Student or educator? Sign up with your school email and get 6 months of Pro free.
CoChat
Sign Up
Cited by 46

The DOI matches its Crossref record; 35 of the 35 references it cites were found in a registry or an index.

Genetic forms of tauopathies: inherited causes and implications of Alzheimer’s disease-like TAU pathology in primary and secondary tauopathies

Langerscheidt, Felix, Wied, Tamara, Al Kabbani, Mohamed Aghyad, van Eimeren, Thilo, Wunderlich, Gilbert, Zempel, Hans·2024·Journal of Neurology
DOI 10.1007/s00415-024-12314-3PMC PMC11136742
Open this paper in CoChat — free account

Abstract

Tauopathies are a heterogeneous group of neurologic diseases characterized by pathological axodendritic distribution, ectopic expression, and/or phosphorylation and aggregation of the microtubule-associated protein TAU, encoded by the gene MAPT. Neuronal dysfunction, dementia, and neurodegeneration are common features of these often detrimental diseases. A neurodegenerative disease is considered a primary tauopathy when MAPT mutations/haplotypes are its primary cause and/or TAU is the main pathological feature. In case TAU pathology is observed but superimposed by another pathological hallmark, the condition is classified as a secondary tauopathy. In some tauopathies (e.g. MAPT-associated frontotemporal dementia (FTD), progressive supranuclear palsy (PSP), corticobasal degeneration (CBD), and Alzheimer's disease (AD)) TAU is recognized as a significant pathogenic driver of the disease. In many secondary tauopathies, including Parkinson's disease (PD) and Huntington's disease (HD), TAU is suggested to contribute to the development of dementia, but in others (e.g. Niemann-Pick disease (NPC)) TAU may only be a bystander. The genetic and pathological mechanisms underlying TAU pathology are often not fully understood. In this review, the genetic predispositions and variants associated with both primary and secondary tauopathies are examined in detail, assessing evidence for the role of TAU in these conditions. We highlight less common genetic forms of tauopathies to increase awareness for these disorders and the involvement of TAU in their pathology. This approach not only contributes to a deeper understanding of these conditions but may also lay the groundwork for potential TAU-based therapeutic interventions for various tauopathies.

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.

A few free checks a day · papers already verified open instantly · results are public

Integrity signals

Registry

Crossref · 10.1007/s00415-024-12314-3

Cites

35 of 35 references verified0 citation errors · 0 not checkable

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.

A few free checks a day · papers already verified open instantly · results are public

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?

