Efficient secretion of a folded protein domain by a monomeric bacterial autotransporter. - Wikidata - awgldk - TriplyDB

Efficient secretion of a folded protein domain by a monomeric bacterial autotransporter.

Efficient secretion of a folded protein domain by a monomeric bacterial autotransporter.

http://www.wikidata.org/entity/Q46785700

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Structure of the outer membrane translocator domain of the Haemophilus influenzae Hia trimeric autotransporter Of linkers and autochaperones: an unambiguous nomenclature to identify common and uncommon themes for autotransporter secretion.Autotransporter structure reveals intra-barrel cleavage followed by conformational changes Active-Site Gating Regulates Substrate Selectivity in a Chymotrypsin-Like Serine Protease Autotransporter passenger domain secretion requires a hydrophobic cavity at the extracellular entrance of the β-domain pore Crystal Structure of the Passenger Domain of the Escherichia coli Autotransporter EspP Molecular Basis for the Activation of a Catalytic Asparagine Residue in a Self-Cleaving Bacterial Autotransporter Crystal Structures of the Outer Membrane Domain of Intimin and Invasin from Enterohemorrhagic E. coli and Enteropathogenic Y. pseudotuberculosis Looks can be deceiving: recent insights into the mechanism of protein secretion by the autotransporter pathway.Reconstitution of bacterial autotransporter assembly using purified components.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.Single-cell characterization of autotransporter-mediated Escherichia coli surface display of disulfide bond-containing proteins.Two-partner secretion of gram-negative bacteria: a single β-barrel protein enables transport across the outer membrane 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.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 Comparative analysis of the biochemical and functional properties of C-terminal domains of autotransporters Importance of conserved residues of the serine protease autotransporter beta-domain in passenger domain processing and beta-barrel assembly 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.Role of the alpha-helical linker of the C-terminal translocator in the biogenesis of the serine protease subfamily of autotransporters Pertactin beta-helix folding mechanism suggests common themes for the secretion and folding of autotransporter proteins.Surface display of proteins by gram-negative bacterial autotransporters.The autodisplay story, from discovery to biotechnical and biomedical applications.Subtypes of the plasmid-encoded serine protease EspP in Shiga toxin-producing Escherichia coli: distribution, secretion, and proteolytic activity Structure and function relationship of the autotransport and proteolytic activity of EspP from Shiga toxin-producing Escherichia coli Secretion of a bacterial virulence factor is driven by the folding of a C-terminal segment.A bioinformatic strategy for the detection, classification and analysis of bacterial autotransporters.Modified recombinant proteins can be exported via the Sec pathway in Escherichia coli.Autotransporter-based cell surface display in Gram-negative bacteria.BrkAutoDisplay: functional display of multiple exogenous proteins on the surface of Escherichia coli by using BrkA autotransporter.Structure, Function, and Assembly of Adhesive Organelles by Uropathogenic Bacteria Autotransporters: The Cellular Environment Reshapes a Folding Mechanism to Promote Protein Transport Identification, characterization, and molecular application of a virulence-associated autotransporter from a pathogenic Pseudomonas fluorescens strain Secretion by numbers: Protein traffic in prokaryotes.An autotransporter display platform for the development of multivalent recombinant bacterial vector vaccines.

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P2860

Efficient secretion of a folded protein domain by a monomeric bacterial autotransporter.

http://www.wikidata.org/entity/Q46785700

description

2005 nî lūn-bûn

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2005年の論文

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2005年学术文章

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2005年学术文章

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2005年学术文章

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2005年学术文章

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2005年学术文章

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2005年学术文章

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2005年學術文章

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2005年學術文章

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name

Efficient secretion of a folded protein domain by a monomeric bacterial autotransporter.

@en

Efficient secretion of a folded protein domain by a monomeric bacterial autotransporter.

@nl

type

label

Efficient secretion of a folded protein domain by a monomeric bacterial autotransporter.

@en

Efficient secretion of a folded protein domain by a monomeric bacterial autotransporter.

@nl

prefLabel

Efficient secretion of a folded protein domain by a monomeric bacterial autotransporter.

@en

Efficient secretion of a folded protein domain by a monomeric bacterial autotransporter.

@nl

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J.1365-2958.2005.04885.X

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Molecular Microbiology

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Efficient secretion of a folded protein domain by a monomeric bacterial autotransporter.

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Harris D Bernstein

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

Janine H Peterson

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Kristen M Skillman

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Rodolfo Ghirlando

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Travis J Barnard

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P2860

X-ray structure of a protein-conducting channel

Use of T7 RNA polymerase to direct expression of cloned genes

Size-Distribution Analysis of Macromolecules by Sedimentation Velocity Ultracentrifugation and Lamm Equation Modeling

Correlation of competence for export with lack of tertiary structure of the mature species: a study in vivo of maltose-binding protein in E. coli

The E. coli signal recognition particle is required for the insertion of a subset of inner membrane proteins

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

Blue native electrophoresis for isolation of membrane protein complexes in enzymatically active form

Arrangement of the translocator of the autotransporter adhesin involved in diffuse adherence on the bacterial surface

Structure of the translocator domain of a bacterial autotransporter

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

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protein folding