{"status":"ok","message-type":"work","message-version":"1.0.0","message":{"indexed":{"date-parts":[[2026,9,24]],"date-time":"2026-09-24T16:57:47Z","timestamp":1790269067966,"version":"4.1.0"},"reference-count":139,"publisher":"MDPI AG","issue":"10","license":[{"start":{"date-parts":[[2023,10,18]],"date-time":"2023-10-18T00:00:00Z","timestamp":1697587200000},"content-version":"vor","delay-in-days":0,"URL":"https:\/\/creativecommons.org\/licenses\/by\/4.0\/"}],"content-domain":{"domain":[],"crossmark-restriction":false},"short-container-title":["Brain Sciences"],"abstract":"<jats:p>Frontotemporal lobar degeneration (FTLD) belongs to a heterogeneous group of highly complex neurodegenerative diseases and represents the second cause of presenile dementia in individuals under 65. Frontotemporal-TDP is a subgroup of frontotemporal dementia characterized by the aggregation of abnormal protein deposits, predominantly transactive response DNA-binding protein 43 (TDP-43), in the frontal and temporal brain regions. These deposits lead to progressive degeneration of neurons resulting in cognitive and behavioral impairments. Limbic age-related encephalopathy (LATE) pertains to age-related cognitive decline primarily affecting the limbic system, which is crucial for memory, emotions, and learning. However, distinct, emerging research suggests a potential overlap in pathogenic processes, with some cases of limbic encephalopathy displaying TDP-43 pathology. Genetic factors play a pivotal role in both disorders. Mutations in various genes, such as progranulin (GRN) and chromosome 9 open reading frame 72 (C9orf72), have been identified as causative in frontotemporal-TDP. Similarly, specific genetic variants have been associated with an increased risk of developing LATE. Understanding these genetic links provides crucial insights into disease mechanisms and the potential for targeted therapies.<\/jats:p>","DOI":"10.3390\/brainsci13101474","type":"journal-article","created":{"date-parts":[[2023,10,18]],"date-time":"2023-10-18T09:55:06Z","timestamp":1697622906000},"page":"1474","update-policy":"https:\/\/doi.org\/10.3390\/mdpi_crossmark_policy","source":"Crossref","is-referenced-by-count":3,"title":["Frontotemporal-TDP and LATE Neurocognitive Disorders: A Pathophysiological and Genetic Approach"],"prefix":"10.3390","volume":"13","author":[{"ORCID":"https:\/\/orcid.org\/0000-0002-7054-3313","authenticated-orcid":false,"given":"Genaro Gabriel","family":"Ortiz","sequence":"first","affiliation":[{"name":"Department of Philosophical and Methodological Disciplines, University Health Sciences Center, University of Guadalajara, Guadalajara 44340, Jalisco, Mexico"},{"name":"Postgraduate Gerontology Program, University Health Sciences Center, University of Guadalajara, Guadalajara 44340, Jalisco, Mexico"}],"role":[{"vocabulary":"crossref","role":"author"}]},{"ORCID":"https:\/\/orcid.org\/0000-0002-2299-6721","authenticated-orcid":false,"given":"Javier","family":"Ram\u00edrez-Jirano","sequence":"additional","affiliation":[{"name":"Neurosciences Division, Western Biomedical Research Center, Mexican Social Security Institute, IMSS, Guadalajara 44340, Jalisco, Mexico"}],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Raul L.","family":"Arizaga","sequence":"additional","affiliation":[{"name":"Public Health Department, School of Medicine, University of Buenos Aires, Buenos Aires C1121ABG, Argentina"}],"role":[{"vocabulary":"crossref","role":"author"}]},{"ORCID":"https:\/\/orcid.org\/0000-0002-1968-4815","authenticated-orcid":false,"given":"Daniela L. C.","family":"Delgado-Lara","sequence":"additional","affiliation":[{"name":"Department of Philosophical and Methodological Disciplines, University Health Sciences Center, University of Guadalajara, Guadalajara 44340, Jalisco, Mexico"},{"name":"Departamento Acad\u00e9mico de Formaci\u00f3n Universitaria, Ciencias de la Salud, Universidad Aut\u00f3noma de Guadalajara, Zapopan 45129, Jalisco, Mexico"}],"role":[{"vocabulary":"crossref","role":"author"}]},{"ORCID":"https:\/\/orcid.org\/0000-0002-8131-6853","authenticated-orcid":false,"given":"Erandis D.","family":"Torres-S\u00e1nchez","sequence":"additional","affiliation":[{"name":"Department of Medical and Life Sciences, University Center of la Cienega, University of Guadalajara, Ocotlan 47820, Jalisco, Mexico"}],"role":[{"vocabulary":"crossref","role":"author"}]}],"member":"1968","published-online":{"date-parts":[[2023,10,18]]},"reference":[{"key":"ref_1","doi-asserted-by":"crossref","first-page":"3584","DOI":"10.1128\/jvi.69.6.3584-3596.1995","article-title":"Cloning and characterization of a novel cellular protein, TDP-43, that binds to human immunodeficiency virus type 1 TAR DNA sequence motifs","volume":"69","author":"Ou","year":"1995","journal-title":"J. Virol."},{"key":"ref_2","doi-asserted-by":"crossref","first-page":"26304","DOI":"10.1074\/jbc.M110.125039","article-title":"Interaction with polyglutamine aggregates reveals a Q\/N-rich domain in TDP-43","volume":"285","author":"Fuentealba","year":"2010","journal-title":"J. Biol. Chem."},{"key":"ref_3","doi-asserted-by":"crossref","first-page":"36337","DOI":"10.1074\/jbc.M104236200","article-title":"Characterization and functional implications of the RNA binding properties of nuclear factor TDP-43, a novel splicing regulator of CFTR exon 9","volume":"276","author":"Buratti","year":"2001","journal-title":"J. Biol. Chem."},{"key":"ref_4","doi-asserted-by":"crossref","first-page":"1204","DOI":"10.1074\/jbc.M110.190884","article-title":"Identification of neuronal RNA targets of TDP-43-containing ribonucleoprotein complexes","volume":"286","author":"Sephton","year":"2011","journal-title":"J. Biol. Chem."