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

Show all 35 references

Research works printed but not linked: 245

  1. Götz J, Halliday G, Nisbet RM (2019) Molecular pathogenesis of the tauopathies. Annu Rev Pathol 14:239–261. https://doi.org/10.1146/annurev-pathmechdis-012418-012936 · DOI · Paper page
  2. Zimmer-Bensch G, Zempel H (2021) Dna methylation in genetic and sporadic forms of neurodegeneration: lessons from Alzheimer’s, related tauopathies and genetic tauopathies. Cells 10:5. https://doi.org/10.3390/cells10113064 · DOI
  3. Guo T, Noble W, Hanger DP (2017) Roles of tau protein in health and disease. Acta Neuropathol 133:665–704. https://doi.org/10.1007/s00401-017-1707-9 · DOI · Paper page
  4. Andreadis A (2012) Tau splicing and the intricacies of dementia. J Cell Physiol 227:1220–1225. https://doi.org/10.1002/jcp.22842 · DOI
  5. Goedert M, Spillantini MG, Jakes R, Rutherford D, Crowther RA (1989) Multiple isoforms of human microtubule-associated protein tau: sequences and localization in neurofibrillary tangles of Alzheimer’s disease. Neuron 3:519–526. https://doi.org/10.1016/0896-6273(89)90210-9 · DOI · Paper page
  6. Goedert M, Spillantini MG, Crowther RA (1992) Cloning of a big tau microtubule-associated protein characteristic of the peripheral nervous system. Proc Natl Acad Sci 89:1983–1987. https://doi.org/10.1073/pnas.89.5.1983 · DOI
  7. Fischer I (2023) Big tau: what we know, and we need to know. Eneuro 10:ENEURO.0052-23.2023. https://doi.org/10.1523/ENEURO.0052-23.2023 · DOI
  8. Zempel H, Mandelkow E (2019) Mechanisms of axonal sorting of tau and influence of the axon initial segment on tau cell polarity. pp 69–77 · DOI
  9. Zempel H, Mandelkow E (2014) Lost after translation: missorting of tau protein and consequences for Alzheimer disease. Trends Neurosci 37:721–732. https://doi.org/10.1016/j.tins.2014.08.004 · DOI · Paper page
  10. Kovacs GG, Ghetti B, Goedert M (2022) Classification of diseases with accumulation of tau protein. Neuropathol Appl Neurobiol 48:5. https://doi.org/10.1111/nan.12792 · DOI
  11. Goedert M, Falcon B, Zhang W, Ghetti B, Scheres SHW (2018) Distinct conformers of assembled tau in Alzheimer’s and Pick’s diseases. Cold Spring Harb Symp Quant Biol 83:163–171. https://doi.org/10.1101/sqb.2018.83.037580 · DOI
  12. Sexton C, Snyder H, Beher D, Boxer AL, Brannelly P, Brion J, Buée L, Cacace AM, Chételat G, Citron M, DeVos SL, Diaz K, Feldman HH, Frost B, Goate AM, Gold M, Hyman B, Johnson K, Karch CM, Kerwin DR, Koroshetz WJ, Litvan I, Morris HR, Mummery CJ, Mutamba J, Patterson MC, Quiroz YT, Rabinovici GD, Rommel A, Shulman MB, Toledo-Sherman LM, Weninger S, Wildsmith KR, Worley SL, Carrillo MC (2022) Current directions in tau research: highlights from tau 2020. Alzheimer’s Dementia 18:988–1007. https://doi.org/10.1002/alz.12452 · DOI
  13. Caroppo P, Prioni S, Maderna E, Grisoli M, Rossi G (2021) New MAPT variant in a FTD patient with Alzheimer’s disease phenotype at onset. Neurol Sci 42:2111–2114. https://doi.org/10.1007/s10072-020-04901-9 · DOI
  14. Keszycki R, Kawles A, Minogue G, Zouridakis A, Macomber A, Gill N, Vu M, Zhang H, Coventry C, Rogalski E, Weintraub S, Mesulam M-M, Geula C, Gefen T (2023) Distinct and shared neuropsychiatric phenotypes in FTLD-tauopathies. Front Aging Neurosci 15:5. https://doi.org/10.3389/fnagi.2023.1164581 · DOI
  15. Chung DC, Roemer S, Petrucelli L, Dickson DW (2021) Cellular and pathological heterogeneity of primary tauopathies. Mol Neurodegener 16:57. https://doi.org/10.1186/s13024-021-00476-x · DOI
  16. Rösler TW, Tayaranian Marvian A, Brendel M, Nykänen NP, Höllerhage M, Schwarz SC, Hopfner F, Koeglsperger T, Respondek G, Schweyer K, Levin J, Villemagne VL, Barthel H, Sabri O, Müller U, Meissner WG, Kovacs GG, Höglinger GU (2019) Four-repeat tauopathies. Progress Neurobiol, Elsevier Ltd. https://doi.org/10.1016/j.pneurobio.2019.101644 · DOI
  17. Kovacs G (2014) Current concepts of neurodegenerative diseases. EMJ Neurology. https://doi.org/10.33590/emjneurol/10314777 · DOI
  18. Kovacs G (2015) Invited review: neuropathology of tauopathies: principles and practice. Neuropathol Appl Neurobiol 41:3–23. https://doi.org/10.1111/nan.12208 · DOI · Paper page
  19. Kovacs G (2014) Introduction. Neuropathology of Neurodegenerative diseases. Cambridge University Press, pp 1–7 · DOI
  20. Irwin DJ (2016) Tauopathies as clinicopathological entities. Parkinsonism Relat Disord Elsevier Ltd 22:S29–S33. https://doi.org/10.1016/j.parkreldis.2015.09.020 · DOI
  21. Benussi A, Padovani A, Borroni B (2015) Phenotypic heterogeneity of monogenic frontotemporal dementia. Front Aging Neurosci. https://doi.org/10.3389/fnagi.2015.00171 · DOI
  22. Borroni B, Graff C, Hardiman O, Ludolph AC, Moreno F, Otto M, Piccininni M, Remes AM, Rowe JB, Seelaar H, Stefanova E, Traykov L, Logroscino G (2022) FRONTotemporal dementia incidence european research study—FRONTIERS: rationale and design. Alzheimer’s Dementia 18:498–506. https://doi.org/10.1002/alz.12414 · DOI
  23. Goedert M, Jakes R (2005) Mutations causing neurodegenerative tauopathies. Biochimica et Biophysica Acta BBA Mol Basis Dis 1739:240–250. https://doi.org/10.1016/j.bbadis.2004.08.007 · DOI · Paper page
  24. Garrett SL, McDaniel D, Obideen M, Trammell AR, Shaw LM, Goldstein FC, Hajjar I (2019) Racial disparity in cerebrospinal fluid amyloid and tau biomarkers and associated cutoffs for mild cognitive impairment. JAMA Netw Open 2:e1917363. https://doi.org/10.1001/jamanetworkopen.2019.17363 · DOI
  25. Hasegawa M, Smith MJ, Goedert M (1998) Tau proteins with FTDP-17 mutations have a reduced ability to promote microtubule assembly. FEBS Lett 437:207–210. https://doi.org/10.1016/S0014-5793(98)01217-4 · DOI
  26. Hong M, Zhukareva V, Vogelsberg-Ragaglia V, Wszolek Z, Miller B, Geschwind D, Bird T, McKeel D, Goate A, Morris J, Wilhelmsen K, Schellenberg G, Trojanowski J, Lee V (1998) Mutation-specific functional impairments in distinct tau isoforms of hereditary FTDP-17. Science 282:1914–1917. https://doi.org/10.1126/science.282.5395.1914 · DOI
  27. Dawson HN, Ferreira A, Eyster MV, Ghoshal N, Binder LI, Vitek MP (2001) Inhibition of neuronal maturation in primary hippocampal neurons from tau deficient mice. J Cell Sci 114:1179–1187. https://doi.org/10.1242/jcs.114.6.1179 · DOI · Paper page
  28. Harada A, Oguchi K, Okabe S, Kuno J, Terada S, Ohshima T, Sato-Yoshitake R, Takei Y, Noda T, Hirokawa N (1994) Altered microtubule organization in small-calibre axons of mice lacking tau protein. Nature 369:488–491. https://doi.org/10.1038/369488a0 · DOI · Paper page
  29. Olszewska DA, Fearon C, McGuigan C, McVeigh TP, Houlden H, Polke JM, Lawlor B, Coen R, Hutchinson M, Hutton M, Beausang A, Delon I, Brett F, Sevastou I, Seto-Salvia N, de Silva R, Lynch T (2021) A clinical, molecular genetics and pathological study of a FTDP-17 family with a heterozygous splicing variant c.823-10G>T at the intron 9/exon 10 of the MAPT gene. Neurobiol Aging 106:343.e1-343.e8. https://doi.org/10.1016/j.neurobiolaging.2021.05.010 · DOI
  30. Rossi G, Tagliavini F (2015) Frontotemporal lobar degeneration: old knowledge and new insight into the pathogenetic mechanisms of tau mutations. Front Aging Neurosci. https://doi.org/10.3389/fnagi.2015.00192 · DOI
  31. Gauthier-Kemper A, Weissmann C, Golovyashkina N, Sebö-Lemke Z, Drewes G, Gerke V, Heinisch JJ, Brandt R (2011) The frontotemporal dementia mutation R406W Blocks Tau’s interaction with the membrane in an annexin A2–dependent manner. J Cell Biol 192:647–661. https://doi.org/10.1083/jcb.201007161 · DOI
  32. Iqbal K, Liu F, Gong C-X, Alonso A del C, Grundke-Iqbal I (2009) Mechanisms of tau-induced neurodegeneration. Acta Neuropathol 118:53–69. https://doi.org/10.1007/s00401-009-0486-3 · DOI · Paper page
  33. Alonso A del C, Mederlyova A, Novak M, Grundke-Iqbal I, Iqbal K (2004) Promotion of hyperphosphorylation by frontotemporal dementia tau mutations. J Biol Chem 279:34873–34881. https://doi.org/10.1074/jbc.M405131200 · DOI
  34. Goedert M, Spillantini MG (2000) Tau mutations in frontotemporal dementia FTDP-17 and their relevance for Alzheimer’s disease. Biochimica et Biophysica Acta BBA Mol Basis Dis 1502:110–121. https://doi.org/10.1016/S0925-4439(00)00037-5 · DOI
  35. Imbimbo BP, Ippati S, Watling M, Balducci C (2022) A critical appraisal of tau-targeting therapies for primary and secondary tauopathies. Alzheimer’s Dementia 18:1008–1037. https://doi.org/10.1002/alz.12453 · DOI
  36. Roth JR, Rush T, Thompson SJ, Aldaher AR, Dunn TB, Mesina JS, Cochran JN, Boyle NR, Dean HB, Yang Z, Pathak V, Ruiz P, Wu M, Day JJ, Bostwick JR, Suto MJ, Augelli-Szafran CE, Roberson ED (2024) Development of small-molecule Tau-SH3 interaction inhibitors that prevent amyloid-β toxicity and network hyperexcitability. Neurotherapeutics 21:e00291. https://doi.org/10.1016/j.neurot.2023.10.001 · DOI
  37. Zhang Z-Y, Harischandra DS, Wang R, Ghaisas S, Zhao JY, McMonagle TP, Zhu G, Lacuarta KD, Song J, Trojanowski JQ, Xu H, Lee VM-Y, Yang X (2023) TRIM11 protects against tauopathies and is down-regulated in Alzheimer’s disease. Science. https://doi.org/10.1126/science.add6696 · DOI
  38. Höglinger GU, Melhem NM, Dickson DW, Sleiman PMA, Wang L-S, Klei L, Rademakers R, de Silva R, Litvan I, Riley DE, van Swieten JC, Heutink P, Wszolek ZK, Uitti RJ, Vandrovcova J, Hurtig HI, Gross RG, Maetzler W, Goldwurm S, Tolosa E, Borroni B, Pastor P, Cantwell LB, Han MR, Dillman A, van der Brug MP, Gibbs JR, Cookson MR, Hernandez DG, Singleton AB, Farrer MJ, Yu C-E, Golbe LI, Revesz T, Hardy J, Lees AJ, Devlin B, Hakonarson H, Müller U, Schellenberg GD (2011) Identification of common variants influencing risk of the tauopathy progressive supranuclear palsy. Nat Genet 43:699–705. https://doi.org/10.1038/ng.859 · DOI · Paper page
