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Strain conformation controls the specificity of cross-species prion transmission in the yeast model. / Grizel, Anastasia V.; Rubel, Aleksandr A.; Chernoff, Yury O.

In: Prion, Vol. 10, No. 4, 2016, p. 269-282.

Research output: Contribution to journal › Article

Harvard

Grizel, AV, Rubel, AA & Chernoff, YO 2016, 'Strain conformation controls the specificity of cross-species prion transmission in the yeast model', Prion, vol. 10, no. 4, pp. 269-282. https://doi.org/10.1080/19336896.2016.1204060

APA

Grizel, A. V., Rubel, A. A., & Chernoff, Y. O. (2016). Strain conformation controls the specificity of cross-species prion transmission in the yeast model. Prion, 10(4), 269-282. https://doi.org/10.1080/19336896.2016.1204060

Vancouver

Grizel AV, Rubel AA, Chernoff YO. Strain conformation controls the specificity of cross-species prion transmission in the yeast model. Prion. 2016;10(4):269-282. https://doi.org/10.1080/19336896.2016.1204060

Author

Grizel, Anastasia V. ; Rubel, Aleksandr A. ; Chernoff, Yury O. / Strain conformation controls the specificity of cross-species prion transmission in the yeast model. In: Prion. 2016 ; Vol. 10, No. 4. pp. 269-282.

BibTeX

@article{c6358d05d8f7426f80af04c6aa1285d7,
title = "Strain conformation controls the specificity of cross-species prion transmission in the yeast model",
abstract = "Transmissible self-assembled fibrous cross-β polymer infectious proteins (prions) cause neurodegenerative diseases in mammals and control non-Mendelian heritable traits in yeast. Cross-species prion transmission is frequently impaired, due to sequence differences in prion- forming proteins. Recent studies of prion species barrier on the model of closely related yeast species show that colocalization of divergent proteins is not sufficient for the cross-species prion transmission, and that an identity of specific amino acid sequences and a type of prion conformational variant (strain) play a major role in the control of transmission specificity. In contrast, chemical compounds primarily influence transmission specificity via favoring certain strain conformations, while the species origin of the host cell has only a relatively minor input. Strain alterations may occur during cross-species prion conversion in some combinations. The model is discussed which suggests that different recipient proteins can",
keywords = "Amyloid, prion variant, [PSI + ], Saccharomyces cerevisiae, Saccharomyces paradoxus, Saccharomyces uvarum, Sup35.",
author = "Grizel, {Anastasia V.} and Rubel, {Aleksandr A.} and Chernoff, {Yury O.}",
year = "2016",
doi = "10.1080/19336896.2016.1204060",
language = "English",
volume = "10",
pages = "269--282",
journal = "Prion",
issn = "1933-6896",
publisher = "Landes Bioscience",
number = "4",

}

RIS

TY - JOUR

T1 - Strain conformation controls the specificity of cross-species prion transmission in the yeast model

AU - Grizel, Anastasia V.

AU - Rubel, Aleksandr A.

AU - Chernoff, Yury O.

PY - 2016

Y1 - 2016

N2 - Transmissible self-assembled fibrous cross-β polymer infectious proteins (prions) cause neurodegenerative diseases in mammals and control non-Mendelian heritable traits in yeast. Cross-species prion transmission is frequently impaired, due to sequence differences in prion- forming proteins. Recent studies of prion species barrier on the model of closely related yeast species show that colocalization of divergent proteins is not sufficient for the cross-species prion transmission, and that an identity of specific amino acid sequences and a type of prion conformational variant (strain) play a major role in the control of transmission specificity. In contrast, chemical compounds primarily influence transmission specificity via favoring certain strain conformations, while the species origin of the host cell has only a relatively minor input. Strain alterations may occur during cross-species prion conversion in some combinations. The model is discussed which suggests that different recipient proteins can

AB - Transmissible self-assembled fibrous cross-β polymer infectious proteins (prions) cause neurodegenerative diseases in mammals and control non-Mendelian heritable traits in yeast. Cross-species prion transmission is frequently impaired, due to sequence differences in prion- forming proteins. Recent studies of prion species barrier on the model of closely related yeast species show that colocalization of divergent proteins is not sufficient for the cross-species prion transmission, and that an identity of specific amino acid sequences and a type of prion conformational variant (strain) play a major role in the control of transmission specificity. In contrast, chemical compounds primarily influence transmission specificity via favoring certain strain conformations, while the species origin of the host cell has only a relatively minor input. Strain alterations may occur during cross-species prion conversion in some combinations. The model is discussed which suggests that different recipient proteins can

KW - Amyloid

KW - prion variant

KW - [PSI + ]

KW - Saccharomyces cerevisiae

KW - Saccharomyces paradoxus

KW - Saccharomyces uvarum

KW - Sup35.

U2 - 10.1080/19336896.2016.1204060

DO - 10.1080/19336896.2016.1204060

M3 - Article

VL - 10

SP - 269

EP - 282

JO - Prion

JF - Prion

SN - 1933-6896

IS - 4

ER -

ID: 7573300