Ubiquitin-independent function of optineurin in autophagic clearance of protein aggregates

The zebrafish book : a guide for the laboratory use of zebrafish (Danio rerio)

Westerfield, M. (1995) · Medical Entomology and Zoology · Cited by 6,813

p62/SQSTM1 Binds Directly to Atg8/LC3 to Facilitate Degradation of Ubiquitinated Protein Aggregates by Autophagy

Pankiv, S., Clausen, T. H., Lamark, T., Brech, A., Bruun, J.-A., Outzen, H., Øvervatn, A., Bjørkøy, G., & Johansen, T. (2007) · Journal of Biological Chemistry · doi:10.1074/jbc.m702824200 · Cited by 4,578

Motor Neuron Degeneration in Mice that Express a Human Cu,Zn Superoxide Dismutase Mutation

Gurney, M. E., Pu, H., Chiu, A. Y., Dal Canto, M. C., Polchow, C. Y., Alexander, D. D., Caliendo, J., Hentati, A., Kwon, Y. W., Deng, H.-X., et al. (1994) · Science · doi:10.1126/science.8209258 · Cited by 4,143

Van Damme A.

Haine, M. M.-L., & Meeùs, N. (1986) · Cited by 3,464

The Role of Atg Proteins in Autophagosome Formation

Mizushima, N., Yoshimori, T., & Ohsumi, Y. (2011) · Annual Review of Cell and Developmental Biology · doi:10.1146/annurev-cellbio-092910-154005 · Cited by 2,978

Network organization of the human autophagy system

Behrends, C., Sowa, M. E., Gygi, S. P., & Harper, J. W. (2010) · Nature · doi:10.1038/nature09204 · Cited by 1,554

Nix is a selective autophagy receptor for mitochondrial clearance

Novak, I., Kirkin, V., McEwan, D. G., Zhang, J., Wild, P., Rozenknop, A., Rogov, V., Löhr, F., Popovic, D., Occhipinti, A., et al. (2010) · The EMBO Reports · doi:10.1038/embor.2009.256 · Cited by 1,309 · cited 2×

Phosphorylation of the Autophagy Receptor Optineurin Restricts Salmonella Growth

Wild, P., Farhan, H., McEwan, D. G., Wagner, S., Rogov, V. V., Brady, N. R., Richter, B., Korac, J., Waidmann, O., Choudhary, C., et al. (2011) · Science · doi:10.1126/science.1205405 · Cited by 1,298

A Role for Ubiquitin in Selective Autophagy

Kirkin, V., McEwan, D. G., Novak, I., & Đikić, I. (2009) · Molecular Cell · doi:10.1016/j.molcel.2009.04.026 · Cited by 1,268

Mutations of optineurin in amyotrophic lateral sclerosis

Maruyama, H., Morino, H., Ito, H., Izumi, Y., Kato, H., Watanabe, Y., Kinoshita, Y., Kamada, M., Nodera, H., Suzuki, H., et al. (2010) · Nature · doi:10.1038/nature08971 · Cited by 1,265

FUS/TLS acts as an aggregation-dependent modifier of polyglutamine disease model mice

Kino, Y., Washizu, C., Kurosawa, M., Yamada, M., Doi, H., Takumi, T., Adachi, H., Katsuno, M., Sobue, G., Hicks, G. G., et al. (2016) · Scientific Reports · doi:10.1038/srep35236 · Cited by 21

Optineurin deletion disrupts metabotropic glutamate receptor 5-mediated regulation of ERK1/2, GSK3β/ZBTB16, mTOR/ULK1 signaling in autophagy

Ibrahim, K. S., McLaren, C., Abd‐Elrahman, K. S., & Ferguson, S. S. G. (2021) · Biochemical Pharmacology · doi:10.1016/j.bcp.2021.114427 · Cited by 21

The fine-tuning of proteolytic pathways in Alzheimer’s disease

Cecarini, V., Bonfili, L., Cuccioloni, M., Mozzicafreddo, M., Angeletti, M., Keller, J. N., & Eleuteri, A. M. (2016) · Cellular and Molecular Life Sciences · doi:10.1007/s00018-016-2238-6 · Cited by 21

From the Cover: Alterations in Optineurin Expression and Localization in Pre-clinical Parkinson’s Disease Models