  39. Valentino RR, Koga S, Walton RL, Soto-Beasley AI, Kouri N, DeTure MA, Murray ME, Johnson PW, Petersen RC, Boeve BF, Uitti RJ, Wszolek ZK, Dickson DW, Ross OA, Heckman MG (2020) MAPT subhaplotypes in corticobasal degeneration: assessing associations with disease risk, severity of tau pathology, and clinical features. Acta Neuropathol Commun. https://doi.org/10.1186/s40478-020-01097-z · DOI
  40. Wen Y, Zhou Y, Jiao B, Shen L (2021) Genetics of progressive supranuclear palsy: a review. J Parkinson’s Dis. https://doi.org/10.3233/JPD-202302 · DOI
  41. Probst A, Langui D, Lautenschlager C, Ulrich J, Brion JP, Anderton BH (1988) Progressive supranuclear palsy: extensive neuropil threads in addition to neurofibrillary tangles. Acta Neuropathol 77:61–68. https://doi.org/10.1007/BF00688244 · DOI
  42. Yamada T, McGeer PL, McGeer EG (1992) Appearance of paired nucleated, tau-positive glia in patients with progressive supranuclear palsy brain tissue. Neurosci Lett 135:99–102. https://doi.org/10.1016/0304-3940(92)90145-W · DOI
  43. Rowe JB, Holland N, Rittman T (2021) Progressive supranuclear palsy: diagnosis and management. Pract Neurol 21:376–383. https://doi.org/10.1136/practneurol-2020-002794 · DOI
  44. Li Y, Chen JA, Sears RL, Gao F, Klein ED, Karydas A, Geschwind MD, Rosen HJ, Boxer AL, Guo W, Pellegrini M, Horvath S, Miller BL, Geschwind DH, Coppola G (2014) An epigenetic signature in peripheral blood associated with the haplotype on 17q21.31, a risk factor for neurodegenerative tauopathy. PLoS Genet 10:e1004211. https://doi.org/10.1371/journal.pgen.1004211 · DOI
  45. Debnath M, Dey S, Sreenivas N, Pal PK, Yadav R (2022) Genetic and epigenetic constructs of progressive supranuclear palsy. Ann Neurosci 29:177–188. https://doi.org/10.1177/09727531221089396 · DOI
  46. Jabbari E, Koga S, Valentino RR, Reynolds RH, Ferrari R, Tan MMX, Rowe JB, Dalgard CL, Scholz SW, Dickson DW, Warner TT, Revesz T, Höglinger GU, Ross OA, Ryten M, Hardy J, Shoai M, Morris HR, Mok KY, Murphy DP, Al-Sarraj S, Troakes C, Gentleman SM, Allinson KSJ, Jaunmuktane Z, Holton JL, Lees AJ, Morris CM, Compta Y, Gelpi E, van Swieten JC, Rajput A, Ferguson L, Cookson MR, Gibbs JR, Blauwendraat C, Ding J, Chia R, Traynor BJ, Pantelyat A, Viollet C, Traynor BJ, Pletnikova O, Troncoso JC, Rosenthal LS, Boxer AL, Respondek G, Arzberger T, Roeber S, Giese A, Burn DJ, Pavese N, Gerhard A, Kobylecki C, Leigh PN, Church A, Hu M (2021) Genetic determinants of survival in progressive supranuclear palsy: a genome-wide association study. Lancet Neurol 20:107–116. https://doi.org/10.1016/S1474-4422(20)30394-X · DOI · Paper page
  47. Melquist S, Craig DW, Huentelman MJ, Crook R, Pearson JV, Baker M, Zismann VL, Gass J, Adamson J, Szelinger S, Corneveaux J, Cannon A, Coon KD, Lincoln S, Adler C, Tuite P, Calne DB, Bigio EH, Uitti RJ, Wszolek ZK, Golbe LI, Caselli RJ, Graff-Radford N, Litvan I, Farrer MJ, Dickson DW, Hutton M, Stephan DA (2007) Identification of a novel risk locus for progressive supranuclear palsy by a pooled genomewide scan of 500,288 single-nucleotide polymorphisms. Am J Human Genetics 80:769–778. https://doi.org/10.1086/513320 · DOI
  48. Chen JA, Chen Z, Won H, Huang AY, Lowe JK, Wojta K, Yokoyama JS, Bensimon G, Leigh PN, Payan C, Shatunov A, Jones AR, Lewis CM, Deloukas P, Amouyel P, Tzourio C, Dartigues J-F, Ludolph A, Boxer AL, Bronstein JM, Al-Chalabi A, Geschwind DH, Coppola G (2018) Joint genome-wide association study of progressive supranuclear palsy identifies novel susceptibility loci and genetic correlation to neurodegenerative diseases. Mol Neurodegener 13:41. https://doi.org/10.1186/s13024-018-0270-8 · DOI
  49. Couto B, Martinez-Valbuena I, Lee S, Alfradique-Dunham I, Perrin RJ, Perlmutter JS, Cruchaga C, Kim A, Visanji N, Sato C, Rogaeva E, Lang AE, Kovacs GG (2022) Protracted course progressive supranuclear palsy. Eur J Neurol 29:2220–2231. https://doi.org/10.1111/ene.15346 · DOI
  50. Mahapatra RK, Edwards MJ, Schott JM, Bhatia KP (2004) Corticobasal degeneration. Lancet Neurol 3:736–743. https://doi.org/10.1016/S1474-4422(04)00936-6 · DOI
  51. Dickson DW (2009) Sporadic Tauopathies: Pick’s disease, corticobasal, degeneration progressive supranuclear palsy and argyrophilic grain disease. The neuropathology of Dementia. Cambridge University Press, pp 227–256
  52. Dickson DW (1999) Neuropathologic differentiation of progressive supranuclear palsy and corticobasal degeneration. J Neurol 246:II6–II15. https://doi.org/10.1007/BF03161076 · DOI
  53. Gibb WRG, Luthert PJ, Marsden CD (1989) Corticobasal degeneration. Brain. http://brain.oxfordjournals.org/ · DOI
  54. Feany MB, Dickson DW (1995) Widespread cytoskeletal pathology characterizes corticobasal degeneration. Am J Pathol 146:1388
  55. Uchihara T (2014) Pretangles and neurofibrillary changes: similarities and differences between AD and CBD based on molecular and morphological evolution. Neuropathology 34:571–577. https://doi.org/10.1111/neup.12108 · DOI
  56. Komori T, Arai N, Oda M, Nakayama H, Mori H, Yagishita S, Takahashi T, Amano N, Murayama S, Murakami S, Shibata N, Kobayashi M, Sasaki S, Iwata M (1998) Astrocytic plaques and tufts of abnormal fibers do not coexist in corticobasal degeneration and progressive supranuclear palsy. Acta Neuropathol 96:401–408. https://doi.org/10.1007/s004010050911 · DOI
  57. Leveille E, Ross OA, Gan-Or Z (2021) Tau and MAPT genetics in tauopathies and synucleinopathies. Parkinsonism Relat Disord 90:142–154. https://doi.org/10.1016/j.parkreldis.2021.09.008 · DOI
  58. Donnelly MP, Paschou P, Grigorenko E, Gurwitz D, Mehdi SQ, Kajuna SLB, Barta C, Kungulilo S, Karoma NJ, Lu R-B, Zhukova OV, Kim J-J, Comas D, Siniscalco M, New M, Li P, Li H, Manolopoulos VG, Speed WC, Rajeevan H, Pakstis AJ, Kidd JR, Kidd KK (2010) The distribution and most recent common ancestor of the 17q21 inversion in humans. Am J Human Genetics 86:161–171. https://doi.org/10.1016/j.ajhg.2010.01.007 · DOI
  59. Strickland SL, Reddy JS, Allen M, N’songo A, Burgess JD, Corda MM, Ballard T, Wang X, Carrasquillo MM, Biernacka JM, Jenkins GD, Mukherjee S, Boehme K, Crane P, Kauwe JS, Ertekin-Taner N (2020) MAPT haplotype-stratified GWAS reveals differential association for AD risk variants. Alzheimer’s Dementia 16:983–1002. https://doi.org/10.1002/alz.12099 · DOI
  60. Heckman MG, Brennan RR, Labbé C, Soto AI, Koga S, DeTure MA, Murray ME, Petersen RC, Boeve BF, van Gerpen JA, Uitti RJ, Wszolek ZK, Rademakers R, Dickson DW, Ross OA (2019) Association of MAPT subhaplotypes with risk of progressive supranuclear palsy and severity of tau pathology. JAMA Neurol 76:710. https://doi.org/10.1001/jamaneurol.2019.0250 · DOI
  61. Miguel L, Frebourg T, Campion D, Lecourtois M (2020) Moderate overexpression of tau in drosophila exacerbates amyloid-β-induced neuronal phenotypes and correlates with tau oligomerization. J Alzheimer’s Dis 74:637–647. https://doi.org/10.3233/JAD-190906 · DOI
  62. Zhang W, Tarutani A, Newell KL, Murzin AG, Matsubara T, Falcon B, Vidal R, Garringer HJ, Shi Y, Ikeuchi T, Murayama S, Ghetti B, Hasegawa M, Goedert M, Scheres SHW (2020) Novel tau filament fold in corticobasal degeneration. Nature 580:283–287. https://doi.org/10.1038/s41586-020-2043-0 · DOI
  63. Canu E, Boccardi M, Ghidoni R, Benussi L, Testa C, Pievani M, Bonetti M, Binetti G, Frisoni GB (2009) H1 haplotype of the MAPT gene is associated with lower regional gray matter volume in healthy carriers. Eur J Hum Genet 17:287–294. https://doi.org/10.1038/ejhg.2008.185 · DOI
  64. Falcon B, Zhang W, Murzin AG, Murshudov G, Garringer HJ, Vidal R, Crowther RA, Ghetti B, Scheres SHW, Goedert M (2018) Structures of filaments from Pick’s disease reveal a novel tau protein fold. Nature 561:137–140. https://doi.org/10.1038/s41586-018-0454-y · DOI
  65. Ikeda C, Yokota O, Miki T, Takenoshita S, Ishizu H, Mori Y, Yamazaki K, Ozaki Y, Ueno S-I, Ishihara T, Hasegawa M, Terada S, Yamada N (2017) Pick’s disease with neuronal four-repeat tau accumulation in the basal ganglia, brain stem nuclei and cerebellum. Neuropathology 37:544–559. https://doi.org/10.1111/neup.12394 · DOI
  66. Dickson DW (1998) Pick’s disease: a modern approach. Brain Pathol 8:339–354. https://doi.org/10.1111/j.1750-3639.1998.tb00158.x · DOI
  67. Olfati N, Shoeibi A, Litvan I (2022) Clinical spectrum of tauopathies. Front Neurol. https://doi.org/10.3389/fneur.2022.944806 · DOI
  68. Lilly R, Cummings JL, Benson DF, Frankel M (1983) The human Klüver-Bucy syndrome. Neurology 33:1141–1141. https://doi.org/10.1212/WNL.33.9.1141 · DOI
  69. Bronner IF, Ter Meulen BC, Azmani A, Severijnen LA, Willemsen R, Kamphorst W, Ravid R, Heutink P, Van Swieten JC (2005) Hereditary Pick’s disease with the G272V tau mutation shows predominant three-repeat tau pathology. Brain 128:2645–2653. https://doi.org/10.1093/brain/awh591 · DOI
  70. Schweighauser M, Garringer HJ, Klingstedt T, Nilsson KPR, Masuda-Suzukake M, Murrell JR, Risacher SL, Vidal R, Scheres SHW, Goedert M, Ghetti B, Newell KL (2023) Mutation ∆K281 in MAPT causes Pick’s disease. Acta Neuropathol. https://doi.org/10.1007/s00401-023-02598-6 · DOI
  71. Siano G, Micaelli M, Scarlatti A, Quercioli V, Di Primio C, Cattaneo A (2020) The Q336H MAPT mutation linked to Pick’s disease leads to increased binding of tau to the microtubule network via altered conformational and phosphorylation effects. Front Mol Neurosci 8:13. https://doi.org/10.3389/fnmol.2020.569395 · DOI
