新学術領域研究(研究領域提案型) 脳タンパク質老化と認知症制御

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論文 A02

A02-1

  1. Takasug T, Minegishi S, Asada A, Saito, T, Kawahara H, Hisanaga S. Two degradation pathways of the p35 Cdk5 activation subunit, dependent and independent of ubiquitination.J. Biol. Chem. 2016; 291, 4649-4657.
  2. Kimura T, Hatsuta H, Masuda-Suzukake M, Hosokawa M, Ishiguro K, Akiyama H, Murayama S, Hasegawa M, Hisanaga S. The abundance of nonphosphorylated tau in mouse and human tauopathy brains revealed by the use of Phos-tag method.Am. J. Pathol. 2016;186, 398-409.
  3. Watanabe, H., Atsuta, N., Hirakawa, A., Nakamura, R., Nakatochi, M., Ishigaki S., Iida, A., Ikegawa, S., Kubo, M., Yokoi, D., Watanabe, H., Ito, M., Katsuno, M., Izumi, Y., Morita, M., Kanai, K., Taniguchi, A., Aiba, I., Abe, K., Mizoguchi, K., Oda, M., Kano, O., Okamoto, K., Kuwabara, S., Hasegawa, K., Imai, T., Kawata, A., Aoki, M., Tsuji, S., Nakashima, K., Kaji, R., and Sobue, G. (2016). A rapid functional decline type of amyotrophic lateral sclerosis is linked to low expression of TTN.J Neurol Neurosurg PsychiatryIn press.
  4. Moreira PS, Sotiropoulos I, Silva J, Takashima A, Sousa N, Leite-Almeida H, Costa PS. The Advantages of Structural Equation Modeling to Address the Complexity of Spatial Reference Learning.Front Behav Neurosci. 2016 Feb 26;10:18. doi: 10.3389/fnbeh.2016.00018.
  5. Ohta E, Nihira T, Uchino A, Imaizumi Y, Okada Y, Akamatsu W, Takahashi K, Hayakawa H, Nagai M, Ohyama M, Ryo M, Ogino M, Murayama S, Takashima A, Nishiyama K, Mizuno Y, Mochizuki H, Obata F, Okano H. I2020T mutant LRRK2 iPSC-derived neurons in the Sagamihara family exhibit increased Tau phosphorylation through the AKT/GSK-3β signaling pathway.Hum Mol Genet. 2015;24(17):4879-900. doi: 10.1093/hmg/ddv212. Epub 2015 Jun 8.
  6. Xie C, Soeda Y, Shinzaki Y, In Y, Tomoo K, Ihara Y, Miyasaka T. Identification of key amino acids responsible for the distinct aggregation properties of microtubule-associated protein 2 and tau.J Neurochem. 2015;135(1):19-26. doi: 10.1111/jnc.13228. Epub 2015 Aug 26
  7. Yagishita S, Murayama M, Ebihara T, Maruyama K, Takashima A. Glycogen Synthase Kinase-3β-mediated Phosphorylation in the Most C-terminal Region of Protein Interacting with C Kinase 1 (PICK1) Regulates the Binding of PICK1 to Glutamate Receptor Subunit GluA2.J Biol Chem. 2015;290(49):29438-48. doi: 10.1074/jbc.M114.619668. Epub 2015 Oct 15.
  8. Soeda Y, Yoshikawa M, Almeida OF, Sumioka A, Maeda S, Osada H, Kondoh Y, Saito A, Miyasaka T, Kimura T, Suzuki M, Koyama H, Yoshiike Y, Sugimoto H, Ihara Y, and Takashima A. Toxic tau oligomer formation blocked by capping of cysteine residues with 1,2-dihydroxybenzene groups.Nat Commun. 2015;6:10216. doi: 10.1038/ncomms10216.
  9. Sotiropoulos I, Silva J, Kimura T, Rodrigues AJ, Costa P, Almeida OF, Sousa N, Takashima A. Female Hippocampus Vulnerability to Environmental Stress as Precipitating Factor in Tau Aggregation Pathology.J Alzheimers Dis. 2015;43(3):763-74. doi: 10.3233/JAD-140693.
