References
- Abner E.L., Kryscio R.J., Schmitt F.A., Santacruz K.S., Jicha G.A., Lin Y., Neltner J.M., Smith C.D., Van Eldik L.J., Nelson P.T.: “End-stage” neurofibrillary tangle pathology in preclinical Alzheimer’s disease: Fact or fiction? J. Alzheimers Dis., 2011; 25: 445–453
- Ahmed T., Van der Jeugd A., Blum D., Galas M.C., D’Hooge R., Buee L., Balschun D.: Cognition and hippocampal synaptic plasticity in mice with a homozygous tau deletion. Neurobiol. Aging, 2014; 35: 2474–2478
- Amadoro G., Corsetti V., Ciotti M.T., Florenzano F., Capsoni S., Amato G., Calissano P.: Endogenous Aβ causes cell death via early tau hyperphosphorylation. Neurobiol. Aging, 2011; 32: 969–990
- An W.L., Cowburn R.F., Li L., Braak H., Alafuzoff I., Iqbal K., Iqbal I.G., Winblad B., Pei J.J.: Up-regulation of phosphorylated/activated p70 S6 kinase and its relationship to neurofibrillary pathology in Alzheimer’s disease. Am. J. Pathol., 2003; 163: 591–607
- Arun P., Oguntayo S., Albert S.V., Gist I., Wang Y., Nambiar M.P., Long J.B.: Acute decrease in alkaline phosphatase after brain injury: A potential mechanism for tauopathy. Neurosci. Lett., 2015; 609: 152–158
- Avila J., Jiménez J.S., Sayas C.L., Bolós M., Zabala J.C., Rivas G., Hernández F.: Tau structures. Front. Aging Neurosci., 2016; 8: 262
- Ayala Y.M., Zago P., D’Ambrogio A., Xu Y.F., Petrucelli L., Buratti E., Baralle F.E.: Structural determinants of the cellular localization and shuttling of TDP-43. J. Cell Sci., 2008; 121: 3778–3785
- Bartels T., Choi J.G., Selkoe D.J.: α-Synuclein occurs physiologically as a helically folded tetramer that resists aggregation. Nature, 2011; 477: 107–110
- Berning B.A., Walker A.K.: The pathobiology of TDP-43 C-terminal fragments in ALS and FTLD. Front. Neurosci., 2019; 13: 335
- Brandt R., Léger J., Lee G.: Interaction of tau with the neural plasma membrane mediated by tau’s aminoterminal projection domain. J. Cell Biol., 1995; 131: 1327–1340
- Burré J., Sharma M., Südhof T.C.: α-Synuclein assembles into higher-order multimers upon membrane binding to promote SNARE complex formation. Proc. Natl. Acad. Sci. USA, 2014; 111: E4274–E4283
- Bussell R.Jr., Eliezer D.: Effects of Parkinson’s disease-linked mutations on the structure of lipid-associated α-synuclein. Biochemistry, 2004; 43: 4810–4818
- Chartier-Harlin M.C., Kachergus J., Roumier C., Mouroux V., Douay X., Lincoln S., Levecque C., Larvor L., Andrieux J., Hulihan M., Waucquier N., Defebvre L., Amouyel P., Farrer M., Destée A.: α-synuclein locus duplication as a cause of familial Parkinson’s disease. Lancet, 2004; 364: 1167–1169
- Chen R.H., Wislet-Gendebien S., Samuel F., Visanji N.P., Zhang G., Marsilio D., Langman T., Fraser P.E., Tandon A.: α-Synuclein membrane association is regulated by the Rab3a recycling machinery and presynaptic activity. J. Biol. Chem., 2013; 288: 7438–7449
- Cherry J.D., Tripodis Y., Alvarez V.E., Huber B., Kiernan P.T., Daneshvar D.H., Mez J., Montenigro P.H., Solomon T.M., Alosco M.L., Stern R.A., McKee A.C., Stein T.D.: Microglial neuroinflammation contributes to tau accumulation in chronic traumatic encephalopathy. Acta Neuropathol. Commun., 2016; 4: 112
- Chiang C.H., Grauffel C., Wu L.S., Kuo P.H., Doudeva L.G., Lim C., Shen C.K., Yuan H.S.: Structural analysis of disease-related TDP-43 D169G mutation: Linking enhanced stability and caspase cleavage efficiency to protein accumulation. Sci. Rep., 2016; 6: 21581
