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Structure of the Dual Enzyme Ire1 Reveals the Basis for Catalysis and Regulation in Nonconventional RNA Splicing
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Coot : model-building tools for molecular graphics
Emsley, P., & Cowtan, K. (2004) · Acta Crystallographica Section D Biological Crystallography · doi:10.1107/s0907444904019158 · Cited by 30,571
Mutation of the mouse klotho gene leads to a syndrome resembling ageing
Kuro-o, M., Matsumura, Y., Aizawa, H., Kawaguchi, H., Suga, T., Utsugi, T., Ohyama, Y., Kurabayashi, M., Kaname, T., Kume, E., et al. (1997) · Nature · doi:10.1038/36285 · Cited by 3,837
The differentiation and stress response factor XBP-1 drives multiple myeloma pathogenesis
Carrasco, D. R., Sukhdeo, K., Protopopova, M., Sinha, R., Enos, M., Carrasco, D. E., Zheng, M., Mani, M., Henderson, J., Pinkus, G. S., et al. (2007) · Cancer Cell · doi:10.1016/j.ccr.2007.02.015 · Cited by 414
Cited by
Targeting hypoxia in cancer therapy
Wilson, W. R., & Hay, M. P. (2011) · Nature Reviews Cancer · doi:10.1038/nrc3064 · Cited by 3,172
Mechanisms, regulation and functions of the unfolded protein response
Hetz, C., Zhang, K., & Kaufman, R. J. (2020) · Nature Reviews Molecular Cell Biology · doi:10.1038/s41580-020-0250-z · Cited by 2,666
Endoplasmic Reticulum Stress Sensing in the Unfolded Protein Response
Gardner, B. M., Pincus, D., Gotthardt, K., Gallagher, C. M., & Walter, P. (2013) · Cold Spring Harbor Perspectives in Biology · doi:10.1101/cshperspect.a013169 · Cited by 721
Nucleases: diversity of structure, function and mechanism
Yang, W. (2011) · Quarterly Reviews of Biophysics · doi:10.1017/s0033583510000181 · Cited by 692
Single-cell eQTL mapping identifies cell type–specific genetic control of autoimmune disease
Yazar, S., Alquicira-Hernandez, J., Wing, K., Senabouth, A., Gordon, M. G., Andersen, S., Lu, Q., Rowson, A., Taylor, T. R. P., Clarke, L., et al. (2022) · Science · doi:10.1126/science.abf3041 · Cited by 682
Metadata
- Authors
- Lee, K. P. K., Dey, M., Neculai, D., Cao, C., Dever, T. E., & Sicheri, F.
- Venue
- Cell
- Publisher
- Elsevier BV
- Published
- 2008-01
- Volume
- 132
- Issue
- 1
- Pages
- 89-100
- ISSN
- 0092-8674 (ISSN-L)
- OpenAlex
- W2167095297
- Cited by
- 379
- References
- 3
- FWCI
- 9.72
- Type
- journal article
- Language
- en
- Open access
- bronze
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- CoChat. (2026). Citation check: Structure of the Dual Enzyme Ire1 Reveals the Basis for Catalysis and Regulation in Nonconventional RNA Splicing. https://app.cochat.ai/papers/10.1016/j.cell.2007.10.057
- The paper
- Lee, K. P. K., Dey, M., Neculai, D., Cao, C., Dever, T. E., & Sicheri, F. (2008). Structure of the Dual Enzyme Ire1 Reveals the Basis for Catalysis and Regulation in Nonconventional RNA Splicing. Cell. https://doi.org/10.1016/j.cell.2007.10.057
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Bibliographic data: Semantic Scholar, OpenAlex, Crossref.
Contains information from the Semantic Scholar Academic Graph Datasets, made available under the ODC Attribution License (ODC-BY 1.0).
Semantic Scholar’s data is described in: Kinney, R., et al. (2023). The Semantic Scholar Open Data Platform. arXiv:2301.10140.
