A novel brain-enriched E3 ubiquitin ligase RNF182 is up regulated in the brains of Alzheimer's patients and targets ATP6V0C for degradation
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BACKGROUND: Alterations in multiple cellular pathways contribute to the development of chronic neurodegeneration such as a sporadic Alzheimer's disease (AD). These, in turn, involve changes in gene expression, amongst which are genes regulating protein processing and turnover such as the components of the ubiquitin-proteosome system. Recently, we have identified a cDNA whose expression was altered in AD brains. It contained an open reading frame of 247 amino acids and represented a novel RING finger protein, RNF182. Here we examined its biochemical properties and putative role in brain cells. RESULTS: RNF182 is a low abundance cytoplasmic protein expressed preferentially in the brain. Its expression was elevated in post-mortem AD brain tissue and the gene could be up regulated in vitro in cultured neurons subjected to cell death-inducing injuries. Subsequently, we have established that RNF182 protein possessed an E3 ubiquitin ligase activity and stimulated the E2-dependent polyubiquitination in vitro. Yeast two-hybrid screening, overexpression and co-precipitation approaches revealed, both in vitro and in vivo, an interaction between RNF182 and ATP6V0C, known for its role in the formation of gap junction complexes and neurotransmitter release channels. The data indicated that RNF182 targeted ATP6V0C for degradation by the ubiquitin-proteosome pathway. Overexpression of RNF182 reduced cell viability and it would appear that by itself the gene can disrupt cellular homeostasis. CONCLUSION: Taken together, we have identified a novel brain-enriched RING finger E3 ligase, which was up regulated in AD brains and neuronal cells exposed to injurious insults. It interacted with ATP6V0C protein suggesting that it may play a very specific role in controlling the turnover of an essential component of neurotransmitter release machinery.
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Several CNS-specific E3 ligases have emerged, such as RNF182 and TRIM9.
“several central nervous system (CNS)-specific E3 ligases have emerged, such as RNF182 (ref.148) and tripartite motif-containing protein 9 (TRIM9)149”
From PROTAC targeted protein degraders: the past is prologue (2022) · cites this paper as [148]
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Mutations in the parkin gene cause autosomal recessive juvenile parkinsonism
Kitada, T., Asakawa, S., Hattori, N., Matsumine, H., Yamamura, Y., Minoshima, S., Yokochi, M., Mizuno, Y., & Shimizu, N. (1998) · Nature · doi:10.1038/33416 · Cited by 5,227 · see citing works
Characteristics of a human cell line transformed by DNA from human adenovirus type 5
Graham, F. L., Russell, W. C., Smiley, J., & Nairn, R. (1977) · Journal of General Virology · doi:10.1099/0022-1317-36-1-59 · Cited by 4,793 · see citing works
RING fingers mediate ubiquitin-conjugating enzyme (E2)-dependent ubiquitination
Lorick, K. L., Jensen, J. P., Fang, S., Ong, A. M., Hatakeyama, S., & Weissman, A. M. (1999) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.96.20.11364 · Cited by 1,151 · see citing works
