The ER-quality control. Upon translocation to the ER the N-glycan is ligated to the nascent chain. Then two glucosidases I and II remove glucose group. The mono-glucosylated glycoprotein then interacts with calnexin/calreticulin. These chaperones recruit the oxireductase ERp57. Cleavage of the last glucose residue by glucosidase II leads to the release of chaperones. At this stage if the protein is properly folded it will exit the ER. The incorrectly folded protein is the substrate of UDP/glucose:glycoprotein glucosyltransferase, which puts glucose back to the misfolded protein. If the protein fails to fold properly even after several cycles, the manose residue is removed by the mannosidase I. This modified glycan is recognized by the (ER degradation enhancing mannosidase-like protein) (EDEM). This targets the misfolded protein for ER-associated degradation (ERAD). The factors missing in trypanosomes but exist in other eukaryotes are crossed.