The DOI matches its Crossref record; 48 of the 48 references it cites were found in a registry or an index.
CYLD Deubiquitinates RIP1 in the TNFα-Induced Necrosome to Facilitate Kinase Activation and Programmed Necrosis
Open accessAbstract
BACKGROUND: Necroptosis/programmed necrosis is initiated by a macro-molecular protein complex termed the necrosome. Receptor interacting protein kinase 1 (RIPK1/RIP1) and RIP3 are key components of the necrosome. TNFα is a prototypic inducer of necrosome activation, and it is widely believed that deubiquitination of RIP1 at the TNFR-1 signaling complex precedes transition of RIP1 into the cytosol where it forms the RIP1-RIP3 necrosome. Cylindromatosis (CYLD) is believed to promote programmed necrosis by facilitating RIP1 deubiquitination at this membrane receptor complex. METHODOLOGY/PRINCIPAL FINDINGS: We demonstrate that RIP1 is indeed the primary target of CYLD in TNFα-induced programmed necrosis. We observed that CYLD does not regulate RIP1 ubiquitination at the TNF receptor. TNF and zVAD-induced programmed necrosis was highly attenuated in CYLD(-/-) cells. However, in the presence of cycloheximide or SMAC mimetics, programmed necrosis was only moderately reduced in CYLD(-/-) cells. Under the latter conditions, RIP1-RIP3 necrosome formation is only delayed, but not abolished in CYLD(-/-) cells. We further demonstrate that RIP1 within the NP-40 insoluble necrosome is ubiquitinated and that CYLD regulates RIP1 ubiquitination in this compartment. Hence, RIP1 ubiquitination in this late-forming complex is greatly increased in CYLD(-/-) cells. Increased RIP1 ubiquitination impairs RIP1 and RIP3 phosphorylation, a signature of kinase activation. CONCLUSIONS/SIGNIFICANCE: Our results show that CYLD regulates RIP1 ubiquitination in the TNFα-induced necrosome, but not in the TNFR-1 signaling complex. In cells sensitized to programmed necrosis with SMAC mimetics, CYLD is not essential for necrosome assembly. Since SMAC mimetics induces the loss of the E3 ligases cIAP1 and cIAP2, reduced RIP1 ubiquitination could lead to reduced requirement for CYLD to remove ubiquitin chains from RIP1 in the TNFR-1 complex. As increased RIP1 ubiquitination in the necrosome correlates with impaired RIP1 and RIP3 phosphorylation and function, these results suggest that CYLD controls RIP1 kinase activity during necrosome assembly.
Overview
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
Cites
Statistics
Verification
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.
Claims other papers make about this one
Each is checked against this paper’s own text: does it say what the citing paper says it does?
In the citing paper
“Accordingly, necroptosis relies on the deubiquitinating activity of CYLD [338], which is also a proteolytic target of CASP8 [494–496].”
From Molecular mechanisms of cell death: recommendations of the nomenclature committee on cell death 2018. (2018) · cites this paper as [495]
Self-check
Percentages, sums and reported differences re-computed from the paper’s own numbers.
The self-check needs the paper’s full text.