  10. Udagawa, T., Fujioka, Y., Tanaka, M., Honda, D., Yokoi, S., Riku, Y., Ibi, D., Nagai, T., Yamada, K., Watanabe, H., Katsuno, M., Inada, T., Ohno, K., Sokabe, M., Okado, H., Ishigaki S., and Sobue, G. (2015). FUS regulates AMPA receptor function and FTLD/ALS-associated behaviour via GluA1 mRNA stabilization.Nat Commun 6, 7098. (*corresponding author)
  11. Oh-Hashi, K., Sone, A., Hikiji, T., Hirata, Y., Vitiello, M., Fedele, M., Ishigaki S., Sobue, G., and Kiuchi, K. (2015). Transcriptional and post-transcriptional regulation of transmembrane protein 132A.Mol Cell Biochem 405 291-299.
  12. Masuda, A., Takeda, J., Okuno, T., Okamoto, T., Ohkawara, B., Ito, M., Ishigaki S., Sobue, G., and Ohno, K. (2015). Position-specific binding of FUS to nascent RNA regulates mRNA length.Genes Dev 29. 2016, 1045-1057.
  13. Hikiji, T., Norisada, J., Hirata, Y., Okuda, K., Nagasawa, H., Ishigaki S., Sobue, G., Kiuchi, K., and Oh-hashi, K. (2015). A highly sensitive assay of IRE1 activity using the small luciferase NanoLuc: Evaluation of ALS-related genetic and pathological factors.Biochem Biophys Res Commun. 2016;463, 881-887.
  14. Foyez, T., Takeda-Uchimura, Y., Ishigaki S., Narentuya, Zhang, Z., Sobue, G., Kadomatsu, K., and Uchimura, K. (2015). Microglial Keratan Sulfate Epitope Elicits in Central Nervous Tissues of Transgenic Model Mice and Patients with Amyotrophic Lateral Sclerosis.Am J Pathol. 2015;185, 3053-3065.
  15. Ohoka A, Kajita M, Ikenouchi J, Yako Y, Kitamoto S, Kon S, Ikegawa M, Shimada T, Ishikawa S, Fujita Y. EPLIN is a crucial regulator for extrusion of RasV12 – transformed cells. J Cell Sci . 2015;128, 781–789
  16. Mani H., Tanaka H., Adachi T., Ikegawa M., Dai P., Fujita N., Takamatsu T. How Does the Ca2+-paradox Injury Induce Contracture in the Heart?- A Combined Study of the intracellular Ca2+ Dynamics and Cell Structures in Perfused Hearts-.Acta Histochem Cytochem . 2015;48(1)
  17. Miyasaka T, Xie C, Yoshimura S, Shinzaki Y, Yoshina S, Kage-Nakadai E, Mitani S, Ihara Y. Curcumin improves tau-induced neuronal dysfunction of nematodes.Neurobiol Aging. 2016;39:69-81. doi: 10.1016/j.neurobiolaging.2015.11.004. Epub 2015;PMID: 26923403
  18. Takada S, Mizuno K, Saito T, Asada A, Giese KP, Hisanaga S. Effects of p35 mutations associated with mental retardation on the cellular function of p35-CDK5.PLOSONE. 2015;10, e0140821.
  19. Takahashi M, Miyata H, Kametani F, Nonaka T, Akiyama H, Hisanaga S, Hasegawa M. Extracellular association of APP and tau fibrils induces intracellular aggregate formation of tau.Acta Neuropatho l. 2015;129, 893-907.
