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Nature|September 19, 1991
Hsp104 is a highly conserved protein with two essential nucleotide-binding sitesD A Parsell, Y Sanchez, J D Stitzel, et al.The EMBO Journal|November 15, 2001
Strains of [PSI(+)] are distinguished by their efficiencies of prion-mediated conformational conversionS M Uptain, G J Sawicki, B Caughey, et al.Medical Microbiology and Immunology|January 5, 2002
Heat shock protein 100 and the amastigote stage-specific A2 proteins of Leishmania donovaniJ Clos, L Klaholz, M Kroemer, et al.Proceedings of the National Academy of Sciences of the United States of America|February 12, 1998
Chaperone-supervised conversion of prion protein to its protease-resistant formS K DebBurman, G J Raymond, B Caughey, et al.International Journal of Environmental Research and Public Health|May 14, 2022
Student and Nature Interactions and Their Impact on Mental Health during the COVID-19 PandemicJonah E Trevino, Muntazar Monsur, Carol S Lindquist, et al.Genetics|October 19, 2001
Molecular population genetics and evolution of a prion-like protein in Saccharomyces cerevisiaeM A Jensen, H L True, Y O Chernoff, et al.Trends in Biochemical Sciences|August 1, 1996
HSP100/Clp proteins: a common mechanism explains diverse functionsE C Schirmer, J R Glover, M A Singer, et al.Nature|December 1, 1994
Protein disaggregation mediated by heat-shock protein Hsp104D A Parsell, A S Kowal, M A Singer, et al.Plant Physiology|November 1, 1988
Characterization of an HSP70 Cognate Gene Family in ArabidopsisC H Wu, T Caspar, J Browse, et al.Genes & Development|August 1, 1992
The consequences of expressing hsp70 in Drosophila cells at normal temperaturesJ H Feder, J M Rossi, J Solomon, et al.Pageof 40