A conserved stable core structure in the passenger domain beta-helix of autotransporter virulence proteins.
about
The translocation domain in trimeric autotransporter adhesins is necessary and sufficient for trimerization and autotransportationOf linkers and autochaperones: an unambiguous nomenclature to identify common and uncommon themes for autotransporter secretion.Crystal Structure of the Autochaperone Region from the Shigella flexneri Autotransporter IcsACrystal Structure of the Passenger Domain of the Escherichia coli Autotransporter EspPSecretion of the Intimin Passenger Domain Is Driven by Protein Folding.Looks can be deceiving: recent insights into the mechanism of protein secretion by the autotransporter pathway.The passenger-associated transport repeat promotes virulence factor secretion efficiency and delineates a distinct autotransporter subtype.Stepwise folding of an autotransporter passenger domain is not essential for its secretionA conserved aromatic residue in the autochaperone domain of the autotransporter Hbp is critical for initiation of outer membrane translocationType V Secretion: the Autotransporter and Two-Partner Secretion PathwaysClusters of isoleucine, leucine, and valine side chains define cores of stability in high-energy states of globular proteins: Sequence determinants of structure and stability.Two-Partner Secretion: Combining Efficiency and Simplicity in the Secretion of Large Proteins for Bacteria-Host and Bacteria-Bacteria InteractionsSecretion of a bacterial virulence factor is driven by the folding of a C-terminal segment.Autotransporter-based cell surface display in Gram-negative bacteria.Multiple driving forces required for efficient secretion of autotransporter virulence proteinsDegP Chaperone Suppresses Toxic Inner Membrane Translocation Intermediates.Flagellar localization of a Helicobacter pylori autotransporter protein.Autotransporters: The Cellular Environment Reshapes a Folding Mechanism to Promote Protein TransportAn alternative outer membrane secretion mechanism for an autotransporter protein lacking a C-terminal stable core.Interactions between EB1 and microtubules: dramatic effect of affinity tags and evidence for cooperative behavior.Serine protease autotransporters of enterobacteriaceae (SPATEs): biogenesis and function.Autoprocessing of the Escherichia coli AIDA-I autotransporter: a new mechanism involving acidic residues in the junction region.Subdomain 2 of the Autotransporter Pet Is the Ligand Site for Recognizing the Pet Receptor on the Epithelial Cell Surface.Size and conformation limits to secretion of disulfide-bonded loops in autotransporter proteins.Structural characteristics of the plasmid-encoded toxin from enteroaggregative Escherichia coli.Identification and mechanism of evolution of new alleles coding for the AIDA-I autotransporter of porcine pathogenic Escherichia coli.A structurally informed autotransporter platform for efficient heterologous protein secretion and display.A novel mode of translocation for cytolethal distending toxin.An Acinetobacter trimeric autotransporter adhesin reaped from cells exhibits its nonspecific stickiness via a highly stable 3D structure.A host-specific factor is necessary for efficient folding of the autotransporter plasmid-encoded toxin.A generalised module for the selective extracellular accumulation of recombinant proteinsATP-independent control of autotransporter virulence protein transport via the folding properties of the secreted protein.Structure-function analysis of the TibA self-associating autotransporter reveals a modular organization.Purification of recombinant high molecular weight two-partner secretion proteins from Escherichia coli.Molecular basis for the folding of β-helical autotransporter passenger domains.
P2860
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P2860
A conserved stable core structure in the passenger domain beta-helix of autotransporter virulence proteins.
description
2008 nî lūn-bûn
@nan
2008年の論文
@ja
2008年学术文章
@wuu
2008年学术文章
@zh-cn
2008年学术文章
@zh-hans
2008年学术文章
@zh-my
2008年学术文章
@zh-sg
2008年學術文章
@yue
2008年學術文章
@zh
2008年學術文章
@zh-hant
name
A conserved stable core struct ...... ransporter virulence proteins.
@en
A conserved stable core struct ...... ransporter virulence proteins.
@nl
type
label
A conserved stable core struct ...... ransporter virulence proteins.
@en
A conserved stable core struct ...... ransporter virulence proteins.
@nl
prefLabel
A conserved stable core struct ...... ransporter virulence proteins.
@en
A conserved stable core struct ...... ransporter virulence proteins.
@nl
P356
P1433
P1476
A conserved stable core struct ...... ransporter virulence proteins.
@en
P2093
Jonathan P Renn
P304
P356
10.1002/BIP.20924
P577
2008-05-01T00:00:00Z