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

ホーム > 業績 > 論文 A02

論文 A02

A02-1

  1. Ishigaki S, Fujioka Y, Okada Y, Riku Y, Udagawa T, Honda D, Yokoi S, Endo K, Ikenaka K, Takagi S, Iguchi Y, Sahara N, Takashima A, Okano H, Yoshida M, Warita H, Aoki M, Watanabe H, Okado H, Katsuno M, Sobue G. Altered Tau Isoform Ratio Caused by Loss of FUS and SFPQ Function Leads to FTLD-like Phenotypes.Cell Rep. 2017 Jan 31; 18(5): 1118-1131. doi: 10.1016/j.celrep.2017.01.013. PubMed PMID:28147269.
  2. Ano Y, Dhata A, Taniguchi Y, Hoshi A, Uchida K, Takashima A, Nakayama H. Iso-α-acids, bitter components of beer, prevent inflammation and cognitive decline induced in a mouse model of Alzheimer’s disease.J Biol Chem. 2017 Jan 13. pii: jbc.M116.763813. doi: 10.1074/jbc.M116.763813. [Epub ahead of print] PubMed PMID: 28087694.
  3. Yagishita S, Suzuki S, Yoshikawa K, Iida K, Hirata A, Suzuki M, Takashima A, Maruyama K, Hirasawa A, Awaji T. Treatment of intermittent hypoxia increases phosphorylated tau in the hippocampus via biological processes common to aging.Mol Brain. 2017 Jan 5; 10(1):2. doi: 10.1186/s13041-016-0282-7. PubMed PMID: 28057021; PubMed Central PMCID: PMC5217192.
  4. Yoshitake J, Takashima A. and et a1(8th of 8 people) Modification of Tau by 8-nitro-cGMPJ Biol Chem. (2016) in press investigated.
  5. Takashima A. Mechanism of neurodegeneration through tau and therapy for Alzheimer disease.Journal of Sport and Health Science(2016), in press investigated.
  6. Furusawa, K., Asada, A., Urrutia, P., Gonzalez-Billault, C., Fukuda, M., Hisanaga, S. Cdk5 regulation of the GRAB-mediated Rab8-Rab11 cascade in axon outgrowth.J. Neurosci. 37:790-806, 2017.
  7. Akasaka-Manya, K., Kawamura, M., Tsumoto, H., Saitoh, Y., Shinobu Kitazume, S., Hatsuda, H., Miura, Y., Hisanaga, S., Murayama, S., Hashimoto, Y., Manya, H., Endo, T. Excess APP O-glycosylation by GalNAc-T6 decreases Aβ production.J. Biochem. 161:99-111, 2017.
  8. Kimura, T., Hosokawa, T., Taoka, M., Tsutsumi, K., Ando, K., Ishiguro, K., Hosokawa, M., Hasegawa, M., Hisanaga, S. Quantitative and combinatory determination of in situ phosphorylation of tau and its FTDP-17 mutants.Sci Rep.6 :33479, 2016.
  9. F Sharma, S., Tsutsumi, K., Saito, T., Asada, A., Ando, K., Tomomura, T., Hisanaga, S. The kinase activity of endosomal kinase LMTK1A regulates its cellular localization and interactions with cytoskeletons.Genes Cells. 21: 1080-1094. 2016.
  10. Tarutani, A., Suzuki, G., Shimozawa, A., Nonaka , T., Akiyama, H., Hisanaga, S., and Hasegawa, M. Effect of Fragmented Pathogenic α-Synuclein Seeds on Prion-like Propagation.J. Biol. Chem., J. Biol. Chem ., 291:18675-18688. 2016./li>
  11. Oikawa, T., Nonaka, T., Hisanaga, S., Hasegawa, M. (2016) a-Synuclein fibrils exhibit gain-of-toxic-function, promoting tau aggregation and inhibiting microtubule assembly.J Biol Chem. 291:15046-15056, 2016
  12. Shimonaka, S, Nonaka, T, Suzuki, G, Hisanaga, S, Hasegawa, M. Templated Aggregation of TAR DNA-binding Protein of 43 kDa (TDP-43) by Seeding with TDP-43 Peptide Fibrils.J Biol Chem. 291:8896-907. 2016
  13. 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. 186:398-409, 2016.
  14. Ando, K., Oka, M., Ohtake, Y., Hayashishita, M., Shimizu, S., Hisanaga, S., Iijima, K. M. Tau phosphorylation at Alzheimer’s disease-related Ser356 contributes to tau stabilization when PAR-1/MARK activity is elevated. Biochem.Biophys. Res. Commun . 478:929-934. 2016.
  15. Xie C, Miyasaka T. The role of the carboxyl-terminal sequence of tau and MAP2 in the pathogenesis of dementia.Frontiers in Molecular Neuroscience(2016) 9, Article 158
  16. Ikegawa M, Miyasaka T, Kakuda N, Ihara Y, Imaging Mass Spectrometry for the Research of Alzheimer’s Disease.J Mass Spectrom. Soc. Jpn, (2016) 64, 17-20.
  17. 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 Psychiatry87, 851-858./li>
  18. Nakashima H, Ohkawara B, Ishigaki S, Fukudome T, Ito K, Tsushima M, Konishi H, Okuno T, Yoshimura T, Ito M, Masuda A, Sobue G, Kiyama H, Ishiguro N, Ohno K. (2016) R-spondin 2 promotes acetylcholine receptor clustering at the neuromuscular junction via Lgr5.Sci Rep22, 28512.
  19. Riku Y, Watanabe H, Yoshida M, Mimuro M, Iwasaki Y, Masuda M, Ishigaki S, Katsuno M, Sobue G. (2016) Marked Involvement of the Striatal Efferent System in TAR DNA-Binding Protein 43 kDa-Related Frontotemporal Lobar Degeneration and Amyotrophic Lateral Sclerosis.J Neuropathol Exp Neurol[Epub ahead of print]
  20. Masuda, M., Senda, J., Watanabe, H., Epifanio, B., Tanaka, Y., Imai, K., Riku, Y., Li, Y., Nakamura, R., Ito, M., Ishigaki, S., Atsuta, N., Koike, H., Katsuno, M., Hattori, N., Naganawa, S., and Sobue, G. (2016). Involvement of the caudate nucleus head and its networks in sporadic amyotrophic lateral sclerosis-frontotemporal dementia continuum.Amyotroph Lateral Scler Frontotemporal Degener17, 571-579.
