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ABINs: A20 binding inhibitors of NF-κB and apoptosis signaling
Open accessAbstract
ABINs have been described as three different proteins (ABIN-1, ABIN-2, ABIN-3) that bind the ubiquitin-editing nuclear factor-kappaB (NF-kappaB) inhibitor protein A20 and which show limited sequence homology. Overexpression of ABINs inhibits NF-kappaB activation by tumor necrosis factor (TNF) and several other stimuli. Similar to A20, ABIN-1 and ABIN-3 expression is NF-kappaB dependent, implicating a potential role for the A20/ABIN complex in the negative feedback regulation of NF-kappaB activation. Adenoviral gene transfer of ABIN-1 has been shown to reduce NF-kappaB activation in mouse liver and lungs. However, ABIN-1 as well as ABIN-2 deficient mice exhibit only slightly increased or normal NF-kappaB activation, respectively, possibly reflecting redundant NF-kappaB inhibitory activities of multiple ABINs. Other functions of ABINs might be non-redundant. For example, ABIN-1 shares with A20 the ability to inhibit TNF-induced apoptosis and as a result ABIN-1 deficient mice die during embryogenesis due to TNF-dependent fetal liver apoptosis. On the other hand, ABIN-2 is required for optimal TPL-2 dependent extracellularly regulated kinase activation in macrophages treated with TNF or Toll-like receptor ligands. ABINs have recently been shown to contain an ubiquitin-binding domain that is essential for their NF-kappaB inhibitory and anti-apoptotic activities. In this context, ABINs were proposed to function as adaptors between ubiquitinated proteins and other regulatory proteins. Alternatively, ABINs might disrupt signaling complexes by competing with other ubiquitin-binding proteins for the binding to specific ubiquitinated targets. Altogether, these findings implicate an important role for ABINs in the regulation of immunity and tissue homeostasis.
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“For TNIP1, its gene product (TNF-α-induced protein 3-interacting protein 1) is involved in the inhibition of the TNF-α signaling pathway and nuclear factor κB activation/translocation33.”
From New insights into the genetic etiology of Alzheimer’s disease and related dementias (2022) · cites this paper as [33]
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Cites
Introduction to NF-κB: players, pathways, perspectives
Gilmore, T. D. (2006) · Oncogene · doi:10.1038/sj.onc.1209954 · Cited by 2,293
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
A serine/threonine kinase gene defective in Peutz–Jeghers syndrome
Hemminki, A., Markie, D., Tomlinson, I. P. M., Avizienyte, E., Roth, S., Loukola, A., Bignell, G. R., Warren, W., Aminoff, M., Höglund, P., et al. (1998) · Nature · doi:10.1038/34432 · Cited by 1,680
Genome-wide scan reveals association of psoriasis with IL-23 and NF-κB pathways
Nair, R. P., Duffin, K. C., Helms, C., Ding, J., Stuart, P. E., Goldgar, D. E., Gudjonsson, J. E., Li, Y., Tejasvi, T., Feng, B., et al. (2009) · Nature Genetics · doi:10.1038/ng.311 · Cited by 1,433
Failure to Regulate TNF-Induced NF-κB and Cell Death Responses in A20-Deficient Mice
