Standard

Structure-based view on [PSI+] prion properties. / Bondarev, S.A.; Zhouravleva, G.A.; Belousov, M.V.; Kajava, A.V.

In: Prion, Vol. 9, No. 3, 2015, p. 190-199.

Research output: Contribution to journal › Article

Harvard

Bondarev, SA, Zhouravleva, GA, Belousov, MV & Kajava, AV 2015, 'Structure-based view on [PSI+] prion properties', Prion, vol. 9, no. 3, pp. 190-199. https://doi.org/10.1080/19336896.2015.1044186

APA

Bondarev, S. A., Zhouravleva, G. A., Belousov, M. V., & Kajava, A. V. (2015). Structure-based view on [PSI+] prion properties. Prion, 9(3), 190-199. https://doi.org/10.1080/19336896.2015.1044186

Vancouver

Bondarev SA, Zhouravleva GA, Belousov MV, Kajava AV. Structure-based view on [PSI+] prion properties. Prion. 2015;9(3):190-199. https://doi.org/10.1080/19336896.2015.1044186

Author

Bondarev, S.A. ; Zhouravleva, G.A. ; Belousov, M.V. ; Kajava, A.V. / Structure-based view on [PSI+] prion properties. In: Prion. 2015 ; Vol. 9, No. 3. pp. 190-199.

BibTeX

@article{86905713fc3a43abbdf4f3380be793f2,
title = "Structure-based view on [PSI+] prion properties",
abstract = "Yeast [PSI+] prion is one of the most suitable and well characterized system for the investigation of the prion phenomenon. However, until recently, the lack of data on the 3D arrangement of Sup35p prion fibrils hindered progress in this area. The recent arrival in this field of new experimental techniques led to the parallel and in-register superpleated β-structure as a consensus model for Sup35p fibrils. Here, we analyzed the effect of amino acid substitutions of the Sup35 protein through the prism of this structural model. Application of a newly developed computational approach, called ArchCandy, gives us a better understanding of the effect caused by mutations on the fibril forming potential of Sup35 protein. This bioinformatics tool can be used for the design of new mutations with desired modification of prion properties. Thus, we provide examples of how today, having progress toward elucidation of the structural arrangement of Sup35p fibrils, researchers can advance more efficiently to a better understa",
keywords = "Amyloid, Asu mutations, EM, NMR, Nuclear magnetic resonance, PNM, Prion, Protein Misfolding, Protein Structure, STEM, Saccharomyces cerevisiae, Superpleated β-Structure, [PSI+], [PSI+] no more, antisupressor mutations, electron microscopy, scanning transmission electron microscopy",
author = "S.A. Bondarev and G.A. Zhouravleva and M.V. Belousov and A.V. Kajava",
year = "2015",
doi = "10.1080/19336896.2015.1044186",
language = "English",
volume = "9",
pages = "190--199",
journal = "Prion",
issn = "1933-6896",
publisher = "Landes Bioscience",
number = "3",

}

RIS

TY - JOUR

T1 - Structure-based view on [PSI+] prion properties

AU - Bondarev, S.A.

AU - Zhouravleva, G.A.

AU - Belousov, M.V.

AU - Kajava, A.V.

PY - 2015

Y1 - 2015

N2 - Yeast [PSI+] prion is one of the most suitable and well characterized system for the investigation of the prion phenomenon. However, until recently, the lack of data on the 3D arrangement of Sup35p prion fibrils hindered progress in this area. The recent arrival in this field of new experimental techniques led to the parallel and in-register superpleated β-structure as a consensus model for Sup35p fibrils. Here, we analyzed the effect of amino acid substitutions of the Sup35 protein through the prism of this structural model. Application of a newly developed computational approach, called ArchCandy, gives us a better understanding of the effect caused by mutations on the fibril forming potential of Sup35 protein. This bioinformatics tool can be used for the design of new mutations with desired modification of prion properties. Thus, we provide examples of how today, having progress toward elucidation of the structural arrangement of Sup35p fibrils, researchers can advance more efficiently to a better understa

AB - Yeast [PSI+] prion is one of the most suitable and well characterized system for the investigation of the prion phenomenon. However, until recently, the lack of data on the 3D arrangement of Sup35p prion fibrils hindered progress in this area. The recent arrival in this field of new experimental techniques led to the parallel and in-register superpleated β-structure as a consensus model for Sup35p fibrils. Here, we analyzed the effect of amino acid substitutions of the Sup35 protein through the prism of this structural model. Application of a newly developed computational approach, called ArchCandy, gives us a better understanding of the effect caused by mutations on the fibril forming potential of Sup35 protein. This bioinformatics tool can be used for the design of new mutations with desired modification of prion properties. Thus, we provide examples of how today, having progress toward elucidation of the structural arrangement of Sup35p fibrils, researchers can advance more efficiently to a better understa

KW - Amyloid

KW - Asu mutations

KW - EM

KW - NMR

KW - Nuclear magnetic resonance

KW - PNM

KW - Prion

KW - Protein Misfolding

KW - Protein Structure

KW - STEM

KW - Saccharomyces cerevisiae

KW - Superpleated β-Structure

KW - [PSI+]

KW - [PSI+] no more

KW - antisupressor mutations

KW - electron microscopy

KW - scanning transmission electron microscopy

U2 - 10.1080/19336896.2015.1044186

DO - 10.1080/19336896.2015.1044186

M3 - Article

VL - 9

SP - 190

EP - 199

JO - Prion

JF - Prion

SN - 1933-6896

IS - 3

ER -

ID: 3932259