Cited by 459

The DOI matches its Crossref record; 63 of the 63 references it cites were found in a registry or an index.

The inhibition of TDP-43 mitochondrial localization blocks its neuronal toxicity

Open access

Wang, Wenzhang, Wang, Luwen, Lu, Junjie, Siedlak, Sandra L, Fujioka, Hisashi, Liang, Jingjing, Jiang, Sirui, Ma, Xiaopin, Jiang, Zhen, da Rocha, Edroaldo Lummertz, Sheng, Max, Choi, Heewon, Lerou, Paul H, Li, Hu, Wang, Xinglong·2016·Nature Medicine

DOI 10.1038/nm.4130

Open this paper in CoChat — free account

Abstract

Genetic mutations in TAR DNA-binding protein 43 (TARDBP, also known as TDP-43) cause amyotrophic lateral sclerosis (ALS), and an increase in the presence of TDP-43 (encoded by TARDBP) in the cytoplasm is a prominent histopathological feature of degenerating neurons in various neurodegenerative diseases. However, the molecular mechanisms by which TDP-43 contributes to ALS pathophysiology remain elusive. Here we have found that TDP-43 accumulates in the mitochondria of neurons in subjects with ALS or frontotemporal dementia (FTD). Disease-associated mutations increase TDP-43 mitochondrial localization. In mitochondria, wild-type (WT) and mutant TDP-43 preferentially bind mitochondria-transcribed messenger RNAs (mRNAs) encoding respiratory complex I subunits ND3 and ND6, impair their expression and specifically cause complex I disassembly. The suppression of TDP-43 mitochondrial localization abolishes WT and mutant TDP-43-induced mitochondrial dysfunction and neuronal loss, and improves phenotypes of transgenic mutant TDP-43 mice. Thus, our studies link TDP-43 toxicity directly to mitochondrial bioenergetics and propose the targeting of TDP-43 mitochondrial localization as a promising therapeutic approach for neurodegeneration.

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

Crossref · 10.1038/nm.4130

Cites

63 of 63 references verified0 citation errors · 0 not checkable

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.

Self-check

Percentages, sums and reported differences re-computed from the paper’s own numbers.

The self-check needs the paper’s full text.