Lee, E. G., Boone, D. L., Chai, S., Libby, S. L., Chien, M., Lodolce, J. P., & Ma, A. (2000) · Science · doi:10.1126/science.289.5488.2350 · Cited by 1,409
Peutz-Jeghers syndrome is caused by mutations in a novel serine threoninekinase
Jenne, D. E., Reomann, H., Nezu, J., Friedel, W., Loff, S., Jeschke, R., Müller, O., Back, W. E., & Zimmer, M. (1998) · Nature Genetics · doi:10.1038/ng0198-38 · Cited by 1,201
The ubiquitin-modifying enzyme A20 is required for termination of Toll-like receptor responses
Boone, D. L., Turer, E. E., Lee, E. G., Ahmad, R., Wheeler, M. T., Tsui, C., Hurley, P. J., Chien, M., Chai, S., Hitotsumatsu, O., et al. (2004) · Nature Immunology · doi:10.1038/ni1110 · Cited by 1,104
A physical and functional map of the human TNF-α/NF-κB signal transduction pathway
Bouwmeester, T., Bauch, A., Ruffner, H., Angrand, P., Bergamini, G., Croughton, K., Cruciat, C., Eberhard, D., Gagneur, J., Ghidelli, S., et al. (2004) · Nature Cell Biology · doi:10.1038/ncb1086 · Cited by 1,030
Nuclear factor-?B: its role in health and disease
Kumar, A., Takada, Y., Boriek, A., & Aggarwal, B. (2004) · Journal of Molecular Medicine · doi:10.1007/s00109-004-0555-y · Cited by 933
Bukrinsky, M., Haggerty, S., Dempsey, M. P., Sharova, N., Adzhubei, A. A., Spitz, L., Lewis, P. F., Goldfarb, D. S., Emerman, M., & Stevenson, M. (1993) · Nature · doi:10.1038/365666a0 · Cited by 801
Flagged first, then by citations
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Items 101–180 of 180
Chen, S., Yang, X., Cheng, W., Ma, Y., Shang, Y., Cao, L., Chen, S., Chen, Y. Z., Wang, M., & Guo, D. (2017) · Retrovirology · doi:10.1186/s12977-017-0338-5 · Cited by 18
Zhang, D., Cheng, L.-Q., Zhai, Z., Lin, F., Zhong, B.-Y., You, Y., Zhang, N., Song, Z., Yang, X.-C., Chen, F.-R., et al. (2013) · The Journal of Rheumatology · doi:10.3899/jrheum.121391 · Cited by 18
Rudraiah, S., Shamilov, R., & Aneskievich, B. J. (2018) · Cellular Signalling · doi:10.1016/j.cellsig.2018.02.004 · Cited by 17
Zhou, X., Lu, W., Wang, Y., Li, J., & Luo, Y. (2020) · Evidence-based Complementary and Alternative Medicine · doi:10.1155/2020/6980398 · Cited by 17
Yasuike, M., Takano, T., Kondo, H., Hırono, I., & Aoki, T. (2010) · Fish & Shellfish Immunology · doi:10.1016/j.fsi.2010.07.008 · Cited by 16
Voutsadakis, I. A., & Cairoli, A. (2011) · Leukemia & lymphoma/Leukemia and lymphoma · doi:10.3109/10428194.2011.623255 · Cited by 16
Tumor necrosis factor α-induced protein 3 (A20) is dysregulated in pediatric Crohn disease
Zaidi, D., Huynh, H. Q., Carroll, M. W., Baksh, S., & Wine, E. (2018) · Clinical and Experimental Gastroenterology · doi:10.2147/ceg.s148217 · Cited by 15
Manipulation of Viral Infection by Deubiquitinating Enzymes: New Players in Host–Virus Interactions
Gu, Z., & Shi, W. (2016) · Future Microbiology · doi:10.2217/fmb-2016-0091 · Cited by 17
Oka, S., Higuchi, T., Furukawa, H., Nakamura, M., Komori, A., Abiru, S., Nagaoka, S., Hashimoto, S., Naganuma, A., Naeshiro, N., et al. (2018) · Journal of Human Genetics · doi:10.1038/s10038-018-0440-0 · Cited by 14
Erythropoietin Treatment Ameliorates Lupus Nephritis of MRL/lpr Mice
Zhang, Z., Liu, D., Zhang, X., & Wang, X. (2018) · Inflammation · doi:10.1007/s10753-018-0832-5 · Cited by 14
