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c‐IAP1 and UbcH5 promote K11‐linked polyubiquitination of RIP1 in TNF signalling
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Citations
Cites
RING Domain E3 Ubiquitin Ligases
Deshaies, R. J., & Joazeiro, C. A. P. (2009) · Annual Review of Biochemistry · doi:10.1146/annurev.biochem.78.101807.093809 · Cited by 2,679
IAP proteins: blocking the road to death's door
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IAP Antagonists Induce Autoubiquitination of c-IAPs, NF-κB Activation, and TNFα-Dependent Apoptosis
Varfolomeev, E., Blankenship, J. W., Wayson, S. M., Fedorova, A. V., Kayagaki, N., Garg, P., Zobel, K., Dynek, J. N., Elliott, L. O., Wallweber, H. J. A., et al. (2007) · Cell · doi:10.1016/j.cell.2007.10.030 · Cited by 1,218 · cited 6×
“NIK protein levels decreased drastically upon co-expression with either c-IAP1 or c-IAP2, as shown previously (Varfolomeev et al, 2007).”
BackgroundMethodInfluentialBoth cIAP1 and cIAP2 regulate TNFα-mediated NF-κB activation
Mahoney, D. J., Cheung, H. H., Mrad, R. L., Plenchette, S., Simard, C., Enwere, E., Arora, V., Mak, T. W., Lacasse, E. C., Waring, J., et al. (2008) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.0711122105 · Cited by 540
Ubiquitination of RIP Is Required for Tumor Necrosis Factor α-induced NF-κB Activation
Li, H., Kobayashi, M., Blonska, M., You, Y., & Lin, X. (2006) · Journal of Biological Chemistry · doi:10.1074/jbc.m600620200 · Cited by 277
Cited by
Komander, D., & Rape, M. (2012) · Annual Review of Biochemistry · doi:10.1146/annurev-biochem-060310-170328 · Cited by 3,679
Regulation of tumour necrosis factor signalling: live or let die
Brenner, D., Blaser, H., & Mak, T. W. (2015) · Nature Reviews Immunology · doi:10.1038/nri3834 · Cited by 998
Linear ubiquitination prevents inflammation and regulates immune signalling
Gerlach, B., Cordier, S. M., Schmukle, A. C., Emmerich, C. H., Rieser, E., Haas, T. L., Webb, A. I., Rickard, J. A., Anderton, H., Wong, W. W.-L., et al. (2011) · Nature · doi:10.1038/nature09816 · Cited by 940
Targeting IAP proteins for therapeutic intervention in cancer
Fulda, S., & Vucic, D. (2012) · Nature Reviews Drug Discovery · doi:10.1038/nrd3627 · Cited by 837
Self-citationSHARPIN forms a linear ubiquitin ligase complex regulating NF-κB activity and apoptosis
Ikeda, F., Deribe, Y. L., Skånland, S. S., Stieglitz, B., Grabbe, C., Franz-Wachtel, M., van Wijk, S. J. L., Goswami, P., Nagy, V., Terzic, J., et al. (2011) · Nature · doi:10.1038/nature09814 · Cited by 745
Atypical ubiquitylation — the unexplored world of polyubiquitin beyond Lys48 and Lys63 linkages
Kulathu, Y., & Komander, D. (2012) · Nature Reviews Molecular Cell Biology · doi:10.1038/nrm3394 · Cited by 619
The IκB kinase complex in NF‐κB regulation and beyond
Hinz, M., & Scheidereit, C. (2014) · The EMBO Reports · doi:10.1002/embr.201337983 · Cited by 572
Kinase inhibition in autoimmunity and inflammation
Zarrin, A. A., Bao, K., Lupardus, P., & Vucic, D. (2021) · Nature Reviews Drug Discovery · doi:10.1038/s41573-020-0082-8 · Cited by 431
Self-citationOxidative stress, neurodegeneration, and the balance of protein degradation and protein synthesis
Dasuri, K., Zhang, L., & Keller, J. N. (2013) · Free Radical Biology and Medicine · doi:10.1016/j.freeradbiomed.2012.09.016 · Cited by 371
Dondelinger, Y., Aguileta, M. A., Goossens, V, Dubuisson, C., Grootjans, S., Dejardin, E., Vandenabeele, P., & Bertrand, M. J. M. (2013) · Cell Death & Differentiation · doi:10.1038/cdd.2013.94 · Cited by 312
TBK1 and IKKε prevent TNF-induced cell death by RIPK1 phosphorylation
Lafont, E., Draber, P., Rieser, E., Reichert, M., Kupka, S., de Miguel, D., Draberova, H., von Mässenhausen, A., Bhamra, A., Henderson, S., et al. (2018) · Nature Cell Biology · doi:10.1038/s41556-018-0229-6 · Cited by 283
Regulation of NF-κB by ubiquitination
Chen, J., & Chen, Z. J. (2013) · Current Opinion in Immunology · doi:10.1016/j.coi.2012.12.005 · Cited by 258
Flygare, J. A., Beresini, M., Budha, N., Chan, H., Chan, I. T., Cheeti, S., Cohen, F., Deshayes, K., Doerner, K., Eckhardt, S. G., et al. (2012) · Journal of Medicinal Chemistry · doi:10.1021/jm300060k · Cited by 252
Self-citationUbiquitin in the immune system
Zinngrebe, J., Montinaro, A., Peltzer, N., & Walczak, H. (2014) · The EMBO Reports · doi:10.1002/embr.201338025 · Cited by 227
Poly-ubiquitination in TNFR1-mediated necroptosis
Dondelinger, Y., Darding, M., Bertrand, M. J. M., & Walczak, H. (2016) · Cellular and Molecular Life Sciences · doi:10.1007/s00018-016-2191-4 · Cited by 173
Linear ubiquitination at a glance
Spit, M., Rieser, E., & Walczak, H. (2019) · Journal of Cell Science · doi:10.1242/jcs.208512 · Cited by 94
YOD1/TRAF6 association balances p62-dependent IL-1 signaling to NF-κB
Schimmack, G., Schorpp, K., Kutzner, K., Gehring, T., Brenke, J. K., Hadian, K., & Krappmann, D. (2017) · eLife · doi:10.7554/elife.22416 · Cited by 84
NEMO Links Nuclear Factor-κB to Human Diseases
Maubach, G., Schmädicke, A.-C., & Naumann, M. (2017) · Trends in Molecular Medicine · doi:10.1016/j.molmed.2017.10.004 · Cited by 77
Both K63 and K48 ubiquitin linkages signal lysosomal degradation of the LDL receptor
Zhang, L., Xu, M., Scotti, E., Chen, Z. J., & Tontonoz, P. (2013) · Journal of Lipid Research · doi:10.1194/jlr.m035774 · Cited by 60
Metadata
- Authors
- Dynek, J. N., Goncharov, T., Dueber, E. C., Fedorova, A. V., Izrael‐Tomasevic, A., Phu, L., Helgason, E., Fairbrother, W. J., Deshayes, K., Kirkpatrick, D. S., & Vucic, D.
- Venue
- The EMBO Journal
- Published
- 2010-11-26
- Volume
- 29
- Issue
- 24
- Pages
- 4198-4209
- ISSN
- 0261-4189 (ISSN-L)
- 1460-2075
- OpenAlex
- W2097724407
- Cited by
- 352
- References
- 5
- FWCI
- 9.21
- Type
- journal article
- Language
- en
- Open access
- bronze
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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.