  20. Umeda T, Maekawa S, Kimura T, Takashima A, Tomiyama T, Mori H. Neurofibrillary tangle formation by introducing wild-type human tau into APP transgenic mice.Acta Neuropathol. 2014 May; 127(5):685-98. doi:10.1007/s00401-014-1259-1. Epub 2014 Feb 15. PMID: 24531886
  21. Sahara N, Murayama M, Higuchi M, Suhara T, Takashima A. Biochemical Distribution of Tau Protein in Synaptosomal Fraction of Transgenic Mice Expressing Human P301LTau. Front Neurol. 2014 Mar 11;5:26. doi: 10.3389/fneur.2014.00026. eCollection 2014. PMID: 24653715
  22. Riku, Y., Watanabe, H., Yoshida, M., Tatsumi, S., Mimuro, M., Iwasaki, Y., Katsuno, M., Iguchi, Y., Masuda, M., Senda, J., Ishigaki S., Udagawa, T., and Sobue, G. (2014). Lower motor neuron involvement in TAR DNA-binding protein of 43 kDa-related frontotemporal lobar degeneration and amyotrophic lateral sclerosis.JAMA Neurol 71. 172-179.
  23. Kimura T, Ishiguro K, Hisanaga S. Physiological and pathological phosphorylation of tau by Cdk5.Frontiers Mol. Neurosci. 2014;7, 65.
  24. Kobayashi H, Saito T, Sato K, Furusawa K, Hosokawa T, Tsutsumi K, Asada A, Kamada S, Ohshima T, Hisanaga S. Phosphorylation of Cdk5 at Tyr15 is inhibited by Cdk5 activators and does not contribute to the activation of Cdk5.J. Biol. Chem. 2014;289, 19627-19636.
  25. Ito Y, Asada A, Kobayashi H, Takano T, Sharma G, Saito T, Ohta Y, Amano M, Kaibuchi K, Hisanaga S. Preferential targeting of p39-activated Cdk5 to Rac1-induced lamellipodia.Mol Cell Neurosci.. 2014;61, 34-45.
  26. Furusawa K, Asada A, Saito T, Hisanaga S. The effect of Cyclin-dependent kinase 5 on voltage-dependent calcium channels in PC12 cells varies according to channel type and cell differentiation state..J. Neurochem. 2014; 130, 498-506, 2014.
  27. Takahashi M, Ishida M, Saito T, Ohshima T, Hisanaga S. Valproic acid downregulates Cdk5 activity via transcription of p35 mRNA.Biochem. Biophysic Res Commun. 2014;447, 678-682.
  28. Takano T, Urushibara T, Yoshioka N. Saito T. Fukuda M, Tomomura M, Hisanaga S. LMTK1 regulates dendritic formation by regulating movement of Rab11A-positive endosomes.Mol Biol. Cell. 2014;25, 1755-1768.
  29. Tanabe K, Yamazaki H, Inaguma Y, Asada A, Kimura T, Takahashi J, Taoka M, Ohshima T, Furuichi T, Isobe T, Nagat K, Shirao T, Hisanaga S. Phosphorylation of drebrin by cyclin-dependent kinase 5 and its role in neuronal migration.PLOSONE.2014;9, e92291.
  30. Asada A, Yamazaki R, Kino Y, Saito T, Kimura T, Miyake M, Nobuyuki Nukina N, Hisanaga S. Cyclin-dependent kinase 5 phosphorylates and induces the degradation of ataxin-2.Neurosci. Lett. 2014;563, 112-117.
  31. Xie C, Miyasaka T, (他7名). The Homologous Carboxyl-Terminal Domains of Microtubule-Associated Protein 2 and TAU Induce Neuronal Dysfunction and Have Differential Fates in the Evolution of Neurofibrillary Tangles. PLoS One. 2014;9:e89796.
  32. Takashima A. Tauopathies and Tau Oligomers. J Alzheimer’s Dis. 2013;37:565-8.
  33. Maruyama M, Shimada H, (他17名), Takashima A, (他5名). Imaging of tau pathology in a tauopathy mouse model and in Alzheimer patients compared to normal controls. Neuron. 2013;79:1094-108.