Citations
Cites
Induction of TNF receptor I-mediated apoptosis via two sequential signaling complexes
Micheau, O., & Tschopp, J. (2003) · Cell · doi:10.1016/s0092-8674(03)00521-x · Cited by 2,738
Mixed Lineage Kinase Domain-like Protein Mediates Necrosis Signaling Downstream of RIP3 Kinase
Sun, L., Wang, H., Wang, Z., He, S., Chen, S., Liao, D., Wang, L., Yan, J., Liu, W., Lei, X., et al. (2012) · Cell · doi:10.1016/j.cell.2011.11.031 · Cited by 2,698
Cho, Y., Challa, S., Moquin, D., Genga, R., Ray, T. D., Guildford, M., & Chan, F. K.-M. (2009) · Cell · doi:10.1016/j.cell.2009.05.037 · Cited by 2,435
Self-citationMolecular 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
Receptor Interacting Protein Kinase-3 Determines Cellular Necrotic Response to TNF-α
He, S., Wang, L., Miao, L., Wang, T., Du, F., Zhao, L., & Wang, X. (2009) · Cell · doi:10.1016/j.cell.2009.05.021 · Cited by 2,214
RIP3, an Energy Metabolism Regulator That Switches TNF-Induced Cell Death from Apoptosis to Necrosis
Zhang, D.-W., Shao, J., Lin, J., Zhang, N., Lu, B.-J., Lin, S.-C., Dong, M.-Q., & Han, J. (2009) · Science · doi:10.1126/science.1172308 · Cited by 1,931
De-ubiquitination and ubiquitin ligase domains of A20 downregulate NF-κB signalling
Wertz, I. E., O’Rourke, K. M., Zhou, H., Eby, M. T., Aravind, L., Seshagiri, S., Wu, P., Wiesmann, C., Baker, R. T., Boone, D. L., et al. (2004) · Nature · doi:10.1038/nature02794 · Cited by 1,889
TNF-α Induces Two Distinct Caspase-8 Activation Pathways
Wang, L., Du, F., & Wang, X. (2008) · Cell · doi:10.1016/j.cell.2008.03.036 · Cited by 1,398
Catalytic activity of the caspase-8–FLIPL complex inhibits RIPK3-dependent necrosis
Oberst, A., Dillon, C. P., Weinlich, R., McCormick, L. L., Fitzgerald, P., Pop, C., Hakem, R., Salvesen, G. S., & Green, D. R. (2011) · Nature · doi:10.1038/nature09852 · Cited by 1,278 · cited 1×
“necrosis during embryonic development [7-9], to enforce”
Li, J., McQuade, T., Siemer, A. B., Napetschnig, J., Moriwaki, K., Hsiao, Y.-S., Damko, E., Moquin, D., Walz, T., McDermott, A., et al. (2012) · Cell · doi:10.1016/j.cell.2012.06.019 · Cited by 1,222
Self-citation
Flagged first, then by citations
Cited by
Sorted by citations
Items 201–300 of 321
Diverse pathways to neuronal necroptosis in Alzheimer's disease
Jayaraman, A., & Reynolds, R. (2022) · European Journal of Neuroscience · doi:10.1111/ejn.15662 · Cited by 21
Tankyrase-mediated ADP-ribosylation is a regulator of TNF-induced death
Liu, L., Sandow, J. J., Pedrioli, D. M. L., Samson, A. L., Silke, N., Kratina, T., Ambrose, R. L., Doerflinger, M., Hu, Z., Morrish, E., et al. (2022) · Science Advances · doi:10.1126/sciadv.abh2332 · Cited by 24
Programmed necrosis and its role in management of breast cancer
Thakur, B., Kumar, Y., & Bhatia, A. (2019) · Pathology - Research and Practice · doi:10.1016/j.prp.2019.152652 · Cited by 21
Tumor-intrinsic and immune modulatory roles of receptor-interacting protein kinases
Rucker, A. J., & Chan, F. K.-M. (2022) · Trends in Biochemical Sciences · doi:10.1016/j.tibs.2021.12.004 · Cited by 20
Self-citationNecroptosis in human cancers with special emphasis on oral squamous cell carcinoma