Mechanisms of Neuroblastoma Cell Growth Inhibition by CARP-1 Functional Mimetics
Muthu, M., Cheriyan, V. T., Munie, S., Levi, E., Frank, J., Ashour, A. E., Singh, M. S., & Rishi, A. K. (2014) · PLoS ONE · doi:10.1371/journal.pone.0102567 · Cited by 14
Samulevich, M. L., Carman, L. E., & Aneskievich, B. J. (2024) · Biomedicines · doi:10.3390/biomedicines12122723 · Cited by 13
Qu, Y., Qu, B., Wang, X., Wu, R., & Zhang, X. (2015) · Cell Biochemistry and Function · doi:10.1002/cbf.3117 · Cited by 13
Advances in the Genetics of Spondyloarthritis and Clinical Implications
O’Rielly, D. D., & Rahman, P. (2013) · Current Rheumatology Reports · doi:10.1007/s11926-013-0347-x · Cited by 15
Yang, Y., Fan, J., Han, S., & Li, E. (2019) · OncoTargets and Therapy · doi:10.2147/ott.s216138 · Cited by 12
Association between genetic variants and esophageal cancer risk
Yue, C., Li, M., Da, C., Meng, H., Lv, S., & Zhao, X. (2017) · Oncotarget · doi:10.18632/oncotarget.17006 · Cited by 12
Coilin as a regulator of NF-kB mediated inflammation in preeclampsia
Logan, M. K., Lett, K. E., McLaurin, D. M., & Hebert, M. D. (2022) · Biology Open · doi:10.1242/bio.059326 · Cited by 11
Heutz, J. W., Rogier, C., Niemantsverdriet, E., van den Eeden, S. J. F., de Jong, P. H. P., Lubberts, E., Geluk, A., & Mil, A. H. M. V. D. H. (2023) · Lara D. Veeken · doi:10.1093/rheumatology/kead238 · Cited by 11
An anti-inflammatory role of A20 zinc finger protein during trauma combined with endotoxin challenge
Liu, B., Jiang, D., Ou, Y., Hu, Z., Jiang, J., & Lei, X. (2013) · Journal of Surgical Research · doi:10.1016/j.jss.2013.06.031 · Cited by 11
Genetic polymorphisms in TNIP1 increase the risk of gastric carcinoma
Liu, Z., Shi, Y., Na, Y., Zhang, Q., Cao, S., Duan, X., Zhang, X., Yang, H., Jin, T., & Li, Y. (2016) · Oncotarget · doi:10.18632/oncotarget.9637 · Cited by 11
ABIN-1 Negatively Regulates μ-Opioid Receptor Function
Zhou, P., Jiang, J., Yan, H. M., Li, Y., Zhao, J., Wang, X., Su, R., & Gong, Z. (2017) · Molecular Pharmacology · doi:10.1124/mol.117.109009 · Cited by 11
Peng, K., Li, Y., Lu, C., & Hu, S. (2020) · Clinical and Experimental Pharmacology and Physiology · doi:10.1111/1440-1681.13291 · Cited by 10
Encarnacao, P. C., Ramirez, V. P., Zhang, C., & Aneskievich, B. J. (2013) · Biochemical Journal · doi:10.1042/bj20121666 · Cited by 9
Precision medicine in lupus nephritis: can biomarkers get us there?
Caster, D. J., Merchant, M. L., Klein, J. B., & Powell, D. W. (2018) · Translational research · doi:10.1016/j.trsl.2018.08.002 · Cited by 9
Ren, X., Wang, H., Li, C., Jiang, J.-F., Xiong, S.-D., Jin, X., Wu, L. J., & Wang, J. (2016) · Journal of Biological Chemistry · doi:10.1074/jbc.m115.706135 · Cited by 9
Thorlakson, H. H., Engen, S. A., Schreurs, O., Schenck, K., & Blix, I. J. S. (2017) · Archives of Oral Biology · doi:10.1016/j.archoralbio.2017.04.008 · Cited by 9
Lin, J., Yang, S., Wang, Y., Fang, W.-F., Tang, K., & Cheng, C. (2019) · Clinical Endocrinology · doi:10.1111/cen.14090 · Cited by 9
Kidane, Y. H., Lawrence, C. B., & Murali, T. M. (2013) · BMC Microbiology · doi:10.1186/1471-2180-13-224 · Cited by 8