Ubiquitinated TDP-43 in Frontotemporal Lobar Degeneration and Amyotrophic Lateral Sclerosis
Neumann, M., Sampathu, D. M., Kwong, L. K., Truax, A. C., Micsenyi, M. C., Chou, T. T., Bruce, J., Schuck, T., Grossman, M., Clark, C. M., et al. (2006) · Science · doi:10.1126/science.1134108 · Cited by 6,576
Locating proteins in the cell using TargetP, SignalP and related tools
Emanuelsson, O., Brunak, S., von Heijne, G., & Nielsen, H. (2007) · Nature Protocols · doi:10.1038/nprot.2007.131 · Cited by 3,188
TDP-43 Mutations in Familial and Sporadic Amyotrophic Lateral Sclerosis
Sreedharan, J., Blair, I. P., Tripathi, V. B., Hu, X., Vance, C., Rogelj, B., Ackerley, S., Durnall, J. C., Williams, K. L., Buratti, E., et al. (2008) · Science · doi:10.1126/science.1154584 · Cited by 2,630
THE MITOCHONDRIAL DEATH/LIFE REGULATOR IN APOPTOSIS AND NECROSIS
Kroemer, G., Dallaporta, B., & Resche-Rigon, M. (1998) · Annual Review of Physiology · doi:10.1146/annurev.physiol.60.1.619 · Cited by 1,963
Culturing hippocampal neurons
Kaech, S., & Banker, G. (2006) · Nature Protocols · doi:10.1038/nprot.2006.356 · Cited by 1,659
Computational Method to Predict Mitochondrially Imported Proteins and their Targeting Sequences
Claros, M. G., & Vincens, P. (1996) · European Journal of Biochemistry · doi:10.1111/j.1432-1033.1996.00779.x · Cited by 1,643
TARDBP mutations in individuals with sporadic and familial amyotrophic lateral sclerosis
Kabashi, E., Valdmanis, P. N., Dion, P., Spiegelman, D., McConkey, B. J., Velde, C. V., Bouchard, J.-P., Lacomblez, L., Pochigaeva, K., Salachas, F., et al. (2008) · Nature Genetics · doi:10.1038/ng.132 · Cited by 1,544
Long pre-mRNA depletion and RNA missplicing contribute to neuronal vulnerability from loss of TDP-43
Polymenidou, M., Lagier-Tourenne, C., Hutt, K. R., Huelga, S. C., Moran, J., Liang, T. Y., Ling, S.-C., Sun, E., Wancewicz, E., Mazur, C., et al. (2011) · Nature Neuroscience · doi:10.1038/nn.2779 · Cited by 1,335
Mitochondrial cristae shape determines respiratory chain supercomplexes assembly and respiratory efficiency
Cogliati, S., Frezza, C., Soriano, M. E., Varanita, T., Quintana-Cabrera, R., Corrado, M., Cipolat, S., Costa, V., Casarin, A., Gomes, L. C., et al. (2013) · Cell · doi:10.1016/j.cell.2013.08.032 · Cited by 1,265
Impaired Balance of Mitochondrial Fission and Fusion in Alzheimer's Disease
Wang, X., Su, B., Lee, H.-G., Li, X., Perry, G., Smith, M. A., & Zhu, X. (2009) · Journal of Neuroscience · doi:10.1523/jneurosci.1357-09.2009 · Cited by 1,224
Self-citation
Characterizing the RNA targets and position-dependent splicing regulation by TDP-43
Tollervey, J. R., Curk, T., Rogelj, B., Briese, M., Cereda, M., Kayikci, M., König, J., Hortobágyi, T., Nishimura, A. L., Župunski, V., et al. (2011) · Nature Neuroscience · doi:10.1038/nn.2778 · Cited by 1,165
Culturing hippocampal neurons.
TANAKA, H. (2002) · Folia Pharmacologica Japonica · doi:10.1254/fpj.119.163 · Cited by 1,126
TDP-43 and FUS in amyotrophic lateral sclerosis and frontotemporal dementia
Mackenzie, I. R., Rademakers, R., & Neumann, M. (2010) · The Lancet Neurology · doi:10.1016/s1474-4422(10)70195-2 · Cited by 975
TDP‐43 immunoreactivity in hippocampal sclerosis and Alzheimer's disease
Amador‐Ortiz, C., Lin, W., Ahmed, Z., Personett, D., Davies, P., Duara, R., Graff‐Radford, N. R., Hutton, M. L., & Dickson, D. W. (2007) · Annals of Neurology · doi:10.1002/ana.21154 · Cited by 916
Amyloid-β overproduction causes abnormal mitochondrial dynamics via differential modulation of mitochondrial fission/fusion proteins
Wang, X., Su, B., Siedlak, S. L., Moreira, P. I., Fujioka, H., Wang, Y., Casadesus, G., & Zhu, X. (2008) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.0804871105 · Cited by 835
Self-citation
Human iPSC-based modeling of late-onset disease via progerin-induced aging
Miller, J. D., Ganat, Y. M., Kishinevsky, S., Bowman, R. L., Liu, B., Tu, E. Y., Mandal, P. K., Vera, E., Shim, J.-W., Kriks, S., et al. (2013) · Cell stem cell · doi:10.1016/j.stem.2013.11.006 · Cited by 777
Phosphorylated TDP‐43 in frontotemporal lobar degeneration and amyotrophic lateral sclerosis
Hasegawa, M., Arai, T., Nonaka, T., Kametani, F., Yoshida, M., Hashizume, Y., Beach, T. G., Buratti, E., Baralle, F., Morita, M., et al. (2008) · Annals of Neurology · doi:10.1002/ana.21425 · Cited by 777
Mitochondrial protein import: from proteomics to functional mechanisms
Schmidt, O., Pfanner, N., & Meisinger, C. (2010) · Nature Reviews Molecular Cell Biology · doi:10.1038/nrm2959 · Cited by 717
TDP-43 mutant transgenic mice develop features of ALS and frontotemporal lobar degeneration
Wegorzewska, I., Bell, S., Cairns, N. J., Miller, T. M., & Baloh, R. H. (2009) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.0908767106 · Cited by 706
The amyloid β-peptide is imported into mitochondria via the TOM import machinery and localized to mitochondrial cristae
Hansson Petersen, C. A., Alikhani, N., Behbahani, H., Wiehager, B., Pavlov, P. F., Alafuzoff, I., Leinonen, V., Ito, A., Winblad, B., Glaser, E., et al. (2008) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.0806192105 · Cited by 693
Gains or losses: molecular mechanisms of TDP43-mediated neurodegeneration
Lee, E. B., Lee, V. M.-Y., & Trojanowski, J. Q. (2012) · Nature Reviews Neuroscience · doi:10.1038/nrn3121 · Cited by 659
RNA recognition motifs: boring? Not quite
Cléry, A., Blatter, M., & Allain, F. H.-T. (2008) · Current Opinion in Structural Biology · doi:10.1016/j.sbi.2008.04.002 · Cited by 635