- Choi B.K., Choi M.G., Kim J.Y., Yang Y., Lai Y., Kweon D.H., Lee N.K., Shin Y.K.: Large α-synuclein oligomers inhibit neuronal SNARE-mediated vesicle docking. Proc. Natl. Acad. Sci. USA, 2013; 110: 4087–4092
- Clavaguera F., Bolmont T., Crowther R.A., Abramowski D., Frank S., Probst A., Fraser G., Stalder A.K., Beibel M., Staufenbiel M., Jucker M., Goedert M., Tolnay M.: Transmission and spreading of tauopathy in transgenic mouse brain. Nat. Cell Biol., 2009; 11: 909–913
- Cohen T.J., Hwang A.W., Restrepo C.R., Yuan C.X., Trojanowski J.Q., Lee V.M.: An acetylation switch controls TDP-43 function and aggregation propensity. Nat. Commun., 2015; 6: 5845
- Conway K.A., Harper J.D., Lansbury P.T.: Accelerated in vitro fibril formation by a mutant α-synuclein linked to early-onset Parkinson disease. Nat. Med., 1998; 4: 1318–1320
- Coskuner O., Wise-Scira O.: Structures and free energy landscapes of the A53T mutant-type α-synuclein protein and impact of A53T mutation on the structures of the wild-type α-synuclein protein with dynamics. ACS Chem. Neurosci., 2013; 4: 1101–1113
- Dawson H.N., Ferreira A., Eyster M.V., Ghoshal N., Binder L.I., Vitek M.P.: Inhibition of neuronal maturation in primary hippocampal neurons from tau deficient mice. J. Cell Sci., 2001; 114: 1179–1187
- Dayanandan R., Van Slegtenhorst M., Mack T.G., Ko L., Yen S.H., Leroy K., Brion J.P., Anderton B.H., Hutton M., Lovestone S.: Mutations in tau reduce its microtubule binding properties in intact cells and affect its phosphorylation. FEBS Lett., 1999; 446: 228–232
- Dementia. https://www.who.int/en/news-room/fact-sheets/detail/dementia (17.04.2020)
- Derisbourg M., Leghay C., Chiappetta G., Fernandez-Gomez F.J., Laurent C., Demeyer D., Carrier S., Buée-Scherrer V., Blum D., Vinh J., Sergeant N., Verdier Y., Buée L., Hamdane M.: Role of the Tau N-terminal region in microtubule stabilization revealed by new endogenous truncated forms. Sci. Rep., 2015; 5: 9659
- Derkinderen P., Scales T.M., Hanger D.P., Leung K.Y., Byers H.L., Ward M.A., Lenz C., Price C., Bird I.N., Perera T., Kellie S., Williamson R., Noble W., Van Etten R.A., Leroy K. i wsp.: Tyrosine 394 is phosphorylated in Alzheimer’s paired helical filament tau and in fetal tau with c-Abl as the candidate tyrosine kinase. J. Neurosci., 2005; 25: 6584–6593
- Dixit R., Ross J.L., Goldman Y.E., Holzbaur E.L.: Differential regulation of dynein and kinesin motor proteins by tau. Science, 2008; 319: 1086–1089
- Doherty C.P.A., Ulamec S.M., Maya-Martinez R., Good S.C., Makepeace J., Khan G.N., van Oosten-Hawle P., Radford S.E., Brockwell D.J.: A short motif in the N-terminal region of α-synuclein is critical for both aggregation and function. Nat. Struct. Mol. Biol., 2020; 27: 249–259
- Dugger B.N., Dickson D.W.: Pathology of neurodegenerative diseases. Cold Spring Harb. Perspect. Biol., 2017; 9: a028035
- Fares M.B., Ait-Bouziad N., Dikiy I., Mbefo M.K., Jovičić A., Kiely A., Holton J.L., Lee S.J., Gitler A.D., Eliezer D., Lashuel H.A.: The novel Parkinson’s disease linked mutation G51D attenuates in vitro aggregation and membrane binding of α-synuclein, and enhances its secretion and nuclear localization in cells. Hum. Mol. Genet., 2014; 23: 4491–4509
