TBK1 controls autophagosomal engulfment of polyubiquitinated mitochondria through p62/SQSTM1 phosphorylation

Autophagy: Renovation of Cells and Tissues

Mizushima, N., & Komatsu, M. (2011) · Cell · doi:10.1016/j.cell.2011.10.026 · Cited by 6,615

Mitochondrial Dysfunction and Oxidative Stress in Neurodegenerative Diseases

Lin, M. T., & Beal, M. F. (2006) · Nature · doi:10.1038/nature05292 · Cited by 6,455

Parkin is recruited selectively to impaired mitochondria and promotes their autophagy

Narendra, D., Tanaka, A., Suen, D.-F., & Youle, R. J. (2008) · The Journal of Cell Biology · doi:10.1083/jcb.200809125 · Cited by 4,026

p62/SQSTM1 forms protein aggregates degraded by autophagy and has a protective effect on huntingtin-induced cell death

Bjørkøy, G., Lamark, T., Brech, A., Outzen, H., Perander, M., Øvervatn, A., Stenmark, H., & Johansen, T. (2005) · The Journal of Cell Biology · doi:10.1083/jcb.200507002 · Cited by 3,276

Mechanisms of mitophagy

Youle, R. J., & Narendra, D. P. (2011) · Nature Reviews Molecular Cell Biology · doi:10.1038/nrm3028 · Cited by 3,273

PINK1/Parkin-mediated mitophagy is dependent on VDAC1 and p62/SQSTM1

Geisler, S., Holmström, K. M., Skujat, D., Fiesel, F. C., Rothfuss, O. C., Kahle, P. J., & Springer, W. (2010) · Nature Cell Biology · doi:10.1038/ncb2012 · Cited by 2,835

PINK1 stabilized by mitochondrial depolarization recruits Parkin to damaged mitochondria and activates latent Parkin for mitophagy

Matsuda, N., Sato, S., Shiba, K., Okatsu, K., Saisho, K., Gautier, C. A., Sou, Y.-S., Saiki, S., Kawajiri, S., Sato, F., et al. (2010) · Journal of Cell Biology · doi:10.1083/jcb.200910140 · Cited by 1,969

Selective autophagy mediated by autophagic adapter proteins

Johansen, T., & Lamark, T. (2011) · Autophagy · doi:10.4161/auto.7.3.14487 · Cited by 1,788

Proteasome and p97 mediate mitophagy and degradation of mitofusins induced by Parkin

Tanaka, A., Cleland, M. M., Xu, S., Narendra, D. P., Suen, D.-F., Karbowski, M., & Youle, R. J. (2010) · Journal of Cell Biology · doi:10.1083/jcb.201007013 · Cited by 1,369

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

Activation of TGF-β-activated kinase 1 (TAK1) restricts Salmonella Typhimurium growth by inducing AMPK activation and autophagy

Liu, W., Jiang, Y., Sun, J. F., Geng, S., Pan, Z., Prinz, R. A., Wang, C., Sun, J., Jiao, X., & Xu, X. (2018) · Cell Death and Disease · doi:10.1038/s41419-018-0612-z · Cited by 57

The multifaceted role of kinases in amyotrophic lateral sclerosis: genetic, pathological and therapeutic implications

Guo, W., Vandoorne, T., Steyaert, J., Staats, K. A., & Bosch, L. V. D. (2020) · Brain · doi:10.1093/brain/awaa022 · Cited by 58

Essential Roles for the Non-Canonical IκB Kinases in Linking Inflammation to Cancer, Obesity, and Diabetes

Shin, C. H., & Choi, D. (2019) · Cells · doi:10.3390/cells8020178 · Cited by 56

PTK2/FAK regulates UPS impairment via SQSTM1/p62 phosphorylation in TARDBP/TDP-43 proteinopathies

Lee, S., Jeon, Y., Cha, S. J., Kim, S., Kwon, Y., Jo, M., Jang, Y.-N., Lee, S., Kim, J., Kim, S. R., et al. (2019) · Autophagy · doi:10.1080/15548627.2019.1686729 · Cited by 59

Restriction of intracellular Salmonella replication by restoring TFEB-mediated xenophagy