  34. Kimura T, Whitcomb DJ, (他11名), Takashima A, Cho K. Microtubule-associated protein tau is essential for long-term depression in the hippocampus. Philos Trans R Soc Lond B Biol Sci. 2013;369:20130144
  35. Ishigaki S, Masuda A, Fujioka Y, Iguchi Y, Katsuno M, Shibata A, Urano F, Sobue G, Ohno K. Position-dependent FUS-RNA interactions regulate alternative splicing events and transcriptions. Sci Rep. 2012;2:529.
  36. Takano, T.以下7名Hisanaga, S. LMTK1/AATYK1 Is a Novel Regulator of Axonal Outgrowth That Acts via Rab11 in a Cdk5-Dependent Manner. J Neurosci. 2012;32:6587-99.
  37. Kimura T, Fukuda T, Sahara N, Yamashita S, Murayama M, Mizoroki T, Yoshiike Y, Lee B, Sotiropoulos I, Maeda S, Takashima A. Aggregation of detergent-insoluble tau is involved in neuronal loss but not in synaptic loss. J Biol Chem. 2010;285:38692-9.
  38. Takashima A. Amyloid-beta, tau, and dementia. J Alzheimers Dis. 2009;17:729-36.
  39. Kimura T, Yamashita S, Fukuda T, Park JM, Murayama M, Mizoroki T, Yoshiike Y, Sahara N, Takashima A. Hyperphosphorylated tau in parahippocampal cortex impairs place learning in aged mice expressing wild-type human tau: Analysis of brain function in a novel neurodegenerative disease model using Mn-enhanced MRI. EMBO J. 2007;26:5143-52.
  40. Planel E, Tatebayashi Y, Miyasaka T, Liu L, Wang L, Herman M, Yu WH, Luchsinger JA, Wadzinski B, Duff KE, Takashima, A. Insulin dysfunction induces in vivo tau hyperphosphorylation through distinct mechanisms. J Neurosci. 2007;27:13635-48.

A02-2

  1. Minikel EV, Vallabh SM, Lek M, Estrada K, Samocha KE, Sathirapongsasuti JF, McLean CY, Tung JY, Yu LP, Gambetti P, Blevins J, Zhang S, Cohen Y, Chen W, Yamada M, Hamaguchi T, Sanjo N, Mizusawa H, Nakamura Y, Kitamoto T, Collins SJ, Boyd A, Will RG, Knight R, Ponto C, Zerr I, Kraus TF, Eigenbrod S, Giese A, Calero M, de Pedro-Cuesta J, Haïk S, Laplanche JL, Bouaziz-Amar E, Brandel JP, Capellari S, Parchi P, Poleggi A, Ladogana A, O’Donnell-Luria AH, Karczewski KJ, Marshall JL, Boehnke M, Laakso M, Mohlke KL, Kähler A, Chambert K, McCarroll S, Sullivan PF, Hultman CM, Purcell SM, Sklar P, van der Lee SJ, Rozemuller A, Jansen C, Hofman A, Kraaij R, van Rooij JG, Ikram MA, Uitterlinden AG, van Duijn CM; Exome Aggregation Consortium (ExAC), Daly MJ, MacArthur DG. Quantifying prion disease penetrance using large population control cohorts.Sci Transl Med. 2016;8(322):322ra9.
  2. Takeuchi A, Kobayashi A, Parchi P, Yamada M, Morita M, Uno S, Kitamoto T. Distinctive properties of plaque-type dura mater graft-associated Creutzfeldt-Jakob disease in cell-protein misfolding cyclic amplification.Lab Invest. 2016 . [Epub ahead of print]
  3. Kobayashi A, Matsuura Y, Iwaki T, Iwasaki Y, Yoshida M, Takahashi H, Murayama S, Takao M, Kato S, Yamada M, Mohri S, Kitamoto T.  Sporadic Creutzfeldt-Jakob Disease MM1+2C and MM1 are Identical in Transmission Properties. Brain Pathol. 2016;26(1):95-101.
