Cited by 1,000

The DOI matches its Crossref record; 6 of the 6 references it cites were found in a registry or an index.

Activation of IKK by TNFα Requires Site-Specific Ubiquitination of RIP1 and Polyubiquitin Binding by NEMO

Open access

Ea, Chee-Kwee, Deng, Li, Xia, Zong-Ping, Pineda, Gabriel, Chen, Zhijian J.·2006·Molecular Cell

DOI 10.1016/j.molcel.2006.03.026

Open this paper in CoChat — free account

The claims and statistics of this paper haven’t been checked yet.

Run the check — free, no account needed. It reads the open-access text and checks the sources it cites.

Integrity signals

Registry

Crossref · 10.1016/j.molcel.2006.03.026

Cites

6 of 6 references verified0 citation errors · 0 not checkable

Statistics

Claims the paper makes

The claims and statistics of this paper haven’t been checked yet.

Run the check — free, no account needed. It reads the open-access text and checks the sources it cites.

Self-check

Percentages, sums and reported differences re-computed from the paper’s own numbers.

The self-check needs the paper’s full text.

Toll-like receptor signalling
Akira, S., & Takeda, K. (2004) · Nature reviews. Immunology · doi:10.1038/nri1391 · Cited by 8,312
Structure of the Cul1–Rbx1–Skp1–F boxSkp2 SCF ubiquitin ligase complex
Zheng, N., Schulman, B. A., Song, L., Miller, J. J., Jeffrey, P. D., Wang, P., Chu, C., Koepp, D. M., Elledge, S. J., Pagano, M., et al. (2002) · Nature · doi:10.1038/416703a · Cited by 1,507
Ubiquitin signalling in the NF-κB pathway
Chen, Z. J. (2005) · Nature Cell Biology · doi:10.1038/ncb0805-758 · Cited by 1,184
Self-citation
TNF-Dependent Recruitment of the Protein Kinase RIP to the TNF Receptor-1 Signaling Complex
Hsu, H., Huang, J., Shu, H.-B., Baichwal, V., & Goeddel, D. V. (1996) · Immunity · doi:10.1016/s1074-7613(00)80252-6 · Cited by 1,182
Tumor necrosis factor: a pleiotropic cytokine and therapuetic target
Tracey, M. D., & Cerami, P. D. (1994) · Annual Review of Medicine · doi:10.1146/annurev.med.45.1.491 · Cited by 1,063
A pervasive role of ubiquitin conjugation in activation and termination of IκB kinase pathways
Krappmann, D., & Scheidereit, C. (2005) · The EMBO Reports · doi:10.1038/sj.embor.7400380 · Cited by 128