  21. Noda, T., Iijima, M., Noda, S., Maeshima, S., Nakanishi, H., Kimura, S., Koike, H., Ishigaki, S., Iguchi, Y., Katsuno, M., and Sobue, G. (2016). Gene Expression Profile of Inflammatory Myopathy with Malignancy is Similar to that of Dermatomyositis rather than Polymyositis.Intern Med55, 2571-2580.
  22. Ishigaki, S.*, Fujioka, Y., Okada, Y., Riku, Y., Udagawa, T., Honda, D., Yokoi, S., Endo, K., Ikenaka, K., Takagi, S., Iguchi, Y., Sahara, N., Takashima, A., Okano, H., Yoshida, M., Warita, H., Aoki, M., Watanabe, H., Okado, H., Katsuno, M., and Sobue, G. (2017). Altered Tau Isoform Ratio Caused by Loss of FUS and SFPQ Function Leads to FTLD-like Phenotypes.Cell Rep18, 1118-1131. (*corresponding author)
  23. 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.
  24. 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.
  25. 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.
  26. 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.
  27. 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.
  28. 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
  29. 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.
  30. 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.
  31. 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.
  32. 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)
  33. 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.
  34. 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.
  35. 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.
  36. 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.
  37. 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
  38. 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)
  39. 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
  40. 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.
  41. 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.
  42. 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
  43. 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
  44. 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.
  45. Kimura T, Ishiguro K, Hisanaga S. Physiological and pathological phosphorylation of tau by Cdk5.Frontiers Mol. Neurosci. 2014;7, 65.
  46. 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.
  47. 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.
  48. 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.
  49. 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.
  50. 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.
  51. 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.
  52. 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.
  53. 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.
  54. Takashima A. Tauopathies and Tau Oligomers. J Alzheimer’s Dis. 2013;37:565-8.
  55. 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.
  56. 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
  57. 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.
  58. 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.
  59. 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.
  60. Takashima A. Amyloid-beta, tau, and dementia. J Alzheimers Dis. 2009;17:729-36.
  61. 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.
  62. 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. Shimozawa A, Ono M, Takahara D, Tarutani A, Imura S, Masuda-Suzukake M, Higuchi M, Yanai K, Hisanaga SI, Hasegawa M. Propagation of pathological α-synuclein in marmoset brain.Acta Neuropathol Commun. 2017 Feb 2;5(1):12. doi: 10.1186/s40478-017-0413-0
  2. Tanaka Y, Suzuki G, Matsuwaki T, Hosokawa M, Serrano G, Beach TG, Yamanouchi K, Hasegawa M, Nishihara M. Progranulin regulates lysosomal function and biogenesis through acidification of lysosomes.Hum Mol Genet. 2017 Jan 10. pii: ddx011. doi: 10.1093/hmg/ddx011.
  3. Tarutani A, Suzuki G, Shimozawa A, Nonaka T, Akiyama H, Hisanaga S, and Hasegawa M. The Effect of Fragmented Pathogenic α-Synuclein Seeds on Prion-like Propagation.J Biol Chem291: 18675-88, 2016.
  4. Kimura T, Hosokawa T, Taoka M, Tsutsumi K, Ando K, Ishiguro K, Hosokawa M, Hasegawa M, Hisanaga S. Quantitative and combinatory determination of in situ phosphorylation of tau and its FTDP-17 mutants.Sci Rep. 6:33479, 2016.
  5. Kim C, Lv G, Lee JS, Jung BC, Masuda-Suzukake M, Hong CS, Valera E, Lee HJ, Paik SR, Hasegawa M, Masliah E, Eliezer D, Lee SJ. Exposure to bacterial endotoxin generates a distinct strain of α-synuclein fibril.Sci Rep/6:30891, 2016
  6. 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 Rep6: 23281, 2016.
  7. 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 Commun4:36, 2016
  8. Shimonaka S, Nonaka T, Suzuki G, Hisanaga SI, Hasegawa M. Templated aggregation of TDP-43 by seeding with TDP-43 peptide fibrils.J Biol Chem291: 8896-907, 2016.
  9. 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 Commun4:33, 2016.
  10. 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 Sci363:245-8, 2016.
  11. 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 Genet25:1420-33, 2016.
  12. 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 Chem291:5473-83, 2016.
  13. 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 Neuropathol131: 267-80, 2016.
  14. 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 Dis88: 148-160, 2016.
  15. 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 Neurol79:295-305, 2016.
  16. 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 Pathol186: 398-409, 2016.
  17. 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 Neurobiol53:5377-83, 2016.
  18. 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 Neurobiol42:242-54, 2016.
  19. 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. 26:488-505, 2016.
  20. 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.Neuropathology36:295-304, 2016.
  21. Hamaguchi T, Taniguchi Y, Sakai K, Kitamoto T, Takao M, Murayama S, Iwasaki Y, Yoshida M, Shimizu H, Kakita A, Takahashi H, Suzuki H, Naiki H, Sanjo N, Mizusawa H, Yamada M. Significant association of cadaveric dura mater grafting with subpial Aβ deposition and meningeal amyloid angiopathy.Acta Neuropathol. 2016 Aug; 132(2): 313-5. doi: 10.1007/s00401-016-1588-3. Epub 2016 Jun 17. No abstract available.
  22. Cescatti M, Saverioni D, Capellari S, Tagliavini F, Kitamoto T, Ironside J, Giese A, Parchi P.  Analysis of Conformational Stability of Abnormal Prion Protein Aggregates across the Spectrum of Creutzfeldt-Jakob Disease Prions.J Virol. 2016 Jun 24; 90(14): 6244-54. doi: 10.1128/ JVI.00144-16. Print 2016 Jul 15.
  23. 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 May; 96(5):581-7. doi: 10.1038/ labinvest.2016.27. Epub 2016 Feb 15.
  24. 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 Jan; 56(1): 223-30. doi: 10.1111/trf.13279. Epub 2015 Sep 8..
  25. Hayashi Y, Iwasaki Y, Takekoshi A, Yoshikura N, Asano T, Mimuro M, Kimura A, Satoh K, Kitamoto T, Yoshida M, Inuzuka T. An autopsy-verified case of FTLD-TDP type A with upper motor neuron-predominant motor neuron disease mimicking MM2-thalamic-type sporadic Creutzfeldt-Jakob disease.Prion . 2016 Nov;10(6):492-501.