  4. Oshita M, Yokoyama T, Takei Y, Takeuchi A, Ironside JW, Kitamoto T, Morita M.
    Efficient propagation of variant Creutzfeldt-Jakob disease prion protein using the cell-protein misfolding cyclic amplification technique with samples containing plasma and heparin.Transfusion. 2016;56(1):223-30.
  5. Hasegawa M, Nonaka T, Masuda-Suzukake M. α-Synuclein: Experimental pathology. Prion Diseases,Cold Spring Harbor Lab Press,2016 Chapter 19, in press.
  6. Hasegawa M. Molecular Mechanisms in the Pathogenesis of Alzheimer’s disease and Tauopathies-Prion-Like Seeded Aggregation and Phosphorylation.Biomolecules. 2016;6(2). pii: E24. Review.
  7. Kametani F, Obi T, Shishido T, Akatsu H, Murayama S, Saito Y, Yoshida M, & Hasegawa M. Mass spectrometric analysis of accumulated TDP-43 in amyotrophic lateral sclerosis brains.Sci Rep. 2016;6:23281. doi: 10.1038/srep23281.
  8. Tan R, Kiernan MC, Kril JJ, Mito R, Masuda-Suzukake M, Hasegawa M, McCann H, Bartley L, Dobson-Stone C, Kwok J, Hornberger M; Hodges J, Halliday G. TDP-43 in the hypoglossal nucleus identifies amyotrophic lateral sclerosis in behavioral variant frontotemporal dementia.J Neurol Sci 2016.in press.
  9. Kawakami I, Kobayashi Z, Arai T, Yokota O, Nonaka T, Aoki N, Niizato K, Oshima K, Higashi S, Katsuse O, Hosokawa M, Hasegawa M and Akiyama H. Chorea as a clinical feature of the basophilic inclusion body disease subtype of fused-in-sarcoma-associated frontotemporal lobar degeneration.Acta Neuropathol Commun2016 Apr 5; 4:36
  10. Shimonaka S, Nonaka T, Suzuki G, Hisanaga SI, Hasegawa M. Templated aggregation of TDP-43 by seeding with TDP-43 peptide fibrils.J Biol Chem. 2016; 291(17):8896-907. doi: 10.1074/jbc.M115.713552.
  11. Behrouzi R, Liu X, Wu D, Robinson AC, Tanaguchi-Watanabe S, Rollinson S, Shi J, Tian J, Hamdalla HH, Ealing J, Richardson A, Jones M, Pickering-Brown S, Davidson YS, Strong MJ, Hasegawa M, Snowden JS, Mann DM. Pathological tau deposition in Motor Neurone Disease and frontotemporal lobar degeneration associated with TDP-43 proteinopathy.Acta Neuropathol Commun. 2016;31;4:33.
  12. Mochizuki Y, Hayashi K, Nakayama Y, Shimizu T, Kamide M, Ogino M, Komori T, Hasegawa M, Isazaki E & Nakano I, ALS patinets with ability to communicate after long-term mechanical ventilation have confined degeeration to the motor neruon system.J Neurol Sci 2016,in press. 
  13. Tanaka Y, Nonaka T, Suzuki G, Kametani F, Hasegawa M. Gain-of-function profilin 1 mutations linked to familial amyotrophic lateral sclerosis cause seed-dependent intracellular TDP-43 aggregation.Hum Mol Genet. 2016; 1;25(7):1420-33. doi: 10.1093/hmg/ddw024.
  14. Nonaka T, Suzuki G, Tanaka Y, Kametani F, Hirai S, Okado H, Miyashita T, Saitoe M, Akiyama H, Masai H, Hasegawa M. Phosphorylation of TAR DNA-binding Protein of 43 kDa (TDP-43) by Truncated Casein Kinase 1δ Triggers Mislocalization and Accumulation of TDP-43.J Biol Chem. 2016, 291(11):5473-83. doi: 10.1074/jbc.M115.695379.
