Structure of the Dual Enzyme Ire1 Reveals the Basis for Catalysis and Regulation in Nonconventional RNA Splicing
Top Cited Papers
- 1 January 2008
- Vol. 132 (1) , 89-100
- https://doi.org/10.1016/j.cell.2007.10.057
Abstract
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This publication has 44 references indexed in Scilit:
- Signal integration in the endoplasmic reticulum unfolded protein responseNature Reviews Molecular Cell Biology, 2007
- The Differentiation and Stress Response Factor XBP-1 Drives Multiple Myeloma PathogenesisCancer Cell, 2007
- Patterns of somatic mutation in human cancer genomesNature, 2007
- The crystal structure of human IRE1 luminal domain reveals a conserved dimerization interface required for activation of the unfolded protein responseProceedings of the National Academy of Sciences, 2006
- IRE1 couples endoplasmic reticulum load to secretory capacity by processing the XBP-1 mRNANature, 2002
- XBP1 mRNA Is Induced by ATF6 and Spliced by IRE1 in Response to ER Stress to Produce a Highly Active Transcription FactorCell, 2001
- tRNA Ligase Is Required for Regulated mRNA Splicing in the Unfolded Protein ResponseCell, 1996
- Threading a database of protein coresProteins-Structure Function and Bioinformatics, 1995
- A transmembrane protein with a cdc 2+ CDC 28 - related kinase activity is required for signaling from the ER to the nucleusPublished by Elsevier ,1993
- Transcriptional induction of genes encoding endoplasmic reticulum resident proteins requires a transmembrane protein kinaseCell, 1993