TBK1: a new player in ALS linking autophagy and neuroinflammation
Open accessAbstract
Amyotrophic lateral sclerosis (ALS) is an adult-onset neurodegenerative disorder affecting motor neurons, resulting in progressive muscle weakness and death by respiratory failure. Protein and RNA aggregates are a hallmark of ALS pathology and are thought to contribute to ALS by impairing axonal transport. Mutations in several genes known to contribute to ALS result in deposition of their protein products as aggregates; these include TARDBP, C9ORF72, and SOD1. In motor neurons, this can disrupt transport of mitochondria to areas of metabolic need, resulting in damage to cells and can elicit a neuroinflammatory response leading to further neuronal damage. Recently, eight independent human genetics studies have uncovered a link between TANK-binding kinase 1 (TBK1) mutations and ALS. TBK1 belongs to the IKK-kinase family of kinases that are involved in innate immunity signaling pathways; specifically, TBK1 is an inducer of type-1 interferons. TBK1 also has a major role in autophagy and mitophagy, chiefly the phosphorylation of autophagy adaptors. Several other ALS genes are also involved in autophagy, including p62 and OPTN. TBK1 is required for efficient cargo recruitment in autophagy; mutations in TBK1 may result in impaired autophagy and contribute to the accumulation of protein aggregates and ALS pathology. In this review, we focus on the role of TBK1 in autophagy and the contributions of this process to the pathophysiology of ALS.
The claims and statistics of this paper haven’t been checked yet.
Run the check — free, no account needed. It reads the open-access text and checks the sources it cites.
Integrity signals
Registry
Cites
Statistics
Claims the paper makes
The claims and statistics of this paper haven’t been checked yet.
Run the check — free, no account needed. It reads the open-access text and checks the sources it cites.
Claims other papers make about this one
Each is checked against this paper’s own text: does it say what the citing paper says it does?
TBK1 is a cytoplasmically-localized homodimeric multidomain protein with an ubiquitin-like domain, an N-terminal serine/threonine kinase domain, and two coiled-coil domains.
“TBK1/NAK/T2K (TANK binding kinase 1) is a cytoplasmically-localized homodimeric multidomain protein with an ubiquitin-like domain, a N-terminal serine/threonine kinase domain, and two coiled-coil domains [192].”
From Autophagy and ALS: mechanistic insights and therapeutic implications (2022) · cites this paper as [192]
Tbk1 deletion disrupts the migration of T-cells that may exert anti-inflammatory effects in ALS models.
“In keeping with this, Tbk1 deletion disrupts the migration of T-cells [216] that may exert anti-inflammatory effects in ALS models [192,217].”
From Autophagy and ALS: mechanistic insights and therapeutic implications (2022) · cites this paper as [192]
ALS-associated mutations in TBK1, OPTN, SQSTM1, and VCP all affect autophagy as well as microglial function and innate immunity.
“ALS-associated mutations in TBK1, OPTN, SQSTM1, and VCP all affect autophagy as well as microglial function and innate immunity [192,205,206,441–443].”
From Autophagy and ALS: mechanistic insights and therapeutic implications (2022) · cites this paper as [192]
Self-check
Percentages, sums and reported differences re-computed from the paper’s own numbers.
The self-check needs the paper’s full text.
