M. Hasegawa

Publications406
h-index85
Citations30,115
Highly Influential Citations1,427
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TDP-43 is a component of ubiquitin-positive tau-negative inclusions in frontotemporal lobar degeneration and amyotrophic lateral sclerosis.
α-Synuclein in filamentous inclusions of Lewy bodies from Parkinson’s disease and dementia with Lewy bodies
TLDR
It is shown thatLewy bodies and Lewy neurites from Parkinson’s disease and dementia with Lewy bodies are stained strongly by antibodies directed against amino- terminal and carboxyl-terminal sequences of α-synuclein, showing the presence of full- length or close to full-length α- synuclein.
alpha-Synuclein is phosphorylated in synucleinopathy lesions.
TLDR
It is shown by mass spectrometry analysis and studies with an antibody that specifically recognizes phospho-Ser 129 of alpha-synuclein, that this residue is selectively and extensively phosphorylated in synucleinopathy lesions and promoted fibril formation in vitro.
alpha-Synuclein in filamentous inclusions of Lewy bodies from Parkinson's disease and dementia with lewy bodies.
TLDR
It is shown thatLewy bodies and Lewy neurites from Parkinson's disease and dementia with Lewy bodies are stained strongly by antibodies directed against amino- terminal and carboxyl-terminal sequences of alpha-synuclein, showing the presence of full- length or close to full-length alpha- synuclein.
Phosphorylated TDP‐43 in frontotemporal lobar degeneration and amyotrophic lateral sclerosis
TLDR
The aim of this study was to identify the phosphorylation sites and responsible kinases, and to clarify the pathological significance ofosphorylation of TDP‐43.
α-Synuclein is phosphorylated in synucleinopathy lesions
TLDR
It is shown by mass spectrometry analysis and studies with an antibody that specifically recognizes phospho-Ser 129 of α-synuclein, that this residue is selectively and extensively phosphorylated in synucleinopathy lesions and promoted fibril formation in vitro.
Drug Screening for ALS Using Patient-Specific Induced Pluripotent Stem Cells
TLDR
The new work provides an encouraging step toward using motor neurons generated from iPSCs derived from ALS patients to learn more about what triggers the death of motor neurons in this disease and to identify new candidate drugs that may be able to slow or reverse the devastating loss ofMotor neurons.
Assembly of microtubule-associated protein tau into Alzheimer-like filaments induced by sulphated glycosaminoglycans
TLDR
It is shown that non-phosphorylated recombinant tau iso-forms with three microtubule-binding repeats form paired helical-like filaments under physiological conditions in vitro, when incubated with sulphated glycosaminoglycans such as heparin or heparan sulphate.
Proline-directed and Non-proline-directed Phosphorylation of PHF-tau (*)
TLDR
The abnormal phosphorylation of PHF-tau can be considered to consist of fetal typeosphorylation and additional proline-directed and non-proline- directed phosphorylated peptides.
Inhibition of Heparin-induced Tau Filament Formation by Phenothiazines, Polyphenols, and Porphyrins*
TLDR
Biochemical analysis revealed the formation of soluble oligomeric tau in the presence of the inhibitory compounds, suggesting that this may be the mechanism by which tau filament formation is inhibited.
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