Heavy chain binding protein recognizes incompletely disulfide-bonded forms of vesicular stomatitis virus G protein.
Open Access
- 1 April 1990
- journal article
- research article
- Published by Elsevier in Journal of Biological Chemistry
- Vol. 265 (12), 6879-6883
- https://doi.org/10.1016/s0021-9258(19)39231-2
Abstract
No abstract availableThis publication has 33 references indexed in Scilit:
- Protein folding in mitochondria requires complex formation with hsp60 and ATP hydrolysisNature, 1989
- The role of stress proteins in membrane biogenesisTrends in Biochemical Sciences, 1988
- Differential effects of mutations in three domains on folding, quaternary structure, and intracellular transport of vesicular stomatitis virus G protein.The Journal of cell biology, 1988
- A subfamily of stress proteins facilitates translocation of secretory and mitochondrial precursor polypeptidesNature, 1988
- 70K heat shock related proteins stimulate protein translocation into microsomesNature, 1988
- Effects of mutations in three domains of the vesicular stomatitis viral glycoprotein on its lateral diffusion in the plasma membrane [published erratum appers in J Cell Biol 1988 Jan;106(1):325]The Journal of cell biology, 1987
- Expression of wild-type and mutant forms of influenza hemagglutinin: The role of folding in intracellular transportCell, 1986
- Speculations on the functions of the major heat shock and glucose-regulated proteinsCell, 1986
- Posttranslational association of immunoglobulin heavy chain binding protein with nascent heavy chains in nonsecreting and secreting hybridomas.The Journal of cell biology, 1986
- Structural requirements of a membrane-spanning domain for protein anchoring and cell surface transportCell, 1985