},{"key":"ref_5","doi-asserted-by":"crossref","first-page":"459","DOI":"10.1038\/nn.2779","article-title":"Long pre-mRNA depletion and RNA missplicing contribute to neuronal vulnerability from loss of TDP-43","volume":"14","author":"Polymenidou","year":"2011","journal-title":"Nat. Neurosci."},{"key":"ref_6","doi-asserted-by":"crossref","first-page":"452","DOI":"10.1038\/nn.2778","article-title":"Characterizing the RNA targets and position-dependent splicing regulation by TDP-43","volume":"14","author":"Tollervey","year":"2011","journal-title":"Nat. Neurosci."},{"key":"ref_7","doi-asserted-by":"crossref","first-page":"277","DOI":"10.1038\/emboj.2010.310","article-title":"TDP-43 regulates its mRNA levels through a negative feedback loop","volume":"30","author":"Ayala","year":"2011","journal-title":"EMBO J."},{"key":"ref_8","doi-asserted-by":"crossref","first-page":"461","DOI":"10.1097\/01.jnen.0000240474.27791.f3","article-title":"RNA in brain disease: No longer just \u201cthe messenger in the middle\u201d","volume":"66","author":"Nelson","year":"2007","journal-title":"J. Neuropathol. Exp. Neurol."},{"key":"ref_9","doi-asserted-by":"crossref","first-page":"806","DOI":"10.1038\/35888","article-title":"Potent and specific genetic interference by double-stranded RNA in Caenorhabditis elegans","volume":"391","author":"Fire","year":"1998","journal-title":"Nature"},{"key":"ref_10","doi-asserted-by":"crossref","first-page":"415","DOI":"10.1038\/nature01957","article-title":"The nuclear RNase III Drosha initiates microRNA processing","volume":"425","author":"Lee","year":"2003","journal-title":"Nature"},{"key":"ref_11","doi-asserted-by":"crossref","first-page":"3","DOI":"10.1016\/j.virusres.2004.01.009","article-title":"Derivation and function of small interfering RNAs and microRNAs","volume":"102","author":"Cullen","year":"2004","journal-title":"Virus Res."},{"key":"ref_12","doi-asserted-by":"crossref","first-page":"235","DOI":"10.1016\/j.jsb.2009.06.006","article-title":"TDP-43 localizes in mRNA transcription and processing sites in mammalian neurons","volume":"167","author":"Casafont","year":"2009","journal-title":"J. Struct. Biol."},{"key":"ref_13","doi-asserted-by":"crossref","first-page":"1398","DOI":"10.1016\/j.bbagrm.2015.10.015","article-title":"From transcriptomic to protein level changes in TDP-43 and FUS loss-of-function cell models","volume":"1849","author":"Colombrita","year":"2015","journal-title":"Biochim. Biophys. Acta"},{"key":"ref_14","doi-asserted-by":"crossref","unstructured":"Roberts, T.C., Morris, K.V., and Wood, M.J.A. (2014). The role of long non-coding RNAs in neurodevelopment, brain function and neurological disease. Philos. Trans. R. Soc. B Biol. Sci., 369.","DOI":"10.1098\/rstb.2013.0507"},{"key":"ref_15","doi-asserted-by":"crossref","first-page":"31","DOI":"10.1186\/1756-6606-6-31","article-title":"The long non-coding RNA nuclear-enriched abundant transcript 1_2 induces paraspeckle formation in the motor neuron during the early phase of amyotrophic lateral sclerosis","volume":"6","author":"Nishimoto","year":"2013","journal-title":"Mol. Brain"},{"key":"ref_16","doi-asserted-by":"crossref","first-page":"976","DOI":"10.3390\/biology2030976","article-title":"The role of nuclear bodies in gene expression and disease","volume":"2","author":"Morimoto","year":"2013","journal-title":"Biology"},{"key":"ref_17","doi-asserted-by":"crossref","first-page":"445","DOI":"10.1016\/j.nbd.2015.07.011","article-title":"Long noncoding RNAs in TDP-43 and FUS\/TLS-related frontotemporal lobar degeneration (FTLD)","volume":"82","author":"Lourenco","year":"2015","journal-title":"Neurobiol. Dis."},{"key":"ref_18","doi-asserted-by":"crossref","first-page":"64","DOI":"10.1186\/1750-1326-6-64","article-title":"TDP-43 knockdown impairs neurite outgrowth dependent on its target histone deacetylase 6","volume":"6","author":"Fiesel","year":"2011","journal-title":"Mol. Neurodegener."},{"key":"ref_19","doi-asserted-by":"crossref","first-page":"1280","DOI":"10.1080\/15476286.2014.996081","article-title":"TDP-43 regulates \u03b2-adducin (Add2) transcript stability","volume":"11","author":"Costessi","year":"2014","journal-title":"RNA Biol."},{"key":"ref_20","doi-asserted-by":"crossref","first-page":"15635","DOI":"10.1074\/jbc.M111.333450","article-title":"TDP-43 and FUS RNA-binding proteins bind distinct sets of cytoplasmic messenger RNAs and differently regulate their post-transcriptional fate in motoneuron-like cells","volume":"287","author":"Colombrita","year":"2012","journal-title":"J. Biol. Chem."},{"key":"ref_21","doi-asserted-by":"crossref","first-page":"5791","DOI":"10.1038\/ncomms6791","article-title":"Identification of a subnuclear body involved in sequence-specific cytokine RNA processing","volume":"6","author":"Lee","year":"2015","journal-title":"Nat. Commun."},{"key":"ref_22","doi-asserted-by":"crossref","first-page":"16086","DOI":"10.1523\/JNEUROSCI.4105-11.2011","article-title":"Local RNA translation at the synapse and in disease","volume":"31","author":"Bassell","year":"2011","journal-title":"J. Neurosci."},{"key":"ref_23","doi-asserted-by":"crossref","first-page":"3703","DOI":"10.1093\/hmg\/dds205","article-title":"The ALS disease protein TDP-43 is actively transported in motor neuron axons and regulates axon outgrowth","volume":"21","author":"Fallini","year":"2012","journal-title":"Hum. Mol. Genet."},{"key":"ref_24","doi-asserted-by":"crossref","first-page":"536","DOI":"10.1016\/j.neuron.2013.12.018","article-title":"Axonal transport of TDP-43 mRNA granules is impaired by ALS-causing mutations","volume":"81","author":"Alami","year":"2014","journal-title":"Neuron"},{"key":"ref_25","doi-asserted-by":"crossref","first-page":"529","DOI":"10.1002\/glia.22453","article-title":"Hyposmolality differentially and spatiotemporally modulates levels of glutamine synthetase and serine racemase in rat supraoptic nucleus","volume":"61","author":"Wang","year":"2013","journal-title":"Glia"},{"key":"ref_26","doi-asserted-by":"crossref","first-page":"1104","DOI":"10.1021\/pr901076y","article-title":"Global analysis of TDP-43 interacting proteins reveals strong association with RNA splicing and translation machinery","volume":"9","author":"Freibaum","year":"2010","journal-title":"J. Proteome Res."