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RIPK1 maintains epithelial homeostasis by inhibiting apoptosis and necroptosis
Open accessAbstract
Necroptosis has emerged as an important pathway of programmed cell death in embryonic development, tissue homeostasis, immunity and inflammation. RIPK1 is implicated in inflammatory and cell death signalling and its kinase activity is believed to drive RIPK3-mediated necroptosis. Here we show that kinase-independent scaffolding RIPK1 functions regulate homeostasis and prevent inflammation in barrier tissues by inhibiting epithelial cell apoptosis and necroptosis. Intestinal epithelial cell (IEC)-specific RIPK1 knockout caused IEC apoptosis, villus atrophy, loss of goblet and Paneth cells and premature death in mice. This pathology developed independently of the microbiota and of MyD88 signalling but was partly rescued by TNFR1 (also known as TNFRSF1A) deficiency. Epithelial FADD ablation inhibited IEC apoptosis and prevented the premature death of mice with IEC-specific RIPK1 knockout. However, mice lacking both RIPK1 and FADD in IECs displayed RIPK3-dependent IEC necroptosis, Paneth cell loss and focal erosive inflammatory lesions in the colon. Moreover, a RIPK1 kinase inactive knock-in delayed but did not prevent inflammation caused by FADD deficiency in IECs or keratinocytes, showing that RIPK3-dependent necroptosis of FADD-deficient epithelial cells only partly requires RIPK1 kinase activity. Epidermis-specific RIPK1 knockout triggered keratinocyte apoptosis and necroptosis and caused severe skin inflammation that was prevented by RIPK3 but not FADD deficiency. These findings revealed that RIPK1 inhibits RIPK3-mediated necroptosis in keratinocytes in vivo and identified necroptosis as a more potent trigger of inflammation compared with apoptosis. Therefore, RIPK1 is a master regulator of epithelial cell survival, homeostasis and inflammation in the intestine and the skin.
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“Likewise, the absence of Ripk1 from keratinocytes promotes spontaneous necroptosis and consequent cutaneous inflammation, which can be prevented by the co-deletion of Ripk3, Mlkl, or Zbp1 but not Fadd [440, 502].”
From Molecular mechanisms of cell death: recommendations of the nomenclature committee on cell death 2018. (2018) · cites this paper as [502]
In the citing paper
“Conditional knockout mouse models demonstrate the key role of RIPK1 for the preservation of intestinal and cutaneous homeostasis and survival [502, 503].”
From Molecular mechanisms of cell death: recommendations of the nomenclature committee on cell death 2018. (2018) · cites this paper as [502]
In the citing paper
“In particular, mice lacking Ripk1 in intestinal epithelial cells display increased rates of spontaneous CASP8-driven apoptosis and develop severe inflammatory lesions leading to premature death, a detrimental phenotype that can be prevented by co-deleting Fadd or (to a lesser degree) Tnfrsf1a [502].”
From Molecular mechanisms of cell death: recommendations of the nomenclature committee on cell death 2018. (2018) · cites this paper as [502]
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“During NASH development, RIPK1 limited the progression of liver fibrosis in hepatocytes [85, 86].”
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“After TNFR is rapidly internalized upon ligand binding, RIPK-1 becomes deubiquitinated by the cylindromatotis deubiquitinase (CYLD), as indicated [35, 259-262].”
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“However, deleting Ripk1 in keratinocytes resulted in RIPK3-mediated necroptosis causing excessive inflammation and Ripk1-deficient hematopoietic cells underwent increased apoptosis and necroptosis (8, 9).”
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“Previous studies have shown that systemic, or intestinal epithelial specific, loss of RIPK1 resulted in the sporadic development of intestinal inflammation in mice [14, 39, 40], while conflicting results have been reported from studies using Ripk3-deficient mice.”
ResultXin, J., You, D., Breslin, P., Li, J., Zhang, J., Wei, W., Cannova, J., Volk, A. G., Gutierrez, R., Xiao, Y., et al. (2016) · Leukemia · doi:10.1038/leu.2016.287 · Cited by 46
25 years of research put RIPK1 in the clinic
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The latest information on the RIPK1 post-translational modifications and functions
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The Receptor Interacting Protein Kinases in the Liver
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Combined Knockout of RIPK3 and MLKL Reveals Unexpected Outcome in Tissue Injury and Inflammation
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“Deleting either Ripk3 or Mlkl can suppress skin inflammation in RIPK1deficient mice (Dannappel et al., 2014), and the fact that Ripk3 or Mlkl deficiency ameliorates liver inflammation and splenomegaly in Sharpin-deficient mice (Rickard et al., 2014a), suggesting that MLKL follows RIPK3 directly in…”
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“Staining was visualized with ABC Kit Vectastain Elite and DAB substrate (both Vector Laboratories) followed by haematoxylin counterstaining [19].”