  72. Valentino RR, Scotton Mbioch WJ, Roemer SF, Lashley T, Heckman MG, Shoai M, Martinez-Carrasco A, Tamvaka N, Walton RL, Baker MC, Macpherson HL, Real R, Soto-Beasley AI, Mok K, Revesz T, Warner TT, Jaunmuktane Z, Boeve BF, Christopher E.A., Deture M, Duara R, Graff-Radford NR, Josephs KA, Knopman DS, Koga S, Murray ME, Lyons KE, Pahwa R, Parisi JE, Petersen RC, Whitwell J, Grinberg LT, Miller B, Schlereth A, Seeley WW, Spina S, Grossman M, Irwin DJ, Lee EB, Suh E, Trojanowski JQ, Van Deerlin VM, Wolk DA, Connors TR, Dooley PM, Frosch MP, Oakley DH, Aldecoa I, Balasa M, Gelpi E, Borrego-Écija S, Maria de Eugenio Huélamo R, Gascon-Bayarri J, Sánchez-Valle R, Sanz-Cartagena P, Piñol-Ripoll G, Molina-Porcel L, Bigio EH, Flanagan ME, Gefen T, Rogalski EJ, Weintraub S, Redding-Ochoa J, Chang K, Troncoso JC, Prokop S, Newell KL, Ghetti B, Jones M, Richardson A, Robinson AC, Roncaroli F, Snowden J, Allinson K, Green O, Rowe JB, Singh P, Beach TG, Serrano GE, Flowers XE, Goldman JE, Heaps AC, Leskinen SP, Teich AF, Black SE, Keith JL, Masellis M, Bodi I, King A, Sarraj S-A (2023) Creating the Pick’s disease international consortium: association study of MAPT H2 haplotype with risk of Pick’s disease. medRxiv. https://doi.org/10.1101/2023.04.17.23288471. · DOI
  73. Dermaut B, Kumar-Singh S, Engelborghs S, Theuns J, Rademakers R, Saerens J, Pickut BA, Peeters K, Van Den Broeck M, Vennekens K, Claes S, Cruts M, Cras P, Martin J-J, Van Broeckhoven C, De Deyn PP (2004) A novel presenilin 1 mutation associated with Pick’s disease but not ?-Amyloid plaques. Ann Neurol 55:617–626. https://doi.org/10.1002/ana.20083 · DOI
  74. Neumann M, Schulz-Schaeffer W, Anthony Crowther R, Smith MJ, Spillantini MG, Goedert M, Kretzschmar HA (2001) Pick’s disease associated with the novel tau gene mutation K369I. Ann Neurol 50:503–513. https://doi.org/10.1002/ana.1223 · DOI
  75. Tacik P, DeTure M, Hinkle KM, Lin WL, Sanchez-Contreras M, Carlomagno Y, Pedraza O, Rademakers R, Ross OA, Wszolek ZK, Dickson DW (2015) A Novel tau mutation in exon 12, P. Q336H, causes hereditary pick disease. J Neuropathol Exp Neurol 74:1042–1052. https://doi.org/10.1097/NEN.0000000000000248 · DOI
  76. Yoshida K, Hata Y, Ichimata S, Okada K, Nishida N (2023) Argyrophilic grain disease is common in older adults and may be a risk factor for suicide: a study of japanese forensic autopsy cases. Transl Neurodegener 12:16. https://doi.org/10.1186/s40035-023-00352-2 · DOI
  77. Gil MJ, Manzano MS, Cuadrado ML, Fernández C, Góméz E, Matesanz C, Calero M, Rábano A (2018) Argyrophilic grain pathology in frontotemporal lobar degeneration: demographic, clinical, neuropathological, and genetic features. J Alzheimer’s Dis 63:1109–1117. https://doi.org/10.3233/JAD-171115 · DOI
  78. Kovacs G, Pittman A, Revesz T, Luk C, Lees A, Kiss E, Tariska P, Laszlo L, Molnár K, Molnar MJ, Tolnay M, de Silva R (2008) MAPT S305I mutation: implications for argyrophilic grain disease. Acta Neuropathol 116:103–118. https://doi.org/10.1007/s00401-007-0322-6 · DOI
  79. Rönnbäck A, Nennesmo I, Tuominen H, Grueninger F, Viitanen M, Graff C (2014) Neuropathological characterization of two siblings carrying the MAPT S305S mutation demonstrates features resembling argyrophilic grain disease. Acta Neuropathol 127:297–298. https://doi.org/10.1007/s00401-013-1229-z · DOI
  80. Villela D, Kimura L, Schlesinger D, Gonçalves A, Pearson PL, Suemoto CK, Pasqualucci C, Krepischi AC, Grinbergand LT, Rosenberg C (2013) Germline DNA copy number variation in individuals with argyrophilic grain disease reveals CTNS as a plausible candidate gene. Genet Mol Biol 36:498–501. https://doi.org/10.1590/S1415-47572013000400006 · DOI
  81. Das S, Ishaque A (2018) Argyrophilic grain disease: a clinicopathological review of an overlooked tauopathy. Folia Neuropathol 56:277–283. https://doi.org/10.5114/fn.2018.80859 · DOI
  82. Togo T, Sahara N, Yen S-H, Cookson N, Ishizawa T, Hutton M, de Silva R, Lees A, Dickson DW (2002) Argyrophilic grain disease is a sporadic 4-repeat tauopathy. J Neuropathol Exp Neurol 61:547–556. https://doi.org/10.1093/jnen/61.6.547 · DOI · Paper page
  83. Ferrer I (2023) The unique neuropathological vulnerability of the human brain to aging. Ageing Res Rev 87:101916. https://doi.org/10.1016/j.arr.2023.101916 · DOI
  84. Jicha GA, Nelson PT (2019) Hippocampal sclerosis, argyrophilic grain disease, and primary age-related tauopathy. CONTINUUM Lifelong Learning in Neurology 25:208–233. https://doi.org/10.1212/CON.0000000000000697 · DOI
  85. Götz J, Halliday G, Nisbet RM (2018) Molecular pathogenesis of the tauopathies. Annu Rev Pathol Mech Dis. https://doi.org/10.1146/annurev-pathmechdis · DOI
  86. Buciuc M, Koga S, Pham NTT, Duffy JR, Knopman DS, Ali F, Boeve BF, Graff-Radford J, Botha H, Lowe VJ, Nguyen A, Reichard RR, Dickson DW, Petersen RC, Whitwell JL, Josephs KA (2023) The many faces of globular glial tauopathy: a clinical and imaging study. Eur J Neurol 30:321–333. https://doi.org/10.1111/ene.15603 · DOI
  87. Tacik P, DeTure M, Lin WL, Sanchez Contreras M, Wojtas A, Hinkle KM, Fujioka S, Baker MC, Walton RL, Carlomagno Y, Brown PH, Strongosky AJ, Kouri N, Murray ME, Petrucelli L, Josephs KA, Rademakers R, Ross OA, Wszolek ZK, Dickson DW (2015) A novel tau mutation, p. K317N, causes globular glial tauopathy. Acta Neuropathol 130:199–214. https://doi.org/10.1007/s00401-015-1425-0 · DOI
  88. Tacik P, Sanchez-Contreras M, DeTure M, Murray ME, Rademakers R, Ross OA, Wszolek ZK, Parisi JE, Knopman DS, Petersen RC, Dickson DW (2017) Clinicopathologic heterogeneity in frontotemporal dementia and parkinsonism linked to chromosome 17 (FTDP-17) due to microtubule-associated protein tau (MAPT) p. P301L mutation, including a patient with globular glial tauopathy. Neuropathol Appl Neurobiol 43:200–214. https://doi.org/10.1111/nan.12367 · DOI
  89. Kovacs G, Robinson JL, Xie SX, Lee EB, Grossman M, Wolk DA, Irwin DJ, Weintraub D, Kim CF, Schuck T, Yousef A, Wagner ST, Suh E, Van Deerlin VM, Lee VM-Y, Trojanowski JQ (2017) Evaluating the patterns of aging-related tau astrogliopathy unravels novel insights into brain aging and neurodegenerative diseases. J Neuropathol Exp Neurol 76:270–288. https://doi.org/10.1093/jnen/nlx007 · DOI · Paper page
  90. de Silva R, Lashley T, Strand C, Shiarli A-M, Shi J, Tian J, Bailey KL, Davies P, Bigio EH, Arima K, Iseki E, Murayama S, Kretzschmar H, Neumann M, Lippa C, Halliday G, MacKenzie J, Ravid R, Dickson D, Wszolek Z, Iwatsubo T, Pickering-Brown SM, Holton J, Lees A, Revesz T, Mann DMA (2006) An immunohistochemical study of cases of sporadic and inherited frontotemporal lobar degeneration using 3R- and 4R-specific tau monoclonal antibodies. Acta Neuropathol 111:329–340. https://doi.org/10.1007/s00401-006-0048-x · DOI
  91. Iida MA, Farrell K, Walker JM, Richardson TE, Marx GA, Bryce CH, Purohit D, Ayalon G, Beach TG, Bigio EH, Cortes EP, Gearing M, Haroutunian V, McMillan CT, Lee EB, Dickson DW, McKee AC, Stein TD, Trojanowski JQ, Woltjer RL, Kovacs GG, Kofler JK, Kaye J, White CL, Crary JF (2021) Predictors of cognitive impairment in primary age-related tauopathy: an autopsy study. Acta Neuropathol Commun 9:134. https://doi.org/10.1186/s40478-021-01233-3 · DOI
  92. Santa-Maria I, Haggiagi A, Liu X, Wasserscheid J, Nelson PT, Dewar K, Clark LN, Crary JF (2012) The MAPT H1 haplotype is associated with tangle-predominant dementia. Acta Neuropathol 124:693–704. https://doi.org/10.1007/s00401-012-1017-1 · DOI
  93. Crary J (2016) Primary age-related tauopathy and the amyloid cascade hypothesis: the exception that proves the rule? J Neurol Neuromed 1:53–57. https://doi.org/10.29245/2572.942X/2016/6.1059 · DOI
  94. Kovacs G, Yousef A, Kaindl S, Lee VM, Trojanowski JQ (2018) Connexin-43 and aquaporin-4 are markers of ageing-related tau astrogliopathy (ARTAG)-related astroglial response. Neuropathol Appl Neurobiol 44:491–505. https://doi.org/10.1111/nan.12427 · DOI
  95. Rodriguez RD, Grinberg LT (2015) Argyrophilic grain disease: an underestimated tauopathy. Dementia Neuropsychol 9:2–8. https://doi.org/10.1590/S1980-57642015DN91000002 · DOI
  96. Bahia VS, Takada LT, Deramecourt V (2013) Neuropathology of frontotemporal lobar degeneration: a review. Dementia Neuropsychol 7:19–26. https://doi.org/10.1590/S1980-57642013DN70100004 · DOI · Paper page
  97. Mutreja Y, Combs B, Gamblin TC (2019) FTDP-17 mutations alter the aggregation and microtubule stabilization propensity of tau in an isoform-specific fashion. Biochemistry 58:742–754. https://doi.org/10.1021/acs.biochem.8b01039 · DOI
  98. Caroppo P, Le Ber I, Clot F, Rivaud-Péchoux S, Camuzat A, De Septenville A, Boutoleau-Bretonnière C, Mourlon V, Sauvée M, Lebouvier T, Bonnet A-M, Levy R, Vercelletto M, Brice A (2014) DCTN1 mutation analysis in families with progressive supranuclear palsy-like phenotypes. JAMA Neurol 71:208. https://doi.org/10.1001/jamaneurol.2013.5100 · DOI
  99. Olfati N, Ghodsi H, Bayram E, Litvan I (2023) Why therapeutic trials fail in primary tauopathies. Mov Disord 38:545–550. https://doi.org/10.1002/mds.29322 · DOI
  100. Goate A, Chartier-Harlin M-C, Mullan M, Brown J, Crawford F, Fidani L, Giuffra L, Haynes A, Irving N, James L, Mant R, Newton P, Rooke K, Roques P, Talbot C, Pericak-Vance M, Roses A, Williamson R, Rossor M, Owen M, Hardy J (1991) Segregation of a missense mutation in the amyloid precursor protein gene with familial Alzheimer’s disease. Nature 349:704–706. https://doi.org/10.1038/349704a0 · DOI · Paper page
  101. Hardy J, Selkoe DJ (2002) The amyloid hypothesis of Alzheimer’s disease: progress and problems on the road to therapeutics. Science 297:353–356. https://doi.org/10.1126/science.1072994 · DOI · Paper page
  102. Blurton-Jones M, LaFerla F (2006) Pathways by which Aβ facilitates tau pathology. Curr Alzheimer Res 3:437–448. https://doi.org/10.2174/156720506779025242 · DOI
  103. Goedert M (1993) Tau protein and the neurofibrillary pathology of Alzheimer’s disease. Trends Neurosci 16:460–465. https://doi.org/10.1016/0166-2236(93)90078-Z · DOI
  104. Alafuzoff I (2018) Minimal neuropathologic diagnosis for brain banking in the normal middle-aged and aged brain and in neurodegenerative disorders. Handbook Clin Neurol 150:131–141. https://doi.org/10.1016/B978-0-444-63639-3.00010-4 · DOI