- Fischer D., Mukrasch M.D., Biernat J., Bibow S., Blackledge M., Griesinger C., Mandelkow E., Zweckstetter M.: Conformational changes specific for pseudophosphorylation at serine 262 selectively impair binding of tau to microtubules. Biochemistry, 2009; 48: 10047–10055
- Flores B.N., Li X., Malik A.M., Martinez J., Beg A.A., Barmada S.J.: An intramolecular salt bridge linking TDP43 RNA binding, protein stability, and TDP43-dependent neurodegeneration. Cell. Rep., 2019; 27: 1133–1150.e8
- François-Moutal L., Perez-Miller S., Scott D.D., Miranda V.G., Mollasalehi N., Khanna M.: Structural insights into TDP-43 and effects of post-translational modifications. Front. Mol. Neurosci., 2019; 12: 301
- Fraser P.E., Yang D.S., Yu G., Lévesque L., Nishimura M., Arawaka S., Serpell L.C., Rogaeva E., St George-Hyslop P.: Presenilin structure, function and role in Alzheimer disease. Biochim. Biophys. Acta, 2000; 1502: 1–15
- Frenkel-Pinter M., Stempler S., Tal-Mazaki S., Losev Y., Singh-Anand A., Escobar-Álvarez D., Lezmy J., Gazit E., Ruppin E., Segal D.: Altered protein glycosylation predicts Alzheimer’s disease and modulates its pathology in disease model Drosophila. Neurobiol. Aging, 2017; 56: 159–171
- Fusco G., Chen S.W., Williamson P.T.F., Cascella R., Perni M., Jarvis J.A., Cecchi C., Vendruscolo M., Chiti F., Cremades N., Ying L., Dobson C.M., De Simone A.: Structural basis of membrane disruption and cellular toxicity by α-synuclein oligomers. Science, 2017; 358: 1440–1443
- Gámez-Valero A., Beyer K.: Alternative Splicing of alpha- and beta-synuclein genes plays differential roles in synucleinopathies. Genes, 2018; 9: 63
- Garnier C., Devred F., Byrne D., Puppo R., Roman A.Y., Malesinski S., Golovin A.V., Lebrun R., Ninkina N.N., Tsvetkov P.O.: Zinc binding to RNA recognition motif of TDP-43 induces the formation of amyloid-like aggregates. Sci. Rep., 2017; 7: 6812
- Gauthier-Kemper A., Suárez Alonso M., Sündermann F., Niewidok B., Fernandez M.P., Bakota L., Heinisch J.J., Brandt R.: Annexins A2 and A6 interact with the extreme N terminus of tau and thereby contribute to tau’s axonal localization. J. Biol. Chem., 2018; 293: 8065–8076
- Gong C.X., Singh T.J., Grundke-Iqbal I., Iqbal K.: Phosphoprotein phosphatase activities in Alzheimer disease brain. J. Neurochem., 1993; 61: 921–927
- Götz J., Probst A., Spillantini M.G., Schäfer T., Jakes R., Bürki K., Goedert M.: Somatodendritic localization and hyperphosphorylation of tau protein in transgenic mice expressing the longest human brain tau isoform. EMBO J., 1995; 14: 1304–1313
- Gómez-Santos C., Ferrer I., Reiriz J., Viñals F., Barrachina M., Ambrosio S.: MPP+ increases alpha-synuclein expression and ERK/MAP-kinase phosphorylation in human neuroblastoma SH-SY5Y cells. Brain Res., 2002; 935: 32–39
- Hans F., Eckert M., von Zweydorf F., Gloeckner C.J., Kahle P.J.: Identification and characterization of ubiquitinylation sites in TAR DNA-binding protein of 43 kDa (TDP-43). J. Biol. Chem., 2018; 293: 16083–16099
- Heicklen-Klein A., Ginzburg I.: Tau promoter confers neuronal specificity and binds Sp1 and AP-2. J. Neurochem., 2000; 75: 1408–1418
- Highley J.R., Kirby J., Jansweijer J.A., Webb P.S., Hewamadduma C.A., Heath P.R., Higginbottom A., Raman R., Ferraiuolo L., Cooper-Knock J., McDermott C.J., Wharton S.B., Shaw P.J., Ince P.G.: Loss of nuclear TDP-43 in amyotrophic lateral sclerosis (ALS) causes altered expression of splicing machinery and widespread dysregulation of RNA splicing in motor neurones. Neuropathol. Appl. Neurobiol., 2014; 40: 670–685
