Membrane Protein Topology of Oleosin Is Constrained by Its Long Hydrophobic Domain
Open Access
- 1 March 2002
- journal article
- Published by Elsevier in Journal of Biological Chemistry
- Vol. 277 (10) , 8602-8610
- https://doi.org/10.1074/jbc.m103712200
Abstract
No abstract availableKeywords
This publication has 38 references indexed in Scilit:
- Distant Downstream Sequence Determinants Can Control N-tail Translocation during Protein Insertion into the Endoplasmic Reticulum MembranePublished by Elsevier ,2000
- The Translocon: A Dynamic Gateway at the ER MembraneAnnual Review of Cell and Developmental Biology, 1999
- Transmembrane Protein Insertion Orientation in Yeast Depends on the Charge Difference across Transmembrane Segments, Their Total Hydrophobicity, and Its DistributionJournal of Biological Chemistry, 1998
- Membrane Protein Biogenesis: Regulated Complexity at the Endoplasmic ReticulumCell, 1997
- Anionic phospholipids are determinants of membrane protein topologyThe EMBO Journal, 1997
- Multiple Determinants Direct the Orientation of Signal–Anchor Proteins: The Topogenic Role of the Hydrophobic Signal DomainThe Journal of cell biology, 1997
- The Role of Charged Residues in Determining Transmembrane Protein Insertion Orientation in YeastJournal of Biological Chemistry, 1996
- Control of topology and mode of assembly of a polytopic membrane protein by positively charged residuesNature, 1989
- Predicting the orientation of eukaryotic membrane-spanning proteins.Proceedings of the National Academy of Sciences, 1989
- Multiple Mechanisms of Protein Insertion into and Across MembranesScience, 1985