  105. Kyalu Ngoie ZN, Balty C, Pyr dit Ruys S, Vanparys AAT, Huyghe NDG, Herinckx G, Johanns M, Boyer E, Kienlen-Campard P, Rider MH, Vertommen D, Hanseeuw BJ (2023) Specific post-translational modifications of soluble tau protein distinguishes Alzheimer’s disease and primary tauopathies. Nat Commun14:3706. https://doi.org/10.1038/s41467-023-39328-1 · DOI
  106. Bellenguez C, Küçükali F, Jansen IE, Kleineidam L, Moreno-Grau S, Amin N, Naj AC, Campos-Martin R, Grenier-Boley B, Andrade V, Holmans PA, Boland A, Damotte V, van der Lee SJ, Costa MR, Kuulasmaa T, Yang Q, de Rojas I, Bis JC, Yaqub A, Prokic I, Chapuis J, Ahmad S, Giedraitis V, Aarsland D, Garcia-Gonzalez P, Abdelnour C, Alarcón-Martín E, Alcolea D, Alegret M, Alvarez I, Álvarez V, Armstrong NJ, Tsolaki A, Antúnez C, Appollonio I, Arcaro M, Archetti S, Pastor AA, Arosio B, Athanasiu L, Bailly H, Banaj N, Baquero M, Barral S, Beiser A, Pastor AB, Below JE, Benchek P, Benussi L, Berr C, Besse C, Bessi V, Binetti G, Bizarro A, Blesa R, Boada M, Boerwinkle E, Borroni B, Boschi S, Bossù P, Bråthen G, Bressler J, Bresner C, Brodaty H, Brookes KJ, Brusco LI, Buiza-Rueda D, Bûrger K, Burholt V, Bush WS, Calero M, Cantwell LB, Chene G, Chung J, Cuccaro ML, Carracedo Á, Cecchetti R, Cervera-Carles L, Charbonnier C, Chen H-H, Chillotti C, Ciccone S, Claassen JAHR, Clark C, Conti E, Corma-Gómez A, Costantini E, Custodero C, Daian D, Dalmasso MC, Daniele A, Dardiotis E, Dartigues J-F, de Deyn PP, de Paiva Lopes K, de Witte LD, Debette S et al (2022) New insights into the genetic etiology of Alzheimer’s disease and related dementias. Nat Genet 54:412–436. https://doi.org/10.1038/s41588-022-01024-z · DOI · Paper page
  107. Andrews SJ, Renton AE, Fulton-Howard B, Podlesny-Drabiniok A, Marcora E, Goate AM (2023) The complex genetic architecture of Alzheimer’s disease: novel insights and future directions. EBioMedicine 90:104511. https://doi.org/10.1016/j.ebiom.2023.104511 · DOI · Paper page
  108. Koutsodendris N, Blumenfeld J, Agrawal A, Traglia M, Grone B, Zilberter M, Yip O, Rao A, Nelson MR, Hao Y, Thomas R, Yoon SY, Arriola P, Huang Y (2023) Neuronal APOE4 removal protects against tau-mediated gliosis, neurodegeneration and myelin deficits. Nature Aging 3:275–296. https://doi.org/10.1038/s43587-023-00368-3 · DOI · Paper page
  109. Takahashi M, Miyata H, Kametani F, Nonaka T, Akiyama H, Hisanaga S, Hasegawa M (2015) Extracellular association of APP and tau fibrils induces intracellular aggregate formation of tau. Acta Neuropathol 129:895–907. https://doi.org/10.1007/s00401-015-1415-2 · DOI
  110. Soto-Faguás CM, Sanchez-Molina P, Saura CA (2021) Loss of presenilin function enhances tau phosphorylation and aggregation in mice. Acta Neuropathol Commun 9:162. https://doi.org/10.1186/s40478-021-01259-7 · DOI
  111. Lundberg M, Sng LMF, Szul P, Dunne R, Bayat A, Burnham SC, Bauer DC, Twine NA (2023) Novel Alzheimer’s disease genes and epistasis identified using machine learning GWAS platform. Sci Rep 13:17662. https://doi.org/10.1038/s41598-023-44378-y · DOI
  112. Yan X, Nykänen N-P, Brunello CA, Haapasalo A, Hiltunen M, Uronen R-L, Huttunen HJ (2016) FRMD4A-cytohesin signaling modulates cellular release of tau. J Cell Sci. https://doi.org/10.1242/jcs.180745 · DOI
  113. Al Kabbani MA, Wunderlich G, Köhler C, Zempel H (2022) AAV-based gene therapy approaches for genetic forms of tauopathies and related neurogenetic disorders. Biocell 46:847–853. https://doi.org/10.32604/biocell.2022.018144 · DOI
  114. Pan L, Meng L, He M, Zhang Z (2021) Tau in the pathophysiology of Parkinson’s disease. J Mol Neurosci 71:2179–2191. https://doi.org/10.1007/s12031-020-01776-5 · DOI
  115. Shahmoradian SH, Lewis AJ, Genoud C, Hench J, Moors TE, Navarro PP, Castaño-Díez D, Schweighauser G, Graff-Meyer A, Goldie KN, Sütterlin R, Huisman E, Ingrassia A, de Gier Y, Rozemuller AJM, Wang J, De Paepe A, Erny J, Staempfli A, Hoernschemeyer J, Großerüschkamp F, Niedieker D, El-Mashtoly SF, Quadri M, Van IJcken WFJ, Bonifati V, Gerwert K, Bohrmann B, Frank S, Britschgi M, Stahlberg H, Van de Berg, WDJ, Lauer ME (2019) Lewy pathology in Parkinson’s disease consists of crowded organelles and lipid membranes. Nature Neurosci22:1099–1109. https://doi.org/10.1038/s41593-019-0423-2 · DOI
  116. Arima K, Mizutani T, Alim MA, Tonozuka-Uehara H, Izumiyama Y, Hirai S, Uéda K (2000) NACP/α-synuclein and tau constitute two distinctive subsets of filaments in the same neuronal inclusions in brains from a family of parkinsonism and dementia with lewy bodies: double-immunolabeling fluorescence and electron microscopic studies. Acta Neuropathol 100:115–121. https://doi.org/10.1007/s004010050002 · DOI
  117. Aarsland D, Andersen K, Larsen JP, Lolk A (2003) Prevalence and characteristics of dementia in Parkinson disease. Arch Neurol 60:387. https://doi.org/10.1001/archneur.60.3.387 · DOI
  118. Han J, Fan Y, Wu P, Huang Z, Li X, Zhao L, Ji Y, Zhu M (2021) Parkinson’s disease dementia: synergistic effects of alpha-synuclein, tau, beta-amyloid, and iron. Front Aging Neurosci 13:1–13. https://doi.org/10.3389/fnagi.2021.743754 · DOI
  119. Irwin DJ, Lee VM, Trojanowski JQ (2013) Amyloid beta-peptide and the dementia of Parkinson’s disease. Nat Rev Neurosci 14:626–636. https://doi.org/10.1038/nrn3549.Parkinson · DOI
  120. Henderson MX, Sengupta M, Trojanowski JQ, Lee VMY (2019) Alzheimer’s disease tau is a prominent pathology in LRRK2 Parkinson’s disease. Acta Neuropathol Commun 7:1–16. https://doi.org/10.1186/s40478-019-0836-x · DOI
  121. Sanchez-Contreras M, Heckman MG, Tacik P, Diehl N, Brown PH, Soto-Ortolaza AI, Christopher EA, Walton RL, Ross OA, Golbe LI, Graff-Radford N, Wszolek ZK, Dickson DW, Rademakers R (2017) Study of LRRK2 variation in tauopathy: progressive supranuclear palsy and corticobasal degeneration. Mov Disord 32:115–123. https://doi.org/10.1002/mds.26815 · DOI
  122. Zabetian CP, Hutter CM, Factor SA, Nutt JG, Higgins DS, Griffith A, Roberts JW, Leis BC, Kay DM, Yearout D, Montimurro JS, Edwards KL, Samii A, Payami H (2007) Association analysis of MAPT H1 haplotype and subhaplotypes in Parkinson’s disease. Ann Neurol 62:137–144. https://doi.org/10.1002/ana.21157 · DOI
  123. Tauber CV, Schwarz SC, Rösler TW, Arzberger T, Gentleman S, Windl O, Krumbiegel M, Reis A, Ruf VC, Herms J, Höglinger GU (2023) Different MAPT haplotypes influence expression of total MAPT in postmortem brain tissue. Acta Neuropathol Commun 11:40. https://doi.org/10.1186/s40478-023-01534-9 · DOI
  124. Ye M, Zhou D, Zhou Y, Sun C (2015) Parkinson’s disease-associated PINK1G309D mutation increases abnormal phosphorylation of tau. IUBMB Life 67:286–290. https://doi.org/10.1002/iub.1367 · DOI
  125. Roy B, Jackson GR (2014) Interactions between tau and α-synuclein augment neurotoxicity in a drosophila model of Parkinson’s disease. Hum Mol Genet 23:3008–3023. https://doi.org/10.1093/hmg/ddu011 · DOI · Paper page
  126. Bogetofte H, Ryan BJ, Jensen P, Schmidt SI, Vergoossen DLE, Barnkob MB, Kiani LN, Chughtai U, Heon-Roberts R, Caiazza MC, McGuinness W, Márquez-Gómez R, Vowles J, Bunn FS, Brandes J, Kilfeather P, Connor JP, Fernandes HJR, Caffrey TM, Meyer M, Cowley SA, Larsen MR, Wade-Martins R (2023) Post-translational proteomics platform identifies neurite outgrowth impairments in Parkinson’s disease GBA-N370S dopamine neurons. Cell Rep 42:112180. https://doi.org/10.1016/j.celrep.2023.112180 · DOI
  127. Wang Y, Liu W, He X, Zhou F (2013) Parkinson’s disease-associated Dj-1 mutations increase abnormal phosphorylation of tau protein through Akt/Gsk-3β pathways. J Mol Neurosci 51:911–918. https://doi.org/10.1007/s12031-013-0099-0 · DOI
  128. Vacchi E, Kaelin-Lang A, Melli G (2020) Tau and alpha synuclein synergistic effect in neurodegenerative diseases: when the periphery is the core. Int J Mol Sci 21:5030. https://doi.org/10.3390/ijms21145030 · DOI
  129. Menšíková K, Matěj R, Colosimo C, Rosales R, Tučková L, Ehrmann J, Hraboš D, Kolaříková K, Vodička R, Vrtěl R, Procházka M, Nevrlý M, Kaiserová M, Kurčová S, Otruba P, Kaňovský P (2022) Lewy body disease or diseases with lewy bodies? npj Parkinson’s Dis. https://doi.org/10.1038/s41531-021-00273-9 · DOI
  130. Fathy YY, Jonkman LE, Bol JJ, Timmermans E, Jonker AJ, Rozemuller AJM, van de Berg WDJ (2022) Axonal degeneration in the anterior insular cortex is associated with Alzheimer’s co-pathology in Parkinson’s disease and dementia with Lewy bodies. Transl Neurodegener 11:52. https://doi.org/10.1186/s40035-022-00325-x · DOI
  131. van Steenoven I, Aarsland D, Weintraub D, Londos E, Blanc F, van der Flier WM, Teunissen CE, Mollenhauer B, Fladby T, Kramberger MG, Bonanni L, Lemstra AW (2016) Cerebrospinal fluid Alzheimer’s disease biomarkers across the spectrum of Lewy body diseases: results from a large multicenter Cohort. Zetterberg, H., Ed. J Alzheimer’s Dis 54:287–295. https://doi.org/10.3233/JAD-160322 · DOI
  132. Smith BR, Nelson KM, Kemper LJ, Leinonen-Wright K, Petersen A, Keene CD, Ashe KH (2019) A soluble tau fragment generated by caspase-2 is associated with dementia in Lewy body disease. Acta Neuropathol Commun 7:124. https://doi.org/10.1186/s40478-019-0765-8 · DOI
  133. Tolea MI, Galvin JE (2018) The genetics of dementia with Lewy bodies. Handbook Clin Neurol. https://doi.org/10.1016/B978-0-444-64076-5.00028-4 · DOI
  134. Van Der Lee SJ, Van Steenoven I, Van De Beek M, Tesi N, Jansen IE, Van Schoor NM, Reinders MJT, Huisman M, Scheltens P, Teunissen CE, Holstege H, Van Der Flier WM, Lemstra AW (2021) Genetics contributes to concomitant pathology and clinical presentation in dementia with Lewy bodies. J Alzheimer’s Dis 83:269–279. https://doi.org/10.3233/JAD-210365 · DOI
