Bick, Julie-Ann, Åslund, Fredrik, Chen, Yichang, Leustek, Thomas
5′-Adenylylsulfate (APS) reductase (EC 1.8.99.-) catalyzes the reduction of activated sulfate to sulfite in plants. The evidence presented here shows that a domain of the enzyme is a glutathione...
Efficient folding of proteins with multiple disulfide bonds in the Escherichia coli cytoplasm
Bessette, Paul H., Åslund, Fredrik, Beckwith, Jon, Georgiou, George
Under physiological conditions, the Escherichia coli cytoplasm is maintained in a reduced state that strongly disfavors the formation of stable disulfide bonds in proteins. However, mutants in which...
Åslund, Fredrik, Zheng, Ming, Beckwith, Jon, Storz, Gisela
The Escherichia coli transcription factor OxyR is activated by the formation of an intramolecular disulfide bond and subsequently is deactivated by enzymatic reduction of the disulfide bond. Here we...
Bick, Julie-Ann, Åslund, Fredrik, Chen, Yichang, Leustek, Thomas
5′-Adenylylsulfate (APS) reductase (EC 1.8.99.-) catalyzes the reduction of activated sulfate to sulfite in plants. The evidence presented here shows that a domain of the enzyme is a glutathione...
Efficient folding of proteins with multiple disulfide bonds in the Escherichia coli cytoplasm
Bessette, Paul H., Åslund, Fredrik, Beckwith, Jon, Georgiou, George
Under physiological conditions, the Escherichia coli cytoplasm is maintained in a reduced state that strongly disfavors the formation of stable disulfide bonds in proteins. However, mutants in which...
Åslund, Fredrik, Zheng, Ming, Beckwith, Jon, Storz, Gisela
The Escherichia coli transcription factor OxyR is activated by the formation of an intramolecular disulfide bond and subsequently is deactivated by enzymatic reduction of the disulfide bond. Here we...