Interaction of FkpA, a peptidyl-prolyl cis/trans isomerase with EspP autotransporter protein.
about
Type V secretion: mechanism(s) of autotransport through the bacterial outer membraneBacterial serine proteases secreted by the autotransporter pathway: classification, specificity, and role in virulencePrevalence, biogenesis, and functionality of the serine protease autotransporter EspPLooks can be deceiving: recent insights into the mechanism of protein secretion by the autotransporter pathway.A mortise-tenon joint in the transmembrane domain modulates autotransporter assembly into bacterial outer membranes.The Bam machine: a molecular cooper.Proteinaceous determinants of surface colonization in bacteria: bacterial adhesion and biofilm formation from a protein secretion perspective.Microbial peptidyl-prolyl cis/trans isomerases (PPIases): virulence factors and potential alternative drug targets.Autotransporter-based cell surface display in Gram-negative bacteria.Expression during host infection and localization of Yersinia pestis autotransporter proteins.The RpoE Stress Response Pathway Mediates Reduction of the Virulence of Enteropathogenic Escherichia coli by Zinc.Outer membrane targeting of secretin PulD protein relies on disordered domain recognition by a dedicated chaperone.Molecular characterization of UpaB and UpaC, two new autotransporter proteins of uropathogenic Escherichia coli CFT073.Reconstitution of a nanomachine driving the assembly of proteins into bacterial outer membranes.Functional heterogeneity of the UpaH autotransporter protein from uropathogenic Escherichia coli.Acquisition of omptin reveals cryptic virulence function of autotransporter YapE in Yersinia pestisProteolytic processing of the Yersinia pestis YapG autotransporter by the omptin protease Pla and the contribution of YapG to murine plague pathogenesisRole for Skp in LptD assembly in Escherichia coli.An alternative outer membrane secretion mechanism for an autotransporter protein lacking a C-terminal stable core.The β-Barrel Assembly Machinery Complex.Biochemical characterization of the SPATE members EspPα and EspI.Biochemical characterization of two Azotobacter vinelandii FKBPs and analysis of their interaction with the small subunit of carbamoyl phosphate synthetase.Discovery of a novel periplasmic protein that forms a complex with a trimeric autotransporter adhesin and peptidoglycan.Molecular basis for the folding of β-helical autotransporter passenger domains.Analyzing the Role of Periplasmic Folding Factors in the Biogenesis of OMPs and Members of the Type V Secretion System.
P2860
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P2860
Interaction of FkpA, a peptidyl-prolyl cis/trans isomerase with EspP autotransporter protein.
description
2010 nî lūn-bûn
@nan
2010 թուականի Օգոստոսին հրատարակուած գիտական յօդուած
@hyw
2010 թվականի օգոստոսին 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
Interaction of FkpA, a peptidy ...... EspP autotransporter protein.
@ast
Interaction of FkpA, a peptidy ...... EspP autotransporter protein.
@en
type
label
Interaction of FkpA, a peptidy ...... EspP autotransporter protein.
@ast
Interaction of FkpA, a peptidy ...... EspP autotransporter protein.
@en
prefLabel
Interaction of FkpA, a peptidy ...... EspP autotransporter protein.
@ast
Interaction of FkpA, a peptidy ...... EspP autotransporter protein.
@en
P2860
P356
P1433
P1476
Interaction of FkpA, a peptidy ...... EspP autotransporter protein.
@en
P2093
Fernando Ruiz-Perez
Ian R Henderson
P2860
P304
P356
10.4161/GMIC.1.5.13436
P577
2010-08-29T00:00:00Z