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  • Author: King CY
  • References

Author: King CY


References 14 references


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  • King CY (2025) Total propagation of yeast prion conformers in ssz1∆ upf1∆ Hsp104T160M triple mutants. Curr Genet 71(1):8 PMID:40156734
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  • King CY (2022) The Mutability of Yeast Prions. Viruses 14(11) PMID:36366434
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  • Huang YW, et al. (2021) Mutable yeast prion variants are stabilized by a defective Hsp104 chaperone. Mol Microbiol 115(4):774-788 PMID:33190361
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  • Huang YW and King CY (2020) A complete catalog of wild-type Sup35 prion variants and their protein-only propagation. Curr Genet 66(1):97-122 PMID:31183511
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  • Yu CI and King CY (2019) Forms and abundance of chaperone proteins influence yeast prion variant competition. Mol Microbiol 111(3):798-810 PMID:30582872
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  • Huang YW, et al. (2015) W8, a new Sup35 prion strain, transmits distinctive information with a conserved assembly scheme. Prion 9(3):207-27 PMID:26038983
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  • Wong SH and King CY (2015) Amino Acid Proximities in Two Sup35 Prion Strains Revealed by Chemical Cross-linking. J Biol Chem 290(41):25062-71 PMID:26265470
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  • Lin JY, et al. (2011) Inter-allelic prion propagation reveals conformational relationships among a multitude of [PSI] strains. PLoS Genet 7(9):e1002297 PMID:21980301
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  • Chang HY, et al. (2008) Strain-specific sequences required for yeast [PSI+] prion propagation. Proc Natl Acad Sci U S A 105(36):13345-50 PMID:18757753
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  • King CY, et al. (2006) Transformation of yeast by infectious prion particles. Methods 39(1):68-71 PMID:16759879
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  • Diaz-Avalos R, et al. (2005) Strain-specific morphologies of yeast prion amyloid fibrils. Proc Natl Acad Sci U S A 102(29):10165-70 PMID:16006506
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  • King CY and Diaz-Avalos R (2004) Protein-only transmission of three yeast prion strains. Nature 428(6980):319-23 PMID:15029195
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  • King CY (2001) Supporting the structural basis of prion strains: induction and identification of [PSI] variants. J Mol Biol 307(5):1247-60 PMID:11292339
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  • King CY, et al. (1997) Prion-inducing domain 2-114 of yeast Sup35 protein transforms in vitro into amyloid-like filaments. Proc Natl Acad Sci U S A 94(13):6618-22 PMID:9192614
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