NLRP3 lacking the leucine-rich repeat domain can be fully activated via the canonical inflammasome pathway

Activation of the NLRP3 inflammasome is associated with various diseases but its activation mechanism is not fully understood. Here, the authors determine the impact of different NLRP3 domains on sensing NLRP3 triggers, inflammasome assembly and regulation of NLRP3 inflammasome activation.

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Autores principales:	Iva Hafner-Bratkovič, Petra Sušjan, Duško Lainšček, Ana Tapia-Abellán, Kosta Cerović, Lucija Kadunc, Diego Angosto-Bazarra, Pablo Pelegrin, Roman Jerala
Formato:	article
Lenguaje:	EN
Publicado:	Nature Portfolio 2018
Materias:	Science Q
Acceso en línea:	https://doaj.org/article/1ef3edb735df4712b0a5732ea7fa1100
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spelling	oai:doaj.org-article:1ef3edb735df4712b0a5732ea7fa11002021-12-02T16:49:19ZNLRP3 lacking the leucine-rich repeat domain can be fully activated via the canonical inflammasome pathway10.1038/s41467-018-07573-42041-1723https://doaj.org/article/1ef3edb735df4712b0a5732ea7fa11002018-12-01T00:00:00Zhttps://doi.org/10.1038/s41467-018-07573-4https://doaj.org/toc/2041-1723Activation of the NLRP3 inflammasome is associated with various diseases but its activation mechanism is not fully understood. Here, the authors determine the impact of different NLRP3 domains on sensing NLRP3 triggers, inflammasome assembly and regulation of NLRP3 inflammasome activation.Iva Hafner-BratkovičPetra SušjanDuško LainščekAna Tapia-AbellánKosta CerovićLucija KaduncDiego Angosto-BazarraPablo PelegrinRoman JeralaNature PortfolioarticleScienceQENNature Communications, Vol 9, Iss 1, Pp 1-18 (2018)
institution	DOAJ
collection	DOAJ
language	EN
topic	Science Q
spellingShingle	Science Q Iva Hafner-Bratkovič Petra Sušjan Duško Lainšček Ana Tapia-Abellán Kosta Cerović Lucija Kadunc Diego Angosto-Bazarra Pablo Pelegrin Roman Jerala NLRP3 lacking the leucine-rich repeat domain can be fully activated via the canonical inflammasome pathway
description	Activation of the NLRP3 inflammasome is associated with various diseases but its activation mechanism is not fully understood. Here, the authors determine the impact of different NLRP3 domains on sensing NLRP3 triggers, inflammasome assembly and regulation of NLRP3 inflammasome activation.
format	article
author	Iva Hafner-Bratkovič Petra Sušjan Duško Lainšček Ana Tapia-Abellán Kosta Cerović Lucija Kadunc Diego Angosto-Bazarra Pablo Pelegrin Roman Jerala
author_facet	Iva Hafner-Bratkovič Petra Sušjan Duško Lainšček Ana Tapia-Abellán Kosta Cerović Lucija Kadunc Diego Angosto-Bazarra Pablo Pelegrin Roman Jerala
author_sort	Iva Hafner-Bratkovič
title	NLRP3 lacking the leucine-rich repeat domain can be fully activated via the canonical inflammasome pathway
title_short	NLRP3 lacking the leucine-rich repeat domain can be fully activated via the canonical inflammasome pathway
title_full	NLRP3 lacking the leucine-rich repeat domain can be fully activated via the canonical inflammasome pathway
title_fullStr	NLRP3 lacking the leucine-rich repeat domain can be fully activated via the canonical inflammasome pathway
title_full_unstemmed	NLRP3 lacking the leucine-rich repeat domain can be fully activated via the canonical inflammasome pathway
title_sort	nlrp3 lacking the leucine-rich repeat domain can be fully activated via the canonical inflammasome pathway
publisher	Nature Portfolio
publishDate	2018
url	https://doaj.org/article/1ef3edb735df4712b0a5732ea7fa1100
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NLRP3 lacking the leucine-rich repeat domain can be fully activated via the canonical inflammasome pathway

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