Krishnan, R. P., Pandiar, D., Ramani, P., & Jayaraman, S. (2023) · Journal of Stomatology Oral and Maxillofacial Surgery · doi:10.1016/j.jormas.2023.101565 · Cited by 21
Zhang, X., Chen, X., Qian, F., Zhu, Y., He, G., Yang, J., Wu, X., Zhang, H., Yu, X., & Liu, X. (2023) · Clinical and Translational Medicine · doi:10.1002/ctm2.1398 · Cited by 20
Emerging Roles for RIPK1 and RIPK3 in Pathogen-Induced Cell Death and Host Immunity
Saleh, D., & Degterev, A. (2015) · Current topics in microbiology and immunology · doi:10.1007/82_2015_449 · Cited by 19
Deubiquitinating Enzymes: A Critical Regulator of Mitosis
Park, J., Cho, J., Kim, E. E., & Song, E. J. (2019) · International Journal of Molecular Sciences · doi:10.3390/ijms20235997 · Cited by 19
Deng, B., Yang, D., Wu, H., Wang, L., Wu, R., Zhu, H., Huang, A., Song, J., Cai, T., Liu, S., et al. (2022) · Cell Death Discovery · doi:10.1038/s41420-022-00869-x · Cited by 18
Panda, S. P., Kesharwani, A., Mallick, S. P., Prasanth, D., Pasala, P. K., & Tatipamula, V. B. (2023) · Biochemical Pharmacology · doi:10.1016/j.bcp.2023.115591 · Cited by 18
Kim‐Campbell, N., Gómez, H., & Bayır, H. (2019) · Elsevier eBooks · doi:10.1016/b978-0-323-44942-7.00020-0 · Cited by 18
Salvadores, N., & Court, F. A. (2020) · Expert Opinion on Therapeutic Targets · doi:10.1080/14728222.2020.1758668 · Cited by 18
Budroni, V., & Versteeg, G. A. (2021) · Viruses · doi:10.3390/v13040584 · Cited by 21
The death-inducing activity of RIPK1 is regulated by the pH environment
Moriwaki, K., Balaji, S., & Chan, F. K.-M. (2020) · Science Signaling · doi:10.1126/scisignal.aay7066 · Cited by 18
Self-citationDeubiquitinases: Modulators of Different Types of Regulated Cell Death
Lee, C.-S., Kim, S., Hwang, G., & Song, J. (2021) · International Journal of Molecular Sciences · doi:10.3390/ijms22094352 · Cited by 17
Leng, Y., Zhang, Y., Li, X., Wang, Z., Zhuang, Q., & Lu, Y. (2021) · Frontiers in Pharmacology · doi:10.3389/fphar.2021.762334 · Cited by 18
Kang, K., Park, C., & Chan, F. K.-M. (2022) · Journal of Cell Science · doi:10.1242/jcs.260091 · Cited by 19
Self-citationMALT1 promotes necroptosis in stroke rat brain via targeting the A20/RIPK3 pathway
Peng, Z.-M., Zhang, Y., Dan, W., Zhang, X., Liu, B., Peng, J., & Luo, X. (2023) · Archives of Biochemistry and Biophysics · doi:10.1016/j.abb.2023.109502 · Cited by 16
Immune dysregulation in SHARPIN-deficient mice is dependent on CYLD-mediated cell death
Ang, R. L., Chan, M., Legarda, D., Sundberg, J. P., Sun, S., Gillespie, V., Chun, N. H., Heeger, P. S., Xiong, H., Lira, S. A., et al. (2021) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.2001602118 · Cited by 16
Progress in studies of necroptosis and its relationship to disease processes
Wang, Z., Guo, L., Wang, S., Chen, D., Yan, J., Liu, F., Huang, J.-F., & Xiong, K. (2018) · Pathology - Research and Practice · doi:10.1016/j.prp.2018.09.002 · Cited by 15
Burning controversies in NETs and autoimmunity: The mysteries of cell death and autoimmune disease
Dwivedi, N., & Radic, M. Z. (2018) · Autoimmunity · doi:10.1080/08916934.2018.1523395 · Cited by 18