  26. Hayashi Y, Yoshikura N, Takekoshi A, Yamada M, Asano T, Kimura A, Satoh K, Kitamoto T, Inuzuka T. Preserved regional cerebral blood flow in the occipital cortices, brainstem, and cerebellum of patients with V180I-129M genetic Creutzfeldt-Jakob disease in serial SPECT studies.J Neurol Sci. 2016 Nov 15;370:145-151. doi: 10.1016/j.jns.2016.09.043.
  27. Iwasaki Y, Mori K, Ito M, Mimuro M, Kitamoto T, Yoshida M.  An autopsied case of MM1 + MM2-cortical with thalamic-type sporadic Creutzfeldt-Jakob disease presenting with hyperintensities on diffusion-weighted MRI before clinical onset.Neuropathology. 2016 Jul 20.  doi: 10.1111/neup.12327. [Epub ahead of print]
  28. Nakatani E, Kanatani Y, Kaneda H, Nagai Y, Teramukai S, Nishimura T, Zhou B, Kojima S, Kono H, Fukushima M, Kitamoto T, Mizusawa H.  Specific clinical signs and symptoms are predictive of clinical course in sporadic Creutzfeldt-Jakob disease.Eur J Neurol. 2016 Sep;23(9):1455-62. doi: 10.1111/ene.13057.
  29. 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.
  30. 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]
  31. 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.
  32. 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.
  33. Hasegawa M, Nonaka T, Masuda-Suzukake M. α-Synuclein: Experimental pathology. Prion Diseases,Cold Spring Harbor Lab Press,2016 Chapter 19, in press.
  34. 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.
  35. 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.
  36. 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.
  37. 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
  38. 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.
  39. 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.
  40. 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. 
  41. 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.
  42. 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.
  43. 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.
  44. 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.
  45. 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.
  46. 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.
  47. 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]
  48. 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
  49. 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.
  50. 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]
  51. 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.
  52. 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.
  53. 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.
  54. 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.
  55. 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.
  56. 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.
  57. 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]
  58. 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.
  59. 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.
  60. 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.
  61. 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.
  62. 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.
  63. 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.
  64. 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.
  65. 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.
  66. 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.
  67. 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.
  68. 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.
  69. 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.
  70. 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.
  71. 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.
  72. Davidson YS, Barker H, Robinson AC, Thompson JC, Harris J, Troakes C, Smith B, Al-Saraj S, Shaw C, Rollinson S, Masuda-Suzukake M, Hasegawa M, Pickering-Brown S, Snowden JS, Mann DM. (2014) Brain distribution of dipeptide repeat proteins in frontotemporal lobar degeneration and motor neurone disease associated with expansions in C9ORF72. doi: 10.1186/2051-5960-2-70Acta Neuropathol Commun. 2014;2:70.
  73. Kawakami I, Hasegawa M, Arai T, Ikeda K, Oshima K, Niizato K, Aoki N, Omi K, Higashi S, Hosokawa M, Hirayasu Y, Akiyama H. (2014) Tau accumulation in the nucleus accumbens in tangle-predominant dementia. doi: 10.1186/2051-5960-2-40.Acta Neuropathol Commun. 2014;2(1):40
  74. Masuda-Suzukake M, Nonaka T, Hosokawa M, Kubo M, Shimozawa A, Akiyama H, Hasegawa M. (2014) Pathological alpha-synuclein propagates through neural networks.Acta Neuropathol Commun. 2014;2:88. doi: 10.1186/PREACCEPT-1296467154135944.
  75. Konno T, Tada M, Shiga A, Tsujino A, Eguchi H, Masuda-Suzukake M, Hasegawa M, Nishizawa M, Onodera O, Kakita K, Takahashi H. (2014) C9ORF72 repeat-associated non-ATG-translated polypeptides are distributed independently of TDP-43 in a Japanese patient with c9ALS. doi: 10.1111/nan.12157Neuropathol Appl Neurobiol. 2014;40(6):783-788.
  76. Yamashita S, Sakashita N, Yamashita T, Tawara N, Tasaki M, Kawakami K, Komohara Y, Fujiwara Y, Kamikawa M, Nakagawa T, Hirano T, Maeda Y, Hasegawa M, Takeya M, Ando Y. (2014) Concomitant accumulation of α-synuclein and TDP-43 in a patient with corticobasal degeneration. doi: 10.1007/s00415-014-7491-8J Neurol. 2014;261(11):2209-2217.
  77. Asada A, Yamazaki R, Kino Y, Saito T, Kimura T, Miyake M, Hasegawa M, Nukina N, Hisanaga S. (2014) Cyclin-dependent kinase 5 phosphorylates and induces the degradation of ataxin-2. doi: 10.1016/j.neulet.2014.01.046Neurosci Lett. 2014;563:112-117.
  78. Yamashita M, Nonaka T, Hirai S, Miwa A, Okado H, Arai T, Hosokawa M, Akiyama H, Hasegawa M. Distinct pathways leading to TDP-43-induced cellular dysfunctions. Hum Mol Genet. 2014;23:4345-56.
  79. Hasegawa M, Watanabe S, Kondo H, Akiyama H, Mann D M A, Saito Y, Murayama S. 3R and 4R tau isoforms in paired helical filaments in Alzheimer’s disease. Acta Neuropathol. 2014;127:303-5.
  80. 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; S0969-2126.
  81. Nonaka T, Masuda-Suzukake M, Arai T, Hasegawa Y, Akatsu H, Obi T, Yoshida M, Murayama S, Mann DM a, Akiyama H, Hasegawa M. Prion-like properties of pathological TDP-43 aggregates from diseased brains. Cell Rep. 2013;4:124-34.
  82. Kobayashi A, Iwasaki Y, Otsuka H, Yamada M, Yoshida M, Matsuura Y, Mohri S, Kitamoto T. Deciphering the pathogenesis of sporadic Creutzfeldt-Jakob disease with codon 129 M/V and type 2 abnormal prion protein. Acta Neuropathol Commun. 2013;1:74.
  83. Takeuchi A, Kobayashi A, Ironside JW, Mohri S, Kitamoto T. Characterization of variant Creutzfeldt-Jakob disease prions in prion protein-humanized mice carrying distinct codon 129 genotypes. J Biol Chem.2013;288:21659-66.
  84. Masuda-Suzukake M, Nonaka T, Hosokawa M, Oikawa T, Arai T, Akiyama H, Mann D, Hasegawa M. Prion-like spreading of pathological alpha-synuclein in brain. Brain. 2013;136:1128-38.
  85. Nonaka T, Watanabe ST, Iwatsubo T, Hasegawa M. Seeded aggregation and toxicity of a-synuclein and tau: cellular models of neurodegenerative diseases. J Biol Chem. 2010;285:34885-98.