Wise, J. P., & Cannon, J. (2016) · Toxicological Sciences · doi:10.1093/toxsci/kfw133 · Cited by 20

Human Induced Pluripotent Stem Cell Models of Neurodegenerative Disorders for Studying the Biomedical Implications of Autophagy

Seranova, E., Palhegyi, A. M., Verma, S., Dimova, S., Lasry, R., Naama, M., Sun, C., Barrett, T. G., Rosenstock, T. R., Kumar, D., et al. (2020) · Journal of Molecular Biology · doi:10.1016/j.jmb.2020.01.024 · Cited by 20

The Role of Mitophagy in Various Neurological Diseases as a Therapeutic Approach

Kaur, S., Sharma, N., Kumar, V., Sharma, D., Devi, B., Kapil, L., Singh, C., & Singh, A. (2022) · Cellular and Molecular Neurobiology · doi:10.1007/s10571-022-01302-8 · Cited by 21

The interplay of microRNAs and transcription factors in autophagy regulation in nonalcoholic fatty liver disease

Kim, Y., Lee, D.-H., Park, S., Jeon, T., & Jung, C. H. (2021) · Experimental & Molecular Medicine · doi:10.1038/s12276-021-00611-0 · Cited by 19

Yeast genetic interaction screen of human genes associated with amyotrophic lateral sclerosis: identification of MAP2K5 kinase as a potential drug targetPreprint

Jo, M., Chung, A. Y., Yachie, N., Seo, M., Jeon, H., Nam, Y., Seo, Y., Kim, E., Zhong, Q., Vidal, M., et al. (2017) · Genome Research · doi:10.1101/gr.211649.116 · Cited by 18

Protein Aggregates and Aggrephagy in Myopathies

Gibertini, S., Ruggieri, A., Cheli, M., & Maggi, L. (2023) · International Journal of Molecular Sciences · doi:10.3390/ijms24098456 · Cited by 20

Molecular Insights into Aggrephagy: Their Cellular Functions in the Context of Neurodegenerative Diseases

Cóppola-Segovia, V., & Reggiori, F. (2024) · Journal of Molecular Biology · doi:10.1016/j.jmb.2024.168493 · Cited by 18

Could astrocytes be the primary target of an offending agent causing the primary degenerative diseases of the human central nervous system? A hypothesis

Sica, R. E. P. (2015) · Medical Hypotheses · doi:10.1016/j.mehy.2015.02.004 · Cited by 18

Autophagy in the mammalian nervous system: a primer for neuroscientists

Suomi, F., & McWilliams, T. G. (2019) · Neuronal Signaling · doi:10.1042/ns20180134 · Cited by 18

α-Synuclein ubiquitination – functions in proteostasis and development of Lewy bodies

Ho, H.-H., & Wing, S. S. (2024) · Frontiers in Molecular Neuroscience · doi:10.3389/fnmol.2024.1498459 · Cited by 19

Stochastics of degradation: the autophagic-lysosomal system of the cell

Kudriaeva, A. A., Av, S., & Belogurov, A. A. (2020) · Acta Naturae · doi:10.32607/actanaturae.10936 · Cited by 20

Current Understanding of Protein Aggregation in Neurodegenerative Diseases

Hu, C., Lin, M., Wang, C., & Zhang, S. (2025) · International Journal of Molecular Sciences · doi:10.3390/ijms262110568 · Cited by 21

The diverse role of optineurin in pathogenesis of disease

Guo, Q., Wang, J., & Weng, Q. (2020) · Biochemical Pharmacology · doi:10.1016/j.bcp.2020.114157 · Cited by 19

The Differential Profiling of Ubiquitin‐Proteasome and Autophagy Systems in Different Tissues before the Onset of H untington's Disease Models

Her, L., Lin, J., Fu, M., Chang, Y., Li, C., Tang, T., Jhang, Y.-L., Chang, C., Shih, M., Cheng, P., et al. (2014) · Brain Pathology · doi:10.1111/bpa.12191 · Cited by 16

The role of autophagy in the pathogenesis and treatment of amyotrophic lateral sclerosis (ALS) and frontotemporal dementia (FTD)

