What is he best known for?
The fields of study he is best known for:
Takeshi Nishino focuses on Biochemistry, Xanthine oxidase, Xanthine dehydrogenase, Enzyme and Cofactor.
His Molecular biology research extends to the thematically linked field of Biochemistry.
His Xanthine oxidase research is multidisciplinary, incorporating perspectives in Dehydrogenase and Superoxide.
His research in Dehydrogenase intersects with topics in Oxidase test, Xanthine and Flavin group.
Takeshi Nishino interconnects Oxidoreductase and Stereochemistry in the investigation of issues within Xanthine dehydrogenase.
His Enzyme study incorporates themes from Catalysis and Molybdenum.
His most cited work include:
- Crystal structures of bovine milk xanthine dehydrogenase and xanthine oxidase: Structure-based mechanism of conversion (483 citations)
- Flavoprotein structure and mechanism. 4. Xanthine oxidase and xanthine dehydrogenase. (345 citations)
- An Extremely Potent Inhibitor of Xanthine Oxidoreductase CRYSTAL STRUCTURE OF THE ENZYME-INHIBITOR COMPLEX AND MECHANISM OF INHIBITION (291 citations)
What are the main themes of his work throughout his whole career to date?
Takeshi Nishino mainly focuses on Biochemistry, Xanthine dehydrogenase, Xanthine oxidase, Xanthine and Stereochemistry.
Biochemistry is a component of his Enzyme, Oxidase test, Flavin group, Active site and Cofactor studies.
His Xanthine dehydrogenase research includes themes of Molybdenum cofactor, Flavoprotein, Crystal structure, Febuxostat and NAD+ kinase.
The Xanthine oxidase study which covers Dehydrogenase that intersects with Amino acid.
His biological study deals with issues like Uric acid, which deal with fields such as Purine.
His study looks at the relationship between Stereochemistry and fields such as Substrate, as well as how they intersect with chemical problems.
He most often published in these fields:
- Biochemistry (68.42%)
- Xanthine dehydrogenase (49.62%)
- Xanthine oxidase (28.57%)
What were the highlights of his more recent work (between 2008-2021)?
- Xanthine dehydrogenase (49.62%)
- Biochemistry (68.42%)
- Stereochemistry (24.81%)
In recent papers he was focusing on the following fields of study:
Takeshi Nishino mostly deals with Xanthine dehydrogenase, Biochemistry, Stereochemistry, Xanthine and Xanthine Oxidoreductase.
His work carried out in the field of Xanthine dehydrogenase brings together such families of science as Molybdenum cofactor, Crystal structure, Oxidase test, Gene knockin and Hypoxanthine.
His study involves Febuxostat, Xanthine oxidase, Active site and Enzyme, a branch of Biochemistry.
His study in Xanthine oxidase is interdisciplinary in nature, drawing from both Chondrogenesis, Molybdenum, Pathologic calcification, Cofactor and Flavin group.
His Stereochemistry research is multidisciplinary, incorporating elements of Oxidoreductase and Biophysics.
His studies in Xanthine integrate themes in fields like Calcification, Chondrocyte, Alkaline phosphatase and Cell biology.
Between 2008 and 2021, his most popular works were:
- Molybdenum enzymes in higher organisms (145 citations)
- Molybdenum enzymes in higher organisms (145 citations)
- FYX-051: A Novel and Potent Hybrid-Type Inhibitor of Xanthine Oxidoreductase (68 citations)
In his most recent research, the most cited papers focused on:
Takeshi Nishino spends much of his time researching Xanthine dehydrogenase, Molybdenum, Stereochemistry, Biochemistry and Xanthine oxidase.
His study brings together the fields of Xanthine and Xanthine dehydrogenase.
Takeshi Nishino has included themes like Oxipurinol and Hypoxanthine in his Molybdenum study.
His work deals with themes such as Oxidoreductase, Flavin group, NAD+ kinase and Electron transfer, which intersect with Stereochemistry.
With his scientific publications, his incorporates both Biochemistry and European union.
Xanthine oxidase and Cofactor are commonly linked in his work.
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