MethodSelf-citationPhosphorylation-dependent pseudokinase domain dimerization drives full-length MLKL oligomerization
Meng, Y., Garnish, S. E., Davies, K. A., Black, K. A., Leis, A. P., Horne, C. R., Hildebrand, J. M., Hoblos, H., Fitzgibbon, C., Young, S. N., et al. (2023) · Nature Communications · doi:10.1038/s41467-023-42255-w · Cited by 44
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RIP1 kinase mediates angiogenesis by modulating macrophages in experimental neovascularization
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RIPK1 Promotes Energy Sensing by the mTORC1 Pathway
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“To characterize the structure of N-terminal four-helix bundle (4HB) domain and the first brace 91 helix of mouse MLKL (residues 1-158; termed mouse MLKL(1-158) herein) in solution, we 92 subjected 2H,15N,13C-labelled protein to non-uniformly sampled three-dimensional NMR 93 methodology.”
BackgroundMethodInfluentialÁgueda-Pinto, A., Alves, L. Q., Neves, F., McFadden, G., Jacobs, B. L., Castro, L. F. C., Rahman, M. M., & Esteves, P. J. (2021) · Frontiers in Immunology · doi:10.3389/fimmu.2021.747737 · Cited by 40
“For example, deleting either RIPK3 or MLKL can lead to the suppression of skin and liver inflammation in mice (45, 46).”
BackgroundDendritic Cell RIPK1 Maintains Immune Homeostasis by Preventing Inflammation and Autoimmunity
O’Donnell, J. A., Lehman, J. W., Roderick, J. E., Martinez‐Marin, D., Zelic, M., Doran, C. G., Hermance, N. M., Lyle, S. R., Pasparakis, M., Fitzgerald, K. A., et al. (2017) · The Journal of Immunology · doi:10.4049/jimmunol.1701229 · Cited by 39
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Development of a RIPK1 degrader to enhance antitumor immunity
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“Unlike Ripk1 KO mice, which die within 1 – 3 days of age due to the critical role of RIPK1 in multiple tissues and organs 35 , the phenotypes of homozygous loss-of-function RIPK1 mutations in humans are relatively less severe 36 .”
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The serine threonine kinase RIP3: lost and found
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“uations RIP1 is thought to negatively regulate RIP3-dependent cell death activity to some extent (22-25).”
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“Further investigation revealed that MLKL drives a necroptosisdependent harmful phenotype in a number of tissue-specific, genetically modified mice, such as RIPK1 (epidermal RIPK1 deletion) [66], Caspase-8 (skin specific Caspase-8 inactivation) [58] and Fadd (intestinal epithelial cell-specific deletion of Fadd) [67].”
Krishna-Subramanian, S., Singer, S., Armaka, M., Bañales, J. M., Hölzer, K., Schirmacher, P., Walczak, H., Kollias, G. A., Pasparakis, M., & Kondylis, V. (2019) · Cell Death and Differentiation · doi:10.1038/s41418-019-0330-9 · Cited by 35
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A family harboring an MLKL loss of function variant implicates impaired necroptosis in diabetes
Hildebrand, J. M., Lo, B., Tomei, S., Mattei, V., Young, S. N., Fitzgibbon, C., Murphy, J. M., & Fadda, A. A. (2021) · Cell Death and Disease · doi:10.1038/s41419-021-03636-5 · Cited by 35
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Microbial signals, MyD88, and lymphotoxin drive TNF-independent intestinal epithelial tissue damage
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“Kondylis V, et al. The interplay of IKK, NF-κB and RIPK1 signaling in the regulation of cell death, tissue homeostasis and inflammation.”
BackgroundInfluentialKinase-independent functions of RIPK1 regulate hepatocyte survival and liver carcinogenesis
Van, T.-M., Polykratis, A., Straub, B. K., Kondylis, V., Papadopoulou, N., & Pasparakis, M. (2017) · Journal of Clinical Investigation · doi:10.1172/jci92508 · Cited by 35
“Alfp-Cre (28), Ripk1fl/fl (8), Ripk1fl/D138N (33), Tnfr1fl/fl (29), Faddfl/fl (31), Traddfl/fl (30), and RelAfl/fl (46) mice were reported earlier.”
