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rdf:type |
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lifeskim:mentions |
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pubmed:issue |
1
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pubmed:dateCreated |
2005-1-11
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pubmed:abstractText |
The unfolded protein response (UPR) allows intracellular feedback regulation that adjusts the protein-folding capacity of the endoplasmic reticulum (ER) according to need. The signal from the ER lumen is transmitted by the ER-transmembrane kinase Ire1, which upon activation displays a site-specific endoribonuclease activity. Endonucleolytic cleavage of the intron from the HAC1 mRNA (encoding a UPR-specific transcription factor) is the first step in a nonconventional mRNA splicing pathway; the released exons are then joined by tRNA ligase. Because only the spliced mRNA is translated, splicing is the key regulatory step of the UPR.
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pubmed:commentsCorrections |
http://linkedlifedata.com/resource/pubmed/commentcorrection/15642095-10026192,
http://linkedlifedata.com/resource/pubmed/commentcorrection/15642095-10346810,
http://linkedlifedata.com/resource/pubmed/commentcorrection/15642095-10357823,
http://linkedlifedata.com/resource/pubmed/commentcorrection/15642095-10564271,
http://linkedlifedata.com/resource/pubmed/commentcorrection/15642095-10847680,
http://linkedlifedata.com/resource/pubmed/commentcorrection/15642095-11063255,
http://linkedlifedata.com/resource/pubmed/commentcorrection/15642095-11069889,
http://linkedlifedata.com/resource/pubmed/commentcorrection/15642095-11106749,
http://linkedlifedata.com/resource/pubmed/commentcorrection/15642095-11163209,
http://linkedlifedata.com/resource/pubmed/commentcorrection/15642095-11175748,
http://linkedlifedata.com/resource/pubmed/commentcorrection/15642095-11256944,
http://linkedlifedata.com/resource/pubmed/commentcorrection/15642095-11333017,
http://linkedlifedata.com/resource/pubmed/commentcorrection/15642095-11343907,
http://linkedlifedata.com/resource/pubmed/commentcorrection/15642095-11595189,
http://linkedlifedata.com/resource/pubmed/commentcorrection/15642095-11779464,
http://linkedlifedata.com/resource/pubmed/commentcorrection/15642095-11779465,
http://linkedlifedata.com/resource/pubmed/commentcorrection/15642095-11780124,
http://linkedlifedata.com/resource/pubmed/commentcorrection/15642095-11821395,
http://linkedlifedata.com/resource/pubmed/commentcorrection/15642095-12110171,
http://linkedlifedata.com/resource/pubmed/commentcorrection/15642095-12142265,
http://linkedlifedata.com/resource/pubmed/commentcorrection/15642095-7693513,
http://linkedlifedata.com/resource/pubmed/commentcorrection/15642095-8423809,
http://linkedlifedata.com/resource/pubmed/commentcorrection/15642095-8513503,
http://linkedlifedata.com/resource/pubmed/commentcorrection/15642095-8898193,
http://linkedlifedata.com/resource/pubmed/commentcorrection/15642095-8898194,
http://linkedlifedata.com/resource/pubmed/commentcorrection/15642095-9323131,
http://linkedlifedata.com/resource/pubmed/commentcorrection/15642095-9381177,
http://linkedlifedata.com/resource/pubmed/commentcorrection/15642095-9382810,
http://linkedlifedata.com/resource/pubmed/commentcorrection/15642095-9637683,
http://linkedlifedata.com/resource/pubmed/commentcorrection/15642095-9755171,
http://linkedlifedata.com/resource/pubmed/commentcorrection/15642095-9837962,
http://linkedlifedata.com/resource/pubmed/commentcorrection/15642095-9862963,
http://linkedlifedata.com/resource/pubmed/commentcorrection/15642095-9930704
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pubmed:language |
eng
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pubmed:journal |
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pubmed:citationSubset |
IM
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pubmed:chemical |
http://linkedlifedata.com/resource/pubmed/chemical/Basic-Leucine Zipper Transcription...,
http://linkedlifedata.com/resource/pubmed/chemical/HAC1 protein, S cerevisiae,
http://linkedlifedata.com/resource/pubmed/chemical/IRE1 protein, S cerevisiae,
http://linkedlifedata.com/resource/pubmed/chemical/Membrane Glycoproteins,
http://linkedlifedata.com/resource/pubmed/chemical/Protein-Serine-Threonine Kinases,
http://linkedlifedata.com/resource/pubmed/chemical/RNA, Fungal,
http://linkedlifedata.com/resource/pubmed/chemical/RNA, Messenger,
http://linkedlifedata.com/resource/pubmed/chemical/RNA Ligase (ATP),
http://linkedlifedata.com/resource/pubmed/chemical/Recombinant Fusion Proteins,
http://linkedlifedata.com/resource/pubmed/chemical/Repressor Proteins,
http://linkedlifedata.com/resource/pubmed/chemical/Saccharomyces cerevisiae Proteins,
http://linkedlifedata.com/resource/pubmed/chemical/Transcription Factors
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pubmed:status |
MEDLINE
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pubmed:issn |
1465-6914
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pubmed:author |
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pubmed:issnType |
Electronic
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pubmed:volume |
6
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pubmed:owner |
NLM
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pubmed:authorsComplete |
Y
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pubmed:pagination |
R3
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pubmed:dateRevised |
2009-11-18
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pubmed:meshHeading |
pubmed-meshheading:15642095-Alternative Splicing,
pubmed-meshheading:15642095-Basic-Leucine Zipper Transcription Factors,
pubmed-meshheading:15642095-Computational Biology,
pubmed-meshheading:15642095-Consensus Sequence,
pubmed-meshheading:15642095-Genome, Fungal,
pubmed-meshheading:15642095-Genomics,
pubmed-meshheading:15642095-Membrane Glycoproteins,
pubmed-meshheading:15642095-Oligonucleotide Array Sequence Analysis,
pubmed-meshheading:15642095-Protein-Serine-Threonine Kinases,
pubmed-meshheading:15642095-RNA, Fungal,
pubmed-meshheading:15642095-RNA, Messenger,
pubmed-meshheading:15642095-RNA Ligase (ATP),
pubmed-meshheading:15642095-Recombinant Fusion Proteins,
pubmed-meshheading:15642095-Repressor Proteins,
pubmed-meshheading:15642095-Saccharomyces cerevisiae,
pubmed-meshheading:15642095-Saccharomyces cerevisiae Proteins,
pubmed-meshheading:15642095-Sensitivity and Specificity,
pubmed-meshheading:15642095-Substrate Specificity,
pubmed-meshheading:15642095-Transcription Factors
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pubmed:year |
2005
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pubmed:articleTitle |
Genome-scale approaches for discovering novel nonconventional splicing substrates of the Ire1 nuclease.
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pubmed:affiliation |
Howard Hughes Medical Institute and Department of Biochemistry and Biophysics, University of California at San Francisco, San Francisco, CA 94143-2200, USA. niwa@ucsd.edu
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pubmed:publicationType |
Journal Article,
Research Support, U.S. Gov't, P.H.S.,
Research Support, Non-U.S. Gov't
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