},{"key":"ref_27","doi-asserted-by":"crossref","first-page":"288","DOI":"10.1111\/jnc.12194","article-title":"TDP-43 associates with stalled ribosomes and contributes to cell survival during cellular stress","volume":"126","author":"Higashi","year":"2013","journal-title":"J. Neurochem."},{"key":"ref_28","doi-asserted-by":"crossref","first-page":"15962","DOI":"10.1523\/JNEUROSCI.2526-14.2014","article-title":"Futsch\/MAP1B mRNA is a translational target of TDP-43 and is neuroprotective in a Drosophila model of amyotrophic lateral sclerosis","volume":"34","author":"Coyne","year":"2014","journal-title":"J. Neurosci."},{"key":"ref_29","doi-asserted-by":"crossref","first-page":"231","DOI":"10.1007\/s00401-012-1006-4","article-title":"TDP-43 regulates the mammalian spinogenesis through translational repression of Rac1","volume":"124","author":"Majumder","year":"2012","journal-title":"Acta Neuropathol."},{"key":"ref_30","doi-asserted-by":"crossref","first-page":"86","DOI":"10.1093\/brain\/awv308","article-title":"MTHFSD and DDX58 are novel RNA-binding proteins abnormally regulated in amyotrophic lateral sclerosis","volume":"139","author":"MacNair","year":"2016","journal-title":"Brain"},{"key":"ref_31","doi-asserted-by":"crossref","first-page":"38","DOI":"10.1038\/nrn3121","article-title":"Gains or losses: Molecular mechanisms of TDP43-mediated neurodegeneration","volume":"13","author":"Lee","year":"2011","journal-title":"Nat. Rev. Neurosci."},{"key":"ref_32","doi-asserted-by":"crossref","first-page":"54","DOI":"10.1111\/jnc.13588","article-title":"Molecular neuropathology of frontotemporal dementia: Insights into disease mechanisms from post-mortem studies","volume":"138","author":"Mackenzie","year":"2016","journal-title":"J. Neurochem."},{"key":"ref_33","doi-asserted-by":"crossref","first-page":"349","DOI":"10.1007\/s00401-009-0547-7","article-title":"Evaluation of subcortical pathology and clinical correlations in FTLD-U subtypes","volume":"118","author":"Josephs","year":"2009","journal-title":"Acta Neuropathol."},{"key":"ref_34","doi-asserted-by":"crossref","first-page":"111","DOI":"10.1007\/s00401-011-0845-8","article-title":"A harmonized classification system for FTLD-TDP pathology","volume":"122","author":"Mackenzie","year":"2011","journal-title":"Acta Neuropathol."},{"key":"ref_35","doi-asserted-by":"crossref","first-page":"60","DOI":"10.1002\/ana.21425","article-title":"Phosphorylated TDP-43 in frontotemporal lobar degeneration and amyotrophic lateral sclerosis","volume":"64","author":"Hasegawa","year":"2008","journal-title":"Ann. Neurol."},{"key":"ref_36","doi-asserted-by":"crossref","first-page":"137","DOI":"10.1007\/s00401-008-0477-9","article-title":"Phosphorylation of S409\/410 of TDP-43 is a consistent feature in all sporadic and familial forms of TDP-43 proteinopathies","volume":"117","author":"Neumann","year":"2009","journal-title":"Acta Neuropathol."},{"key":"ref_37","doi-asserted-by":"crossref","first-page":"320","DOI":"10.1016\/j.mcn.2007.03.007","article-title":"TDP43 is a human low molecular weight neurofilament (hNFL) mRNA-binding protein","volume":"35","author":"Strong","year":"2007","journal-title":"Mol. Cell. Neurosci."},{"key":"ref_38","doi-asserted-by":"crossref","first-page":"405","DOI":"10.1016\/j.bbrc.2009.03.038","article-title":"Identification of casein kinase-1 phosphorylation sites on TDP-43","volume":"382","author":"Kametani","year":"2009","journal-title":"Biochem. Biophys. Res. Commun."},{"key":"ref_39","doi-asserted-by":"crossref","first-page":"8516","DOI":"10.1074\/jbc.M809462200","article-title":"Expression of TDP-43 C-terminal Fragments in Vitro Recapitulates Pathological Features of TDP-43 Proteinopathies","volume":"284","author":"Igaz","year":"2009","journal-title":"J. Biol. Chem."},{"key":"ref_40","doi-asserted-by":"crossref","first-page":"3353","DOI":"10.1093\/hmg\/ddp275","article-title":"Truncation and pathogenic mutations facilitate the formation of intracellular aggregates of TDP-43","volume":"18","author":"Nonaka","year":"2009","journal-title":"Hum. Mol. Genet."},{"key":"ref_41","doi-asserted-by":"crossref","first-page":"13302","DOI":"10.1074\/jbc.M800342200","article-title":"Disturbance of nuclear and cytoplasmic TAR DNA-binding protein (TDP-43) induces disease-like redistribution, sequestration, and aggregate formation","volume":"283","author":"Winton","year":"2008","journal-title":"J. Biol. Chem."},{"key":"ref_42","doi-asserted-by":"crossref","first-page":"18809","DOI":"10.1073\/pnas.0908767106","article-title":"TDP-43 mutant transgenic mice develop features of ALS and frontotemporal lobar degeneration","volume":"106","author":"Wegorzewska","year":"2009","journal-title":"Proc. Natl. Acad. Sci. USA"},{"key":"ref_43","doi-asserted-by":"crossref","first-page":"10851","DOI":"10.1523\/JNEUROSCI.1630-10.2010","article-title":"Wild-type human TDP-43 expression causes TDP-43 phosphorylation, mitochondrial aggregation, motor deficits, and early mortality in transgenic mice","volume":"30","author":"Xu","year":"2010","journal-title":"J. Neurosci."},{"key":"ref_44","doi-asserted-by":"crossref","first-page":"33","DOI":"10.1186\/1750-1326-5-33","article-title":"Phosphorylation regulates proteasomal-mediated degradation and solubility of TAR DNA binding protein-43 C-terminal fragments","volume":"5","author":"Zhang","year":"2010","journal-title":"Mol. Neurodegener."