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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Main Author: Krishnananda Chattopadhyay
Format: article
Language:EN
Published: Nature Portfolio 2021
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Online Access:https://doaj.org/article/762ae43a100140e2ad6ddda9465b7a31
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spelling oai:doaj.org-article:762ae43a100140e2ad6ddda9465b7a312021-12-02T15:07:32ZProbing the influence of mutations on FUS condensates, one molecule at a time10.1038/s42003-020-01560-62399-3642https://doaj.org/article/762ae43a100140e2ad6ddda9465b7a312021-01-01T00:00:00Zhttps://doi.org/10.1038/s42003-020-01560-6https://doaj.org/toc/2399-3642Protein 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.Krishnananda ChattopadhyayNature PortfolioarticleBiology (General)QH301-705.5ENCommunications Biology, Vol 4, Iss 1, Pp 1-2 (2021)
institution DOAJ
collection DOAJ
language EN
topic Biology (General)
QH301-705.5
spellingShingle Biology (General)
QH301-705.5
Krishnananda Chattopadhyay
Probing the influence of mutations on FUS condensates, one molecule at a time
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 article
author Krishnananda Chattopadhyay
author_facet Krishnananda Chattopadhyay
author_sort Krishnananda Chattopadhyay
title 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_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_sort probing the influence of mutations on fus condensates, one molecule at a time
publisher Nature Portfolio
publishDate 2021
url https://doaj.org/article/762ae43a100140e2ad6ddda9465b7a31
work_keys_str_mv AT krishnanandachattopadhyay probingtheinfluenceofmutationsonfuscondensatesonemoleculeatatime
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