Mancilla‐Herrera, I., Alvarado‐Moreno, J. A., Cérbulo‐Vázquez, A., Prieto‐Chávez, J. L., Ferat-Osorio, E. A., López-Macías, C. I. R., Estrada-Parra, S. A., Isibasi, A., & Arriaga‐Pizano, L. (2015) · Cell Biology International · doi:10.1002/cbin.10440 · Cited by 9
Shamilov, R., Vinogradova, O., & Aneskievich, B. J. (2020) · Biomolecules · doi:10.3390/biom10111531 · Cited by 9
Targeting TNIP1 as a new therapeutic avenue for major depressive disorder
Hung, Y.-Y., Tsai, C.-Y., Lee, C.-T., Fu, H., Chou, C., Yang, Y.-C., Chen, J., & Kang, H. (2025) · Brain Behavior and Immunity · doi:10.1016/j.bbi.2025.02.015 · Cited by 7
Zhang, J., Chen, Y., Shao, Y., Wu, Q., Guan, M., Zhang, W., Wan, J., & Yu, B. (2012) · Autoimmune Diseases · doi:10.1155/2012/265823 · Cited by 7
Hong, J., Lin, S., Kuo, B.-J., & Lo, Y.-C. (2021) · Journal of Molecular Biology · doi:10.1016/j.jmb.2021.167116 · Cited by 7
Sakai, Y., Uchida, K., & Nakayama, H. (2011) · Inflammation Research · doi:10.1007/s00011-011-0406-6 · Cited by 7
Expression and role of TNIP2 in multiple organ dysfunction syndrome following severe trauma
Gong, H., Sheng, X., Xue, J., & Zhu, D. (2019) · Molecular Medicine Reports · doi:10.3892/mmr.2019.9893 · Cited by 7
Genetic variants in IL-17A rs10484879 and serum levels of IL-17A are associated with psoriasis risk
Akşan, B., & Akadam-Teker, B. (2021) · Archives of Dermatological Research · doi:10.1007/s00403-021-02308-w · Cited by 6
Bălăcescu, L., Bălăcescu, O., Crişan, N., Fetică, B., Petruţ, B., Bungărdean, C. I., Rus, M., Tudoran, O. M., Meurice, G., Irimie, A., et al. (2011) · PubMed · Cited by 6
Immunomodulatory Functions of the Gastrointestinal Tract
Welcome, M. O. (2018) · Springer eBooks · doi:10.1007/978-3-319-91056-7_10 · Cited by 6
Anemia in acute experimental beryllium poisoning.
Stokinger, H. E., & Stroud, C. A. (1951) · PubMed · Cited by 6
Dobrowolski, C., Lao, S. M., Kharouf, F., Parnizari, P., Wither, J., Gladman, D. D., Garcia, L. W., Jauhal, A., & Touma, Z. (2024) · Advances in clinical chemistry · doi:10.1016/bs.acc.2024.10.002 · Cited by 5
Shen, K., & Zhang, Q. (2024) · Annals of Translational Medicine · doi:10.21037/atm-24-32 · Cited by 5
Murata, K., Villena, J., Tomosada, Y., Hara, R., Chiba, E., Shimazu, T., Aso, H., Suda, Y., Iwabuchi, N., Xiao, J., et al. (2013) · Open Journal of Veterinary Medicine · doi:10.4236/ojvm.2013.32023 · Cited by 5
Zhou, F., Liu, Z., Cai, H., Miao, Z., Wei, F., & Song, C. (2020) · Experimental and Therapeutic Medicine · doi:10.3892/etm.2020.9130 · Cited by 5
Zhou, P., Jiang, J., Dong, Z., Yan, H. M., You, Z.-D., Su, R., & Gong, Z. (2015) · Life Sciences · doi:10.1016/j.lfs.2015.10.032 · Cited by 5
Hu, W., Zhou, S., Yang, J. S., & Meng, F. (2011) · Enzyme Research · doi:10.4061/2011/328249 · Cited by 4
Cell-type-specific functionality encoded within the intrinsically disordered regions of OCT4
Ozkan, B., de Anda, M. R., Hall-Ponselé, E., Migueles, M. R. P., Alshaikh, A., Hanzevacki, M., Naama, M., Furlong, K., Roberts, G. A., Beniazza, M., et al. (2025) · Nature Communications · doi:10.1038/s41467-025-63806-3 · Cited by 3
Lee, Y., Elvitigala, D. A. S., Whang, I., Lee, S., Kim, H., Zoysa, M. D., Oh, C., Kang, D.-H., & Lee, J. (2014) · Fish & Shellfish Immunology · doi:10.1016/j.fsi.2014.06.014 · Cited by 3