},{"key":"ref_45","doi-asserted-by":"crossref","first-page":"39","DOI":"10.1002\/ana.23870","article-title":"CDC7 inhibition blocks pathological TDP-43 phosphorylation and neurodegeneration","volume":"74","author":"Liachko","year":"2013","journal-title":"Ann. Neurol."},{"key":"ref_46","doi-asserted-by":"crossref","unstructured":"Liachko, N.F., McMillan, P.J., Strovas, T.J., Loomis, E., Greenup, L., Murrell, J.R., Ghetti, B., Raskind, M.A., Montine, T.J., and Bird, T.D. (2014). The tau tubulin kinases TTBK1\/2 promote accumulation of pathological TDP-43. PLoS Genet., 10.","DOI":"10.1371\/journal.pgen.1004803"},{"key":"ref_47","doi-asserted-by":"crossref","unstructured":"Li, H.Y., Yeh, P.A., Chiu, H.C., Tang, C.Y., and Tu, B.P. (2011). Hyperphosphorylation as a defense mechanism to reduce TDP-43 aggregation. PLoS ONE, 6.","DOI":"10.1371\/journal.pone.0023075"},{"key":"ref_48","doi-asserted-by":"crossref","first-page":"1082","DOI":"10.1111\/j.1471-4159.2009.06211.x","article-title":"Proteolytic processing of TAR DNA binding protein-43 by caspases produces C-terminal fragments with disease defining properties independent of progranulin","volume":"110","author":"Dormann","year":"2009","journal-title":"J. Neurochem."},{"key":"ref_49","doi-asserted-by":"crossref","first-page":"862","DOI":"10.1016\/j.nbd.2011.12.002","article-title":"Oxidative stress induced by glutathione depletion reproduces pathological modifications of TDP-43 linked to TDP-43 proteinopathies","volume":"45","author":"Iguchi","year":"2012","journal-title":"Neurobiol. Dis."},{"key":"ref_50","doi-asserted-by":"crossref","first-page":"4103","DOI":"10.1074\/jbc.M112.419945","article-title":"Parkin ubiquitinates Tar-DNA binding protein-43 (TDP-43) and promotes its cytosolic accumulation via interaction with histone deacetylase 6 (HDAC6)","volume":"288","author":"Hebron","year":"2013","journal-title":"J. Biol. Chem."},{"key":"ref_51","doi-asserted-by":"crossref","first-page":"18845","DOI":"10.1074\/jbc.M111.231118","article-title":"A \u201ctwo-hit\u201d hypothesis for inclusion formation by carboxyl-terminal fragments of TDP-43 protein linked to RNA depletion and impaired microtubule-dependent transport","volume":"286","author":"Pesiridis","year":"2011","journal-title":"J. Biol. Chem."},{"key":"ref_52","doi-asserted-by":"crossref","first-page":"39","DOI":"10.1016\/j.ygcen.2011.02.005","article-title":"The role of ubiquitin-proteasome system in ageing","volume":"172","author":"Low","year":"2011","journal-title":"Gen. Comp. Endocrinol."},{"key":"ref_53","doi-asserted-by":"crossref","first-page":"19164","DOI":"10.1074\/jbc.M114.561704","article-title":"UBE2E ubiquitin-conjugating enzymes and ubiquitin isopeptidase Y regulate TDP-43 protein ubiquitination","volume":"289","author":"Hans","year":"2014","journal-title":"J. Biol. Chem."},{"key":"ref_54","doi-asserted-by":"crossref","first-page":"179","DOI":"10.1038\/nature09299","article-title":"Enhancement of proteasome activity by a small-molecule inhibitor of USP14","volume":"467","author":"Lee","year":"2010","journal-title":"Nature"},{"key":"ref_55","doi-asserted-by":"crossref","first-page":"1668","DOI":"10.1126\/science.1154584","article-title":"TDP-43 mutations in familial and sporadic amyotrophic lateral sclerosis","volume":"319","author":"Sreedharan","year":"2008","journal-title":"Science"},{"key":"ref_56","doi-asserted-by":"crossref","first-page":"10530","DOI":"10.1523\/JNEUROSCI.3421-07.2007","article-title":"Progranulin mediates caspase-dependent cleavage of TAR DNA binding protein-43","volume":"27","author":"Zhang","year":"2007","journal-title":"J. Neurosci."},{"key":"ref_57","doi-asserted-by":"crossref","first-page":"13171","DOI":"10.1074\/jbc.M110.197483","article-title":"TDP-43-induced death is associated with altered regulation of BIM and Bcl-xL and attenuated by caspase-mediated TDP-43 cleavage","volume":"286","author":"Suzuki","year":"2011","journal-title":"J. Biol. Chem."},{"key":"ref_58","doi-asserted-by":"crossref","unstructured":"Voigt, A., Herholz, D., Fiesel, F.C., Kaur, K., M\u00fcller, D., Karsten, P., Weber, S.S., Kahle, P.J., Marquardt, T., and Schulz, J.B. (2010). TDP-43-mediated neuron loss in vivo requires RNA-binding activity. PLoS ONE, 5.","DOI":"10.1371\/journal.pone.0012247"},{"key":"ref_59","doi-asserted-by":"crossref","first-page":"1051","DOI":"10.1111\/j.1471-4159.2009.06383.x","article-title":"TDP-43 is recruited to stress granules in conditions of oxidative insult","volume":"111","author":"Colombrita","year":"2009","journal-title":"J. Neurochem."},{"key":"ref_60","doi-asserted-by":"crossref","first-page":"4345","DOI":"10.1093\/hmg\/ddu152","article-title":"Distinct pathways leading to TDP-43-induced cellular dysfunctions","volume":"23","author":"Yamashita","year":"2014","journal-title":"Hum. Mol. Genet."},{"key":"ref_61","doi-asserted-by":"crossref","first-page":"726","DOI":"10.1172\/JCI44867","article-title":"Dysregulation of the ALS-associated gene TDP-43 leads to neuronal death and degeneration in mice","volume":"121","author":"Igaz","year":"2011","journal-title":"J. Clin. Investig."},{"key":"ref_62","doi-asserted-by":"crossref","first-page":"4824","DOI":"10.1038\/ncomms5824","article-title":"Full-length TDP-43 forms toxic amyloid oligomers that are present in frontotemporal lobar dementia-TDP patients","volume":"5","author":"Fang","year":"2014","journal-title":"Nat. Commun."},{"key":"ref_63","doi-asserted-by":"crossref","first-page":"423","DOI":"10.1007\/s00401-013-1238-y","article-title":"Sequential distribution of pTDP-43 pathology in behavioral variant frontotemporal dementia (bvFTD)","volume":"127","author":"Brettschneider","year":"2014","journal-title":"Acta Neuropathol."