Self-citationLi, D., Ai, Y., Guo, J., Dong, B., Lin, L., Cai, G., Chen, S., Xu, D., Wang, F., & Wang, X. (2020) · eLife · doi:10.7554/elife.61564 · Cited by 33
“…by double knockout RIP3 or MLKL; and cellular necroptosis induction by TNF-α or TLRs are dramatically enhanced if caspase-8 activity is suppressed (Dannappel et al., 2014; Dillon et al., 2014; Gunther et al., 2011; He et al., 2009; Kaiser et al., 2011; Newton et al., 2019; Oberst et al., 2011;…”
BackgroundMCL1 Is Required for Maintenance of Intestinal Homeostasis and Prevention of Carcinogenesis in Mice
Healy, M. E., Boege, Y., Hodder, M. C., Böhm, F., Malehmir, M., Scherr, A., Jetzer, J., Chan, L. K., Parrotta, R., Jacobs, K., et al. (2020) · Gastroenterology · doi:10.1053/j.gastro.2020.03.017 · Cited by 33
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“Mitochondrial dysfunction and increased oxidative stress levels in NP cells were observed in a compressed rat model, indicating that RIPK1 plays a significant role in mediating apoptosis and necroptosis in NP cells [54].”
Croker, B. A., Silke, J., & Gerlic, M. (2015) · Current Opinion in Hematology · doi:10.1097/moh.0000000000000148 · Cited by 33
Atg14protects the intestinal epithelium from TNF-triggered villus atrophy
Jung, H., Leal-Ekman, J. S., Lu, Q., & Stappenbeck, T. S. (2019) · Autophagy · doi:10.1080/15548627.2019.1596495 · Cited by 34
“within the Ripk1 VC model is accompanied by increased epithelial cell death in the intestinal epithelium [13,14].”
BackgroundNF-κB inhibition in keratinocytes causes RIPK1-mediated necroptosis and skin inflammation
Kumari, S., Van, T.-M., Preukschat, D., Schünke, H., Basic, M., Bleich, A., Klein, U., & Pasparakis, M. (2021) · Life Science Alliance · doi:10.26508/lsa.202000956 · Cited by 31
“Ikk2fl/fl (Pasparakis et al, 2002), Faddfl/fl (Mc Guire et al, 2010), K14Cre (Hafner et al, 2004),Mlkl−/− (Dannappel et al, 2014), Ripk1D138N/D138N (Polykratis et al, 2014), Relafl/fl (Luedde et al, 2008), c-Relfl/fl (Heise et al, 2014), Tnfr1fl/fl (Van Hauwermeiren et al, 2013), Ripk3−/− (Newton…”
Self-citationYin, Z., Chen, W., Yin, J., Sun, J., Xie, Q., Wu, M. C., Zeng, F., & Ren, H. (2021) · npj Breast Cancer · doi:10.1038/s41523-021-00261-5 · Cited by 31
Ghazavi, F., Huysentruyt, J., Coninck, J. D., Kourula, S., Martens, S., Hassannia, B., Wartewig, T., Divert, T., Roelandt, R., Popper, B., et al. (2022) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.2024508119 · Cited by 31
Epithelial Cell Death and Inflammation in Skin
Kumari, S., & Pasparakis, M. (2015) · Current topics in microbiology and immunology · doi:10.1007/82_2015_466 · Cited by 33
“Unlike RIPK1 mice, mutant mice expressing an inactive kinase RIPK1 allele did not develop skin lesions showing that the protective role of RIPK1 in keratinocyte death and skin inflammation is due to its kinase-independent scaffolding function (Dannappel et al. 2014; Polykratis et al. 2014).”
BackgroundInfluentialSelf-citationTargeting RIP Kinases in Chronic Inflammatory Disease
Speir, M., Djajawi, T. M., Conos, S. A., Tye, H., & Lawlor, K. E. (2021) · Biomolecules · doi:10.3390/biom11050646 · Cited by 30
“Epithelial-specific knockout of RIPK1 (Ripk1E-KO) TNFR1-induced RIPK3and ZBP1-RIPK3-MLKLdependent necroptosis Psoriasis-like disease [30,61,137]”
BackgroundInflammatory cell death induced by cytotoxic lymphocytes: a dangerous but necessary liaison
de Miguel, D., Ramírez-Labrada, A., Uranga-Murillo, I., Hidalgo, S., Santiago, L., Gálvez, E. M., Arias, M. A., & Pardo, J. (2021) · FEBS Journal · doi:10.1111/febs.16093 · Cited by 33
“Therefore, RIPK1 acts as a regulator hub for both 11 apoptosis and necroptosis, especially in TNF signalling [75-77].”
