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Application of the Bacterial C-DAG System for Analysis of the Ability of Amyloids to Seed Protein Aggregation In Vitro. / Трубицина, Нина Павловна; Землянко, Ольга Михайловна; Журавлева, Галина Анатольевна; Бондарев, Станислав Александрович.

In: Microbiology (Russian Federation), Vol. 93, No. 5, 30.09.2024, p. 700-702.

Research output: Contribution to journal › Article › peer-review

Harvard

Трубицина, НП, Землянко, ОМ, Журавлева, ГА & Бондарев, СА 2024, 'Application of the Bacterial C-DAG System for Analysis of the Ability of Amyloids to Seed Protein Aggregation In Vitro', Microbiology (Russian Federation), vol. 93, no. 5, pp. 700-702. https://doi.org/10.1134/s0026261723604967

APA

Трубицина, Н. П., Землянко, О. М., Журавлева, Г. А., & Бондарев, С. А. (2024). Application of the Bacterial C-DAG System for Analysis of the Ability of Amyloids to Seed Protein Aggregation In Vitro. Microbiology (Russian Federation), 93(5), 700-702. https://doi.org/10.1134/s0026261723604967

Vancouver

Трубицина НП, Землянко ОМ, Журавлева ГА, Бондарев СА. Application of the Bacterial C-DAG System for Analysis of the Ability of Amyloids to Seed Protein Aggregation In Vitro. Microbiology (Russian Federation). 2024 Sep 30;93(5):700-702. https://doi.org/10.1134/s0026261723604967

Author

Трубицина, Нина Павловна ; Землянко, Ольга Михайловна ; Журавлева, Галина Анатольевна ; Бондарев, Станислав Александрович. / Application of the Bacterial C-DAG System for Analysis of the Ability of Amyloids to Seed Protein Aggregation In Vitro. In: Microbiology (Russian Federation). 2024 ; Vol. 93, No. 5. pp. 700-702.

BibTeX

@article{c77694d59fab42aeababb83d383c16aa,
title = "Application of the Bacterial C-DAG System for Analysis of the Ability of Amyloids to Seed Protein Aggregation In Vitro",
abstract = "Abstract: The search for new amyloid proteins and investigation of their properties, is an actual task, which addressed by using a number of model systems. One of the most popular is the C-DAG approach, based on the analysis of aggregation of the studied proteins on the surface of Escherichia coli cells. According to the original protocol, it can be used to demonstrate one of the characteristic properties of amyloids: the ability to bind the amyloid-specific dye Congo red, exhibiting apple-green birefringence. The C-DAG technique provides also for analysis of the aggregate morphology and their resistance to detergents. In the present work, using Sup35NM as an example, we tested whether the aggregates on the surface of bacterial cells can act as inducers of aggregation of the relevant protein.",
keywords = "Амилоиды, C-DAG, E. coli, Sup35, aggregation kinetics, amyloids",
author = "Трубицина, {Нина Павловна} and Землянко, {Ольга Михайловна} and Журавлева, {Галина Анатольевна} and Бондарев, {Станислав Александрович}",
year = "2024",
month = sep,
day = "30",
doi = "10.1134/s0026261723604967",
language = "English",
volume = "93",
pages = "700--702",
journal = "МИКРОБИОЛОГИЯ",
issn = "0026-3656",
publisher = "Издательство {"}Наука{"}",
number = "5",

}

RIS

TY - JOUR

T1 - Application of the Bacterial C-DAG System for Analysis of the Ability of Amyloids to Seed Protein Aggregation In Vitro

AU - Трубицина, Нина Павловна

AU - Землянко, Ольга Михайловна

AU - Журавлева, Галина Анатольевна

AU - Бондарев, Станислав Александрович

PY - 2024/9/30

Y1 - 2024/9/30

N2 - Abstract: The search for new amyloid proteins and investigation of their properties, is an actual task, which addressed by using a number of model systems. One of the most popular is the C-DAG approach, based on the analysis of aggregation of the studied proteins on the surface of Escherichia coli cells. According to the original protocol, it can be used to demonstrate one of the characteristic properties of amyloids: the ability to bind the amyloid-specific dye Congo red, exhibiting apple-green birefringence. The C-DAG technique provides also for analysis of the aggregate morphology and their resistance to detergents. In the present work, using Sup35NM as an example, we tested whether the aggregates on the surface of bacterial cells can act as inducers of aggregation of the relevant protein.

AB - Abstract: The search for new amyloid proteins and investigation of their properties, is an actual task, which addressed by using a number of model systems. One of the most popular is the C-DAG approach, based on the analysis of aggregation of the studied proteins on the surface of Escherichia coli cells. According to the original protocol, it can be used to demonstrate one of the characteristic properties of amyloids: the ability to bind the amyloid-specific dye Congo red, exhibiting apple-green birefringence. The C-DAG technique provides also for analysis of the aggregate morphology and their resistance to detergents. In the present work, using Sup35NM as an example, we tested whether the aggregates on the surface of bacterial cells can act as inducers of aggregation of the relevant protein.

KW - Амилоиды

KW - C-DAG

KW - E. coli

KW - Sup35

KW - aggregation kinetics

KW - amyloids

UR - https://www.mendeley.com/catalogue/1da7ebc4-e4a2-3cf2-8e40-e3c5e7483253/

U2 - 10.1134/s0026261723604967

DO - 10.1134/s0026261723604967

M3 - Article

VL - 93

SP - 700

EP - 702

JO - МИКРОБИОЛОГИЯ

JF - МИКРОБИОЛОГИЯ

SN - 0026-3656

IS - 5

ER -

ID: 124647881