King, C. -Y., Tittmann, P., Gross, H., Gebert, R., Aebi, M. & Wuthrich, K. (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 , 6618–6622.
King, C. Y. (2001). Supporting the structural basis of prion strains: induction and identification of [PSI] variants. J. Mol. Biol. 307 , 1247–1260.
King, C. Y. & Diaz-Avalos, R. (2004). Protein-only transmission of three yeast prion strains. Nature 428, 319–323.
Diaz-Avalos, R., King, C.-Y., Wall, J., Simon, M., and Caspar, D. L. (2005) Strain-specific morphologies of yeast prion amyloid fibers. Proc. Natl. Acad. Sci. USA 102, 10165-10170.
King, C.-Y., Wang, H.-L., and Chang, H.-Y. (2006) Transformation of yeast by infectious prion particles. Methods 39, 68-71.
Chang HY, Lin JY, Lee HC, Wang HL, King CY. Strain-specific sequences required for yeast [PSI+] prion propagation. Proc Natl Acad Sci U S A. 2008 Sep 9;105(36):13345-50.
Lin, J.-Y., Liao, T.-Y., Lee, H.-C. & King, C.-Y. (2011) Inter-allelic prion propagation reveals conformational relationships among a multitude of [PSI] strains. PLoS Genet.. 7(9), 1-9, 2011.
Huang, Y. W., Chang, Y. C., Diaz-Avalos, R., and King, C. Y.(2015) W8, a new Sup35 prion strain, transmits distinctive information with a conserved assembly scheme. Prion. 9, 207–227, 2015-04.
Shenq-Huey Wong and Chih-Yen King.(2015) Amino Acid Proximities in Two Sup35 Prion Strains Revealed by Chemical Cross-Linking. Journal of Biological Chemistry. 290, 25062-25071, 2015-10.
Yu CI, *King CY (2019) Forms and abundance of chaperone proteins influence yeast prion variant competition. Molecular Microbiology 111: 798-810
Huang YW, *King CY (2020) A complete catalog of wild-type Sup35 prion variants and their protein-only propagation. Current Genetics 66: 97-122
Huang YW, Kushnirov, VV, *King CY (2020) Mutable yeast prion variants are stabilized by a defective Hsp104 chaperone. Molecular Microbiology, in print (published online 11/15)