Ammanathan, V., Mishra, P., Chavalmane, A. K., Muthusamy, S., Jadhav, V., Chandrashekaran, S., & Manjithaya, R. R. (2019) · Autophagy · doi:10.1080/15548627.2019.1689770 · Cited by 54

Primary open angle glaucoma genetics: The common variants and their clinical associations (Review)

Trivli, A., Zervou, M. I., Goulielmos, G. N., Spandidos, D. A., & Detorakis, Ε. T. (2020) · Molecular Medicine Reports · doi:10.3892/mmr.2020.11215 · Cited by 55

Neuronal autophagy and axon degeneration

Wang, Y., Song, M., & Song, F. (2018) · Cellular and Molecular Life Sciences · doi:10.1007/s00018-018-2812-1 · Cited by 55

The interplay between autophagy and cGAS-STING signaling and its implications for cancer

Schmid, M., Fischer, P., Engl, M., Widder, J., Gruber, S., & Slade, D. (2024) · Frontiers in Immunology · doi:10.3389/fimmu.2024.1356369 · Cited by 61

p62/SQSTM1 in liver diseases: the usual suspect with multifarious identities

Tan, C. T., Soh, N. J. H., Chang, H., & Yu, V. C. K. (2021) · FEBS Journal · doi:10.1111/febs.16317 · Cited by 52

The Multifunctional Protein p62 and Its Mechanistic Roles in Cancers

Ning, S., & Wang, L. (2018) · Current Cancer Drug Targets · doi:10.2174/1568009618666181016164920 · Cited by 55

Mitochondrial quality control in amyotrophic lateral sclerosis: towards a common pathway?

Khalil, B., & Liévens, J.-C. (2017) · Neural Regeneration Research · doi:10.4103/1673-5374.211179 · Cited by 51

Lowering Mutant Huntingtin Levels and Toxicity: Autophagy-Endolysosome Pathways in Huntington's Disease

Valionyte, E., Yang, Y., Roberts, S. L., Kelly, J., Lu, B., & Luo, S. (2019) · Journal of Molecular Biology · doi:10.1016/j.jmb.2019.11.012 · Cited by 51

Multiple pathways for mitophagy: A neurodegenerative conundrum for Parkinson’s disease

Chu, C. T. (2018) · Neuroscience Letters · doi:10.1016/j.neulet.2018.04.004 · Cited by 50

Deletion of Tbk1 disrupts autophagy and reproduces behavioral and locomotor symptoms of FTD-ALS in mice

Duan, W., Guo, M., Yi, L., Zhang, J., Bi, Y., Liu, Y., Li, Y., Li, Z., Ma, Y., Zhang, G., et al. (2019) · Aging · doi:10.18632/aging.101936 · Cited by 51

Effects of ALS-associated TANK binding kinase 1 mutations on protein–protein interactions and kinase activity

Ye, J., Cheung, J., Gerbino, V., Ahlsén, G., Zimanyi, C. M., Hirsh, D., & Maniatis, T. (2019) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.1915732116 · Cited by 49

TBK1 phosphorylates mutant Huntingtin and suppresses its aggregation and toxicity in Huntington's disease models

Hegde, R. N., Chiki, A., Petricca, L., Martufi, P., Arbez, N., Mouchiroud, L., Auwerx, J. H., Landles, C., Bates, G. P., Singh‐Bains, M. K., et al. (2020) · The EMBO Journal · doi:10.15252/embj.2020104671 · Cited by 50

Parkin overexpression alleviates cardiac aging through facilitating K63-polyubiquitination of TBK1 to facilitate mitophagy

Gao, B., Yu, W., Lv, P., Liang, X., Sun, S., & Zhang, Y. (2020) · Biochimica et Biophysica Acta (BBA) - Molecular Basis of Disease · doi:10.1016/j.bbadis.2020.165997 · Cited by 48

Dysfunctional Autophagy and Endolysosomal System in Neurodegenerative Diseases: Relevance and Therapeutic Options

Giovedı̀, S., Ravanelli, M. M., Parisi, B., Bettegazzi, B., & Guarnieri, F. C. (2020) · Frontiers in Cellular Neuroscience · doi:10.3389/fncel.2020.602116 · Cited by 53

Emerging and converging molecular mechanisms in dystonia

González-Latapí, P., Marotta, N., & Mencacci, N. E. (2021) · Journal of Neural Transmission · doi:10.1007/s00702-020-02290-z · Cited by 48

