Bioactive peptides play important roles in metabolic regulation and modulation and many are used as therapeutics. These peptides often possess disulfide bonds, which are important for their structure, function and stability. A systematic network of enzymes--a disulfide bond generating enzyme, a disulfide bond donor enzyme and a redox cofactor--that function inside the cell dictates the formation and maintenance of disulfide bonds. The main pathways that catalyze disulfide bond formation in peptides and proteins in prokaryotes and eukaryotes are remarkably similar and share several mechanistic features. This review summarizes the formation of disulfide bonds in peptides and proteins by cellular and recombinant machinery
Abstract Bacteria are simple and cost effective hosts for producing recombinant proteins. However, t...
The major function of disulfide bonds is not only the stabilization of protein structures. Over the ...
A repeating theme in the structural biology of disulfide oxidants and isomerases is the extraordinar...
The native structures of proteins and peptides are stabilized by a number of interactions that dicta...
Protein disulfide bonds are an important co- and post-translational modification for proteins enteri...
AbstractProtein disulfide bonds are an important co- and post-translational modification for protein...
The identification of protein disulfide isomerase (PDI), almost 50 years ago, opened the way to the ...
The prevailing view is that disulfide bonds have been added during evolution to enhance the stabilit...
Abstract About one-third of mammalian proteins are secreted proteins and membrane proteins. Most of ...
Disulfide-containing proteins are ideal models for studies of protein folding as the folding interme...
ABSTRACT: The protein DsbA facilitates disulfide bond formation in the periplasm of Escherichia coli...
Protein disulfide bonds link cysteine residues in the polypeptide chain. The bonds contribute, somet...
AbstractDisulfide bonds are covalent bonds formed post-translationally by the oxidation of a pair of...
Disulfide bonds are unique among post-translational modifications, as they add covalent crosslinks t...
Cellular compartments differ dramatically in their redox potentials. This translates directly into v...
Abstract Bacteria are simple and cost effective hosts for producing recombinant proteins. However, t...
The major function of disulfide bonds is not only the stabilization of protein structures. Over the ...
A repeating theme in the structural biology of disulfide oxidants and isomerases is the extraordinar...
The native structures of proteins and peptides are stabilized by a number of interactions that dicta...
Protein disulfide bonds are an important co- and post-translational modification for proteins enteri...
AbstractProtein disulfide bonds are an important co- and post-translational modification for protein...
The identification of protein disulfide isomerase (PDI), almost 50 years ago, opened the way to the ...
The prevailing view is that disulfide bonds have been added during evolution to enhance the stabilit...
Abstract About one-third of mammalian proteins are secreted proteins and membrane proteins. Most of ...
Disulfide-containing proteins are ideal models for studies of protein folding as the folding interme...
ABSTRACT: The protein DsbA facilitates disulfide bond formation in the periplasm of Escherichia coli...
Protein disulfide bonds link cysteine residues in the polypeptide chain. The bonds contribute, somet...
AbstractDisulfide bonds are covalent bonds formed post-translationally by the oxidation of a pair of...
Disulfide bonds are unique among post-translational modifications, as they add covalent crosslinks t...
Cellular compartments differ dramatically in their redox potentials. This translates directly into v...
Abstract Bacteria are simple and cost effective hosts for producing recombinant proteins. However, t...
The major function of disulfide bonds is not only the stabilization of protein structures. Over the ...
A repeating theme in the structural biology of disulfide oxidants and isomerases is the extraordinar...