BackgroundTargeting Necroptosis as a Promising Therapy for Alzheimer’s Disease
Zhao, W., Liu, Y., Xu, L., He, Y., Cai, Z., Yu, J., Zhang, W., Xing, C., Zhuang, C., & Qu, Z. (2022) · ACS Chemical Neuroscience · doi:10.1021/acschemneuro.2c00172 · Cited by 31
Z‐ Nucleic Acid Sensing and Activation of ZBP1 in Cellular Physiology and Disease Pathogenesis
Mishra, S., Dey, A. A., & Kesavardhana, S. (2025) · Immunological Reviews · doi:10.1111/imr.13437 · Cited by 30
“ZBP1 promotes necroptosis and inflammation in FADD or caspase- 8-deficient IECs [82, 83].”
Biochemistry of Autoinflammatory Diseases: Catalyzing Monogenic Disease
Beck, D. B., & Aksentijevich, I. A. (2019) · Frontiers in Immunology · doi:10.3389/fimmu.2019.00101 · Cited by 29
“RIPK1 has been extensively studied in murine models, with knockout mice displaying postnatal lethality due to systemic inflammation and increased cell death (101, 102).”
BackgroundRIPK1 prevents aberrant ZBP1-initiated necroptosis
Berghe, T. V., & Kaiser, W. J. (2016) · Oncotarget · doi:10.18632/oncotarget.13926 · Cited by 29
Du, J., & Wang, Z. (2024) · Biomedicines · doi:10.3390/biomedicines12071525 · Cited by 28
“Moreover, RIPK1 is essential for maintaining the survival of intestinal epithelial cells (IECs) by blocking apoptosis and necroptosis [109].”
BackgroundRIPK1 downregulation in keratinocyte enhances TRAIL signaling in psoriasis
Saito, N., Honma, M., Shibuya, T., Iinuma, S., Igawa, S., Kishibe, M., & Ishida‐Yamamoto, A. (2018) · Journal of Dermatological Science · doi:10.1016/j.jdermsci.2018.04.007 · Cited by 28
Cartilage Trauma Induces Necroptotic Chondrocyte Death and Expulsion of Cellular Contents
Stolberg-Stolberg, J., Sambale, M., Hansen, U. J., Schäfer, A., Raschke, M. C. E. J., Bertrand, J., Pap, T., & Sherwood, J. (2020) · International Journal of Molecular Sciences · doi:10.3390/ijms21124204 · Cited by 28
“Although recent literature also describes RIPK1-independent necroptosis, the combination of assessing RIPK3, MLKL, and p-MLKL expression and responsiveness to necrostatin1 treatment is viewed as the gold standard for detecting necroptosis and is regarded as superior in accuracy compared to early studies addressing the…”
BackgroundA tale of two domains – a structural perspective of the pseudokinase, MLKL
Czabotar, P. E., & Murphy, J. M. (2015) · FEBS Journal · doi:10.1111/febs.13504 · Cited by 29
Hou, B., Liu, M., Chen, Y., Ni, W., Suo, X.-G., Xu, Y. G., He, Q., Meng, X., & Hao, Z. (2022) · Frontiers in Pharmacology · doi:10.3389/fphar.2022.1041117 · Cited by 27
“RIPK1, RIPK3 and MLKL are all targets of intervention against necroptosis-mediated inflammation and pathology (Dannappel et al., 2014; Mulay et al., 2016; Martens et al., 2020; Liu et al., 2022).”