Pseftogas, A., Xanthopoulos, K., Poutahidis, T., Ainali, C., Dafou, D., Panteris, E., Kern, J. G., Varelas, X., Hardas, A., Gonidas, C., et al. (2020) · Cancers · doi:10.3390/cancers12082047 · Cited by 15
Ji, W., Yang, M., Praggastis, A., Li, Y., Zhou, H. J., He, Y., Ghazvinian, R., Cincotta, D. J., Rice, K. P., & Wang, M. (2014) · PLoS ONE · doi:10.1371/journal.pone.0103224 · Cited by 14
Proteolytic control of regulated necrosis
Chico, J. F., Saggau, C., & Adam, D. (2017) · Biochimica et Biophysica Acta (BBA) - Molecular Cell Research · doi:10.1016/j.bbamcr.2017.05.025 · Cited by 16
Chan, H. H., Koh, R. Y., Lim, C. L., & Leong, C. O. (2019) · Current Alzheimer Research · doi:10.2174/1567205016666191023102422 · Cited by 15
Non-coding RNAs in necroptosis, pyroptosis, and ferroptosis in cardiovascular diseases
Cai, Y., Zhou, Y., Li, Z., Xia, P., ChenFu, X., Shi, A., Zhang, J., & Yu, P. (2022) · Frontiers in Cardiovascular Medicine · doi:10.3389/fcvm.2022.909716 · Cited by 14
Cui, X., Wang, R., & Wang, Z. (2018) · Food & Function · doi:10.1039/c7fo01040k · Cited by 14
A biochemical necroptosis model explains cell-type-specific responses to cell death cues
Ildefonso, G. V., Metzig, M. O., Hoffmann, A., Harris, L. A., & Lopez, C. F. (2023) · Biophysical Journal · doi:10.1016/j.bpj.2023.01.035 · Cited by 14
Potu, H., Kandarpa, M., Peterson, L. F., Donato, N. J., & Talpaz, M. (2019) · Oncotarget · doi:10.18632/oncotarget.27196 · Cited by 13
Bai, J.-Q., Li, P., Li, H., & Li, H. (2023) · European Journal of Pharmacology · doi:10.1016/j.ejphar.2023.176235 · Cited by 12
Exploitation of necroptosis for treatment of caspase-compromised cancers
Cho, Y. S., & Park, H. L. (2017) · Oncology Letters · doi:10.3892/ol.2017.6285 · Cited by 12
Καρατζάς, Δ., Xanthopoulos, K., Kotantaki, P., Pseftogas, A., Teliousis, K., Hatzivassiliou, E., Kontoyiannis, D. L., Poutahidis, T., & Mosialos, G. (2016) · Cellular Oncology · doi:10.1007/s13402-016-0279-3 · Cited by 12
Necroptosis in Pneumonia: Therapeutic Strategies and Future Perspectives
Mei, X., Zhang, Y., Wang, S., Wang, H., Chen, R., Ma, K., Yang, Y., Jiang, P., Feng, Z., Zhang, C., et al. (2024) · Viruses · doi:10.3390/v16010094 · Cited by 11
Pseftogas, A., Gonidas, C., & Mosialos, G. (2016) · The International Journal of Biochemistry & Cell Biology · doi:10.1016/j.biocel.2016.11.011 · Cited by 11
Repressive Control of Keratinocyte Cytoplasmic Inflammatory Signaling
Carman, L. E., Samulevich, M. L., & Aneskievich, B. J. (2023) · International Journal of Molecular Sciences · doi:10.3390/ijms241511943 · Cited by 10
Cullin Deneddylation Suppresses the Necroptotic Pathway in Cardiomyocytes
Lewno, M. T., Cui, T., & Wang, X. (2021) · Frontiers in Physiology · doi:10.3389/fphys.2021.690423 · Cited by 10
RIPK1-TRAF2 interplay on the TNF/NF-κB signaling, cell death, and cancer development in the liver
Yamamoto, S., & Iwakuma, T. (2017) · Translational Cancer Research · doi:10.21037/tcr.2017.04.01 · Cited by 9
The roles of long non-coding RNAs in the necroptotic signaling of colon cancer cells
Bozgeyi̇k, E., Bağış, H., Bozgeyik, İ., & Kocahan, S. (2023) · Molecular Biology Reports · doi:10.1007/s11033-023-08441-1 · Cited by 9
Regulation of apoptosis by ubiquitination in liver cancer.