Beckers, J., & Damme, P. V. (2025) · Autophagy Reports · doi:10.1080/27694127.2025.2474796 · Cited by 19

Mechanistic insights into the interactions of TAX1BP1 with RB1CC1 and mammalian ATG8 family proteins

Zhang, M., Wang, Y., Gong, X., Wang, Y., Zhang, Y., Tang, Y., Zhou, X., Liu, H., Huang, Y., Zhang, J., et al. (2024) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.2315550121 · Cited by 17

Dysregulation of autophagy in gastric carcinoma: Pathways to tumor progression and resistance to therapy

Wen, W., Ertaş, Y. N., Erdem, A., & Zhang, Y. (2024) · Cancer Letters · doi:10.1016/j.canlet.2024.216857 · Cited by 18

Axonopathy Underlying Amyotrophic Lateral Sclerosis: Unraveling Complex Pathways and Therapeutic Insights

Luan, T., Li, Q., Huang, Z., Feng, Y., Xu, D., Zhou, Y., Hu, Y., & Wang, T. (2024) · Neuroscience Bulletin · doi:10.1007/s12264-024-01267-2 · Cited by 15

The GST-BHMT assay reveals a distinct mechanism underlying proteasome inhibition-induced macroautophagy in mammalian cells

Rui, Y., Xu, Z., Chen, Z., & Zhang, S. (2015) · Autophagy · doi:10.1080/15548627.2015.1034402 · Cited by 15

Optineurin Deficiency and Insufficiency Lead to Higher Microglial TDP-43 Protein Levels

Prtenjača, N., Rob, M., Alam, M. S., Markovinović, A., Stuani, C., Buratti, E., & Munitić, I. (2022) · International Journal of Molecular Sciences · doi:10.3390/ijms23126829 · Cited by 13

Manipulating autophagic degradation in human diseases: from mechanisms to interventions

Zhang, Y., Liu, X., Klionsky, D. J., Lu, B., & Zhong, Q. (2022) · Life Medicine · doi:10.1093/lifemedi/lnac043 · Cited by 14

OPTN gene therapy increases autophagy and protects mitochondria in SOD1 ‐G93A‐expressing transgenic mice and cells

Wen, D., Ji, Y., Li, Y., Duan, W., Wang, Y., Li, Z., Tao, M., & Liu, Y. (2023) · FEBS Journal · doi:10.1111/febs.17009 · Cited by 18

Novel prospects in targeting neurodegenerative disorders via autophagy

Khan, S., Upadhyay, S., & Hassan, M. I. (2024) · European Journal of Pharmacology · doi:10.1016/j.ejphar.2024.177060 · Cited by 15

Spink2 Modulates Apoptotic Susceptibility and Is a Candidate Gene in the Rgcs1 QTL That Affects Retinal Ganglion Cell Death after Optic Nerve Damage

Dietz, J. A., Maes, M. E., Huang, S., Yandell, B. S., Schlamp, C. L., Montgomery, A. D., Allingham, R. R., Hauser, M. A., & Nickells, R. W. (2014) · PLoS ONE · doi:10.1371/journal.pone.0093564 · Cited by 14

Identification of a splice variant of optineurin which is defective in autophagy and phosphorylation

Moharir, S. C., Bansal, M., Ramachandran, G., Ramaswamy, R., Rawat, S., Raychaudhuri, S., & Swarup, G. (2018) · Biochimica et Biophysica Acta (BBA) - Molecular Cell Research · doi:10.1016/j.bbamcr.2018.08.009 · Cited by 12

The Role of Non-Coding RNAs in Autophagy During Carcinogenesis

de la Cruz‐Ojeda, P., Flores-Campos, R., Navarro‐Villarán, E., & Muntané, J. (2022) · Frontiers in Cell and Developmental Biology · doi:10.3389/fcell.2022.799392 · Cited by 14

Mitochondria at the crossroads: Quality control mechanisms in neuronal senescence and neurodegeneration

Zheng, Y., Yang, J., Li, X., Qi, L., Zheng, Z., Kong, J., Zhang, G., & Guo, Y. (2025) · Neurobiology of Disease · doi:10.1016/j.nbd.2025.106862 · Cited by 14

