Maturation pathway of Escherichia coli heat-stable enterotoxin I: requirement of DsbA for disulfide bond formation. - Wikidata - wikimedia - TriplyDB

Maturation pathway of Escherichia coli heat-stable enterotoxin I: requirement of DsbA for disulfide bond formation.

Maturation pathway of Escherichia coli heat-stable enterotoxin I: requirement of DsbA for disulfide bond formation.

http://www.wikidata.org/entity/Q39931909

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Diarrheagenic Escherichia coli Structure and Functional Properties of Bacillus subtilis Endospore Biogenesis Factor StoA Crystal Structure and Biophysical Properties of Bacillus subtilis BdbD: AN OXIDIZING THIOL:DISULFIDE OXIDOREDUCTASE CONTAINING A NOVEL METAL SITE Molecular architecture of Streptococcus pneumoniae surface thioredoxin-fold lipoproteins crucial for extracellular oxidative stress resistance and maintenance of virulence Enteric bacterial toxins: mechanisms of action and linkage to intestinal secretion.Full capacity of recombinant Escherichia coli heat-stable enterotoxin fusion proteins for extracellular secretion, antigenicity, disulfide bond formation, and activity.Disulfide oxidoreductase activity of Shigella flexneri is required for release of Ipa proteins and invasion of epithelial cells.Prosequence switching: an effective strategy to produce biologically active E. coli heat-stable enterotoxin STh.Protein folding in the bacterial periplasm 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.Potential role of thiol:disulfide oxidoreductases in the pathogenesis of Helicobacter pylori.Animal Enterotoxigenic Escherichia coli.Heat-stable enterotoxin of enterotoxigenic Escherichia coli as a vaccine target Cure and curse: E. coli heat-stable enterotoxin and its receptor guanylyl cyclase C Virulence regulons of enterotoxigenic Escherichia coli.Carboxy-terminal region involved in activity of Escherichia coli TolC DsbA of Pseudomonas aeruginosa is essential for multiple virulence factors Amino acid residues in the pro region of Escherichia coli heat-stable enterotoxin I that affect efficiency of translocation across the inner membrane.Disulfide bond formation and secretion of Escherichia coli heat-stable enterotoxin II.Extracellular secretion of Escherichia coli heat-stable enterotoxin I across the outer membrane.The identification of exported proteins with gene fusions to invasin.Characterization of a highly toxic, large molecular size heat-stable enterotoxin produced by a clinical isolate of Yersinia enterocolitica.MacAB is involved in the secretion of Escherichia coli heat-stable enterotoxin II.Functional analysis of paralogous thiol-disulfide oxidoreductases in Streptococcus gordonii.Two periplasmic disulfide oxidoreductases, DsbA and SrgA, target outer membrane protein SpiA, a component of the Salmonella pathogenicity island 2 type III secretion system.

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P2860

Maturation pathway of Escherichia coli heat-stable enterotoxin I: requirement of DsbA for disulfide bond formation.

http://www.wikidata.org/entity/Q39931909

description

1994 nî lūn-bûn

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1994年の論文

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1994年論文

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1994年論文

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1994年論文

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1994年論文

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1994年論文

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1994年论文

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1994年论文

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1994年论文

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name

Maturation pathway of Escheric ...... for disulfide bond formation.

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Maturation pathway of Escheric ...... for disulfide bond formation.

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type

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Maturation pathway of Escheric ...... for disulfide bond formation.

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Maturation pathway of Escheric ...... for disulfide bond formation.

@nl

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Maturation pathway of Escheric ...... for disulfide bond formation.

@en

Maturation pathway of Escheric ...... for disulfide bond formation.

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JB.176.10.2906-2913.1994

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Journal of Bacteriology

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Maturation pathway of Escheric ...... for disulfide bond formation.

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Baba T

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Fujii Y

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Kameyama M

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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

Molecular structure of the toxin domain of heat-stable enterotoxin produced by a pathogenic strain of Escherichia coli. A putative binding site for a binding protein on rat intestinal epithelial cell membranes

Reduction of the secretory response to Escherichia coli heat-stable enterotoxin by thiol and disulfide compounds.

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

Construction of versatile expression cloning vehicles using the lipoprotein gene of Escherichia coli.

Identification and characterization of an Escherichia coli gene required for the formation of correctly folded alkaline phosphatase, a periplasmic enzyme.

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

The reactive and destabilizing disulfide bond of DsbA, a protein required for protein disulfide bond formation in vivo.

Rectification of two Escherichia coli heat-stable enterotoxin allele sequences and lack of biological effect of changing the carboxy-terminal tyrosine to histidine.

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2906-2913

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scholarly article

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10.1128/JB.176.10.2906-2913.1994

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10

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176

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1994-05-01T00:00:00Z

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8188592

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Escherichia coli

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205446

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