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
Most proteins destined for the extracellular space require disulfide bonds for folding and stability...
Most proteins destined for the extracellular space require disulfide bonds for folding and stability...
Disulfide bonds are required for the stability and function of many proteins. A large number of thio...
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...
Disulfide bond formation in proteins is an effective tool of both structure stabilization and redox ...
The efficient folding, assembly and secretion of proteins from mammalian cells is a critically impor...
The efficient folding, assembly and secretion of proteins from mammalian cells is a critically impor...
The endoplasmic reticulum (ER) provides an environment that is highly optimized for oxidative protei...
The past year has provided more detail on the formation of native disulphide bonds during protein fo...
Native disulphide bonds are essential for the structure and function of many membrane and secretory ...
AbstractLiving cells must be able to respond to physiological and environmental fluctuations that th...
The identification of protein disulfide isomerase (PDI), almost 50 years ago, opened the way to the ...
Protein disulfide bonds are an important co- and post-translational modification for proteins enteri...
The relationship between protein synthesis, folding and disulfide formation within the endoplasmic r...
Most proteins destined for the extracellular space require disulfide bonds for folding and stability...
Most proteins destined for the extracellular space require disulfide bonds for folding and stability...
Disulfide bonds are required for the stability and function of many proteins. A large number of thio...
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...
Disulfide bond formation in proteins is an effective tool of both structure stabilization and redox ...
The efficient folding, assembly and secretion of proteins from mammalian cells is a critically impor...
The efficient folding, assembly and secretion of proteins from mammalian cells is a critically impor...
The endoplasmic reticulum (ER) provides an environment that is highly optimized for oxidative protei...
The past year has provided more detail on the formation of native disulphide bonds during protein fo...
Native disulphide bonds are essential for the structure and function of many membrane and secretory ...
AbstractLiving cells must be able to respond to physiological and environmental fluctuations that th...
The identification of protein disulfide isomerase (PDI), almost 50 years ago, opened the way to the ...
Protein disulfide bonds are an important co- and post-translational modification for proteins enteri...
The relationship between protein synthesis, folding and disulfide formation within the endoplasmic r...
Most proteins destined for the extracellular space require disulfide bonds for folding and stability...
Most proteins destined for the extracellular space require disulfide bonds for folding and stability...
Disulfide bonds are required for the stability and function of many proteins. A large number of thio...
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