The DOI matches its Crossref record; 35 of the 35 references it cites were found in a registry or an index.
Haploinsufficiency of TBK1 causes familial ALS and fronto-temporal dementia
Open accessAbstract
Amyotrophic lateral sclerosis (ALS) is a genetically heterogeneous neurodegenerative syndrome hallmarked by adult-onset loss of motor neurons. We performed exome sequencing of 252 familial ALS (fALS) and 827 control individuals. Gene-based rare variant analysis identified an exome-wide significant enrichment of eight loss-of-function (LoF) mutations in TBK1 (encoding TANK-binding kinase 1) in 13 fALS pedigrees. No enrichment of LoF mutations was observed in a targeted mutation screen of 1,010 sporadic ALS and 650 additional control individuals. Linkage analysis in four families gave an aggregate LOD score of 4.6. In vitro experiments confirmed the loss of expression of TBK1 LoF mutant alleles, or loss of interaction of the C-terminal TBK1 coiled-coil domain (CCD2) mutants with the TBK1 adaptor protein optineurin, which has been shown to be involved in ALS pathogenesis. We conclude that haploinsufficiency of TBK1 causes ALS and fronto-temporal dementia.
Overview
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
Verification
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?
In the citing paper
“Neuropathological analysis of CNS tissue from ALS patients with TBK1 mutations shows SQSTM1- and TARDBP-positive inclusions in motor neurons and glia [206,210,211], along with reduced TBK1 mRNA and protein, suggesting haploinsufficiency mechanisms [205,206].”
From Autophagy and ALS: mechanistic insights and therapeutic implications (2022) · cites this paper as [206]
In the citing paper
“Whole exome sequencing studies revealed that mutations in TBK1 are also responsible for ~1% of patients with familial or otherwise sporadic ALS [205,206].”
From Autophagy and ALS: mechanistic insights and therapeutic implications (2022) · cites this paper as [206]
In the citing paper
“Consistent with this, most ALS-associated TBK1 mutations affect the kinase and the coiled-coiled domains, both of which are vital for TBK1 function [206].”
From Autophagy and ALS: mechanistic insights and therapeutic implications (2022) · cites this paper as [206]
In the citing paper
“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 [206]
In the citing paper
“Additionally, mutations in TBK1 are associated with developing FTD,317,318”
From Microglia in neurodegenerative diseases: mechanism and potential therapeutic targets (2023) · cites this paper as [318]
Self-check
Percentages, sums and reported differences re-computed from the paper’s own numbers.
The self-check needs the paper’s full text.
Citations
Cites
Analysis of Relative Gene Expression Data Using Real-Time Quantitative PCR and the 2−ΔΔCT Method
Livak, K. J., & Schmittgen, T. D. (2001) · Methods · doi:10.1006/meth.2001.1262 · Cited by 180,860
PLINK: a tool set for whole-genome association and population-based linkage analyses.
Purcell, S., Neale, B., Todd-Brown, K., Thomas, L., Ferreira, M. A. R., Bender, D., Maller, J., Sklar, P., de Bakker, P. I. W., Daly, M. J., et al. (2007) · The American Journal of Human Genetics · doi:10.1086/519795 · Cited by 34,089
Coot : model-building tools for molecular graphics
Emsley, P., & Cowtan, K. (2004) · Acta Crystallographica Section D Biological Crystallography · doi:10.1107/s0907444904019158 · Cited by 30,571
Repertoires of Autophagy in the Pathogenesis of Ocular Diseases
