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Protein Science : a Publication of the Protein Society|December 24, 2003
A new native EcHsp31 structure suggests a key role of structural flexibility for chaperone functionPaulene M Quigley, Konstantin Korotkov, François Baneyx, et al.Proceedings of the National Academy of Sciences of the United States of America|March 7, 2003
The 1.6-A crystal structure of the class of chaperones represented by Escherichia coli Hsp31 reveals a putative catalytic triadPaulene M Quigley, Konstantin Korotkov, Francois Baneyx, et al.The Journal of Biological Chemistry|November 5, 2003
The role of lysine 532 in the catalytic mechanism of human topoisomerase IHeidrun Interthal, Paulene M Quigley, Wim G J Hol, et al.Proceedings of the National Academy of Sciences of the United States of America|June 3, 2004
The linker-loop region of Escherichia coli chaperone Hsp31 functions as a gate that modulates high-affinity substrate binding at elevated temperaturesM S R Sastry, Paulene M Quigley, Wim G J Hol, et al.Pageof 1