The phenotypic variability of amyotrophic lateral sclerosis
Swinnen, B., & Robberecht, W. (2014) · Nature Reviews Neurology · doi:10.1038/nrneurol.2014.184 · Cited by 603
Necroptosis: A Specialized Pathway of Programmed Necrosis
Galluzzi, L., & Kroemer, G. (2008) · Cell · doi:10.1016/j.cell.2008.12.004 · Cited by 561
Wild-Type Human TDP-43 Expression Causes TDP-43 Phosphorylation, Mitochondrial Aggregation, Motor Deficits, and Early Mortality in Transgenic Mice
Xu, Y.-F., Gendron, T. F., Zhang, Y.-J., Lin, W.-L., D'Alton, S., Sheng, H., Casey, M. C., Tong, J., Knight, J., Yu, X., et al. (2010) · The Journal of Neuroscience · doi:10.1523/jneurosci.1630-10.2010 · Cited by 555
Cytoplasmic Mislocalization of TDP-43 Is Toxic to Neurons and Enhanced by a Mutation Associated with Familial Amyotrophic Lateral Sclerosis
Barmada, S. J., Skibinski, G., Korb, E., Rao, E. J., Wu, J. Y., & Finkbeiner, S. (2010) · The Journal of Neuroscience · doi:10.1523/jneurosci.4988-09.2010 · Cited by 554
ALS-linked TDP-43 mutations produce aberrant RNA splicing and adult-onset motor neuron disease without aggregation or loss of nuclear TDP-43
Arnold, E. S., Ling, S.-C., Huelga, S. C., Lagier-Tourenne, C., Polymenidou, M., Ditsworth, D., Kordasiewicz, H. B., McAlonis-Downes, M., Platoshyn, O., Parone, P. A., et al. (2013) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.1222809110 · Cited by 492
Multiple roles of TDP-43 in gene expression, splicing regulation, and human disease
Buratti, E. (2008) · Frontiers in Bioscience · doi:10.2741/2727 · Cited by 491
Identification of Neuronal RNA Targets of TDP-43-containing Ribonucleoprotein Complexes
Sephton, C. F., Cenik, C., Kucukural, A., Dammer, E. B., Cenik, B., Han, Y., Dewey, C. M., Roth, F. P., Herz, J., Peng, J., et al. (2011) · Journal of Biological Chemistry · doi:10.1074/jbc.m110.190884 · Cited by 434
Advances in understanding the molecular basis of frontotemporal dementia
Rademakers, R., Neumann, M., & Mackenzie, I. R. (2012) · Nature Reviews Neurology · doi:10.1038/nrneurol.2012.117 · Cited by 412
Biochemical Assays of Respiratory Chain Complex Activity
Kirby, D. M., Thorburn, D. R., Turnbull, D. M., & Taylor, R. W. (2007) · Methods in Cell Biology · doi:10.1016/s0091-679x(06)80004-x · Cited by 384
Activation of p38 Kinase Links Tau Phosphorylation, Oxidative Stress, and Cell Cycle-Related Events in Alzheimer Disease
Zhu, X., Rottkamp, C. A., Boux, H., Takeda, A., Perry, G., & Smith, M. A. (2000) · Journal of Neuropathology & Experimental Neurology · doi:10.1093/jnen/59.10.880 · Cited by 378
Staging TDP-43 pathology in Alzheimer’s disease
Josephs, K. A., Murray, M. E., Whitwell, J. L., Parisi, J. E., Petrucelli, L., Jack, C. R., Petersen, R. C., & Dickson, D. W. (2014) · Acta Neuropathologica · doi:10.1007/s00401-013-1211-9 · Cited by 366
Dynamin-Like Protein 1 Reduction Underlies Mitochondrial Morphology and Distribution Abnormalities in Fibroblasts from Sporadic Alzheimer's Disease Patients
Wang, X., Su, B., Fujioka, H., & Zhu, X. (2008) · The American Journal of Pathology · doi:10.2353/ajpath.2008.071208 · Cited by 341
Self-citation
The ALS disease-associated mutant TDP-43 impairs mitochondrial dynamics and function in motor neurons
Wang, W., Li, L., Lin, W.-L., Dickson, D. W., Petrucelli, L., Zhang, T., & Wang, X. (2013) · Human Molecular Genetics · doi:10.1093/hmg/ddt319 · Cited by 338
Self-citation
Abnormal mitochondrial transport and morphology are common pathological denominators in SOD1 and TDP43 ALS mouse models
Magrané, J., Cortez, C., Gan, W.-B., & Manfredi, G. (2014) · Human Molecular Genetics · doi:10.1093/hmg/ddt528 · Cited by 333
Multiple pathways for sorting mitochondrial precursor proteins
Bolender, N., Sickmann, A., Wagner, R., Meisinger, C., & Pfanner, N. (2008) · EMBO reports · doi:10.1038/sj.embor.7401126 · Cited by 322
The Human Brain in a Dish: The Promise of iPSC-Derived Neurons
Dolmetsch, R., & Geschwind, D. H. (2011) · Cell · doi:10.1016/j.cell.2011.05.034 · Cited by 304
A Stable Lead by Modification of Sato's Method
(1986) · Journal of Electron Microscopy · doi:10.1093/oxfordjournals.jmicro.a050582 · Cited by 252
Bioenergetic analysis of isolated cerebrocortical nerve terminals on a microgram scale: spare respiratory capacity and stochastic mitochondrial failure
Choi, S. W., Gerencser, A. A., & Nicholls, D. G. (2009) · Journal of Neurochemistry · doi:10.1111/j.1471-4159.2009.06055.x · Cited by 203
TDP-43: gumming up neurons through protein–protein and protein–RNA interactions
Buratti, E., & Baralle, F. E. (2012) · Trends in Biochemical Sciences · doi:10.1016/j.tibs.2012.03.003 · Cited by 194
Pink1 regulates the oxidative phosphorylation machinery via mitochondrial fission
Liu, W., Acín-Peréz, R., Geghman, K. D., Manfredi, G., Lu, B., & Li, C. (2011) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.1107332108 · Cited by 190
Partial loss of TDP-43 function causes phenotypes of amyotrophic lateral sclerosis
Yang, C., Wang, H., Qiao, T., Yang, B., Aliaga, L., Qiu, L., Tan, W., Salameh, J., McKenna-Yasek, D. M., Smith, T., et al. (2014) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.1322641111 · Cited by 185
De novo mutations in the mitochondrial ND3 gene as a cause of infantile mitochondrial encephalopathy and complex I deficiency
McFarland, R., Kirby, D. M., Fowler, K. J., Ohtake, A., Ryan, M. T., Amor, D. J., Fletcher, J. M., Dixon, J. W., Collins, F. A., Turnbull, D. M., et al. (2004) · Annals of Neurology · doi:10.1002/ana.10787 · Cited by 180
