Federico Katzen, Geoffrey Chang, Wieslaw Kudlicki
Recent technical advances have revitalized cell-free expression systems to meet the increasing demands for protein synthesis. Cell-free systems offer several advantages over traditional cell-based...
DsbC activation by the N-terminal domain of DsbD
Goldstone, David, Haebel, Peter W., Katzen, Federico, Bader, Martin W., Bardwell, James C. A., Beckwith, Jon, ...
The correct formation of disulfide bonds in the periplasm of Escherichia coli involves Dsb proteins, including two related periplasmic disulfide-bond isomerases, DsbC and DsbG. DsbD is a membrane...
Katzen, Federico, Becker, Anke, Ielmini, M. Verónica, Oddo, Cristian G., Ielpi, Luis
We describe useful vectors to select double-crossover events directly in site-directed marker exchange mutagenesis in gram-negative bacteria. These vectors contain the gusA marker gene, providing...
Katzen, Federico, Ferreiro, Diego U., Oddo, Cristian G., Ielmini, M. Verónica, Becker, Anke, Pühler, Alfred, ...
Xanthan is an industrially important exopolysaccharide produced by the phytopathogenic, gram-negative bacterium Xanthomonas campestris pv. campestris. It is composed of polymerized pentasaccharide...
Katzen, Federico, Deshmukh, Meenal, Daldal, Fevzi, Beckwith, Jon
Modular organization of proteins has been postulated as a widely used strategy for protein evolution. The multidomain transmembrane protein DsbD catalyzes the transfer of electrons from the cytoplasm...
Haebel, Peter W., Goldstone, David, Katzen, Federico, Beckwith, Jon, Metcalf, Peter
The Escherichia coli disulfide bond isomerase DsbC rearranges incorrect disulfide bonds during oxidative protein folding. It is specifically activated by the periplasmic N-terminal domain (DsbDα) of...
Katzen, Federico, Beckwith, Jon
The central hydrophobic domain of the membrane protein DsbD catalyzes the transfer of electrons from the cytoplasm to the periplasm of Escherichia coli. Two cysteine residues embedded in...
DsbC activation by the N-terminal domain of DsbD
Goldstone, David, Haebel, Peter W., Katzen, Federico, Bader, Martin W., Bardwell, James C. A., Beckwith, Jon, ...
The correct formation of disulfide bonds in the periplasm of Escherichia coli involves Dsb proteins, including two related periplasmic disulfide-bond isomerases, DsbC and DsbG. DsbD is a membrane...
Katzen, Federico, Becker, Anke, Ielmini, M. Verónica, Oddo, Cristian G., Ielpi, Luis
We describe useful vectors to select double-crossover events directly in site-directed marker exchange mutagenesis in gram-negative bacteria. These vectors contain the gusA marker gene, providing...
Katzen, Federico, Ferreiro, Diego U., Oddo, Cristian G., Ielmini, M. Verónica, Becker, Anke, Pühler, Alfred, ...
Xanthan is an industrially important exopolysaccharide produced by the phytopathogenic, gram-negative bacterium Xanthomonas campestris pv. campestris. It is composed of polymerized pentasaccharide...
Katzen, Federico, Deshmukh, Meenal, Daldal, Fevzi, Beckwith, Jon
Modular organization of proteins has been postulated as a widely used strategy for protein evolution. The multidomain transmembrane protein DsbD catalyzes the transfer of electrons from the cytoplasm...
Haebel, Peter W., Goldstone, David, Katzen, Federico, Beckwith, Jon, Metcalf, Peter
The Escherichia coli disulfide bond isomerase DsbC rearranges incorrect disulfide bonds during oxidative protein folding. It is specifically activated by the periplasmic N-terminal domain (DsbDα) of...
Katzen, Federico, Beckwith, Jon
The central hydrophobic domain of the membrane protein DsbD catalyzes the transfer of electrons from the cytoplasm to the periplasm of Escherichia coli. Two cysteine residues embedded in...
Cappuccio, Jenny A., Blanchette, Craig D., Sulchek, Todd A., Arroyo, Erin S., Kralj, Joel M., Hinz, Angela K., ...
Here we demonstrate rapid production of solubilized and functional membrane protein by simultaneous cell-free expression of an apolipoprotein and a membrane protein in the presence of lipids, leading...