Li, Y., Jiang, Q. L., Cao, G.-F., Yao, J., & Yan, B. (2015) · Cellular Physiology and Biochemistry · doi:10.1159/000373980 · Cited by 16,351
Haploview: analysis and visualization of LD and haplotype maps
Barrett, J. C., Fry, B., Maller, J., & Daly, M. J. (2004) · Bioinformatics · doi:10.1093/bioinformatics/bth457 · Cited by 14,551
Mutation of the mouse klotho gene leads to a syndrome resembling ageing
Kuro-o, M., Matsumura, Y., Aizawa, H., Kawaguchi, H., Suga, T., Utsugi, T., Ohyama, Y., Kurabayashi, M., Kaname, T., Kume, E., et al. (1997) · Nature · doi:10.1038/36285 · Cited by 3,837
Merlin—rapid analysis of dense genetic maps using sparse gene flow trees
Abecasis, G. R., Cherny, S. S., Cookson, W., & Cardon, L. R. (2001) · Nature Genetics · doi:10.1038/ng786 · Cited by 3,323
Li, B., & Leal, S. M. (2008) · The American Journal of Human Genetics · doi:10.1016/j.ajhg.2008.06.024 · Cited by 1,527
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
Self-citationMutations 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
Flagged first, then by citations
Cited by
Sorted by citations
Items 301–400 of 788
Optineurin Regulates the Interferon Response in a Cell Cycle-Dependent Manner
Génin, P., Cuvelier, F., Lambin, S., Filipe, J. C.-R., Autrusseau, E., Laurent‐Winter, C., Laplantine, E., & Weil, R. (2015) · PLoS Pathogens · doi:10.1371/journal.ppat.1004877 · Cited by 45
OPTN 691_692insAG is a founder mutation causing recessive ALS and increased risk in heterozygotes
Goldstein, O., Nayshool, O., Nefussy, B., Traynor, B. J., Renton, A. E., Gana‐Weisz, M., Drory, V. E., & Orr‐Urtreger, A. (2016) · Neurology · doi:10.1212/wnl.0000000000002334 · Cited by 45
An, D., Fujiki, R., Iannitelli, D. E., Smerdon, J. W., Maity, S., Rose, M. F., Gelber, A., Wanaselja, E. K., Yagudayeva, I., Lee, J. Y., et al. (2019) · eLife · doi:10.7554/elife.44423 · Cited by 42
Pham, J., Keon, M., Brennan, S. E., & Saksena, N. (2020) · International Journal of Molecular Sciences · doi:10.3390/ijms21103464 · Cited by 45
Mitophagy and Neurodegeneration: Between the Knowns and the Unknowns
Jetto, C. T., Nambiar, A., & Manjithaya, R. R. (2022) · Frontiers in Cell and Developmental Biology · doi:10.3389/fcell.2022.837337 · Cited by 44
The Genetics of C9orf72 ExpansionsPreprint
Gijselinck, I., Cruts, M., & Broeckhoven, C. V. (2017) · Cold Spring Harbor Perspectives in Medicine · doi:10.1101/cshperspect.a026757 · Cited by 43
TDP-43 Proteinopathy Specific Biomarker Development
Cordts, I., Wachinger, A., Scialò, C., Lingor, P., Polymenidou, M., Buratti, E., & Feneberg, E. (2023) · Cells · doi:10.3390/cells12040597 · Cited by 50
The TBK 1‐binding domain of optineurin promotes type I interferon responses
Meena, N. P., Zhu, G., Mittelstadt, P. R., Torchia, M. L. G., Pourcelot, M., Arnoult, D., Ashwell, J. D., & Munitić, I. (2016) · FEBS Letters · doi:10.1002/1873-3468.12176 · Cited by 43
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
Amyotrophic Lateral Sclerosis, a Multisystem Pathology: Insights into the Role of TNF α
Tortarolo, M., Coco, D. L., Veglianese, P., Vallarola, A., Giordana, M. T., Marcon, G., Beghi, E., Poloni, M., Strong, M. J., Iyer, A. M., et al. (2017) · Mediators of Inflammation · doi:10.1155/2017/2985051 · Cited by 43
Genetic screening of ANXA11 revealed novel mutations linked to amyotrophic lateral sclerosis