Li, Y., Zhu, J., Yu, Z., Zhai, F., Li, H., & Jin, X. (2023) · PubMed Central · Cited by 14
Chen, Q., Lei, Y., Liu, J., Wang, Z., & Cao, H. (2021) · Brain Research · doi:10.1016/j.brainres.2021.147572 · Cited by 9
Feng, T., Chen, W., Zhang, C., Xiang, J., Ding, H., Wu, L., & Geng, D. (2017) · Neurochemical Research · doi:10.1007/s11064-017-2244-6 · Cited by 9
Chemical regulation of signaling pathways to programmed necrosis
Bae, J. H., Shim, J., & Cho, Y. S. (2014) · Archives of Pharmacal Research · doi:10.1007/s12272-014-0385-6 · Cited by 9
Autophagy and Cell Death in Alzheimer’s, Parkinson’s and Prion Diseases
Ribarič, S., & Ribarič, I. M. (2019) · IntechOpen eBooks · doi:10.5772/intechopen.86706 · Cited by 9
Luo, T.-W., Sang, N., Liu, Y., Zhou, Y., Wu, R. X., Bagdasarian, F. A., Wey, H., Lang, J., Wang, C., & Bai, P. (2024) · Bioorganic Chemistry · doi:10.1016/j.bioorg.2024.107279 · Cited by 8
Emerging Insights Into Necroptosis: Implications for Renal Health and Diseases
Gupta, A., Chakole, S. V., Agrawal, S., Khekade, H., Prasad, R., Lohakare, T., & Wanjari, M. B. (2023) · Cureus · doi:10.7759/cureus.43609 · Cited by 8
Alzheimer’s disease: a jigsaw puzzle comprised of different types of programmed cell death pieces
Wang, Y., Mu, D., Li, Y., Liu, C., Feng, J., Lai, Y., & Lou, G. (2025) · Brain Research · doi:10.1016/j.brainres.2025.149861 · Cited by 7
Zhang, J., Hao, Y., Wang, Y., Han, Y., Zhang, S., & Niu, Q. L. (2021) · Chemosphere · doi:10.1016/j.chemosphere.2021.130484 · Cited by 7
Programmed cell death in cancer: targeting necroptosis to kill tumor cell
Liang, J., Tan, C., Li, X., Fan, J., & Liu, B. (2026) · Cell Death Discovery · doi:10.1038/s41420-026-03002-4 · Cited by 7
Necroptosis in the sarcoma immune microenvironment: From biology to therapy
Ye, H., Lu, M., Tu, C., & Li, M. (2023) · International Immunopharmacology · doi:10.1016/j.intimp.2023.110603 · Cited by 6
Necroptosis in obesity: a complex cell death event
Liu, Z., Wang, S., Wang, W., Lv, R., & Sun, C. (2024) · APOPTOSIS · doi:10.1007/s10495-024-02055-z · Cited by 7
Cross-regulation of Listeria monocytogenes and the host ubiquitin system in listeriosis
Zhuang, Y., Fischer, J. B., Nishanth, G., & Schlüter, D. (2024) · European Journal of Cell Biology · doi:10.1016/j.ejcb.2024.151401 · Cited by 6
SPATA2 – Keeping the TNF signal short and sweet
Feltham, R., Webb, A. I., & Silke, J. (2016) · The EMBO Journal · doi:10.15252/embj.201695061 · Cited by 6
Necroptosis, ADAM proteases and intestinal (dys)function
Heib, M., Rose‐John, S., & Adam, D. (2020) · International review of cytology · doi:10.1016/bs.ircmb.2020.02.001 · Cited by 7
The good, the bad, and the modified: CYLD’s post-translational tale
Macé, Y., Bidère, N., & Douanne, T. (2025) · Frontiers in Cell Death · doi:10.3389/fceld.2025.1583221 · Cited by 5
Deubiquitinases in metabolic diseases, fibrosis and cancer of the liver
Thakur, A., Kubaichuk, K. I., & Kietzmann, T. (2025) · Biochimica et Biophysica Acta (BBA) - Molecular Cell Research · doi:10.1016/j.bbamcr.2025.120021 · Cited by 5
CYLD suppresses LPS-induced inflammation through RIP1 deubiquitination in rainbow trout
Jang, J. H., Kim, H. R., Kim, H. J., & Cho, J. H. (2025) · Fish & Shellfish Immunology · doi:10.1016/j.fsi.2025.110489 · Cited by 5
Dovitinib Ameliorates Inflammation-Related Diseases by Inhibiting Necroptosis and Ferroptosis
Lin, Y., Feng, J., Zhao, M., Zhang, L., Li, Y., Chen, X., Lin, C., Lin, J., Lin, Q., Li, J., et al. (2025) · ACS Chemical Biology · doi:10.1021/acschembio.5c00327 · Cited by 5
