Protein refolding is required for assembly of the type three secretion needle
about
Atomic model of the type III secretion system needleBacterial type III secretion systems: specialized nanomachines for protein delivery into target cellsThe crystal structures of theSalmonellatype III secretion system tip protein SipD in complex with deoxycholate and chenodeoxycholateCrystal Structure of PrgI-SipD: Insight into a Secretion Competent State of the Type Three Secretion System Needle Tip and its Interaction with Host LigandsStructure of a type III secretion needle at 7-A resolution provides insights into its assembly and signaling mechanismsThe Structure and Function of Type III Secretion SystemsThe common structural architecture of Shigella flexneri and Salmonella typhimurium type three secretion needlesProtein export according to schedule: architecture, assembly, and regulation of type III secretion systems from plant- and animal-pathogenic bacteria.Structure of the Vibrio cholerae Type IVb Pilus and stability comparison with the Neisseria gonorrhoeae type IVa pilusCharacterization of the interaction between the Salmonella type III secretion system tip protein SipD and the needle protein PrgI by paramagnetic relaxation enhancement.Role of Salmonella Pathogenicity Island 1 protein IacP in Salmonella enterica serovar typhimurium pathogenesis.Amino acids 89-96 of Salmonella typhimurium flagellin represent the major domain responsible for TLR5-independent adjuvanticity in the humoral immune responseThe Salmonella type III secretion system inner rod protein PrgJ is partially folded.Type-III secretion filaments as scaffolds for inorganic nanostructures.EscE and EscG are cochaperones for the type III needle protein EscF of enteropathogenic Escherichia coliStructure and biophysics of type III secretion in bacteriaHuman NAIP and mouse NAIP1 recognize bacterial type III secretion needle protein for inflammasome activation.The inner rod protein controls substrate switching and needle length in a Salmonella type III secretion system.S-nitrosylation of UCHL1 induces its structural instability and promotes α-synuclein aggregation.Solid-state NMR spectroscopy on complex biomolecules.The blueprint of the type-3 injectisome.Assembly of the bacterial type III secretion machinery.Building a secreting nanomachine: a structural overview of the T3SS.Salmonella and the Inflammasome: Battle for Intracellular Dominance.Nuclear magnetic resonance (NMR) applied to membrane-protein complexes.EspC forms a filamentous structure in the cell envelope of Mycobacterium tuberculosis and impacts ESX-1 secretion.Nuclear Magnetic Resonance Characterization of the Type III Secretion System Tip Chaperone Protein PcrG of Pseudomonas aeruginosa.Reassessment of MxiH subunit orientation and fold within native Shigella T3SS needles using surface labelling and solid-state NMR.Fractional deuteration applied to biomolecular solid-state NMR spectroscopyNeedle length control and the secretion substrate specificity switch are only loosely coupled in the type III secretion apparatus of ShigellaNMR model of PrgI-SipD interaction and its implications in the needle-tip assembly of the Salmonella type III secretion systemThree-dimensional electron microscopy reconstruction and cysteine-mediated crosslinking provide a model of the type III secretion system needle tip complex.Discovery of the type VII ESX-1 secretion needle?A protein secreted by the type III secretion system controls needle filament assemblyBacterial type III secretion systems: a complex device for the delivery of bacterial effector proteins into eukaryotic host cells
P2860
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P2860
Protein refolding is required for assembly of the type three secretion needle
description
2010 nî lūn-bûn
@nan
2010 թուականի Յուլիսին հրատարակուած գիտական յօդուած
@hyw
2010 թվականի հուլիսին հրատարակված գիտական հոդված
@hy
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
name
Protein refolding is required for assembly of the type three secretion needle
@ast
Protein refolding is required for assembly of the type three secretion needle
@en
Protein refolding is required for assembly of the type three secretion needle
@nl
type
label
Protein refolding is required for assembly of the type three secretion needle
@ast
Protein refolding is required for assembly of the type three secretion needle
@en
Protein refolding is required for assembly of the type three secretion needle
@nl
prefLabel
Protein refolding is required for assembly of the type three secretion needle
@ast
Protein refolding is required for assembly of the type three secretion needle
@en
Protein refolding is required for assembly of the type three secretion needle
@nl
P2093
P2860
P356
P1476
Protein refolding is required for assembly of the type three secretion needle
@en
P2093
Adam Lange
Andreas F Thünemann
Arturo Zychlinsky
Britta Laube
Christian Ader
Christian Goosmann
Friedmar Delissen
Hezi Tenenboim
Holger Schmidt
Marc Baldus
P2860
P2888
P304
P356
10.1038/NSMB.1822
P577
2010-07-01T00:00:00Z
P5875
P6179
1037437249