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Author Wickner, Reed B. ♦ Kelly, Amy C.
Source SpringerLink
Content type Text
Publisher Springer International Publishing
File Format PDF
Copyright Year ©2015
Language English
Subject Domain (in DDC) Natural sciences & mathematics ♦ Life sciences; biology
Subject Keyword Amyloid ♦ Ure2p ♦ Sup35p ♦ HET-s ♦ Rnq1 ♦ Parallel in-register beta sheet ♦ Cell Biology ♦ Biomedicine general ♦ Life Sciences ♦ Biochemistry
Abstract Prions, infectious proteins, can transmit diseases or be the basis of heritable traits (or both), mostly 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.
ISSN 1420682X
Age Range 18 to 22 years ♦ above 22 year
Educational Use Research
Education Level UG and PG
Learning Resource Type Article
Publisher Date 2015-12-28
Publisher Place Cham
e-ISSN 14209071
Journal Cellular and Molecular Life Sciences
Volume Number 73
Issue Number 6
Page Count 14
Starting Page 1131
Ending Page 1144


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Source: SpringerLink