T. Nonaka

发表

Shigella Protein IpaH9.8 Is Secreted from Bacteria within Mammalian Cells and Transported to the Nucleus*

C. Sasakawa, M. Hori, T. Toyotome, 2001, The Journal of Biological Chemistry.

Drug Screening for ALS Using Patient-Specific Induced Pluripotent Stem Cells

H. Hioki, T. Kaneko, F. Gage, 2012, Science Translational Medicine.

TDP-43 stabilises the processing intermediates of mitochondrial transcripts

M. Hasegawa, R. Simpson, M. Taoka, 2017, Scientific Reports.

Distinct pathways leading to TDP-43-induced cellular dysfunctions.

H. Akiyama, M. Hasegawa, M. Yamashita, 2014, Human molecular genetics.

Naohiro Egawa Cells Drug Screening for ALS Using Patient-Specific Induced Pluripotent Stem

H. Hioki, T. Kaneko, F. Gage, 2012 .

The effect of truncation on prion-like properties of α-synuclein

F. Kametani, M. Hasegawa, A. Tamaoka, 2018, The Journal of Biological Chemistry.

Abnormal phosphorylation of Ser409/410 of TDP‐43 in FTLD‐U and ALS

T. Beach, H. Akiyama, M. Hasegawa, 2008, FEBS letters.

Identification of amino‐terminally cleaved tau fragments that distinguish progressive supranuclear palsy from corticobasal degeneration

H. Akiyama, M. Hasegawa, A. Mochizuki, 2004, Annals of neurology.

Administration of truncated secretory leukoprotease inhibitor ameliorates bleomycin-induced pulmonary fibrosis in hamsters.

T. Nonaka, H. Mitsuhashi, I. Hamamura, 1996, American journal of respiratory and critical care medicine.

Phosphorylated alpha-synuclein is ubiquitinated in alpha-synucleinopathy lesions.

J. Trojanowski, D. Mann, T. Iwatsubo, 2002, The Journal of biological chemistry.

Templated Aggregation of TAR DNA-binding Protein of 43 kDa (TDP-43) by Seeding with TDP-43 Peptide Fibrils*

M. Hasegawa, T. Nonaka, G. Suzuki, 2016, The Journal of Biological Chemistry.

Truncation and pathogenic mutations facilitate the formation of intracellular aggregates of TDP-43

H. Akiyama, F. Kametani, M. Hasegawa, 2009, Alzheimer's & Dementia.

Comorbid pathologies of neurodegenerative diseases Molecular mechanisms of the co-deposition of multiple pathological proteins in neurodegenerative diseases

Masato Hasegawa, M. Hasegawa, T. Nonaka, 2018 .

Phosphorylated and aggregated TDP-43 with seeding properties are induced upon mutant Huntingtin (mHtt) polyglutamine expression in human cellular models

M. Hasegawa, L. Schaeffer, P. Leblanc, 2019, Cellular and Molecular Life Sciences.

Gain-of-function profilin 1 mutations linked to familial amyotrophic lateral sclerosis cause seed-dependent intracellular TDP-43 aggregation.

F. Kametani, M. Hasegawa, T. Nonaka, 2016, Human molecular genetics.

Kinase Inhibitor Screening Identifies Cyclin-Dependent Kinases and Glycogen Synthase Kinase 3 as Potential Modulators of TDP-43 Cytosolic Accumulation during Cell Stress

Grace E. Lidgerwood, P. Crouch, M. Hasegawa, 2013, PloS one.

C-Jun N-terminal kinase controls TDP-43 accumulation in stress granules induced by oxidative stress

C. Masters, P. Crouch, Qiao-Xin Li, 2011, Molecular Neurodegeneration.

Neuron-specific methylome analysis reveals epigenetic regulation and tau-related dysfunction of BRCA1 in Alzheimer’s disease

S. Tsuji, T. Iwatsubo, T. Ushijima, 2017, Proceedings of the National Academy of Sciences.

Epitope mapping of antibodies against TDP-43 and detection of protease-resistant fragments of pathological TDP-43 in amyotrophic lateral sclerosis and frontotemporal lobar degeneration.

