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Histochem Cell Biol. 2002 Feb;117(2):151-7. Epub 2002 Jan 19.

Formation, isomerisation and reduction of disulphide bonds during protein quality control in the endoplasmic reticulum.

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  • 1DiBiT-HSR and Universit√† Vita-Salute San Raffaele, Milan, Italy.


Efficient protein folding and quality control in the endoplasmic reticulum (ER) require that disulphide bonds are formed in nascent proteins, isomerised during assisted folding and reduced in terminally misfolded molecules. Recent findings in yeast and mammalian cells indicate that specific protein-protein interactions underlie redox control in the ER, allowing these competing reactions to occur simultaneously during protein quality control.

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