- Hirokawa N., Shiomura Y., Okabe S.: Tau proteins: the molecular structure and mode of binding on microtubules. J. Cell Biol., 1988; 107: 1449–1459
- Hosokawa M., Kondo H., Serrano G.E., Beach T.G., Robinson A.C., Mann D.M., Akiyama H., Hasegawa M., Arai T.: Accumulation of multiple neurodegenerative disease-related proteins in familial fronto-temporal lobar degeneration associated with granulin mutation. Sci. Rep., 2017; 7: 1513
- Huin V., Buée L., Behal H., Labreuche J., Sablonnière B., Dhaenens C.M.: Alternative promoter usage generates novel shorter MAPT mRNA transcripts in Alzheimer’s disease and progressive supranuclear palsy brains. Sci. Rep., 2017; 7: 12589
- Iguchi Y., Katsuno M., Ikenaka K., Ishigaki S., Sobue G.: Amyotrophic lateral sclerosis: An update on recent genetic insights. J Neurol., 2013; 260: 2917–2927
- Ittner L.M., Götz J.: Amyloid-β and tau – a toxic pas de deux in Alzheimer’s disease. Nat. Rev. Neurosci., 2011; 12: 65–72
- Ittner L.M., Ke Y.D., Delerue F., Bi M., Gladbach A., van Eersel J., Wölfing H., Chieng B.C., Christie M.J., Napier I.A., Eckert A., Staufenbiel M., Hardeman E., Götz J.: Dendritic function of tau mediates amyloid-β toxicity in Alzheimer’s disease mouse models. Cell, 2010; 142: 387–397
- Jakes R., Spillantini M.G., Goedert M.: Identification of two distinct synucleins from human brain. FEBS Lett., 1994; 345: 27–32
- Jao C.C., Der-Sarkissian A., Chen J., Langen R.: Structure of membrane-bound alpha-synuclein studied by site-directed spin labeling. Proc. Natl. Acad. Sci. USA, 2004; 101: 8331–8336
- Jiang L.L., Xue W., Hong J.Y., Zhang J.T., Li M.J., Yu S.N., He J.H., Hu H.Y.: The N-terminal dimerization is required for TDP-43 splicing activity. Sci. Rep., 2017; 7: 6196
- Jin H., Kanthasamy A., Ghosh A., Yang Y., Anantharam V., Kanthasamy A.G.: α-Synuclein negatively regulates protein kinase Cδ expression to suppress apoptosis in dopaminergic neurons by reducing p300 histone acetyltransferase activity. J. Neurosci., 2011; 31: 2035–2051
- Johnson G.V., Seubert P., Cox T.M., Motter R., Brown J.P., Galasko D.: The tau protein in human cerebrospinal fluid in Alzheimer’s disease consists of proteolytically derived fragments. J. Neurochem., 1997; 68: 430–433
- Kametani F., Nonaka T., Suzuki T., Arai T., Dohmae N., Akiyama H., Hasegawa M.: Identification of casein kinase-1 phosphorylation sites on TDP-43. Biochem. Biophys. Res. Commun., 2009; 382: 405–409
- Kanaan N.M., Morfini G.A., LaPointe N.E., Pigino G.F., Patterson K.R., Song Y., Andreadis A., Fu Y., Brady S.T., Binder L.I.: Pathogenic forms of tau inhibit kinesin-dependent axonal transport through a mechanism involving activation of axonal phosphotransferases. J. Neurosci., 2011; 31: 9858–9868
- Kawahara M., Ohtsuka I., Yokoyama S., Kato-Negishi M., Sadakane Y.: Membrane incorporation, channel formation, and disruption of calcium homeostasis by Alzheimer’s β-amyloid protein. Int. J. Alzheimers Dis., 2011; 2011: 304583
- Kenessey A., Nacharaju P., Ko L.W., Yen S.H.: Degradation of tau by lysosomal enzyme cathepsin D: Implication for Alzheimer neurofibrillary degeneration. J. Neurochem., 1997; 69: 2026–2038
