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Masato Hasegawa

Showing results (41-50 of 286) with videos related to

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FEBS Letters|August 12, 2004
Phosphorylated alpha-synuclein in normal mouse brainYu Hirai, Shinobu C Fujita, Takeshi Iwatsubo, et al.
Methods in Molecular Biology (Clifton, N.J.)|May 27, 2021
Common Marmoset Model of α-Synuclein PropagationMasami Masuda-Suzukake, Aki Shimozawa, Masashi Hashimoto, et al.
The Journal of Biological Chemistry|September 1, 2010
Seeded aggregation and toxicity of {alpha}-synuclein and tau: cellular models of neurodegenerative diseasesTakashi Nonaka, Sayuri T Watanabe, Takeshi Iwatsubo, et al.
Human Molecular Genetics|February 25, 2016
Gain-of-function profilin 1 mutations linked to familial amyotrophic lateral sclerosis cause seed-dependent intracellular TDP-43 aggregationYoshinori Tanaka, Takashi Nonaka, Genjiro Suzuki, et al.
Seishin Shinkeigaku Zasshi = Psychiatria Et Neurologia Japonica|August 6, 2011
[A new dementia group caused by TDP-43 abnormality]Tetsuaki Arai, Masato Hosokawa, Masato Hasegawa, et al.
Human Molecular Genetics|June 12, 2009
Truncation and pathogenic mutations facilitate the formation of intracellular aggregates of TDP-43Takashi Nonaka, Fuyuki Kametani, Tetsuaki Arai, et al.
ACS Chemical Neuroscience|October 5, 2022
Synthesis and Evaluation of <sup>18</sup>F-Labeled Chalcone Analogue for Detection of α-Synuclein Aggregates in the Brain Using the Mouse ModelSho Kaide, Hiroyuki Watanabe, Shimpei Iikuni, et al.
Journal of Neuropathology and Experimental Neurology|November 20, 2008
Colocalization of transactivation-responsive DNA-binding protein 43 and huntingtin in inclusions of Huntington diseaseClaudia Schwab, Tetsuaki Arai, Masato Hasegawa, et al.
The Journal of Biological Chemistry|February 19, 2016
Templated Aggregation of TAR DNA-binding Protein of 43 kDa (TDP-43) by Seeding with TDP-43 Peptide FibrilsShotaro Shimonaka, Takashi Nonaka, Genjiro Suzuki, et al.
Acta Neuropathologica Communications|April 20, 2018
Potent prion-like behaviors of pathogenic α-synuclein and evaluation of inactivation methodsAiri Tarutani, Tetsuaki Arai, Shigeo Murayama, et al.
Pageof 29

Showing results (41-50 of 286) with videos related to

Sort By:
Pageof 29
FEBS Letters|August 12, 2004
Phosphorylated alpha-synuclein in normal mouse brainYu Hirai, Shinobu C Fujita, Takeshi Iwatsubo, et al.
Methods in Molecular Biology (Clifton, N.J.)|May 27, 2021
Common Marmoset Model of α-Synuclein PropagationMasami Masuda-Suzukake, Aki Shimozawa, Masashi Hashimoto, et al.
The Journal of Biological Chemistry|September 1, 2010
Seeded aggregation and toxicity of {alpha}-synuclein and tau: cellular models of neurodegenerative diseasesTakashi Nonaka, Sayuri T Watanabe, Takeshi Iwatsubo, et al.
Human Molecular Genetics|February 25, 2016
Gain-of-function profilin 1 mutations linked to familial amyotrophic lateral sclerosis cause seed-dependent intracellular TDP-43 aggregationYoshinori Tanaka, Takashi Nonaka, Genjiro Suzuki, et al.
Seishin Shinkeigaku Zasshi = Psychiatria Et Neurologia Japonica|August 6, 2011
[A new dementia group caused by TDP-43 abnormality]Tetsuaki Arai, Masato Hosokawa, Masato Hasegawa, et al.
Human Molecular Genetics|June 12, 2009
Truncation and pathogenic mutations facilitate the formation of intracellular aggregates of TDP-43Takashi Nonaka, Fuyuki Kametani, Tetsuaki Arai, et al.
ACS Chemical Neuroscience|October 5, 2022
Synthesis and Evaluation of <sup>18</sup>F-Labeled Chalcone Analogue for Detection of α-Synuclein Aggregates in the Brain Using the Mouse ModelSho Kaide, Hiroyuki Watanabe, Shimpei Iikuni, et al.
Journal of Neuropathology and Experimental Neurology|November 20, 2008
Colocalization of transactivation-responsive DNA-binding protein 43 and huntingtin in inclusions of Huntington diseaseClaudia Schwab, Tetsuaki Arai, Masato Hasegawa, et al.
The Journal of Biological Chemistry|February 19, 2016
Templated Aggregation of TAR DNA-binding Protein of 43 kDa (TDP-43) by Seeding with TDP-43 Peptide FibrilsShotaro Shimonaka, Takashi Nonaka, Genjiro Suzuki, et al.
Acta Neuropathologica Communications|April 20, 2018
Potent prion-like behaviors of pathogenic α-synuclein and evaluation of inactivation methodsAiri Tarutani, Tetsuaki Arai, Shigeo Murayama, et al.
Pageof 29