Cites
Tissue-based map of the human proteome
Uhlén, M., Fagerberg, L., Hallström, B. M., Lindskog, C., Oksvold, P., Mardinoglu, A., Sivertsson, Å., Kampf, C., Sjöstedt, E., Asplund, A., et al. (2015) · Science · doi:10.1126/science.1260419 · Cited by 15,286 · see citing works
Rosen, D. R., Siddique, T., Patterson, D., Figlewicz, D. A., Sapp, P., Hentati, A., Donaldson, D., Goto, J., O'Regan, J. P., Deng, H.-X., et al. (1993) · Nature · doi:10.1038/362059a0 · Cited by 7,062 · see citing works
DeJesus-Hernandez, M., Mackenzie, I. R., Boeve, B. F., Boxer, A. L., Baker, M., Rutherford, N. J., Nicholson, A. M., Finch, N. A., Flynn, H., Adamson, J., et al. (2011) · Neuron · doi:10.1016/j.neuron.2011.09.011 · Cited by 4,936 · see citing works
Suppression of basal autophagy in neural cells causes neurodegenerative disease in mice
Hara, T., Nakamura, K., Matsui, M., Yamamoto, A., Nakahara, Y., Suzuki-Migishima, R., Yokoyama, M., Mishima, K., Saito, I., Okano, H., et al. (2006) · Nature · doi:10.1038/nature04724 · Cited by 3,882 · see citing works
Antimicrobial Autophagy: A Conserved Innate Immune Response in Drosophila
Moy, R. H., & Cherry, S. R. (2013) · Journal of Innate Immunity · doi:10.1159/000350326 · Cited by 3,549 · see citing works
Loss of autophagy in the central nervous system causes neurodegeneration in mice
Komatsu, M., Waguri, S., Chiba, T., Murata, S., Iwata, J.-I., Tanida, I., Ueno, T., Koike, M., Uchiyama, Y., Kominami, E., et al. (2006) · Nature · doi:10.1038/nature04723 · Cited by 3,500 · see citing works
The ubiquitin kinase PINK1 recruits autophagy receptors to induce mitophagy
Lazarou, M., Sliter, D. A., Kane, L. A., Sarraf, S. A., Wang, C., Burman, J. L., Sideris, D. P., Fogel, A. I., & Youle, R. J. (2015) · Nature · doi:10.1038/nature14893 · Cited by 2,774 · see citing works
Signaling to NF-κB by Toll-like receptors
Kawai, T., & Akira, S. (2007) · Trends in Molecular Medicine · doi:10.1016/j.molmed.2007.09.002 · Cited by 2,395 · see citing works
A ubiquitin-like system mediates protein lipidation
Ichimura, Y., Kirisako, T., Takao, T., Satomi, Y., Shimonishi, Y., Ishihara, N., Mizushima, N., Tanida, I., Kominami, E., Ohsumi, M., et al. (2000) · Nature · doi:10.1038/35044114 · Cited by 2,064 · see citing works
ULK-Atg13-FIP200 Complexes Mediate mTOR Signaling to the Autophagy Machinery
Jung, C. H., Jun, C. B., Ro, S.-H., Kim, Y.-M., Otto, N. M., Cao, J., Kundu, M., & Kim, D.-H. (2009) · Molecular Biology of the Cell · doi:10.1091/mbc.e08-12-1249 · Cited by 2,025 · see citing works
A protein conjugation system essential for autophagy
Mizushima, N., Noda, T., Yoshimori, T., Tanaka, Y., Ishii, T., George, M. D., Klionsky, D. J., Ohsumi, M., & Ohsumi, Y. (1998) · Nature · doi:10.1038/26506 · Cited by 1,701 · see citing works
Apoptosis in neurodegenerative disorders
Mattson, M. P. (2000) · Nature Reviews Molecular Cell Biology · doi:10.1038/35040009 · Cited by 1,605 · see citing works
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 · see citing works
Exome sequencing in amyotrophic lateral sclerosis identifies risk genes and pathways
Cirulli, E. T., Lasseigne, B. N., Petrovski, S., Sapp, P. C., Dion, P. A., Leblond, C. S., Couthouis, J., Lu, Y.-F., Wang, Q., Krueger, B. J., et al. (2015) · Science · doi:10.1126/science.aaa3650 · Cited by 966 · see citing works
Riluzole for amyotrophic lateral sclerosis (ALS)/motor neuron disease (MND)
Miller, R. G., Jd, M., Lyon, M., & Moore, D. (2002) · Cochrane Database of Systematic Reviews · doi:10.1002/14651858.cd001447 · Cited by 910 · see citing works
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 · see citing works
Thurston, T. L. M., Ryzhakov, G., Bloor, S., von Muhlinen, N., & Randow, F. (2009) · Nature Immunology · doi:10.1038/ni.1800 · Cited by 872 · see citing works
Chiò, A., Logroscino, G., Traynor, B. J., Collins, J., Simeone, J. C., Goldstein, L. A., & White, L. A. (2013) · Neuroepidemiology · doi:10.1159/000351153 · Cited by 862 · see citing works
Mitochondria and neuronal activity
Kann, O., & Kovács, R. (2006) · American Journal of Physiology-Cell Physiology · doi:10.1152/ajpcell.00222.2006 · Cited by 847 · see citing works
Haploinsufficiency of TBK1 causes familial ALS and fronto-temporal dementia
Freischmidt, A., Wieland, T., Richter, B., Ruf, W., Schaeffer, V., Müller, K., Marroquin, N., Nordin, F., Hübers, A., Weydt, P., et al. (2015) · Nature Neuroscience · doi:10.1038/nn.4000 · Cited by 786 · see citing works
HDAC6 controls autophagosome maturation essential for ubiquitin‐selective quality‐control autophagy
Lee, J., Koga, H., Kawaguchi, Y., Tang, W., Wong, E., Gao, Y., Pandey, U. B., Kaushik, S., Tresse, E., Lu, J., et al. (2010) · The EMBO Journal · doi:10.1038/emboj.2009.405 · Cited by 756 · see citing works
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 · cited 1× · see citing works
“Whilst wild-type TBK1 localizes to damaged mitochondria, the E696K mutant exhibited severely reduced colocalization with damaged mitochondria [69].”