Expression of mutant TDP-43 induces neuronal dysfunction in transgenic mice
Xu, Y.-F., Zhang, Y.-J., Lin, W.-L., Cao, X., Stetler, C., Dickson, D. W., Lewis, J., & Petrucelli, L. (2011) · Molecular Neurodegeneration · doi:10.1186/1750-1326-6-73 · Cited by 178
The mitochondrial ND6 gene is a hot spot for mutations that cause Leber's hereditary optic neuropathy
Chinnery, P. F., Brown, D. T., Andrews, R. M., Singh-Kler, R., Riordan-Eva, P., Lindley, J., Applegarth, D. A., Turnbull, D. M., & Howell, N. (2001) · Brain · doi:10.1093/brain/124.1.209 · Cited by 169
Targeted Depletion of TDP-43 Expression in the Spinal Cord Motor Neurons Leads to the Development of Amyotrophic Lateral Sclerosis-like Phenotypes in Mice
Wu, L.-S., Cheng, W.-C., & Shen, C.-K. J. (2012) · Journal of Biological Chemistry · doi:10.1074/jbc.m112.359000 · Cited by 159
Organization of the mitochondrial translation machinery studied in situ by cryoelectron tomography
Pfeffer, S., Woellhaf, M. W., Herrmann, J. M., & Förster, F. G. (2015) · Nature Communications · doi:10.1038/ncomms7019 · Cited by 146
Maturation process of TDP-43-positive neuronal cytoplasmic inclusions in amyotrophic lateral sclerosis with and without dementia
Mori, F., Tanji, K., Zhang, H., Nishihira, Y., Tan, C., Takahashi, H., & Wakabayashi, K. (2008) · Acta Neuropathologica · doi:10.1007/s00401-008-0396-9 · Cited by 135
Design and Structure of Peptide and Peptidomimetic Antagonists of Protein- Protein Interaction
Sillerud, L. O., & Larson, R. A. (2005) · Current Protein and Peptide Science · doi:10.2174/1389203053545462 · Cited by 129
A rotarod suitable for quantitative measurements of motor incoordination in naive mice
Jones, B. J., & Roberts, D. J. (1968) · Naunyn-Schmiedeberg s Archives of Pharmacology · doi:10.1007/bf00537801 · Cited by 117
C57BL/6J congenic Prp-TDP43A315T mice develop progressive neurodegeneration in the myenteric plexus of the colon without exhibiting key features of ALS
Hatzipetros, T., Bogdanik, L. P., Tassinari, V. R., Kidd, J. D., Moreno, A. J., Davis, C., Osborne, M. A., Austin, A., Vieira, F. G., Lutz, C. M., et al. (2013) · Brain Research · doi:10.1016/j.brainres.2013.10.013 · Cited by 113
Prevention of intestinal obstruction reveals progressive neurodegeneration in mutant TDP-43 (A315T)mice
Herdewyn, S., Cirillo, C., Bosch, L. V. D., Robberecht, W., Berghe, P. V., & Damme, P. V. (2014) · Molecular Neurodegeneration · doi:10.1186/1750-1326-9-24 · Cited by 94
Identification of RNA bound to the TDP-43 ribonucleoprotein complex in the adult mouse brain
Narayanan, R. K., Mangelsdorf, M., Panwar, A., Butler, T. J., Noakes, P. G., & Wallace, R. H. (2012) · Amyotrophic Lateral Sclerosis and Frontotemporal Degeneration · doi:10.3109/21678421.2012.734520 · Cited by 89
Disease causing mutants of TDP-43 nucleic acid binding domains are resistant to aggregation and have increased stability and half-life
Austin, J. A., Wright, G. S. A., Watanabe, S., Grossmann, J. G., Antonyuk, S. V., Yamanaka, K., & Hasnain, S. S. (2014) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.1317317111 · Cited by 89
Severe subcortical TDP-43 pathology in sporadic frontotemporal lobar degeneration with motor neuron disease
Brandmeir, N. J., Geser, F., Kwong, L. K., Zimmerman, E. A., Qian, J., Lee, V. M. ‐., & Trojanowski, J. Q. (2007) · Acta Neuropathologica · doi:10.1007/s00401-007-0315-5 · Cited by 87
Increased metal content in the TDP-43A315T transgenic mouse model of frontotemporal lobar degeneration and amyotrophic lateral sclerosis
Dang, T. N. T., Lim, N. K.-H., Grubman, A., Li, Q., Volitakis, I., White, A. R., & Crouch, P. J. (2014) · Frontiers in Aging Neuroscience · doi:10.3389/fnagi.2014.00015 · Cited by 57
Mitochondrial Division in Rat Cardiomyocytes: An Electron Microscope Study
Fujioka, H., Tandler, B., & Hoppel, C. L. (2012) · The Anatomical Record · doi:10.1002/ar.22523 · Cited by 51
Self-citation
TDP43-Positive Intraneuronal Inclusions in a Patient with Motor Neuron Disease and Parkinson’s Disease
Chanson, J., Echaniz‐Laguna, A., Vogel, T., Mohr, M., Benoilid, A., Kaltenbach, G., & Kiesmann, M. (2010) · Neurodegenerative Diseases · doi:10.1159/000273591 · Cited by 42
TDP-43 in ubiquitinated inclusions in the inferior olives in frontotemporal lobar degeneration and in other neurodegenerative diseases: a degenerative process distinct from normal ageing
Davidson, Y. S., Amin, H., Kelley, T., Shi, J., Tian, J., Kumaran, R., Lashley, T., Lees, A. J., DuPlessis, D., Neary, D., et al. (2009) · Acta Neuropathologica · doi:10.1007/s00401-009-0526-z · Cited by 34
The Distribution of Genomic Variations in Human iPSCs Is Related to Replication-Timing Reorganization during Reprogramming
Lu, J., Li, H., Hu, M., Sasaki, T., Eastman, A. E., Gilbert, D. M., Liu, J. S., Collins, J. J., & Lerou, P. H. (2014) · Cell Reports · doi:10.1016/j.celrep.2014.03.007 · Cited by 29
Self-citation
Decreased Cytochrome c Oxidase Subunit VIIa in Aged Rat Heart Mitochondria: Immunocytochemistry
Fujioka, H., Moghaddas, S., Murdock, D. G., Lesnefsky, E. J., Tandler, B., & Hoppel, C. L. (2011) · The Anatomical Record · doi:10.1002/ar.21486 · Cited by 15
Self-citation
Endogenous progesterone levels and frontotemporal dementia: modulation of TDP-43 and Tau levelsin vitroand treatment of the A315TTARDBPmouse model
Dang, T. N. T., Dobson‐Stone, C., Glaros, E. N., Kim, W. S., Hallupp, M., Bartley, L., Piguet, O., Hodges, J. R., Halliday, G. M., Double, K. L., et al. (2013) · Disease Models & Mechanisms · doi:10.1242/dmm.011460 · Cited by 13