Herpesvirus Regulation of Selective Autophagy

Vo, M. T., & Choi, Y. B. (2021) · Viruses · doi:10.3390/v13050820 · Cited by 13

BRCC36 associates with FLT3‐ITD to regulate its protein stability and intracellular signaling in acute myeloid leukemia

Liu, J., Isaji, T., Komatsu, S., Sun, Y., Xu, X., Fukuda, T., Fujimura, T., Takahashi, S., & Gu, J. (2024) · Cancer Science · doi:10.1111/cas.16090 · Cited by 12

Glaucoma-associated Optineurin mutations increase transcellular degradation of mitochondria in a vertebrate optic nerve

Jeong, Y., Davis, C.-H. O., Muscarella, A. M., Navarro, H. H., Deshpande, V. A., Moore, L. G., Keun-young Kim, A., Ellisman, M. H., & Marsh‐Armstrong, N. (2025) · eLife · doi:10.7554/elife.103844 · Cited by 12

Inborn errors of autophagy and infectious diseases

Sabli, I. K. D., & Sancho‐Shimizu, V. (2021) · Current Opinion in Immunology · doi:10.1016/j.coi.2021.07.005 · Cited by 12

The genetic basis of amyotrophic lateral sclerosis: recent breakthroughs

Robberecht, W., & Eykens, C. (2015) · Advances in Genomics and Genetics · doi:10.2147/agg.s57397 · Cited by 14

Molecular effect of an OPTN common variant associated to Paget's disease of bone

Silva, I. A. L., Conceição, N., Gagnon, É., Brown, J. P., Cancela, M. L., & Michou, L. (2018) · PLoS ONE · doi:10.1371/journal.pone.0197543 · Cited by 12

Disrupted endoplasmic reticulum-mediated autophagosomal biogenesis in a Drosophila model of C9-ALS-FTD

Sung, H., & Lloyd, T. E. (2023) · Autophagy · doi:10.1080/15548627.2023.2249750 · Cited by 11

Molecular genetics of inherited normal tension glaucoma

Pan, Y., & Iwata, T. (2024) · Indian Journal of Ophthalmology · doi:10.4103/ijo.ijo_3204_23 · Cited by 11

RCHY1 and OPTN are required for melanophagy, selective autophagy of melanosomes

Lee, K. W., Ryu, K., Kim, M., Lim, S., Kim, J., Kim, J. Y., Hwangbo, C., Yoo, J., Cho, Y., & Kim, K. D. (2024) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.2318039121 · Cited by 12

A CRISPR view on autophagy

Liang, J. R., & Corn, J. E. (2022) · Trends in Cell Biology · doi:10.1016/j.tcb.2022.04.006 · Cited by 12

Coordinative regulation of ERAD and selective autophagy in plants

Chen, Q., Wu, Y., Yu, F., & Xie, Q. (2022) · Essays in Biochemistry · doi:10.1042/ebc20210099 · Cited by 11

Ubiquitin proteasome system and glaucoma: A survey of genetics and molecular biology studies supporting a link with pathogenic and therapeutic relevance

Pandino, I., Giammaria, S., Zingale, G. A., Roberti, G., Michelessi, M., Coletta, M., Manni, G., Agnifili, L., Vercellin, A. C. V., Harris, A., et al. (2023) · Molecular Aspects of Medicine · doi:10.1016/j.mam.2023.101226 · Cited by 11

Regulated proteolysis as an element of ER stress and autophagy: Implications for intestinal inflammation

Stengel, S. T., Messner, B., Falk‐Paulsen, M., Sommer, N., & Rosenstiel, P. C. (2017) · Biochimica et Biophysica Acta (BBA) - Molecular Cell Research · doi:10.1016/j.bbamcr.2017.07.008 · Cited by 11

Autophagy Disruptions Associated With Altered Optineurin Expression in Extranigral Regions in a Rotenone Model of Parkinson's Disease

Wise, J. P., Price, C. G., Amaro, J. A., & Cannon, J. R. (2018) · Frontiers in Neuroscience · doi:10.3389/fnins.2018.00289 · Cited by 11

Rab GTPases are evolutionarily conserved signals mediating selective autophagy

Zhao, P., Tian, R., Song, D., Zhu, Q., Ding, X., Zhang, J., Cao, B., Zhang, M., Xu, Y., Fang, J., et al. (2025) · The Journal of Cell Biology · doi:10.1083/jcb.202410150 · Cited by 10

