Por favor, use este identificador para citar o enlazar este ítem:
https://doi.org/10.1038/s41467-018-07573-4
![](/digitum/image/email_logo.png)
![](/digitum/image/logo-facebook.png)
Registro completo de metadatos
Campo DC | Valor | Lengua/Idioma |
---|---|---|
dc.contributor.author | Hafner-Bratkovic, Iva | - |
dc.contributor.author | Susjan, Petra | - |
dc.contributor.author | Lainscek, Dusko | - |
dc.contributor.author | Tapia-Abellán, Ana | - |
dc.contributor.author | Cerovic, Kosta | - |
dc.contributor.author | Kadunc, Lucija | - |
dc.contributor.author | Angosto-Bazarra, Diego | - |
dc.contributor.author | Pelegrin, Pablo | - |
dc.contributor.author | Jerala, Roman | - |
dc.contributor.other | Facultades, Departamentos, Servicios y Escuelas::Departamentos de la UMU::Bioquímica y Biología Molecular B e Inmunología | - |
dc.date.accessioned | 2024-01-30T11:18:40Z | - |
dc.date.available | 2024-01-30T11:18:40Z | - |
dc.date.issued | 2018 | - |
dc.identifier.citation | Nature Communications, volumen 9, nº 1, año 2018, número de artículo 5182 (18 páginas). | es |
dc.identifier.uri | http://hdl.handle.net/10201/138131 | - |
dc.description | ©2018. This manuscript version is made available under the CC-BY-NC-ND 4.0 license http://creativecommons.org/licenses/by-nc-nd/4.0/ This document is the Accepted, version of a Published Work that appeared in final form in Nature Communications. To access the final edited and published work see https://doi.org/10.1038/s41467-018-07573-4 | - |
dc.description.abstract | NLRP3 is a cytosolic sensor triggered by different pathogen- and self-derived signals that plays a central role in a variety of pathological conditions, including sterile inflammation. The leucine- rich repeat domain is present in several innate immune receptors, where it is frequently responsible for sensing danger signals and regulation of activation. We show by reconstitution of truncated and chimeric variants into NLRP3-/- macrophages that the leucine-rich repeat domain is dispensable for activation and self-regulation of NLRP3 by several different triggers. The pyrin domain on the other hand is required to maintain NLRP3 in the inactive conformation. A fully responsive minimal NLRP3 truncation variant reconstituted peritonitis in NLRP3-/- mice. We demonstrate that in contrast to pathogen-activated NLRC4, the constitutively active NLRP3 molecule cannot engage wild-type NLRP3 molecules in a self-catalytic oligomerization. This lack of signal amplification is likely a protective mechanism to decrease sensitivity to endogenous triggers to impede autoinflammation. | es |
dc.format | application/pdf | es |
dc.format.extent | 48 | es |
dc.language | eng | es |
dc.publisher | Nature | es |
dc.relation | Slovenian Research Agency (J3-5503, J3-6791), Instituto Salud Carlos III–Fondo Europeo de Desarrollo Regional (PI13/00174), European Research Council (ERC-2013- CoG 614578), COST Action BM-1406. | es |
dc.rights | info:eu-repo/semantics/openAccess | es |
dc.rights | Attribution-NonCommercial-NoDerivatives 4.0 Internacional | * |
dc.rights.uri | http://creativecommons.org/licenses/by-nc-nd/4.0/ | * |
dc.subject | Interleukin-1β | es |
dc.subject | Macrophage | es |
dc.subject | Inflammasome | es |
dc.subject | NLRP3 | es |
dc.subject | Inflammation | es |
dc.subject.other | CDU::6 - Ciencias aplicadas | es |
dc.title | NLRP3 lacking the leucine-rich repeat domain can be fully activated via the canonical inflammasome pathway | es |
dc.type | info:eu-repo/semantics/article | es |
dc.relation.publisherversion | https://www.nature.com/articles/s41467-018-07573-4 | es |
dc.identifier.doi | https://doi.org/10.1038/s41467-018-07573-4 | - |
Aparece en las colecciones: | Artículos: Bioquímica y Biología Molecular "B" e Inmunología |
Ficheros en este ítem:
Fichero | Descripción | Tamaño | Formato | |
---|---|---|---|---|
suppl 2018 Nat Comm.pdf | Versión aceptada del artículo | 2,49 MB | Adobe PDF | ![]() Visualizar/Abrir |
Este ítem está sujeto a una licencia Creative Commons Licencia Creative Commons