},{"key":"ref_64","doi-asserted-by":"crossref","first-page":"1577","DOI":"10.1016\/j.bbadis.2011.09.005","article-title":"Molecular properties of TAR DNA binding protein-43 fragments are dependent upon its cleavage site","volume":"1812","author":"Furukawa","year":"2011","journal-title":"Biochim. Biophys. Acta"},{"key":"ref_65","doi-asserted-by":"crossref","first-page":"337","DOI":"10.1007\/s12035-012-8380-8","article-title":"Mechanisms of granulin deficiency: Lessons from cellular and animal models","volume":"47","author":"Kleinberger","year":"2013","journal-title":"Mol. Neurobiol."},{"key":"ref_66","doi-asserted-by":"crossref","first-page":"1161","DOI":"10.1016\/S0006-291X(05)80908-8","article-title":"Granulins, a novel class of peptide from leukocytes","volume":"173","author":"Bateman","year":"1990","journal-title":"Biochem. Biophys. Res. Commun."},{"key":"ref_67","doi-asserted-by":"crossref","first-page":"311","DOI":"10.2353\/ajpath.2010.090915","article-title":"Accelerated lipofuscinosis and ubiquitination in granulin knockout mice suggest a role for progranulin in successful aging","volume":"177","author":"Ahmed","year":"2010","journal-title":"Am. J. Pathol."},{"key":"ref_68","doi-asserted-by":"crossref","first-page":"123","DOI":"10.1007\/s00401-009-0616-y","article-title":"Progranulin expression is upregulated after spinal contusion in mice","volume":"119","author":"Naphade","year":"2010","journal-title":"Acta Neuropathol."},{"key":"ref_69","doi-asserted-by":"crossref","first-page":"1191","DOI":"10.1097\/NEN.0b013e3181fc9aea","article-title":"Microglial upregulation of progranulin as a marker of motor neuron degeneration","volume":"69","author":"Philips","year":"2010","journal-title":"J. Neuropathol. Exp. Neurol."},{"key":"ref_70","doi-asserted-by":"crossref","first-page":"467","DOI":"10.1212\/WNL.0b013e31820a0e3b","article-title":"TMEM106B regulates progranulin levels and the penetrance of FTLD in GRN mutation carriers","volume":"76","author":"Finch","year":"2011","journal-title":"Neurology"},{"key":"ref_71","doi-asserted-by":"crossref","first-page":"581","DOI":"10.1001\/archneurol.2010.350","article-title":"Association of TMEM106B gene polymorphism with age at onset in granulin mutation carriers and plasma granulin protein levels","volume":"68","author":"Cruchaga","year":"2011","journal-title":"Arch Neurol."},{"key":"ref_72","doi-asserted-by":"crossref","first-page":"19355","DOI":"10.1074\/jbc.M112.365098","article-title":"Membrane orientation and subcellular localization of transmembrane protein 106B (TMEM106B), a major risk factor for frontotemporal lobar degeneration","volume":"287","author":"Lang","year":"2012","journal-title":"J. Biol. Chem."},{"key":"ref_73","doi-asserted-by":"crossref","first-page":"11213","DOI":"10.1523\/JNEUROSCI.0521-12.2012","article-title":"TMEM106B, the risk gene for frontotemporal dementia, is regulated by the microRNA-132\/212 cluster and affects progranulin pathways","volume":"32","author":"Unger","year":"2012","journal-title":"J. Neurosci."},{"key":"ref_74","unstructured":"L\u00e9ger, J.M., and Mas, J.L. (2015). D\u00e9mences, Doin-John Libbey Eurotext."},{"key":"ref_75","doi-asserted-by":"crossref","first-page":"e83189","DOI":"10.7554\/eLife.83189","article-title":"Translation of dipeptide repeat proteins in C9ORF72 ALS\/FTD through unique and redundant AUG initiation codons","volume":"12","author":"Sonobe","year":"2023","journal-title":"eLife"},{"key":"ref_76","doi-asserted-by":"crossref","unstructured":"Kortazar-Zubizarreta, I., Manero-Azua, A., Afonso-Ag\u00fcera, J., and de Nanclares, G.P. (2023). C9ORF72 Gene GGGGCC Hexanucleotide Expansion: A High Clinical Variability from Amyotrophic Lateral Sclerosis to Frontotemporal Dementia. J. Pers. Med., 13.","DOI":"10.3390\/jpm13091396"},{"key":"ref_77","doi-asserted-by":"crossref","first-page":"5764","DOI":"10.1038\/s41467-023-41511-3","article-title":"Phenylalanine-tRNA aminoacylation is compromised by ALS\/FTD-associated C9orf72 C4G2 repeat RNA","volume":"14","author":"Yin","year":"2023","journal-title":"Nat. Commun."},{"key":"ref_78","doi-asserted-by":"crossref","first-page":"3091","DOI":"10.1093\/brain\/awl267","article-title":"Progranulin gene mutations associated with frontotemporal dementia and progressive non-fluent aphasia","volume":"129","author":"Snowden","year":"2006","journal-title":"Brain"},{"key":"ref_79","doi-asserted-by":"crossref","first-page":"e88","DOI":"10.1212\/WNL.0000000000012174","article-title":"Primary Progressive Aphasia Associated With GRN Mutations: New Insights Into the Nonamyloid Logopenic Variant","volume":"97","author":"Saracino","year":"2021","journal-title":"Neurology"},{"key":"ref_80","doi-asserted-by":"crossref","first-page":"939","DOI":"10.3233\/JAD-140717","article-title":"A mutation in the 5\u2019-UTR of GRN gene associated with frontotemporal lobar degeneration: Phenotypic variability and possible pathogenetic mechanisms","volume":"42","author":"Puoti","year":"2014","journal-title":"J. Alzheimers Dis."},{"key":"ref_81","doi-asserted-by":"crossref","first-page":"S21","DOI":"10.1212\/WNL.56.suppl_4.S21","article-title":"Missense and splice site mutations in tau associated with FTDP-17: Multiple pathogenic mechanisms","volume":"56","author":"Hutton","year":"2001","journal-title":"Neurology"},{"key":"ref_82","doi-asserted-by":"crossref","first-page":"702","DOI":"10.1038\/31508","article-title":"Association of missense and 5\u2019-splice-site mutations in tau with the inherited dementia FTDP-17","volume":"393","author":"Hutton","year":"1998","journal-title":"Nature"},{"key":"ref_83","doi-asserted-by":"crossref","first-page":"222.e9","DOI":"10.1016\/j.neurobiolaging.2016.07.028","article-title":"TYROBP genetic variants in early-onset Alzheimer\u2019s disease","volume":"48","author":"Pottier","year":"2016","journal-title":"Neurobiol. Aging"},{"key":"ref_84","doi-asserted-by":"crossref","first-page":"377","DOI":"10.1038\/ng1332","article-title":"Inclusion body myopathy associated with Paget disease of bone and frontotemporal dementia is caused by mutant valosin-containing protein","volume":"36","author":"Watts","year":"2004","journal-title":"Nat. Genet."