  86. Nonaka T, Kametani1 F, Arai T, Akiyama H, Hasegawa M. Truncation and pathogenic mutations facilitate the formation of intracellular aggregates of TDP-43. Hum Mol Genet. 2009;18:3353-64.
  87. Hasegawa M, Arai T, Nonaka T, Kametani F, Yoshida M, Hashizume Y, Beach TG, Buratti E, Baralle F, Morita M, Nakano I, Oda T, Tsuchiya K, Akiyama H. Phosphorylated TDP-43 in frontotemporal lobar degeneration and ALS. Ann Neurol. 2008;64:60-70.

A02-3

  1. Kanazawa M, Miura M, Toriyabe M, Koyama M, Hatakeyama M, Ishikawa M, Nakajima T, Onodera O, Takahashi T, Nishizawa M, Shimohata T. Microglia preconditioned by oxygen-glucose deprivation promote functional recovery in ischemic rats.Sci Rep.2017 Feb 14;7:42582. doi: 10.1038/srep42582.
  2. Watanabe Y, Kitamura K, Nakamura K, Sanpei K, Wakasugi M, Yokoseki A, KabasawaK, Onodera O, Ikeuchi T, Kuwano R, Momotsu T, Narita I, Endo N. Associationbetween dialysis treatment and cognitive decline: A study from the Project inSado for Total Health (PROST), Japan.Geriatr Gerontol Int. 2016 Nov 21. doi: 10.1111/ggi.12937.
  3. Hayashi K, Mochizuki Y, Takeuchi R, Shimizu T, Nagao M, Watabe K, Arai N,Oyanagi K, Onodera O, Hayashi M, Takahashi.H, Kakita A, IsozakiE. Clinicopathological characteristics of patients with amyotrophic lateralsclerosis resulting in a totally locked-in state (communication Stage V).ActaNeuropathol Commun. 2016 Sep 30;4(1):107.
  4. Kitamura K, Watanabe Y, Nakamura K, Sanpei K, Wakasugi M, Yokoseki A, Onodera O, Ikeuchi T, Kuwano R, Momotsu T, Narita I, Endo N. Modifiable FactorsAssociated with Cognitive Impairment in 1,143 Japanese Outpatients: The Projectin Sado for Total Health (PROST).Dement Geriatr Cogn Dis Extra. 2016 Aug12; 6(2):341-349. eCollection 2016 May-Aug.
  5. Aizawa Y, Koyama A, Ishihara T, Onodera O, Saitoh A. Performance of areal-time PCR-based approach and droplet digital PCR in detecting humanparechovirus type 3 RNA.J Clin Virol. 2016 Nov; 84:27-31.
  6. Konno T, Yoshida K, Mizuno T, Kawarai T, Tada M, Nozaki H, Ikeda SI, NishizawaM, Onodera O, Wszolek ZK, Ikeuchi T. Clinical and genetic characterization ofadult-onset leukoencephalopathy with axonal spheroids and pigmented gliaassociated with CSF1R mutation.Eur J Neurol. 2017 Jan;24(1):37-45.
  7. Konno T, Broderick DF, Mezaki N, Isami A, Kaneda D, Tashiro Y, Tokutake T,Keegan BM, Woodruff BK, Miura T, Nozaki H, Nishizawa M, Onodera O, WszolekZK,Ikeuchi T. Diagnostic Value of Brain Calcifications in Adult-OnsetLeukoencephalopathy with Axonal Spheroids and Pigmented Glia.AJNR Am JNeuroradiol. 2017 Jan;38(1):77-83.
  8. Koyama, Akihide; Sugai, Akihiro; Kato, Taisuke; Ishihara, Tomohiko; Shiga, Atsushi; Toyoshima, Yasuko; Koyama, Misaki; Konno, Takuya; Hirokawa, Sachiko; Yokoseki, Akio; Nishizawa, Masatoyo; Kakita, Akiyoshi; Takahashi, Hitoshi; Onodera, Osamu. Increased cytoplasmic TARDBP mRNA in affected spinal motor neurons in ALS caused by abnormal
    autoregulation of TDP-43. Nuc.Acids. Res2016. in press
  9. Tada M, Konno T, Tada M, Tezuka T, Miura T, Mezaki N, Okazaki K, Arakawa M,Itoh K, Yamamoto T, Yokoo H, Yoshikura N, Ishihara K, Horie M, TakebayashiH,Toyoshima Y, Naito M, Onodera O, Nishizawa M, Takahashi H, Ikeuchi T, Kakita A.Characteristic microglial features in patients with hereditary diffuseleukoencephalopathy with spheroids.Ann Neurol 2016 Oct;80(4):554-65.
  10. Jiang H, Shimizu H, Shiga A, Tanaka M, Onodera O, Kakita A, Takahashi H.Familial amyotrophic lateral sclerosis with an I104F mutation in the SOD1 gene:Multisystem degeneration with neurofilamentous aggregates and SOD1 inclusions.Neuropathology. 2017 Feb;37(1):69-77.
  11. Takeuchi R, Tada M, Shiga A, Toyoshima Y, Konno T, Sato T, Nozaki H, Kato T, Horie M, Shimizu H, Takebayashi H, Onodera O, Nishizawa M, Kakita A, Takahashi H. Heterogeneity of cerebral TDP-43 pathology in sporadic amyotrophic lateralsclerosis: Evidence for clinico-pathologic subtypes.Acta NeuropatholCommun.2016 Jun 23;4(1):61.
  12. Koyama A, Sugai A, Kato T, Ishihara T, Shiga A, Toyoshima Y, Koyama M, Konno T, Hirokawa S, Yokoseki A, Nishizawa M, Kakita A, Takahashi H, Onodera O. Increased cytoplasmic TARDBP mRNA in affected spinal motor neurons in ALS caused by abnormal autoregulation of TDP-43.Nucleic Acids Res. 2016 Jul8;44(12):5820-36.
  13. Nozaki H, Kato T, Nihonmatsu M, Saito Y, Mizuta I, Noda T, Koike R, Miyazaki K, Kaito M, Ito S, Makino M, Koyama A, Shiga A, Uemura M, Sekine Y, Murakami A,Moritani S, Hara K, Yokoseki A, Kuwano R, Endo N, Momotsu T, Yoshida M, NishizawaM, Mizuno T, Onodera O. Distinct molecular mechanisms of HTRA1 mutants in manifesting heterozygotes with CARASIL.Neurology. 2016 May 24;86(21):1964-74.
