Publication

Filter Retardation Assay for Detecting and Quantifying Polyglutamine Aggregates Using Lysates

Sin, O., Mata-Cabana, A., Seinstra, R. I. & Nollen, E. A. A., 5-Oct-2018, In : JMIR research protocols. 8, 19, 9 p., 3042.

Research output: Contribution to journalArticleAcademicpeer-review

APA

Sin, O., Mata-Cabana, A., Seinstra, R. I., & Nollen, E. A. A. (2018). Filter Retardation Assay for Detecting and Quantifying Polyglutamine Aggregates Using Lysates. JMIR research protocols, 8(19), [3042]. https://doi.org/10.21769/BioProtoc.3042

Author

Sin, Olga ; Mata-Cabana, Alejandro ; Seinstra, Renée I ; Nollen, Ellen A A. / Filter Retardation Assay for Detecting and Quantifying Polyglutamine Aggregates Using Lysates. In: JMIR research protocols. 2018 ; Vol. 8, No. 19.

Harvard

Sin, O, Mata-Cabana, A, Seinstra, RI & Nollen, EAA 2018, 'Filter Retardation Assay for Detecting and Quantifying Polyglutamine Aggregates Using Lysates', JMIR research protocols, vol. 8, no. 19, 3042. https://doi.org/10.21769/BioProtoc.3042

Standard

Filter Retardation Assay for Detecting and Quantifying Polyglutamine Aggregates Using Lysates. / Sin, Olga; Mata-Cabana, Alejandro; Seinstra, Renée I; Nollen, Ellen A A.

In: JMIR research protocols, Vol. 8, No. 19, 3042, 05.10.2018.

Research output: Contribution to journalArticleAcademicpeer-review

Vancouver

Sin O, Mata-Cabana A, Seinstra RI, Nollen EAA. Filter Retardation Assay for Detecting and Quantifying Polyglutamine Aggregates Using Lysates. JMIR research protocols. 2018 Oct 5;8(19). 3042. https://doi.org/10.21769/BioProtoc.3042


BibTeX

@article{0aa8bc6bd70a405eb9b45649e619e404,
title = "Filter Retardation Assay for Detecting and Quantifying Polyglutamine Aggregates Using Lysates",
abstract = "Protein aggregation is a hallmark of several neurodegenerative diseases and is associated with impaired protein homeostasis. This imbalance is caused by the loss of the protein's native conformation, which ultimately results in its aggregation or abnormal localization within the cell. Using a C. elegans model of polyglutamine diseases, we describe in detail the filter retardation assay, a method that captures protein aggregates in a cellulose acetate membrane and allows its detection and quantification by immunoblotting.",
author = "Olga Sin and Alejandro Mata-Cabana and Seinstra, {Ren{\'e}e I} and Nollen, {Ellen A A}",
year = "2018",
month = "10",
day = "5",
doi = "10.21769/BioProtoc.3042",
language = "English",
volume = "8",
journal = "JMIR research protocols",
issn = "1929-0748",
publisher = "JMIR PUBLICATIONS, INC",
number = "19",

}

RIS

TY - JOUR

T1 - Filter Retardation Assay for Detecting and Quantifying Polyglutamine Aggregates Using Lysates

AU - Sin, Olga

AU - Mata-Cabana, Alejandro

AU - Seinstra, Renée I

AU - Nollen, Ellen A A

PY - 2018/10/5

Y1 - 2018/10/5

N2 - Protein aggregation is a hallmark of several neurodegenerative diseases and is associated with impaired protein homeostasis. This imbalance is caused by the loss of the protein's native conformation, which ultimately results in its aggregation or abnormal localization within the cell. Using a C. elegans model of polyglutamine diseases, we describe in detail the filter retardation assay, a method that captures protein aggregates in a cellulose acetate membrane and allows its detection and quantification by immunoblotting.

AB - Protein aggregation is a hallmark of several neurodegenerative diseases and is associated with impaired protein homeostasis. This imbalance is caused by the loss of the protein's native conformation, which ultimately results in its aggregation or abnormal localization within the cell. Using a C. elegans model of polyglutamine diseases, we describe in detail the filter retardation assay, a method that captures protein aggregates in a cellulose acetate membrane and allows its detection and quantification by immunoblotting.

U2 - 10.21769/BioProtoc.3042

DO - 10.21769/BioProtoc.3042

M3 - Article

VL - 8

JO - JMIR research protocols

JF - JMIR research protocols

SN - 1929-0748

IS - 19

M1 - 3042

ER -

ID: 67725504