The crosstalk of NAD, ROS and autophagy in cellular health and ageing

Sedlackova, L., & Korolchuk, V. I. (2020) · Biogerontology · doi:10.1007/s10522-020-09864-0 · Cited by 48

Targeting TANK-binding kinase 1 (TBK1) in cancer

Revach, O., Liu, S., & Jenkins, R. W. (2020) · Expert Opinion on Therapeutic Targets · doi:10.1080/14728222.2020.1826929 · Cited by 49

FIP200 controls the TBK1 activation threshold at SQSTM1/p62-positive condensates

Schlütermann, D., Berleth, N., Deitersen, J., Hieke, N., Friesen, O., Wu, W., Stuhldreier, F., Sun, Y., Berning, L., Friedrich, A., et al. (2021) · Scientific Reports · doi:10.1038/s41598-021-92408-4 · Cited by 47

The pleiotropic functions of autophagy in metastasis

Marsh, T., Tolani, B., & Debnath, J. (2021) · Journal of Cell Science · doi:10.1242/jcs.247056 · Cited by 49

Central role for p62/SQSTM1 in the elimination of toxic tau species in a mouse model of tauopathy

Ono, M., Komatsu, M., Ji, B., Takado, Y., Shimojo, M., Minamihisamatsu, T., Warabi, E., Yanagawa, T., Matsumoto, G., Aoki, I., et al. (2022) · Aging Cell · doi:10.1111/acel.13615 · Cited by 45

Vaspin prevents myocardial injury in rats model of diabetic cardiomyopathy by enhancing autophagy and inhibiting inflammation

Li, X., Ke, X., Li, Z., & Li, B. (2019) · Biochemical and Biophysical Research Communications · doi:10.1016/j.bbrc.2019.04.110 · Cited by 45

Systemic overexpression of SQSTM1/p62 accelerates disease onset in a SOD1H46R-expressing ALS mouse model

Mitsui, S., Otomo, A., Nozaki, M., Ono, S., Sato, K., Shirakawa, R., Adachi, H., Aoki, M., Sobue, G., Shang, H., et al. (2018) · Molecular Brain · doi:10.1186/s13041-018-0373-8 · Cited by 48

TBK1 from orange-spotted grouper exerts antiviral activity against fish viruses and regulates interferon response

Hu, Y., Huang, Y., Liu, J., Zhang, J., Qin, Q., & Huang, X. (2017) · Fish & Shellfish Immunology · doi:10.1016/j.fsi.2017.12.010 · Cited by 43

TANK-binding kinase 1 (TBK1): An emerging therapeutic target for drug discovery

Xiang, S., Song, S., Tang, H., Smaill, J. B., Wang, A., Xie, H., & Lu, X. (2021) · Drug Discovery Today · doi:10.1016/j.drudis.2021.05.016 · Cited by 41

A critical role of Hrd1 in the regulation of optineurin degradation and aggresome formation

Mao, J., Qin, X., Liu, C., Ying, Z., Wang, H., & Wang, G. (2017) · Human Molecular Genetics · doi:10.1093/hmg/ddx096 · Cited by 41

A review on the role of TANK-binding kinase 1 signaling in cancer

Alam, M., Hasan, G. M., & Hassan, M. I. (2021) · International Journal of Biological Macromolecules · doi:10.1016/j.ijbiomac.2021.06.022 · Cited by 43

Sexual Dimorphism and Aging in the Human Hyppocampus: Identification, Validation, and Impact of Differentially Expressed Genes by Factorial Microarray and Network Analysis

Guebel, D. V., & Torres, N. V. (2016) · Frontiers in Aging Neuroscience · doi:10.3389/fnagi.2016.00229 · Cited by 41

PINK1-Parkin signaling in Parkinson’s disease: Lessons from Drosophila

Imai, Y. (2020) · Neuroscience Research · doi:10.1016/j.neures.2020.01.016 · Cited by 42

Mitophagy in Huntington's disease

Šonský, I., Vodička, P., Kepková, K. V., & Hansíková, H. (2021) · Neurochemistry International · doi:10.1016/j.neuint.2021.105147 · Cited by 42

Influenza A virus use of BinCARD1 to facilitate the binding of viral NP to importin α7 is counteracted by TBK1-p62 axis-mediated autophagy