- Khalaf O., Fauvet B., Oueslati A., Dikiy I., Mahul-Mellier A.L., Ruggeri F.S., Mbefo M.K., Vercruysse F., Dietler G., Lee S.J., Eliezer D., Lashuel H.A.: The H50Q mutation enhances α-synuclein aggregation, secretion, and toxicity. J. Biol. Chem., 2014; 289: 21856–21876
- Kosik K.S., Orecchio L.D., Bakalis S., Neve R.L.: Developmentally regulated expression of specific tau sequences. Neuron, 1989; 2: 1389–1397
- Kühnlein P., Sperfeld A.D., Vanmassenhove B., Van Deerlin V., Lee V.M., Trojanowski J.Q., Kretzschmar H.A., Ludolph A.C., Neumann M.: Two German kindreds with familial amyotrophic lateral sclerosis due to TARDBP mutations. Arch. Neurol., 2008; 65: 1185–1189
- Kumar S., Jangir D.K., Kumar R., Kumari M., Bhavesh N.S., Maiti T.K.: Role of sporadic Parkinson disease associated mutations A18T and A29S in enhanced α-synuclein fibrillation and cytotoxicity. ACS Chem. Neurosci., 2018; 9: 230–240
- Lei P., Ayton S., Finkelstein D.I., Spoerri L., Ciccotosto G.D., Wright D.K., Wong B.X., Adlard P.A., Cherny R.A., Lam L.Q., Roberts B.R., Volitakis I., Egan G.F., McLean C.A., Cappai R. i wsp.: Tau deficiency induces parkinsonism with dementia by impairing APP-mediated iron export. Nat. Med., 2012; 18: 291–295
- Liu F., Grundke-Iqbal I., Iqbal K., Gong C.X.: Contributions of protein phosphatases PP1, PP2A, PP2B and PP5 to the regulation of tau phosphorylation. Eur. J. Neurosci., 2005; 22: 1942–1950
- Liu Y., Lv K., Li Z., Yu A.C., Chen J., Teng J.: PACSIN1, a Tau-interacting protein, regulates axonal elongation and branching by facilitating microtubule instability. J. Biol. Chem., 2012; 287: 39911–39924
- Lu J., Duan W., Guo Y., Jiang H., Li Z., Huang J., Hong K., Li C.: Mitochondrial dysfunction in human TDP-43 transfected NSC34 cell lines and the protective effect of dimethoxy curcumin. Brain Res. Bull., 2012; 89: 185–190
- Lundblad M., Decressac M., Mattsson B., Björklund A.: Impaired neurotransmission caused by overexpression of α-synuclein in nigral dopamine neurons. Proc. Natl. Acad. Sci. USA, 2012; 109: 3213–3219
- Maroteaux L., Campanelli J.T., Scheller R.H.: Synuclein: A neuron-specific protein localized to the nucleus and presynaptic nerve terminal. J. Neurosci., 1988; 8: 2804–2815
- Martin L., Latypova X., Terro F.: Post-translational modifications of tau protein: Implications for Alzheimer’s disease. Neurochem. Int., 2011; 58: 458–471
- Matsuoka Y., Picciano M., Malester B., LaFrancois J., Zehr C., Daeschner J.M., Olschowka J.A., Fonseca M.I., O’Banion M.K., Tenner A.J., Lemere C.A., Duff K.: Inflammatory responses to amyloidosis in a transgenic mouse model of Alzheimer’s disease. Am. J. Pathol., 2001; 158: 1345–1354
- Meade R.M., Fairlie D.P., Mason J.M.: Alpha-synuclein structure and Parkinson’s disease – lessons and emerging principles. Mol. Neurodegener., 2019; 14: 29
- Mena R., Luna-Muñoz J.C.: Stages of pathological tau-protein processing in Alzheimer’s disease: From soluble aggregations to polymerization into insoluble Tau-PHFs. W: Current Hypotheses and Research Milestones in Alzheimer’s Disease, red.: R.B. Maccoini, G. Perry. Springer US, New York 2009, 79–91
- Min S.W., Cho S.H., Zhou Y., Schroeder S., Haroutunian V., Seeley W.W., Huang E.J., Shen Y., Masliah E., Mukherjee C., Meyers D., Cole P.A., Ott M., Gan L.: Acetylation of tau inhibits its degradation and contributes to tauopathy. Neuron, 2010; 67: 953–966