D. Mann, H. Akiyama, F. Kametani, 2012, Biochemical and biophysical research communications.

[Molecular dissection of TDP-43 in ALS and FTLD].

H. Akiyama, F. Kametani, M. Hasegawa, 2010, Rinsho shinkeigaku = Clinical neurology.

Cysteine misincorporation in bacterially expressed human α‐synuclein

M. Goedert, M. Hasegawa, N. Dohmae, 2006 .

Phosphorylated TDP-43 in frontotemporal lobar degeneration and ALS

M. Morita, T. Beach, H. Akiyama, 2009 .

Analyses of the MAPT, PGRN, and C9orf72 mutations in Japanese patients with FTLD, PSP, and CBS.

N. Hattori, M. Hasegawa, H. Yoshino, 2013, Parkinsonism & related disorders.

Characterization of mineral deposits formed in cultures of a hamster tartrate-resistant acid phosphatase (TRAP) and alkaline phosphatase (ALP) double-positive cell line (CCP)

T. Nonaka, S. Imajoh-ohmi, Michiteru Yoshida, 2002, Cell and Tissue Research.

Methylene blue and dimebon inhibit aggregation of TDP‐43 in cellular models

M. Goedert, H. Akiyama, F. Kametani, 2009, FEBS letters.

Neuronal and glial inclusions in frontotemporal dementia with or without motor neuron disease are immunopositive for p62

H. Akiyama, M. Hasegawa, T. Nonaka, 2003, Neuroscience Letters.

Chorea as a clinical feature of the basophilic inclusion body disease subtype of fused-in-sarcoma-associated frontotemporal lobar degeneration

H. Akiyama, M. Hasegawa, T. Nonaka, 2016, Acta Neuropathologica Communications.

Phosphorylation of TAR DNA-binding Protein of 43 kDa (TDP-43) by Truncated Casein Kinase 1δ Triggers Mislocalization and Accumulation of TDP-43*

H. Akiyama, F. Kametani, M. Hasegawa, 2016, The Journal of Biological Chemistry.

Inhibition of TDP-43 Accumulation by Bis(thiosemicarbazonato)-Copper Complexes

P. Crouch, M. Hasegawa, Anthony R White, 2012, PloS one.

Histamine-induced differentiation of HL-60 cells. The role of cAMP and protein kinase A.

T. Nonaka, K. Tasaka, M. Mio, 1992, Biochemical pharmacology.

Ciclesonide uptake and metabolism in human alveolar type II epithelial cells (A549)

Y. Katsuura, T. Nonaka, R. Nave, 2007, BMC pharmacology.

[TDP-43 proteinopathies, toward understanding of the molecular pathogenesis].

H. Akiyama, F. Kametani, M. Hasegawa, 2009, Rinsho shinkeigaku = Clinical neurology.

Casein kinase 1δ/ε phosphorylates fused in sarcoma (FUS) and ameliorates FUS-mediated neurodegeneration

T. Iwatsubo, F. Kametani, M. Hasegawa, 2022, The Journal of biological chemistry.

Extensive deamidation at asparagine residue 279 accounts for weak immunoreactivity of tau with RD4 antibody in Alzheimer’s disease brain

D. Mann, H. Akiyama, F. Kametani, 2013, Acta Neuropathologica Communications.

TDP-43 is deposited in the Guam parkinsonism-dementia complex brains.

H. Akiyama, M. Hasegawa, K. Oyanagi, 2007, Brain : a journal of neurology.

Effect of TEI-9874, an inhibitor of immunoglobulin E production, on allergen-induced asthmatic model in rats.