  14. Koyama, Akihide; Sugai, Akihiro; Kato, Taisuke; Ishihara, Tomohiko; Shiga, Atsushi; Toyoshima, Yasuko; Koyama, Misaki; Konno, Takuya; Hirokawa, Sachiko; Yokoseki, Akio; Nishizawa, Masatoyo; Kakita, Akiyoshi; Takahashi, Hitoshi; Onodera, Osamu. Increased cytoplasmic TARDBP mRNA in affected spinal motor neurons in ALS caused by abnormal autoregulation of TDP-43.Nuc.Acids. Res2016. in press.
  15. Nozaki H, Kato T, Nihonmatsu M, Saito Y, Mizuta I, Noda T, Koike R, Miyazaki K, Kaito M, Ito S, Makino M, Koyama A, Shiga A, Uemura M, Sekine Y, Murakami A, Moritani S, Hara K, Yokoseki A, Kuwano R, Endo N, Momotsu T, Yoshida M, Nishizawa M, Mizuno T, Onodera O. Distinct molecular mechanisms of HTRA1 mutants in manifesting heterozygotes with CARASIL.
    Neurology. 2016; pii: 10.1212/WNL.0000000000002694.
  16. 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.
  17. Tada M, Nishizawa M, Onodera O. Roles of inositol 1,4,5-trisphosphate receptors in spinocerebellar ataxias.Neurochem Int. 2016;94:1-8.
  18. Onodera O, Nozaki H, Fukutake T. CARASIL. In: Pagon RA, Adam MP, Ardinger HH, Wallace SE, Amemiya A, Bean LJH, Bird TD, Fong CT, Mefford HC, Smith RJH, Stephens K, editors. GeneReviews® [Internet]. Seattle (WA):University of Washington, Seattle; 2016. Available from http://www.ncbi.nlm.nih.gov/books/NBK32533/”
  19. Watanabe Y, Kitamura K, Nakamura K, Sanpei K, Wakasugi M, Yokoseki A, Onodera O, Ikeuchi T, Kuwano R, Momotsu T, Narita I, Endo N. Elevated C-Reactive Protein Is Associated with Cognitive Decline in Outpatients of a General Hospital: The Project in Sado for Total Health (PROST).Dement Geriatr Cogn Dis Extra. 2016;6(1):10-9.
  20. Watanabe Y, Kitamura K, Nakamura K, Sanpei K, Wakasugi M, Yokoseki A, Onodera O, Ikeuchi T, Kuwano R, Momotsu T, Narita I, Endo N. Elevated C-Reactive Protein Is Associated with Cognitive Decline in Outpatients of a General Hospital: The Project in Sado for Total Health (PROST).Dement Geriatr Cogn Dis Extra. 2016;6(1):10-9. doi: 10.1159/000442585. eCollection 2016 Jan-Apr.
  21. Mitsui J, Matsukawa T, Sasaki H, Yabe I, Matsushima M, Dürr A, Brice A, Takashima H, Kikuchi A, Aoki M, Ishiura H, Yasuda T, Date H, Ahsan B, Iwata A, Goto J, Ichikawa Y, Nakahara Y, Momose Y, Takahashi Y, Hara K, Kakita A, Yamada M, Takahashi H, Onodera O, Nishizawa M, Watanabe H, Ito M, Sobue G, Ishikawa K, Mizusawa H, Kanai K, Hattori T, Kuwabara S, Arai K, Koyano S, Kuroiwa Y, Hasegawa K, Yuasa T, Yasui K, Nakashima K, Ito H, Izumi Y, Kaji R, Kato T, Kusunoki S, Osaki Y, Horiuchi M, Kondo T, Murayama S, Hattori N, Yamamoto M, Murata M, Satake W, Toda T, Filla A, Klockgether T, Wüllner U, Nicholson G, Gilman S, Tanner CM, Kukull WA, Stern MB, Lee VM, Trojanowski JQ, Masliah E, Low PA, Sandroni P, Ozelius LJ, Foroud T, Tsuji S. Variants associated with
    Gaucher disease in multiple system atrophy.Ann Clin Transl Neurol. 2015;2(4):417-26. “
  22. Tada M, Nishizawa M, Onodera O. Redefining cerebellar ataxia in degenerative ataxias: lessons from recent research on cerebellar systems.J Neurol Neurosurg Psychiatry . 2015;86(8):922-8.
  23. Nozaki H, Sekine Y, Fukutake T, Nishimoto Y, Shimoe Y, Shirata A, Yanagawa S, Hirayama M, Tamura M, Nishizawa M, Onodera O. Characteristic features and progression of abnormalities on MRI for CARASIL.Neurology. 2015;4;85(5):459-63.
  24. Akimoto C, Volk AE, van Blitterswijk M, Van den Broeck M, Leblond CS, Lumbroso S, Camu W, Neitzel B, Onodera O, van Rheenen W, Pinto S, Weber M, Smith B, Proven M, Talbot K, Keagle P, Chesi A, Ratti A, van der Zee J, Alstermark H, Birve A, Calini D, Nordin A, Tradowsky DC, Just W, Daoud H, Angerbauer S, DeJesus-Hernandez M, Konno T, Lloyd-Jani A, de Carvalho M, Mouzat K, Landers JE, Veldink JH, Silani V, Gitler AD, Shaw CE, Rouleau GA, van den Berg LH, Van Broeckhoven C, Rademakers R, Andersen PM, Kubisch C. A blinded international study on the reliability of genetic testing for GGGGCC-repeat expansions in C9orf72 reveals marked differences in results among 14 laboratories.J Med Genet. 2014;51(6):419-24.
  25. Yasui K, Yabe I, Yoshida K, Kanai K, Arai K, Ito M, Onodera O, Koyano S, Isozaki E, Sawai S, Adachi Y, Sasaki H, Kuwabara S, Hattori T, Sobue G, Mizusawa H, Tsuji S, Nishizawa M, Nakashima K. A 3-year cohort study of the natural history of spinocerebellar ataxia type 6 in Japan.Orphanet J Rare Dis. 2014;9:118.
  26. Tamiya G, Makino S, Hayashi M, Abe A, Numakura C, Ueki M, Tanaka A, Ito C, Toshimori K, Ogawa N, Terashima T, Maegawa H, Yanagisawa D, Tooyama I, Tada M, Onodera O, Hayasaka K. A mutation of COX6A1 causes a recessive axonal or mixed form of Charcot-Marie-Tooth disease.Am J Hum Genet. 2014; 4;95(3):294-300.
