Protein N-glycosylation, protein folding, and protein quality control-Reference-Cited by-同舟云学术

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Protein N-glycosylation, protein folding, and protein quality control

Published:2010-11-26 Issue:6 Volume:30 Page:497-506
ISSN:1016-8478
Container-title:Molecules and Cells
language:en
Short-container-title:Mol Cells

Author:

Roth Jürgen,Zuber Christian,Park Sujin,Jang Insook,Lee Yangsin,Kysela Katarina Gaplovska,Fourn Valérie,Santimaria Roger,Guhl Bruno,Cho Jin Won

Publisher

Springer Science and Business Media LLC

Subject

Cell Biology,Molecular Biology,General Medicine

Link

http://link.springer.com/content/pdf/10.1007/s10059-010-0159-z.pdf

Reference111 articles.

1. Alanen, A., Pira, U., Lassila, O., Roth, J., and Franklin, R.M. (1985). Mott cells are plasma cells defective in immunoglobulin secretion. Eur. J. Immunol. 15, 235–242.

2. Avezov, E., Frenkel, Z., Ehrlich, M., Herscovics, A., and Lederkremer, G.Z. (2008). Endoplasmic reticulum (ER) mannosidase I is compartmentalized and required for N-glycan trimming to Man5-6GlcNAc2 in glycoprotein ER-associated degradation. Mol. Biol. Cell 19, 216–225.

3. Bannykh, S.I., Rowe, T., and Balch, W.E. (1996). The organization of endoplasmic reticulum export complexes. J. Cell Biol. 135, 19–35.

4. Bergeron, J.J.M., Brenner, M.B., Thomas, D.Y., and Williams, D.B. (1994). Calnexin — a membrane-bound chaperone of the endoplasmic reticulum. Trends Biochem. Sci. 19, 124–128.

5. Bernales, S., Papa, F.R., and Walter, P. (2006). Intracellular signaling by the unfolded protein response. Annu. Rev. Cell Dev. Biol. 22, 487–508.

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