TDP-43 Triggers Mitochondrial DNA Release via mPTP to Activate cGAS/STING in ALS
Yu, C.-H., Davidson, S., Harapas, C. R., Hilton, J. B., Mlodzianoski, M. J., Laohamonthonkul, P., Louis, C., Low, R. R. J., Moecking, J., De Nardo, D., et al. (2020) · Cell · doi:10.1016/j.cell.2020.09.020 · Cited by 1,019
Molecular Mechanisms of TDP-43 Misfolding and Pathology in Amyotrophic Lateral Sclerosis
Prasad, A., Bharathi, V., Sivalingam, V., Girdhar, A., & Patel, B. K. (2019) · Frontiers in Molecular Neuroscience · doi:10.3389/fnmol.2019.00025 · Cited by 774
Novel genes associated with amyotrophic lateral sclerosis: diagnostic and clinical implications
Chia, R., Chiò, A., & Traynor, B. J. (2018) · The Lancet Neurology · doi:10.1016/s1474-4422(17)30401-5 · Cited by 573
Cytoplasmic functions of long noncoding RNAs
Noh, J. H., Kim, K. M., McClusky, W. G., Abdelmohsen, K., & Gorospe, M. (2018) · WIREs RNA · doi:10.1002/wrna.1471 · Cited by 432
Neuronal Cell Death Mechanisms in Major Neurodegenerative Diseases
Chi, H., Chang, H.-Y., & Sang, T.-K. (2018) · International Journal of Molecular Sciences · doi:10.3390/ijms19103082 · Cited by 412