},{"key":"ref_85","doi-asserted-by":"crossref","first-page":"766","DOI":"10.1016\/j.nmd.2009.08.003","article-title":"Valosin containing protein associated inclusion body myopathy: Abnormal vacuolization, autophagy and cell fusion in myoblasts","volume":"19","author":"Vesa","year":"2009","journal-title":"Neuromuscul. Disord."},{"key":"ref_86","doi-asserted-by":"crossref","first-page":"1741","DOI":"10.1093\/hmg\/ddq050","article-title":"Transgenic mice expressing mutant forms VCP\/p97 recapitulate the full spectrum of IBMPFD including degeneration in muscle, brain and bone","volume":"19","author":"Custer","year":"2010","journal-title":"Hum. Mol. Genet."},{"key":"ref_87","doi-asserted-by":"crossref","first-page":"e2222","DOI":"10.1002\/mgg3.2222","article-title":"A novel splice-site mutation in CHMP2B associated with frontotemporal dementia: The first report from China and literature review","volume":"11","author":"Li","year":"2023","journal-title":"Mol. Genet. Genom. Med."},{"key":"ref_88","doi-asserted-by":"crossref","first-page":"806","DOI":"10.1038\/ng1609","article-title":"Mutations in the endosomal ESCRTIII-complex subunit CHMP2B in frontotemporal dementia","volume":"37","author":"Skibinski","year":"2005","journal-title":"Nat. Genet."},{"key":"ref_89","doi-asserted-by":"crossref","first-page":"1556","DOI":"10.1212\/WNL.0b013e31826e25df","article-title":"SQSTM1 mutations in frontotemporal lobar degeneration and amyotrophic lateral sclerosis","volume":"79","author":"Rubino","year":"2012","journal-title":"Neurology"},{"key":"ref_90","doi-asserted-by":"crossref","first-page":"1396","DOI":"10.1080\/15548627.2019.1686729","article-title":"PTK2\/FAK regulates UPS impairment via SQSTM1\/p62 phosphorylation in TARDBP\/TDP-43 proteinopathies","volume":"16","author":"Lee","year":"2020","journal-title":"Autophagy"},{"key":"ref_91","doi-asserted-by":"crossref","first-page":"808","DOI":"10.1016\/j.neuron.2017.07.025","article-title":"TIA1 Mutations in Amyotrophic Lateral Sclerosis and Frontotemporal Dementia Promote Phase Separation and Alter Stress Granule Dynamics","volume":"95","author":"Mackenzie","year":"2017","journal-title":"Neuron"},{"key":"ref_92","doi-asserted-by":"crossref","first-page":"37","DOI":"10.1083\/jcb.200712039","article-title":"Progranulin functions as a neurotrophic factor to regulate neurite outgrowth and enhance neuronal survival","volume":"181","author":"Lambrechts","year":"2008","journal-title":"J. Cell Biol."},{"key":"ref_93","doi-asserted-by":"crossref","first-page":"11126","DOI":"10.1523\/JNEUROSCI.6244-10.2011","article-title":"Progranulin deficiency decreases gross neural connectivity but enhances transmission at individual synapses","volume":"31","author":"Tapia","year":"2011","journal-title":"J. Neurosci."},{"key":"ref_94","doi-asserted-by":"crossref","unstructured":"Kocerha, J., Kouri, N., Baker, M., Finch, N., DeJesus-Hernandez, M., Gonzalez, J., Chidamparam, K., Josephs, K.A., Boeve, B.F., and Graff-Radford, N.R. (2011). Altered microRNA expression in frontotemporal lobar degeneration with TDP-43 pathology caused by progranulin mutations. BMC Genom., 12.","DOI":"10.1186\/1471-2164-12-527"},{"key":"ref_95","doi-asserted-by":"crossref","first-page":"921","DOI":"10.1016\/j.cell.2016.04.001","article-title":"Progranulin Deficiency Promotes Circuit-Specific Synaptic Pruning by Microglia via Complement Activation","volume":"165","author":"Lui","year":"2016","journal-title":"Cell"},{"key":"ref_96","doi-asserted-by":"crossref","first-page":"33","DOI":"10.1186\/1750-1326-7-33","article-title":"Progranulin regulates neuronal outgrowth independent of sortilin","volume":"7","author":"Gass","year":"2012","journal-title":"Mol. Neurodegener."},{"key":"ref_97","doi-asserted-by":"crossref","first-page":"118","DOI":"10.1016\/j.brainres.2012.01.047","article-title":"Progranulin: An emerging target for FTLD therapies","volume":"1462","author":"Gass","year":"2012","journal-title":"Brain Res."},{"key":"ref_98","doi-asserted-by":"crossref","first-page":"654","DOI":"10.1016\/j.neuron.2010.09.034","article-title":"Sortilin-mediated endocytosis determines levels of the frontotemporal dementia protein, progranulin","volume":"68","author":"Hu","year":"2010","journal-title":"Neuron"},{"key":"ref_99","doi-asserted-by":"crossref","first-page":"e157161","DOI":"10.1172\/JCI157161","article-title":"Progranulin deficiency promotes neuroinflammation and neuron loss following toxin-induced injury","volume":"132","author":"Martens","year":"2022","journal-title":"J. Clin. Investig."},{"key":"ref_100","doi-asserted-by":"crossref","unstructured":"Suh, H.S., Choi, N., Tarassishin, L., and Lee, S.C. (2012). Regulation of progranulin expression in human microglia and proteolysis of progranulin by matrix metalloproteinase-12 (MMP-12). PLoS ONE, 7.","DOI":"10.1371\/journal.pone.0035115"},{"key":"ref_101","doi-asserted-by":"crossref","first-page":"1","DOI":"10.1016\/j.brainres.2010.09.099","article-title":"Progranulin deficiency leads to enhanced cell vulnerability and TDP-43 translocation in primary neuronal cultures","volume":"1366","author":"Guo","year":"2010","journal-title":"Brain Res."},{"key":"ref_102","doi-asserted-by":"crossref","first-page":"735","DOI":"10.1111\/j.1471-4159.2010.06961.x","article-title":"Increased caspase activation and decreased TDP-43 solubility in progranulin knockout cortical cultures","volume":"115","author":"Kleinberger","year":"2010","journal-title":"J. Neurochem."},{"key":"ref_103","doi-asserted-by":"crossref","first-page":"1744","DOI":"10.1074\/jbc.M705115200","article-title":"Missense mutations in the progranulin gene linked to frontotemporal lobar degeneration with ubiquitin-immunoreactive inclusions reduce progranulin production and secretion","volume":"283","author":"Shankaran","year":"2008","journal-title":"J. Biol. Chem."