- Mohite G.M., Navalkar A., Kumar R., Mehra S., Das S., Gadhe L.G., Ghosh D., Alias B., Chandrawanshi V., Ramakrishnan A., Mehra S., Maji S.K.: The familial α-synuclein A53E mutation enhances cell death in response to environmental toxins due to a larger population of oligomers. Biochemistry, 2018; 57: 5014–5028
- Neumann M., Kwong L.K., Lee E.B., Kremmer E., Flatley A., Xu Y., Forman M.S., Troost D., Kretzschmar H.A., Trojanowski J.Q., Lee V.M.: Phosphorylation of S409/410 of TDP-43 is a consistent feature in all sporadic and familial forms of TDP-43 proteinopathies. Acta Neuropathol., 2009; 117: 137–149
- Neumann M., Sampathu D.M., Kwong L.K., Truax A.C., Micsenyi M.C., Chou T.T., Bruce J., Schuck T., Grossman M., Clark C.M., McCluskey L.F., Miller B.L., Masliah E., Mackenzie I.R., Feldman H. i wsp.: Ubiquitinated TDP-43 in frontotemporal lobar degeneration and amyotrophic lateral sclerosis. Science, 2006; 314: 130–133
- Neve R.L., Harris P., Kosik K.S., Kurnit D.M., Donlon T.A.: Identification of cDNA clones for the human microtubule-associated protein tau and chromosomal localization of the genes for tau and microtubule-associated protein 2. Brain. Res., 1986; 387: 271–280
- Ou S.H., Wu F., Harrich D., García-Martínez L.F., Gaynor R.B.: Cloning and characterization of a novel cellular protein, TDP-43, that binds to human immunodeficiency virus type 1 TAR DNA sequence motifs. J. Virol., 1995; 69: 3584–3596
- Ozer R.S., Halpain S.: Phosphorylation-dependent localization of microtubule-associated protein MAP2c to the actin cytoskeleton. Mol. Biol. Cell, 2000; 11: 3573–3587
- Pandey N., Schmidt R.E., Galvin J.E.: The alpha-synuclein mutation E46K promotes aggregation in cultured cells. Exp. Neurol., 2006; 197: 515–520
- Pesiridis G.S., Lee V.M., Trojanowski J.Q.: Mutations in TDP-43 link glycine-rich domain functions to amyotrophic lateral sclerosis. Hum. Mol. Genet., 2009; 18: R156–R162
- Pinarbasi E.S., Cağatay T., Fung H.Y.J., Li Y.C., Chook Y.M., Thomas P.J.: Active nuclear import and passive nuclear export are the primary determinants of TDP-43 localization. Sci. Rep., 2018; 8: 7083
- Plotegher N., Kumar D., Tessari I., Brucale M., Munari F., Tosatto L., Belluzzi E., Greggio E., Bisaglia M., Capaldi S., Aioanei D., Mammi S., Monaco H.L., Samo B., Bubacco L.: The chaperone-like protein 14-3-3η interacts with human α-synuclein aggregation intermediates rerouting the amyloidogenic pathway and reducing α-synuclein cellular toxicity. Hum. Mol. Genet., 2014; 23: 5615–5629
- Polymenidou M., Lagier-Tourenne C., Hutt K.R., Huelga S.C., Moran J., Liang T.Y., Ling S.C., Sun E., Wancewicz E., Mazur C., Kordasiewicz H., Sedaghat Y., Donohue J.P., Shiue L., Bennett C.F. i wsp.: Long pre-mRNA depletion and RNA missplicing contribute to neuronal vulnerability from loss of TDP-43. Nat. Neurosci., 2011; 14: 459–468
- Prasad A., Sivalingam V., Bharathi V., Girdhar A., Patel B.K.: The amyloidogenicity of a C-terminal region of TDP-43 implicated in amyotrophic lateral sclerosis can be affected by anions, acetylation and homodimerization. Biochimie, 2018; 150: 76–87
- Qureshi H.Y., Paudel H.K.: Parkinsonian neurotoxin 1-methyl-4-phenyl-1,2,3,6-tetrahydropyridine (MPTP) and α-synuclein mutations promote Tau protein phosphorylation at Ser262 and destabilize microtubule cytoskeleton in vitro. J. Biol. Chem., 2011; 286: 5055–5068
- Ramaswami M., Taylor J.P., Parker R.: Altered ribostasis: RNA-protein granules in degenerative disorders. Cell, 2013; 154: 727–736
