Size and conformation limits to secretion of disulfide-bonded loops in autotransporter proteins. - Wikidata - awgldk - TriplyDB

Size and conformation limits to secretion of disulfide-bonded loops in autotransporter proteins.

Size and conformation limits to secretion of disulfide-bonded loops in autotransporter proteins.

http://www.wikidata.org/entity/Q39711041

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The translocation domain in trimeric autotransporter adhesins is necessary and sufficient for trimerization and autotransportation 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.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.The inverse autotransporter intimin exports its passenger domain via a hairpin intermediate.A mortise-tenon joint in the transmembrane domain modulates autotransporter assembly into bacterial outer membranes.Mutational and topological analysis of the Escherichia coli BamA protein.Charge-dependent secretion of an intrinsically disordered protein via the autotransporter pathway.Single-cell characterization of autotransporter-mediated Escherichia coli surface display of disulfide bond-containing proteins.Dynamic association of BAM complex modules includes surface exposure of the lipoprotein BamC.A bioinformatic strategy for the detection, classification and analysis of bacterial autotransporters.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.Reconstitution of a nanomachine driving the assembly of proteins into bacterial outer membranes.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.Bacterial whole-cell biocatalysts by surface display of enzymes: toward industrial application.EHEC Adhesins The β-Barrel Assembly Machinery Complex.Antigen localisation influences the magnitude and kinetics of the endogenous adaptive immune response to recombinant Salmonella vaccines.Improved cell surface display of Salmonella enterica serovar Enteritidis antigens in Escherichia coli.Increased severity of respiratory infections associated with elevated anti-LPS IgG2 which inhibits serum bactericidal killing.A structurally informed autotransporter platform for efficient heterologous protein secretion and display.Probing the applicability of autotransporter based surface display with the EstA autotransporter of Pseudomonas stutzeri A15.A generalised module for the selective extracellular accumulation of recombinant proteins ATP-independent control of autotransporter virulence protein transport via the folding properties of the secreted protein.Discovery of a novel periplasmic protein that forms a complex with a trimeric autotransporter adhesin and peptidoglycan.Fusion with the cold-active esterase facilitates autotransporter-based surface display of the 10th human fibronectin domain in Escherichia coli.Job contenders: roles of the β-barrel assembly machinery and the translocation and assembly module in autotransporter secretion.Comparing autotransporter β-domain configurations for their capacity to secrete heterologous proteins to the cell surface.Molecular basis for the folding of β-helical autotransporter passenger domains.Identification of BamC on the Surface of E. coli.N for AsN - O for StrOcture? A strand-loop-strand motif for prokaryotic O-glycosylation

P2860

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P2860

Size and conformation limits to secretion of disulfide-bonded loops in autotransporter proteins.

http://www.wikidata.org/entity/Q39711041

description

2011 nî lūn-bûn

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2011年の論文

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2011年論文

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name

Size and conformation limits t ...... s in autotransporter proteins.

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Size and conformation limits t ...... s in autotransporter proteins.

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type

label

Size and conformation limits t ...... s in autotransporter proteins.

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Size and conformation limits t ...... s in autotransporter proteins.

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Size and conformation limits t ...... s in autotransporter proteins.

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Size and conformation limits t ...... s in autotransporter proteins.

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Journal of Biological Chemistry

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Size and conformation limits t ...... ps in autotransporter proteins

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P2093

Adam F Cunningham

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

Amanda E Rossiter

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Douglas F Browning

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Rebecca E Fitzpatrick

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Yanina R Sevastsyanovich

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P2860

Construction of Escherichia coli K-12 in-frame, single-gene knockout mutants: the Keio collection

Crystal structure of the FimD usher bound to its cognate FimC-FimH substrate

Crystal structure of the Helicobacter pylori vacuolating toxin p55 domain

Autotransporter structure reveals intra-barrel cleavage followed by conformational changes

Insight into disulfide bond catalysis in Chlamydia from the structure and function of DsbH, a novel oxidoreductase

Active-Site Gating Regulates Substrate Selectivity in a Chymotrypsin-Like Serine Protease

Crystal structure of a full-length autotransporter

Autotransporter passenger domain secretion requires a hydrophobic cavity at the extracellular entrance of the β-domain pore

Structure of Bordetella pertussis virulence factor P.69 pertactin

One-step inactivation of chromosomal genes in Escherichia coli K-12 using PCR products

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286

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Timothy J Wells

Denisse L Leyton

Michael Overduin

Ian R Henderson

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2011-10-17T00:00:00Z

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51721340

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