  15. Taniguchi‑Watanabe S, Arai T, Kametani F, Nonaka T, Masuda‑Suzukake M, Tarutani A, Murayama S, Saito Y, Arima K, Yoshida M. Akiyama H, Robinson A, Mann D, Iwatsubo T, Hasegawa M. Biochemical classification of tauopathies by immunoblot, protein sequence and mass spectrometric analyses of sarkosyl-insoluble and trypsin-resistant tau.Acta Neuropathol. 2016;131: 267-80.
  16. Cacabelos D, Ayala V, Granado-Serrano AB, Jové M, Torres P, Boada J, Cabré R, Ramírez-Núñez O, Gonzalo H, Soler-Cantero A, Serrano JC, Bellmunt MJ, Romero MP, Motilva MJ, Nonaka T, Hasegawa M, Ferrer I, Pamplona R, Portero-Otín M. Interplay between TDP-43 and docosahexaenoic acid-related processes in amyotrophic lateral sclerosis.Neurobiol Dis. 2016;88: 148-160. doi: 10.1016/j.nbd.2016.01.007.
  17. Tan R, Kril J, McGinley C, Hassani M, Suzukake M, Hasegawa M, Remika M, Kiernan M, Halliday G.Cellebeller neuronal loss in ALS cases with ATXN2 intermediate repeat expansions.Ann Neurol 2016 in press.2016; doi: 10.1002/ana.24565.
  18. Kimura T, Hatsuta H, Masuda-Suzukake M, Hosokawa M, Ishiguro K, Akiyama H, Murayama S, Hasegawa M, Hisanaga S. The abundance of nonphosphorylated tau in mouse and human tauopathy brains revealed by the use of Phos-tag method.Am J Pathol. 2016;186: 398-409, 2016.
  19. Nagata E, Nonaka T, Moriya Y, Fujii N, Okada Y, Tsukamoto H, Itoh J, Okada C, Satoh T, Arai T, Hasegawa M, Takizawa S. Inositol Hexakisphosphate Kinase 2 Promotes Cell Death in Cells with Cytoplasmic TDP-43 Aggregation.Mol Neurobiol. 2016. [Epub ahead of print]
  20. Davidson Y, Robinson A, Liu X, Wu D, Troakes C, Rollinson S, Masuda-Suzuke M, Suzuki G, Nonaka T, Shi J, Tian J, Hamdallah H, Ealing J, Richardson A, Jones M, Pickering-Brown S, Snowden J, Hasegawa M, Mann M. Neurodegeneration in Frontotemporal Lobar Degeneration and Motor Neurone Disease associated with expansions in C9orf72 is linked to TDP-43 pathology and not associated with aggregated forms of dipeptide repeat proteins.Neuropathol Appl Neurobiol. 2016;42(3):242-54. doi: 10.1111/nan.12292
  21. Ikeda C, Yokota O, Nagao S, Ishizu H, Oshima E, Hasegawa M, Okahisa Y, Terada S, Yamada N. The relationship between development of neuronal and astrocytic tau pathologies in subcortical nuclei and progression of argyrophilic grain disease.Brain Pathol. 2016 in press. doi: 10.1111/bpa.12319.
  22. Kobayashi A, Parchi P, Yamada M, Mohri S, Kitamoto T. Neuropathological and biochemical criteria to identify acquired Creutzfeldt-Jakob disease among presumed sporadic cases.Neuropathology. 2015. [Epub ahead of print]
  23. Hayashi Y, Iwasaki Y, Yoshikura N, Asano T, Hatano T, Tatsumi S, Satoh K, Kimura A, Kitamoto T, Yoshida M, Inuzuka T. Decreased regional cerebral blood flow in the bilateral thalami and medulla oblongata determined by an easy Z-score (eZIS) analysis of (99m)Tc-ECD-SPECT images in a case of MM2-thalamic-type sporadic Creutzfeldt-Jakob disease.J Neurol Sci. 2015;358(1-2):447-52.
