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doi: 10.1046/j.1523-1755.1999.00624.x

[DOI] [PubMed] [Google Scholar] 6.Martnez-Chantar M.L., Vzquez-Chantada M., Ariz U., Martnez N., Varela M., Luka Z., Capdevila A., Rodrguez J., Aransay A.M., Matthiesen R., et al

Abstract It has long been assumed that the oxidized form of glutathione, the tripeptide glutamatecysteineglycine, is a source of oxidizing equivalents needed for the formation of disulphide bonds in proteins within the endoplasmic reticulum (ER), although the in vivo function of glutathione in the ER has never been studied directly

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