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Yeast-based search for new human amyloidogenicproteins. / Romanova, Nina V.; Zelinsky, Andrey A.; Bondarev, Stanislav A.; Chandramowlishwaranb, Pavithra; Deckner, Zachery; Kajava, Andrey V.; Rubel, Aleksandr A.; Chernoff, Yury O.

In: Prion, Vol. 10, No. sup. 1, 18.04.2016.

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

Harvard

Romanova, NV, Zelinsky, AA, Bondarev, SA, Chandramowlishwaranb, P, Deckner, Z, Kajava, AV, Rubel, AA & Chernoff, YO 2016, 'Yeast-based search for new human amyloidogenicproteins', Prion, vol. 10, no. sup. 1. https://doi.org/10.1080/19336896.2016.1162644

APA

Romanova, N. V., Zelinsky, A. A., Bondarev, S. A., Chandramowlishwaranb, P., Deckner, Z., Kajava, A. V., Rubel, A. A., & Chernoff, Y. O. (2016). Yeast-based search for new human amyloidogenicproteins. Prion, 10(sup. 1). https://doi.org/10.1080/19336896.2016.1162644

Vancouver

Romanova NV, Zelinsky AA, Bondarev SA, Chandramowlishwaranb P, Deckner Z, Kajava AV et al. Yeast-based search for new human amyloidogenicproteins. Prion. 2016 Apr 18;10(sup. 1). https://doi.org/10.1080/19336896.2016.1162644

Author

Romanova, Nina V. ; Zelinsky, Andrey A. ; Bondarev, Stanislav A. ; Chandramowlishwaranb, Pavithra ; Deckner, Zachery ; Kajava, Andrey V. ; Rubel, Aleksandr A. ; Chernoff, Yury O. / Yeast-based search for new human amyloidogenicproteins. In: Prion. 2016 ; Vol. 10, No. sup. 1.

BibTeX

@article{2ea33d8a75e74cbc99914723f9e9936a,
title = "Yeast-based search for new human amyloidogenicproteins",
abstract = "Many neurodegenerative diseases are associated with accumulation of toxic, highly structured self-assembled protein aggregates, termed amyloids. Recently emerging evidence indicates that many amyloids possess transmissible (prion-like) properties. In yeast, endogenous prions transmit phenotypically detectable traits. Some amyloid-likeandprion-likeprotein polymers have been linked to biologically positive phenomena. In vitro experiments suggest that many proteins possess amyloidogenic properties. However, formation and propagation of amyloids are difficult to investigate in vivo due to complexity of the human organism. Therefore, we have established a yeast model for studying prion properties of mammalian proteins. We have demonstrated that fusion of a mammalian amyloidogenic protein to the prion domain of the yeast prion protein Sup35 enables such a chimeric construct to nucleate a prion in the absence of any pre-existing prions in the yeast cell. Phenotypic and biochemical detection assays, previously develop",
author = "Romanova, {Nina V.} and Zelinsky, {Andrey A.} and Bondarev, {Stanislav A.} and Pavithra Chandramowlishwaranb and Zachery Deckner and Kajava, {Andrey V.} and Rubel, {Aleksandr A.} and Chernoff, {Yury O.}",
year = "2016",
month = apr,
day = "18",
doi = "10.1080/19336896.2016.1162644",
language = "English",
volume = "10",
journal = "Prion",
issn = "1933-6896",
publisher = "Landes Bioscience",
number = "sup. 1",

}

RIS

TY - JOUR

T1 - Yeast-based search for new human amyloidogenicproteins

AU - Romanova, Nina V.

AU - Zelinsky, Andrey A.

AU - Bondarev, Stanislav A.

AU - Chandramowlishwaranb, Pavithra

AU - Deckner, Zachery

AU - Kajava, Andrey V.

AU - Rubel, Aleksandr A.

AU - Chernoff, Yury O.

PY - 2016/4/18

Y1 - 2016/4/18

N2 - Many neurodegenerative diseases are associated with accumulation of toxic, highly structured self-assembled protein aggregates, termed amyloids. Recently emerging evidence indicates that many amyloids possess transmissible (prion-like) properties. In yeast, endogenous prions transmit phenotypically detectable traits. Some amyloid-likeandprion-likeprotein polymers have been linked to biologically positive phenomena. In vitro experiments suggest that many proteins possess amyloidogenic properties. However, formation and propagation of amyloids are difficult to investigate in vivo due to complexity of the human organism. Therefore, we have established a yeast model for studying prion properties of mammalian proteins. We have demonstrated that fusion of a mammalian amyloidogenic protein to the prion domain of the yeast prion protein Sup35 enables such a chimeric construct to nucleate a prion in the absence of any pre-existing prions in the yeast cell. Phenotypic and biochemical detection assays, previously develop

AB - Many neurodegenerative diseases are associated with accumulation of toxic, highly structured self-assembled protein aggregates, termed amyloids. Recently emerging evidence indicates that many amyloids possess transmissible (prion-like) properties. In yeast, endogenous prions transmit phenotypically detectable traits. Some amyloid-likeandprion-likeprotein polymers have been linked to biologically positive phenomena. In vitro experiments suggest that many proteins possess amyloidogenic properties. However, formation and propagation of amyloids are difficult to investigate in vivo due to complexity of the human organism. Therefore, we have established a yeast model for studying prion properties of mammalian proteins. We have demonstrated that fusion of a mammalian amyloidogenic protein to the prion domain of the yeast prion protein Sup35 enables such a chimeric construct to nucleate a prion in the absence of any pre-existing prions in the yeast cell. Phenotypic and biochemical detection assays, previously develop

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 - sup. 1

ER -

ID: 50884683