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TY - JOUR AU - Braakman, Ineke AU - Helenius, Jonne AU - Helenius, Ari PY - 1992 DA - 1992/03/01 TI - Role of ATP and disulphide bonds during protein folding in the endoplasmic reticulum JO - Nature SP - 260 EP - 262 VL - 356 IS - 6366 AB - BEING topologically equivalent to the extracellular space, the lumen of the endoplasmic reticulum (ER) provides a unique folding environment for newly synthesized proteins. Unlike other compartments in the cell where folding occurs, the ER is oxidizing and therefore can promote the formation of disulphide bonds1. The reducing agent dithiothreitol, when added to living cells, inhibits disulphide formation with profound effects on folding2. Taking advantage of this effect, we demonstrate here that folding of influenza haemagglutinin is energy dependent. Metabolic energy is required to support the correct folding and disulphide bond formation in this well characterized viral glycoprotein, to rescue misfolded proteins from disulphide-linked aggregates, and to maintain the oxidized protein in its folded and oligomerization-competent state. SN - 1476-4687 UR - https://doi.org/10.1038/356260a0 DO - 10.1038/356260a0 ID - Braakman1992 ER -