  135. Rongve A, Witoelar A, Ruiz A, Athanasiu L, Abdelnour C, Clarimon J, Heilmann-Heimbach S, Hernández I, Moreno-Grau S, de Rojas I, Morenas-Rodríguez E, Fladby T, Sando SB, Bråthen G, Blanc F, Bousiges O, Lemstra AW, van Steenoven I, Londos E, Almdahl IS, Pålhaugen L, Eriksen JA, Djurovic S, Stordal E, Saltvedt I, Ulstein ID, Bettella F, Desikan RS, Idland AV, Toft M, Pihlstrøm L, Snaedal J, Tárraga L, Boada M, Lleó A, Stefánsson H, Stefánsson K, Ramírez A, Aarsland D, Andreassen OA (2019) GBA and APOE Ε4 associate with sporadic dementia with Lewy bodies in European genome wide association study. Sci Rep 9:1–8. https://doi.org/10.1038/s41598-019-43458-2 · DOI
  136. Bencze J, Seo W, Hye A, Aarsland D, Hortobágyi T (2020) Dementia with Lewy bodies—a clinicopathological update. Free Neuropathol. https://doi.org/10.17879/freeneuropathology-2020-2613 · DOI
  137. Bras J, Guerreiro R, Darwent L, Parkkinen L, Ansorge O, Escott-Price V, Hernandez DG, Nalls MA, Clark LN, Honig LS, Marder K, Van Der Flier WM, Lemstra A, Scheltens P, Rogaeva E, St George-Hyslop P, Londos E, Zetterberg H, Ortega-Cubero S, Pastor P, Ferman TJ, Graff-Radford NR, Ross OA, Barber I, Braae A, Brown K, Morgan K, Maetzler W, Berg D, Troakes C, Al-Sarraj S, Lashley T, Compta Y, Revesz T, Lees A, Cairns N, Halliday GM, Mann D, Pickering-Brown S, Dickson DW, Singleton A, Hardy J (2014) Genetic analysis implicates APOE, SNCA and suggests lysosomal dysfunction in the etiology of dementia with Lewy bodies. Hum Mol Genet 23:6139–6146. https://doi.org/10.1093/hmg/ddu334 · DOI · Paper page
  138. Chia R, Sabir MS, Bandres-Ciga S, Saez-Atienzar S, Reynolds RH, Gustavsson E, Walton RL, Ahmed S, Viollet C, Ding J, Makarious MB, Diez-Fairen M, Portley MK, Shah Z, Abramzon Y, Hernandez DG, Blauwendraat C, Stone DJ, Eicher J, Parkkinen L, Ansorge O, Clark L, Honig LS, Marder K, Lemstra A, St George-Hyslop P, Londos E, Morgan K, Lashley T, Warner TT, Jaunmuktane Z, Galasko D, Santana I, Tienari PJ, Myllykangas L, Oinas M, Cairns NJ, Morris JC, Halliday GM, Van Deerlin VM, Trojanowski JQ, Grassano M, Calvo A, Mora G, Canosa A, Floris G, Bohannan RC, Brett F, Gan-Or Z, Geiger JT, Moore A, May P, Krüger R, Goldstein DS, Lopez G, Tayebi N, Sidransky E, Sotis AR, Sukumar G, Alba C, Lott N, Martinez EMG, Tuck M, Singh J, Bacikova D, Zhang X, Hupalo DN, Adeleye A, Wilkerson MD, Pollard HB, Norcliffe-Kaufmann L, Palma JA, Kaufmann H, Shakkottai VG, Perkins M, Newell KL, Gasser T, Schulte C, Landi F, Salvi E, Cusi D, Masliah E, Kim RC, Caraway CA, Monuki ES, Brunetti M, Dawson TM, Rosenthal LS, Albert MS, Pletnikova O, Troncoso JC, Flanagan ME, Mao Q, Bigio EH, Rodríguez-Rodríguez E, Infante J, Lage C, González-Aramburu I et al (2021) Genome sequencing analysis identifies new loci associated with Lewy body dementia and provides insights into its genetic architecture. Nat Genet 53:294–303. https://doi.org/10.1038/s41588-021-00785-3 · DOI · Paper page
  139. Calafate S, Flavin W, Verstreken P, Moechars D (2016) Loss of Bin1 promotes the propagation of tau pathology. Cell Rep 17:931–940. https://doi.org/10.1016/j.celrep.2016.09.063 · DOI · Paper page
  140. De Rossi P, Nomura T, Andrew RJ, Masse NY, Sampathkumar V, Musial TF, Sudwarts A, Recupero AJ, Le Metayer T, Hansen MT, Shim H-N, Krause SV, Freedman DJ, Bindokas VP, Kasthuri N, Nicholson DA, Contractor A, Thinakaran G (2020) Neuronal BIN1 regulates presynaptic neurotransmitter release and memory consolidation. Cell Rep 30:3520-3535.e7. https://doi.org/10.1016/j.celrep.2020.02.026 · DOI
  141. Zhang J-N, Li Q, Yang F (2023) Role of epigenetic modifications in Parkinson’s disease. Epigenomics 15:573–576. https://doi.org/10.2217/epi-2023-0211 · DOI
  142. Borsche M, Pereira SL, Klein C, Grünewald A (2021) Mitochondria and Parkinson’s disease: clinical, molecular, and translational aspects. J Parkinson’s Dis 11:45–60. https://doi.org/10.3233/JPD-201981 · DOI
  143. Rodger AT, ALNasser M, Carter WG (2023) Are therapies that target α-synuclein effective at halting Parkinson’s disease progression? A systematic review. Int J Mol Sci 24:11022. https://doi.org/10.3390/ijms241311022 · DOI
  144. Over L, Brüggemann N, Lohmann K (2021) Therapies for genetic forms of Parkinson’s disease: systematic literature review. Bonne, G., Ed. J Neuromuscul Dis 8:341–356. https://doi.org/10.3233/JND-200598 · DOI
  145. Bergeron D, Poulin S, Laforce R (2018) Cognition and anatomy of adult Niemann-Pick disease type C: insights for the Alzheimer field. Cogn Neuropsychol 35:209–222. https://doi.org/10.1080/02643294.2017.1340264 · DOI
  146. Vélez Pinos PJ, Saavedra Palacios MS, Colina Arteaga PA, Arevalo Cordova TD (2023) Niemann-Pick disease: a case report and literature review. Cureus. https://doi.org/10.7759/cureus.33534 · DOI
  147. Malnar M, Hecimovic S, Mattsson N, Zetterberg H (2014) Bidirectional links between Alzheimer’s disease and Niemann-Pick type C disease. Neurobiol Dis 72:37–47. https://doi.org/10.1016/j.nbd.2014.05.033 · DOI
  148. Suzuki K, Parker CC, Pentchev PG, Katz D, Ghetti B, D’Agostino AN, Carstea ED (1995) Neurofibrillary tangles in Niemann-Pick disease type C. Acta Neuropathol 89:227–238. https://doi.org/10.1007/BF00309338 · DOI
  149. Xiao X, Liao X, Zhou Y, Weng L, Guo L, Zhou L, Wang X, Liu X, Liu H, Bi X, Xu T, Zhu Y, Yang Q, Zhang S, Hao X, Liu Y, Zhang W, Li J, Shen L, Jiao B (2022) Variants in the Niemann-Pick type C genes are not associated with Alzheimer’s disease: a large case-control study in the chinese population. Neurobiol Aging 116:49–54. https://doi.org/10.1016/j.neurobiolaging.2022.04.008 · DOI
  150. Boenzi S, Dardis A, Russo P, Bellofatto M, Imbriglio T, Fico T, De Michele G, De Rosa A (2019) Screening for Niemann-Pick type C disease in neurodegenerative diseases. J Clin Neurosci 68:266–267. https://doi.org/10.1016/j.jocn.2019.06.025 · DOI
  151. Zech M, Nübling G, Castrop F, Jochim A, Schulte EC, Mollenhauer B, Lichtner P, Peters A, Gieger C, Marquardt T, Vanier MT, Latour P, Klünemann H, Trenkwalder C, Diehl-Schmid J, Perneczky R, Meitinger T, Oexle K, Haslinger B, Lorenzl S, Winkelmann J (2013) Niemann-Pick C disease gene mutations and age-related neurodegenerative disorders. Wider, C., Ed.,. PLoS ONE 8:e82879. https://doi.org/10.1371/journal.pone.0082879 · DOI
  152. Glöckner F, Ohm TG (2014) Tau pathology induces intraneuronal cholesterol accumulation. J Neuropathol Exp Neurol 73:846–854. https://doi.org/10.1097/NEN.0000000000000103 · DOI
  153. Szabo L, Cummins N, Paganetti P, Odermatt A, Papassotiropoulos A, Karch C, Götz J, Eckert A, Grimm A (2023) ER-mitochondria contacts and cholesterol metabolism are disrupted by disease-associated tau protein. EMBO Rep. https://doi.org/10.15252/embr.202357499 · DOI
  154. Pacheco CD, Elrick MJ, Lieberman AP (2009) Tau deletion exacerbates the phenotype of Niemann-Pick type C mice and implicates autophagy in pathogenesis. Hum Mol Genet 18:956–965. https://doi.org/10.1093/hmg/ddn423 · DOI
  155. Smith AF, Vanderah TW, Erickson RP (2020) Haploinsufficiency of tau decreases survival of the mouse model of Niemann-Pick disease type C1 but does not alter tau phosphorylation. J Appl Genet 61:567–570. https://doi.org/10.1007/s13353-020-00572-6 · DOI
  156. Padilla C, Montal V, Walpert MJ, Hong YT, Fryer TD, Coles JP, Aigbirhio FI, Hartley SL, Cohen AD, Tudorascu DL, Christian BT, Handen BL, Klunk WE, Holland AJ, Zaman SH (2022) Cortical atrophy and amyloid and tau deposition in down syndrome: a longitudinal study. Alzheimer’s Dementia Diagn Assess Dis Monit 14:5. https://doi.org/10.1002/dad2.12288 · DOI
  157. Hartley SL, Handen BL, Tudorascu D, Lee L, Cohen A, Piro-Gambetti B, Zammit M, Klunk W, Laymon C, Zaman S, Ances BM, Sabbagh M, Christian BT (2022) Role of tau deposition in early cognitive decline in down syndrome. Alzheimer’s Dementia Diagn Assess Dis Monit 14:5. https://doi.org/10.1002/dad2.12256 · DOI
  158. Ichimata S, Martinez-Valbuena I, Forrest SL, Kovacs GG (2022) Expanding the spectrum of amyloid-β plaque pathology: the down syndrome associated ‘bird-nest plaque.’ Acta Neuropathol 144:1171–1174. https://doi.org/10.1007/s00401-022-02500-w · DOI
  159. Ichimata S, Yoshida K, Visanji NP, Lang AE, Nishida N, Kovacs GG (2022) Patterns of mixed pathologies in down syndrome. Giaccone, G., Ed.,. J Alzheimer’s Dis 87:595–607. https://doi.org/10.3233/JAD-215675 · DOI
  160. Lana-Elola E, Watson-Scales SD, Fisher EMC, Tybulewicz VLJ (2011) Down syndrome: searching for the genetic culprits. Dis Model Mech 4:586–595. https://doi.org/10.1242/dmm.008078 · DOI
  161. Tosh JL, Rhymes ER, Mumford P, Whittaker HT, Pulford LJ, Noy SJ, Cleverley K, Strydom A, Fisher E, Wiseman F, Nizetic D, Hardy J, Tybulewicz V, Karmiloff-Smith A, Walker MC, Tybulewicz VLJ, Wykes RC, Fisher EMC, Wiseman FK (2021) Genetic dissection of down syndrome-associated alterations in APP/amyloid-β biology using mouse models. Sci Rep 11:5736. https://doi.org/10.1038/s41598-021-85062-3 · DOI · Paper page
  162. Ryoo S-R, Jeong HK, Radnaabazar C, Yoo J-J, Cho H-J, Lee H-W, Kim I-S, Cheon Y-H, Ahn YS, Chung S-H, Song W-J (2007) DYRK1A-mediated hyperphosphorylation of tau. J Biol Chem 282:34850–34857. https://doi.org/10.1074/jbc.M707358200 · DOI
  163. Grigorova M, Mak E, Brown SSG, Beresford-Webb J, Hong YT, Fryer TD, Coles JP, Aigbirhio FI, Tudorascu D, Cohen A, Christian BT, Ances B, Handen BL, Laymon CM, Klunk WE, Clare ICH, Holland AJ, Zaman SH (2022) Amyloid- β and tau deposition influences cognitive and functional decline in down syndrome. Neurobiol Aging 119:36–45. https://doi.org/10.1016/j.neurobiolaging.2022.07.003 · DOI
  164. Zammit MD, Tudorascu DL, Laymon CM, Hartley SL, Ellison PA, Zaman SH, Ances BM, Johnson SC, Stone CK, Sabbagh MN, Mathis CA, Klunk WE, Cohen AD, Handen BL, Christian BT (2021) Neurofibrillary tau depositions emerge with subthreshold cerebral beta-amyloidosis in down syndrome. NeuroImage Clin 31:102740. https://doi.org/10.1016/j.nicl.2021.102740 · DOI