BackgroundA comprehensive review of amyotrophic lateral sclerosis
Zarei, S., Carr, K., Reiley, L. E., Diaz, K., Guerra, O., Altamirano, P., Pagani, W., Lodin, D., Orozco, G., & Chinea, A. R. (2015) · Surgical Neurology International · doi:10.4103/2152-7806.169561 · Cited by 737 · see citing works
Kong, J., & Xu, Z. (1998) · Journal of Neuroscience · doi:10.1523/jneurosci.18-09-03241.1998 · Cited by 723 · see citing works
TBK-1 Promotes Autophagy-Mediated Antimicrobial Defense by Controlling Autophagosome Maturation
Pilli, M., Arko-Mensah, J., Ponpuak, M., Roberts, E., Master, S., Mandell, M. A., Dupont, N., Ornatowski, W., Jiang, S., Bradfute, S. B., et al. (2012) · Immunity · doi:10.1016/j.immuni.2012.04.015 · Cited by 655 · see citing works
Fecto, F. (2011) · Archives of Neurology · doi:10.1001/archneurol.2011.250 · Cited by 650 · see citing works
Bowling, A. C., Schulz, J. B., Brown, R. H., & Beal, M. F. (1993) · Journal of Neurochemistry · doi:10.1111/j.1471-4159.1993.tb07478.x · Cited by 629 · see citing works
<i>C9orf72</i> is required for proper macrophage and microglial function in mice
O’Rourke, J. G., Bogdanik, L., Yáñez, A., Lall, D., Wolf, A. J., Muhammad, A. K. M. G., Ho, R., Carmona, S., Vit, J. P., Zarrow, J., et al. (2016) · Science · doi:10.1126/science.aaf1064 · Cited by 550 · see citing works
Zhang, C., & Cuervo, A. M. (2008) · Nature Medicine · doi:10.1038/nm.1851 · Cited by 520 · see citing works
Toxicity of Familial ALS-Linked SOD1 Mutants from Selective Recruitment to Spinal Mitochondria
Liu, J., Lillo, C., Jonsson, P. A., Velde, C. V., Ward, C. M., Miller, T. M., Subramaniam, J. R., Rothstein, J. D., Marklund, S. L., Andersen, P. M., et al. (2004) · Neuron · doi:10.1016/j.neuron.2004.06.016 · Cited by 506 · see citing works
Lee, Y., Chen, H.-J., Peres, J., Gómez-Deza, J., Attig, J., Štalekar, M., Troakes, C., Nishimura, A. L., Scotter, E. L., Vance, C. A., et al. (2013) · Cell Reports · doi:10.1016/j.celrep.2013.10.049 · Cited by 487 · see citing works
Sarcopenia and its implications for the elderly
Roubenoff, R. (2000) · European Journal of Clinical Nutrition · doi:10.1038/sj.ejcn.1601024 · Cited by 448 · see citing works
Dynein-dependent Movement of Autophagosomes Mediates Efficient Encounters with Lysosomes
Kimura, S., Noda, T., & Yoshimori, T. (2008) · Cell Structure and Function · doi:10.1247/csf.08005 · Cited by 436 · see citing works
Neuronal autophagy and neurodegenerative diseases
Son, J. H., Shim, J. H., Kim, K., Ha, J., & Han, J. (2012) · Experimental & Molecular Medicine · doi:10.3858/emm.2012.44.2.031 · Cited by 342 · see citing works
Magrané, J., Cortez, C. A., Gan, W., & Manfredi, G. (2013) · Human Molecular Genetics · doi:10.1093/hmg/ddt528 · Cited by 334 · see citing works
Emerging mechanisms of molecular pathology in ALS
Peters, O. M., Ghasemi, M., & Brown, R. H. (2015) · Journal of Clinical Investigation · doi:10.1172/jci71601 · Cited by 319 · see citing works
