Secretion of a bacterial virulence factor is driven by the folding of a C-terminal segment. - Wikidata - wikimedia - TriplyDB

Secretion of a bacterial virulence factor is driven by the folding of a C-terminal segment.

Secretion of a bacterial virulence factor is driven by the folding of a C-terminal segment.

http://www.wikidata.org/entity/Q34200224

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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 Crystal Structure of the Autochaperone Region from the Shigella flexneri Autotransporter IcsA Crystal Structure of the Passenger Domain of the Escherichia coli Autotransporter EspP Crystal Structures of the Outer Membrane Domain of Intimin and Invasin from Enterohemorrhagic E. coli and Enteropathogenic Y. pseudotuberculosis Membrane-protein structure determination by solid-state NMR spectroscopy of microcrystals Secretion 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.The inverse autotransporter intimin exports its passenger domain via a hairpin intermediate.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.Mechanistic link between β barrel assembly and the initiation of autotransporter secretion.Intimin and invasin export their C-terminus to the bacterial cell surface using an inverse mechanism compared to classical autotransport.Autotransporter protein secretion.Sequential and spatially restricted interactions of assembly factors with an autotransporter beta domain.Residues in a conserved α-helical segment are required for cleavage but not secretion of an Escherichia coli serine protease autotransporter passenger domain.Two-Partner Secretion: Combining Efficiency and Simplicity in the Secretion of Large Proteins for Bacteria-Host and Bacteria-Bacteria Interactions Transport proteins promoting Escherichia coli pathogenesis.Identification of Shigella flexneri IcsA residues affecting interaction with N-WASP, and evidence for IcsA-IcsA co-operative interaction.Protein folding in the cell: challenges and progress.Autotransporter-based cell surface display in Gram-negative bacteria.Secretome of obligate intracellular Rickettsia.Multiple driving forces required for efficient secretion of autotransporter virulence proteins DegP Chaperone Suppresses Toxic Inner Membrane Translocation Intermediates.Structure, Function, and Assembly of Adhesive Organelles by Uropathogenic Bacteria Autotransporters: The Cellular Environment Reshapes a Folding Mechanism to Promote Protein Transport An alternative outer membrane secretion mechanism for an autotransporter protein lacking a C-terminal stable core.Autotransporters with GDSL passenger domains: molecular physiology and biotechnological applications.Structure and function of the Haemophilus influenzae autotransporters.EHEC Adhesins New findings on the function and potential applications of the trimeric autotransporter adhesin.Expression of the Gene for Autotransporter AutB of Neisseria meningitidis Affects Biofilm Formation and Epithelial Transmigration.Not just an antibiotic target: Exploring the role of type I signal peptidase in bacterial virulence.Size and conformation limits to secretion of disulfide-bonded loops in autotransporter proteins.A structurally informed autotransporter platform for efficient heterologous protein secretion and display.A generalised module for the selective extracellular accumulation of recombinant proteins

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P2860

Secretion of a bacterial virulence factor is driven by the folding of a C-terminal segment.

http://www.wikidata.org/entity/Q34200224

description

2010 nî lūn-bûn

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2010 թուականի Սեպտեմբերին հրատարակուած գիտական յօդուած

@hyw

2010 թվականի սեպտեմբերին հրատարակված գիտական հոդված

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2010年の論文

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2010年論文

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2010年論文

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2010年論文

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2010年論文

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2010年論文

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2010年论文

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name

Secretion of a bacterial virul ...... lding of a C-terminal segment.

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Secretion of a bacterial virul ...... lding of a C-terminal segment.

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Secretion of a bacterial virul ...... lding of a C-terminal segment.

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type

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Secretion of a bacterial virul ...... lding of a C-terminal segment.

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Secretion of a bacterial virul ...... lding of a C-terminal segment.

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Secretion of a bacterial virul ...... lding of a C-terminal segment.

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Secretion of a bacterial virul ...... lding of a C-terminal segment.

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Secretion of a bacterial virul ...... lding of a C-terminal segment.

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Secretion of a bacterial virul ...... lding of a C-terminal segment.

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Proceedings of the National Academy of Sciences of the United States of America

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Secretion of a bacterial virul ...... olding of a C-terminal segment

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Harris D Bernstein

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Janine H Peterson

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Nathalie Dautin

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Pu Tian

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P2860

Crystal structure of the Helicobacter pylori vacuolating toxin p55 domain

Autotransporter structure reveals intra-barrel cleavage followed by conformational changes

Crystal structure of a full-length autotransporter

Structure of Bordetella pertussis virulence factor P.69 pertactin

A novel intein-like autoproteolytic mechanism in autotransporter proteins.

Interaction of an autotransporter passenger domain with BamA during its translocation across the bacterial outer membrane.

Cleavage of a bacterial autotransporter by an evolutionarily convergent autocatalytic mechanism.

Hydrophobic residues of the autotransporter EspP linker domain are important for outer membrane translocation of its passenger.

Structure of the translocator domain of a bacterial autotransporter

Characterization of the Neisseria Iga beta-core. The essential unit for outer membrane targeting and extracellular protein secretion.

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