Teyssou, E., Muratet, F., Amador, M. D. M., Ferrien, M., Lautrette, G., Machat, S., Boillée, S., Larmonier, T., Saker, S., Leguern, É., et al. (2020) · Neurobiology of Aging · doi:10.1016/j.neurobiolaging.2020.10.015 · Cited by 40
Self-citationA 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
Modelling amyotrophic lateral sclerosis in rodents
Todd, T. W., & Petrucelli, L. (2022) · Nature reviews. Neuroscience · doi:10.1038/s41583-022-00564-x · Cited by 44
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 43
Low autophagy capacity implicated in motor system vulnerability to mutant superoxide dismutase
Tokuda, E., Brännström, T., Andersen, P. M., & Marklund, S. L. (2016) · Acta Neuropathologica Communications · doi:10.1186/s40478-016-0274-y · Cited by 44
Self-citationHou, L., Jiao, B., Xiao, T., Zhou, L., Zhou, Z., Du, J., Yan, X., Wang, J., Tang, B., & Shen, L. H. (2016) · Scientific Reports · doi:10.1038/srep32478 · Cited by 41
Neuroinflammation — using big data to inform clinical practice
Dendrou, C. A., McVean, G., & Fugger, L. H. (2016) · Nature Reviews Neurology · doi:10.1038/nrneurol.2016.171 · Cited by 43
Crisafulli, S. G., Brajkovic, S., Mis, M. S. C., Parente, V., & Corti, S. P. (2017) · Molecular Neurobiology · doi:10.1007/s12035-017-0532-4 · Cited by 41
Konopka, A., & Atkin, J. D. (2018) · International Journal of Molecular Sciences · doi:10.3390/ijms19103137 · Cited by 41
Quan, M., Song, X., Liu, H.-J., Deng, X.-H., Hou, H.-Q., Li-ping, C., Ma, T., Han, X., He, X.-X., Jia, Z., et al. (2019) · Journal of Neuroinflammation · doi:10.1186/s12974-019-1438-z · Cited by 42
Mitochondrial Transport and Turnover in the Pathogenesis of Amyotrophic Lateral Sclerosis
Granatiero, V., & Manfredi, G. (2019) · Biology · doi:10.3390/biology8020036 · Cited by 41
Medchalmi, S., Tare, P., Sayyad, Z., & Swarup, G. (2021) · FEBS Journal · doi:10.1111/febs.15752 · Cited by 42
A neurodegenerative disease landscape of rare mutations in Colombia due to founder effects
Acosta‐Uribe, J., Aguillon, D. F., Cochran, J. N., Giraldo, M., Madrigal, L., Killingsworth, B. W., Singhal, R., Labib, S., Alzate, D., Velilla, L. M., et al. (2022) · Genome Medicine · doi:10.1186/s13073-022-01035-9 · Cited by 43
PEX11β and FIS1 cooperate in peroxisome division independently of mitochondrial fission factor
Schrader, T. A., Carmichael, R. E., Islinger, M., Costello, J. L., Hacker, C., Bonekamp, N. A., Weishaupt, J. H., Andersen, P. M., & Schrader, M. (2022) · Journal of Cell Science · doi:10.1242/jcs.259924 · Cited by 39
Self-citationHe, D., Xu, Y. C., Liu, M., & Cui, L. (2023) · Aging and Disease · doi:10.14336/ad.2023.0519 · Cited by 44
Mechanisms of neuronal survival safeguarded by endocytosis and autophagy
Overhoff, M., Bruyckere, E. D., & Kononenko, N. L. (2020) · Journal of Neurochemistry · doi:10.1111/jnc.15194 · Cited by 40
WDR41 supports lysosomal response to changes in amino acid availability
Amick, J., Tharkeshwar, A. K., Amaya, & Ferguson, S. M. (2018) · Molecular Biology of the Cell · doi:10.1091/mbc.e17-12-0703 · Cited by 39
Genetics of movement disorders in the next‐generation sequencing era
Olgiati, S., Quadri, M., & Bonifati, V. (2016) · Movement Disorders · doi:10.1002/mds.26521 · Cited by 43
Amyotrophic lateral sclerosis: recent genetic highlights
White, M. A., & Sreedharan, J. (2016) · Current Opinion in Neurology · doi:10.1097/wco.0000000000000367 · Cited by 40
Lanuza, M. A., Just‐Borràs, L., Hurtado, E., Cilleros‐Mañé, V., Tomàs, M., García, N., & Tomàs, J. M. (2019) · Cells · doi:10.3390/cells8121578 · Cited by 41