Colangelo, V., Schurr, J., Ball, M. J., Pelaez, R. P., Bazan, N. G., & Lukiw, W. J. (2002) · Journal of Neuroscience Research · doi:10.1002/jnr.10351 · Cited by 517 · see citing works
Pleasure, S. J., & LEE, V. M.-Y. (1993) · Journal of Neuroscience Research · doi:10.1002/jnr.490350603 · Cited by 437 · see citing works
Boutell, C., Sadis, S., & Everett, R. D. (2002) · Journal of Virology · doi:10.1128/jvi.76.2.841-850.2002 · Cited by 386 · see citing works
Milner, R. J., & Sutcliffe, J. G. (1983) · Nucleic Acids Research · doi:10.1093/nar/11.16.5497 · Cited by 329 · see citing works
Structure and Properties of the Vacuolar (H+)-ATPases
Forgac, M. D. (1999) · Journal of Biological Chemistry · doi:10.1074/jbc.274.19.12951 · Cited by 306 · see citing works
A Gene Expression Profile of Alzheimer's Disease
Loring, J. F., Wen, X., Lee, J. M., Seilhamer, J. J., & Somogyi, R. (2001) · DNA and Cell Biology · doi:10.1089/10445490152717541 · Cited by 300 · see citing works
In vivo evidence of CHIP up‐regulation attenuating tau aggregation
Sahara, N., Murayama, M., Mizoroki, T., Urushitani, M., Imai, Y., Takahashi, R., Murata, S., Tanaka, K., & Takashima, A. (2005) · Journal of Neurochemistry · doi:10.1111/j.1471-4159.2005.03272.x · Cited by 208 · see citing works
Role of the ubiquitin proteasome system in Alzheimer's disease
Upadhya, S. C., & Hegde, A. N. (2007) · BMC Biochemistry · doi:10.1186/1471-2091-8-s1-s12 · Cited by 184 · see citing works
Staring, a Novel E3 Ubiquitin-Protein Ligase That Targets Syntaxin 1 for Degradation
Chin, L., Vavalle, J. P., & Li, L. (2002) · Journal of Biological Chemistry · doi:10.1074/jbc.m203300200 · Cited by 121 · see citing works
Niikura, T., Hashimoto, Y., Tajima, H., Ishizaka, M., Yamagishi, Y., Kawasumi, M., Nawa, M., Terashita, K., Aiso, S., & Nishimoto, I. (2003) · European Journal of Neuroscience · doi:10.1046/j.1460-9568.2003.02553.x · Cited by 115 · see citing works
Siah-1 Facilitates Ubiquitination and Degradation of Synphilin-1
Nagano, Y., Yamashita, H., Takahashi, T., Kishida, S., Nakamura, T., Iseki, E., Hattori, N., Mizuno, Y., Kikuchi, A., & Matsumoto, M. (2003) · Journal of Biological Chemistry · doi:10.1074/jbc.m306347200 · Cited by 113 · see citing works
Pasinetti, G. M. (2001) · Journal of Neuroscience Research · doi:10.1002/jnr.1176 · Cited by 111 · see citing works
Microarray Analysis in Alzheimer's Disease and Normal Aging
Ricciarelli, R., d’Abramo, C., Massone, S., Marinari, U. M., Pronzato, M. A., & Tabaton, M. (2004) · IUBMB Life · doi:10.1080/15216540412331286002 · Cited by 88 · see citing works
Antoine, J.-C. G., Cinotti, L., Tilikete, C., Bouhour, F., Camdessanch�, J. P., Confavreux, C., Vighetto, A., Renault‐Mannel, V., Michel, D., & Honnorat, J. (2000) · Annals of Neurology · doi:10.1002/1531-8249(200007)48:1 · Cited by 86 · see citing works
Drmanac, S., Stavropoulos, N. A., Labat, I., Vonau, J., Hauser, B. A., Soares, M. B., & Drmanac, R. (1996) · Genomics · doi:10.1006/geno.1996.0517 · Cited by 80 · see citing works
Dorfin Localizes to Lewy Bodies and Ubiquitylates Synphilin-1
Ito, T., Niwa, J.-I., Hishikawa, N., Ishigaki, S., Doyu, M., & Sobue, G. (2003) · Journal of Biological Chemistry · doi:10.1074/jbc.m302763200 · Cited by 78 · see citing works
