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Glucose on the sugar side chains of proteins keeps unfolded proteins in the ER. Mannoses on sugar side chains act as a timer for protein folding. Unfolded proteins in the ER are threaded through a retrotranslocon into the cytosol where they are ubiquitylated and digested. IRE1, ATF6 and PERK sense the amount of unfolded protein and generates several responses to reduce the effects and amount of unfolded protein.
There are various concepts that attempt to explain how exactly a protein undergoes folding and organisation from the unfolded or random coil state to the native folded state but the most promising is that the secondary structure forms before most proteins are able to compact extensively(2).