Wang, X., Jiang, L., Wang, G., Shi, W., Hu, Y., Wang, B., Zeng, X., Tian, G., Deng, G., Shi, J., et al. (2022) · Cellular and Molecular Immunology · doi:10.1038/s41423-022-00906-w · Cited by 40

Amyotrophic lateral sclerosis: recent genetic highlights

White, M. A., & Sreedharan, J. (2016) · Current Opinion in Neurology · doi:10.1097/wco.0000000000000367 · Cited by 40

The role of sequestosome 1/p62 protein in amyotrophic lateral sclerosis and frontotemporal dementia pathogenesis

Foster, A. D., & Rea, S. L. (2020) · Neural Regeneration Research · doi:10.4103/1673-5374.284977 · Cited by 41

MYC- and MIZ1-Dependent Vesicular Transport of Double-Strand RNA Controls Immune Evasion in Pancreatic Ductal Adenocarcinoma

Krenz, B., Gebhardt-Wolf, A., Ade, C. P., Gaballa, A., Roehrig, F., Vendelova, E., Baluapuri, A., Eilers, U., Gallant, P., D’Artista, L., et al. (2021) · Cancer Research · doi:10.1158/0008-5472.can-21-1677 · Cited by 41

The transcription factor NRF1 (NFE2L1) activates aggrephagy by inducing p62 and GABARAPL1 after proteasome inhibition to maintain proteostasis

Hatanaka, A., Nakada, S., Matsumoto, G., Satoh, K., Aketa, I., Watanabe, A., Hirakawa, T., Tsujita, T., Waku, T., & Kobayashi, A. (2023) · Scientific Reports · doi:10.1038/s41598-023-41492-9 · Cited by 36

The Physiological functions of IKK-selective substrate identification and their critical roles in diseases

Yu, J.-S., Jin, J., & Li, Y. (2020) · STEMedicine · doi:10.37175/stemedicine.v1i4.49 · Cited by 37

A Cell-Based High-Throughput Screening Identified Two Compounds that Enhance PINK1-Parkin Signaling

Shiba-Fukushima, K., Inoshita, T., Sano, O., Iwata, H., Ishikawa, K.-I., Okano, H., Akamatsu, W., Imai, Y., & Hattori, N. (2020) · iScience · doi:10.1016/j.isci.2020.101048 · Cited by 37

USP13 deubiquitinates p62/SQSTM1 to induce autophagy and Nrf2 release for activating antioxidant response genes

Lee, B., Kim, Y. H., Lee, W., Choi, H. Y., Lee, J., Kim, J., Mai, D. N., Jung, S. F., Kwak, M. S., & Shin, J. (2023) · Free Radical Biology and Medicine · doi:10.1016/j.freeradbiomed.2023.09.024 · Cited by 34

NDP52 interacts with mitochondrial RNA poly(A) polymerase to promote mitophagy

Furuya, N., Kakuta, S., Sumiyoshi, K., Ando, M., Nonaka, R., Suzuki, A., Kazuno, S., Saiki, S., & Hattori, N. (2018) · EMBO Reports · doi:10.15252/embr.201846363 · Cited by 36

Enhancing mitophagy as a therapeutic approach for neurodegenerative diseases

Aman, Y., Ryan, B. J., Torsetnes, S. B., Knapskog, A., Watne, L. O., McEwan, W. A., & Fang, E. F. (2020) · International review of neurobiology · doi:10.1016/bs.irn.2020.02.008 · Cited by 36

TBK1 interacts with tau and enhances neurodegeneration in tauopathy

Abreha, M. H., Ojelade, S. A., Dammer, E. B., McEachin, Z. T., Duong, D. M., Gearing, M., Bassell, G. J., Lah, J. J., Levey, A. I., Shulman, J. M., et al. (2021) · Journal of Biological Chemistry · doi:10.1016/j.jbc.2021.100760 · Cited by 33

Roles of IκB kinases and TANK-binding kinase 1 in hepatic lipid metabolism and nonalcoholic fatty liver disease

Huh, J. Y., & Saltiel, A. R. (2021) · Experimental & Molecular Medicine · doi:10.1038/s12276-021-00712-w · Cited by 39

Mitochondrial Modulations, Autophagy Pathways Shifts in Viral Infections: Consequences of COVID-19