T. Nonaka, K. Takahashi, H. Mitsuhashi, 2000, European journal of pharmacology.

Uptake and metabolism of ciclesonide and retention of desisobutyryl-ciclesonide for up to 24 hours in rabbit nasal mucosa

T. Nonaka, Hideyuki Sato, R. Nave, 2007, BMC Pharmacology.

The Wnt/Ca2+ pathway is involved in interneuronal communication mediated by tunneling nanotubes

M. Hasegawa, C. Zurzolo, Yuan-Ju Wu, 2019, The EMBO journal.

Prolonged nitric oxide treatment induces tau aggregation in SH-SY5Y cells

M. Hasegawa, Y. Chin, T. Nonaka, 2011, Neuroscience Letters.

α-synuclein strains that cause distinct pathologies differentially inhibit proteasome

M. Hasegawa, Y. Saeki, T. Nonaka, 2020, bioRxiv.

Kinetic characterization of lysine-specific metalloendopeptidases from Grifola frondosa and Pleurotus ostreatus fruiting bodies.

T. Nonaka, K. Takio, Y. Hashimoto, 1998, Journal of biochemistry.

C9ORF72 dipeptide repeat poly-GA inclusions promote intracellular aggregation of phosphorylated TDP-43

M. Hasegawa, H. Okado, T. Nonaka, 2018, Human molecular genetics.

Reducing TDP-43 aggregation does not prevent its cytotoxicity

M. Cynader, W. Jia, T. Nonaka, 2013, Acta neuropathologica communications.

[Intracellular seeded aggregation of TDP-43].

M. Hasegawa, T. Nonaka, 2012, Rinsho shinkeigaku = Clinical neurology.

Phosphorylated and ubiquitinated TDP‐43 pathological inclusions in ALS and FTLD‐U are recapitulated in SH‐SY5Y cells

H. Akiyama, M. Hasegawa, E. Buratti, 2009, FEBS letters.

Intracellular dynamics of Ataxin-2 in the human brains with normal and frontotemporal lobar degeneration with TDP-43 inclusions

H. Akiyama, M. Hasegawa, T. Nonaka, 2020, Acta neuropathologica communications.

Establishment and characterization of tartrate-resistant acid phosphatase and alkaline phosphatase double positive cell lines

H. Moriya, T. Nonaka, S. Imajoh-ohmi, 2001, Cell and Tissue Research.

In Vitro Metabolism of Ciclesonide in the Upper and Lower Airways

Y. Katsuura, T. Nonaka, Hideyuki Sato, 2007 .

Pharmacological activities of TEI‐8362, a novel inhibitor of human neutrophil elastase

T. Nonaka, K. Fujii, H. Mitsuhashi, 1999, British journal of pharmacology.

Differential diagnosis of amyotrophic lateral sclerosis from Guillain–Barré syndrome by quantitative determination of TDP-43 in cerebrospinal fluid

H. Akiyama, M. Hasegawa, M. Yamashita, 2014, The International journal of neuroscience.

BopC Is a Novel Type III Effector Secreted by Bordetella bronchiseptica and Has a Critical Role in Type III-dependent Necrotic Cell Death*

A. Abe, A. Kuwae, T. Nonaka, 2006, Journal of Biological Chemistry.

Cleavage at the carboxyl-terminus of Ku80 during apoptosis in human Jurkat T cells.

Masahiko Kato, T. Nonaka, S. Imajoh-ohmi, 2005, Journal of biochemistry.

Shigella flexneri YSH6000 induces two types of cell death, apoptosis and oncosis, in the differentiated human monoblastic cell line U937.

C. Sasakawa, A. Kuwae, T. Nonaka, 1999, FEMS microbiology letters.

Shigella £exneri YSH6000 induces two types of cell death, apoptosis and oncosis, in the di¡erentiated human monoblastic cell line U937

C. Sasakawa, A. Kuwae, T. Nonaka, 1999 .

Shigella-induced necrosis and apoptosis of U937 cells and J774 macrophages.

