Article ; Online: Structural Bases of Prion Variation in Yeast
International Journal of Molecular Sciences, Vol 23, Iss 5738, p
2022 Volume 5738
Abstract: Amyloids are protein aggregates with a specific filamentous structure that are related to a number of human diseases, and also to some important physiological processes in animals and other kingdoms of life. Amyloids in yeast can stably propagate as ... ...
| Abstract | Amyloids are protein aggregates with a specific filamentous structure that are related to a number of human diseases, and also to some important physiological processes in animals and other kingdoms of life. Amyloids in yeast can stably propagate as heritable units, prions. Yeast prions are of interest both on their own and as a model for amyloids and prions in general. In this review, we consider the structure of yeast prions and its variation, how such structures determine the balance of aggregated and soluble prion protein through interaction with chaperones and how the aggregated state affects the non-prion functions of these proteins. |
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| Keywords | amyloid ; prion ; prion structure ; yeast ; Sup35 ; chaperones ; Biology (General) ; QH301-705.5 ; Chemistry ; QD1-999 |
| Language | English |
| Publishing date | 2022-05-01T00:00:00Z |
| Publisher | MDPI AG |
| Document type | Article ; Online |
| Database | BASE - Bielefeld Academic Search Engine (life sciences selection) |
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