Disulfide bond formation and secretion of Escherichia coli heat-stable enterotoxin II. - Wikidata - wikimedia - TriplyDB

Disulfide bond formation and secretion of Escherichia coli heat-stable enterotoxin II.

Disulfide bond formation and secretion of Escherichia coli heat-stable enterotoxin II.

http://www.wikidata.org/entity/Q39837913

about

Staphylococcus aureus DsbA does not have a destabilizing disulfide. A new paradigm for bacterial oxidative folding The Salmonella SPI1 type three secretion system responds to periplasmic disulfide bond status via the flagellar apparatus and the RcsCDB system Characterization of SrgA, a Salmonella enterica serovar Typhimurium virulence plasmid-encoded paralogue of the disulfide oxidoreductase DsbA, essential for biogenesis of plasmid-encoded fimbriae.STb and AIDA-I: the missing link?Protein folding in the bacterial periplasm The disulfide bond in the Aeromonas hydrophila lipase/acyltransferase stabilizes the structure but is not required for secretion or activity.Key players involved in bacterial disulfide-bond formation.Transcriptional regulation of the assT-dsbL-dsbI gene cluster in Salmonella enterica serovar Typhi IMSS-1 depends on LeuO, H-NS, and specific growth conditions.Envelope stress responses and Gram-negative bacterial pathogenesis.Potential role of thiol:disulfide oxidoreductases in the pathogenesis of Helicobacter pylori.Animal Enterotoxigenic Escherichia coli.Toxins from bacteria.Pathogenesis of adherent-invasive Escherichia coli.Disulfide bond in Pseudomonas aeruginosa lipase stabilizes the structure but is not required for interaction with its foldase.Carboxy-terminal region involved in activity of Escherichia coli TolC Extracellular secretion of Escherichia coli heat-stable enterotoxin I across the outer membrane.Effect of Escherichia coli STb toxin on NIH-3T3 cells.The identification of exported proteins with gene fusions to invasin.MacAB is involved in the secretion of Escherichia coli heat-stable enterotoxin II.The Escherichia coli enterotoxin STb permeabilizes piglet jejunal brush border membrane vesicles.LC-MS analysis of pig intestine sulfatides: interaction with Escherichia coli STb enterotoxin and characterization of molecular species present.Two periplasmic disulfide oxidoreductases, DsbA and SrgA, target outer membrane protein SpiA, a component of the Salmonella pathogenicity island 2 type III secretion system.Isolation and characterization of a chromosomally encoded disulphide oxidoreductase from Salmonella enterica serovar Typhimurium.

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P2860

Disulfide bond formation and secretion of Escherichia coli heat-stable enterotoxin II.

http://www.wikidata.org/entity/Q39837913

description

1995 nî lūn-bûn

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1995年の論文

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1995年学术文章

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1995年学术文章

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1995年学术文章

@zh-hans

1995年学术文章

@zh-my

1995年学术文章

@zh-sg

1995年學術文章

@yue

1995年學術文章

@zh

1995年學術文章

@zh-hant

name

Disulfide bond formation and secretion of Escherichia coli heat-stable enterotoxin II.

@en

Disulfide bond formation and secretion of Escherichia coli heat-stable enterotoxin II.

@nl

type

label

Disulfide bond formation and secretion of Escherichia coli heat-stable enterotoxin II.

@en

Disulfide bond formation and secretion of Escherichia coli heat-stable enterotoxin II.

@nl

prefLabel

Disulfide bond formation and secretion of Escherichia coli heat-stable enterotoxin II.

@en

Disulfide bond formation and secretion of Escherichia coli heat-stable enterotoxin II.

@nl

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P356

JB.177.16.4579-4586.1995

P1433

Journal of Bacteriology

P1476

Disulfide bond formation and secretion of Escherichia coli heat-stable enterotoxin II.

@en

P2093

Akashi N

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Baba T

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Fujii Y

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Okamoto K

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Yamanaka H

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P2860

A pathway for disulfide bond formation in vivo

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

Crystal structure of the DsbA protein required for disulphide bond formation in vivo

Vectors for selective expression of cloned DNAs by T7 RNA polymerase

Characterization of a periplasmic thiol:disulfide interchange protein required for the functional maturation of secreted virulence factors of Vibrio cholerae

In vitro catalysis of oxidative folding of disulfide-bonded proteins by the Escherichia coli dsbA (ppfA) gene product.

Polymyxin B-Induced Release of Low-Molecular-Weight, Heat-Labile Enterotoxin from Escherichia coli.

Mutants in disulfide bond formation that disrupt flagellar assembly in Escherichia coli.

Secretion of methanol-insoluble heat-stable enterotoxin (STB): energy- and secA-dependent conversion of pre-STB to an intermediate indistinguishable from the extracellular toxin.

Assay for enterotoxigenic Escherichia coli heat-stable toxin b in rats and mice.

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4579-4586

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scholarly article

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10.1128/JB.177.16.4579-4586.1995

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16

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177

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1995-08-01T00:00:00Z

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Escherichia coli

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177220

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