A. Kuwae, T. Nonaka, S. Imajoh-ohmi, 2003, Microbiology.

Methylene Blue Reduced Abnormal Tau Accumulation in P301L Tau Transgenic Mice

H. Akiyama, M. Hasegawa, M. Yamashita, 2012, PloS one.

In vitro activation of the corticosteroid ciclesonide in animal nasal mucosal homogenates

T. Nonaka, Hideyuki Sato, R. Nave, 2007, Biopharmaceutics & drug disposition.

Prion-like spreading of pathological α-synuclein in brain

Masato Hasegawa, Tetsuaki Arai, Masato Hosokawa, 2013, Brain : a journal of neurology.

Cysteine misincorporation in bacterially expressed human alpha-synuclein.

M. Goedert, M. Hasegawa, N. Dohmae, 2006, FEBS letters.

Prion-like properties of assembled TDP-43

M. Hasegawa, T. Nonaka, 2019, Current Opinion in Neurobiology.

[Frontotemporal dementia (FTD) and genetic mutations including progranulin gene].

M. Morita, T. Beach, H. Akiyama, 2008, Rinsho shinkeigaku = Clinical neurology.

Phosphorylated and aggregated TDP-43 with seeding properties are induced upon mutant Huntingtin (mHtt) polyglutamine expression in human cellular models

M. Hasegawa, L. Schaeffer, P. Leblanc, 2019, Cellular and Molecular Life Sciences.

Transcriptional regulation of the hypocretin/orexin gene by NR6A1.

E. Mignot, Susumu Tanaka, T. Kodama, 2010, Biochemical and biophysical research communications.

Inositol Hexakisphosphate Kinase 2 Promotes Cell Death in Cells with Cytoplasmic TDP-43 Aggregation

E. Nagata, M. Hasegawa, J. Itoh, 2015, Molecular Neurobiology.

Amino Acid Sequences of Metalloendopeptidases Specific for Acyl-Lysine Bonds from Grifola frondosa and Pleurotus ostreatus Fruiting Bodies*

N. Dohmae, T. Nonaka, K. Takio, 1997, The Journal of Biological Chemistry.

Supramolecular structure of the Shigella type III secretion machinery: the needle part is changeable in length and essential for delivery of effectors

C. Sasakawa, E. Katayama, A. Kuwae, 2000, The EMBO journal.

Characterization of a thermostable lysine-specific metalloendopeptidase from the fruiting bodies of a basidiomycete, Grifola frondosa.

N. Dohmae, T. Nonaka, Y. Hashimoto, 1995, Journal of biochemistry.

Human NPCs can degrade α–syn fibrils and transfer them preferentially in a cell contact-dependent manner possibly through TNT-like structures

M. Hasegawa, C. Zurzolo, T. Nonaka, 2019, Neurobiology of Disease.

TDP-43 is a component of ubiquitin-positive tau-negative inclusions in frontotemporal lobar degeneration and amyotrophic lateral sclerosis.

H. Akiyama, M. Hasegawa, H. Mori, 2006, Biochemical and biophysical research communications.

Prion-like properties of pathological TDP-43 aggregates from diseased brains.

D. Mann, H. Akiyama, M. Hasegawa, 2013, Cell reports.

Chorea as a clinical feature of the basophilic inclusion body disease subtype of fused-in-sarcoma-associated frontotemporal lobar degeneration

H. Akiyama, M. Hasegawa, T. Nonaka, 2016, Acta neuropathologica communications.

Identification of casein kinase-1 phosphorylation sites on TDP-43.

H. Akiyama, F. Kametani, M. Hasegawa, 2009, Biochemical and biophysical research communications.

Prion-like mechanisms and potential therapeutic targets in neurodegenerative disorders.

M. Hasegawa, T. Nonaka, M. Masuda-Suzukake, 2017, Pharmacology & therapeutics.

Casein kinase 2 is the major enzyme in brain that phosphorylates Ser129 of human α‐synuclein: Implication for α‐synucleinopathies

D. Mann, T. Iwatsubo, M. Goedert, 2007 .

Monitoring of caspase-8/FLICE processing and activation upon Fas stimulation with novel antibodies directed against a cleavage site for caspase-8 and its substrate, FLICE-like inhibitory protein (FLIP).