Matsumoto, G., Shimogori, T., Hattori, N., & Nukina, N. (2015) · Human Molecular Genetics · doi:10.1093/hmg/ddv179 · Cited by 317 · see citing works
Pottier, C., Bieniek, K. F., Finch, N., van de Vorst, M., Baker, M., Perkersen, R., Brown, P., Ravenscroft, T., van Blitterswijk, M., Nicholson, A. M., et al. (2015) · Acta Neuropathologica · doi:10.1007/s00401-015-1436-x · Cited by 312 · see citing works
Mechanisms and pathways of innate immune activation and regulation in health and cancer
Cui, J., Chen, Y., Wang, H. Y., & Wang, R. (2014) · Human Vaccines & Immunotherapeutics · doi:10.4161/21645515.2014.979640 · Cited by 310 · see citing works
Sullivan, P. M., Zhou, X., Robins, A. M., Paushter, D. H., Kim, D., Smolka, M. B., & Hu, F. (2016) · Acta Neuropathologica Communications · doi:10.1186/s40478-016-0324-5 · Cited by 295 · see citing works
Casadio, M., Ciancanelli, M. J., Ou, Y.-H., Lorenzo, L., Klaudel‐Dreszler, M., Pauwels, E., Sancho‐Shimizu, V., de Diego, R. P., Abhyankar, A., Israelsson, E., et al. (2012) · The Journal of Experimental Medicine · doi:10.1084/jem.20111316 · Cited by 278 · see citing works
Crystal Structure and Mechanism of Activation of TANK-Binding Kinase 1
Larabi, A., Devos, J. M., Ng, S., Nanao, M., Round, A. R., Maniatis, T., & Panne, D. (2013) · Cell Reports · doi:10.1016/j.celrep.2013.01.034 · Cited by 251 · see citing works
Autophagy in Spinal Cord Motor Neurons in Sporadic Amyotrophic Lateral Sclerosis
Sasaki, S. (2011) · Journal of Neuropathology & Experimental Neurology · doi:10.1097/nen.0b013e3182160690 · Cited by 249 · see citing works
Molecular basis of Tank-binding kinase 1 activation by transautophosphorylation
Ma, X., Helgason, E., Phung, Q. T., Quan, C. L., Iyer, R. S., Lee, M. W., Bowman, K. K., Starovasnik, M. A., & Dueber, E. C. (2012) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.1121552109 · Cited by 240 · see citing works
Lindberg, M. J., Byström, R., Boknäs, N., Andersen, P. M., & Oliveberg, M. (2005) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.0501957102 · Cited by 232 · see citing works
Increased autophagy in transgenic mice with a G93A mutant SOD1 gene
Morimoto, N., Nagai, M., Ohta, Y., Miyazaki, K., Kurata, T., Morimoto, M., Murakami, T., Takehisa, Y., Ikeda, Y., Kamiya, T., et al. (2007) · Brain Research · doi:10.1016/j.brainres.2007.06.045 · Cited by 223 · see citing works
Structure and Ubiquitination-Dependent Activation of TANK-Binding Kinase 1
Tu, D., Zhu, Z., Zhou, A. Y., Yun, C., Lee, K., Toms, A. V., Li, Y., Dunn, G. P., Chan, E. M., Thai, T. C., et al. (2013) · Cell Reports · doi:10.1016/j.celrep.2013.01.033 · Cited by 215 · see citing works
Helgason, E., Phung, Q. T., & Dueber, E. C. (2013) · FEBS Letters · doi:10.1016/j.febslet.2013.01.059 · Cited by 185 · see citing works
Glial toll-like receptor signaling in central nervous system infection and autoimmunity
