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Takahiko Shimizu

Researcher at Chiba University

Publications -  119
Citations -  4802

Takahiko Shimizu is an academic researcher from Chiba University. The author has contributed to research in topics: Superoxide dismutase & Oxidative stress. The author has an hindex of 36, co-authored 117 publications receiving 4141 citations. Previous affiliations of Takahiko Shimizu include Hiroshima University & Kyoto University.

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Drusen, choroidal neovascularization, and retinal pigment epithelium dysfunction in SOD1-deficient mice: a model of age-related macular degeneration.

TL;DR: It is shown that mice deficient in Cu, Zn-superoxide dismutase (SOD1) have features typical of age-related macular degeneration in humans, and these findings provide evidence for the free radical theory of aging.
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Neurotoxicity and Physicochemical Properties of Aβ Mutant Peptides from Cerebral Amyloid Angiopathy: IMPLICATION FOR THE PATHOGENESIS OF CEREBRAL AMYLOID ANGIOPATHY AND ALZHEIMER'S DISEASE

TL;DR: Attenuated total reflection-Fourier transform infrared spectroscopy spectra suggested that beta-sheet content of the Abeta mutants correlates with their aggregation, however, beta-turn is also a critical secondary structure because residues at positions 22 and 23 that preferably form two-residue beta- turn significantly enhanced the aggregative ability.
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Oxidative stress causes heart failure with impaired mitochondrial respiration.

TL;DR: It is shown for the first time that the oxidative stress caused specific morphological changes of mitochondria, excess formation of superoxide, reduction of ATP, and transcriptional alterations of genes associated with heart failure in respect to cardiac contractility played a pivotal role in the development and progression of heart failure.
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Biological Significance of Isoaspartate and Its Repair System

TL;DR: The formation of isoaspartate is enhanced in amyloid-beta (Abeta) peptides in Alzheimer's disease (AD) and PIMT-deficient mice manifested neurodegenerative changes concomitant with the accumulation of L-isoaspartates in the brain.
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Analysis of the Secondary Structure of β-Amyloid (Aβ42) Fibrils by Systematic Proline Replacement

TL;DR: The results demonstrate well the large difference in aggregative ability and neurotoxicity between Aβ42 and Aβ40 and are a basis for designing new aggregation inhibitors of Aβ peptides.