T. Nonaka, S. Imajoh-ohmi, Y. Niikura, 2002, Journal of biochemistry.

Caspases cleave the amino-terminal calpain inhibitory unit of calpastatin during apoptosis in human Jurkat T cells.

M. Maki, T. Nonaka, S. Imajoh-ohmi, 2000, Journal of biochemistry.

Human tauopathy-derived tau strains determine the substrates recruited for templated amplification

D. Mann, M. Hasegawa, S. Murayama, 2021, Brain : a journal of neurology.

Biochemical classification of tauopathies by immunoblot, protein sequence and mass spectrometric analyses of sarkosyl-insoluble and trypsin-resistant tau

D. Mann, K. Arima, T. Iwatsubo, 2015, Acta Neuropathologica.

Extensive deamidation at asparagine residue 279 accounts for weak immunoreactivity of tau with RD4 antibody in Alzheimer’s disease brain

D. Mann, H. Akiyama, F. Kametani, 2013, Acta neuropathologica communications.

Phosphorylated TDP‐43 in frontotemporal lobar degeneration and amyotrophic lateral sclerosis

M. Morita, H. Akiyama, F. Kametani, 2008, Annals of neurology.

Seeded aggregation and toxicity of {alpha}-synuclein and tau: cellular models of neurodegenerative diseases.

T. Iwatsubo, M. Hasegawa, T. Nonaka, 2010, The Journal of biological chemistry.

Conversion of Wild-type α-Synuclein into Mutant-type Fibrils and Its Propagation in the Presence of A30P Mutant*

M. Hasegawa, T. Nonaka, S. Hisanaga, 2009, Journal of Biological Chemistry.

Extracellular association of APP and tau fibrils induces intracellular aggregate formation of tau

H. Akiyama, F. Kametani, M. Hasegawa, 2015, Acta Neuropathologica.

Ubiquitination of α-Synuclein†

T. Iwatsubo, M. Hasegawa, T. Nonaka, 2005 .

Ubiquitination of alpha-synuclein.

T. Iwatsubo, M. Hasegawa, T. Nonaka, 2005, Biochemistry.

Interplay between TDP-43 and docosahexaenoic acid-related processes in amyotrophic lateral sclerosis

M. Hasegawa, M. Portero-Otín, M. Motilva, 2016, Neurobiology of Disease.

Phosphorylated α-Synuclein Is Ubiquitinated in α-Synucleinopathy Lesions*

J. Trojanowski, D. Mann, T. Iwatsubo, 2002, The Journal of Biological Chemistry.

Phosphorylation of endogenous α-synuclein induced by extracellular seeds initiates at the pre-synaptic region and spreads to the cell body

M. Hasegawa, T. Nonaka, G. Suzuki, 2022, Scientific reports.

Enolase, a cellular glycolytic enzyme, is required for efficient transcription of Sendai virus genome.

T. Nonaka, S. Imajoh-ohmi, K. Mizumoto, 2001, Biochemical and biophysical research communications.

Pathological alpha-synuclein propagates through neural networks

H. Akiyama, M. Hasegawa, T. Nonaka, 2014, Acta neuropathologica communications.

The Effect of Fragmented Pathogenic α-Synuclein Seeds on Prion-like Propagation*

H. Akiyama, M. Hasegawa, T. Nonaka, 2016, The Journal of Biological Chemistry.

Prion-like properties of alpha-synuclein fibrils 1 Effect of Fragmented Pathogenic α-Synuclein Seeds on Prion-like Propagation

H. Akiyama, M. Hasegawa, T. Nonaka, 2016 .

Molecular analysis and biochemical classification of TDP-43 proteinopathy.

