG.Shigella IpaD has a dual role: signal transduction from the type III secretion system needle tip and intracellular secretion regulation.Nonreducing terminal modifications determine the chain length of polymannose O antigens of Escherichia coli and couple chain termination to polymer export via an ATP-binding cassette transporter.
P2860
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P2860
Interactions of the type III secretion pathway proteins LcrV and LcrG from Yersinia pestis are mediated by coiled-coil domains.
description
2002 nî lūn-bûn
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2002年の論文
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2002年論文
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2002年論文
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2002年論文
@zh-hk
2002年論文
@zh-mo
2002年論文
@zh-tw
2002年论文
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2002年论文
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name
Interactions of the type III s ...... diated by coiled-coil domains.
@en
type
label
Interactions of the type III s ...... diated by coiled-coil domains.
@en
prefLabel
Interactions of the type III s ...... diated by coiled-coil domains.
@en
P2093
P2860
P50
P356
P1476
Interactions of the type III s ...... ediated by coiled-coil domains
@en
P2093
Daniel G Lawton
Katherine A Brown
Sophie E C Leary
P2860
P304
38714-38722
P356
10.1074/JBC.M203632200
P407
P577
2002-07-09T00:00:00Z