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http://purl.uniprot.org/citations/34387857http://www.w3.org/1999/02/22-rdf-syntax-ns#typehttp://purl.uniprot.org/core/Journal_Citation
http://purl.uniprot.org/citations/34387857http://www.w3.org/2000/01/rdf-schema#comment"Pellino proteins are E3 ubiquitin ligases involved in the innate immune system. Recently, Pellino-2 was reported to modulate the activation of the mouse Nlrp3 inflammasome. We examined the intracellular localization of human Pellino-2 in THP1-derived macrophages during activation with LPS and ATP. We observed that Pellino-2 changed intracellular localization and colocalized with the inflammasome proteins NLRP3 and ASC late in the assembly of the inflammasome. Colocalization with NLRP3 and ASC was also seen in cells maintained in potassium-free medium. The colocalization and inflammasome activation were abrogated by several potassium channel inhibitors, supporting a role for potassium efflux in modulating intracellular localization of Pellino-2. The data suggest that Pellino-2 is essential for mediating the effect of potassium efflux on inflammasome activation."xsd:string
http://purl.uniprot.org/citations/34387857http://purl.org/dc/terms/identifier"doi:10.1002/1873-3468.14176"xsd:string
http://purl.uniprot.org/citations/34387857http://purl.uniprot.org/core/author"Bredrup C."xsd:string
http://purl.uniprot.org/citations/34387857http://purl.uniprot.org/core/author"Bruland O."xsd:string
http://purl.uniprot.org/citations/34387857http://purl.uniprot.org/core/author"Rodahl E."xsd:string
http://purl.uniprot.org/citations/34387857http://purl.uniprot.org/core/author"Cristea I."xsd:string
http://purl.uniprot.org/citations/34387857http://purl.uniprot.org/core/date"2021"xsd:gYear
http://purl.uniprot.org/citations/34387857http://purl.uniprot.org/core/name"FEBS Lett"xsd:string
http://purl.uniprot.org/citations/34387857http://purl.uniprot.org/core/pages"2437-2446"xsd:string
http://purl.uniprot.org/citations/34387857http://purl.uniprot.org/core/title"K+ regulates relocation of Pellino-2 to the site of NLRP3 inflammasome activation in macrophages."xsd:string
http://purl.uniprot.org/citations/34387857http://purl.uniprot.org/core/volume"595"xsd:string
http://purl.uniprot.org/citations/34387857http://www.w3.org/2004/02/skos/core#exactMatchhttp://purl.uniprot.org/pubmed/34387857
http://purl.uniprot.org/citations/34387857http://xmlns.com/foaf/0.1/primaryTopicOfhttps://pubmed.ncbi.nlm.nih.gov/34387857
http://purl.uniprot.org/uniprot/#_Q659D8-mappedCitation-34387857http://www.w3.org/1999/02/22-rdf-syntax-ns#objecthttp://purl.uniprot.org/citations/34387857
http://purl.uniprot.org/uniprot/#_Q9H716-mappedCitation-34387857http://www.w3.org/1999/02/22-rdf-syntax-ns#objecthttp://purl.uniprot.org/citations/34387857
http://purl.uniprot.org/uniprot/#_Q9HAT8-mappedCitation-34387857http://www.w3.org/1999/02/22-rdf-syntax-ns#objecthttp://purl.uniprot.org/citations/34387857
http://purl.uniprot.org/uniprot/Q659D8http://purl.uniprot.org/core/mappedCitationhttp://purl.uniprot.org/citations/34387857
http://purl.uniprot.org/uniprot/Q9HAT8http://purl.uniprot.org/core/mappedCitationhttp://purl.uniprot.org/citations/34387857
http://purl.uniprot.org/uniprot/Q9H716http://purl.uniprot.org/core/mappedCitationhttp://purl.uniprot.org/citations/34387857