Autophagy-independent cytoprotection by optineurin from toxicity of aggregates formed by mutant huntingtin and mutant ataxin-3

Moharir, S. C., Raghawan, A. K., Ramaswamy, R., & Swarup, G. (2022) · The Journal of Biochemistry · doi:10.1093/jb/mvac011 · Cited by 10

NDP52 and its emerging role in pathogenesis

Bruqi, K., & Strappazzon, F. (2025) · Cell Death and Disease · doi:10.1038/s41419-025-07668-z · Cited by 10

Advances in the Differentiation of Retinal Ganglion Cells from Human Pluripotent Stem Cells

Ohlemacher, S. K., Langer, K. B., Fligor, C. M., Feder, E. M., Edler, M., & Meyer, J. S. (2019) · Advances in experimental medicine and biology · doi:10.1007/978-3-030-28471-8_5 · Cited by 11

Autophagy at the synapse, an early site of dysfunction in neurodegeneration

Jasutkar, H. G., & Yamamoto, A. (2023) · Current Opinion in Physiology · doi:10.1016/j.cophys.2023.100631 · Cited by 9

Supramolecular Complexes in Cell Death and Inflammation and Their Regulation by Autophagy

Gentle, I. E. (2019) · Frontiers in Cell and Developmental Biology · doi:10.3389/fcell.2019.00073 · Cited by 9

Autophagy and Motor Neuron Diseases

Zhang, X., Yang, K., & Le, W. (2020) · Advances in experimental medicine and biology · doi:10.1007/978-981-15-4272-5_3 · Cited by 9

Adaptation of Proteasomes and Lysosomes to Cellular Environments

Mebratu, Y. A., Negasi, Z. H., Dutta, S., Rojas, J., & Tesfaigzi, Y. (2020) · Cells · doi:10.3390/cells9102221 · Cited by 9

PEX14 acts as a molecular link between optineurin and the autophagic machinery to induce pexophagy

Li, H., Chen, S., Lismont, C., Vandewinkel, B., Hussein, M. A. F., Costa, C. F., Imberechts, D., Liu, Y., Azevedo, J. E., Vandenberghe, W., et al. (2025) · The Journal of Cell Biology · doi:10.1083/jcb.202411184 · Cited by 8

Macroautophagy of Aggregation-Prone Proteins in Neurodegenerative Disease

Fox, L. M., & Yamamoto, A. (2015) · Elsevier eBooks · doi:10.1016/b978-0-12-801043-3.00007-8 · Cited by 9

Epigenetics in the formation of pathological aggregates in amyotrophic lateral sclerosis

Noches, V., Campos‐Melo, D., Droppelmann, C. A., & Strong, M. J. (2024) · Frontiers in Molecular Neuroscience · doi:10.3389/fnmol.2024.1417961 · Cited by 8

Transcriptomic Changes Associated with Loss of Cell Viability Induced by Oxysterol Treatment of a Retinal Photoreceptor-Derived Cell Line: An In Vitro Model of Smith–Lemli–Opitz Syndrome

Pfeffer, B. A., Xu, L., & Fliesler, S. J. (2021) · International Journal of Molecular Sciences · doi:10.3390/ijms22052339 · Cited by 7

Autophagy as a protective mechanism in oxidative stress

Зенков, Н. К., Chehushkov, A., Kozhin, P. M., Мартинович, Г. Г., Кандалинцева, Н. В., & Брониславовна, М. Е. (2019) · Bulletin of Siberian Medicine · doi:10.20538/1682-0363-2019-2-195-214 · Cited by 8

Choosing Lunch: The Role of Selective Autophagy Adaptor Proteins

Leyva-Paredes, K., Castrejón-Jiménez, N. S., Arrieta-Oliva, H. I., Baltierra‐Uribe, S. L., & García‐Pérez, B. E. (2016) · InTech eBooks · doi:10.5772/63977 · Cited by 6

Targeting selective autophagy in CNS disorders by small-molecule compounds

Zheng, Y., Zhou, Z., Liu, M., & Chen, Z. (2024) · Pharmacology & Therapeutics · doi:10.1016/j.pharmthera.2024.108729 · Cited by 6