Carpentier, P. A., Duncan, D. S., & Miller, S. D. (2007) · Brain Behavior and Immunity · doi:10.1016/j.bbi.2007.08.011 · Cited by 178 · see citing works
Loss of <i>TBK1</i> is a frequent cause of frontotemporal dementia in a Belgian cohort
Gijselinck, I., Van Mossevelde, S., van der Zee, J., Sieben, A., Philtjens, S., Heeman, B., Engelborghs, S., Vandenbulcke, M., De Baets, G., Bäumer, V., et al. (2015) · Neurology · doi:10.1212/wnl.0000000000002220 · Cited by 174 · see citing works
Sasaki, S., & Iwata, M. (1996) · Neurology · doi:10.1212/wnl.47.2.535 · Cited by 169 · see citing works
The Function of Autophagy in Neurodegenerative Diseases
Kiriyama, Y., & Nochi, H. (2015) · International Journal of Molecular Sciences · doi:10.3390/ijms161125990 · Cited by 168 · see citing works
Exposure to chemicals and metals and risk of amyotrophic lateral sclerosis: A systematic review
Sutedja, N. A., Veldink, J. H., Fischer, K., Kromhout, H., Heederik, D. J. J., Huisman, M. H. B., Wokke, J. H. J., & van den Berg, L. H. (2009) · Amyotrophic Lateral Sclerosis · doi:10.3109/17482960802455416 · Cited by 161 · see citing works
Neuronal macroautophagy: From development to degeneration
Boland, B., & Nixon, R. A. (2006) · Molecular Aspects of Medicine · doi:10.1016/j.mam.2006.08.009 · Cited by 156 · see citing works
Mórotz, G. M., Vos, K. J. D., Vagnoni, A., Ackerley, S., Shaw, C. E., & Miller, C. C. J. (2012) · Human Molecular Genetics · doi:10.1093/hmg/dds011 · Cited by 139 · see citing works
Functional Dissection of the TBK1 Molecular Network
Goncalves, A., Bürckstümmer, T., Dixit, E., Scheicher, R., Górna, M. W., Karayel, E., Sugar, C., Stukalov, A., Berg, T., Kralovics, R., et al. (2011) · PLoS ONE · doi:10.1371/journal.pone.0023971 · Cited by 136 · see citing works
Involvement of the ubiquitin‐like domain of TBK1/IKK‐i kinases in regulation of IFN‐inducible genes
Ikeda, F., Hecker, C., Rozenknop, A., Nordmeier, R. D., Rogov, V. V., Hofmann, K., Akira, S., Dötsch, V., & Đikić, I. (2007) · The EMBO Journal · doi:10.1038/sj.emboj.7601773 · Cited by 121 · see citing works
Li, F., Xie, X., Wang, Y., Liu, J., Cheng, X., Guo, Y., Gong, Y., Hu, S., & Pan, L. (2016) · Nature Communications · doi:10.1038/ncomms12708 · Cited by 121 · see citing works
Dissection of TBK1 signaling via phosphoproteomics in lung cancer cells
Kim, J., Welsh, E. A., Oguz, U., Fang, B., Bai, Y., Kinose, F., Bronk, C. C., Rix, L. L. R., Beg, A. A., Rix, U., et al. (2013) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.1220674110 · Cited by 120 · see citing works
Regulation of T-cell activation and migration by the kinase TBK1 during neuroinflammation
Yu, J., Zhou, X., Chang, M., Nakaya, M., Chang, J.-H., Xiao, Y., William Lindsey, J., Dorta-Estremera, S., Cao, W., Zal, A., et al. (2015) · Nature Communications · doi:10.1038/ncomms7074 · Cited by 118 · see citing works
Nakashima, H., Nguyen, T., Goins, W. F., & Chiocca, E. A. (2014) · Journal of Biological Chemistry · doi:10.1074/jbc.m114.593871 · Cited by 108 · see citing works