Singh, S. P., Amar, S., Gehlot, P., Patra, S. K., Kanwar, N., & Kanwal, A. (2021) · International Journal of Molecular Sciences · doi:10.3390/ijms22158180 · Cited by 35

Toll‐like receptor signalling cross‐activates the autophagic pathway to restrictSalmonellaTyphimurium growth in macrophages

Liu, W., Zhuang, J., Jiang, Y., Sun, J. F., Prinz, R. A., Sun, J., Jiao, X., & Xu, X. (2019) · Cellular Microbiology · doi:10.1111/cmi.13095 · Cited by 34

Autophagic sequestration of SQSTM1 disrupts the aggresome formation of ubiquitinated proteins during proteasome inhibition

Zhang, C., Huang, C. L., Xia, H., Xu, H., Tang, Q., & Bi, F. (2022) · Cell Death and Disease · doi:10.1038/s41419-022-05061-8 · Cited by 33

A regulatory circuit comprising the CBP and SIRT7 regulates FAM134B-mediated ER-phagy

Wang, X., Jiang, X. M., Li, B., Zheng, J., Guo, J., Gao, L., Du, M., Weng, X., Li, L., Chen, S., et al. (2023) · The Journal of Cell Biology · doi:10.1083/jcb.202201068 · Cited by 29

Autophagy and lysosomal pathways in nervous system disorders

Bingol, B. (2018) · Molecular and Cellular Neuroscience · doi:10.1016/j.mcn.2018.04.009 · Cited by 32

Autophagy and neurodegeneration: Unraveling the role of C9ORF72 in the regulation of autophagy and its relationship to ALS-FTD pathology

Diab, R., Pilotto, F., & Saxena, S. (2023) · Frontiers in Cellular Neuroscience · doi:10.3389/fncel.2023.1086895 · Cited by 35

Response to Bruton’s tyrosine kinase inhibitors in aggressive lymphomas linked to chronic selective autophagy

Phelan, J. D., Scheich, S., Choi, J., Wright, G. W., Häupl, B., Young, R. M., Rieke, S. A., Pape, M., Ji, Y., Urlaub, H., et al. (2024) · Cancer Cell · doi:10.1016/j.ccell.2023.12.019 · Cited by 31

MicroRNA-199a Inhibits Cellular Autophagy and Downregulates IFN-β Expression by Targeting TBK1 in Mycobacterium bovis Infected Cells

Wang, J., Hussain, T. A., Yue, R., Liao, Y., Li, Q., Yao, J., Song, Y., Sun, X., Wang, N., Xu, L., et al. (2018) · Frontiers in Cellular and Infection Microbiology · doi:10.3389/fcimb.2018.00238 · Cited by 30

Emerging Trends in the Field of Inflammation and Proteinopathy in ALS/FTD Spectrum Disorder

Marchi, F. D., Franjkic, T., Schito, P., Russo, T., Nimac, J., Chami, A. A., Mele, A., Vidatic, L., Križ, J., Julien, J., et al. (2023) · Biomedicines · doi:10.3390/biomedicines11061599 · Cited by 30

Familial normal tension glaucoma genetics

Fox, A. R., & Fingert, J. H. (2023) · Progress in Retinal and Eye Research · doi:10.1016/j.preteyeres.2023.101191 · Cited by 32

ALS-associated TBK1 variant p.G175S is defective in phosphorylation of p62 and impacts TBK1-mediated signalling and TDP-43 autophagic degradation

Foster, A., Downing, P., Figredo, E., Polain, N., Stott, A., Layfield, R., & Rea, S. L. (2020) · Molecular and Cellular Neuroscience · doi:10.1016/j.mcn.2020.103539 · Cited by 29

The converging roles of sequestosome-1/p62 in the molecular pathways of amyotrophic lateral sclerosis (ALS) and frontotemporal dementia (FTD)

Davidson, J. M., Chung, R. S., & Lee, A. (2022) · Neurobiology of Disease · doi:10.1016/j.nbd.2022.105653 · Cited by 29

Cell death cascade and molecular therapy in ADAR2-deficient motor neurons of ALS

Yamashita, T., & Kwak, S. (2018) · Neuroscience Research · doi:10.1016/j.neures.2018.06.004 · Cited by 28

