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Genes & Development|August 1, 1989
Induction of a heat shock-like response by unfolded protein in Escherichia coli: dependence on protein level not protein degradationD A Parsell, R T SauerThe Journal of Biological Chemistry|May 5, 1989
The structural stability of a protein is an important determinant of its proteolytic susceptibility in Escherichia coliD A Parsell, R T SauerPhilosophical Transactions of the Royal Society of London. Series B, Biological Sciences|March 29, 1993
The role of heat-shock proteins in thermotoleranceD A Parsell, J Taulien, S LindquistThe Journal of Biological Chemistry|February 11, 1994
Saccharomyces cerevisiae Hsp104 protein. Purification and characterization of ATP-induced structural changesD A Parsell, A S Kowal, S LindquistCurrent Biology : CB|March 1, 1995
Heat-shock proteins Hsp104 and Hsp70 reactivate mRNA splicing after heat inactivationJ L Vogel, D A Parsell, S LindquistGenes & Development|February 1, 1990
Carboxy-terminal determinants of intracellular protein degradationD A Parsell, K R Silber, R T SauerNature|September 19, 1991
Hsp104 is a highly conserved protein with two essential nucleotide-binding sitesD A Parsell, Y Sanchez, J D Stitzel, et al.Biochemistry|August 21, 1990
An essential proline in lambda repressor is required for resistance to intracellular proteolysisJ F Reidhaar-Olson, D A Parsell, R T SauerNature|December 1, 1994
Protein disaggregation mediated by heat-shock protein Hsp104D A Parsell, A S Kowal, M A Singer, et al.The Journal of Biological Chemistry|November 1, 1996
Relaxin binds to and elicits a response from cells of the human monocytic cell line, THP-1D A Parsell, J Y Mak, E P Amento, et al.Pageof 2