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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. p. 85-105.

Research output: Chapter in Book/Report/Conference proceeding › Chapter › peer-review

Harvard

Rubel, AA, Saifitdinova, AF & Romanova, NV 2017, Protein assembly disorders and protein-based inheritance. in Genetics, Evolution and Radiation: Crossing Borders, The Interdisciplinary Legacy of Nikolay W. Timofeeff-Ressovsky. Springer Nature, pp. 85-105. https://doi.org/10.1007/978-3-319-48838-7_8

APA

Rubel, A. A., Saifitdinova, A. F., & Romanova, N. V. (2017). Protein assembly disorders and protein-based inheritance. In Genetics, Evolution and Radiation: Crossing Borders, The Interdisciplinary Legacy of Nikolay W. Timofeeff-Ressovsky (pp. 85-105). Springer Nature. https://doi.org/10.1007/978-3-319-48838-7_8

Vancouver

Rubel AA, Saifitdinova AF, Romanova NV. Protein assembly disorders and protein-based inheritance. In Genetics, Evolution and Radiation: Crossing Borders, The Interdisciplinary Legacy of Nikolay W. Timofeeff-Ressovsky. Springer Nature. 2017. p. 85-105 https://doi.org/10.1007/978-3-319-48838-7_8

Author

Rubel, Aleksander A. ; Saifitdinova, Alsu F. ; Romanova, Nina V. / Protein assembly disorders and protein-based inheritance. Genetics, Evolution and Radiation: Crossing Borders, The Interdisciplinary Legacy of Nikolay W. Timofeeff-Ressovsky. Springer Nature, 2017. pp. 85-105

BibTeX

@inbook{47389bd2ad2e42d78d3114c96f8de4bf,
title = "Protein assembly disorders and protein-based inheritance",
abstract = "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.",
keywords = "Amyloids, Prions, Protein templates, Prp, Transmissible spongiform encephalopathies",
author = "Rubel, {Aleksander A.} and Saifitdinova, {Alsu F.} and Romanova, {Nina V.}",
year = "2017",
month = jan,
day = "1",
doi = "10.1007/978-3-319-48838-7_8",
language = "English",
isbn = "9783319488370",
pages = "85--105",
booktitle = "Genetics, Evolution and Radiation",
publisher = "Springer Nature",
address = "Germany",

}

RIS

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