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

Membrane protein topology of oleosin is constrained by its long hydrophobic domain.

The Journal of biological chemistry - 8 Mar 2002

Abell Ben M, High Stephen, Moloney Maurice M

Abstract excerpt

Oleosin proteins from Arabidopsis assume a unique endoplasmic reticulum (ER) topology with a membrane-integrated hydrophobic (H) domain of 72 residues, flanked by two cytosolic hydrophilic domains. We have investigated the targeting and topological determinants present within the oleosin polypeptide sequence using ER-derived canine pancreatic microsomes. Our data indicate that oleosins are integrated into...

Read the complete abstract on PubMed

Topics

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

Share to Cytosol
Share to Dogs
Share to Endoplasmic Reticulum

Methodology Data sources Editorial policy Privacy About Contact Helena Bioinformatics

Share to Microsomes

Share to Pancreas

Share to Protein Biosynthesis

Share to Protein Processing, Post-Translational

Share to Protein Transport

Source

Identifiers

PMID: 11673452
DOI: 10.1074/jbc.M103712200

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 · 12 closest

Membrane protein topology of oleosin is constrained by its long hydrophobic domain.PMID 11673452Read ↗

Role of the proline knot motif in oleosin endoplasmic reticulum topology and oil body targeting.Semantic proximity Read ↗

In vivo targeting of a sunflower oil body protein in yeast secretory (sec) mutants.Semantic proximity Read ↗

Targeting and translocation of proteins to the endoplasmic reticulum at a glanceSemantic proximity Read ↗

Identification and assessment of the role of a nominal phospholipid binding region of ORP1S (oxysterol-binding-protein-related protein 1 short) in the regulation of vesicular transport.Semantic proximity Read ↗

A new targeting motif for endoplasmic reticulum surface proteinsSemantic proximity Read ↗

Transmembrane topology of the protein palmitoyl transferase Akr1.Semantic proximity Read ↗

Links between lipid homeostasis, organelle morphodynamics and protein trafficking in eukaryotic and plant secretory pathways.Semantic proximity Read ↗

Sec62 protein mediates membrane insertion and orientation of moderately hydrophobic signal anchor proteins in the endoplasmic reticulum (ER).Semantic proximity Read ↗

Targeting to the endoplasmic reticulum by dilysine motifs: role of coat proteins.Semantic proximity Read ↗

Arresting a Torsin ATPase reshapes the endoplasmic reticulum.Semantic proximity Read ↗

Endoplasmic Reticulum (ER) Membrane Proteins (LUNAPARKs) are Required for Proper Configuration of the Cortical ER Network in Plant Cells.Semantic proximity Read ↗

Efficient mitochondrial targeting relies on co-operation of multiple protein signals in plants.Semantic proximity Read ↗

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