Rare Variant Burden Analysis within Enhancers Identifies CAV1 as an ALS Risk Gene
Cooper‐Knock, J., Zhang, S., Kenna, K. P., Moll, T., Franklin, J., Allen, S., Nezhad, H. G., Iacoangeli, A., Yacovzada, N., Eitan, C., et al. (2020) · Cell Reports · doi:10.1016/j.celrep.2020.108456 · Cited by 40
Self-citationApproaches to gene modulation therapy for ALS
Meijboom, K. E., & Brown, R. H. (2022) · Neurotherapeutics · doi:10.1007/s13311-022-01285-w · Cited by 38
Cui, R., Tuo, M., Li, P., & Zhou, C. (2018) · Neurological Sciences · doi:10.1007/s10072-018-3246-0 · Cited by 38
Rosenbohm, A., Nagel, G., Peter, R. S., Brehme, T., Köenig, W., Dupuis, L., Rothenbacher, D., Ludolph, A. C., & for the ALS Registry Study Group (2018) · JAMA Neurology · doi:10.1001/jamaneurol.2017.5129 · Cited by 38
Self-citationFoster, A. D., & Rea, S. L. (2020) · Neural Regeneration Research · doi:10.4103/1673-5374.284977 · Cited by 41
Emerging genetic complexity and rare genetic variants in neurodegenerative brain diseases
Perrone, F., Cacace, R., van der Zee, J., & Broeckhoven, C. V. (2021) · Genome Medicine · doi:10.1186/s13073-021-00878-y · Cited by 38
Genetic inactivation of RIP1 kinase does not ameliorate disease in a mouse model of ALS
Domínguez, S. L., Varfolomeev, E. E., Brendza, R. P., Stark, K., Tea, J. S., Imperio, J., Ngu, H., Earr, T., Foreman, O., Webster, J. D., et al. (2020) · Cell Death and Differentiation · doi:10.1038/s41418-020-00625-7 · Cited by 35
Canonical and Noncanonical Autophagy Pathways in Microglia
Jülg, J., Strohm, L., & Behrends, C. (2020) · Molecular and Cellular Biology · doi:10.1128/mcb.00389-20 · Cited by 40
Baskoylu, S., Chapkis, N., Unsal, B., Lins, J., Schuch, K. N., Simon, J., & Hart, A. C. (2022) · Cell Reports · doi:10.1016/j.celrep.2021.110195 · Cited by 39
Wilke, C., Baets, J., Bleecker, J. D., Deconinck, T., Biskup, S., Hayer, S. N., Zuchner, S. L., Schüle, R., Jonghe, P. D., & Synofzik, M. (2017) · Neurobiology of Aging · doi:10.1016/j.neurobiolaging.2017.10.010 · Cited by 36
Jagaraj, C. J., Parakh, S., & Atkin, J. D. (2021) · Frontiers in Cellular Neuroscience · doi:10.3389/fncel.2020.581950 · Cited by 38
Current Concepts on Genetic Aspects of Mitochondrial Dysfunction in Amyotrophic Lateral Sclerosis
Jankovic, M., Novakovic, I., Gamil Anwar Dawod, P., Gamil Anwar Dawod, A., Drinic, A., Abdel Motaleb, F. I., Ducic, S., & Nikolic, D. (2021) · International Journal of Molecular Sciences · doi:10.3390/ijms22189832 · Cited by 36
The Regulation of Rab GTPases by Phosphorylation
Xu, L., Nagai, Y., Kajihara, Y., Ito, G., & Tomita, T. (2021) · Biomolecules · doi:10.3390/biom11091340 · Cited by 36
Promising Targets for the Treatment of Neurodegenerative Diseases
Haeberlein, S. B., & Harris, T. (2015) · Clinical Pharmacology & Therapeutics · doi:10.1002/cpt.195 · Cited by 35
Strong, M. J. (2017) · Current Opinion in Neurology · doi:10.1097/wco.0000000000000488 · Cited by 37
Lattante, S., Doronzio, P. N., Marangi, G., Conte, A., Bisogni, G., Bernardo, D., Russo, T., Lamberti, D., Patrizi, S. T., Apollo, F., et al. (2019) · Neurobiology of Aging · doi:10.1016/j.neurobiolaging.2019.03.010 · Cited by 36
Koşukçu, C., Taşkıran, E. Z., Batu, E. D., Sağ, E., Bilginer, Y., Alikaşifoğlu, M., & Özen, S. (2020) · Rheumatology · doi:10.1093/rheumatology/keaa165 · Cited by 33
Selective Neuron Vulnerability in Common and Rare Diseases—Mitochondria in the Focus
Paß, T., Wiesner, R. J., & Pla‐Martín, D. (2021) · Frontiers in Molecular Biosciences · doi:10.3389/fmolb.2021.676187 · Cited by 37