Pillai, S., Nguyen, J. V., Johnson, J., Haura, E. B., Coppola, D., & Chellappan, S. (2015) · Nature Communications · doi:10.1038/ncomms10072 · Cited by 103 · see citing works
Maharjan, N., Künzli, C., Buthey, K., & Saxena, S. (2016) · Molecular Neurobiology · doi:10.1007/s12035-016-9850-1 · Cited by 99 · see citing works
Modification of BECN1 by ISG15 plays a crucial role in autophagy regulation by type I IFN/interferon
Xu, D., Zhang, T., Xiao, J., Zhu, K., Wei, R., Wu, Z., Meng, H., Li, Y., & Yuan, J. (2015) · Autophagy · doi:10.1080/15548627.2015.1023982 · Cited by 98 · see citing works
Van Mossevelde, S., van der Zee, J., Gijselinck, I., Engelborghs, S., Sieben, A., Van Langenhove, T., De Bleecker, J., Baets, J., Vandenbulcke, M., Van Laere, K., et al. (2016) · Brain · doi:10.1093/brain/awv358 · Cited by 98 · see citing works
Neuroinflammation in motor neuron disease
Endo, F., Komine, O., & Yamanaka, K. (2016) · Clinical and Experimental Neuroimmunology · doi:10.1111/cen3.12309 · Cited by 93 · see citing works
Mutational analysis of MATR3 in Taiwanese patients with amyotrophic lateral sclerosis
Lin, K., Tsai, P., Liao, Y., Chen, W., Tsai, C., Soong, B., & Lee, Y. (2015) · Neurobiology of Aging · doi:10.1016/j.neurobiolaging.2015.02.008 · Cited by 91 · see citing works
Le Ber, I., De Septenville, A., Millecamps, S., Camuzat, A., Caroppo, P., Couratier, P., Blanc, F., Lacomblez, L., Sellal, F., Fleury, M.-C., et al. (2015) · Neurobiology of Aging · doi:10.1016/j.neurobiolaging.2015.08.009 · Cited by 89 · see citing works
Neuroinflammation in motor neuron disease.
Komine, O., & Yamanaka, K. (2015) · Europe PMC (PubMed Central) · doi:10.18999/nagjms.77.4.537 · Cited by 87 · see citing works
TBK1Gene Duplication and Normal-Tension Glaucoma
Ritch, R. H., Darbro, B. W., Menon, G., Khanna, C. L., Solivan-Timpe, F., Roos, B. R., Sarfarzi, M., Kawase, K., Yamamoto, T., Robin, A. L., et al. (2014) · JAMA Ophthalmology · doi:10.1001/jamaophthalmol.2014.104 · Cited by 86 · see citing works
Role of autophagy in the pathogenesis of amyotrophic lateral sclerosis
Lee, J. K., Shin, J. H., Lee, J. E., & Choi, E.-J. (2015) · Biochimica et Biophysica Acta (BBA) - Molecular Basis of Disease · doi:10.1016/j.bbadis.2015.08.005 · Cited by 84 · see citing works
Copy Number Variations of TBK1 in Australian Patients With Primary Open-Angle Glaucoma
Awadalla, M. S., Fingert, J. H., Roos, B. R., Chen, S. D. M., Holmes, R., Graham, S. L., Chehade, M., Galanopolous, A., Ridge, B., Souzeau, E., et al. (2014) · American Journal of Ophthalmology · doi:10.1016/j.ajo.2014.09.044 · Cited by 82 · see citing works
The mouse C9ORF72 ortholog is enriched in neurons known to degenerate in ALS and FTD
Suzuki, N., Maroof, A. M., Merkle, F. T., Koszka, K., Intoh, A., Armstrong, I. K. G., Moccia, R., Davis‐Dusenbery, B. N., & Eggan, K. C. (2013) · Nature Neuroscience · doi:10.1038/nn.3566 · Cited by 77 · see citing works