D. Mann, H. Akiyama, F. Kametani, 2012, Brain : a journal of neurology.

Development of a novel tau propagation mouse model endogenously expressing 3 and 4 repeat tau isoforms.

M. Hasegawa, H. Shitara, T. Nonaka, 2021, Brain : a journal of neurology.

Response to Comment on “Drug Screening for ALS Using Patient-Specific Induced Pluripotent Stem Cells”

H. Hioki, T. Kaneko, F. Gage, 2013, Science Translational Medicine.

Parkinson’s disease-associated iPLA2-VIA/PLA2G6 regulates neuronal functions and α-synuclein stability through membrane remodeling

N. Hattori, T. Hatano, Y. Miki, 2019, Proceedings of the National Academy of Sciences.

α-Synuclein fibrils subvert lysosome structure and function for the propagation of protein misfolding between cells through tunneling nanotubes

J. Bonifacino, M. Hasegawa, C. Zurzolo, 2021, PLoS biology.

Small Molecule Inhibitors of α-Synuclein Filament Assembly†

T. Iwatsubo, M. Hasegawa, T. Nonaka, 2006 .

Inositol Hexakisphosphate Kinase 2 Promotes Cell Death in Cells with Cytoplasmic TDP-43 Aggregation

E. Nagata, M. Hasegawa, J. Itoh, 2016, Molecular Neurobiology.

Molecular Dissection of TDP-43 Proteinopathies

H. Akiyama, F. Kametani, M. Hasegawa, 2011, Journal of Molecular Neuroscience.

[Significance of the TDP-43 deposition in FTLD-U and ALS].

M. Morita, T. Beach, H. Akiyama, 2008, Rinsho shinkeigaku = Clinical neurology.

Mitochondrial ferritin protects SH-SY5Y cells against H2O2-induced oxidative stress and modulates α-synuclein expression

D. Yanagisawa, I. Tooyama, T. Nonaka, 2017, Experimental Neurology.

A Cellular Model To Monitor Proteasome Dysfunction by α-Synuclein

Masato Hasegawa, M. Hasegawa, T. Nonaka, 2009, Biochemistry.

TDP-43 Prions.

Masato Hasegawa, M. Hasegawa, T. Nonaka, 2018, Cold Spring Harbor perspectives in medicine.

Casein kinase 2 is the major enzyme in brain that phosphorylates Ser129 of human alpha-synuclein: Implication for alpha-synucleinopathies.

D. Mann, T. Iwatsubo, M. Goedert, 2007, FEBS letters.

Dextran sulphate-induced tau assemblies cause endogenous tau aggregation and propagation in wild-type mice

M. Goedert, M. Hasegawa, T. Nonaka, 2020, Brain communications.

α-Synuclein: Experimental Pathology.

M. Hasegawa, T. Nonaka, M. Masuda-Suzukake, 2016, Cold Spring Harbor perspectives in medicine.

P4-261 Small molecule inhibitors of alpha-synuclein filament assembly

T. Iwatsubo, M. Goedert, M. Hasegawa, 2006, Alzheimer's & Dementia.

Inhibition of α‐synuclein fibril assembly by small molecules: Analysis using epitope‐specific antibodies

M. Goedert, M. Hasegawa, Koichi Kato, 2009, FEBS letters.

1 SEEDED AGGREGATION AND TOXICITY OF α-SYNUCLEIN AND TAU : CELLULAR MODELS OF NEURODEGENERATIVE DISEASES

T. Iwatsubo, M. Hasegawa, T. Nonaka, 2010 .

α-Synuclein Fibrils Exhibit Gain of Toxic Function, Promoting Tau Aggregation and Inhibiting Microtubule Assembly*

M. Hasegawa, A. Tamaoka, T. Nonaka, 2016, The Journal of Biological Chemistry.

In vitro recapitulation of aberrant protein inclusions in neurodegenerative diseases

M. Hasegawa, T. Nonaka, 2011, Communicative & integrative biology.

Seeded Aggregation and Toxicity of α-Synuclein and Tau

T. Iwatsubo, M. Hasegawa, T. Nonaka, 2010, The Journal of Biological Chemistry.

[The Propagation Hypothesis of Prion-like Protein Agregates in Neurodegenerative Diseases].