Genome-wide siRNA screening reveals that DCAF4-mediated ubiquitination of optineurin stimulates autophagic degradation of Cu,Zn-superoxide dismutase

Homma, K., Takahashi, H., Tsuburaya, N., Naguro, I., Fujisawa, T., & Ichijo, H. (2020) · Journal of Biological Chemistry · doi:10.1074/jbc.ra119.010239 · Cited by 6

Autophagy-Lysosome Dysfunction in Amyotrophic Lateral Sclerosis and Frontotemporal Lobar Degeneration

Sullivan, P. M., Zhou, X., & Hu, F. (2017) · InTech eBooks · doi:10.5772/intechopen.69371 · Cited by 6

Molecular aspects of cytoprotection by Optineurin during stress and disease

Swarup, G., Medchalmi, S., Ramachandran, G., & Sayyad, Z. (2025) · Biochimica et Biophysica Acta (BBA) - Molecular Cell Research · doi:10.1016/j.bbamcr.2024.119895 · Cited by 6

Co‐chaperone BAG3 enters autophagic pathway via its interaction with microtubule associated protein 1 light chain 3 beta

Körschgen, H., Baeken, M. W., Schmitt, D., Nagel, H., & Behl, C. (2023) · Traffic · doi:10.1111/tra.12916 · Cited by 5

Roflupram alleviates autophagy defects and reduces mutant hSOD1-induced motor neuron damage in cell and mouse models of amyotrophic lateral sclerosis

Huo, D., Liang, W., Wang, D., Liu, Q., Wang, H., Wang, Y., Zhang, C., Cong, C., Su, X., Tan, X., et al. (2024) · Neuropharmacology · doi:10.1016/j.neuropharm.2023.109812 · Cited by 5

OPTN deficiency through CRISPR/Cas9 downregulates autophagy and mitophagy in a SOD1-G93A-expressing transgenic cell line

Wen, D., Li, Q., Li, Y., Yan, W., Wang, Y., & Liu, Y. (2025) · IBRO Neuroscience Reports · doi:10.1016/j.ibneur.2025.07.011 · Cited by 5

Optineurin Dysfunction in Amyotrophic Lateral Sclerosis: Why So Puzzling?

Prtenjača, N. (2020) · Periodicum Biologorum · doi:10.18054/pb.v121-122i1-2.10627 · Cited by 5

Targeting macroautophagy to combat neurodegenerative disease: strategies and considerations

Duncan, G. M., & Yamamoto, A. (2025) · Autophagy Reports · doi:10.1080/27694127.2025.2571940 · Cited by 6

Genetic and clinical analysis of OPTN in amyotrophic lateral sclerosis

Xiao, Y., Tan, Y., Li, C., Wei, Q., Jiang, Q., Wang, S., Yang, T., Lin, J., Zhang, L., & Shang, H. (2025) · Journal of Medical Genetics · doi:10.1136/jmg-2024-109978 · Cited by 4

Optineurin overexpression ameliorates neurodegeneration through regulating neuroinflammation and mitochondrial quality in a murine model of amyotrophic lateral sclerosis

Zhao, S., Chen, R., An, Y., Zhang, Y., Ma, C., Gao, Y., Lu, Y., Yang, F., Bai, X., & Zhang, J. (2025) · Frontiers in Aging Neuroscience · doi:10.3389/fnagi.2025.1522073 · Cited by 4

Early-onset glaucoma

van der Heide, C. J., Miller, M. A., & Fingert, J. H. (2019) · Elsevier eBooks · doi:10.1016/b978-0-12-816222-4.00007-1 · Cited by 4

TBK1 Induces the Formation of Optineurin Filaments That Condensate with Polyubiquitin and LC3 for Cargo Sequestration

Herrera, M. G., Kühn, L., Jungbluth, L., Bader, V., Krause, L. J., Kartte, D., Adriaenssens, E., Martens, S., Tatzelt, J., Sachse, C., et al. (2025) · Advanced Science · doi:10.1002/advs.202509927 · Cited by 3

Post-translational modifications of selective autophagy receptors: orchestrating cellular homeostasis, disease pathogenesis, and therapeutic opportunities

