Roles of periplasmic chaperone proteins in the biogenesis of serine protease autotransporters of Enterobacteriaceae. - Wikidata - awgldk - TriplyDB

Roles of periplasmic chaperone proteins in the biogenesis of serine protease autotransporters of Enterobacteriaceae.

Roles of periplasmic chaperone proteins in the biogenesis of serine protease autotransporters of Enterobacteriaceae.

http://www.wikidata.org/entity/Q30157137

about

Type V secretion: mechanism(s) of autotransport through the bacterial outer membrane Bacterial serine proteases secreted by the autotransporter pathway: classification, specificity, and role in virulence Prevalence, biogenesis, and functionality of the serine protease autotransporter EspP Of linkers and autochaperones: an unambiguous nomenclature to identify common and uncommon themes for autotransporter secretion.Bacterial Secretion Systems: An Overview A novel virulence strategy for Pseudomonas aeruginosa mediated by an autotransporter with arginine-specific aminopeptidase activity Maximized Autotransporter-Mediated Expression (MATE) for Surface Display and Secretion of Recombinant Proteins in Escherichia coli Looks can be deceiving: recent insights into the mechanism of protein secretion by the autotransporter pathway.LytM proteins play a crucial role in cell separation, outer membrane composition, and pathogenesis in nontypeable Haemophilus influenzae.Reconstitution of bacterial autotransporter assembly using purified components.A mortise-tenon joint in the transmembrane domain modulates autotransporter assembly into bacterial outer membranes.Stepwise folding of an autotransporter passenger domain is not essential for its secretion Charge-dependent secretion of an intrinsically disordered protein via the autotransporter pathway.SurA is involved in the targeting to the outer membrane of a Tat signal sequence-anchored protein.Autotransporter protein secretion.The Bam machine: a molecular cooper.The essential β-barrel assembly machinery complex components BamD and BamA are required for autotransporter biogenesis.Interaction of FkpA, a peptidyl-prolyl cis/trans isomerase with EspP autotransporter protein.Type V Secretion: the Autotransporter and Two-Partner Secretion Pathways Importance of conserved residues of the serine protease autotransporter beta-domain in passenger domain processing and beta-barrel assembly A large family of anti-activators accompanying XylS/AraC family regulatory proteins Microbial peptidyl-prolyl cis/trans isomerases (PPIases): virulence factors and potential alternative drug targets.A bioinformatic strategy for the detection, classification and analysis of bacterial autotransporters.Host-Toxin Interactions Involving EspC and Pet, Two Serine Protease Autotransporters of the Enterobacteriaceae.Role of the periplasmic chaperones Skp, SurA, and DegQ in outer membrane protein biogenesis in Neisseria meningitidis.Autotransporter-based cell surface display in Gram-negative bacteria.Secretome of obligate intracellular Rickettsia.Adhesin degradation accelerates delivery of heat-labile toxin by enterotoxigenic Escherichia coli Expression during host infection and localization of Yersinia pestis autotransporter proteins.Multiple driving forces required for efficient secretion of autotransporter virulence proteins 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.HtrA chaperone activity contributes to host cell binding in Campylobacter jejuni.Skin-Derived C-Terminal Filaggrin-2 Fragments Are Pseudomonas aeruginosa-Directed Antimicrobials Targeting Bacterial Replication.DegP Chaperone Suppresses Toxic Inner Membrane Translocation Intermediates.VirK is a periplasmic protein required for efficient secretion of plasmid-encoded toxin from enteroaggregative Escherichia coli.Trimeric autotransporter adhesins in members of the Burkholderia cepacia complex: a multifunctional family of proteins implicated in virulence.Structure, Function, and Assembly of Adhesive Organelles by Uropathogenic Bacteria Functional heterogeneity of the UpaH autotransporter protein from uropathogenic Escherichia coli.Acquisition of omptin reveals cryptic virulence function of autotransporter YapE in Yersinia pestis

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P2860

Roles of periplasmic chaperone proteins in the biogenesis of serine protease autotransporters of Enterobacteriaceae.

http://www.wikidata.org/entity/Q30157137

description

2009 nî lūn-bûn

@nan

2009 թուականի Սեպտեմբերին հրատարակուած գիտական յօդուած

@hyw

2009 թվականի սեպտեմբերին հրատարակված գիտական հոդված

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2009年の論文

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2009年論文

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2009年論文

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2009年論文

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2009年論文

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2009年論文

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2009年论文

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name

Roles of periplasmic chaperone ...... porters of Enterobacteriaceae.

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Roles of periplasmic chaperone ...... porters of Enterobacteriaceae.

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type

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Roles of periplasmic chaperone ...... porters of Enterobacteriaceae.

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Roles of periplasmic chaperone ...... porters of Enterobacteriaceae.

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Roles of periplasmic chaperone ...... porters of Enterobacteriaceae.

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Roles of periplasmic chaperone ...... porters of Enterobacteriaceae.

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P1433

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P1433

Journal of Bacteriology

P1476

Roles of periplasmic chaperone ...... porters of Enterobacteriaceae.

@en

P2093

Amanda E Rossiter

http://www.w3.org/2001/XMLSchema#string

Fernando Ruiz-Perez

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Ian R Henderson

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Yinghua Zhang

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P2860

CLUSTAL W: improving the sensitivity of progressive multiple sequence alignment through sequence weighting, position-specific gap penalties and weight matrix choice

Membrane protein insertion: mixing eukaryotic and prokaryotic concepts.

Cleavage of structural proteins during the assembly of the head of bacteriophage T4

Crystal structure of DegP (HtrA) reveals a new protease-chaperone machine

Crystallographic structure of SurA, a molecular chaperone that facilitates folding of outer membrane porins

The Periplasmic Bacterial Molecular Chaperone SurA Adapts its Structure to Bind Peptides in Different Conformations to Assert a Sequence Preference for Aromatic Residues

Structural basis for the regulated protease and chaperone function of DegP

The SurA periplasmic PPIase lacking its parvulin domains functions in vivo and has chaperone activity.

Role of a highly conserved bacterial protein in outer membrane protein assembly

Recognition of unique carboxyl-terminal motifs by distinct PDZ domains

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6571-6583

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scholarly article

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10.1128/JB.00754-09

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21

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191

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Denisse L Leyton

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2009-09-04T00:00:00Z

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26793364

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19734313

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molecular chaperones

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2795308

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