Autophagy Dysfunction in ALS: from Transport to Protein Degradation
Cozzi, M., & Ferrari, V. (2022) · Journal of Molecular Neuroscience · doi:10.1007/s12031-022-02029-3 · Cited by 38
Wei, Q., Zhou, Q., Chen, Y., Ou, R., Cao, B., Xu, Y., Yang, J., & Shang, H. (2017) · Scientific Reports · doi:10.1038/srep44606 · Cited by 37
Gossye, H., Van Broeckhoven, C., & Engelborghs, S. (2019) · Frontiers in Neuroscience · doi:10.3389/fnins.2019.00757 · Cited by 34
Control of mRNA Translation in ALS Proteinopathy
Cestra, G., Rossi, S., Salvio, M. D., & Cozzolino, M. (2017) · Frontiers in Molecular Neuroscience · doi:10.3389/fnmol.2017.00085 · Cited by 36
Recent advances in the molecular genetics of frontotemporal lobar degeneration
Rainero, I. (2017) · Functional Neurology · doi:10.11138/fneur/2017.32.1.007 · Cited by 34
Zhu, X., Padmanabhan, R., Copeland, B. R., Bridgers, J., Ren, Z., Kamalakaran, S., O’Driscoll-Collins, A., Berkovic, S. F., Scheffer, I. E., Poduri, A., et al. (2017) · PLoS Genetics · doi:10.1371/journal.pgen.1007104 · Cited by 35
Network approach identifies Pacer as an autophagy protein involved in ALS pathogenesis
Beltrán, S., Nassif, M., Vicencio, E., Arcos, J., Labrador, L., Cortés, B. I., Cortéz, C., Bergmann, C. A., Espinoza, S., Hernandez, M. F., et al. (2019) · Molecular Neurodegeneration · doi:10.1186/s13024-019-0313-9 · Cited by 35
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
Mitophagy regulation in aging and neurodegenerative disease
Banarase, T. A., Sammeta, S. S., Wankhede, N. L., Mangrulkar, S. V., Rahangdale, S. R., Aglawe, M. M., Taksande, B. G., Upaganlawar, A. B., Umekar, M. J., & Kale, M. B. (2023) · Biophysical Reviews · doi:10.1007/s12551-023-01057-6 · Cited by 35
Parkinsonism in frontotemporal dementias
Rowe, J. B. (2019) · International review of neurobiology · doi:10.1016/bs.irn.2019.10.012 · Cited by 35
Drewry, D. H., Annor‐Gyamfi, J. K., Wells, C. I., Pickett, J. E., Dederer, V., Preuß, F., Mathea, S., & Axtman, A. D. (2021) · Journal of Medicinal Chemistry · doi:10.1021/acs.jmedchem.1c00440 · Cited by 33
Anoar, S., Woodling, N. S., & Niccoli, T. (2021) · Frontiers in Neuroscience · doi:10.3389/fnins.2021.786076 · Cited by 37
Sreedharan, J., Blakeney, I., & Brown, R. H. (2020) · Elsevier eBooks · doi:10.1016/b978-0-12-813866-3.00020-5 · Cited by 32
Mitochondria: A Promising Convergent Target for the Treatment of Amyotrophic Lateral Sclerosis
Cunha‐Oliveira, T., Montezinho, L., Simões, R. F., de Carvalho, M., Ferreiro, E. B., & Silva, F. S. G. (2024) · Cells · doi:10.3390/cells13030248 · Cited by 33
Divergence, Convergence, and Therapeutic Implications: A Cell Biology Perspective of C9ORF72-ALS/FTD
Tang, X., Toro, A., Sahana, T. G., Gao, J., Chalk, J. L., Oskarsson, B., & Zhang, K. (2020) · Molecular Neurodegeneration · doi:10.1186/s13024-020-00383-7 · Cited by 34
DeLoach, A., Cozart, M. A., Kiaei, A., & Kiaei, M. (2015) · Expert Opinion on Drug Discovery · doi:10.1517/17460441.2015.1067197 · Cited by 36
New ALS‐Related Genes Expand the Spectrum Paradigm of Amyotrophic Lateral Sclerosis
Sabatelli, M., Marangi, G., Conte, A., Tasca, G. A., Zollino, M., & Lattante, S. (2016) · Brain Pathology · doi:10.1111/bpa.12354 · Cited by 32
A Clinical Guide to Frontotemporal Dementias
Ljubenkov, P. A., & Miller, B. L. (2016) · FOCUS The Journal of Lifelong Learning in Psychiatry · doi:10.1176/appi.focus.20160018 · Cited by 36
