Hydrophobic residues of the autotransporter EspP linker domain are important for outer membrane translocation of its passenger.
about
Prevalence, biogenesis, and functionality of the serine protease autotransporter EspPOf linkers and autochaperones: an unambiguous nomenclature to identify common and uncommon themes for autotransporter secretion.Autotransporter structure reveals intra-barrel cleavage followed by conformational changesCrystal Structure of the Passenger Domain of the Escherichia coli Autotransporter EspPMolecular Basis for the Activation of a Catalytic Asparagine Residue in a Self-Cleaving Bacterial AutotransporterLooks can be deceiving: recent insights into the mechanism of protein secretion by the autotransporter pathway.Stepwise folding of an autotransporter passenger domain is not essential for its secretionAutotransporter protein secretion.Residues in a conserved α-helical segment are required for cleavage but not secretion of an Escherichia coli serine protease autotransporter passenger domain.A conserved aromatic residue in the autochaperone domain of the autotransporter Hbp is critical for initiation of outer membrane translocationRoles of periplasmic chaperone proteins in the biogenesis of serine protease autotransporters of Enterobacteriaceae.Cleavage of a bacterial autotransporter by an evolutionarily convergent autocatalytic mechanism.Role of the alpha-helical linker of the C-terminal translocator in the biogenesis of the serine protease subfamily of autotransportersPertactin beta-helix folding mechanism suggests common themes for the secretion and folding of autotransporter proteins.Surface display of proteins by gram-negative bacterial autotransporters.Subtypes of the plasmid-encoded serine protease EspP in Shiga toxin-producing Escherichia coli: distribution, secretion, and proteolytic activityStructure and function relationship of the autotransport and proteolytic activity of EspP from Shiga toxin-producing Escherichia coliSecretion of a bacterial virulence factor is driven by the folding of a C-terminal segment.Protein secretion in the absence of ATP: the autotransporter, two-partner secretion and chaperone/usher pathways of gram-negative bacteria (review).Autotransporter-based cell surface display in Gram-negative bacteria.Multiple driving forces required for efficient secretion of autotransporter virulence proteinsSecretion by numbers: Protein traffic in prokaryotes.The AraC Negative Regulator family modulates the activity of histone-like proteins in pathogenic bacteria.The periplasmic folding of a cysteineless autotransporter passenger domain interferes with its outer membrane translocation.Identification of the Autochaperone Domain in the Type Va Secretion System (T5aSS): Prevalent Feature of Autotransporters with a β-Helical Passenger.
P2860
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P2860
Hydrophobic residues of the autotransporter EspP linker domain are important for outer membrane translocation of its passenger.
description
2004 nî lūn-bûn
@nan
2004 թուականի Մայիսին հրատարակուած գիտական յօդուած
@hyw
2004 թվականի մայիսին հրատարակված գիտական հոդված
@hy
2004年の論文
@ja
2004年論文
@yue
2004年論文
@zh-hant
2004年論文
@zh-hk
2004年論文
@zh-mo
2004年論文
@zh-tw
2004年论文
@wuu
name
Hydrophobic residues of the au ...... ranslocation of its passenger.
@ast
Hydrophobic residues of the au ...... ranslocation of its passenger.
@en
type
label
Hydrophobic residues of the au ...... ranslocation of its passenger.
@ast
Hydrophobic residues of the au ...... ranslocation of its passenger.
@en
prefLabel
Hydrophobic residues of the au ...... ranslocation of its passenger.
@ast
Hydrophobic residues of the au ...... ranslocation of its passenger.
@en
P2860
P356
P1476
Hydrophobic residues of the au ...... ranslocation of its passenger.
@en
P2093
Jorge J Velarde
P2860
P304
31495-31504
P356
10.1074/JBC.M404424200
P407
P577
2004-05-19T00:00:00Z