| Year | 1997 | Journal | Trends Cell Biol |
| Volume | 7 | Issue | 5 |
| Pages | 193-200 | PubMed ID | 17708944 |
| Mgi Jnum | J:39858 | Mgi Id | MGI:87207 |
| Doi | 10.1016/S0962-8924(97)01032-5 | Citation | (1997) Calnexin, calreticulin and the folding of glycoproteins. Trends Cell Biol 7(5):193-200 |
| abstractText | Calnexin and calreticulin are molecular chaperones in the endoplasmic reticulum (ERJ. They are lectins that interact with newly synthesized glycoproteins that have undergone partial trimming of their core N-linked oligosaccharides. Together with the enzymes responsible for glucose removal and a glucosyltransferase that re-glucosylates already-trimmed glycoproteins, they provide a novel mechanism for promoting folding, oligomeric assembly and quality control in the ER. |