  165. Shi J, Zhang T, Zhou C, Chohan MO, Gu X, Wegiel J, Zhou J, Hwang Y-W, Iqbal K, Grundke-Iqbal I, Gong C-X, Liu F (2008) Increased dosage of Dyrk1A alters alternative splicing factor (ASF)-regulated alternative splicing of tau in down syndrome. J Biol Chem 283:28660–28669. https://doi.org/10.1074/jbc.M802645200 · DOI
  166. Duchon A, Herault Y (2016) DYRK1A, a dosage-sensitive gene involved in neurodevelopmental disorders, is a target for drug development in down syndrome. Front Behav Neurosci. https://doi.org/10.3389/fnbeh.2016.00104 · DOI · Paper page
  167. Kim H, Lee K-S, Kim A-K, Choi M, Choi K, Kang M, Chi S-W, Lee M-S, Lee J-S, Lee S-Y, Song W-J, Yu K, Cho S (2016) A chemical with proven clinical safety restores down syndrome-related phenotypes via DYRK1A inhibition. Dis Model Mech. https://doi.org/10.1242/dmm.025668 · DOI
  168. Souchet B, Audrain M, Billard JM, Dairou J, Fol R, Orefice NS, Tada S, Gu Y, Dufayet-Chaffaud G, Limanton E, Carreaux F, Bazureau J-P, Alves S, Meijer L, Janel N, Braudeau J, Cartier N (2019) Inhibition of DYRK1A proteolysis modifies its kinase specificity and rescues Alzheimer phenotype in APP/PS1 mice. Acta Neuropathol Commun 7:46. https://doi.org/10.1186/s40478-019-0678-6 · DOI
  169. Zhu B, Parsons T, Stensen W, Mjøen Svendsen JS, Fugelli A, Hodge JJL (2022) DYRK1a inhibitor mediated rescue of drosophila models of Alzheimer’s disease-down syndrome phenotypes. Front Pharmacol 13:4. https://doi.org/10.3389/fphar.2022.881385 · DOI
  170. Curtis ME, Smith T, Yu D, Praticò D (2022) Association of retromer deficiency and tau pathology in down syndrome. Ann Neurol 91:561–567. https://doi.org/10.1002/ana.26321 · DOI
  171. Fernandez-Gomez F, Tran H, Dhaenens C-M, Caillet-Boudin M-L, Schraen-Maschke S, Blum D, Sablonnière B, Buée-Scherrer V, Buee L, Sergeant N (2019) Myotonic dystrophy: an RNA toxic gain of function tauopathy? Tau Biol. https://doi.org/10.1007/978-981-32-9358-8_17 · DOI
  172. Brook JD, McCurrach ME, Harley HG, Buckler AJ, Church D, Aburatani H, Hunter K, Stanton VP, Thirion JP, Hudson T (1992) Molecular basis of myotonic dystrophy: expansion of a trinucleotide (CTG) repeat at the 3’ end of a transcript encoding a protein kinase family member. Cell 68:799–808. https://doi.org/10.1016/0092-8674(92)90154-5 · DOI · Paper page
  173. Liu J, Guo Z-N, Yan X-L, Yang Y, Huang S (2021) Brain pathogenesis and potential therapeutic strategies in myotonic dystrophy type 1. Front Aging Neurosci 13:4. https://doi.org/10.3389/fnagi.2021.755392 · DOI
  174. Dhaenens CM, Schraen-Maschke S, Tran H, Vingtdeux V, Ghanem D, Leroy O, Delplanque J, Vanbrussel E, Delacourte A, Vermersch P, Maurage CA, Gruffat H, Sergeant A, Mahadevan MS, Ishiura S, Buée L, Cooper TA, Caillet-Boudin ML, Charlet-Berguerand N, Sablonnière B, Sergeant N (2008) Overexpression of MBNL1 fetal isoforms and modified splicing of tau in the DM1 brain: two individual consequences of CUG trinucleotide repeats. Exp Neurol 210:467–478. https://doi.org/10.1016/j.expneurol.2007.11.020 · DOI
  175. Dhaenens CM, Tran H, Frandemiche M-L, Carpentier C, Schraen-Maschke S, Sistiaga A, Goicoechea M, Eddarkaoui S, Van Brussels E, Obriot H, Labudeck A, Gevaert MH, Fernandez-Gomez F, Charlet-Berguerand N, Deramecourt V, Maurage CA, Buée L, de Munain AL, Sablonnière B, Caillet-Boudin ML, Sergeant N (2011) Mis-splicing of tau exon 10 in myotonic dystrophy type 1 is reproduced by overexpression of CELF2 but not by MBNL1 silencing. Biochimica et Biophysica Acta BBA Mol Basis Dis 1812:732–742. https://doi.org/10.1016/j.bbadis.2011.03.010 · DOI
  176. Weijs R, Okkersen K, van Engelen B, Küsters B, Lammens M, Aronica E, Raaphorst J, van Cappellen van Walsum A (2021) Human brain pathology in myotonic dystrophy type 1: a systematic review. Neuropathology41:3–20. https://doi.org/10.1111/neup.12721 · DOI
  177. Jiang H, Mankodi A, Swanson MS, Moxley RT, Thornton CA (2004) Myotonic dystrophy type 1 is associated with nuclear foci of mutant RNA, sequestration of muscleblind proteins and deregulated alternative splicing in neurons. Hum Mol Genet 13:3079–3088. https://doi.org/10.1093/hmg/ddh327 · DOI
  178. Caillet-Boudin M-L, Fernandez-Gomez F-J, Tran H, Dhaenens C-M, Buee L, Sergeant N (2014) Brain pathology in myotonic dystrophy: when tauopathy meets spliceopathy and RNAopathy. Front Mol Neurosci 6:5. https://doi.org/10.3389/fnmol.2013.00057 · DOI
  179. Laforce RJ, Dallaire-Théroux C, Racine AM, Dent G, Salinas-Valenzuela C, Poulin E, Cayer A-M, Bédard-Tremblay D, Rouleau-Bonenfant T, St-Onge F, Schraen-Maschke S, Beauregard J-M, Sergeant N, Puymirat J (2022) Tau positron emission tomography, cerebrospinal fluid and plasma biomarkers of neurodegeneration, and neurocognitive testing: an exploratory study of participants with myotonic dystrophy type 1. J Neurol 269:3579–3587. https://doi.org/10.1007/s00415-022-10970-x · DOI
  180. López-Martínez A, Soblechero-Martín P, De-la-Puente-Ovejero L, Nogales-Gadea G, Arechavala-Gomeza V (2020) An overview of alternative splicing defects implicated in myotonic dystrophy type I. Genes 11:1109. https://doi.org/10.3390/genes11091109 · DOI
  181. Itoh K, Mitani M, Kawamoto K, Futamura N, Funakawa I, Jinnai K, Fushiki S (2010) Neuropathology does not correlate with regional differences in the extent of expansion of CTG repeats in the brain with myotonic dystrophy type 1. Acta Histochem Cytochem 43:149–156. https://doi.org/10.1267/ahc.10019 · DOI
  182. Sano T, Kawazoe T, Shioya A, Mori-Yoshimura M, Oya Y, Maruo K, Nishino I, Hoshino M, Murayama S, Saito Y (2022) Unique Lewy pathology in myotonic dystrophy type 1. Neuropathology 42:104–116. https://doi.org/10.1111/neup.12790 · DOI
  183. Meola G, Cardani R (2015) Myotonic dystrophy type 2: an update on clinical aspects, genetic and pathomolecular mechanism. J Neuromuscul Dis 2:S59–S71. https://doi.org/10.3233/JND-150088 · DOI
  184. Liquori CL, Ricker K, Moseley ML, Jacobsen JF, Kress W, Naylor SL, Day JW, Ranum LP (2001) Myotonic dystrophy type 2 caused by a CCTG expansion in intron 1 of ZNF9. Science 293:864–867. https://doi.org/10.1126/science.1062125 · DOI
  185. Maurage CA, Udd B, Ruchoux MM, Vermersch P, Kalimo H, Krahe R, Delacourte A, Sergeant N (2005) Similar brain tau pathology in DM2/PROMM and DM1/Steinert disease. Neurology 65:1636–1638. https://doi.org/10.1212/01.wnl.0000184585.93864.4e · DOI
  186. The Huntington’s Disease Collaborative Research Group (1993) A novel gene containing a trinucleotide repeat that is expanded and unstable on Huntington’s disease chromosomes. Cell 72:971–983. https://doi.org/10.1016/0092-8674(93)90585-E · DOI · Paper page
  187. Cisbani G, Cicchetti F (2012) An in vitro perspective on the molecular mechanisms underlying mutant huntingtin protein toxicity. Cell Death Dis 3:e382–e382. https://doi.org/10.1038/cddis.2012.121 · DOI
  188. Gratuze M, Cisbani G, Cicchetti F, Planel E (2016) Is Huntington’s disease a tauopathy? Brain 139:1014–1025. https://doi.org/10.1093/brain/aww021 · DOI
  189. Salem S, Cicchetti F (2023) Untangling the role of tau in Huntington’s disease pathology. J Huntington’s Dis 12:15–29. https://doi.org/10.3233/JHD-220557 · DOI
  190. Vuono R, Winder-Rhodes S, de Silva R, Cisbani G, Drouin-Ouellet J, Spillantini MG, Cicchetti F, Barker RA (2015) The role of tau in the pathological process and clinical expression of Huntington’s disease. Brain 138:1907–1918. https://doi.org/10.1093/brain/awv107 · DOI
  191. Masnata M, Salem S, de Rus Jacquet A, Anwer M, Cicchetti F (2020) Targeting tau to treat clinical features of Huntington’s disease. Front Neurol 11:5. https://doi.org/10.3389/fneur.2020.580732 · DOI
  192. Petry S, Nateghi B, Keraudren R, Sergeant N, Planel E, Hébert SS, St-Amour I (2023) Differential regulation of tau Exon 2 and 10 isoforms in Huntington’s disease brain. Neuroscience 518:54–63. https://doi.org/10.1016/j.neuroscience.2022.07.014 · DOI
  193. Mees I, Nisbet RM, Hannan AJ, Renoir T (2023) Implications of tau dysregulation in Huntington’s disease and potential for new therapeutics. J Huntington’s Dis 12:1–13. https://doi.org/10.3233/JHD-230569 · DOI
  194. Alpaugh M, Masnata M, de Rus Jacquet A, Lepinay E, Denis HL, Saint-Pierre M, Davies P, Planel E, Cicchetti F (2022) Passive immunization against phosphorylated tau improves features of Huntington’s disease pathology. Mol Ther 30:1500–1522. https://doi.org/10.1016/j.ymthe.2022.01.020 · DOI · Paper page
  195. Mees I, Li S, Beauchamp LC, Barnham KJ, Dutschmann M, Hannan AJ, Renoir T (2022) Loss-of-function and gain-of-function studies refute the hypothesis that tau protein is causally involved in the pathogenesis of Huntington’s disease. Hum Mol Genet 31:1997–2009. https://doi.org/10.1093/hmg/ddac001 · DOI
  196. Mees I, Tran H, Roberts A, Lago L, Li S, Roberts BR, Hannan AJ, Renoir T (2022) Quantitative phosphoproteomics reveals extensive protein phosphorylation dysregulation in the cerebral cortex of Huntington’s disease mice prior to onset of symptoms. Mol Neurobiol 59:2456–2471. https://doi.org/10.1007/s12035-021-02698-y · DOI
  197. Biffi A (2022) Main features of hereditary cerebral amyloid angiopathies: a systematic review. Cereb Circ Cogn Behav 3:100124. https://doi.org/10.1016/j.cccb.2022.100124 · DOI
  198. Cisternas P, Taylor X, Lasagna-Reeves CA (2019) The amyloid-tau-neuroinflammation axis in the context of cerebral amyloid angiopathy. Int J Mol Sci 20:6319. https://doi.org/10.3390/ijms20246319 · DOI
  199. Garringer HJ, Sammeta N, Oblak A, Ghetti B, Vidal R (2017) Amyloid and intracellular accumulation of BRI2. Neurobiol Aging 52:90–97. https://doi.org/10.1016/j.neurobiolaging.2016.12.018 · DOI
  200. Garringer HJ, Murrell J, Sammeta N, Gnezda A, Ghetti B, Vidal R (2013) Increased tau phosphorylation and tau truncation, and decreased synaptophysin levels in mutant BRI2/tau transgenic mice. Chiesa, R., Ed.,. PLoS ONE 8:e56426. https://doi.org/10.1371/journal.pone.0056426 · DOI

