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10.1007/s00018-015-2109-6

http://scihub22266oqcxt.onion/10.1007/s00018-015-2109-6
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C4762734!4762734!26713322
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suck abstract from ncbi

pmid26713322      Cell+Mol+Life+Sci 2016 ; 73 (6): 1131-44
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  • Prions are Affected by Evolution at Two Levels #MMPMID26713322
  • Wickner RB; Kelly AC
  • Cell Mol Life Sci 2016[Mar]; 73 (6): 1131-44 PMID26713322show ga
  • Prions, infectious proteins, can transmit diseases or be the basis of heritable traits (or both), most based on amyloid forms of the prion protein. A single protein sequence can be the basis for many prion strains/variants, with different biological properties based on different amyloid conformations, each rather stably propagating. Prions are unique in that evolution and selection work at both the level of the chromosomal gene encoding the protein, and on the prion itself selecting prion variants. Here we summarize what is known about the evolution of prion proteins, both the genes and the prions themselves. We contrast the one known functional prion, [Het-s] of Podospora anserina, with the known disease prions, the yeast prions [PSI+] and [URE3] and the transmissible spongiform encephalopathies of mammals.
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