  24. Iwasaki Y, Akagi A, Mimuro M, Kitamoto T, Yoshida M. Factors influencing the survival period in Japanese patients with sporadic Creutzfeldt-Jakob disease.J Neurol Sci. 2015;357(1-2):63-8.
  25. Kobayashi A, Teruya K, Matsuura Y, Shirai T, Nakamura Y, Yamada M, Mizusawa H, Mohri S, Kitamoto T. The influence of PRNP polymorphisms on human prion disease susceptibility: an update.Acta Neuropathol. 2015;130(2):159-70.
  26. Kon T, Miki Y, Arai A, Funamizu Y, Ueno T, Haga R, Nishijima H, Suzuki C, Nunomura J, Baba M, Oyama Y, Shiga Y, Kitamoto T, Tomiyama M. Creutzfeldt-Jakob disease with homozygous M232R mutation: A case report.J Neurol Sci. 2015; 352(1-2):108-9.
  27. Kobayashi A, Parchi P, Yamada M, Brown P, Saverioni D, Matsuura Y, Takeuchi A, Mohri S, Kitamoto T. Transmission properties of atypical Creutzfeldt-Jakob disease: a clue to disease etiology? J Virol. 2015;89(7):3939-46.
  28. Nakamaura Y, Ae R, Takumi I, Sanjo N, Kitamoto T, Yamada M, Mizusawa H. Descriptive Epidemiology of Prion Disease in Japan: 1999-2012.J Epidemiol. 2015;25(1):8-14.
  29. Iwasaki Y, Mori K, Ito M, Tatsumi S, Mimuro M, Kuwano R, Hasegawa M, Yoshida M. An autopsied case of unclassifiable sporadic four-repeat tauopathy presenting with parkinsonism and speech disturbances.Neuropathology. 2015; doi: 10.1111/neup.12274. [Epub ahead of print]
  30. Takahashi M, Miyata H, Kametani F, Nonaka T, Akiyama H, Hisanaga S, Hasegawa M. Extracellular association of APP and tau fibrils induces intracellular aggregate formation of tau.Acta Neuropathol. 2015;29: 895- 907.
  31. Matsumoto SE, Motoi Y, Ishiguro K, Tabira T, Kametani F, Hasegawa M, Hattori N. The twenty-four KDa C-terminal tau fragment increases with aging in tauopathy mice: implications of prion-like properties.Hum Mol Genet. 2015;24: 6403-16.
  32. Hosokawa M, Arai T, Masuda-Suzukake M, Kondo H, Matsuwaki T, Nishihara M, Hasegawa M, Akiyama H. (2015) Progranulin Reduction Is Associated With Increased Tau Phosphorylation in P301L Tau Transgenic Mice.J Neuropathol Exp Neurol. 2015;74:158-65.
  33. Baborie A, Griffiths TD, Jaros E, Perry R, McKeith IG, Burn DJ, Masuda-Suzukake M, Hasegawa M, Rollinson S, Pickering-Brown S, Robinson AC, Davidson YS, Mann DM. Accumulation of dipeptide repeat proteins predates that of TDP-43 in Frontotemporal Lobar Degeneration associated with hexanucleotide repeat expansions in C9ORF72 gene.Neuropathol Appl Neurobiol. 2015;41: 601-12. doi: 10.1111/nan.12178.
  34. Okamoto K, Fujita Y, Hoshino E, Tamura Y, Fukuda T, Hasegawa M, Takatama M. An autopsy case of familial amyotrophic lateral sclerosis with a TARDBP Q343R mutation.Neuropathology. 2015;35: 462-8. doi: 10.1111/neup.12209.
  35. Shirai T, Saito M, Kobayashi A, Asano M, Hizume M, Ikeda S, Teruya K, Morita M, Kitamoto T. Evaluating prion models on comprehensive mutation data of mouse PrP.Structure. 2014;22(4):560-71.
  36. Barria MA, Balachandran A, Morita M, Kitamoto T, Barron R, Manson J, Knight R, Ironside JW, Head MW. Molecular barriers to zoonotic transmission of prions.Emerg Infect Dis. 2014;20(1):88-97.
