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Role of self-organising myddosome oligomers in inflammatory signalling by Toll-like receptors
A paper published in BMC Biology characterises biophysically oligomeric and filamentous structures formed spontaneously by the Toll-like receptor signalling adaptor MyD88. Naturally occurring mutants of MyD88 that cause immunodeficiency are unable to form these structures. By contrast a somatic muta...
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Formato: | Online Artículo Texto |
Lenguaje: | English |
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BioMed Central
2019
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Acceso en línea: | https://www.ncbi.nlm.nih.gov/pmc/articles/PMC6383289/ https://www.ncbi.nlm.nih.gov/pubmed/30786893 http://dx.doi.org/10.1186/s12915-019-0637-5 |
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author | Gay, Nicholas J. |
author_facet | Gay, Nicholas J. |
author_sort | Gay, Nicholas J. |
collection | PubMed |
description | A paper published in BMC Biology characterises biophysically oligomeric and filamentous structures formed spontaneously by the Toll-like receptor signalling adaptor MyD88. Naturally occurring mutants of MyD88 that cause immunodeficiency are unable to form these structures. By contrast a somatic mutant that promotes the survival of tumour cells forms oligomers much more readily than the wild-type protein. These findings suggest that assembly of oligomeric MyD88 is critical for the regulation of inflammatory signalling. |
format | Online Article Text |
id | pubmed-6383289 |
institution | National Center for Biotechnology Information |
language | English |
publishDate | 2019 |
publisher | BioMed Central |
record_format | MEDLINE/PubMed |
spelling | pubmed-63832892019-03-01 Role of self-organising myddosome oligomers in inflammatory signalling by Toll-like receptors Gay, Nicholas J. BMC Biol Commentary A paper published in BMC Biology characterises biophysically oligomeric and filamentous structures formed spontaneously by the Toll-like receptor signalling adaptor MyD88. Naturally occurring mutants of MyD88 that cause immunodeficiency are unable to form these structures. By contrast a somatic mutant that promotes the survival of tumour cells forms oligomers much more readily than the wild-type protein. These findings suggest that assembly of oligomeric MyD88 is critical for the regulation of inflammatory signalling. BioMed Central 2019-02-20 /pmc/articles/PMC6383289/ /pubmed/30786893 http://dx.doi.org/10.1186/s12915-019-0637-5 Text en © The Author(s). 2019 Open AccessThis article is distributed under the terms of the Creative Commons Attribution 4.0 International License (http://creativecommons.org/licenses/by/4.0/), which permits unrestricted use, distribution, and reproduction in any medium, provided 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 Creative Commons Public Domain Dedication waiver (http://creativecommons.org/publicdomain/zero/1.0/) applies to the data made available in this article, unless otherwise stated. |
spellingShingle | Commentary Gay, Nicholas J. Role of self-organising myddosome oligomers in inflammatory signalling by Toll-like receptors |
title | Role of self-organising myddosome oligomers in inflammatory signalling by Toll-like receptors |
title_full | Role of self-organising myddosome oligomers in inflammatory signalling by Toll-like receptors |
title_fullStr | Role of self-organising myddosome oligomers in inflammatory signalling by Toll-like receptors |
title_full_unstemmed | Role of self-organising myddosome oligomers in inflammatory signalling by Toll-like receptors |
title_short | Role of self-organising myddosome oligomers in inflammatory signalling by Toll-like receptors |
title_sort | role of self-organising myddosome oligomers in inflammatory signalling by toll-like receptors |
topic | Commentary |
url | https://www.ncbi.nlm.nih.gov/pmc/articles/PMC6383289/ https://www.ncbi.nlm.nih.gov/pubmed/30786893 http://dx.doi.org/10.1186/s12915-019-0637-5 |
work_keys_str_mv | AT gaynicholasj roleofselforganisingmyddosomeoligomersininflammatorysignallingbytolllikereceptors |