- Rocca W.A.: The burden of Parkinson’s disease: A worldwide perspective. Lancet Neurol., 2018; 17: 928–929
- Russo M.A., Tomino C., Vernucci E., Limana F., Sansone L., Frustaci A., Tafani M.: Hypoxia and inflammation as a consequence of β-fibril accumulation: A perspective view for new potential therapeutic targets. Oxid. Med. Cell. Longev., 2019; 2019: 7935310
- Salvatori I., Ferri A., Scaricamazza S., Giovannelli I., Serrano A., Rossi S., D’Ambrosi N., Cozzolino M., Giulio A.D., Moreno S., Valle C., Carrì M.T.: Differential toxicity of TAR DNA-binding protein 43 iso-forms depends on their submitochondrial localization in neuronal cells. J. Neurochem., 2018; 146: 585–597
- Saman S., Kim W., Raya M., Visnick Y., Miro S., Saman S., Jackson B., McKee A.C., Alvarez V.E., Lee N.C., Hall G.F.: Exosome-associated tau is secreted in tauopathy models and is selectively phosphorylated in cerebrospinal fluid in early Alzheimer disease. J. Biol. Chem., 2012; 287: 3842–3849
- Siddiqui I.J., Pervaiz N., Abbasi A.A.: The Parkinson Disease gene SNCA: Evolutionary and structural insights with pathological implication. Sci. Rep., 2016; 6: 24475
- Singleton A.B., Farrer M., Johnson J., Singleton A., Hague S., Kachergus J., Hulihan M., Peuralinna T., Dutra A., Nussbaum R., Lincoln S., Crawley A., Hanson M., Maraganore D., Adler C. i wsp.: α-synuclein locus triplication causes Parkinson’s disease. Science, 2003; 302: 841
- Spillantini M.G., Divane A., Goedert M.: Assignment of human α-synuclein (SNCA) and β-synuclein (SNCB) genes to chromosomes 4q21 and 5q35. Genomics, 1995; 27: 379–381
- Sprovieri T., Ungaro C., Perrone B., Naimo G.D., Spataro R., Cavallaro S., La Bella V., Conforti F.L.: A novel S379A TARDBP mutation associated to late-onset sporadic ALS. Neurol. Sci., 2019; 40: 2111–2118
- Stefanoska K., Volkerling A., Bertz J., Poljak A., Ke Y.D., Ittner L.M., Ittner A.: An N-terminal motif unique to primate tau enables differential protein-protein interactions. J. Biol. Chem., 2018; 293: 3710–3719
- Strang K.H., Golde T.E., Giasson B.I.: MAPT mutations, tauopathy, and mechanisms of neurodegeneration. Lab. Invest., 2019; 99: 912–928
- Sultan A., Nesslany F., Violet M., Bégard S., Loyens A., Talahari S., Mansuroglu Z., Marzin D., Sergeant N., Humez S., Colin M., Bonnefoy E., Buée L., Galas M.C.: Nuclear tau, a key player in neuronal DNA protection. J. Biol. Chem., 2011; 286: 4566–4575
- Takeda T.: Possible concurrence of TDP-43, tau and other proteins in amyotrophic lateral sclerosis/frontotemporal lobar degeneration. Neuropathology, 2018; 38: 72–81
- TARDBP TAR DNA binding protein [Homo sapiens (human)] – Gene – NCBI. https://www.ncbi.nlm.nih.gov/gene/23435 (02.06.2020)
- Turner B.J., Bäumer D., Parkinson N.J., Scaber J., Ansorge O., Talbot K.: TDP-43 expression in mouse models of amyotrophic lateral sclerosis and spinal muscular atrophy. BMC Neurosci., 2008; 9: 104
- van Swieten J., Spillantini M.G.: Hereditary frontotemporal dementia caused by Tau gene mutations. Brain Pathol., 2007; 17: 63–73
- Vicente Miranda H., Cássio R., Correia-Guedes L., Gomes M.A., Chegão A., Miranda E., Soares T., Coelho M., Rosa M.M., Ferreira J.J., Outeiro T.F.: Posttranslational modifications of blood-derived alpha-synuclein as biochemical markers for Parkinson’s disease. Sci. Rep., 2017; 7: 13713