Linear ubiquitination at damaged lysosomes induces local NFKB activation and controls cell survival

Zein, L., Dietrich, M., Balta, D., Bader, V., Scheuer, C., Zellner, S., Weinelt, N., Vandrey, J., Mari, M. C., Behrends, C., et al. (2025) · Autophagy · doi:10.1080/15548627.2024.2443945 · Cited by 31

Autophagy and Redox Homeostasis in Parkinson’s: A Crucial Balancing Act

Jiménez-Moreno, N., & Lane, J. D. (2020) · Oxidative Medicine and Cellular Longevity · doi:10.1155/2020/8865611 · Cited by 26

Proteomics-Based Approach Identifies Altered ER Domain Properties by ALS-Linked VAPB Mutation

Yamanaka, T., Nishiyama, R., Shimogori, T., & Nukina, N. (2020) · Scientific Reports · doi:10.1038/s41598-020-64517-z · Cited by 26

TDP-43 proteinopathy in frontotemporal lobar degeneration and amyotrophic lateral sclerosis: From pathomechanisms to therapeutic strategies

Ho, P., Hsieh, T., & Tsai, K. (2024) · Ageing Research Reviews · doi:10.1016/j.arr.2024.102441 · Cited by 28

TRIM21-mediated ubiquitination of SQSTM1/p62 abolishes its Ser403 phosphorylation and enhances palmitic acid cytotoxicity

Yang, P., Gao, S., Shen, J., Liu, T., Lu, K., Han, X., Wang, J., Ni, H., Ding, W., Hong Li, A., et al. (2024) · Autophagy · doi:10.1080/15548627.2024.2394308 · Cited by 25

N-Acyldopamine induces aggresome formation without proteasome inhibition and enhances protein aggregation via p62/SQSTM1 expression

Matsumoto, G., Inobe, T., Amano, T., Murai, K., Nukina, N., & Mori, N. (2018) · Scientific Reports · doi:10.1038/s41598-018-27872-6 · Cited by 24

Autophagy and antiviral defense

Ke, P. (2021) · IUBMB Life · doi:10.1002/iub.2582 · Cited by 23

Molecular Signaling to Preserve Mitochondrial Integrity against Ischemic Stress in the Heart: Rescue or Remove Mitochondria in Danger

Yu, J. D., & Miyamoto, S. (2021) · Cells · doi:10.3390/cells10123330 · Cited by 25

Autophagy deficiency abolishes liver mitochondrial DNA segregation

Tostes, K., dos Santos, A. C., Alves, L. D. O., Bechara, L. R. G., Marascalchi, R., Macabelli, C. H., Grejo, M. P., Festuccia, W. T., Gottlieb, R. A., Ferreira, J. C. B., et al. (2022) · Autophagy · doi:10.1080/15548627.2022.2038501 · Cited by 25

The role of cardiolipin in mitochondrial dynamics and quality control in neuronal ischemia/reperfusion injury

Emaus, K. J., Fogo, G. M., Wider, J. M., & Sanderson, T. H. (2025) · Cell Death and Disease · doi:10.1038/s41419-025-07786-8 · Cited by 28

microRNA-based autophagy inhibition as targeted therapy in pancreatic cancer

Liang, S., Li, X., Gao, C., & Zhang, L. (2020) · Biomedicine & Pharmacotherapy · doi:10.1016/j.biopha.2020.110799 · Cited by 25

Acute TBK1/IKK-ε Inhibition Enhances the Generation of Disease-Associated Microglia-Like Phenotype Upon Cortical Stab-Wound Injury

Rehman, R., Tar, L., Olamide, A. J., Li, Z., Kassubek, J., Böckers, T. M., Weishaupt, J. H., Ludolph, A. C., Wiesner, D., & Roselli, F. (2021) · Frontiers in Aging Neuroscience · doi:10.3389/fnagi.2021.684171 · Cited by 24

Slingshot homolog-1–mediated Nrf2 sequestration tips the balance from neuroprotection to neurodegeneration in Alzheimer’s disease

Cazzaro, S., Woo, J. A., Wang, X., Liu, T., Rego, S., Kee, T. R., Koh, Y., Vázquez‐Rosa, E., Pieper, A. A., & Kang, D. E. (2023) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.2217128120 · Cited by 23

