Cargando…
Posttranslational folding of vesicular stomatitis virus G protein in the ER: involvement of noncovalent and covalent complexes
In this study, we show that posttranslational folding of Vesicular Stomatitis virus G protein subunits can involve noncovalent, multimeric complexes as transient intermediates. The complexes are heterogeneous in size (4-21S20,W), contain several G glycopolypeptides, and are associated with BiP/GRP78...
Formato: | Texto |
---|---|
Lenguaje: | English |
Publicado: |
The Rockefeller University Press
1993
|
Materias: | |
Acceso en línea: | https://www.ncbi.nlm.nih.gov/pmc/articles/PMC2119544/ https://www.ncbi.nlm.nih.gov/pubmed/8381122 |
Ejemplares similares
-
Quality control in the endoplasmic reticulum: folding and misfolding of vesicular stomatitis virus G protein in cells and in vitro
Publicado: (1990) -
Differential effects of mutations in three domains on folding, quaternary structure, and intracellular transport of vesicular stomatitis virus G protein
Publicado: (1988) -
Newly synthesized G protein of vesicular stomatitis virus is not transported to the Golgi complex in mitotic cells
Publicado: (1985) -
Structure of the Vesicular Stomatitis Virus L Protein in Complex with Its Phosphoprotein Cofactor
por: Jenni, Simon, et al.
Publicado: (2020) -
Structure of the Vesicular Stomatitis Virus N(0)-P Complex
por: Leyrat, Cédric, et al.
Publicado: (2011)