Show all 6 references

Molecular mechanisms of cell death: recommendations of the nomenclature committee on cell death 2018.
Galluzzi, L., Vitale, I., Aaronson, S. A., Abrams, J. M., Adam, D., Agostinis, P., Alnemri, E. S., Altucci, L., Amelio, I., Andrews, D. W., et al. (2018) · Cell Death & Differentiation · doi:10.1038/s41418-017-0012-4 · Cited by 6,680
Shared Principles in NF-κB Signaling
Hayden, M. S., & Ghosh, S. (2008) · Cell · doi:10.1016/j.cell.2008.01.020 · Cited by 4,494
Molecular definitions of cell death subroutines: recommendations of the Nomenclature Committee on Cell Death 2012
Galluzzi, L., Vitale, I., Abrams, J. M., Alnemri, E. S., Baehrecke, E. H., Blagosklonny, M. V., Dawson, T. M., Dawson, V. L., El-Deiry, W. S., Fulda, S., et al. (2012) · Cell Death & Differentiation · doi:10.1038/cdd.2011.96 · Cited by 2,421
Molecular mechanisms of necroptosis: an ordered cellular explosion
Vandenabeele, P., Galluzzi, L., Vanden Berghe, T., & Kroemer, G. (2010) · Nature Reviews Molecular Cell Biology · doi:10.1038/nrm2970 · Cited by 2,382
Crosstalk in NF-κB Signaling Pathways
Oeckinghaus, A., Hayden, M. S., & Ghosh, S. (2011) · Nature Immunology · doi:10.1038/ni.2065 · Cited by 1,942
NF-κB, the first quarter-century: remarkable progress and outstanding questions
Hayden, M. S., & Ghosh, S. (2012) · Genes & Development · doi:10.1101/gad.183434.111 · Cited by 1,693
The Role of Inflammatory and Anti-Inflammatory Cytokines in the Pathogenesis of Osteoarthritis
Wojdasiewicz, P., Poniatowski, Ł. A., & Szukiewicz, D. (2014) · Mediators of Inflammation · doi:10.1155/2014/561459 · Cited by 1,608
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
Post-translational modifications in signal integration
Deribe, Y. L., Pawson, T., & Dikic, I. (2010) · Nature Structural & Molecular Biology · doi:10.1038/nsmb.1842 · Cited by 876
The emerging complexity of protein ubiquitination
Komander, D. (2009) · Biochemical Society Transactions · doi:10.1042/bst0370937 · Cited by 821
The outs and the ins of sphingosine-1-phosphate in immunity
Spiegel, S., & Milstien, S. (2011) · Nature Reviews Immunology · doi:10.1038/nri2974 · Cited by 810
Post-translational modifications regulating the activity and function of the nuclear factor kappa B pathway
Perkins, N. D. (2006) · Oncogene · doi:10.1038/sj.onc.1209937 · Cited by 674
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
The Signaling Adaptor p62 Is an Important NF-κB Mediator in Tumorigenesis
Duran, A., Linares, J. F., Galvez, A. S., Wikenheiser, K., Flores, J. M., Diaz-Meco, M. T., & Moscat, J. (2008) · Cancer Cell · doi:10.1016/j.ccr.2008.02.001 · Cited by 541
Both 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
Caspase 8 inhibits programmed necrosis by processing CYLD
O’Donnell, M. A., Perez-Jimenez, E., Oberst, A., Ng, A., Massoumi, R., Xavier, R., Green, D. R., & Ting, A. T. (2011) · Nature Cell Biology · doi:10.1038/ncb2362 · Cited by 494
The Role of the Kinases RIP1 and RIP3 in TNF-Induced Necrosis
Vandenabeele, P., Declercq, W., Van Herreweghe, F., & Vanden Berghe, T. (2010) · Science Signaling · doi:10.1126/scisignal.3115re4 · Cited by 482
Dying cells actively regulate adaptive immune responses
Yatim, N., Cullen, S., & Albert, M. L. (2017) · Nature Reviews Immunology · doi:10.1038/nri.2017.9 · Cited by 442
NF-κB-Independent Role of IKKα/IKKβ in Preventing RIPK1 Kinase-Dependent Apoptotic and Necroptotic Cell Death during TNF Signaling
Dondelinger, Y., Jouan-Lanhouet, S., Divert, T., Theatre, E., Bertin, J., Gough, P. J., Giansanti, P., Heck, A. J. R., Dejardin, E., Vandenabeele, P., et al. (2015) · Molecular Cell · doi:10.1016/j.molcel.2015.07.032 · Cited by 431
RIPK1 inhibits ZBP1-driven necroptosis during development
Newton, K., Wickliffe, K. E., Maltzman, A., Dugger, D. L., Strasser, A., Pham, V. C., Lill, J. R., Roose-Girma, M., Warming, S., Solon, M., et al. (2016) · Nature · doi:10.1038/nature20559 · Cited by 390
Regulation of RIPK1 activation by TAK1-mediated phosphorylation dictates apoptosis and necroptosis
Geng, J., Ito, Y., Shi, L., Amin, P., Chu, J., Ouchida, A. T., Mookhtiar, A. K., Zhao, H., Xu, D., Shan, B., et al. (2017) · Nature Communications · doi:10.1038/s41467-017-00406-w · Cited by 325
Novel cross-talk within the IKK family controls innate immunity
Clark, K., Peggie, M., Plater, L., Sorcek, R. J., Young, E. R. R., Madwed, J. B., Hough, J., McIver, E. G., & Cohen, P. (2011) · Biochemical Journal · doi:10.1042/bj20101701 · Cited by 326
CYLD Deubiquitinates RIP1 in the TNFα-Induced Necrosome to Facilitate Kinase Activation and Programmed Necrosis
Moquin, D. M., McQuade, T., & Chan, F. K.-M. (2013) · PLoS ONE · doi:10.1371/journal.pone.0076841 · Cited by 320
RIPK1 ensures intestinal homeostasis by protecting the epithelium against apoptosis
Takahashi, N., Vereecke, L., Bertrand, M. J. M., Duprez, L., Berger, S. B., Divert, T., Gonçalves, A., Sze, M., Gilbert, B., Kourula, S., et al. (2014) · Nature · doi:10.1038/nature13706 · Cited by 318
The E3 ubiquitin ligase Nrdp1 'preferentially' promotes TLR-mediated production of type I interferon
Wang, C., Chen, T., Zhang, J., Yang, M., Li, N., Xu, X., & Cao, X. (2009) · Nature Immunology · doi:10.1038/ni.1742 · Cited by 317
RIPK3 contributes to TNFR1-mediated RIPK1 kinase-dependent apoptosis in conditions of cIAP1/2 depletion or TAK1 kinase inhibition
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
Ubiquitination of RIP1 Regulates an NF-κB-Independent Cell-Death Switch in TNF Signaling
