Background: Disulfide-rich proteins or DRPs are versatile bioactive compounds that encompass a wide variety of pharmacological, therapeutic, and/or biotechnological applications. Still, the production of DRPs in sufficient quantities is a major bottleneck for their complete structural or functional characterization. Recombinant expression of such small proteins containing multiple disulfide bonds in the bacteria E. coli is considered difficult and general methods and protocols, particularly on a high throughput scale, are limited
In bacteria, disulfide bonds confer stability on many proteins exported to the cell envelope or beyo...
This review will focus on what is NOT known about protein disulfide-isomerases, rather than on what ...
In Escherichia coli , DsbA introduces disulphide bonds into secreted proteins. DsbA is recycled by D...
International audienceBackgroundDisulfide-rich proteins or DRPs are versatile bioactive compounds th...
Abstract Bacteria are simple and cost effective hosts for producing recombinant proteins. However, t...
textHeterologous proteins containing multiple disulfide bonds cannot fold efficiently when expresse...
textBacterial proteins do not contain more than one or two of disulfide bonds in their native struct...
Abstract Background Production of correctly disulfide bonded proteins to high yields remains a chall...
textDisulfide bond formation is an essential process for the folding and biological activity of most...
Escherichia coli (E. coli) is the most widely used expression system for the production of recombina...
Abstract Background: The production of recombinant proteins containing disulfide bonds in Escherich...
Abstract Background Production of correctly disulfide bonded proteins to high yields remains a chall...
Correct formation of disulfide bonds is critical for protein folding. We find that cells lacking pro...
The present invention provides artificial enzymes comprising, e.g., an N-terminal domain derived fro...
Biochemical studies have shown that the periplasmic protein disulfide oxidoreductase DsbC can isomer...
In bacteria, disulfide bonds confer stability on many proteins exported to the cell envelope or beyo...
This review will focus on what is NOT known about protein disulfide-isomerases, rather than on what ...
In Escherichia coli , DsbA introduces disulphide bonds into secreted proteins. DsbA is recycled by D...
International audienceBackgroundDisulfide-rich proteins or DRPs are versatile bioactive compounds th...
Abstract Bacteria are simple and cost effective hosts for producing recombinant proteins. However, t...
textHeterologous proteins containing multiple disulfide bonds cannot fold efficiently when expresse...
textBacterial proteins do not contain more than one or two of disulfide bonds in their native struct...
Abstract Background Production of correctly disulfide bonded proteins to high yields remains a chall...
textDisulfide bond formation is an essential process for the folding and biological activity of most...
Escherichia coli (E. coli) is the most widely used expression system for the production of recombina...
Abstract Background: The production of recombinant proteins containing disulfide bonds in Escherich...
Abstract Background Production of correctly disulfide bonded proteins to high yields remains a chall...
Correct formation of disulfide bonds is critical for protein folding. We find that cells lacking pro...
The present invention provides artificial enzymes comprising, e.g., an N-terminal domain derived fro...
Biochemical studies have shown that the periplasmic protein disulfide oxidoreductase DsbC can isomer...
In bacteria, disulfide bonds confer stability on many proteins exported to the cell envelope or beyo...
This review will focus on what is NOT known about protein disulfide-isomerases, rather than on what ...
In Escherichia coli , DsbA introduces disulphide bonds into secreted proteins. DsbA is recycled by D...