200 of 245 shown

Cited by

See all 46

Metadata

Authors
Langerscheidt, F., Wied, T., Al Kabbani, M. A., van Eimeren, T., Wunderlich, G., & Zempel, H.
Venue
Journal of Neurology
Publisher
Springer Science and Business Media LLC
Published
2024-03-30
Volume
271
Issue
6
Pages
2992-3018
ISSN
  • 0340-5354
  • 1432-1459
DOI
10.1007/s00415-024-12314-3
PMC
PMC11136742
Cited by
46
References
35
Language
en
Licence
Funders
Universitätsklinikum Köln

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

How to cite

Cite CoChat for the checks on this page, and the paper for its own findings.

This page
CoChat. (2026). Citation check: Genetic forms of tauopathies: inherited causes and implications of Alzheimer’s disease-like TAU pathology in primary and secondary tauopathies. https://app.cochat.ai/papers/10.1007/s00415-024-12314-3
The paper
Langerscheidt, F., Wied, T., Al Kabbani, M. A., van Eimeren, T., Wunderlich, G., & Zempel, H. (2024). Genetic forms of tauopathies: inherited causes and implications of Alzheimer’s disease-like TAU pathology in primary and secondary tauopathies. Journal of Neurology. https://doi.org/10.1007/s00415-024-12314-3

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.