Standard

Identification of new human amyloidogenic proteins. / Zelinsky, Andrey; Romanova, Nina; Kajava, Andrey; Rubel, Aleksandr; Chandramowlishwaran, Pavithra; Chernoff, Yury.

2017. Abstract from EMBO Conference Protein Quality Control: Success and failure in health and disease 2017, Жирона, Spain.

Research output: Contribution to conference › Abstract › peer-review

Harvard

Zelinsky, A, Romanova, N, Kajava, A, Rubel, A, Chandramowlishwaran, P & Chernoff, Y 2017, 'Identification of new human amyloidogenic proteins', EMBO Conference Protein Quality Control: Success and failure in health and disease 2017, Жирона, Spain, 14/05/17 - 19/05/17.

APA

Zelinsky, A., Romanova, N., Kajava, A., Rubel, A., Chandramowlishwaran, P., & Chernoff, Y. (2017). Identification of new human amyloidogenic proteins. Abstract from EMBO Conference Protein Quality Control: Success and failure in health and disease 2017, Жирона, Spain.

Vancouver

Zelinsky A, Romanova N, Kajava A, Rubel A, Chandramowlishwaran P, Chernoff Y. Identification of new human amyloidogenic proteins. 2017. Abstract from EMBO Conference Protein Quality Control: Success and failure in health and disease 2017, Жирона, Spain.

Author

Zelinsky, Andrey ; Romanova, Nina ; Kajava, Andrey ; Rubel, Aleksandr ; Chandramowlishwaran, Pavithra ; Chernoff, Yury. / Identification of new human amyloidogenic proteins. Abstract from EMBO Conference Protein Quality Control: Success and failure in health and disease 2017, Жирона, Spain.

BibTeX

@conference{08a5e29427c34ef2bd9b8d05856a4c98,
title = "Identification of new human amyloidogenic proteins",
abstract = "Amyloids are self-assembled fibrous cross-beta protein aggregates, associated with a variety of human diseases and implicated in some positive biological functions. We have developed a new yeast-based experimental assay for identification of amyloidogenic proteins, and applied this assay to human proteins, that contain cross-beta structures as predicted by in silico algorithm ArchCandy. Our data confirm that at least some of these proteins indeed form amyloids. Specifically, some isoforms of the PHC3 protein, a member of chromatin-modifying complex PRC1, possess amyloidogenic properties. We propose that amyloid formation modulates the function of PRC1 in epigenetic regulation of chromatin. Our data provide a new strategy for identifying biologically important amyloids in human proteome.Authors acknowledge support from RSF (14-50-00069) and from SPbSU Resource Centers “Development of Molecular and CellularTechnologies” and “Biobank”.",
keywords = "амилоиды, дрожжевая модель",
author = "Andrey Zelinsky and Nina Romanova and Andrey Kajava and Aleksandr Rubel and Pavithra Chandramowlishwaran and Yury Chernoff",
note = "Protein quality control: success and failure in health and disease. 14th – 19th May 2017.; EMBO Conference Protein Quality Control: Success and failure in health and disease 2017, EMBO ; Conference date: 14-05-2017 Through 19-05-2017",
year = "2017",
language = "English",

}

RIS

TY - CONF

T1 - Identification of new human amyloidogenic proteins

AU - Zelinsky, Andrey

AU - Romanova, Nina

AU - Kajava, Andrey

AU - Rubel, Aleksandr

AU - Chandramowlishwaran, Pavithra

AU - Chernoff, Yury

N1 - Protein quality control: success and failure in health and disease. 14th – 19th May 2017.

PY - 2017

Y1 - 2017

N2 - Amyloids are self-assembled fibrous cross-beta protein aggregates, associated with a variety of human diseases and implicated in some positive biological functions. We have developed a new yeast-based experimental assay for identification of amyloidogenic proteins, and applied this assay to human proteins, that contain cross-beta structures as predicted by in silico algorithm ArchCandy. Our data confirm that at least some of these proteins indeed form amyloids. Specifically, some isoforms of the PHC3 protein, a member of chromatin-modifying complex PRC1, possess amyloidogenic properties. We propose that amyloid formation modulates the function of PRC1 in epigenetic regulation of chromatin. Our data provide a new strategy for identifying biologically important amyloids in human proteome.Authors acknowledge support from RSF (14-50-00069) and from SPbSU Resource Centers “Development of Molecular and CellularTechnologies” and “Biobank”.

AB - Amyloids are self-assembled fibrous cross-beta protein aggregates, associated with a variety of human diseases and implicated in some positive biological functions. We have developed a new yeast-based experimental assay for identification of amyloidogenic proteins, and applied this assay to human proteins, that contain cross-beta structures as predicted by in silico algorithm ArchCandy. Our data confirm that at least some of these proteins indeed form amyloids. Specifically, some isoforms of the PHC3 protein, a member of chromatin-modifying complex PRC1, possess amyloidogenic properties. We propose that amyloid formation modulates the function of PRC1 in epigenetic regulation of chromatin. Our data provide a new strategy for identifying biologically important amyloids in human proteome.Authors acknowledge support from RSF (14-50-00069) and from SPbSU Resource Centers “Development of Molecular and CellularTechnologies” and “Biobank”.

KW - амилоиды

KW - дрожжевая модель

M3 - Abstract

T2 - EMBO Conference Protein Quality Control: Success and failure in health and disease 2017

Y2 - 14 May 2017 through 19 May 2017

ER -

ID: 49747606