Fang, M., Du, H., Hu, Y., ZHOU, X., Ouyang, H., Zhang, W., Jia, X., Li, J., Wang, Y., Nie, Q., et al. (2011) · Journal of Genetics · doi:10.1007/s12041-011-0025-6 · Cited by 3
Wang, L., Xu, X., Huo, N., Guo, H., Wang, D., & Liu, H. (2013) · Biochemistry and Cell Biology · doi:10.1139/bcb-2013-0043 · Cited by 3
Shi, Y., Zhang, L., Bao, Y., Wu, P., & Zhang, X. (2021) · Medicine · doi:10.1097/md.0000000000024843 · Cited by 3
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Nagao, T., Yoshifuji, K., Sadato, D., Motomura, Y., Saito, M., Yamamoto, K., Yamamoto, K., & Nogami, A. (2022) · Experimental Hematology · doi:10.1016/j.exphem.2022.09.005 · Cited by 3
Expression and role of ABIN1 in sepsis: In vitro and in vivo studies
Li, H., Sun, A., Meng, T., & Zhu, Y. (2020) · Open Medicine · doi:10.1515/med-2021-0008 · Cited by 3
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Cording, S., Berrabah, S., Lhermitte, L., Malamut, G., & Cerf–Bensussan, N. (2022) · Springer eBooks · doi:10.1007/978-3-030-90142-4_3 · Cited by 2
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Cai, T., & Huang, C. (2010) · Springer eBooks · doi:10.1007/978-1-4419-7554-6_3 · Cited by 2
Samulevich, M. L., Carman, L. E., Shamilov, R., & Aneskievich, B. J. (2025) · Biomolecules · doi:10.3390/biom15030453 · Cited by 1
Genetics and Epigenetic in Systemic Lupus Erythematosus
Suad, M. A. (2012) · InTech eBooks · doi:10.5772/28596 · Cited by 1
Liu, L., Zhou, H., Yang, J., & Sun, L. (2016) · Meta Gene · doi:10.1016/j.mgene.2016.10.007 · Cited by 1
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Samulevich, M. L., Carman, L. E., & Aneskievich, B. J. (2024) · Methods in molecular biology · doi:10.1007/7651_2024_525 · Cited by 1
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Jadot, V., Krzesinski, J.-M., Frenckell, C. V., Bovy, C., & Bouquegneau, A. (2017) · Néphrologie & Thérapeutique · doi:10.1016/j.nephro.2017.05.002 · Cited by 1
Analysis of Variation in Clubfoot Candidate Genes
Ester, A. R. (2010) · Digital Commons-TMC (Texas Medical Center)
Nagashima, R., Kawakami, F., Takahashi, S., Obata, F., & Kubo, M. (2014) · Viral Immunology · doi:10.1089/vim.2013.0113
Heger, K.-D. (2014) · MPG.PuRe (Max Planck Society) · doi:10.5282/edoc.17240
Novel function of RECS1 as a negative regulator of TNF-α-induced NF-κB activation
Liao, Z., Wu, M., & Chen, X. (2009) · Molecular and Cellular Biochemistry · doi:10.1007/s11010-009-0306-z
RetractedCreation of a Retroviral RNAi Knockdown System to Investigate Gene Variants in SLE
Lifeso, K. (2013) · TSpace (University of Toronto)
Perfil circadiano da expressão de microRNAs em células
Paulo, S. (2014)
Update on the Genetics of Psoriatic Arthritis
O’Rielly, D. D., Eder, L., & Rahman, P. (2016) · Springer eBooks · doi:10.1007/978-3-319-19530-8_11
Zaidi, D. (2017) · ERA: Education and Research Archive (University of Alberta) · doi:10.7939/r3ft8dx3q
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Golovach, I. Y., & Yehudіna, Y. D. (2019) · KIDNEYS · doi:10.22141/2307-1257.8.2.2019.166666
Belz, G. T. (2020) · Faculty Opinions – Post-Publication Peer Review of the Biomedical Literature · doi:10.3410/f.734631183.793575826