Genetics and genetic testing for glaucoma
Miller, M., Fingert, J. H., & Bettis, D. I. (2016) · Current Opinion in Ophthalmology · doi:10.1097/icu.0000000000000344 · Cited by 31
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 in ageing and ageing-related neurodegenerative diseases
Karabiyik, C., Frake, R. A., Park, S. J., Tanasa, M. P., & Rubinsztein, D. C. (2021) · Ageing and Neurodegenerative Diseases · doi:10.20517/and.2021.05 · Cited by 31
Mechanistic Insights into Selective Autophagy Subtypes in Alzheimer’s Disease
Guan, X., Iyaswamy, A., Sreenivasmurthy, S. G., Su, C.-F., Zhu, Z., Liu, J., Kan, Y., Cheung, K., Lu, J., Tan, J., et al. (2022) · International Journal of Molecular Sciences · doi:10.3390/ijms23073609 · Cited by 32
Diab, R., Pilotto, F., & Saxena, S. (2023) · Frontiers in Cellular Neuroscience · doi:10.3389/fncel.2023.1086895 · Cited by 35
Caroppo, P., Camuzat, A., de Septenville, A. L., Couratier, P., Lacomblez, L., Auriacombe, S., Flabeau, O., Jornéa, L., Blanc, F., Sellal, F., et al. (2015) · Alzheimer s & Dementia Diagnosis Assessment & Disease Monitoring · doi:10.1016/j.dadm.2015.10.002 · Cited by 33
Casterton, R., Hunt, R. J., & Fanto, M. (2020) · Journal of Molecular Biology · doi:10.1016/j.jmb.2020.02.018 · Cited by 34
Das, S., Murumulla, L., Ghosh, P., & Challa, S. (2025) · BioMetals · doi:10.1007/s10534-025-00665-x · Cited by 30
Recent advances in understanding frontotemporal degeneration
Borroni, B., & Benussi, A. (2019) · F1000Research · doi:10.12688/f1000research.20330.1 · Cited by 30
Papendorf, J. J., Krüger, E., & Ebstein, F. (2022) · Cells · doi:10.3390/cells11091422 · Cited by 34
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
SQSTM1/p62 variants in 486 patients with familial ALS from Germany and Sweden
Yilmaz, R., Müller, K., Brenner, D., Volk, A. E., Borck, G., Hermann, A., Meitinger, T., Strom, T. M., Danzer, K. M., Ludolph, A. C., et al. (2019) · Neurobiology of Aging · doi:10.1016/j.neurobiolaging.2019.10.018 · Cited by 30
Self-citationBiological Spectrum of Amyotrophic Lateral Sclerosis PrionsPreprint
Polymenidou, M., & Cleveland, D. W. (2017) · Cold Spring Harbor Perspectives in Medicine · doi:10.1101/cshperspect.a024133 · Cited by 29
Neurodegenerative diseases have genetic hallmarks of autoinflammatory disease
Richards, R. I., Robertson, S. A., & Kastner, D. L. (2018) · Human Molecular Genetics · doi:10.1093/hmg/ddy139 · Cited by 27
Hirsch‐Reinshagen, V., Alfaify, O. A., Hsiung, G. R., Pottier, C. P., Baker, M. C., Perkerson, R. B., Rademakers, R., Briemberg, H., Foti, D. J., & Mackenzie, I. R. (2019) · Amyotrophic Lateral Sclerosis and Frontotemporal Degeneration · doi:10.1080/21678421.2019.1632347 · Cited by 30
New insights on the disease contribution of neuroinflammation in amyotrophic lateral sclerosis
Chiot, A., Lobsiger, C. S., & Boillée, S. (2019) · Current Opinion in Neurology · doi:10.1097/wco.0000000000000729 · Cited by 34
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
Hemizygous deletion of Tbk1 worsens neuromuscular junction pathology in TDP-43 transgenic mice
Sieverding, K., Ulmer, J., Bruno, C., Satoh, T., Tsao, W., Freischmidt, A., Akira, S., Wong, P. C., Ludolph, A. C., Danzer, K. M., et al. (2020) · Experimental Neurology · doi:10.1016/j.expneurol.2020.113496 · Cited by 30
Self-citationPathological phase transitions in ALS-FTD impair dynamic RNA–protein granules
Nedelsky, N. B., & Taylor, J. P. (2021) · RNA · doi:10.1261/rna.079001.121 · Cited by 31
