AbstractNative disulphide-bond formation during protein folding in the endoplasmic reticulum requires oxidative machinery, the components and mechanism of which are not yet fully understood. Two recent papers have identified a novel protein component that appears to play a key role in this important redox pathway
: The molecular networks that control endoplasmic reticulum (ER) redox conditions in mammalian cells...
Many proteins of the secretory pathway contain disulfide bonds that are essential for structure and ...
Oxidizing conditions must be maintained in the endoplasmic reticulum (ER) to allow the formation of ...
Native disulphide-bond formation duping protein folding in the endoplasmic reticulum requires oxidat...
AbstractNative disulphide-bond formation during protein folding in the endoplasmic reticulum require...
AbstractOxidative protein folding in the luminal compartment of the endoplasmic reticulum is thought...
The reversal of thiol oxidation in proteins within the endoplasmic reticulum (ER) is crucial for pro...
The efficient folding, assembly and secretion of proteins from mammalian cells is a critically impor...
Protein folding homeostasis in the endoplasmic reticulum (ER) requires efficient protein thiol oxida...
The endoplasmic reticulum (ER) provides an environment that is highly optimized for oxidative protei...
The efficient folding, assembly and secretion of proteins from mammalian cells is a critically impor...
Thesis (Ph.D.)--Massachusetts Institute of Technology, Dept. of Biology, 1999.Includes bibliographic...
The relationship between protein synthesis, folding and disulfide formation within the endoplasmic r...
Disulfide bond formation in proteins is an effective tool of both structure stabilization and redox ...
In eukaryotic cells, protein disulfide bond formation occurs in the lumen of the ER as part of the f...
: The molecular networks that control endoplasmic reticulum (ER) redox conditions in mammalian cells...
Many proteins of the secretory pathway contain disulfide bonds that are essential for structure and ...
Oxidizing conditions must be maintained in the endoplasmic reticulum (ER) to allow the formation of ...
Native disulphide-bond formation duping protein folding in the endoplasmic reticulum requires oxidat...
AbstractNative disulphide-bond formation during protein folding in the endoplasmic reticulum require...
AbstractOxidative protein folding in the luminal compartment of the endoplasmic reticulum is thought...
The reversal of thiol oxidation in proteins within the endoplasmic reticulum (ER) is crucial for pro...
The efficient folding, assembly and secretion of proteins from mammalian cells is a critically impor...
Protein folding homeostasis in the endoplasmic reticulum (ER) requires efficient protein thiol oxida...
The endoplasmic reticulum (ER) provides an environment that is highly optimized for oxidative protei...
The efficient folding, assembly and secretion of proteins from mammalian cells is a critically impor...
Thesis (Ph.D.)--Massachusetts Institute of Technology, Dept. of Biology, 1999.Includes bibliographic...
The relationship between protein synthesis, folding and disulfide formation within the endoplasmic r...
Disulfide bond formation in proteins is an effective tool of both structure stabilization and redox ...
In eukaryotic cells, protein disulfide bond formation occurs in the lumen of the ER as part of the f...
: The molecular networks that control endoplasmic reticulum (ER) redox conditions in mammalian cells...
Many proteins of the secretory pathway contain disulfide bonds that are essential for structure and ...
Oxidizing conditions must be maintained in the endoplasmic reticulum (ER) to allow the formation of ...
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