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2. N-terminal domain of yeast Hsp104 chaperone is dispensable for thermotolerance and prion propagation but necessary for curing prions by Hsp104 overexpression. Hung GC, Masison DC. Genetics; 2006 Jun; 173(2):611-20. PubMed ID: 16582428 [Abstract] [Full Text] [Related]
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14. Low activity of select Hsp104 mutants is sufficient to propagate unstable prion variants. Dulle JE, True HL. Prion; 2013 Jan 30; 7(5):394-403. PubMed ID: 24064980 [Abstract] [Full Text] [Related]
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19. Amino acid residue 184 of yeast Hsp104 chaperone is critical for prion-curing by guanidine, prion propagation, and thermotolerance. Jung G, Jones G, Masison DC. Proc Natl Acad Sci U S A; 2002 Jul 23; 99(15):9936-41. PubMed ID: 12105276 [Abstract] [Full Text] [Related]