<div><p>(A) Colored overlay of the stained 2D gel (shown in green) and the phosphor image (shown in red) of differentially trapped protein extract from exponentially growing E. coli wild-type cells. Proteins with a high <sup>14</sup>C activity/protein ratio appear red, while proteins with a low ratio appear green. Proteins that were found to have significantly lower ratio of <sup>14</sup>C activity/protein in the <i>dsbA</i>::kan strain (B and C) are labeled.</p> <p>(B) Overlay of the stained 2D gel (shown in green) and the phosphor image (shown in red) of a differentially trapped protein extract from exponentially growing <i>dsbA</i>::kan cells. Proteins that were found to have a significantly lower <sup>14</sup>C activity/prot...
Since its discovery in 1991, the bacterial periplasmic oxidative folding catalyst DsbA has been the ...
Protein disulfide bond formation in Escherichia coli requires the periplasmic protein DsbA. We descr...
We describe a mutation (d&A) that renders Esche-richia coli severely defective in disulfide bond...
AbstractDsbA is a periplasmic, disulfide bond formation factor of E. coli. We studied in vivo redox ...
The formation of a disulfide bond results from the oxidation of two cysteine thiol groups, with the ...
The biological kingdoms have evolved elaborate systems that ensure the catalysis of protein disulfid...
<div><p>(A) Colored overlay of the Coomassie blue–stained 2D gel (shown in green) and the phosphor i...
DsbA is the major oxidase responsible for generation of disulfide bonds in proteins of E. coli envel...
SummaryOxidation of cysteine pairs to disulfide requires cellular factors present in the bacterial p...
AbstractGenetic studies have recently identified DsbG, a new member of the dsb group of redox protei...
<div><p>(A) Overlay of the stained 2D gel (shown in green) and the phosphor image (shown in red) of ...
The discovery of the oxidoreductase disulfide bond protein A (DsbA) in 1991 opened the way to the un...
ABSTRACT: The protein DsbA facilitates disulfide bond formation in the periplasm of Escherichia coli...
Disulfide bond (DSB) formation is catalyzed by disulfide bond proteins and is critical for the prope...
Many proteins secreted to the bacterial cell envelope contain cysteine residues that are involved in...
Since its discovery in 1991, the bacterial periplasmic oxidative folding catalyst DsbA has been the ...
Protein disulfide bond formation in Escherichia coli requires the periplasmic protein DsbA. We descr...
We describe a mutation (d&A) that renders Esche-richia coli severely defective in disulfide bond...
AbstractDsbA is a periplasmic, disulfide bond formation factor of E. coli. We studied in vivo redox ...
The formation of a disulfide bond results from the oxidation of two cysteine thiol groups, with the ...
The biological kingdoms have evolved elaborate systems that ensure the catalysis of protein disulfid...
<div><p>(A) Colored overlay of the Coomassie blue–stained 2D gel (shown in green) and the phosphor i...
DsbA is the major oxidase responsible for generation of disulfide bonds in proteins of E. coli envel...
SummaryOxidation of cysteine pairs to disulfide requires cellular factors present in the bacterial p...
AbstractGenetic studies have recently identified DsbG, a new member of the dsb group of redox protei...
<div><p>(A) Overlay of the stained 2D gel (shown in green) and the phosphor image (shown in red) of ...
The discovery of the oxidoreductase disulfide bond protein A (DsbA) in 1991 opened the way to the un...
ABSTRACT: The protein DsbA facilitates disulfide bond formation in the periplasm of Escherichia coli...
Disulfide bond (DSB) formation is catalyzed by disulfide bond proteins and is critical for the prope...
Many proteins secreted to the bacterial cell envelope contain cysteine residues that are involved in...
Since its discovery in 1991, the bacterial periplasmic oxidative folding catalyst DsbA has been the ...
Protein disulfide bond formation in Escherichia coli requires the periplasmic protein DsbA. We descr...
We describe a mutation (d&A) that renders Esche-richia coli severely defective in disulfide bond...