  27. Nozaki H, Nishizawa M, Onodera O. Features of cerebral autosomal recessive arteriopathy with subcortical infarcts and leukoencephalopathy.Stroke. 2014;45(11):3447-53.
  28. 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.
  29. 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.
  30. 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.
  31. Ishihara T, Ariizumi Y, Shiga A, et al. Decreased number of Gemini of coiled bodies and U12 snRNA level in amyotrophic lateral sclerosis. Hum Mol Genet. 2013;22:4136-47.
  32. Shiga A, Nozaki H, Yokoseki A, et al. Cerebral small-vessel disease protein HTRA1 controls the amount of TGF-β 1 via cleavage of proTGF-beta 1. Hum Mol Genet. 2011;20:1800-10.
  33. Takahashi T, Katada S, Onodera O. Polyglutamine Diseases: Where does Toxicity Come from? What is Toxicity? Where are We Going? J Mol Cell Biol 2010;2:180-91.
  34. Tada M, Yokoseki A, Sato T, Makifuchi T, Onodera O. Early-Onset Ataxia with Ocular Motor Apraxia and Hypoalbuminemia/Ataxia with Oculomotor Apraxia 1. In: Ahmad SI, ed.Diseases of DNA Repair; 2010:21-33.
  35. Hara K, Shiga A, Fukutake T, et al. Association of HTRA1 Mutations and Familial Ischemic Cerebral Small-Vessel Disease. N Engl J Med. 2009;360:1729-39.
  36. Yokoseki A, Shiga A, Tan C-F, et al. TDP-43 mutation in familial amyotrophic lateral sclerosis. Ann Neurol. 2008;63:538-42.
  37. Takahashi T, Kikuchi S, Katada S, Nagai Y, Nishizawa M, Onodera O. Soluble polyglutamine oligomers formed prior to inclusion body formation are cytotoxic. Hum Mol Genet. 2008;17: 345-56.
  38. Nishihira Y, Tan C-F, Onodera O, et al. Sporadic amyotrophic lateral sclerosis: two pathological patterns shown by analysis of distribution of TDP-43-immunoreactive neuronal and glial cytoplasmic inclusions. Acta Neuropathol. 2008;116:169-82.
  39. Takahashi T, Tada M, Igarashi S, et al. Aprataxin, causative gene product for EAOH/AOA1, repairs DNA single-strand breaks with damaged 3 ‘-phosphate and 3 ‘-phosphoglycolate ends. Nucleic Acids Res. 2007;35:3797-809.
  40. Date H, Onodera O, Tanaka H, et al. Early-onset ataxia with ocular motor apraxia and hypoalbuminemia is caused by mutations in a new HIT superfamily gene. Nat Genet. 2001;29:184-8.

A02-公募班員

  1. Baba T, Hosokai Y, Nishio Y, Kikuchi A, Hirayama K, Suzuki K, Hasegawa T, Aoki M, Takeda A, Mori E. Longitudinal study of cognitive and cerebral metabolic changes in Parkinson’s disease.J Neurol Sci372, 288-293, 2017
  2. Kikuchi A, Okamura N, Hasegawa T, Harada R, Watanuki S, Funaki Y, Kobayashi M, Tano O, Baba T, Sugeno N, Oshima R, Yoshida S, Kobayashi J, Ezura M, Hiraoka K, Mugikura S, Takase K, Iwata R, Taki Y, Furukawa K, HArai H, Furumoto S, Tashiro M, Yanai K, Kudo Y, Takeda A,Aoki M. In vivo visualization of tau pathology using 18F-THK5351 PET in corticobasal syndrome.Neurology87, 2309-2316, 2016
  3. Oshima R, Hasegawa T*, Tamai K, Sugeno N, Yoshida S, Kobayashi J, Kikuchi A, Baba T, Futatsugi A, Sato I, Satoh K, Takeda A, Aoki M, Tanaka N. ESCRT-0 dysfunction compromises autophagic degradation of protein aggregates and facilitates ER stress-mediated neurodegeneration via apoptotic and necroptotic pathways.Sci Rep6:24997, 2016 DOI: 10.1038/srep24997
  4. Odagiri H, Baba T, Nishio Y, Iizuka O, Matsuda M, Inoue K, Kikuchi A, Hasegawa T, Aoki M, Takeda A, Taki Y, Mori E. On the utility of MIBG SPECT/CT in evaluating cardiac sympathetic dysfunction in Lewy body diseases.PLoS One11(4), e0152746, 2016 DOI: 10.1371/journal.pone.0152746
  5. Okano M, Matsuo H, Nishimura Y, Hozumi K, Yoshioka S, Tonoki A, Itoh M. Mib1 modulates dynamin 2 recruitment via Snx18 to promote Dll1 endocytosis for efficient Notch signaling.Genes Cells. 2016 May;21(5):425-41. doi: 10.1111/gtc.12350.
  6. Mizoguchi T, Kawakami K, Itoh M. Genesis. Zebrafish lines expressing UAS-driven red probes for monitoring cytoskeletal dynamics.Genesis2016 Sep; 54(9):483-9. doi: 10.1002/dvg.22955.
  7. Matsuda M, Rand K, Palardy G, Shimizu N, Ikeda H, Dalle Nogare D, Itoh M, Chitnis AB. Epb41l5 competes with Delta as a substrate for Mib1 to coordinate specification and differentiation of neurons.Development. 2016 Sep 1;143(17):3085-96. doi: 10.1242/dev.138743.
  8. Liu L, Wada H, Matsubara N, Hozumi K, Itoh M. Identification of Domains for Efficient Notch Signaling Activity in Immobilized Notch Ligand Proteins.J Cell Biochem. 2017 Apr;118(4):785-796.
  9. Tanabe K, Itoh M, Tonoki A. Age-Related Changes in Insulin-like Signaling Lead to Intermediate-Term Memory Impairment in Drosophila.Cell Rep. 2017 Feb 14;18(7):1598-1605. doi: 10.1016/j.celrep.2017.01.053.