Reddy, P. H., & McWeeney, S. K. (2005) · Neurobiology of Aging · doi:10.1016/j.neurobiolaging.2005.04.014 · Cited by 73 · see citing works
Shen, H., Sikorska, M., Leblanc, J. E., Walker, P. R., & Liu, Q. Y. (2006) · APOPTOSIS · doi:10.1007/s10495-006-6303-8 · Cited by 66 · see citing works
Self-citationNeurotransmitter release: the dark side of the vacuolar‐H+ATPase
Morel, N. (2003) · Biology of the Cell · doi:10.1016/s0248-4900(03)00075-3 · Cited by 65 · see citing works
Fang, H., Chartier, J., Sodja, C., Desbois, A., Ribecco‐Lutkiewicz, M., Walker, P. R., & Sikorska, M. (2003) · Journal of Biological Chemistry · doi:10.1074/jbc.m211539200 · Cited by 61 · see citing works
Self-citationData mining of gene expression changes in Alzheimer brain
Walker, P. R., Smith, B., Liu, Q. Y., Famili, A. F., Valdés, J. J., Liu, Z., & Lach, B. (2004) · Artificial Intelligence in Medicine · doi:10.1016/j.artmed.2004.01.008 · Cited by 60 · see citing works
Self-citationDuctin – a proton pump component, a gap junction channel and a neurotransmitter release channel
Finbow, M. E., Harrison, M. A., & Jones, P. (1995) · BioEssays · doi:10.1002/bies.950170311 · Cited by 59 · see citing works
Siah1 Interacts with the Scaffold Protein POSH to Promote JNK Activation and Apoptosis
Xu, Z., Sproul, A. A., Wang, W., Kukekov, N. V., & Greene, L. A. (2005) · Journal of Biological Chemistry · doi:10.1074/jbc.m509060200 · Cited by 58 · see citing works
Molecular cloning of cDNA encoding the 16 KDa subunit of vacuolar H+-ATPase from mouse cerebellum
Hanada, H., Hasebe, M., Moriyama, Y., Maeda, M., & Futai, M. (1991) · Biochemical and Biophysical Research Communications · doi:10.1016/0006-291x(91)90391-j · Cited by 51 · see citing works
Lee, S.-J., Choi, J.-Y., Sung, Y.-M., Park, H., Rhim, H., & Kang, S. (2001) · FEBS Letters · doi:10.1016/s0014-5793(01)02689-8 · Cited by 46 · see citing works
Identification of functional dopamine receptors in human teratocarcinoma NT2 cells
Sodja, C., Fang, H., Dasgupta, T., Ribecco, M. T. S., Walker, P. R., & Sikorska, M. (2002) · Molecular Brain Research · doi:10.1016/s0169-328x(01)00324-2 · Cited by 46 · see citing works
Self-citationDNaseY: A Rat DNaseI-like Gene Coding for a Constitutively Expressed Chromatin-Bound Endonuclease‡
Liu, Q. Y., Pandey, S., Singh, R. K., Lin, W., Ribecco, M. T. S., Borowy‐Borowski, H., Smith, B., Leblanc, J. E., Walker, P. R., & Sikorska, M. (1998) · Biochemistry · doi:10.1021/bi9800597 · Cited by 44 · see citing works
Self-citationvon Rotz, R. C., Kins, S., Hipfel, R., von der Kammer, H., & Nitsch, R. M. (2005) · European Journal of Neuroscience · doi:10.1111/j.1460-9568.2005.03977.x · Cited by 21 · see citing works
Lee, I., Skinner, M. A., Guo, H., Sujan, A., & Pierce, M. (2004) · Journal of Biological Chemistry · doi:10.1074/jbc.m405717200 · Cited by 21 · see citing works
Liu, Q. Y., Sooknanan, R., Malek, L. T., Ribecco‐Lutkiewicz, M., Lei, J. X., Shen, H., Lach, B., Walker, P. R., Martin, J., & Sikorska, M. (2006) · BMC Genomics · doi:10.1186/1471-2164-7-286 · Cited by 12 · see citing works
Self-citationNeurodegeneration caused by ER stress?