  37. Qina T, Sanjo N, Hizume M, Higuma M, Tomita M, Atarashi R, Satoh K, Nozaki I, Hamaguchi T, Nakamura Y, Kobayashi A, Kitamoto T, Murayama S, Murai H, Yamada M, Mizusawa H. Clinical features of genetic Creutzfeldt-Jakob disease with V180I mutation in the prion protein gene.BMJ Open. 2014;4(5):e004968.
  38. Iwasaki Y, Tatsumi S, Mimuro M, Kitamoto T, Yoshida M. Comparison of the clinical course of Japanese MM1-type sporadic Creutzfeldt-Jakob disease between subacute spongiform encephalopathy and panencephalopathic-type.Clin Neurol Neurosurg. 2014;121:59-63.
  39. Iwasaki Y, Tatsumi S, Mimuro M, Kitamoto T, Hashizume Y, Yoshida M. Relation between clinical findings and progression of cerebral cortical pathology in MM1-type sporadic Creutzfeldt-Jakob disease: Proposed staging of cerebral cortical pathology.J Neurol Sci. 2014;341(1-2):97-104.
  40. Kobayashi A, Matsuura Y, Mohri S, Kitamoto T.  Distinct origins of dura mater graft-associated Creutzfeldt-Jakob disease: past and future problems. Acta Neuropathol Commun. 2014;2(1):32.
  41. Tajima Y, Satoh C, Mito Y, Kitamoto T. Creutzfeldt-Jakob disease with a codon 210 mutation: first pathological observation in a Japanese patient.Neuropathology Intern Med. 2014;53(5):483-7.
  42. Araki K, Nakano Y, Kobayashi A, Matsudaira T, Sugiura A, Takao M, Kitamoto T, Murayama S, Obi T.  Extensive cortical spongiform changes with cerebellar small amyloid plaques: The clinicopathological case of MV2K+C subtype in Creutzfeldt-Jakob disease.Neuropathology . 2014 34(6):541-6.
  43. Iwasaki Y, Mori K, Ito M, Nokura K, Tatsumi S, Mimuro M, Kitamoto T, Yoshida M. Gerstmann-Straeussler-Scheinker disease with P102L prion protein gene mutation presenting with rapidly progressive clinical course.Clin Neuropathol. 2014; 33(5):344-53.
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A02-3

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  3. Yokoyama Y, Toyoshima Y, Shiga A, Tada M, Kitamura H, Hasegawa K, Onodera O, Ikeuchi T, Someya T, Nishizawa M, Kakita A, Takahashi H. Pathological and Clinical Spectrum of Progressive Supranuclear Palsy: With Special Reference to Astrocytic Tau Pathology.Brain Pathol. 2016;26(2):155-66.
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  15. Konno T, Tada M, Shiga A, Tsujino A, Eguchi H, Masuda-Suzukake M, Hasegawa M, Nishizawa M, Onodera O,Kakita A, Takahashi H. C9ORF72 repeat-associated non-ATG-translated polypeptides are distributed independently of TDP-43 in a Japanese patient with c9ALS.Neuropathol Appl Neurobiol. 2014;40(6):783-8.
  16. Fu YJ, Aida I, Tada M, Tada M, Toyoshima Y, Takeda S, Nakajima T, Naito H, Nishizawa M, Onodera O, Kakita A, Takahashi H. Progressive myoclonus epilepsy: extraneuronal brown pigment deposition and system neurodegeneration in the brains of Japanese patients with novel SCARB2 mutations.Neuropathol Appl Neurobiol. 2014 Aug;40(5):551-63.
  17. Kimura T, Jiang H, Konno T, Seto M, Iwanaga K, Tsujihata M, Satoh A, Onodera O,Kakita A, Takahashi H. Bunina bodies in motor and non-motor neurons revisited: a pathological study of an ALS patient after long-term survival on a respirator.Neuropathology. 2014 Aug;34(4):392-7.
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