Mutation Screening of the CHCHD10 Gene in Chinese Patients with Amyotrophic Lateral Sclerosis
Zhou, Q., Chen, Y., Wei, Q., Cao, B., Wu, Y., Zhao, B., Ou, R., Yang, J., Chen, X., Hadano, S., et al. (2016) · Molecular Neurobiology · doi:10.1007/s12035-016-9888-0 · Cited by 29
PTK2B promotes TBK1 and STING oligomerization and enhances the STING-TBK1 signaling
Lin, Y., Yang, J., Yang, Q., Zeng, S., Zhang, J., Zhu, Y., Tong, Y., Li, L., Tan, W., Chen, D., et al. (2023) · Nature Communications · doi:10.1038/s41467-023-43419-4 · Cited by 28
Kumar, V., Islam, A., Hassan, M. I., & Ahmad, F. (2016) · Biochimica et Biophysica Acta (BBA) - Molecular Basis of Disease · doi:10.1016/j.bbadis.2016.06.011 · Cited by 29
A novel neurodegenerative spectrum disorder in patients with MLKL deficiency
Faergeman, S. L., Evans, H. G., Attfield, K. E., Desel, C., Kuttikkatte, S. B., Sommerlund, M., Jensen, L. T., Frøkiær, J., Friese, M. A., Matthews, P. M., et al. (2020) · Cell Death and Disease · doi:10.1038/s41419-020-2494-0 · Cited by 28
Benson, B. C., Shaw, P. J., Azzouz, M., Highley, J. R., & Hautbergue, G. M. (2021) · Frontiers in Neuroscience · doi:10.3389/fnins.2021.783624 · Cited by 30
Davidson, J. M., Chung, R. S., & Lee, A. (2022) · Neurobiology of Disease · doi:10.1016/j.nbd.2022.105653 · Cited by 29
Myotubularin-related phosphatase 5 is a critical determinant of autophagy in neurons
Chua, J. P., Bedi, K., Paulsen, M. T., Ljungman, M. E., Tank, E. M. H., Kim, E. S., McBride, J. P., Colon, J., Ward, M. E., Weisman, L. S., et al. (2022) · Current Biology · doi:10.1016/j.cub.2022.04.053 · Cited by 28
Neuroinflammatory Pathways in the ALS-FTD Continuum: A Focus on Genetic Variants
Marchi, F. D., Tondo, G., Corrado, L., Menegon, F., Aprile, D., Anselmi, M., D’Alfonso, S., Comi, C., & Mazzini, L. (2023) · Genes · doi:10.3390/genes14081658 · Cited by 31
Almeida, S., Gao, F., Coppola, G., & Gao, F. (2016) · Neurobiology of Aging · doi:10.1016/j.neurobiolaging.2016.03.001 · Cited by 28
Optineurin Functions for Optimal Immunity
Slowicka, K., & Loo, G. (2018) · Frontiers in Immunology · doi:10.3389/fimmu.2018.00769 · Cited by 32
The Microglial Response to Neurodegenerative Disease
Song, W. M., & Colonna, M. (2018) · Advances in immunology · doi:10.1016/bs.ai.2018.04.002 · Cited by 30
A novel TBK1 mutation in a family with diverse frontotemporal dementia spectrum disordersPreprint
Lamb, R., Rohrer, J. D., Real, R., Lubbe, S. J., Waite, A. J., Blake, D. J., Walters, R. J., Lashley, T., Révész, T., Holton, J. L., et al. (2019) · Molecular Case Studies · doi:10.1101/mcs.a003913 · Cited by 31
Fu, Y., Zhang, J., Qin, R., Ren, Y., Zhou, T., Han, B., & Liu, B. (2025) · Pharmacological Reviews · doi:10.1016/j.pharmr.2025.100053 · Cited by 29
Exome sequencing uncovers hidden pathways in familial and sporadic ALS
Bettencourt, C., & Houlden, H. (2015) · Nature Neuroscience · doi:10.1038/nn.4012 · Cited by 29
Metadata
- Authors
- Freischmidt, A., Wieland, T., Richter, B., Ruf, W., Schaeffer, V., Müller, K., Marroquin, N., Nordin, F., Hübers, A., Weydt, P., Pinto, S., Press, R., Millecamps, S., Molko, N., Bernard, E., Desnuelle, C., Soriani, M.-H., Dorst, J., Graf, E., Nordström, U., Feiler, M. S., Putz, S., Boeckers, T. M., Meyer, T., Winkler, A. S., Winkelman, J., de Carvalho, M., Thal, D. R., Otto, M., Brännström, T., Volk, A. E., Kursula, P., Danzer, K. M., Lichtner, P., Dikic, I., Meitinger, T., Ludolph, A. C., Strom, T. M., Andersen, P. M., & Weishaupt, J. H.