See all 459

Authors: Wang, W., Wang, L., Lu, J., Siedlak, S. L., Fujioka, H., Liang, J., Jiang, S., Ma, X., Jiang, Z., da Rocha, E. L., Sheng, M., Choi, H., Lerou, P. H., Li, H., & Wang, X.
Venue: Nature Medicine
Publisher: Springer Science and Business Media LLC
Published: 2016-06-27
Volume: 22
Issue: 8
Pages: 869-878
ISSN: 1078-8956 (ISSN-L)
1546-170X
DOI: 10.1038/nm.4130
OpenAlex: W2472573833
Cited by: 459
References: 63
FWCI: 22.96
Type: journal article
Language: en
Open access: green

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

Data sources

Bibliographic data: Semantic Scholar, OpenAlex, Crossref.

Contains information from the Semantic Scholar Academic Graph Datasets, made available under the ODC Attribution License (ODC-BY 1.0).

Semantic Scholar’s data is described in: Kinney, R., et al. (2023). The Semantic Scholar Open Data Platform. arXiv:2301.10140.

The inhibition of TDP-43 mitochondrial localization blocks its neuronal toxicity

Abstract

Overview

Integrity signals

Verification

Claims the paper makes

Self-check

Citations

Cites

Cited by

Metadata

Record

About these checks

Data sources