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Liao, D.-J., Liu, W., Jiang, Y.-H., Zhao, P., & Yao, Y. (2025) · Biochemical Genetics · doi:10.1007/s10528-025-11034-1
Pratlong, M. (2016) · theses.fr (ABES) · doi:10.70675/2f48e6ddza822z455eza9d5zf10fc679949c
Modèles et algorithmes pour l'évolution biologique
Chabrol, O. (2017) · theses.fr (ABES) · doi:10.70675/23889726zfc97z4d77zbbb6z436783a7cb06
Guégan, N. (2024) · theses.fr (ABES) · doi:10.70675/ec31ff94zb0e6z403ez9f71zfa026392bcb2
Carman, L. E., Samulevich, M. L., Abeywickrama, C. S., Murray, D. T., & Aneskievich, B. J. (2026) · International Journal of Biological Macromolecules · doi:10.1016/j.ijbiomac.2026.152717
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Mara, A. B., Makumi, A., Ozyck, R. G., Scacchia, M., Wesonga, H., Ackermann, M. R., Okumu, N. O., Chebore, W., Hunte, M. L., Miller, J. M., et al. (2026) · Frontiers in Immunology · doi:10.64898/2026.06.24.734280
Clara, C. G. E., Spoelgen, M., Roeser, S. P., Schilling, K., & Baader, S. L. (2026) · The Cerebellum · doi:10.1007/s12311-026-02080-5
Xie, J., Zhou, C., Yao, J., & Zhu, J. (2026) · Research Square · doi:10.21203/rs.3.rs-10563729/v1
ELUCIDATING THE COMPLEX INTERPLAY BETWEEN HOST AND VIRUS By
Gao, L., & Gao, L. (2016)
Metadata
- Authors
- Verstrepen, L., Carpentier, I., Verhelst, K., & Beyaert, R.
- Affiliations
- Vlaams Instituut voor Biotechnologie (BE)
- Corresponding author
- Beyaert, Rudi
- ORCID
- Beyaert, Rudi
- Venue
- Biochemical Pharmacology
- Publisher
- Elsevier BV
- Published
- 2009-07
- Volume
- 78
- Issue
- 2
- Pages
- 105-114
- ISSN
- 0006-2952 (ISSN-L)
- OpenAlex
- W2010220327
- Cited by
- 180
- References
- 76
- Citations by year
- 2026: 5 · 2025: 5 · 2024: 7 · 2023: 1 · 2022: 5 · 2021: 6 · 2020: 10 · 2019: 5 · 2018: 16 · 2017: 16 · 2016: 18 · 2015: 11 · 2014: 12 · 2013: 15 · 2012: 12
- FWCI
- 0.94
- Type
- journal article
- Language
- en
- Open access
- bronze
- doi.org
- Licence
- Locations
- Biochemical Pharmacology (publishedVersion)
- PubMed (publishedVersion)
- HAL (submittedVersion, other-oa)
- Ghent University Academic Bibliography (Ghent University) (submittedVersion)
- Trinity's Access to Research Output (TARA) (Trinity College Dublin) (submittedVersion)
- Funders
- Agentschap voor Innovatie door Wetenschap en Technologie
- Universiteit Gent
- Topics
- Life Sciences › Biochemistry, Genetics and Molecular Biology › Cancer Research › NF-κB Signaling Pathways
- Life Sciences › Immunology and Microbiology › Immunology › Immune Response and Inflammation
- Life Sciences › Biochemistry, Genetics and Molecular Biology › Molecular Biology › Signaling Pathways in Disease
- Keywords
- Abin, A20, NF-κB, ubiquitin-binding domain, TNF-induced apoptosis, negative feedback regulation, ERK activation, macrophages, embryonic lethality, immunity, tissue homeostasis, ubiquitinated proteins
- MeSH terms
- Tumor Necrosis Factor alpha-Induced Protein 3, Amino Acid Sequence, Animals, DNA-Binding Proteins, Humans, Molecular Sequence Data, Nuclear Proteins, Protein Binding, Proteins, Signal Transduction, NF-kappa B, Apoptosis, Intracellular Signaling Peptides and Proteins, Adaptor Proteins, Signal Transducing, Apoptosis Regulatory Proteins
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