Pertactin beta-helix folding mechanism suggests common themes for the secretion and folding of autotransporter proteins. - Wikidata - thesis-toulmin - TriplyDB

Pertactin beta-helix folding mechanism suggests common themes for the secretion and folding of autotransporter proteins.

Pertactin beta-helix folding mechanism suggests common themes for the secretion and folding of autotransporter proteins.

http://www.wikidata.org/entity/Q33237120

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The translocation domain in trimeric autotransporter adhesins is necessary and sufficient for trimerization and autotransportation Type V secretion: mechanism(s) of autotransport through the bacterial outer membrane An Overview of Helicobacter pylori VacA Toxin Biology Bacterial serine proteases secreted by the autotransporter pathway: classification, specificity, and role in virulence Of linkers and autochaperones: an unambiguous nomenclature to identify common and uncommon themes for autotransporter secretion.Crystal structure of the Helicobacter pylori vacuolating toxin p55 domain Structure of the Receptor-Binding Protein of Bacteriophage Det7: a Podoviral Tail Spike in a Myovirus Structural and Functional Studies of Truncated Hemolysin A from Proteus mirabilis Autotransporter passenger domain secretion requires a hydrophobic cavity at the extracellular entrance of the β-domain pore Crystal Structure of the Autochaperone Region from the Shigella flexneri Autotransporter IcsA Crystal Structure of the Passenger Domain of the Escherichia coli Autotransporter EspP Rickettsia Sca2 has evolved formin-like activity through a different molecular mechanism Crystal Structures of the Outer Membrane Domain of Intimin and Invasin from Enterohemorrhagic E. coli and Enteropathogenic Y. pseudotuberculosis Secretion of the Intimin Passenger Domain Is Driven by Protein Folding.Sequential unfolding of the hemolysin two-partner secretion domain from Proteus mirabilis.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.Reconstitution of bacterial autotransporter assembly using purified components.A mortise-tenon joint in the transmembrane domain modulates autotransporter assembly into bacterial outer membranes.Analysis of surface-exposed outer membrane proteins in Helicobacter pylori.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.Single-cell characterization of autotransporter-mediated Escherichia coli surface display of disulfide bond-containing proteins.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 translocation Type V Secretion: the Autotransporter and Two-Partner Secretion Pathways UpaH is a newly identified autotransporter protein that contributes to biofilm formation and bladder colonization by uropathogenic Escherichia coli CFT073 Interaction of an autotransporter passenger domain with BamA during its translocation across the bacterial outer membrane.The Moraxella catarrhalis autotransporter McaP is a conserved surface protein that mediates adherence to human epithelial cells through its N-terminal passenger domain.Topology and maturation of filamentous haemagglutinin suggest a new model for two-partner secretion.Surface display of proteins by gram-negative bacterial autotransporters.Analysis of a beta-helical region in the p55 domain of Helicobacter pylori vacuolating toxin.Two-Partner Secretion: Combining Efficiency and Simplicity in the Secretion of Large Proteins for Bacteria-Host and Bacteria-Bacteria Interactions High-resolution structure of infectious prion protein: the final frontier The T7-related Pseudomonas putida phage φ15 displays virion-associated biofilm degradation properties.Reconstitution of Helicobacter pylori VacA toxin from purified components Prevalence and genetic characterization of pertactin-deficient Bordetella pertussis in Japan.Secretion of a bacterial virulence factor is driven by the folding of a C-terminal segment.

P2860

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P2860

Pertactin beta-helix folding mechanism suggests common themes for the secretion and folding of autotransporter proteins.

http://www.wikidata.org/entity/Q33237120

description

2006 nî lūn-bûn

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2006 թուականի Մարտին հրատարակուած գիտական յօդուած

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2006 թվականի մարտին հրատարակված գիտական հոդված

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2006年の論文

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2006年論文

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2006年論文

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2006年論文

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2006年論文

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2006年論文

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2006年论文

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name

Pertactin beta-helix folding m ...... g of autotransporter proteins.

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Pertactin beta-helix folding m ...... g of autotransporter proteins.

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type

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Pertactin beta-helix folding m ...... g of autotransporter proteins.

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Pertactin beta-helix folding m ...... g of autotransporter proteins.

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prefLabel

Pertactin beta-helix folding m ...... g of autotransporter proteins.

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Pertactin beta-helix folding m ...... g of autotransporter proteins.

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P1433

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PNAS.0507923103

P1433

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

P1476

Pertactin beta-helix folding m ...... g of autotransporter proteins.

@en

P2093

Andrew V McDonnell

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

Christopher C Schuster

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

Kelli A Sorg

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Mary C Finn

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Mirco Junker

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P2860

Gapped BLAST and PSI-BLAST: a new generation of protein database search programs

The Pfam protein families database

The Yersinia adhesin YadA collagen-binding domain structure is a novel left-handed parallel beta-roll

Plasticity and steric strain in a parallel beta-helix: rational mutations in the P22 tailspike protein

Structure of Bordetella pertussis virulence factor P.69 pertactin

The Omp85 family of proteins is essential for outer membrane biogenesis in mitochondria and bacteria.

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

Folding and insertion of the outer membrane protein OmpA is assisted by the chaperone Skp and by lipopolysaccharide.

Export of autotransported proteins proceeds through an oligomeric ring shaped by C-terminal domains.

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4918-4923

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13

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103

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Patricia L Clark

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2006-03-20T00:00:00Z

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7228783

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16549796

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P921

protein folding

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1458770

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