Zhu, W., Wang, X., Li, Q., Jiang, X., & Xu, G. (2026) · Cellular & Molecular Biology Letters · doi:10.1186/s11658-026-00884-1 · Cited by 3

Phosphorylation of Optineurin by protein kinase D regulates Parkin-dependent mitophagy

Weil, R., Laplantine, E., Attailia, M., Oudin, A., Curic, S., Yokota, A., Banide, E., & Génin, P. (2024) · iScience · doi:10.1016/j.isci.2024.111384 · Cited by 3

Exploring the Function of OPTN From Multiple Dimensions

Guo, Y., Tian, Y., Xia, P., Zhou, X., Hu, X., Guo, Z., Ji, P., Yuan, X., Fu, D., Yin, K., et al. (2024) · Cell Biochemistry and Function · doi:10.1002/cbf.70029 · Cited by 3

OPTN protects retinal ganglion cells and ameliorates neuroinflammation in optic neuropathies

Wang, Q., Wang, Y., Jiang, Y., Donahue, R., Cao, G., Yan, W., Guo, H., Li, Z., Liang, J., Hao, J., et al. (2025) · Communications Biology · doi:10.1038/s42003-025-08534-6 · Cited by 3

Stimulation of Tau Degradation

Quintanilla, R. A., Cabezas-Opazo, F., Pallo, S. P., Chesser, A. S., & Johnson, G. V. W. (2016) · Elsevier eBooks · doi:10.1016/b978-0-12-802173-6.00013-7 · Cited by 3

Autophagy in Drosophila and Zebrafish

Duan, X., & Tong, C. (2021) · Advances in experimental medicine and biology · doi:10.1007/978-981-16-2830-6_15 · Cited by 3

Optineurin mediates delivery of membrane from transferrin receptor-positive endosomes to autophagosomesPreprint

Bansal, M., Sirohi, K., Moharir, S. C., & Swarup, G. (2022) · bioRxiv (Cold Spring Harbor Laboratory) · doi:10.1101/2022.01.12.476135 · Cited by 3

Enhanced autophagy drives endothelial tight junction loss, BBB disruption, and behavioral deficits during inflammation

Peng, M., Chen, W., Gao, Q., Zhu, X., Yu, L., Zhang, L., Zou, X., Hu, Z., & Zhang, L. (2026) · Autophagy · doi:10.1080/15548627.2026.2662440 · Cited by 3

Zebrafish optineurin: genomic organization and transcription regulation

Silva, I. A. L., Varela, D., Cancela, M. L., & Conceição, N. (2022) · Genome · doi:10.1139/gen-2022-0019 · Cited by 2

Selectivity and trafficking of autophagic cargoes

Ahsan, N., Jena, K. K., Mehto, S., & Chauhan, S. (2021) · Elsevier eBooks · doi:10.1016/b978-0-12-822003-0.00023-1 · Cited by 2

Autophagy and Huntington's disease

Croce, K. R., Jasutkar, H. G., & Yamamoto, A. (2024) · Elsevier eBooks · doi:10.1016/b978-0-323-95672-7.00018-2 · Cited by 2

The Role of Autophagy Receptors in Mitophagy

Marinković, M., & Novak, I. (2015) · Elsevier eBooks · doi:10.1016/b978-0-12-801032-7.00017-4 · Cited by 2

Multifaceted Genes in Amyotrophic Lateral Sclerosis-Frontotemporal Dementia

(2021) · Frontiers research topics · doi:10.3389/978-2-88966-904-2 · Cited by 3

TBK1 regulates autophagic clearance of soluble mutant huntingtin and inhibits aggregation/toxicity in different models of Huntington’s diseasePreprint

Hegde, R. N., Chiki, A., Petricca, L., Martufi, P., Arbez, N., Mouchiroud, L., Auwerx, J., Landles, C., Bates, G., Singh-Bains, M. K., et al. (2019) · bioRxiv · doi:10.1101/869586 · Cited by 2

Selective Disposal of Insoluble Protein Aggregates

Seneci, P. (2015) · Elsevier eBooks · doi:10.1016/b978-0-12-800186-8.00005-5 · Cited by 1

A Structured Brain-wide and Genome-wide Association Study Using ADNI PET Images

Li, Y., Nan, B., & Zhu, J. (2021) · Canadian Journal of Statistics-revue Canadienne De Statistique · doi:10.1002/cjs.11605 · Cited by 2

