Discover Community Create You

Loading publication...

Noodle always counts identifier-free feature events for service operation. With your permission, Google Analytics can also estimate audience and engagement. Search text, publication identifiers, cookies, IP addresses and browser fingerprints are never included in Noodle's first-party event counters.

Privacy details

Article

Identification of an Entamoeba histolytica gene encoding a protein disulfide isomerase that functionally complements the dsbA mutation in Escherichia coli.

Molecular and biochemical parasitology - 1 Oct 2005

Ramos Marco A, Sanchez-Lopez Rosana, Mares Rosa E, Olvera Felipe, Alagón Alejandro

Abstract excerpt

No abstract is available from the source.

Read the complete abstract on PubMed

Topics

Share this publication in a Topic to start or enrich a Post.

Share to Alkaline Phosphatase
Share to Cloning, Molecular
Share to DNA, Protozoan
Share to Entamoeba histolytica

Methodology Data sources Editorial policy Privacy Delete account & data About Contact Helena Bioinformatics

Share to Genes, Reporter

Share to Genetic Complementation Test

Share to Protein Disulfide-Isomerases

Share to Sequence Homology, Amino Acid

Source

Identifiers

PMID: 15990181
DOI: 10.1016/j.molbiopara.2005.04.013

Provenance

PubMed metadata and Literature Corpus relationships. Corpus snapshot updated 7 Sept 2026. Manifest publication-graph-cohort-2026-09-08.1.

Source receipt: pubmed, retrieved 7 Sept 2026.

Related research

Semantic proximity does not establish scientific evidence. Graph snapshot: 2026-09-29.

Research trail→

Click a neighbor to travelStep 1 · 12 closest

Identification of an Entamoeba histolytica gene encoding a protein disulfide isomerase that functionally complements the dsbA mutation in Escherichia coli.PMID 15990181Read ↗

The disulphide isomerase DsbC cooperates with the oxidase DsbA in a DsbD-independent manner.Semantic proximity Read ↗

Identification and characterization of a new disulfide isomerase-like protein (DsbD) in Escherichia coli.Semantic proximity Read ↗

Eukaryotic protein disulfide isomerase complements Escherichia coli dsbA mutants and increases the yield of a heterologous secreted protein with disulfide bonds.Semantic proximity Read ↗

An in vivo pathway for disulfide bond isomerization in Escherichia coli.Semantic proximity Read ↗

Oxidative folding and reductive activities of EhPDI, a protein disulfide isomerase from Entamoeba histolytica.Semantic proximity Read ↗

Cloning and expression of the gene for a protein disulfide oxidoreductase from Azotobacter vinelandii: complementation of an Escherichia coli dsbA mutant strain.Semantic proximity Read ↗

Nonconsecutive disulfide bond formation in an essential integral outer membrane protein.Semantic proximity Read ↗

Functional and bioinformatics analysis of two Campylobacter jejuni homologs of the thiol-disulfide oxidoreductase, DsbA.Semantic proximity Read ↗

Converting a Sulfenic Acid Reductase into a Disulfide Bond Isomerase.Semantic proximity Read ↗

The protein-disulfide isomerase DsbC cooperates with SurA and DsbA in the assembly of the essential β-barrel protein LptD.Semantic proximity Read ↗

Characterization of DsbC, a periplasmic protein of Erwinia chrysanthemi and Escherichia coli with disulfide isomerase activity.Semantic proximity Read ↗

Engineered pathways for correct disulfide bond oxidation.Semantic proximity Read ↗

⌁Select a neighboring publication to make it the new centre.