},{"key":"ref_104","doi-asserted-by":"crossref","first-page":"67","DOI":"10.1002\/path.4043","article-title":"Cellular ageing, increased mortality and FTLD-TDP-associated neuropathology in progranulin knockout mice","volume":"228","author":"Wils","year":"2012","journal-title":"J. Pathol."},{"key":"ref_105","first-page":"4639","article-title":"Behavioral deficits and progressive neuropathology in progranulin-deficient mice: A mouse model of frontotemporal dementia","volume":"24","author":"Yin","year":"2010","journal-title":"FASEB J."},{"key":"ref_106","doi-asserted-by":"crossref","first-page":"9315","DOI":"10.1523\/JNEUROSCI.4808-14.2015","article-title":"The Progranulin Cleavage Products, Granulins, Exacerbate TDP-43 Toxicity and Increase TDP-43 Levels","volume":"35","author":"Salazar","year":"2015","journal-title":"J. Neurosci."},{"key":"ref_107","doi-asserted-by":"crossref","first-page":"49","DOI":"10.1007\/s00401-007-0223-8","article-title":"The neuropathology and clinical phenotype of FTD with progranulin mutations","volume":"114","author":"Mackenzie","year":"2007","journal-title":"Acta Neuropathol."},{"key":"ref_108","doi-asserted-by":"crossref","first-page":"794","DOI":"10.1093\/brain\/aws001","article-title":"Neuroimaging signatures of frontotemporal dementia genetics: C9ORF72, Tau, progranulin and sporadics","volume":"135","author":"Whitwell","year":"2012","journal-title":"Brain"},{"key":"ref_109","doi-asserted-by":"crossref","first-page":"353","DOI":"10.1007\/s00401-012-1029-x","article-title":"The genetics and neuropathology of frontotemporal lobar degeneration","volume":"124","author":"Sieben","year":"2012","journal-title":"Acta Neuropathol."},{"key":"ref_110","doi-asserted-by":"crossref","first-page":"271","DOI":"10.1097\/NEN.0b013e31816a12a6","article-title":"TAR DNA-binding protein 43 immunohistochemistry reveals extensive neuritic pathology in FTLD-U: A midwest-southwest consortium for FTLD study","volume":"67","author":"Hatanpaa","year":"2008","journal-title":"J. Neuropathol. Exp. Neurol."},{"key":"ref_111","doi-asserted-by":"crossref","first-page":"142","DOI":"10.1097\/nen.0b013e31803020cf","article-title":"Neuropathologic features of frontotemporal lobar degeneration with ubiquitin-positive inclusions with progranulin gene (PGRN) mutations","volume":"66","author":"Josephs","year":"2007","journal-title":"J. Neuropathol. Exp. Neurol."},{"key":"ref_112","doi-asserted-by":"crossref","first-page":"245","DOI":"10.1016\/j.neuron.2011.09.011","article-title":"Expanded GGGGCC hexanucleotide repeat in noncoding region of C9ORF72 causes chromosome 9p-linked FTD and ALS","volume":"72","author":"Mackenzie","year":"2011","journal-title":"Neuron"},{"key":"ref_113","doi-asserted-by":"crossref","first-page":"319","DOI":"10.1007\/s00401-014-1253-7","article-title":"The C9ORF72 expansion mutation: Gene structure, phenotypic and diagnostic issues","volume":"127","author":"Woollacott","year":"2014","journal-title":"Acta Neuropathol."},{"key":"ref_114","doi-asserted-by":"crossref","first-page":"323","DOI":"10.1016\/S1474-4422(12)70043-1","article-title":"Frequency of the C9orf72 hexanucleotide repeat expansion in patients with amyotrophic lateral sclerosis and frontotemporal dementia: A cross-sectional study","volume":"11","author":"Majounie","year":"2012","journal-title":"Lancet Neurol."},{"key":"ref_115","doi-asserted-by":"crossref","first-page":"991","DOI":"10.1517\/14728222.2013.818659","article-title":"c9RAN translation: A potential therapeutic target for the treatment of amyotrophic lateral sclerosis and frontotemporal dementia","volume":"17","author":"Gendron","year":"2013","journal-title":"Expert Opin. Ther. Targets"},{"key":"ref_116","doi-asserted-by":"crossref","first-page":"1335","DOI":"10.1126\/science.1232927","article-title":"The C9orf72 GGGGCC repeat is translated into aggregating dipeptide-repeat proteins in FTLD\/ALS","volume":"339","author":"Mori","year":"2013","journal-title":"Science"},{"key":"ref_117","first-page":"57","article-title":"Brain pathology in myotonic dystrophy: When tauopathy meets spliceopathy and RNAopathy","volume":"6","author":"Tran","year":"2014","journal-title":"Front. Mol. Neurosci."},{"key":"ref_118","doi-asserted-by":"crossref","first-page":"668","DOI":"10.1038\/nn.4272","article-title":"C9ORF72 poly(GA) aggregates sequester and impair HR23 and nucleocytoplasmic transport proteins","volume":"19","author":"Zhang","year":"2016","journal-title":"Nat. Neurosci."},{"key":"ref_119","doi-asserted-by":"crossref","first-page":"407","DOI":"10.1007\/s00401-013-1239-x","article-title":"TMEM106B is a genetic modifier of frontotemporal lobar degeneration with C9orf72 hexanucleotide repeat expansions","volume":"127","author":"Gallagher","year":"2014","journal-title":"Acta Neuropathol."},{"key":"ref_120","doi-asserted-by":"crossref","first-page":"709","DOI":"10.1093\/brain\/awr354","article-title":"Clinical and pathological features of familial frontotemporal dementia caused by C9ORF72 mutation on chromosome 9p","volume":"135","author":"Hsiung","year":"2012","journal-title":"Brain"},{"key":"ref_121","doi-asserted-by":"crossref","first-page":"470","DOI":"10.1002\/ana.21612","article-title":"TARDBP mutations in motoneuron disease with frontotemporal lobar degeneration","volume":"65","author":"Benajiba","year":"2009","journal-title":"Ann. Neurol."},{"key":"ref_122","doi-asserted-by":"crossref","first-page":"R38","DOI":"10.1093\/hmg\/ddq157","article-title":"Inclusion body myopathy, Paget\u2019s disease of the bone and fronto-temporal dementia: A disorder of autophagy","volume":"19","author":"Ju","year":"2010","journal-title":"Hum. Mol. Genet."