Dan, W., Zhong, L., Zhang, Z., Wan, P., Lu, Y., Wang, X., Liu, Z., Chu, X., & Liu, B. (2022) · International Journal of Medical Sciences · doi:10.7150/ijms.68385 · Cited by 5
Wang, Y., Huang, Y., Li, C., Wang, X., Yang, M., Xu, D., Liu, B., & Yuan, X. (2022) · Frontiers in Cell and Developmental Biology · doi:10.3389/fcell.2022.921320 · Cited by 5
Exploiting Cell Death Pathways for Inducible Cell Elimination to Modulate Graft-versus-Host-Disease
Falcon, C., Al‐Obaidi, M., & Stasi, A. D. (2017) · Biomedicines · doi:10.3390/biomedicines5020030 · Cited by 5
IKK-mediated CYLD phosphorylation and cellular redox activity
Erol, A. (2022) · Molecular Medicine · doi:10.1186/s10020-022-00439-y · Cited by 5
Rinotas, V. E., Iliaki, K. K., Pavlidi, L., Meletakos, T., Mosialos, G., & Armaka, M. (2024) · Cell Death and Disease · doi:10.1038/s41419-024-06966-2 · Cited by 4
Sokołowski, M., & Butrym, A. K. (2025) · International Journal of Molecular Sciences · doi:10.3390/ijms262211101 · Cited by 5
Tokumasu, M., Sato, A., Ito-Kureha, T., Yamamoto, M., Ohmine, N., Semba, K., Inoue, J., & Yamamoto, T. S. (2025) · Cancer Gene Therapy · doi:10.1038/s41417-025-00897-6 · Cited by 4
Sokołowski, M., Łacina, P., Bogunia‐Kubik, K., Mazur, G. J., & Butrym, A. K. (2025) · International Journal of Molecular Sciences · doi:10.3390/ijms26115237 · Cited by 4
Inhibition of TBK1/IKKε mediated RIPK1 phosphorylation sensitizes tumors to immune cell killing
Piskopou, A., Vredevoogd, D. W., Kong, X., Peeper, D. S., Altelaar, M. A. F., & Stecker, K. E. (2025) · Cell Death Discovery · doi:10.1038/s41420-025-02841-x · Cited by 4
USP13 depletion sensitizes colorectal cancer cells to necroptosis by destabilizing cIAP2 proteins
Kim, Y. J., Das, T., Park, J., Hwang, I., Kim, E. E., & Song, E. J. (2025) · Cell Death and Differentiation · doi:10.1038/s41418-025-01595-4 · Cited by 3
d’Avila, J. C., Levin, S., & Radi, Z. A. (2017) · Elsevier eBooks · doi:10.1016/b978-0-12-801238-3.64220-4 · Cited by 3
Thakur, B., Verma, R. K., & Bhatia, A. (2024) · Clinical Breast Cancer · doi:10.1016/j.clbc.2024.12.008 · Cited by 3
Septic shock: innate molecular genetic mechanisms of the development of generalized inflammation
Kurmyshkina, O. V., Aa, B., Volkova, T. O., & Poltorak, A. (2015) · Russian Journal of Developmental Biology · doi:10.1134/s1062360415040062 · Cited by 3
Nian, Q., Chi, J., Xiao, Q., Wei, C., Costeas, P., Yang, Z., Liu, L., & WANG, L. (2015) · Oncology Reports · doi:10.3892/or.2015.4114 · Cited by 3
Murakami, T., Hu, Z., Tamura, H., & Nagaoka, I. (2016) · Molecular Medicine Reports · doi:10.3892/mmr.2016.4893 · Cited by 3
Ubiquitin-specific proteases as targets for anticancer drug therapies
Campos-Iglesias, D., López-Otín, C., & Freije, J. M. P. (2020) · Elsevier eBooks · doi:10.1016/b978-0-12-818168-3.00004-8 · Cited by 4
Croker, B. A., Rickard, J. A., Shlomovitz, I., Al‐Obeidi, A., D’Cruz, A. A., & Gerlic, M. (2018) · Wiley eBooks · doi:10.1002/9781119432463.ch6 · Cited by 3
Macrophage-associated kinase signaling in atherosclerosis – a systematic review
Müller, J. S., & van der Vorst, E. P. C. (2026) · Cell Communication and Signaling · doi:10.1186/s12964-026-02829-9 · Cited by 2
Delayed necrostatin-1s infusion attenuates cystic white matter injury in preterm fetal sheep
Lear, B. A., Lear, C. A., Dhillon, S. K., King, V. J., Dean, J. M., Davidson, J. O., Gunn, A. J., & Bennet, L. (2025) · Neurotherapeutics · doi:10.1016/j.neurot.2025.e00775 · Cited by 2
Programmed cell death dynamics during hyperglycemia and ischemic brain injuries.
