最近の研究業績
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- 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.
- Nonaka T, Hasegawa M. TDP-43 Prions. Cold Spring Harb Perspect Med. pii: a024463, 2017.
- 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 5:12, 2017.
- Hasegawa M, Nonaka T, Masuda-Suzukake M. Prion-like mechanisms and potential therapeutic targets in neurodegenerative disorders. Pharmacol Ther. 2017 Apr; 172:22-33.
- Hasegawa M, Nonaka T, Masuda-Suzukake M. α-Synuclein: Experimental Pathology. Cold Spring Harb Perspect Med. 6. pii: a024273, 2016.
- Tanaka Y, Hasegawa M. Profilin 1 mutants form aggregates that induce accumulation of prion-like TDP-43. Prion. 10:283-9, 2016.
- Tarutani A, Suzuki G, Shimozawa A, Nonaka T, Akiyama H, Hisanaga S, Hasegawa M. The Effect of Fragmented Pathogenic α-Synuclein Seeds on Prion-like Propagation. J Biol Chem 291:18675-88, 2016.
- Oikawa T, Nonaka T, Terada M, Tamaoka A, Hisanaga S, Hasegawa M. α-Synuclein Fibrils Exhibit Gain of Toxic Function, Promoting Tau Aggregation and Inhibiting Microtubule Assembly. J Biol Chem 291:15046-56, 2016.
- Hasegawa M. Molecular Mechanisms in the Pathogenesis of Alzheimer's disease and Tauopathies-Prion-Like Seeded Aggregation and Phosphorylation. Biomolecules. 6. pii: E24, 2016.
- Kawakami I, Kobayashi Z, Arai T, Yokota O, Nonaka T, Aoki N, Niizato K, Oshima K, Higashi S, Katsuse O, Hosokawa M, Hasegawa M, Akiyama H. Chorea as a clinical feature of the basophilic inclusion body disease subtype of fused-in-sarcoma-associated frontotemporal lobar degeneration. Acta Neuropathol Commun 4:36, 2016.
- 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 25:1420-33, 2016.
- 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.
- 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 6: 23281, 2016.
- 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 291:5473-83, 2016.
- 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 131: 267-80, 2016.
- 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 29: 895- 907, 2015.
- 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 24: 6403-16, 2015.
- 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 74:158-65, 2015.
- Hasegawa M, Watanabe S, Kondo H, Akiyama H, Mann DM, Saito Y, Murayama S. 3R and 4R tau isoforms in paired helical filaments in Alzheimer's disease. Acta Neuropathol 127:303-5, 2014.
- Masuda-Suzukake M, Nonaka T, Hosokawa M, Kubo M, Shimozawa A, Akiyama H, *Hasegawa M. Pathological alpha-synuclein propagates through neural networks. Acta Neuropathol Commun 2:88, 2014.
- 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 124:344-349, 2014.
- Nonaka, T. et al. Prion-like properties of pathological TDP-43 aggregates from diseased brains. Cell Rep 4: 124-34, 2013.
- Masuda-Suzukake, M. et al. Prion-like spreading of pathological alpha-synuclein in brain. Brain 136, 1128-38, 2013.
- Dan, A. et al. Extensive deamidation at asparagine residue 279 accounts for weak immunoreactivity of tau with RD4 antibody in Alzheimer's disease brain. Acta Neuropathol Commun 1, 54, 2013.
- Tsuji, H. et al. Molecular analysis and biochemical classification of TDP-43 proteinopathy. Brain 135, 3380-91, 2012.
- Nonaka T, Watanabe ST, Iwatsubo T, Hasegawa M. Seeded aggregation and toxicity of alpha-synuclein and tau: cellular models of neurodegenerative diseases. J Biol Chem. 2010, 285:34885-98.
- Nonaka T, Hasegawa M. A Cellular Model To Monitor Proteasome Dysfunction by alpha-Synuclein. Biochemistry 48, 8014-22, 2009.
- 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 18, 3353-3364, 2009.
- Yonetani M, Nonaka T, Masuda M, Inukai Y, Oikawa T, Hisanaga SI, Hasegawa M. Conversion of wild-type alpha -synuclein into mutant-type fibrils and its propagation in the presence of A30P mutant. J Biol Chem 284, 7940 -7950, 2009.
- Inukai Y, Nonaka T, Arai T, Yoshida M, Hashizume Y, Beach TG, Buratti E, Baralle FE, Akiyama H, Hisanaga SI, Hasegawa M, Abnormal phosphorylation of Ser409/410 of TDP-43 in FTLD-U and ALS. FEBS Lett 582, 2899-2904, 2008
- 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 amyotrophic lateral sclerosis. Ann Neurol 64, 60-70, 2008
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