BackgroundZhao, C., & Lin, S. (2025) · Frontiers in Immunology · doi:10.3389/fimmu.2024.1507065 · Cited by 29
Shindo, R., Ohmuraya, M., Komazawa‐Sakon, S., Miyake, S., Deguchi, Y., Yamazaki, S., Nishina, T., Yoshimoto, T., Kakuta, S., Koike, M., et al. (2019) · iScience · doi:10.1016/j.isci.2019.05.011 · Cited by 26
Jiang, S., & Miao, Z. (2023) · PubMed Central · Cited by 29
Cloaked in ubiquitin, a killer hides in plain sight: the molecular regulation of RIPK 1
Justus, S. J., & Ting, A. T. (2015) · Immunological Reviews · doi:10.1111/imr.12304 · Cited by 27
Saracatinib inhibits necroptosis and ameliorates psoriatic inflammation by targeting MLKL
Li, J., Liu, X., Liu, Y., Huang, F., Liang, J., Lin, Y., Hu, F., Feng, J., Han, Z., Chen, Y., et al. (2024) · Cell Death and Disease · doi:10.1038/s41419-024-06514-y · Cited by 26
Defective prelamin A processing promotes unconventional necroptosis driven by nuclear RIPK1
Yang, Y., Zhang, J., Lv, M., Cui, N., Shan, B., Sun, Q., Yan, L., Zhang, M., Zou, C., Yuan, J., et al. (2024) · Nature Cell Biology · doi:10.1038/s41556-024-01374-2 · Cited by 27
“6a), which is consistent with the high expression of RIPK1 in these cells 68–70 .”
Developmental checkpoints guarded by regulated necrosis
Dillon, C. P., Tummers, B., Baran, K., & Green, D. R. (2016) · Cellular and Molecular Life Sciences · doi:10.1007/s00018-016-2188-z · Cited by 28
The Role of the Key Effector of Necroptotic Cell Death, MLKL, in Mouse Models of Disease
Crutchfield, E. C. T., Garnish, S. E., & Hildebrand, J. M. (2021) · Biomolecules · doi:10.3390/biom11060803 · Cited by 27
“More recently, CRISPR-Cas9 engineered Mlkl−/− [17,33,73], constitutively active point mutant MlklD139V [40], affinity tagged Mlkl [67], conditional Mlkl−/− strains [29,67] and antisense oligonucleotide (ASO) in vivo Mlkl knockdown [60] mouse models have also been used in the study of necroptosis.”
MethodQi, Y., Wei, J. S., & Zhang, X. (2021) · Cell Death and Disease · doi:10.1038/s41419-021-04234-1 · Cited by 26
Tisch, N., Mogler, C., Stojanovic, A., Luck, R., Korhonen, E. A., Ellerkmann, A., Adler, H., Singhal, M., Schermann, G., Erkert, L., et al. (2022) · EMBO Molecular Medicine · doi:10.15252/emmm.202114121 · Cited by 26
“After weaning from the mother at ~3 weeks, Casp8ECko mice were treated with a mixture of broad-spectrum antibiotics (Dannappel et al, 2014) via the drinking water until the end of the experiment: Ampicillin 1 g/l (Ratiopharm), Neomycin 1 g/l (Sigma), Meronem 0.5 g/l (Friedrich-Eberth),…”
InfluentialRIPK1 and RIPK3 regulate TNFα-induced β-cell death in concert with caspase activity
Contreras, C., Mukherjee, N., Branco, R. C. S., Lin, L., Hogan, M. F., Cai, E. P., Oberst, A., Kahn, S. E., & Templin, A. T. (2022) · Molecular Metabolism · doi:10.1016/j.molmet.2022.101582 · Cited by 28
Sources, bioaccumulation, and toxicity mechanisms of cadmium in Chlamys farreri
Liu, H., Tian, X., Jiang, L., Han, D., Hu, S., Cui, Y., Jiang, F., Liu, Y., Xu, Y., & Li, H. (2023) · Journal of Hazardous Materials · doi:10.1016/j.jhazmat.2023.131395 · Cited by 26
The Function of Necroptosis and Its Treatment Target in IBD
Akanyibah, F. A., Zhu, Y., Jin, T., Ocansey, D. K. W., Mao, F., & Qiu, W. (2024) · Mediators of Inflammation · doi:10.1155/2024/7275309 · Cited by 27
“Surprisingly, mice de fi cient in RIPK1 and FADD in IECs showed RIPK3-dependent IEC necroptosis, loss of paneth cells, and localized erosive lesions that are in fl ammatory to the colon [82], implying that RIPK1 de fi ciency in IEC-speci fi c cells can lead to RIPK3-dependent necroptosis.”
