Cargando…
Glucosidase Inhibition to Study Calnexin-assisted Glycoprotein Folding in Cells
Calnexin is a chaperone protein that plays a critical role in glycoprotein folding in the endoplasmic reticulum (ER). The function of calnexin depends on its binding to monoglucosylated oligosaccharides on nascent glycoproteins, whereas the generation of monoglucosylated oligosaccharides depends on...
Autores principales: | Wang, Hao, Wu, Qingyu |
---|---|
Formato: | Online Artículo Texto |
Lenguaje: | English |
Publicado: |
Bio-Protocol
2019
|
Materias: | |
Acceso en línea: | https://www.ncbi.nlm.nih.gov/pmc/articles/PMC6953735/ https://www.ncbi.nlm.nih.gov/pubmed/31930159 http://dx.doi.org/10.21769/BioProtoc.3248 |
Ejemplares similares
-
N-glycosylation in the protease domain of trypsin-like serine proteases mediates calnexin-assisted protein folding
por: Wang, Hao, et al.
Publicado: (2018) -
The Number and Location of Glycans on Influenza Hemagglutinin Determine Folding and Association with Calnexin and Calreticulin
por: Hebert, Daniel N., et al.
Publicado: (1997) -
Calnexin and BiP act as sequential molecular chaperones during thyroglobulin folding in the endoplasmic reticulum
Publicado: (1995) -
Folding of Insulin Receptor Monomers Is Facilitated by the Molecular Chaperones Calnexin and Calreticulin and Impaired by Rapid Dimerization
por: Bass, Joseph, et al.
Publicado: (1998) -
Interactions between Newly Synthesized Glycoproteins, Calnexin and a Network of Resident Chaperones in the Endoplasmic Reticulum
por: Tatu, Utpal, et al.
Publicado: (1997)