Výsledky vyhledávání - "Akemi Shodai"

Akademický článek

Efficacy of oligodendrocyte precursor cells as delivery vehicles for single-chain variable fragment to misfolded SOD1 in ALS rat model

Autor: Sumio Minamiyama, Madoka Sakai, Yuko Yamaguchi, Makiko Kusui, Hideki Wada, Ryota Hikiami, Yoshitaka Tamaki, Megumi Asada-Utsugi, Akemi Shodai, Akiko Makino, Noriko Fujiwara, Takashi Ayaki, Takakuni Maki, Hitoshi Warita, Masashi Aoki, Keizo Tomonaga, Ryosuke Takahashi, Makoto Urushitani

Publikováno v: Molecular Therapy: Methods & Clinical Development, Vol 28, Iss , Pp 312-329 (2023)

Superoxide dismutase1 (SOD 1) mutation is a leading cause of familial amyotrophic lateral sclerosis (ALS). Growing evidence suggests that antibody therapy against misfolded SOD1 protein can be therapeutic. However, the therapeutic effects are limited

Externí odkaz: https://doaj.org/article/125f475f713e45e783a43ac5eb717f6d

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Akademický článek

Conformational change of RNA-helicase DHX30 by ALS/FTD-linked FUS induces mitochondrial dysfunction and cytosolic aggregates

Autor: Ryota Hikiami, Toshifumi Morimura, Takashi Ayaki, Tomoyuki Tsukiyama, Naoko Morimura, Makiko Kusui, Hideki Wada, Sumio Minamiyama, Akemi Shodai, Megumi Asada-Utsugi, Shin-ichi Muramatsu, Takatoshi Ueki, Ryosuke Takahashi, Makoto Urushitani

Publikováno v: Scientific Reports, Vol 12, Iss 1, Pp 1-15 (2022)

Abstract Genetic mutations in fused in sarcoma (FUS) cause amyotrophic lateral sclerosis (ALS). Although mitochondrial dysfunction and stress granule have been crucially implicated in FUS proteinopathy, the molecular basis remains unclear. Here, we s

Externí odkaz: https://doaj.org/article/466c0b9b2b744c3492877408d329cf97

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Akademický článek

Failure of DNA double-strand break repair by tau mediates Alzheimer’s disease pathology in vitro

Autor: Megumi Asada-Utsugi, Kengo Uemura, Takashi Ayaki, Maiko T. Uemura, Sumio Minamiyama, Ryota Hikiami, Toshifumi Morimura, Akemi Shodai, Takatoshi Ueki, Ryosuke Takahashi, Ayae Kinoshita, Makoto Urushitani

Publikováno v: Communications Biology, Vol 5, Iss 1, Pp 1-12 (2022)

Phosphorylated microtubule-associated protein tau (p-tau) accumulates at double-strand breaks (DSBs) in neurons. Loss of tau induces failure of DSB repair and excessive DSB accumulation, leading to aberrant p-tau aggregation and apoptotic neurons.

Externí odkaz: https://doaj.org/article/de0adf46df324e2681f7db4538e8e628

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Akademický článek

Conserved acidic amino acid residues in a second RNA recognition motif regulate assembly and function of TDP-43.

Autor: Akemi Shodai, Akemi Ido, Noriko Fujiwara, Takashi Ayaki, Toshifumi Morimura, Miki Oono, Tsukasa Uchida, Ryosuke Takahashi, Hidefumi Ito, Makoto Urushitani

Publikováno v: PLoS ONE, Vol 7, Iss 12, p e52776 (2012)

Accumulating evidence suggests that pathogenic TAR DNA-binding protein (TDP)-43 fragments contain a partial RNA-recognition motif domain 2 (RRM2) in amyotrophic lateral sclerosis (ALS)/frontotemporal lobar degeneration. However, the molecular basis f

Externí odkaz: https://doaj.org/article/f31541792e8d4eaba61f59ca2d2e04d7

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In vivo analysis of aggregation propensity of low levels of mislocalized TDP-43 on cytopathological and behavioral phenotype of ALS/FTLD

Autor: Hideki Wada, Ryota Hikiami, Makiko Kusui, Sumio Minamiyama, Megumi Asada-Utsugi, Akemi Shodai, Shin-ichi Muramatsu, Toshifumi Morimura, Makoto Urushitani

Publikováno v: Neuroscience research.