BackgroundRen, L., Zhang, J., Wang, J., Wei, J., Liu, J., Li, X., Zhu, Y., Li, Y., Guo, C., Duan, J., et al. (2019) · Chemosphere · doi:10.1016/j.chemosphere.2019.04.116 · Cited by 25
Gong, Y., Yang, G., Wang, Q., Wang, Y., & Zhang, X. (2019) · Molecular Cancer Research · doi:10.1158/1541-7786.mcr-19-0612 · Cited by 25
Li, Z., Zhou, X., Zhu, H., Song, X., Gao, H., Niu, Z., & Lu, J. (2020) · Journal of Biochemical and Molecular Toxicology · doi:10.1002/jbt.22665 · Cited by 25
RIPK1 mutations causing infantile-onset IBD with inflammatory and fistulizing features
Sultan, M. I., Adawi, M., Kol, N., McCourt, B. T., Adawi, I., Baram, L., Tal, N., Werner, L., Lev, A., Snapper, S. B., et al. (2022) · Frontiers in Immunology · doi:10.3389/fimmu.2022.1041315 · Cited by 24
“Mice with a specific deletion of RIPK1 in epithelial cells develop spontaneous lethal intestinal inflammation due to enhanced apoptosis and necroptosis of epithelial cells (29, 30).”
BackgroundThe recent progress of the mechanism and regulation of tumor necrosis in colorectal cancer
Zhang, X., & Chen, L. (2015) · Journal of Cancer Research and Clinical Oncology · doi:10.1007/s00432-015-1997-z · Cited by 25
Z-nucleic acid sensor ZBP1 in sterile inflammation
Song, Q., Qi, Z., Wang, K., & Wang, N. (2024) · Clinical Immunology · doi:10.1016/j.clim.2024.109938 · Cited by 26
Dowling, J. P., Nair, A., & Zhang, J. (2015) · Frontiers in Cell and Developmental Biology · doi:10.3389/fcell.2015.00012 · Cited by 24
Metadata
- Authors
- Dannappel, M., Vlantis, K., Kumari, S., Polykratis, A., Kim, C., Wachsmuth, L., Eftychi, C., Lin, J., Corona, T., Hermance, N., Zelic, M., Kirsch, P., Basic, M., Bleich, A., Kelliher, M., & Pasparakis, M.
- Affiliations
- University of Cologne (DE)
- University of Massachusetts Chan Medical School (US)
- Universität Ulm (DE)
- Medizinische Hochschule Hannover (DE)
- Corresponding author
- Pasparakis, Manolis
- ORCID
- Venue
- Nature
- Published
- 2014-08-17
- Volume
- 513
- Issue
- 7516
- Pages
- 90-94
- ISSN
- 0028-0836 (ISSN-L)
- 1476-4687
- PMC
- PMC4206266
- OpenAlex
- W1985231277
- Cited by
- 534
- References
- 47
- Citations by year
- 2026: 21 · 2025: 33 · 2024: 46 · 2023: 36 · 2022: 56 · 2021: 47 · 2020: 47 · 2019: 49 · 2018: 44 · 2017: 33 · 2016: 59 · 2015: 49 · 2014: 14
- FWCI
- 21.20
- Type
- journal article
- Language
- en
- Open access
- green
- www.ncbi.nlm.nih.gov
- Locations
- Nature (publishedVersion)
- PubMed (publishedVersion)
- Kölner Universitäts PublikationsServer (Universität zu Köln) (publishedVersion)
- PubMed Central (acceptedVersion)
- RePEc: Research Papers in Economics (submittedVersion)
- Funders
- National Institute of Allergy and Infectious Diseases (R01AI075118, T32AI095213)
- Topics
- Life Sciences › Biochemistry, Genetics and Molecular Biology › Molecular Biology › Cell death mechanisms and regulation
- Life Sciences › Biochemistry, Genetics and Molecular Biology › Cancer Research › NF-κB Signaling Pathways
- Life Sciences › Immunology and Microbiology › Immunology › Immune Response and Inflammation
- Keywords
- RIPK1, necroptosis, apoptosis, epithelial homeostasis, FADD, caspase-8, RIPK3, intestinal epithelium, skin inflammation, keratinocytes, TNFR1, barrier tissues, inflammation, programmed cell death, Paneth cells, goblet cells, villous atrophy, intestinal inflammation
- MeSH terms
- Animals, Cell Survival, Epithelial Cells, Female, Homeostasis, Inflammation, Intestinal Mucosa, Intestines, Male, Necrosis, Skin, Keratinocytes, Apoptosis, Mice, Knockout, Paneth Cells, Receptors, Tumor Necrosis Factor, Type I, Mice, Caspase 8, Fas-Associated Death Domain Protein, Receptor-Interacting Protein Serine-Threonine Kinases, Myeloid Differentiation Factor 88
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