T. Nonaka, 2019, Brain and nerve = Shinkei kenkyu no shinpo.

Characterization of inhibitor-bound alpha-synuclein dimer: role of alpha-synuclein N-terminal region in dimerization and inhibitor binding.

H. Sasakawa, M. Hasegawa, Koichi Kato, 2010, Journal of molecular biology.

[The molecular mechanisms of intracellular TDP-43 aggregates].

M. Hasegawa, T. Nonaka, T. Arai, 2009, Brain and nerve = Shinkei kenkyu no shinpo.

Comparison of nasal tissue concentrations in rabbits following administration of hypotonic and isotonic ciclesonide suspensions

T. Nonaka, R. Nave, M. Wingertzahn, 2005 .

Assembly of the Type III Secretion Apparatus of Enteropathogenic Escherichia coli

A. Abe, A. Kuwae, T. Nonaka, 2006, Journal of bacteriology.

Cleavage of nonmuscle myosin heavy chain-A during apoptosis in human Jurkat T cells.

Masahiko Kato, T. Nonaka, H. Fukuda, 2005, Journal of biochemistry.

In vitro metabolism of ciclesonide in human nasal epithelial cells

T. Nonaka, Hideyuki Sato, R. Nave, 2007, Biopharmaceutics & drug disposition.

Frontotemporal dementia with Pick-type histology associated with Q336R mutation in the tau gene.

D. Mann, T. Révész, J. Snowden, 2004, Brain : a journal of neurology.

Prion-like properties of pathological TDP-43 aggregates from diseased brains.

D. Mann, H. Akiyama, M. Hasegawa, 2013, Cell reports.

Molecular analysis and biochemical classification of TDP-43 proteinopathy.

D. Mann, H. Akiyama, F. Kametani, 2012, Brain : a journal of neurology.

The effect of truncation on prion-like properties of (cid:2) -synuclein

F. Kametani, T. Nonaka, G. Suzuki, 2018 .

Interplay between TDP-43 and docosahexaenoic acid-related processes in amyotrophic lateral sclerosis

M. Hasegawa, M. Portero-Otín, M. Motilva, 2016, Neurobiology of Disease.

Prion-like mechanisms and potential therapeutic targets in neurodegenerative disorders.

M. Hasegawa, T. Nonaka, Masami Masuda-Suzukake, 2017, Pharmacology & therapeutics.

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

D. Mann, C. Troakes, S. Rollinson, 2015, Neuropathology and applied neurobiology.

Esterases Involved in the Metabolism of Ciclesonide (CIC) in Human Nasal Epithelial Cells (HNEC)

T. Nonaka, R. Nave, M. Wingertzahn, 2006 .

The new missense G376V-TDP-43 variant induces late-onset distal myopathy but not amyotrophic lateral sclerosis

J. Senderek, T. Nonaka, Edwige Belotti, 2023, Brain : a journal of neurology.

Small molecule inhibitors of alpha-synuclein filament assembly.

T. Nonaka, S. Hisanaga, Takayuki Oikawa, 2006, Biochemistry.

TDP-43 Prions.

M. Hasegawa, T. Nonaka, 2018, Cold Spring Harbor perspectives in medicine.

Templated Aggregation of TAR DNA-binding Protein of 43 kDa (TDP-43) by Seeding with TDP-43 Peptide Fibrils*

M. Hasegawa, T. Nonaka, G. Suzuki, 2016, The Journal of Biological Chemistry.

Potency of truncated secretory leukoprotease inhibitor assessed in acute lung injury models in hamsters.

T. Nonaka, H. Mitsuhashi, S. Asano, 1997, The Journal of pharmacology and experimental therapeutics.