},{"key":"ref_123","doi-asserted-by":"crossref","first-page":"1205","DOI":"10.1126\/science.1166066","article-title":"Mutations in the FUS\/TLS gene on chromosome 16 cause familial amyotrophic lateral sclerosis","volume":"323","author":"Kwiatkowski","year":"2009","journal-title":"Science"},{"key":"ref_124","doi-asserted-by":"crossref","first-page":"152","DOI":"10.1097\/nen.0b013e31803020b9","article-title":"TDP-43 in the ubiquitin pathology of frontotemporal dementia with VCP gene mutations","volume":"66","author":"Neumann","year":"2007","journal-title":"J. Neuropathol. Exp. Neurol."},{"key":"ref_125","doi-asserted-by":"crossref","first-page":"1208","DOI":"10.1126\/science.1165942","article-title":"Mutations in FUS, an RNA processing protein, cause familial amyotrophic lateral sclerosis type 6","volume":"323","author":"Vance","year":"2009","journal-title":"Science"},{"key":"ref_126","doi-asserted-by":"crossref","first-page":"2595","DOI":"10.1093\/brain\/awr201","article-title":"FET proteins TAF15 and EWS are selective markers that distinguish FTLD with FUS pathology from amyotrophic lateral sclerosis with FUS mutations","volume":"134","author":"Neumann","year":"2011","journal-title":"Brain"},{"key":"ref_127","doi-asserted-by":"crossref","first-page":"605","DOI":"10.1007\/s00401-009-0581-5","article-title":"Abundant FUS-immunoreactive pathology in neuronal intermediate filament inclusion disease","volume":"118","author":"Neumann","year":"2009","journal-title":"Acta Neuropathol."},{"key":"ref_128","doi-asserted-by":"crossref","first-page":"355","DOI":"10.1146\/annurev-biochem-060614-034325","article-title":"Biochemical Properties and Biological Functions of FET Proteins","volume":"84","author":"Schwartz","year":"2015","journal-title":"Annu. Rev. Biochem."},{"key":"ref_129","doi-asserted-by":"crossref","first-page":"1488","DOI":"10.1038\/nn.3230","article-title":"Divergent roles of ALS-linked proteins FUS\/TLS and TDP-43 intersect in processing long pre-mRNAs","volume":"15","author":"Polymenidou","year":"2012","journal-title":"Nat. Neurosci."},{"key":"ref_130","doi-asserted-by":"crossref","first-page":"4258","DOI":"10.1038\/emboj.2012.261","article-title":"Arginine methylation next to the PY-NLS modulates Transportin binding and nuclear import of FUS","volume":"31","author":"Dormann","year":"2012","journal-title":"EMBO J."},{"key":"ref_131","doi-asserted-by":"crossref","first-page":"1376","DOI":"10.1212\/01.WNL.0000139809.16817.DD","article-title":"Clinical and neuropathologic variation in neuronal intermediate filament inclusion disease","volume":"63","author":"Cairns","year":"2004","journal-title":"Neurology"},{"key":"ref_132","doi-asserted-by":"crossref","first-page":"617","DOI":"10.1007\/s00401-009-0598-9","article-title":"FUS pathology in basophilic inclusion body disease","volume":"118","author":"Munoz","year":"2009","journal-title":"Acta Neuropathol."},{"key":"ref_133","doi-asserted-by":"crossref","first-page":"2841","DOI":"10.1038\/emboj.2010.143","article-title":"ALS-associated fused in sarcoma (FUS) mutations disrupt Transportin-mediated nuclear import","volume":"29","author":"Dormann","year":"2010","journal-title":"EMBO J."},{"key":"ref_134","doi-asserted-by":"crossref","first-page":"285","DOI":"10.1002\/ajmg.b.31158","article-title":"Mutational analysis reveals the FUS homolog TAF15 as a candidate gene for familial amyotrophic lateral sclerosis","volume":"156B","author":"Ticozzi","year":"2011","journal-title":"Am. J. Med. Genet. B Neuropsychiatr. Genet."},{"key":"ref_135","doi-asserted-by":"crossref","first-page":"33","DOI":"10.1007\/s00401-010-0698-6","article-title":"FUS pathology defines the majority of Tau- and TDP-43-negative frontotemporal lobar degeneration","volume":"120","author":"Urwin","year":"2010","journal-title":"Acta Neuropathol."},{"key":"ref_136","doi-asserted-by":"crossref","first-page":"2235.e11","DOI":"10.1016\/j.neurobiolaging.2013.04.004","article-title":"Mutations in protein N-arginine methyltransferases are not the cause of FTLD-FUS","volume":"34","author":"Ravenscroft","year":"2013","journal-title":"Neurobiol. Aging"},{"key":"ref_137","doi-asserted-by":"crossref","first-page":"357","DOI":"10.1038\/77153","article-title":"Loss-of-function mutations in TYROBP (DAP12) result in a presenile dementia with bone cysts","volume":"25","author":"Paloneva","year":"2000","journal-title":"Nat. Genet."},{"key":"ref_138","doi-asserted-by":"crossref","first-page":"200","DOI":"10.1038\/ng.1027","article-title":"Mutations in the colony stimulating factor 1 receptor (CSF1R) gene cause hereditary diffuse leukoencephalopathy with spheroids","volume":"44","author":"Rademakers","year":"2011","journal-title":"Nat. Genet."},{"key":"ref_139","doi-asserted-by":"crossref","first-page":"1361","DOI":"10.1093\/brain\/awu067","article-title":"PRKAR1B mutation associated with a new neurodegenerative disorder with unique pathology","volume":"137","author":"Wong","year":"2014","journal-title":"Brain"}],"container-title":["Brain Sciences"],"original-title":[],"language":"en","link":[{"URL":"https:\/\/www.mdpi.com\/2076-3425\/13\/10\/1474\/pdf","content-type":"unspecified","content-version":"vor","intended-application":"similarity-checking"}],"deposited":{"date-parts":[[2025,10,10]],"date-time":"2025-10-10T21:09:07Z","timestamp":1760130547000},"score":1,"resource":{"primary":{"URL":"https:\/\/www.mdpi.com\/2076-3425\/13\/10\/1474"}},"subtitle":[],"short-title":[],"issued":{"date-parts":[[2023,10,18]]},"references-count":139,"journal-issue":{"issue":"10","published-online":{"date-parts":[[2023,10]]}},"alternative-id":["brainsci13101474"],"URL":"https:\/\/doi.org\/10.3390\/brainsci13101474","relation":{},"ISSN":["2076-3425"],"issn-type":[{"value":"2076-3425","type":"electronic"}],"subject":[],"published":{"date-parts":[[2023,10,18]]}}}