Mitochondria-associated membrane collapse impairs TBK1-mediated proteostatic stress response in ALS

Watanabe, S., Murata, Y., Oka, Y., Oiwa, K., Horiuchi, M., Iguchi, Y., Komine, O., Sobue, A., Katsuno, M., Ogi, T., et al. (2023) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.2315347120 · Cited by 25

Regulation of TBK1 activity by Optineurin contributes to cell cycle-dependent expression of the interferon pathway

Weil, R., Laplantine, E., & Génin, P. (2016) · Cytokine & Growth Factor Reviews · doi:10.1016/j.cytogfr.2016.03.001 · Cited by 24

SSH1 impedes SQSTM1/p62 flux and MAPT/Tau clearance independent of CFL (cofilin) activation

Fang, C. C., Woo, J. A., Liu, T., Zhao, X., Cazzaro, S., Yan, Y., Matlack, J. K., Kee, T. R., LePochat, P., & Kang, D. E. (2020) · Autophagy · doi:10.1080/15548627.2020.1816663 · Cited by 22

cGAS-STING signaling in ischemic diseases

Cai, L., Tan, Y., Ni, D., Peng, J., & Yi, G. (2022) · Clinica Chimica Acta · doi:10.1016/j.cca.2022.04.003 · Cited by 25

Toxoplasma gondii ROP18 I inhibits host innate immunity through cGAS‐STING signaling

Chen, M., Yao, L., Zhou, L., Yang, P., Zou, W., Xu, L., Li, S., & Peng, H. (2022) · The FASEB Journal · doi:10.1096/fj.202101347r · Cited by 21

SQSTM1/p62 and Hepatic Mallory-Denk Body Formation in Alcohol-Associated Liver Disease

Qian, H., & Ding, W. (2023) · American Journal Of Pathology · doi:10.1016/j.ajpath.2023.02.015 · Cited by 22

Emerging roles of TBK1 in cancer immunobiology

Miranda, A., Shirley, C. A., & Jenkins, R. W. (2024) · Trends in cancer · doi:10.1016/j.trecan.2024.02.007 · Cited by 22

Autophagy Promotes Duck Tembusu Virus Replication by Suppressing p62/SQSTM1-Mediated Innate Immune Responses In Vitro

Hu, Z., Pan, Y., Cheng, A., Zhang, X., Wang, M., Chen, S., Zhu, D., Liu, M., Yang, Q., Wu, Y., et al. (2020) · Vaccines · doi:10.3390/vaccines8010022 · Cited by 21

Strategies employed by viruses to manipulate autophagy

Kumar, N. D., Smit, J. M., & Reggiori, F. (2020) · Progress in molecular biology and translational science · doi:10.1016/bs.pmbts.2020.01.004 · Cited by 22

The Role of WIPI2, ATG16L1 and ATG12-ATG5 in Selective and Nonselective Autophagy

Campisi, D., Hawkins, N., Bonjour, K., & Wollert, T. (2025) · Journal of Molecular Biology · doi:10.1016/j.jmb.2025.169138 · Cited by 22

Functional and structural consequences of TBK1 missense variants in frontotemporal lobar degeneration and amyotrophic lateral sclerosis

Gurfinkel, Y., Polain, N., Sonar, K., Nice, P. A., Mancera, R. L., & Rea, S. L. (2022) · Neurobiology of Disease · doi:10.1016/j.nbd.2022.105859 · Cited by 20

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Kurusu, R., Morishita, H., & Komatsu, M. (2023) · The Journal of Biochemistry · doi:10.1093/jb/mvad089 · Cited by 22

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Lin, Y., Lin, T., Chen, C., Wang, R.-H., Lin, Y.-H., Tseng, T.-Y., Zhuang, Y.-J., Tang, S.-Y., Lin, Y.-C., Pang, J.-Y., et al. (2023) · ACS Nano · doi:10.1021/acsnano.3c04739 · Cited by 20

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Wei, J., Wang, X., Yu, D., Tu, Y., & Yu, Y. (2024) · Discover Oncology · doi:10.1007/s12672-024-01525-9 · Cited by 20

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Foster, A., Scott, D., Layfield, R., & Rea, S. L. (2019) · Molecular and Cellular Neuroscience · doi:10.1016/j.mcn.2019.04.001 · Cited by 19

