Результаты исследований: Публикации в книгах, отчётах, сборниках, трудах конференций › глава/раздел › Рецензирование
Protein assembly disorders and protein-based inheritance. / Rubel, Aleksander A.; Saifitdinova, Alsu F.; Romanova, Nina V.
Genetics, Evolution and Radiation: Crossing Borders, The Interdisciplinary Legacy of Nikolay W. Timofeeff-Ressovsky. Springer Nature, 2017. стр. 85-105.Результаты исследований: Публикации в книгах, отчётах, сборниках, трудах конференций › глава/раздел › Рецензирование
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TY - CHAP
T1 - Protein assembly disorders and protein-based inheritance
AU - Rubel, Aleksander A.
AU - Saifitdinova, Alsu F.
AU - Romanova, Nina V.
PY - 2017/1/1
Y1 - 2017/1/1
N2 - Prions are self-perpetuating aggregated fibrous proteins that associated with fatal transmissible spongiform encephalopathies (TSEs) in mammals (including humans), and manifest themselves as non-Mendelian heritable elements in yeast and other fungi. The infectious agent responsible for TSEs is the prion, an abnormally folded and aggregated protein that propagates itself by imposing its conformation onto the cellular prion protein (PrPC) of the host. PrPC is necessary for prion replication and for prion-induced neurodegeneration, yet causes of neuronal injury and death are still poorly understood. Here we view of the prion concept, models describing of the replication and transport of prions particles, structural features and functions of the cellular PrP, the prion strain phenomenon, current developments in diagnostics of prion and potential antiprion therapies. Finally, we discuss how prion-like mechanisms may apply to other protein aggregation diseases.
AB - Prions are self-perpetuating aggregated fibrous proteins that associated with fatal transmissible spongiform encephalopathies (TSEs) in mammals (including humans), and manifest themselves as non-Mendelian heritable elements in yeast and other fungi. The infectious agent responsible for TSEs is the prion, an abnormally folded and aggregated protein that propagates itself by imposing its conformation onto the cellular prion protein (PrPC) of the host. PrPC is necessary for prion replication and for prion-induced neurodegeneration, yet causes of neuronal injury and death are still poorly understood. Here we view of the prion concept, models describing of the replication and transport of prions particles, structural features and functions of the cellular PrP, the prion strain phenomenon, current developments in diagnostics of prion and potential antiprion therapies. Finally, we discuss how prion-like mechanisms may apply to other protein aggregation diseases.
KW - Amyloids
KW - Prions
KW - Protein templates
KW - Prp
KW - Transmissible spongiform encephalopathies
UR - http://www.scopus.com/inward/record.url?scp=85034227144&partnerID=8YFLogxK
U2 - 10.1007/978-3-319-48838-7_8
DO - 10.1007/978-3-319-48838-7_8
M3 - Chapter
AN - SCOPUS:85034227144
SN - 9783319488370
SP - 85
EP - 105
BT - Genetics, Evolution and Radiation
PB - Springer Nature
ER -
ID: 36859051