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pro vyhledávání: '"CHIH-YEN KING"'
Autor:
Chih-Yen King
Publikováno v:
Viruses, Vol 14, Iss 11, p 2337 (2022)
Prions replicate by a self-templating mechanism. Infidelity in the process can lead to the emergence of new infectious structures, referred to as variants or strains. The question of whether prions are prone to mis-templating is not completely answer
Externí odkaz:
https://doaj.org/article/d1c3bcfb0cfb444f978dfed3ae0cb697
Publikováno v:
PLoS Genetics, Vol 7, Iss 9, p e1002297 (2011)
Immense diversity of prion strains is observed, but its underlying mechanism is less clear. Three [PSI] prion strains--named VH, VK, and VL--were previously isolated in the wild-type yeast genetic background. Here we report the generation and charact
Externí odkaz:
https://doaj.org/article/906efb82e09d4f5885f6ad5891c73fd8
Publikováno v:
Molecular Microbiology. 115:774-788
Gorkovskiy et al. observed that many [PSI+ ] prion isolates, obtained in yeast with the mutant Hsp104T160M chaperone, propagate poorly in wild-type cells and suggested that Hsp104 is part of the cellular anti-prion system, curing many nascent [PSI+ ]
Autor:
Chang-I Yu, Chih-Yen King
Publikováno v:
Molecular Microbiology. 111:798-810
[PSI+ ] variants are different infectious conformations of the same Sup35 protein. We show that when [PSI+ ] variants VK and VL co-infect a dividing host, only one prevails in the end and the host genetic background is involved in winner selection. I
Autor:
Yu-Wen Huang, Chih-Yen King
Publikováno v:
Current genetics. 66(1)
Twenty-three prion variants of the wild-type Sup35 protein are obtained, including 19 novel ones and 4 previously documented, namely, VH, VK, VL, and W8. Their uniqueness and non-composite nature are demonstrated. Specific infectivity is generated de
Autor:
Chang-I, Yu, Chih-Yen, King
Publikováno v:
Molecular microbiology. 111(3)
[PSI
Autor:
Shenq-Huey Wong, Chih-Yen King
Publikováno v:
Journal of Biological Chemistry. 290:25062-25071
Strains of the yeast prion [PSI] are different folding patterns of the same Sup35 protein, which stacks up periodically to form a prion fiber. Chemical cross-linking is employed here to probe different fiber structures assembled with a mutant Sup35 f
Autor:
Chih-Yen King, Jonathan S.1 chihyen@sb.fsu.edu, Diaz-Avalos, Ruben1
Publikováno v:
Nature. 3/18/2004, Vol. 428 Issue 6980, p319-323. 5p.
Publikováno v:
Proceedings of the National Academy of Sciences. 105:13345-13350
Amyloid polymorphism underlies the prion strain phenomenon where a single protein polypeptide adopts different chain-folding patterns to form self-propagating cross-β structures. Three strains of the yeast prion [ PSI ], namely [VH], [VK], and [VL],