Takahashi, R. (2004) · Folia Pharmacologica Japonica · doi:10.1254/fpj.124.375 · Cited by 3 · see citing works
Staring, a Novel E3 Ubiquitin-Protein Ligase That Targets Syntaxin 1 for Degradation
Chin, L. S., Vavalle, J. P., & Li, A. (2021) · Carolina Digital Repository (University of North Carolina at Chapel Hill) · doi:10.17615/1b31-j215 · Cited by 2 · see citing works
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PROTAC targeted protein degraders: the past is prologue
Békés, M., Langley, D. R., & Crews, C. M. (2022) · Nature Reviews Drug Discovery · doi:10.1038/s41573-021-00371-6 · Cited by 3,395 · see citing works
Ubiquitin signalling in neurodegeneration: mechanisms and therapeutic opportunities
Schmidt, M. F., Gan, Z. Y., Komander, D., & Dewson, G. (2021) · Cell Death and Differentiation · doi:10.1038/s41418-020-00706-7 · Cited by 373 · see citing works
Tau degradation: The ubiquitin–proteasome system versus the autophagy-lysosome system
Lee, M. J., Lee, J. H., & Rubinsztein, D. C. (2013) · Progress in Neurobiology · doi:10.1016/j.pneurobio.2013.03.001 · Cited by 364 · see citing works
Ubiquitination in postsynaptic function and plasticity
Mabb, A. M., & Ehlers, M. D. (2010) · Annual Review of Cell and Developmental Biology · doi:10.1146/annurev-cellbio-100109-104129 · Cited by 255 · see citing works
The RING finger protein family in health and disease
Cai, C., Tang, Y., Zhai, J., & Zheng, C. (2022) · Signal Transduction and Targeted Therapy · doi:10.1038/s41392-022-01152-2 · Cited by 194 · see citing works
Proteostasis in Huntington's disease: disease mechanisms and therapeutic opportunities
Harding, R., & Tong, Y. (2018) · Acta Pharmacologica Sinica · doi:10.1038/aps.2018.11 · Cited by 111 · see citing works
McGowen, M. R., Grossman, L. I., & Wildman, D. E. (2012) · Proceedings of the Royal Society B Biological Sciences · doi:10.1098/rspb.2012.0869 · Cited by 100 · see citing works
The Role of the Transmembrane RING Finger Proteins in Cellular and Organelle Function
Nakamura, N. (2011) · Membranes · doi:10.3390/membranes1040354 · Cited by 92 · see citing works
Kaneko, M., 岩瀬, 郁., Yamasaki, Y., Takai, T., Wu, Y. L., Kanemoto, S., Matsuhisa, K., Asada, R., Okuma, Y., Watanabe, T., et al. (2016) · Scientific Reports · doi:10.1038/srep30955 · Cited by 81 · see citing works
Mangieri, L. R., Mader, B. J., Thomas, C. E., Taylor, C. A., Luker, A. M., Tse, T. E., Huisingh, C., & Shacka, J. J. (2014) · PLoS ONE · doi:10.1371/journal.pone.0093257 · Cited by 69 · see citing works
Kim, S., Cho, Y.-S., Kim, Y., Park, J., Yoo, S., Gwak, J., Kim, Y., Gwon, Y., Kam, T., & Jung, Y. (2023) · Autophagy · doi:10.1080/15548627.2023.2181614 · Cited by 65 · see citing works
Ubiquitin and Ubiquitin-like Proteins in Cancer, Neurodegenerative Disorders, and Heart Diseases
Hwang, J., Lee, A., & Kho, C. (2022) · International Journal of Molecular Sciences · doi:10.3390/ijms23095053 · Cited by 62 · see citing works
Kumar, P., Pradhan, K., Ramani, K., Ambasta, R. K., & Querfurth, H. W. (2011) · Journal of Neurochemistry · doi:10.1111/j.1471-4159.2011.07588.x · Cited by 61 · see citing works
Okamoto, T., Imaizumi, K., & Kaneko, M. (2020) · International Journal of Molecular Sciences · doi:10.3390/ijms21113921 · Cited by 60 · see citing works
PCDHB14 promotes ferroptosis and is a novel tumor suppressor in hepatocellular carcinoma
Liu, Y., Ouyang, L., Mao, C., Chen, Y., Li, T., Liu, N., Wang, Z., Lai, W., Zhou, Y., Cao, Y., et al. (2022) · Oncogene · doi:10.1038/s41388-022-02370-2 · Cited by 58 · see citing works
Reeves, M. E., Baldwin, S. W., Baldwin, M. L., Chen, S., Moretz, J. M., Aragon, R. J., Li, X., Strong, D. D., Mohan, S., & Amaar, Y. G. (2010) · BMC Cancer · doi:10.1186/1471-2407-10-562 · Cited by 51 · see citing works
Cao, Y., Sun, Y., Chang, H., Sun, X., & Yang, S. (2019) · FEBS Letters · doi:10.1002/1873-3468.13583 · Cited by 51 · see citing works
Ubiquitin biology in neurodegenerative disorders: From impairment to therapeutic strategies
Kumar, D., Ambasta, R. K., & Kumar, P. (2020) · Ageing Research Reviews · doi:10.1016/j.arr.2020.101078 · Cited by 49 · see citing works
Potjewyd, F., & Axtman, A. D. (2021) · Frontiers in Cellular Neuroscience · doi:10.3389/fncel.2021.768655 · Cited by 39 · see citing works
Chernus, J. M., Allen, E. G., Zeng, Z., Hoffmann, E. R., Hassold, T. J., Feingold, E., & Sherman, S. L. (2019) · PLoS Genetics · doi:10.1371/journal.pgen.1008414 · Cited by 32 · see citing works
Nectoux, J., Fichou, Y., Rosas‐Vargas, H., Cagnard, N., Bahi‐Buisson, N., Nusbaum, P., Letourneur, F., Chelly, J., & Bienvenu, T. (2010) · Journal of Cellular and Molecular Medicine · doi:10.1111/j.1582-4934.2010.01107.x · Cited by 29 · see citing works
Targeted protein degradation in CNS disorders: a promising route to novel therapeutics?