  10. Yamada K. Methods Mol Biol. 2017;1523:285-296. In Vivo Microdialysis of Brain Interstitial Fluid for the Determination of Extracellular Tau Levels. Yamada K
     Shibata Y, Tokunaga F, Goto E, Komatsu G, Gohda J, Saeki Y, Tanaka K, Sawasaki T, Inoue S, Oshiumi H, Seya T, Nakano H, Tanaka Y, Iwai K and Inoue J. HTLV-1 Tax Induces Formation of the Active Mactomolecular IKK Complex by Generating Lys63- and Met1-Linked Hybrid Polyubiquitin chains.PLoS Pathog. 13:e1006162. (2017)
  11. Shumpei Fujii, Hiromitsu Tanaka, Tomoo Hirano “Detection and characterization of individual endocytosis of AMPA-type glutamate receptor around postsynaptic membrane”Genes to Cells, in press
  12. Yoon W.H., Sandoval H.,Nagarkar-Jaiswal S.,Jaiswal M.,Yamamoto S., Haelterman N.A., Putluri N., Putluri V., Sreekumar A., Tos T., Aksoy A., Donti T., Graham B.H., Ohno M., Nishi E., Hunter J., Muzny D.M.,Carmichael J.,Shen J.,Arboleda V.A.,Nelson S.F., Wangler M.F.,Karaca E.,Lupski J.R.,Bellen H. Loss of Nardilysin, a mitochondrial co-chaperone for α-Ketoglutarate Dehydrogenase, promotes mTORC1 activation and neurodegeneration.Neuron, 93, 1-17, Jan.4, 2017
  13. Nishi K, Sato Y, Ohno M, Hiraoka Y, Saijo S, Sakamoto J, Chen P-M, Morita Y, Matsuda S, Iwasaki K, Sugizaki K, Harada N, Mukumoto Y, Kiyonari H, Furuyama K, Kawaguchi Y, Uemoto S, Kita T, Inagaki N, Kimura T and Nishi E Nardilysin is required for maintaining pancreatic β-Cell Function.Diabetes, 65(10):3015-27, Oct., 2016
  14. Hiwasa T, Zhang X-M, Kimura R, Ohno M, Chen P-M, Nishi E, Ono K, Kimura T, Kamitsukasa I, Wada T, Aotsuka A, Mine S, Takizawa H, Kashiwado K, Takemoto M, Kobayashi K, Kawamura H, Ishibashi R, Yokote K, Nakamura R, Tomiyoshi G, Shinmen N and Kuroda H. Elevated Adiponectin Antibody Levels in Sera of Patients with Atherosclerosisrelated Coronary Artery Disease, Cerebral Infarction and Diabetes Mellitus.J Circ Biomark, 5:8, 2016
  15. Nandita Rani Das, Hironori Miyata, Hideyuki Hara, Keiji Uchiyama, Junji Chida, Masashi Yano, Hitomi Watanabe, Gen Kondoh, Suehiro Sakaguchi: Effects of prion protein devoid of the N-terminal residues 25-50 on prion pathogenesis in mice. Arch Virol. 2017 Mar 2. doi: 10.1007/s00705-017-3295-3. [Epub ahead of print]
  16. Taichi Hamanaka, Keiko Nishizawa, Yuji Sakasegawa, Ayumi Oguma, Kenta Teruya, Hiroshi Kurahashi, Hideyuki Hara, Suehiro Sakaguchi, Katsumi Doh-ura: Melanin or melanin-like substance interacts with the N-terminal portion of prion protein and inhibits abnormal prion protein formation in prion-infected cells.J Virol. 2017 Jan 11. pii: JVI.01862-16. doi: 10.1128/JVI.01862-16. [Epub ahead of print]
  17. Uemura, T., Ito, S., Ohta, Y., Tachikawa, M., Wada, T., Terasaki, T., and Ohtsuki, S. Abnormal N-Glycosylation of a Novel Missense Creatine Transporter Mutant, G561R, Associated with Cerebral Creatine Deficiency Syndromes Alters Transporter Activity and Localization.Biol Pharm Bull40, 49-55, 2017
  18. Hirayama-Kurogi, M., Takizawa, Y., Kunii, Y., Matsumoto, J., Wada, A., Hino, M., Akatsu, H., Hashizume, Y., Yamamoto, S., Kondo, T., Ito, S., Tachikawa, M., Niwa, S. I., Yabe, H., Terasaki, T., Setou, M., and Ohtsuki, S. Downregulation of GNA13-ERK network in prefrontal cortex of schizophrenia brain identified by combined focused and targeted quantitative proteomics.Journal of proteomics 158, 31-42, 2017
  19. Nakamura, K., Hirayama‐Kurogi, M., Ito, S., Kuno, T., Yoneyama, T., Obuchi, W., Terasaki, T., and Ohtsuki, S. Large‐scale multiplex absolute protein quantification of drug‐metabolizing enzymes and transporters in human intestine, liver, and kidney microsomes by SWATH‐MS: Comparison with MRM/SRM and HR‐MRM/PRM.PROTEOMICS2016
  20. Ito, S., Menard, M., Atkinson, T., Brown, L., Whitfield, J., and Chakravarthy, B. Relative expression of the p75 neurotrophin receptor, tyrosine receptor kinase A, and insulin receptor in SH-SY5Y neuroblastoma cells and hippocampi from Alzheimer’s disease patients.Neurochem Int101, 22-29, 2016
  21. Kuno, T., Hirayama-Kurogi, M., Ito, S., and Ohtsuki, S. Effect of Intestinal Flora on Protein Expression of Drug-Metabolizing Enzymes and Transporters in the Liver and Kidney of Germ-Free and Antibiotics-Treated Mice.Molecular Pharmaceutics132016
  22. Ando K, Oka M, Ohtake M, Hayashishita M, Shimizu S, Hisanaga S, Iijima KMTau phosphorylation at Alzheimer’s disease-related Ser356 contributes to tau stabilization when PAR-1/MARK activity is elevated.Biochemical and Biophysical Research Communications478 (2) 929-934, 2016
  23. Ando K, Maruko-Otake A, Ohtake Y, Hayashishita M, Sekiya M, and Iijima KM. Stabilization of microtubule-unbound tau via tau phosphorylation at Ser262/356 by Par-1/MARK contributes to augmentation of AD-related phosphorylation and Aβ42-induced tau toxicity.PLoS Genetics12(3): e1005917, 2016.
