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protein folding in endoplasmic reticulum

Known as: oxidative protein folding, protein folding in ER 
A protein folding process that takes place in the endoplasmic reticulum (ER). Secreted, plasma membrane and organelle proteins are folded in the ER… Expand
National Institutes of Health

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Highly Cited
2014
Highly Cited
2014
AIMS Ero1 flavoproteins catalyze oxidative folding in the endoplasmic reticulum (ER), consuming oxygen and generating hydrogen… Expand
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Review
2014
Review
2014
SIGNIFICANCE The thioredoxin (Trx) superfamily proteins, including protein disulfide isomerases (PDI) and Dsb protein family, are… Expand
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2013
2013
The endoplasmic reticulum (ER) stress response (ERSR) and associated protein aggregation, is under investigation for its role in… Expand
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Highly Cited
2013
Highly Cited
2013
The mammalian endoplasmic reticulum (ER) harbors disulfide bond-generating enzymes, including Ero1α and peroxiredoxin 4 (Prx4… Expand
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Highly Cited
2009
Highly Cited
2009
MIA40 has a key role in oxidative protein folding in the mitochondrial intermembrane space. We present the solution structure of… Expand
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Highly Cited
2004
Highly Cited
2004
The flavoenzyme Ero1p produces disulfide bonds for oxidative protein folding in the endoplasmic reticulum. Disulfides generated… Expand
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Highly Cited
2004
Highly Cited
2004
In vitro, protein disulfide isomerase (Pdi1p) introduces disulfides into proteins (oxidase activity) and provides quality control… Expand
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Highly Cited
2002
Highly Cited
2002
The endoplasmic reticulum (ER) supports disulfide formation through an essential protein relay involving Ero1p and protein… Expand
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Highly Cited
1998
Highly Cited
1998
The structure of many proteins entering the secretory pathway is dependent on stabilization by disulfide bonds. To support… Expand
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Highly Cited
1993
Highly Cited
1993
Periplasmic protein disulfide isomerase (DsbA) is essential for disulfide formation in Escherichia coli. The tryptophan… Expand
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