Membrane Topology of the 12- and the 25-kDa Subunits of the Mammalian Signal Peptidase Complex
Open Access
- 1 February 1996
- journal article
- research article
- Published by Elsevier in Journal of Biological Chemistry
- Vol. 271 (7) , 3925-3929
- https://doi.org/10.1074/jbc.271.7.3925
Abstract
No abstract availableKeywords
This publication has 32 references indexed in Scilit:
- Sec72p contributes to the selective recognition of signal peptides by the secretory polypeptide translocation complex.The Journal of cell biology, 1994
- Protein translocation into proteoliposomes reconstituted from purified components of the endoplasmic reticulum membraneCell, 1993
- Signal peptidases in prokaryotes and eukaryotes - a new protease familyTrends in Biochemical Sciences, 1992
- The signal sequence receptor has a second subunit and is part of a translocation complex in the endoplasmic reticulum as probed by bifunctional reagents.The Journal of cell biology, 1990
- Purification of microsomal signal peptidase as a complex.Proceedings of the National Academy of Sciences, 1986
- Mammalian Signal Peptidase: Partial Purification and General Characterization of the Signal Peptidase from Microsomal Membranes of Porcine Pancreas1The Journal of Biochemistry, 1984
- Analysis of membrane and surface protein sequences with the hydrophobic moment plotJournal of Molecular Biology, 1984
- Protein translocation across the endoplasmic reticulum. II. Isolation and characterization of the signal recognition particle receptor.The Journal of cell biology, 1982
- Transfer of proteins across membranes. II. Reconstitution of functional rough microsomes from heterologous components.The Journal of cell biology, 1975
- Transfer of proteins across membranes. I. Presence of proteolytically processed and unprocessed nascent immunoglobulin light chains on membrane-bound ribosomes of murine myeloma.The Journal of cell biology, 1975