Mutational analysis of TBK1 in Taiwanese patients with amyotrophic lateral sclerosis
Tsai, P., Liu, Y., Lin, K., Liu, Y., Liao, Y., Hsiao, C.-T., Soong, B., Yip, P., & Lee, Y. (2016) · Neurobiology of Aging · doi:10.1016/j.neurobiolaging.2015.12.022 · Cited by 53 · see citing works
TBK1 is associated with ALS and ALS-FTD in Sardinian patients
Borghero, G., Pugliatti, M., Marrosu, F., Marrosu, M. G., Murru, M. R., Floris, G., Cannas, A., Occhineri, P., Cau, T. B., Loi, D., et al. (2016) · Neurobiology of Aging · doi:10.1016/j.neurobiolaging.2016.03.028 · Cited by 50 · see citing works
Novel TBK1 truncating mutation in a familial amyotrophic lateral sclerosis patient of Chinese origin
Williams, K. L., McCann, E. P., Fifita, J. A., Zhang, K., Duncan, E. L., Leo, P. J., Marshall, M. S., Rowe, D. B., Nicholson, G. A., & Blair, I. P. (2015) · Neurobiology of Aging · doi:10.1016/j.neurobiolaging.2015.08.013 · Cited by 41 · see citing works
Crystal structure of the ubiquitin-like domain of human TBK1
Li, J., Li, J., Miyahira, A. K., Sun, J. G., Liu, Y., Cheng, G., & Liang, H. (2012) · Protein & Cell · doi:10.1007/s13238-012-2929-1 · Cited by 36 · see citing works
Spiller, K. J., Restrepo, C. R., Khan, T., Stieber, A., Kwong, L. K., Trojanowski, J. Q., & Lee, V. M. ‐. (2016) · Acta Neuropathologica Communications · doi:10.1186/s40478-016-0377-5 · Cited by 23 · see citing works
Shu, S., Li, X. L., Liu, Q. F., Liu, F., Cui, B., Liu, M. S., Cui, L., Li, X., & Zhang, X. (2016) · Amyotrophic Lateral Sclerosis and Frontotemporal Degeneration · doi:10.1080/21678421.2016.1183681 · Cited by 18 · see citing works
Flagged first, then by citations
Cited by
Sorted by citations
Mead, R. J., Shan, N., Reiser, H. J., Marshall, F., & Shaw, P. J. (2023) · Nature Reviews Drug Discovery · doi:10.1038/s41573-022-00612-2 · Cited by 505 · see citing works
Neuroinflammation in frontotemporal dementia
Bright, F., Werry, E. L., Dobson-Stone, C., Piguet, O., Ittner, L. M., Halliday, G. M., Hodges, J. R., Kiernan, M. C., Loy, C. T., Kassiou, M., et al. (2019) · Nature Reviews Neurology · doi:10.1038/s41582-019-0231-z · Cited by 280 · see citing works
STING mediates neurodegeneration and neuroinflammation in nigrostriatal α-synucleinopathy
Hinkle, J. T., Patel, J., Panicker, N., Karuppagounder, S. S., Biswas, D., Belingon, B., Chen, R., Brahmachari, S., Pletnikova, O., Troncoso, J. C., et al. (2022) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.2118819119 · Cited by 240 · see citing works
Autophagy and ALS: mechanistic insights and therapeutic implications
Chua, J. P., De Calbiac, H., Kabashi, E., & Barmada, S. J. (2022) · Autophagy · doi:10.1080/15548627.2021.1926656 · Cited by 189 · see citing works
“TBK1 mutations were initially described in conditions with prominent neuroinflammatory responses, including two forms of glaucoma [192,202,203] and herpes simplex encephalitis [204].”