LaRocca, T. J. (2016) · doi:10.35841/neurology-neurorehabilitation.1.2.49-54 · Cited by 2
Immunoprecipitation Strategies to Isolate RIPK1/RIPK3 Complexes in Mouse Macrophages
Siokas, I., Zhang, D., Poltorak, A., Muendlein, H. I., & Degterev, A. (2021) · Current Protocols · doi:10.1002/cpz1.156 · Cited by 2
Ars moriendi: Proteases as sculptors of cellular suicide
Heib, M., Weiß, J., Saggau, C., Hoyer, J., Chico, J. F., Voigt, S., & Adam, D. (2021) · Biochimica et Biophysica Acta (BBA) - Molecular Cell Research · doi:10.1016/j.bbamcr.2021.119191 · Cited by 2
Interaction of HIF-1a with various cell death pathways in tumor immune microenvironment (TIME)
Varkiani, M. M., Faghihkhorasani, F., Moosavi, M., Habibi, R., Mirzaei, H., Karimi, N., Etemad, S., Karami, P., Osati, P., Aref, A. R., et al. (2026) · APOPTOSIS · doi:10.1007/s10495-025-02249-z · Cited by 6
CYLD-mediated DNA damage coordinates pathological cardiac hypertrophy via RIPK1-dependent signaling
Jiang, X., Shi, M., Guo, J., Zhang, J., Li, D., 范祖军, Ren, F., Wu, S., Zeng, J., Wu, J., et al. (2026) · Journal of Molecular and Cellular Cardiology · doi:10.1016/j.yjmcc.2026.03.005 · Cited by 1
Functional Relevance of Deubiquitinases in Life and Disease
Fraile, J. M., López-Otı́n, C., & Freije, J. M. P. (2017) · Springer eBooks · doi:10.1007/978-981-10-2513-6_16 · Cited by 1
Nekroptozis: Serebral ve Miyokardiyal İskemi/Reperfüzyon Hasarı için Terapötik bir Hedef midir?
Yılmaz, Z. (2023) · Harran Üniversitesi Tıp Fakültesi Dergisi · doi:10.35440/hutfd.1341349 · Cited by 1
Qiu, M., Zhang, H., Wang, L., Wei, Y., Emu, Q., Yang, S., & Wang, L. (2023) · Small Ruminant Research · doi:10.1016/j.smallrumres.2023.107143 · Cited by 1
Ranjan, S., Kushwaha, N. S., Trivedi, S., Tiwari, N., & Khan, S. (2024) · Pharmacognosy Magazine · doi:10.1177/09731296241243132 · Cited by 1
Targeting Necroptosis in Antitumor Therapy
Chan, F. K.-M., Nailwal, H., & Moriwaki, K. (2018) · Elsevier eBooks · doi:10.1016/b978-0-12-813753-6.00013-5 · Cited by 1
Self-citationLoss-of-Function RNAi Screen to Identify Necrosis-Signaling Molecules
Moquin, D., & Chan, F. K.-M. (2018) · Methods in molecular biology · doi:10.1007/978-1-4939-8754-2_2 · Cited by 1
Self-citationMechanisms of Cell Death in the Developing Brain
Thornton, C., & Hagberg, H. (2016) · Elsevier eBooks · doi:10.1016/b978-0-323-35214-7.00007-x · Cited by 1
The role of ripk1 in tnf-induced cell death in intestinal epithelial cells
Garcia‐Carbonell, R. (2017) · Dipòsit Digital de la Universitat de Barcelona (Universitat de Barcelona) · Cited by 1
Ganesan, S. (2014) · eScholarship@UMassChan · doi:10.13028/m28c8f · Cited by 1
TRIM27 in HSV-1 Infection: A Story of Loss and Death
Conwell, S. E. (2015) · Digital Access to Scholarship at Harvard (DASH) (Harvard University)
Necrobiology of Liver Cancer: Necrosis and Necroptosis
Zimmermann, A. (2016) · Springer eBooks · doi:10.1007/978-3-319-26587-2_178-1
Functional and Physiological Characteristic of RIPK and MLKL in TNF Signaling
Park, Y.-H., Jeong, M. S., & Jang, S. B. (2016) · Journal of Life Science · doi:10.5352/jls.2016.26.7.868
