Binding of Secretory Precursor Polypeptides to a Translocon Subcomplex Is Regulated by BiP
- 1 January 1997
- Vol. 88 (1) , 85-96
- https://doi.org/10.1016/s0092-8674(00)81861-9
Abstract
No abstract availableKeywords
This publication has 47 references indexed in Scilit:
- Post-translational protein translocation: not all hsc70s are created equalTrends in Biochemical Sciences, 1996
- BiP and Sec63p are required for both co- and posttranslational protein translocation into the yeast endoplasmic reticulum.Proceedings of the National Academy of Sciences, 1995
- Secretory proteins move through the endoplasmic reticulum membrane via an aqueous, gated poreCell, 1994
- DnaJ-like proteins: molecular chaperones and specific regulators of Hsp70Trends in Biochemical Sciences, 1994
- A Sec63p-BiP complex from yeast is required for protein translocation in a reconstituted proteoliposome.The Journal of cell biology, 1993
- Eukaryotic homologues of Escherichia coli dnaJ: a diverse protein family that functions with hsp70 stress proteins.Molecular Biology of the Cell, 1993
- Reconstitution of protein translocation from solubilized yeast membranes reveals topologically distinct roles for BiP and cytosolic Hsc70.The Journal of cell biology, 1993
- Mutations in the signal sequence of prepro-alpha-factor inhibit both translocation into the endoplasmic reticulum and processing by signal peptidase in yeast cells.Molecular and Cellular Biology, 1989
- Single-amino-acid substitutions within the signal sequence of yeast prepro-alpha-factor affect membrane translocation.Molecular and Cellular Biology, 1988
- Translocation in yeast and mammalian cells: not all signal sequences are functionally equivalent.The Journal of cell biology, 1987