Gene Review:
hscB - co-chaperone HscB
Escherichia coli O157:H7 str. Sakai
- Contributions of the LPPVK motif of the iron-sulfur template protein IscU to interactions with the Hsc66-Hsc20 chaperone system. Hoff, K.G., Cupp-Vickery, J.R., Vickery, L.E. J. Biol. Chem. (2003)
- Interaction of the iron-sulfur cluster assembly protein IscU with the Hsc66/Hsc20 molecular chaperone system of Escherichia coli. Hoff, K.G., Silberg, J.J., Vickery, L.E. Proc. Natl. Acad. Sci. U.S.A. (2000)
- The Hsc66-Hsc20 chaperone system in Escherichia coli: chaperone activity and interactions with the DnaK-DnaJ-grpE system. Silberg, J.J., Hoff, K.G., Vickery, L.E. J. Bacteriol. (1998)
- Crystallization and preliminary X-ray crystallographic properties of Hsc20, a J-motif co-chaperone protein from Escherichia coli. Cupp-Vickery, J.R., Vickery, L.E. Protein Sci. (1997)
- Hsc66 substrate specificity is directed toward a discrete region of the iron-sulfur cluster template protein IscU. Hoff, K.G., Ta, D.T., Tapley, T.L., Silberg, J.J., Vickery, L.E. J. Biol. Chem. (2002)
- Hsc66 and Hsc20, a new heat shock cognate molecular chaperone system from Escherichia coli. Vickery, L.E., Silberg, J.J., Ta, D.T. Protein Sci. (1997)