BackgroundHuman TBK1 deficiency leads to autoinflammation driven by TNF-induced cell death
Taft, J., Markson, M., Legarda, D., Patel, R., Chan, M., Malle, L., Richardson, A., Gruber, C., Martín-Fernández, M., Mancini, G. M. S., et al. (2021) · Cell · doi:10.1016/j.cell.2021.07.026 · Cited by 151 · see citing works
Béland, L.-C., Markovinovic, A., Jakovac, H., De Marchi, F., Bilic, E., Mazzini, L., Kriz, J., & Munitic, I. (2020) · Brain Communications · doi:10.1093/braincomms/fcaa124 · Cited by 125 · see citing works
Mitophagy and cGAS–STING crosstalk in neuroinflammation
Zhou, X., Wang, J., Yu, L., Qiao, G., Qin, D., Yuen-Kwan Law, B., Ren, F., Wu, J., & Wu, A. (2024) · Acta Pharmaceutica Sinica B · doi:10.1016/j.apsb.2024.05.012 · Cited by 131 · see citing works
Gerbino, V., Kaunga, E., Ye, J., Canzio, D., O’Keeffe, S., Rudnick, N. D., Guarnieri, P., Lutz, C. M., & Maniatis, T. (2020) · Neuron · doi:10.1016/j.neuron.2020.03.005 · Cited by 102 · see citing works
Genetics of Amyotrophic Lateral Sclerosis
Gregory, J. M., Fagegaltier, D., Phatnani, H., & Harms, M. B. (2020) · Current Genetic Medicine Reports · doi:10.1007/s40142-020-00194-8 · Cited by 83 · see citing works
Implications of Microglia in Amyotrophic Lateral Sclerosis and Frontotemporal Dementia
Haukedal, H., & Freude, K. (2019) · Journal of Molecular Biology · doi:10.1016/j.jmb.2019.02.004 · Cited by 68 · see citing works
Molecular mechanisms of mitophagy and its roles in neurodegenerative diseases
Li, X., Huang, L., Lan, J., Feng, X., Li, P., Wu, L., & Peng, Y. (2021) · Pharmacological Research · doi:10.1016/j.phrs.2020.105240 · Cited by 57 · see citing works
- Authors
- Oakes, J. A., Davies, M. C., & Collins, M. O.
- Affiliations
- University of Sheffield (GB)
- Corresponding author
- Collins, Mark O.
- Venue
- Molecular Brain
- Published
- 2017-02-02
- Volume
- 10
- Issue
- 1
- Pages
- 5-5
- ISSN
- 1756-6606 (ISSN-L)
- PMC
- PMC5288885
- OpenAlex
- W2585432400
- Cited by
- 319
- References
- 79
- Citations by year
- 2026: 19 · 2025: 27 · 2024: 45 · 2023: 30 · 2022: 46 · 2021: 39 · 2020: 49 · 2019: 23 · 2018: 26 · 2017: 14 · 2016: 1
- FWCI
- 4.08
- Type
- journal article
- Language
- en
- Open access
- gold
- doi.org
- Licence
- cc-by
- Locations
- Molecular Brain (publishedVersion, cc-by)
- PubMed Central (publishedVersion, cc-by)
- PubMed (publishedVersion)
- White Rose Research Online (University of Leeds, The University of Sheffield, University of York) (acceptedVersion)
- Funders
- Royal Society (R/144823-11-1)
- Topics
- Health Sciences › Medicine › Neurology › Amyotrophic Lateral Sclerosis Research
- Health Sciences › Medicine › Epidemiology › Autophagy in Disease and Therapy
- Life Sciences › Neuroscience › Cellular and Molecular Neuroscience › Hereditary Neurological Disorders
- Keywords
- amyotrophic lateral sclerosis, TBK1, autophagy, neuroinflammation, protein aggregates, motor neurons, mitophagy, axonal transport, type I interferon signaling, p62, optineurin, ALS genetics, neurodegeneration
- MeSH terms
- Amyotrophic Lateral Sclerosis, Animals, Autophagy, Humans, Inflammation, Models, Biological, Nervous System, Protein Serine-Threonine Kinases
About these checks
Registry, retraction, Cites and statistics results are computed, not judged, with one exception: a printed reference that no index lists is read once by a model before it counts as a citation error. Claims are extracted by a model and kept only when their quote appears verbatim in the text; each cited source is then checked, with a model’s help, for whether it says what the claim relies on. Those verdicts can be wrong — read the claim’s quote and the cited source before relying on one.
Statistics and arithmetic are recomputed, not judged.
Confidence bands are shown only for fields calibrated on our annotated test set. None is calibrated yet, so no band is shown.
What counts as a claim ›How we measure confidence ›How we check this ›
Are you an author, or do you see a problem with this page? Request a review