Kuemper, S., Cairns, A. G., Birchall, K., Yao, Z., & Large, J. M. (2024) · Frontiers in Molecular Neuroscience · doi:10.3389/fnmol.2024.1370509 · Cited by 27 · see citing works
Pan, B., Lu, X., Han, X., Huan, J., Gao, D., Cui, S., Ju, X., Zhang, Y., Xu, S., Song, J., et al. (2021) · ACS Omega · doi:10.1021/acsomega.1c04434 · Cited by 23 · see citing works
Roles of Ubiquitin Ligases and Deubiquitylases in Alzheimer’s Disease
Jia, F., & Fu, L. (2025) · Molecular Neurobiology · doi:10.1007/s12035-025-04739-2 · Cited by 21 · see citing works
Altered Proteostasis in Neurodegenerative Tauopathies
Papanikolopoulou, K., & Skoulakis, E. M. C. (2020) · Advances in experimental medicine and biology · doi:10.1007/978-3-030-38266-7_7 · Cited by 21 · see citing works
Miyashita, T., Wintzer, M. E., Kurotani, T., Konishi, T., Ichinohe, N., & Rockland, K. S. (2009) · Cerebral Cortex · doi:10.1093/cercor/bhp093 · Cited by 21 · see citing works
Biswas, D., Shenoy, S. V., Chetanya, C., Lachén‐Montes, M., Barpanda, A., Athithyan, A. P., Ghosh, S., Ausín, K., Zelaya, M. V., Fernández‐Irigoyen, J., et al. (2021) · Journal of Proteome Research · doi:10.1021/acs.jproteome.1c00511 · Cited by 19 · see citing works
Unique ability of pandemic influenza to downregulate the genes involved in neuronal disorders
Ebrahimie, E., Nurollah, Z., Ebrahimi, M., Hemmatzadeh, F., & Ignjatovic, J. (2015) · Molecular Biology Reports · doi:10.1007/s11033-015-3916-4 · Cited by 16 · see citing works
Geng, R., Zheng, Y., Zhao, L., Huang, X., Qiang, R., Zhang, R., Guo, X., & Li, R. (2020) · Frontiers in Genetics · doi:10.3389/fgene.2020.595733 · Cited by 16 · see citing works
Basappa, J., Turcan, Ş., & Vetter, D. E. (2010) · Journal of Neuroscience Research · doi:10.1002/jnr.22449 · Cited by 15 · see citing works
Kim, A. J., Kim, H., Jee, H. J., Song, N., Kim, M., Bae, Y., Chung, J. H., & Yun, J. (2011) · Biochimica et Biophysica Acta (BBA) - Molecular Cell Research · doi:10.1016/j.bbamcr.2011.03.012 · Cited by 14 · see citing works
Lei, J. X., Cassone, C. G., Luebbert, C., & Liu, Q. Y. (2011) · Molecular Neurodegeneration · doi:10.1186/1750-1326-6-9 · Cited by 13 · see citing works
Self-citationUbiquitin proteasome system networks in the neurological disorders
Anuppalle, M., Maddirevula, S., Huh, T., & Rhee, M. (2013) · Animal Cells and Systems · doi:10.1080/19768354.2013.855256 · Cited by 12 · see citing works
Epithelial-to-mesenchymal transition as a central driver of tumor cell plasticity
Jiménez-Castaño, R., & Nieto, M. A. (2026) · Nature Cancer · doi:10.1038/s43018-026-01154-x · Cited by 11 · see citing works
Inhibition of RNF182 mediated by Bap promotes non-small cell lung cancer progression
Liu, Y., Ouyang, L., Mao, C., Chen, Y., Liu, N., Chen, L., Shi, Y., Xiao, D., Liu, S., & Tao, Y. (2023) · Frontiers in Oncology · doi:10.3389/fonc.2022.1009508 · Cited by 11 · see citing works
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Kanbar, K., Darzi, R. E., & Jaalouk, D. E. (2024) · Frontiers in Genetics · doi:10.3389/fgene.2024.1434002 · Cited by 17 · see citing works