Tao, L. (2018) · Springer eBooks · doi:10.1007/978-3-319-77495-4_5
Chemical Library Screens to Identify Pharmacological Modulators of Necroptosis
Saleh, D., & Degterev, A. (2018) · Methods in molecular biology · doi:10.1007/978-1-4939-8754-2_3
The Molecular Mechanism of Host Responses to Viral Infection
Schock, S. (2014) · eScholarship (California Digital Library)
Targeting Susceptible Signaling Pathways in Chronic Lymphocytic Leukemia
Dielschneider, R. F. (2014) · Mspace (University of Manitoba)
Birth and death of CYLD paralogues in vertebrates
Raza, F., & Hussain, M. (2021) · Gene Reports · doi:10.1016/j.genrep.2021.101190
Necrobiology of Liver Cancer: Necrosis and Necroptosis
Zimmermann, A. (2016) · Springer eBooks · doi:10.1007/978-3-319-26956-6_178
Feng, T., Li, Y., Wu, Y., Wang, J., & Kong, Q. (2023) · International Conference on Bioinformatics and Biomedical Science (ICBBS) · doi:10.1145/3647817.3647821
Metadata
- Authors
- Moquin, D. M., McQuade, T., & Chan, F. K.-M.
- Affiliations
- University of Massachusetts Chan Medical School (US)
- Corresponding author
- Chan, Francis Ka-Ming
- Venue
- PLoS ONE
- Publisher
- Public Library of Science (PLoS)
- Published
- 2013-10-02
- Volume
- 8
- Issue
- 10
- Pages
- e76841
- ISSN
- 1932-6203 (ISSN-L)
- PMC
- PMC3788787
- OpenAlex
- W2060803227
- Cited by
- 320
- References
- 48
- Citations by year
- 2026: 14 · 2025: 22 · 2024: 18 · 2023: 29 · 2022: 21 · 2021: 33 · 2020: 18 · 2019: 26 · 2018: 30 · 2017: 25 · 2016: 33 · 2015: 19 · 2014: 31 · 2013: 1
- FWCI
- 12.55
- Type
- journal article
- Language
- en
- Open access
- gold
- doi.org
- Locations
- PLoS ONE (publishedVersion, cc-by)
- Europe PMC (PubMed Central) (publishedVersion, cc-by)
- PubMed Central (publishedVersion, cc-by)
- PubMed (publishedVersion)
- DOAJ (DOAJ: Directory of Open Access Journals) (submittedVersion)
- Funders
- National Institutes of Health (NIH T32, AI083497)
- National Institute of Allergy and Infectious Diseases (T32 AI07349, R21AI088502, AI083497, AI088502, R01AI083497, T32AI007349)
- Topics
- Life Sciences › Biochemistry, Genetics and Molecular Biology › Molecular Biology › Cell death mechanisms and regulation
- Life Sciences › Biochemistry, Genetics and Molecular Biology › Molecular Biology › Ubiquitin and proteasome pathways
- Life Sciences › Biochemistry, Genetics and Molecular Biology › Cancer Research › NF-κB Signaling Pathways
- Keywords
- CYLD, RIPK1, RIPK3, necrosome, necroptosis, TNF signaling, deubiquitination, ubiquitination, IAP antagonists, cIAP1, cIAP2, E3 ubiquitin ligase, zVAD
- MeSH terms
- Deubiquitinating Enzyme CYLD, Animals, Cycloheximide, Cysteine Endopeptidases, Gene Expression Regulation, Humans, Necrosis, Oligopeptides, Phosphorylation, Tumor Necrosis Factor-alpha, Signal Transduction, GTPase-Activating Proteins, Cell Line, Tumor, Receptors, Tumor Necrosis Factor, Type I, Mice, Receptor-Interacting Protein Serine-Threonine Kinases, Ubiquitination, Gene Knockdown Techniques
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