H
Hiroshi Maeda
Researcher at Kumamoto University
Publications - 915
Citations - 67944
Hiroshi Maeda is an academic researcher from Kumamoto University. The author has contributed to research in topics: Neocarzinostatin & Nitric oxide. The author has an hindex of 103, co-authored 893 publications receiving 63370 citations. Previous affiliations of Hiroshi Maeda include Osaka University & Okayama University.
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Oxygen free radicals as pathogenic molecules in viral diseases.
Hiroshi Maeda,Takaaki Akaike +1 more
TL;DR: O2 - is the prime toxic molecule generated in the viral infection and is sustained by an enhanced supply of catabolic products of ATP and the much-elevated activity of the enzymes involved in this catabolic cascade.
Journal Article
Lipid peroxyl radicals from oxidized oils and heme-iron: implication of a high-fat diet in colon carcinogenesis.
TL;DR: Electron paramagnetic resonance and chemiluminescence studies revealed that oxidized refined vegetable oils, particularly safflower oil, readily generated lipid peroxyl radicals in the presence of various heme compounds, and the peroxy radicals did effectively cleave DNA.
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A serratial protease causes vascular permeability reaction by activation of the Hageman factor-dependent pathway in guinea pigs.
TL;DR: The 56-kilodalton protease isolated from a culture filtrate of Serratia marcescens caused vascular permeability enhancement followed by edema formation when injected into guinea pig peripheral corneas and subconjunctival space or skin, and appears to be operative in the pathogenesis of corneal edema and chemosis.
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Augmentation of tumour delivery of macromolecular drugs with reduced bone marrow delivery by elevating blood pressure.
TL;DR: The results show the advantages of macromolecules over small molecules for AT-II-induced hypertension chemotherapy, and an additive effect to that under normotensive conditions where intratumour macromolescular drug concentrations increase steadily during this period.
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Purification and characterization of four proteases from a clinical isolate of Serratia marcescens kums 3958.
TL;DR: Four distinct proteases were purified to homogeneity from culture filtrates of Serratia marcescens kums 3958, a fresh isolate from a patient with a severe corneal ulcer, revealing that these four enzymes are distinct from each other.