Mislocalization and aggregate formation of TAR DNA-biding protein of 43kD (TDP-43) in the cytoplasm are signatures of amyotrophic lateral sclerosis(ALS) and frontotemporal lobar degeneration (FTLD). However, the role of two cytopathologies in ALS/FTL

Externí odkaz: https://explore.openaire.eu/search/publication?articleId=doi_dedup___::46a81be33a366c23d9fe4483f373867a
http://hdl.handle.net/10422/00013536

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Transglutaminase 2 accelerates neuroinflammation in amyotrophic lateral sclerosis through interaction with misfolded superoxide dismutase 1

Autor: Ayako Okado-Matsumoto, Miki Oono, Koji Abe, Takashi Ayaki, Makoto Urushitani, Akemi Shodai, Ryosuke Takahashi, Yasuyuki Ohta, Akemi Ido, Naoyuki Taniguchi, Hidefumi Ito

Publikováno v: Journal of Neurochemistry. 128:403-418

Although the aberrant assembly of mutant superoxide dismutase 1 (mSOD1) is implicated in the pathogenesis of familial amyotrophic lateral sclerosis (ALS), the molecular basis of superoxide dismutase 1 (SOD1) oligomerization remains undetermined. We i

Externí odkaz: https://explore.openaire.eu/search/publication?articleId=doi_dedup___::3486925572a56f6e876844f11e8ba3c7
https://doi.org/10.1111/jnc.12441

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Aberrant Assembly of RNA Recognition Motif 1 Links to Pathogenic Conversion of TAR DNA-binding Protein of 43 kDa (TDP-43)

Autor: Rina Takahashi, Akemi Ido, Shigeyuki Yokoyama, Makoto Urushitani, Tsukasa Uchida, Ryo Kitahara, Ryosuke Takahashi, Soichiro Kitazawa, Yutaka Muto, Takanori Kigawa, Toshifumi Morimura, S. Suzuki, Takashi Ayaki, Noriko Fujiwara, Hidefumi Ito, Akemi Shodai, Mikako Shirouzu

Publikováno v: Journal of Biological Chemistry. 288:14886-14905

Aggregation of TAR DNA-binding protein of 43 kDa (TDP-43) is a pathological signature of amyotrophic lateral sclerosis (ALS). Although accumulating evidence suggests the involvement of RNA recognition motifs (RRMs) in TDP-43 proteinopathy, it remains

Externí odkaz: https://explore.openaire.eu/search/publication?articleId=doi_dedup___::4303ee04dd9a2b77a4f5cfd89b29c1eb
https://doi.org/10.1074/jbc.m113.451849

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CUL2-mediated clearance of misfolded TDP-43 is paradoxically affected by VHL in oligodendrocytes in ALS

Autor: Yoshitaka Tamaki, Naomi Sakashita, Toshifumi Morimura, Ryosuke Takahashi, Hidefumi Ito, Kazuchika Nishitsuji, Hirofumi Yamashita, Akemi Shodai, Makoto Urushitani, Tsukasa Uchida, Takashi Ayaki, Seiji Kaji, Yoshinori Banno, Takakuni Maki

Publikováno v: Scientific Reports

The molecular machinery responsible for cytosolic accumulation of misfolded TDP-43 in amyotrophic lateral sclerosis (ALS) remains elusive. Here we identified a cullin-2 (CUL2) RING complex as a novel ubiquitin ligase for fragmented forms of TDP-43. T

Externí odkaz: https://explore.openaire.eu/search/publication?articleId=doi_dedup___::83305a92c09c7a1b8b991e807a931f28
https://doi.org/10.1038/srep19118

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Elimination of TDP-43 inclusions linked to amyotrophic lateral sclerosis by a misfolding-specific intrabody with dual proteolytic signals

Autor: Toshifumi Morimura, Ryosuke Takahashi, Sumio Minamiyama, Yoshiaki Furukawa, Ryota Hikiami, Ikuo Tooyama, Takashi Ayaki, Yoshitaka Tamaki, Makoto Urushitani, Akemi Shodai

Publikováno v: Scientific Reports, Vol 8, Iss 1, Pp 1-16 (2018)
Scientific Reports

Aggregation of TAR DNA-binding protein of 43 kDa (TDP-43) is implicated in the pathogenesis of sporadic and certain familial forms of amyotrophic lateral sclerosis (ALS), suggesting elimination of TDP-43 aggregates as a possible therapeutic strategy.

Externí odkaz: https://explore.openaire.eu/search/publication?articleId=doi_dedup___::e1fbdf858e031b10fa0d6a66bb4c0e95
http://hdl.handle.net/10422/00012419

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Immunoreactivity of valosin-containing protein in sporadic amyotrophic lateral sclerosis and in a case of its novel mutant

Publikováno v: Acta Neuropathologica Communications

Background Mutations in the valosin-containing protein (VCP) gene were first found to cause inclusion- body myopathy with early-onset Paget disease and frontotemporal dementia (IBMPFD). Mutations in the VCP gene were later reported to occur in famili

Externí odkaz: https://explore.openaire.eu/search/publication?articleId=doi_dedup___::05d2e80c1bf060ffde6ad8c6c511602e
https://doi.org/10.1186/s40478-014-0172-0

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