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Probing the influence of mutations on FUS condensates, one molecule at a time
Protein aggregation and phase separation appear to play important roles in diseases like amyotrophic lateral sclerosis (ALS) and frontotemporal lobar dementia (FTLD), but the interplay between different participating molecular events-which may facilitate or inhibit one another-can be difficult to st...
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Formato: | Online Artículo Texto |
Lenguaje: | English |
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Nature Publishing Group UK
2021
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Acceso en línea: | https://www.ncbi.nlm.nih.gov/pmc/articles/PMC7782781/ https://www.ncbi.nlm.nih.gov/pubmed/33398047 http://dx.doi.org/10.1038/s42003-020-01560-6 |
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author | Chattopadhyay, Krishnananda |
author_facet | Chattopadhyay, Krishnananda |
author_sort | Chattopadhyay, Krishnananda |
collection | PubMed |
description | Protein aggregation and phase separation appear to play important roles in diseases like amyotrophic lateral sclerosis (ALS) and frontotemporal lobar dementia (FTLD), but the interplay between different participating molecular events-which may facilitate or inhibit one another-can be difficult to study by conventional ensemble methods. In a recent study, Kevin Rhine and co-workers make use of point mutations to demonstrate the contrasting behaviour of condensates arising from Glycine and Arginine FUS mutants using single molecules fluorescence measurements. |
format | Online Article Text |
id | pubmed-7782781 |
institution | National Center for Biotechnology Information |
language | English |
publishDate | 2021 |
publisher | Nature Publishing Group UK |
record_format | MEDLINE/PubMed |
spelling | pubmed-77827812021-01-11 Probing the influence of mutations on FUS condensates, one molecule at a time Chattopadhyay, Krishnananda Commun Biol Research Highlight Protein aggregation and phase separation appear to play important roles in diseases like amyotrophic lateral sclerosis (ALS) and frontotemporal lobar dementia (FTLD), but the interplay between different participating molecular events-which may facilitate or inhibit one another-can be difficult to study by conventional ensemble methods. In a recent study, Kevin Rhine and co-workers make use of point mutations to demonstrate the contrasting behaviour of condensates arising from Glycine and Arginine FUS mutants using single molecules fluorescence measurements. Nature Publishing Group UK 2021-01-04 /pmc/articles/PMC7782781/ /pubmed/33398047 http://dx.doi.org/10.1038/s42003-020-01560-6 Text en © The Author(s) 2021 Open Access This article is licensed under a Creative Commons Attribution 4.0 International License, which permits use, sharing, adaptation, distribution and reproduction in any medium or format, as long as you give appropriate credit to the original author(s) and the source, provide a link to the Creative Commons license, and indicate if changes were made. The images or other third party material in this article are included in the article’s Creative Commons license, unless indicated otherwise in a credit line to the material. If material is not included in the article’s Creative Commons license and your intended use is not permitted by statutory regulation or exceeds the permitted use, you will need to obtain permission directly from the copyright holder. To view a copy of this license, visit http://creativecommons.org/licenses/by/4.0/. |
spellingShingle | Research Highlight Chattopadhyay, Krishnananda Probing the influence of mutations on FUS condensates, one molecule at a time |
title | Probing the influence of mutations on FUS condensates, one molecule at a time |
title_full | Probing the influence of mutations on FUS condensates, one molecule at a time |
title_fullStr | Probing the influence of mutations on FUS condensates, one molecule at a time |
title_full_unstemmed | Probing the influence of mutations on FUS condensates, one molecule at a time |
title_short | Probing the influence of mutations on FUS condensates, one molecule at a time |
title_sort | probing the influence of mutations on fus condensates, one molecule at a time |
topic | Research Highlight |
url | https://www.ncbi.nlm.nih.gov/pmc/articles/PMC7782781/ https://www.ncbi.nlm.nih.gov/pubmed/33398047 http://dx.doi.org/10.1038/s42003-020-01560-6 |
work_keys_str_mv | AT chattopadhyaykrishnananda probingtheinfluenceofmutationsonfuscondensatesonemoleculeatatime |