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http://purl.uniprot.org/citations/22796463http://www.w3.org/1999/02/22-rdf-syntax-ns#typehttp://purl.uniprot.org/core/Journal_Citation
http://purl.uniprot.org/citations/22796463http://www.w3.org/1999/02/22-rdf-syntax-ns#typehttp://purl.uniprot.org/core/Journal_Citation
http://purl.uniprot.org/citations/22796463http://www.w3.org/2000/01/rdf-schema#comment"The unfolded protein response (UPR) activates a set of genes to overcome accumulation of unfolded proteins in the endoplasmic reticulum (ER), a condition termed ER stress, and constitutes an essential part of ER protein quality control that ensures efficient maturation of secretory and membrane proteins in eukaryotes. Recent studies on Arabidopsis and rice identified the signaling pathway in which the ER membrane-localized ribonuclease IRE1 (inositol-requiring enzyme 1) catalyzes unconventional cytoplasmic splicing of mRNA, thereby producing the active transcription factor Arabidopsis bZIP60 (basic leucine zipper 60) and its ortholog in rice. Here we review recent findings identifying the molecular components of the plant UPR, including IRE1/bZIP60 and the membrane-bound transcription factors bZIP17 and bZIP28, and implicating its importance in several physiological phenomena such as pathogen response."xsd:string
http://purl.uniprot.org/citations/22796463http://purl.org/dc/terms/identifier"doi:10.1016/j.tplants.2012.06.014"xsd:string
http://purl.uniprot.org/citations/22796463http://purl.org/dc/terms/identifier"doi:10.1016/j.tplants.2012.06.014"xsd:string
http://purl.uniprot.org/citations/22796463http://purl.uniprot.org/core/author"Iwata Y."xsd:string
http://purl.uniprot.org/citations/22796463http://purl.uniprot.org/core/author"Iwata Y."xsd:string
http://purl.uniprot.org/citations/22796463http://purl.uniprot.org/core/author"Koizumi N."xsd:string
http://purl.uniprot.org/citations/22796463http://purl.uniprot.org/core/author"Koizumi N."xsd:string
http://purl.uniprot.org/citations/22796463http://purl.uniprot.org/core/date"2012"xsd:gYear
http://purl.uniprot.org/citations/22796463http://purl.uniprot.org/core/date"2012"xsd:gYear
http://purl.uniprot.org/citations/22796463http://purl.uniprot.org/core/name"Trends Plant Sci."xsd:string
http://purl.uniprot.org/citations/22796463http://purl.uniprot.org/core/name"Trends Plant Sci."xsd:string
http://purl.uniprot.org/citations/22796463http://purl.uniprot.org/core/pages"720-727"xsd:string
http://purl.uniprot.org/citations/22796463http://purl.uniprot.org/core/pages"720-727"xsd:string
http://purl.uniprot.org/citations/22796463http://purl.uniprot.org/core/title"Plant transducers of the endoplasmic reticulum unfolded protein response."xsd:string
http://purl.uniprot.org/citations/22796463http://purl.uniprot.org/core/title"Plant transducers of the endoplasmic reticulum unfolded protein response."xsd:string
http://purl.uniprot.org/citations/22796463http://purl.uniprot.org/core/volume"17"xsd:string
http://purl.uniprot.org/citations/22796463http://purl.uniprot.org/core/volume"17"xsd:string
http://purl.uniprot.org/citations/22796463http://www.w3.org/2004/02/skos/core#exactMatchhttp://purl.uniprot.org/pubmed/22796463
http://purl.uniprot.org/citations/22796463http://www.w3.org/2004/02/skos/core#exactMatchhttp://purl.uniprot.org/pubmed/22796463
http://purl.uniprot.org/citations/22796463http://xmlns.com/foaf/0.1/primaryTopicOfhttps://pubmed.ncbi.nlm.nih.gov/22796463
http://purl.uniprot.org/citations/22796463http://xmlns.com/foaf/0.1/primaryTopicOfhttps://pubmed.ncbi.nlm.nih.gov/22796463
http://purl.uniprot.org/uniprot/Q9C5S2http://purl.uniprot.org/core/citationhttp://purl.uniprot.org/citations/22796463
http://purl.uniprot.org/uniprot/Q93VJ2http://purl.uniprot.org/core/citationhttp://purl.uniprot.org/citations/22796463