Wang, J., Wei, Z., Gao, Y., Liu, C. J., & Sun, J. (2018) · Journal of Cellular Biochemistry · doi:10.1002/jcb.28038 · Cited by 11 · see citing works
E3 Ubiquitin Ligases: Structures, Biological Functions, Diseases, and Therapy
Wang, H., Peng, J., Li, H., Lan, Y., Guo, J., Qiu, Q., & Huang, X. (2025) · MedComm · doi:10.1002/mco2.70528 · Cited by 10 · see citing works
Kang, D., Baek, Y., & Lee, J. (2022) · Cells · doi:10.3390/cells11244062 · Cited by 9 · see citing works
Cukier, H. N., Duarte, C. L., Laverde-Paz, M. J., Simon, S. A., Booven, D. J. V., Miyares, A. T., Whitehead, P. L., Hamilton‐Nelson, K. L., Adams, L. D., Carney, R. M., et al. (2023) · Neurobiology of Aging · doi:10.1016/j.neurobiolaging.2023.07.007 · Cited by 9 · see citing works
Mahzarnia, A., Lutz, M. W., & Badea, A. (2023) · Journal of Alzheimer s Disease · doi:10.3233/jad-230934 · Cited by 7 · see citing works
Tarbox, H. E., Branch, A., & Fried, S. D. (2025) · Science Advances · doi:10.1126/sciadv.adt3778 · Cited by 8 · see citing works
Leveraging targeted kinase degradation as a novel therapeutic strategy for Alzheimer's disease
Tassinari, E., & Milelli, A. (2025) · RSC Medicinal Chemistry · doi:10.1039/d5md00681c · Cited by 5 · see citing works
Ubiquitin-Proteasome System Dysregulation in Alzheimer’s Disease Impacts Protein AbundancePreprint
Collins, M. A., Friedrich, C., Elcheikhali, M., Stewart, P., Derks, J., Connors, T. R., Altig, K., Melloni, A. N., Petelski, A. A., Oakley, D. H., et al. (2025) · bioRxiv (Cold Spring Harbor Laboratory) · doi:10.1101/2025.05.29.656728 · Cited by 5 · see citing works
Advances in novel modification strategies for enhancing the tumor tissue specificity of PROTACs
Hu, L., Wu, S., Wang, W., He, H., Che, J., Wu, M., & Dong, X. (2025) · European Journal of Medicinal Chemistry · doi:10.1016/j.ejmech.2025.118499 · Cited by 2 · see citing works
Wu, L., Fu, Q., Gao, Y., Jiang, B., Zheng, H., Zhong, Z., Zhang, G., Lu, Y., Zhang, Z., Li, R., et al. (2025) · Journal of Psychiatric Research · doi:10.1016/j.jpsychires.2025.12.037 · Cited by 2 · see citing works
Monaco, M., Pinto, A. M., & Grilli, M. (2026) · Biomedicines · doi:10.3390/biomedicines14010216 · Cited by 2 · see citing works
Wang, Y., Li, B.-W., Xin, C., Zhang, K., Wu, H., Cui, W.-Q., Xu, X.-Q., Zhang, J., & Zhi, H. (2025) · Molecular Neurobiology · doi:10.1007/s12035-025-04785-w · Cited by 2 · see citing works
Ubiquitin ligases: Proteolytic signaling, protein turnover, and disease
dos Passos, P. M. S., de Correia, C. R. S. T. B., de Oliveira, C. A. B., Spagnol, V., Martins, I. F. M., & Teixeira, F. R. (2021) · Elsevier eBooks · doi:10.1016/b978-0-323-85696-6.00010-x · Cited by 2 · see citing works
Methylation in Colorectal Cancer
Mokarram, P., Estiar, M. A., & Ashktorab, H. (2015) · Springer eBooks · doi:10.1007/978-94-017-9639-2_13 · Cited by 1 · see citing works
Zhang, Y., Li, J., Sun, Q., Zhou, P., Wu, P., Ji, Z., Li, Y., & Shi, H. (2025) · Neural Regeneration Research · doi:10.4103/nrr.nrr-d-25-00705 · Cited by 1 · see citing works