  24. Eiichi Tokuda, Itsuki Anzai, Takao Nomura, Keisuke Toichi, Masahiko Watanabe, Shinji Ohara, Seiji Watanabe, Koji Yamanaka, Yuta Morisaki, Hidemi Misawa, and Yoshiaki Furukawa“Immunochemical characterization on pathological oligomers of mutant Cu/Zn-superoxide dismutase in amyotrophic lateral sclerosis”Molecular Neurodegeneration, 2017, 12, 2
  25. Itsuki Anzai, Eiichi Tokuda, Atsushi Mukaiyama, Shuji Akiyama, Fumito Endo, Koji Yamanaka, Hidemi Misawa, and Yoshiaki Furukawa “A misfolded dimer of Cu/Zn-superoxide dismutase leading to pathological oligomerization in amyotrophic lateral sclerosis”Protein Science, 2017, 26, 484-496
  26. Itsuki Anzai, Keisuke Toichi, Eiichi Tokuda, Atsushi Mukaiyama, Shuji Akiyama, and Yoshiaki Furukawa “Screening of Drugs Inhibiting In vitro Oligomerization of Cu/Zn-Superoxide Dismutase with a Mutation Causing Amyotrophic Lateral Sclerosis”Frontiers in Molecular Biosciences, 2016, 3, 40
  27. Yoshiaki Furukawa, Yoh Suzuki, Mami Fukuoka, Kenichi Nagasawa, Kenta Nakagome, Hideaki Shimizu, Atsushi Mukaiyama, and Shuji Akiyama“A molecular mechanism realizing sequence-specific recognition of nucleic acids by TDP-43”Scientific Reports, 2016, 6, 20576
  28. Yoshiaki Furukawa, Itsuki Anzai, Shuji Akiyama, Mizue Imai, Fatima Joy Consul Cruz, Tomohide Saio, Kenichi Nagasawa, Takao Nomura, and Koichiro Ishimori “Conformational Disorder of the Most Immature Cu,Zn-Superoxide Dismutase Leading to Amyotrophic Lateral Sclerosis”The Journal of Biological Chemistry, 2016, 291, 4144-4155
  29. Eiichi Tokuda and Yoshiaki Furukawa“Copper homeostasis as a therapeutic target in amyotrophic lateral sclerosis with SOD1 mutations” Journal of Molecular Sciences, 2016, 17, 636
  30. Tanaka M, Ishizuka K, Nekooki-Machida Y, Endo R, Takashima N, Sasaki H, Komi Y, Gathercole A, Huston E, Ishii K, Hui KK, Kurosawa M, Kim SH, Nukina N, Takimoto E, Houslay MD, Sawa A. Aggregation of scaffolding protein DISC1 dysregulates phosphodiesterase 4 in Huntington’s disease.J Clin Invest. 2017.
  31. Yamanaka T, Tosaki A, Miyazaki H, Kurosawa M, Koike M, Uchiyama Y, Maity SN, Misawa H, Takahashi R, Shimogori T, Hattori N, Nukina N. Differential roles of NF-Y transcription factor in ER chaperone expression and neuronal maintenance in the CNS.Sci Rep. 2016; 6:34575.
  32. Shimizu H, Miyazaki H, Ohsawa N, Shoji S, Ishizuka-Katsura Y, Tosaki A, Oyama F, Terada T, Sakamoto K, Shirouzu M, Sekine S, Nukina N, Yokoyama S. Structure-based site-directed photo-crosslinking analyses of multimeric cell-adhesive interactions of voltage-gated sodium channel beta subunits.Sci Rep. 2016; 6:26618.
  33. Ohno M, Kimura M, Miyazaki H, Okawa K, Onuki R, Nemoto C, Tabata E, Wakita S, Kashimura A, Sakaguchi M, Sugahara Y, Nukina N, Bauer PO, Oyama F. Acidic mammalian chitinase is a proteases-resistant glycosidase in mouse digestive system.Sci Rep. 2016; 6:37756.
  34. Misawa H, Inomata D, Kikuchi M, Maruyama S, Moriwaki Y, Okuda T, Nukina N, Yamanaka T. Reappraisal of VAChT-Cre: Preference in slow motor neurons innervating type I or IIa muscle fibers.Genesis. 2016; 54(11):568-72
  35. Kino Y, Washizu C, Kurosawa M, Yamada M, Doi H, Takumi T, Adachi H, Katsuno M, Sobue G, Hicks GG, Hattori N, Shimogori T, Nukina N. FUS/TLS acts as an aggregation-dependent modifier of polyglutamine disease model mice.Sci Rep. 2016; 6:35236.
  36. Freyermuth F, Rau F, Kokunai Y, Linke T, Sellier C, Nakamori M, Kino Y, Arandel L, Jollet A, Thibault C, Philipps M, Vicaire S, Jost B, Udd B, Day JW, Duboc D, Wahbi K, Matsumura T, Fujimura H, Mochizuki H, Deryckere F, Kimura T, Nukina N, Ishiura S, Lacroix V, Campan-Fournier A, Navratil V, Chautard E, Auboeuf D, Horie M, Imoto K, Lee KY, Swanson MS, Lopez de Munain A, Inada S, Itoh H, Nakazawa K, Ashihara T, Wang E, Zimmer T, Furling D, Takahashi MP, Charlet-Berguerand N. Splicing misregulation of SCN5A contributes to cardiac-conduction delay and heart arrhythmia in myotonic dystrophy.Nat Commun. 2016; 7:11067.
  37. Yokoi N, Fukata Y, Sekiya A, Murakami T, Kobayashi K, Fukata M. (2016) Identification of PSD-95 depalmitoylating enzymes.J Neurosci36:6431-6444. (doi: 10.1523/JNEUROSCI.0419-16.2016) (equally contributed)
  38. Sugio S, Tohyama K, Oku S, Fujiyoshi K, Yoshimura T, Hikishima K, Yano R, Fukuda T, Nakamura M, Okano H, Watanabe M1, Fukata M, Ikenaka K, F Tanaka K. (2017) Astrocyte-mediated infantile-onset leukoencephalopathy mouse model.Glia65:150-168. (doi: 10.1002/glia.23084.)
  39. Cho T, Ishii-Kato A, Fukata Y, Nakayama Y, Iida K, Fukata M, Iida H. (2017) Coupling of a voltage-gated Ca2+ channel homologue with a plasma membrane H+-ATPase in yeast.Genes Cells22:94-104 (doi: 10.1111/gtc.12458.),
  40. Fukata Y, Yokoi N, Miyazaki Y, Fukata M. The LGI1-ADAM22 protein complex in synaptic transmission and synaptic disorders.Neurosci Res(doi: 10.1016/j.neures.2016.09.011), in press
  41. Fukata Y, Fukata M. Epilepsy and synaptic proteins.Curr Opin Neurobiol, in press
  42. Kozo Hamada et al., 『Proceedings of the National Academy of Sciences of the United States of America(PNAS)』 in press