O'Donnell, M. A., Legarda-Addison, D., Skountzos, P., Yeh, W. C., & Ting, A. T. (2007) · Current Biology · doi:10.1016/j.cub.2007.01.027 · Cited by 310
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
Optineurin Negatively Regulates TNFα- Induced NF-κB Activation by Competing with NEMO for Ubiquitinated RIP
Zhu, G., Wu, C.-J., Zhao, Y., & Ashwell, J. D. (2007) · Current Biology · doi:10.1016/j.cub.2007.07.041 · Cited by 282
A Cytoplasmic ATM-TRAF6-cIAP1 Module Links Nuclear DNA Damage Signaling to Ubiquitin-Mediated NF-κB Activation
Hinz, M., Stilmann, M., Arslan, S. Ç., Khanna, K. K., Dittmar, G., & Scheidereit, C. (2010) · Molecular Cell · doi:10.1016/j.molcel.2010.09.008 · Cited by 280
Beyond IκBs: alternative regulation of NF‐KB activity
Neumann, M., & Naumann, M. (2007) · The FASEB Journal · doi:10.1096/fj.06-7615rev · Cited by 267
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
Self-citation
Tumour Necrosis Factor Alpha in Intestinal Homeostasis and Gut Related Diseases
Ruder, B., Atreya, R., & Becker, C. (2019) · International Journal of Molecular Sciences · doi:10.3390/ijms20081887 · Cited by 228
“The IKK complex subsequently phosphorylates the NFκB inhibitor IκB, leading to proteasomal degradation and unmasking of the nuclear localization signal of NFκB family proteins.”
Background
Ubiquitin in the immune system
Zinngrebe, J., Montinaro, A., Peltzer, N., & Walczak, H. (2014) · The EMBO Reports · doi:10.1002/embr.201338025 · Cited by 227
NF-κB-Activating Complex Engaged in Response to EGFR Oncogene Inhibition Drives Tumor Cell Survival and Residual Disease in Lung Cancer
Blakely, C. M., Pazarentzos, E., Olivas, V., Asthana, S., Yan, J. J., Tan, I., Hrustanovic, G., Chan, E., Lin, L., Neel, D. S., et al. (2015) · Cell Reports · doi:10.1016/j.celrep.2015.03.012 · Cited by 204
Structure-guided development of a potent and selective non-covalent active-site inhibitor of USP7.
Lamberto, I., Liu, X., Seo, H.-S., Schauer, N. J., Iacob, R. E., Hu, W., Das, D., Mikhailova, T., Weisberg, E. L., Engen, J. R., et al. (2017) · Cell Chemical Biology · doi:10.1016/j.chembiol.2017.09.003 · Cited by 192
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
Metformin activates chaperone-mediated autophagy and improves disease pathologies in an Alzheimer disease mouse model
Xu, X., Sun, Y., Cen, X., Shan, B., Zhao, Q., Xie, T., Wang, Z., Hou, T., Xue, Y., Zhang, M., et al. (2021) · Protein & Cell · doi:10.1007/s13238-021-00858-3 · Cited by 171
Structural studies of NF-κB signaling
Zheng, C., Yin, Q., & Wu, H. (2011) · Cell Research · doi:10.1038/cr.2010.171 · Cited by 134
The regulation of cancer cell death and metabolism by extracellular matrix attachment
Buchheit, C. L., Rayavarapu, R. R., & Schafer, Z. T. (2012) · Seminars in Cell & Developmental Biology · doi:10.1016/j.semcdb.2012.04.007 · Cited by 115
A20 Ubiquitin Ligase–Mediated Polyubiquitination of RIP1 Inhibits Caspase-8 Cleavage and TRAIL-Induced Apoptosis in Glioblastoma
Bellail, A. C., Olson, J. J., Yang, X., Chen, Z. J., & Hao, C. (2012) · Cancer Discovery · doi:10.1158/2159-8290.cd-11-0172 · Cited by 113
Self-citation
Linear ubiquitination at a glance
Spit, M., Rieser, E., & Walczak, H. (2019) · Journal of Cell Science · doi:10.1242/jcs.208512 · Cited by 94
Location, location, location: A compartmentalized view of TNF-induced necroptotic signaling.
Samson, A. L., Garnish, S. E., Hildebrand, J. M., & Murphy, J. M. (2021) · Science Signaling · doi:10.1126/scisignal.abc6178 · Cited by 82
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
The Autophagy-Initiating Kinase ULK1 Controls RIPK1-Mediated Cell Death
Wu, W., Wang, X., Berleth, N., Deitersen, J., Wallot-Hieke, N., Böhler, P., Schlütermann, D., Stuhldreier, F., Cox, J., Schmitz, K., et al. (2020) · Cell Reports · doi:10.1016/j.celrep.2020.107547 · Cited by 72
Verproside inhibits TNF-α-induced MUC5AC expression through suppression of the TNF-α/NF-κB pathway in human airway epithelial cells
Lee, S. U., Sung, M. H., Ryu, H. W., Lee, J., Kim, H.-S., In, H. J., Ahn, K.-S., Lee, H.-J., Lee, H.-K., Shin, D.-H., et al. (2016) · Cytokine · doi:10.1016/j.cyto.2015.08.262 · Cited by 58
Ubiquitin Specific Protease 21 Is Dispensable for Normal Development, Hematopoiesis and Lymphocyte Differentiation
Pannu, J., Belle, J. I., Förster, M., Duerr, C. U., Shen, S., Kane, L., Harcourt, K., Fritz, J. H., Clare, S., & Nijnik, A. (2015) · PLOS ONE · doi:10.1371/journal.pone.0117304 · Cited by 37
TAB2 Scaffolds TAK1 and NLK in Repressing Canonical Wnt Signaling
Li, M., Wang, H., Huang, T., Wang, J., Ding, Y., Li, Z., Zhang, J., & Li, L. (2010) · Journal of Biological Chemistry · doi:10.1074/jbc.m109.083246 · Cited by 32
The API2–MALT1 fusion exploits TNFR pathway-associated RIP1 ubiquitination to promote oncogenic NF-κB signaling
Rosebeck, S., Rehman, A. O., Apel, I. J., Kohrt, D., Appert, A., O'Donnell, M. A., Ting, A. T., Du, M.-Q., Baens, M., Lucas, P. C., et al. (2014) · Oncogene · doi:10.1038/onc.2013.195 · Cited by 27
Cell-Penetrable Peptide-Conjugated FADD Induces Apoptosis and Regulates Inflammatory Signaling in Cancer Cells
Ranjan, K., Waghela, B. N., Vaidya, F. U., & Pathak, C. (2020) · International Journal of Molecular Sciences · doi:10.3390/ijms21186890 · Cited by 24
Immunogenic cell death mediated TLR3/4-activated MSCs in U87 GBM cell line
Emami Meybodi, S. M., Moradi Moraddahande, F., & Dehghani Firoozabadi, A. (2024) · Heliyon · doi:10.1016/j.heliyon.2024.e29858 · Cited by 3

