Add to ORKGAn important function in protein folding is the formation of disulfide bonds. In different compartments of bacteria specific oxido reductases are responsible for this function. Thanks to the identification of all genes from various model organisms the understanding of the function of the various members of this family has increased dramatically. Zie: Summar
Protein disulfide bond formation is a rate limiting step in protein folding and is catalyzed by enzy...
Disulfide bonds are important for the correct folding, structural integrity, and activity of many bi...
Ten years ago it was thought that disulphide bond formation in prokaryotes occurred spontaneously. N...
An important function in protein folding is the formation of disulfide bonds. In different compartme...
The in vivo formation of disulfide bonds, which is critical for the stability and/or activity of man...
Disulfide bonds in proteins are found between cysteine residues and are usually important for either...
Disulfide bonds are required for the stability and function of many proteins. A large number of thio...
Bacillus subtilis is a well-established cellular factory for proteins and fine chemicals. In particu...
The Bacillus subtilis YkuV responds to environmental oxidative stress and plays an important role fo...
AbstractThiol–disulfide oxidoreductase systems of bacterial cytoplasm and eukaryotic cytosol favor r...
The formation of disulfide bonds between cysteine residues is a rate limiting step in protein foldin...
Disulfide bonds are important for the correct folding, structural integrity, and activity of many bi...
Disulfide bonds are an important post-translational modification that provides stability for many pr...
The formation of a disulfide bond results from the oxidation of two cysteine thiol groups, with the ...
Abstract Bacillus subtilis is a well-established cellular factory for proteins and fine chemicals. I...
Protein disulfide bond formation is a rate limiting step in protein folding and is catalyzed by enzy...
Disulfide bonds are important for the correct folding, structural integrity, and activity of many bi...
Ten years ago it was thought that disulphide bond formation in prokaryotes occurred spontaneously. N...
An important function in protein folding is the formation of disulfide bonds. In different compartme...
The in vivo formation of disulfide bonds, which is critical for the stability and/or activity of man...
Disulfide bonds in proteins are found between cysteine residues and are usually important for either...
Disulfide bonds are required for the stability and function of many proteins. A large number of thio...
Bacillus subtilis is a well-established cellular factory for proteins and fine chemicals. In particu...
The Bacillus subtilis YkuV responds to environmental oxidative stress and plays an important role fo...
AbstractThiol–disulfide oxidoreductase systems of bacterial cytoplasm and eukaryotic cytosol favor r...
The formation of disulfide bonds between cysteine residues is a rate limiting step in protein foldin...
Disulfide bonds are important for the correct folding, structural integrity, and activity of many bi...
Disulfide bonds are an important post-translational modification that provides stability for many pr...
The formation of a disulfide bond results from the oxidation of two cysteine thiol groups, with the ...
Abstract Bacillus subtilis is a well-established cellular factory for proteins and fine chemicals. I...
Protein disulfide bond formation is a rate limiting step in protein folding and is catalyzed by enzy...
Disulfide bonds are important for the correct folding, structural integrity, and activity of many bi...
Ten years ago it was thought that disulphide bond formation in prokaryotes occurred spontaneously. N...