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Alam, M., Ansari, M. M., Noor, S., Mohammad, T., Hasan, G. M., Kazim, S. N., & Hassan, M. I. (2022) · International Journal of Biological Macromolecules · doi:10.1016/j.ijbiomac.2022.03.157 · Cited by 21

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Acharya, D., Sayyad, Z., Hoenigsperger, H., Hirschenberger, M., Zurenski, M. A., Balakrishnan, K., Zhu, J., Gableske, S., Kato, J., Zhang, S., et al. (2025) · Nature Communications · doi:10.1038/s41467-025-59338-5 · Cited by 21

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Zhao, P., & Saltiel, A. R. (2020) · Frontiers in Immunology · doi:10.3389/fimmu.2020.592949 · Cited by 17

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Thinwa, J. W., Zou, Z., Parks, E., Sebti, S., Hui, K. K., Wei, Y., Goodarzi, M., Singh, V., Urquhart, G., Jewell, J. L., et al. (2023) · Journal of Clinical Investigation · doi:10.1172/jci168544 · Cited by 21

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Eren, R. O., Kaya, G. G., Schwarzer, R., & Pasparakis, M. (2024) · Nature Communications · doi:10.1038/s41467-023-44372-y · Cited by 18

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

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Ke, P., Chang, C.-W., & Hsiao, Y.-C. (2022) · Cells · doi:10.3390/cells11071132 · Cited by 17

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Garcia‐Garcia, J., Berge, A. K. M., Overå, K. S., Larsen, K. B., Bhujabal, Z., Brech, A., Abudu, Y. P., Lamark, T., Johansen, T., & Sjøttem, E. (2022) · FEBS Journal · doi:10.1111/febs.16628 · Cited by 17

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Ke, P. (2023) · Cells · doi:10.3390/cells12060956 · Cited by 17

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Pascall, J. C., Webb, L. M. C., Eskelinen, E., Innocentin, S., Attaf, N., & Butcher, G. W. (2018) · PLoS ONE · doi:10.1371/journal.pone.0196504 · Cited by 17

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Maculins, T., Verschueren, E., Hinkle, T. B., Choi, M., Chang, P., Chalouni, C. M., Rao, S. C., Kwon, Y. C., Lim, J., Katakam, A. K., et al. (2021) · eLife · doi:10.7554/elife.62320 · Cited by 16

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Davidson, J. M., Wu, S., Rayner, S. L., Cheng, F., Duncan, K., Russo, C., Newbery, M., Ding, K., Scherer, N. M., Balez, R., et al. (2023) · Molecular Neurobiology · doi:10.1007/s12035-023-03355-2 · Cited by 17

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

TBK1 haploinsufficiency in ALS and FTD compromises membrane trafficking

Lu, Y., Almeida, S., & Gao, F. (2021) · Acta Neuropathologica · doi:10.1007/s00401-021-02331-1 · Cited by 15

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Richter, B., Sliter, D. A., Herhaus, L., Stolz, A., Wang, C., Beli, P., Zaffagnini, G., Wild, P., Martens, S., Wagner, S. A., et al. (2016) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.1523926113 · Cited by 755

The PINK1-PARKIN Mitochondrial Ubiquitylation Pathway Drives a Program of OPTN/NDP52 Recruitment and TBK1 Activation to Promote Mitophagy

Heo, J.-M., Ordureau, A., Paulo, J. A., Rinehart, J., & Harper, J. W. (2015) · Molecular Cell · doi:10.1016/j.molcel.2015.08.016 · Cited by 906

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Saha, B., Olsvik, H. L., Williams, G. L., Oh, S., Evjen, G., Sjøttem, E., & Mandell, M. A. (2024) · Cell Reports · doi:10.1016/j.celrep.2024.114294 · Cited by 20

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Treister, R., Kliger, M., Zuckerman, G. H., Goor-Aryeh, I., & Eisenberg, E. (2011) · European Journal of Pain Supplements · doi:10.1016/s1754-3207(11)70912-9

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Yamano, K., Sawada, M., Kikuchi, R., Nagataki, K., Kojima, W., Endo, R., Kinefuchi, H., Sugihara, A., Fujino, T., Watanabe, A., et al. (2024) · The EMBO Journal · doi:10.1038/s44318-024-00036-1 · Cited by 68