- Affiliations
- Universität Ulm (DE)
- Helmholtz Munich (DE)
- Goethe University Frankfurt (DE)
- Umeå University (SE)
- University of Lisbon (PT)
- Karolinska University Hospital (SE)
- Centre National de la Recherche Scientifique (FR)
- Centre Hospitalier Territorial de Nouvelle-Calédonie (NC)
- Hôpital Pierre Wertheimer (FR)
- Centre Hospitalier Universitaire de Nice (FR)
- Humboldt-Universität zu Berlin (DE)
- Technical University of Munich (DE)
- University of Bergen (NO)
- Corresponding author
- Andersen, Peter M
- Weishaupt, Jochen H
- ORCID
- Freischmidt, Axel
- Wieland, Thomas
- Richter, Benjamin
- Ruf, Wolfgang
- Müller, Kathrin
- Marroquin, Nicolai
- Hübers, Annemarie
- Weydt, Patrick
- Pinto, Susana
- Millecamps, Stéphanie
- Bernard, Emilien
- Desnuelle, Claude
- Dorst, Johannes
- Graf, Elisabeth
- Nordström, Ulrika
- Boeckers, Tobias M
- Meyer, Thomas
- Winkler, Andrea S
- Thal, Dietmar R
- Otto, Markus
- Brännström, Thomas
- Volk, Alexander E
- Kursula, Petri
- Danzer, Karin M
- Lichtner, Peter
- Meitinger, Thomas
- Ludolph, Albert C
- Andersen, Peter M
- Weishaupt, Jochen H
- Venue
- Nature Neuroscience
- Published
- 2015-03-24
- Volume
- 18
- Issue
- 5
- Pages
- 631-636
- ISSN
- 1097-6256 (ISSN-L)
- 1546-1726
- OpenAlex
- W2156054547
- Cited by
- 786
- References
- 35
- Citations by year
- 2026: 29 · 2025: 50 · 2024: 48 · 2023: 47 · 2022: 69 · 2021: 75 · 2020: 100 · 2019: 79 · 2018: 88 · 2017: 78 · 2016: 89 · 2015: 32
- FWCI
- 67.45
- Type
- journal article
- Language
- en
- Open access
- green
- lirias.kuleuven.be
- Licence
- Locations
- Nature Neuroscience (publishedVersion)
- PubMed (publishedVersion)
- Lirias (KU Leuven) (submittedVersion, other-oa)
- HAL (submittedVersion, other-oa)
- mediaTUM – the media and publications repository of the Technical University Munich (Technical University Munich) (submittedVersion)
- Site cant be reached (submittedVersion)
- PuSH - Publication Server of Helmholtz Zentrum München (submittedVersion)
- Portuguese National Funding Agency for Science, Research and Technology (RCAAP Project by FCT) (submittedVersion)
- Funders
- Brain Research Foundation
- Ulla-Carin Lindquists stiftelse för ALS-forskning
- Bundesministerium für Bildung und Forschung (01GI0704)
- Knut och Alice Wallenbergs Stiftelse
- Vetenskapsrådet
- Fondation Charcot
- Bertil Hållstens Forskningsstiftelse
- Swedish Brain Power
- German Network for Motor Neuron Diseases
- Topics
- Health Sciences › Medicine › Clinical Neurology › Amyotrophic Lateral Sclerosis Research
- Life Sciences › Neuroscience › Cellular and Molecular Neuroscience › Hereditary Neurological Disorders
- Life Sciences › Neuroscience › Cellular and Molecular Neuroscience › Alzheimer's disease research and treatments
- Keywords
- TBK1, haploinsufficiency, familial ALS, frontotemporal dementia, optineurin, loss-of-function mutations, coiled-coil domain, autophagy, neuroinflammation, neurodegeneration, genetic linkage, motor neuron degeneration
- MeSH terms
- Alleles, Amyotrophic Lateral Sclerosis, Cells, Cultured, DNA Mutational Analysis, Europe, Female, Gene Frequency, Humans, Male, Pedigree, Protein Serine-Threonine Kinases, Sequence Analysis, DNA, Protein Structure, Tertiary, Codon, Nonsense, Genetic Heterogeneity, Cell Cycle Proteins, Mutation, Missense, Membrane Transport Proteins, Transcription Factor TFIIIA, Genome-Wide Association Study, Frontotemporal Dementia, Exome
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