Autophagy and Huntington’s disease

Mano, T., & Iwata, A. (2022) · Elsevier eBooks · doi:10.1016/b978-0-323-89906-2.00001-0 · Cited by 1

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Al-Mufti, Y., Cranwell, S., & Samant, R. S. (2022) · Elsevier eBooks · doi:10.1016/b978-0-323-91617-2.00004-3 · Cited by 1

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Shilovsky, G. A. (2024) · Molecular Biology · doi:10.1134/s0026893324700390 · Cited by 2

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Zhuang, H., & Ma, X. (2025) · Journal of Cellular Physiology · doi:10.1002/jcp.31512 · Cited by 3

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Durán‐Cristiano, S. C., de Diego-García, L., Martín‐Gil, A., & Carracedo, G. (2025) · Life · doi:10.3390/life15030504 · Cited by 2

Evaluation of aggrephagy markers in myofibrillar myopathies

Iannibelli, E., Ruggieri, A., Maruotti, A., Salerno, F., Cheli, M., Carnazzi, A., Gaetano, L. N. D., Riolo, G., Bortolani, S., Riguzzi, P., et al. (2025) · Acta Neuropathologica Communications · doi:10.1186/s40478-025-02041-9 · Cited by 1

Optineurin regulates motor and learning behaviors by affecting dopaminergic neuron survival in mice

Yang, X., Zheng, R., Zhang, H., Ou, Z., Wan, S., Lin, D., Yan, J., Jin, M., & Tan, J. (2024) · Experimental Neurology · doi:10.1016/j.expneurol.2024.115007 · Cited by 1

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Ali, D. M., & Berger, M. R. (2019) · IntechOpen eBooks · doi:10.5772/intechopen.80981 · Cited by 1

Phosphorylation of the mitochondrial autophagy receptor Nix enhances its interaction with LC3 proteins

Rogov, V., SUZUKI, H., Marinkovi, M., Lang, V., Ryuichi, K. A. T. O., Kawasaki, M., Buljubai, M., prung, M., Rogova, N., Soichi Wakatsuki, A., et al. (2017) · Institutional Repositories DataBase (IRDB) · Cited by 1

Optineurin promotes aggregation of mutant huntingtin and mutant ataxin-3, and reduces cytotoxicity of aggregatesPreprint

Moharir, S. C., Raghawan, A. K., & Swarup, G. (2020) · bioRxiv (Cold Spring Harbor Laboratory) · doi:10.1101/2020.08.13.249201 · Cited by 1

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Qiu, Y., Wang, J., Wang, J., Yang, B., He, Q., & Weng, Q. (2020) · doi:10.22541/au.158920866.62871852

Crystal Structure and Characterization of the SCOC Coiled Coil Domain

Behrens, C. (2014) · eDiss (Georg-August-Universität Göttingen) · doi:10.53846/goediss-4638 · Cited by 1

Experience-dependent phosphoproteomic changes in hippocampus and neocortex correlate with the abundance of spindle oscillations during the transition between SWS and REM sleepPreprint

Souza, A. C., Golbert, D. C. F., Cassoli, J. S., Sánchez-Gendriz, I., Lima, V. V. F., da Silva, F. A. C., Martins‐de‐Souza, D., & Ribeiro, S. T. G. (2022) · Research Square · doi:10.21203/rs.3.rs-1842393/v2 · Cited by 1

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Ljutić, T. (2016)

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Ying, H., & Yue, B. Y. J. T. (2015) · Experimental Eye Research · doi:10.1016/j.exer.2015.06.029 · Cited by 106

Optineurin knock-out forms TDP-43 aggregates to regulate TDP-43 protein levels despite autophagic up-regulation and aberrant TDP-43 expression

Maetani, Y., Kurashige, T., Tada, Y., Kume, K., Watanabe, T., Sotomaru, Y., Yamanaka, K., Maruyama, H., & Kawakami, H. (2025) · Neuroscience Research · doi:10.1016/j.neures.2025.03.005 · Cited by 4

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Zhang, L., Han, J., Yang, Z., Xue, M., & Zheng, C. (2026) · Academia Immunity and Disease · doi:10.20935/acadimmunodis8165