Authors: Ea, C.-K., Deng, L., Xia, Z.-P., Pineda, G., & Chen, Z. J.
Venue: Molecular Cell
Publisher: Elsevier BV
Published: 2006-04
Volume: 22
Issue: 2
Pages: 245-257
ISSN: 1097-2765 (ISSN-L)
DOI: 10.1016/j.molcel.2006.03.026
OpenAlex: W2045991166
Cited by: 1,000
References: 6
FWCI: 21.17
Type: journal article
Language: en
Open access: bronze

About these checks

Registry, retraction, Cites and statistics results are computed, not judged, with one exception: a printed reference that no index lists is read once by a model before it counts as a citation error. Claims are extracted by a model and kept only when their quote appears verbatim in the text; each cited source is then checked, with a model’s help, for whether it says what the claim relies on. Those verdicts can be wrong — read the claim’s quote and the cited source before relying on one.

Statistics and arithmetic are recomputed, not judged.

Confidence bands are shown only for fields calibrated on our annotated test set. None is calibrated yet, so no band is shown.

What counts as a claim ›How we measure confidence ›How we check this ›

Are you an author, or do you see a problem with this page? Request a review

Data sources

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.

Activation of IKK by TNFα Requires Site-Specific Ubiquitination of RIP1 and Polyubiquitin Binding by NEMO

Overview

Integrity signals

Verification

Claims the paper makes

Self-check

Citations

Cites

Cited by

Metadata

Record

About these checks

Data sources