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American Society for Cell Biology, Molecular Biology of the Cell, 4(26), p. 594-604
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Identification of protein disulfide isomerase 1 as a key isomerase for disulfide bond formation in apolipoprotein B100
Journal article published in 2014 by
Shiyu Wang,
Shuin Park,
Vamsi K. Kodali 
,
Jaeseok Han,
Theresa Yip,
Zhouji Chen,
Nicholas O. Davidson,
Randal J. Kaufman
,
Jaeseok Han,
Theresa Yip,
Zhouji Chen,
Nicholas O. Davidson,
Randal J. Kaufman
This paper is made freely available by the publisher.
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Abstract
Pdi1 knockdown decreases apoB100 synthesis, reduces MTP activity and apoB100 lipidation, and impairs the oxidative folding of apoB100, which causes defective VLDL secretion. PDI1 promotes formation of disulfide bonds in apoB100 and serves as its disulfide isomerase.