E3 Ubiquitin Ligases as Molecular Machines and Platforms for Drug Development
Ioris, R. M., Ferris, K., & D’Angiolella, V. (2022) · Wiley eBooks · doi:10.1002/9783527836208.ch3 · Cited by 1 · see citing works
Vastrad, B. M., Vastrad, C. M., & Kotturshetti, I. (2020) · medRxiv · doi:10.1101/2020.12.21.20248688
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Wang, Y., Li, H., Zhang, K.-X., Wu, H., Cui, W., Xu, X., Zhi, H., & Zhang, J.-W. (2023) · Research Square · doi:10.21203/rs.3.rs-3450819/v1
Zhang, J., Nawaz, A., Wang, S., Tian, Q., Geng, C.-Y., Hai-Jin, Y., & Ji, S. (2025) · Archives animal breeding/Archiv für Tierzucht · doi:10.5194/aab-68-299-2025
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He, W., Ch, F., Liu, M., Qin, H., Wu, Y., Deng, C., & Zhu, X. (2026) · Respiratory Research · doi:10.1186/s12931-026-03612-7
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Kearney, A., Łukomska, A., Brady, J., Damania, A., Gupta, M., & Trakhtenberg, E. F. (2026) · Molecular Therapy — Nucleic Acids · doi:10.1016/j.omtn.2026.102922
Overexpression of the Ubiquitin Ligase RNF182 Is Associated with High-Grade Gliomas
Russo, V., Russo, M., Oliva, M. A., Alborghetti, M., Caridi, M., Giangaspero, F., & Arcella, A. (2026) · Cancers · doi:10.3390/cancers18081217
Challenges in recent Alzheimer's disease therapeutic approaches
Kim, C.-H. (2026) · Elsevier eBooks · doi:10.1016/b978-0-443-45844-6.00017-2
- Authors
- Liu, Q., Lei, J. X., Sikorska, M., & Liu, R.
- Affiliations
- University of Ottawa (CA)
- Institute for Biological Sciences (CA)
- University of North Dakota (US)
- Corresponding author
- Liu, Qing
- ORCID
- Liu, Qing
- Venue
- Molecular Neurodegeneration
- Published
- 2008
- Volume
- 3
- Issue
- 1
- Pages
- 4
- ISSN
- 1750-1326 (ISSN-L)
- PMC
- PMC2279130
- OpenAlex
- W2041140379
- Cited by
- 66
- References
- 35
- Citations by year
- 2026: 8 · 2025: 10 · 2024: 3 · 2023: 6 · 2022: 7 · 2021: 5 · 2020: 5 · 2019: 2 · 2018: 3 · 2016: 1 · 2015: 2 · 2014: 1 · 2013: 2 · 2012: 1
- FWCI
- 1.37
- Type
- journal article
- Language
- en
- Open access
- gold
- doi.org
- Licence
- cc-by
- Locations
- Molecular Neurodegeneration (publishedVersion, cc-by)
- PubMed Central (publishedVersion, cc-by)
- PubMed (publishedVersion)
- NPARC (submittedVersion)
- DOAJ (DOAJ: Directory of Open Access Journals) (submittedVersion, cc-by-sa)
- Topics
- Life Sciences › Biochemistry, Genetics and Molecular Biology › Molecular Biology › Ubiquitin and proteasome pathways
- Health Sciences › Medicine › Physiology › Alzheimer's disease research and treatments
- Health Sciences › Medicine › Epidemiology › Autophagy in Disease and Therapy
- Keywords
- E3 ubiquitin ligase, RING finger protein, Alzheimer's disease, ATP6V0C, ubiquitin-proteasome system, protein degradation, polyubiquitination, neuronal injury, gap junctions, neurotransmitter release, postmortem brain, neurodegeneration
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