Standard

Analysis of interspecies prion transmission in yeast. / Rubel, Aleksandr A.; Grizel, Anastasia V.; Bondarev, Stanislav A.; Kachkin, Daniel V.; Chernoff, Yury O.

In: Prion, Vol. 10, No. Suppl.1, 2016.

Research output: Contribution to journal › Meeting Abstract › peer-review

Harvard

Rubel, AA, Grizel, AV, Bondarev, SA, Kachkin, DV & Chernoff, YO 2016, 'Analysis of interspecies prion transmission in yeast', Prion, vol. 10, no. Suppl.1. https://doi.org/10.1080/19336896.2016.1162644

APA

Rubel, A. A., Grizel, A. V., Bondarev, S. A., Kachkin, D. V., & Chernoff, Y. O. (2016). Analysis of interspecies prion transmission in yeast. Prion, 10(Suppl.1). https://doi.org/10.1080/19336896.2016.1162644

Vancouver

Rubel AA, Grizel AV, Bondarev SA, Kachkin DV, Chernoff YO. Analysis of interspecies prion transmission in yeast. Prion. 2016;10(Suppl.1). https://doi.org/10.1080/19336896.2016.1162644

Author

Rubel, Aleksandr A. ; Grizel, Anastasia V. ; Bondarev, Stanislav A. ; Kachkin, Daniel V. ; Chernoff, Yury O. / Analysis of interspecies prion transmission in yeast. In: Prion. 2016 ; Vol. 10, No. Suppl.1.

BibTeX

@article{3fd5cd4385394f7ba8d9fa2b82ba05e6,
title = "Analysis of interspecies prion transmission in yeast",
abstract = "Self-perpetuating cross-β aggregated proteins (prions) are associated with fatal transmissible spongiform encephalopathies in mammals (including humans) and control heritable traits in yeast and other fungi. Prion diseases, such as sheep scrapie, bovine spongiform encephalopathy (BSE), chronic wasting disease (CWD) and human Creutzfeldt-Jakob disease, are transmitted by the prion protein (PrP) that converts normal cellular protein of the same sequence into a polymeric cross-β (prion) isoform. Prion transmission depends on the identity of interacting amino acid sequences, so that the transmission barriers are observed between divergent species. However, these barriers can be overcome. For example, BSE transmission to humans is a huge problem for the cattle industry and for a public health. The mechanisms of cross-species prion transmission are still poorly understood. We used a yeast Sup35/[PSI+] model to explore the molecular basis of prion transmission barriers. In contrast to the previous experimental setti",
author = "Rubel, {Aleksandr A.} and Grizel, {Anastasia V.} and Bondarev, {Stanislav A.} and Kachkin, {Daniel V.} and Chernoff, {Yury O.}",
year = "2016",
doi = "10.1080/19336896.2016.1162644",
language = "English",
volume = "10",
journal = "Prion",
issn = "1933-6896",
publisher = "Landes Bioscience",
number = "Suppl.1",

}

RIS

TY - JOUR

T1 - Analysis of interspecies prion transmission in yeast

AU - Rubel, Aleksandr A.

AU - Grizel, Anastasia V.

AU - Bondarev, Stanislav A.

AU - Kachkin, Daniel V.

AU - Chernoff, Yury O.

PY - 2016

Y1 - 2016

N2 - Self-perpetuating cross-β aggregated proteins (prions) are associated with fatal transmissible spongiform encephalopathies in mammals (including humans) and control heritable traits in yeast and other fungi. Prion diseases, such as sheep scrapie, bovine spongiform encephalopathy (BSE), chronic wasting disease (CWD) and human Creutzfeldt-Jakob disease, are transmitted by the prion protein (PrP) that converts normal cellular protein of the same sequence into a polymeric cross-β (prion) isoform. Prion transmission depends on the identity of interacting amino acid sequences, so that the transmission barriers are observed between divergent species. However, these barriers can be overcome. For example, BSE transmission to humans is a huge problem for the cattle industry and for a public health. The mechanisms of cross-species prion transmission are still poorly understood. We used a yeast Sup35/[PSI+] model to explore the molecular basis of prion transmission barriers. In contrast to the previous experimental setti

AB - Self-perpetuating cross-β aggregated proteins (prions) are associated with fatal transmissible spongiform encephalopathies in mammals (including humans) and control heritable traits in yeast and other fungi. Prion diseases, such as sheep scrapie, bovine spongiform encephalopathy (BSE), chronic wasting disease (CWD) and human Creutzfeldt-Jakob disease, are transmitted by the prion protein (PrP) that converts normal cellular protein of the same sequence into a polymeric cross-β (prion) isoform. Prion transmission depends on the identity of interacting amino acid sequences, so that the transmission barriers are observed between divergent species. However, these barriers can be overcome. For example, BSE transmission to humans is a huge problem for the cattle industry and for a public health. The mechanisms of cross-species prion transmission are still poorly understood. We used a yeast Sup35/[PSI+] model to explore the molecular basis of prion transmission barriers. In contrast to the previous experimental setti

U2 - 10.1080/19336896.2016.1162644

DO - 10.1080/19336896.2016.1162644

M3 - Meeting Abstract

VL - 10

JO - Prion

JF - Prion

SN - 1933-6896

IS - Suppl.1

ER -

ID: 74911796