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

The role of protein disulphide isomerase in the microsomal triacylglycerol transfer protein does not reside in its isomerase activity.

The Biochemical journal - 15 Apr 1996

Lamberg A, Jauhiainen M, Metso J, Ehnholm C, Shoulders C, Scott J, Pihlajaniemi T, Kivirikko K I

Abstract excerpt

The microsomal triacylglycerol transfer protein (MTP), an alpha beta dimer, is obligatory for the assembly of apoB-containing lipoproteins in liver and intestinal cells. The beta subunit is identical with protein disulphide isomerase, a 58 kDa endoplasmic reticulum luminal protein involved in ensuring correct disulphide bond formation of newly synthesized proteins. We report here the expression of the human MTP...

Read the complete abstract on PubMed

Topics

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

Share to Binding Sites
Share to Carrier Proteins

Methodology Data sources Editorial policy Privacy About Contact Helena Bioinformatics

Share to Glycoproteins

Share to In Vitro Techniques

Share to Mutation

Share to Protein Conformation

Share to Recombinant Proteins

Share to Triglycerides

Source

Open in PubMed Open full text

Identifiers

PMID: 8615825
DOI: 10.1042/bj3150533
PMCID: PMC1217228

Provenance

PubMed metadata and Literature Corpus relationships. Corpus snapshot updated 6 Sept 2026. Manifest publication-graph-cohort-2026-09-06.1.

Source receipt: pubmed, retrieved 6 Sept 2026.

Related research

Semantic proximity does not establish scientific evidence.

Research trail→

Click a neighbor to travelStep 1 · 8 closest

The role of protein disulphide isomerase in the microsomal triacylglycerol transfer protein does not reside in its isomerase activity.PMID 8615825Read ↗

Mutations that destabilize the a' domain of human protein-disulfide isomerase indirectly affect peptide binding.Semantic proximity Read ↗

A 30-amino acid truncation of the microsomal triglyceride transfer protein large subunit disrupts its interaction with protein disulfide-isomerase and causes abetalipoproteinemia.Semantic proximity Read ↗

A novel abetalipoproteinemia genotype. Identification of a missense mutation in the 97-kDa subunit of the microsomal triglyceride transfer protein that prevents complex formation with protein disulfide isomerase.Semantic proximity Read ↗

Investigation of the oligomeric status of the peroxisomal isoform of human 3-hydroxy-3-methylglutaryl-CoA lyase.Semantic proximity Read ↗

Removal of a consensus proline is not sufficient to allow tetratricopeptide repeat oligomerization.Semantic proximity Read ↗

Cyclophilin active site mutants have native prolyl isomerase activity with a protein substrate.Semantic proximity Read ↗

Protein aggregation in disease: a role for folding intermediates forming specific multimeric interactions.Semantic proximity Read ↗

General mitochondrial trifunctional protein (TFP) deficiency as a result of either alpha- or beta-subunit mutations exhibits similar phenotypes because mutations in either subunit alter TFP complex expression and subunit turnover.Semantic proximity Read ↗

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