- von Bergen M., Barghorn S., Biernat J., Mandelkow E.M., Mandelkow E.: Tau aggregation is driven by a transition from random coil to beta sheet structure. Biochim. Biophys. Acta, 2005; 1739: 158–166
- Wang Y.T., Kuo P.H., Chiang C.H., Liang J.R., Chen Y.R., Wang S., Shen J.C., Yuan H.S.: The truncated C-terminal RNA recognition motif of TDP-43 protein plays a key role in forming proteinaceous aggregates. J. Biol. Chem., 2013; 288: 9049–9057
- Watanabe A., Hasegawa M., Suzuki M., Takio K., Morishima-Kawashima M., Titani K., Arai T., Kosik K.S., Ihara Y.: In vivo phosphorylation sites in fetal and adult rat tau. J. Biol. Chem., 1993; 268: 25712–25717
- Wilhelmsen K.C., Lynch T., Pavlou E., Higgins M., Nygaard T.G.: Localization of disinhibition-dementia-parkinsonism-amyotrophy complex to 17q21–22. Am. J. Hum. Genet., 1994; 55: 1159–1165
- Wong Y.C., Krainc D.: α-synuclein toxicity in neurodegeneration: mechanism and therapeutic strategies. Nat. Med., 2017; 23: 1–13
- Yamada K., Holth J.K., Liao F., Stewart F.R., Mahan T.E., Jiang H., Cirrito J.R., Patel T.K., Hochgräfe K., Mandelkow E.M., Holtzman D.M.: Neuronal activity regulates extracellular tau in vivo. J. Exp. Med., 2014; 211: 387–393
- Yang W., Wang X., Duan C., Lu L., Yang H.: Alpha-synuclein over-expression increases phosphoprotein phosphatase 2A levels via formation of calmodulin/Src complex. Neurochem. Int., 2013; 63: 180–194
- Yarchoan M., Toledo J.B., Lee E.B., Arvanitakis Z., Kazi H., Han L.Y., Louneva N., Lee V.M., Kim S.F., Trojanowski J.Q., Arnold S.E.: Abnormal serine phosphorylation of insulin receptor substrate 1 is associated with tau pathology in Alzheimer’s disease and tauopathies. Acta Neuropathol., 2014; 128: 679–689
- Yuan A., Kumar A., Peterhoff C., Duff K., Nixon R.A.: Axonal transport rates in vivo are unaffected by tau deletion or overexpression in mice. J. Neurosci., 2008; 28: 1682–1687
- Yuzwa S.A., Macauley M.S., Heinonen J.E., Shan X., Dennis R.J., He Y., Whitworth G.E., Stubbs K.A., McEachern E.J., Davies G.J., Vocadlo D.J.: A potent mechanism-inspired O-GlcNAcase inhibitor that blocks phosphorylation of tau in vivo. Nat. Chem. Biol., 2008; 4: 483–490
- Zarranz J.J., Alegre J., Gómez-Esteban J.C., Lezcano E., Ros R., Ampuero I., Vidal L., Hoenicka J., Rodriguez O., Atarés B., Llorens V., Gomez Tortosa E., del Ser T., Muñoz D.G., de Yebenes J.G.: The new mutation, E46K, of α-synuclein causes Parkinson and Lewy body dementia. Ann. Neurol., 2004; 55: 164–173
- Zempel H., Thies E., Mandelkow E., Mandelkow E.M.: Aβ oligomers cause localized Ca2+ elevation, missorting of endogenous Tau into dendrites, Tau phosphorylation, and destruction of microtubules and spines. J. Neurosci., 2010; 30: 11938–11950
- Zhang Y., Chen K., Sloan S.A., Bennett M.L., Scholze A.R., O’Keeffe S., Phatnani H.P., Guarnieri P., Caneda C., Ruderisch N., Deng S., Liddelow S.A., Zhang C., Daneman R., Maniatis T. i wsp.: An RNA-sequencing transcriptome and splicing database of glia, neurons, and vascular cells of the cerebral cortex. J. Neurosci., 2014; 34: 11929–11947
- Zhang Y.W., Thompson R., Zhang H., Xu H.: APP processing in Alzheimer’s disease. Mol. Brain., 2011; 4: 3
- Zheng W.H., Bastianetto S., Mennicken F., Ma W., Kar S.: Amyloid beta peptide induces tau phosphorylation and loss of cholinergic neurons in rat primary septal cultures. Neuroscience, 2002; 115: 201–211