Miki Nakajima - Toxicology

Author Information

Miki Nakajima is a distinguished researcher in the fields of Drug Metabolism and Toxicology. She is affiliated with the Faculty of Pharmaceutical Sciences and the WPI Nano Life Science Institute at Kanazawa University in Kakuma-machi, Kanazawa, Japan. Her work primarily focuses on understanding the biochemical and molecular mechanisms that influence drug metabolism and toxicity, which is crucial for the development of safer and more effective therapeutic agents.

Research Contributions

Miki Nakajima has made significant contributions to the understanding of drug-metabolizing enzymes and their regulation. Her recent research includes studies on RNA editing and m6A modification in the modulation of drug-metabolizing enzymes, the role of PPARα in regulating human arylacetamide deacetylase, and the development of novel DNA aptamers for CYP24A1 inhibition with potential anticancer activities. She has also investigated the activities of various hydrolases in cynomolgus monkey liver microsomes, the impact of microRNAs in apple-derived nanoparticles on intestinal transport proteins, and the role of arylacetamide deacetylase in drug hydrolysis and activation in mice and humans.

Aliases

Miki Nakajima is also known by the aliases "M Nakajima" and "M. Nakajima".

Publication and Citation Metrics

Metric	Value
Total Citation Count	16,534
h-index	72
Total Paper Count	369

Publications:

A-to-I RNA editing and m6A modification modulating expression of drug-metabolizing enzymes.

DOI: 10.1124/dmd.121.000390

Year: 2022

PPARα regulates the expression of human arylacetamide deacetylase involved in drug hydrolysis and lipid metabolism.

DOI: 10.1016/j.bcp.2022.115010

Year: 2022

Novel DNA Aptamer for CYP24A1 Inhibition with Enhanced Antiproliferative Activity in Cancer Cells.

DOI: 10.1021/acsami.1c22965

Year: 2022

Methionine sulfoxide reductase A in human and mouse tissues is responsible for sulindac activation, making a larger contribution than the gut microbiota.

DOI: 10.1124/dmd.122.000828

Year: 2022

Epicatechin gallate and epigallocatechin gallate are potent inhibitors of human arylacetamide deacetylase.

DOI: 10.1016/J.DMPK.2021.100397

Year: 2021

Hydrolase activities of cynomolgus monkey liver microsomes and recombinant CES1, CES2, and AADAC.

DOI: 10.1016/j.ejps.2021.105807

Year: 2021

MicroRNAs in Apple-Derived Nanoparticles Modulate Intestinal Expression of Organic Anion–Transporting Peptide 2B1/SLCO2B1 in Caco-2 Cells

DOI: 10.1124/dmd.121.000380

Year: 2021

Arylacetamide deacetylase knockout mice are sensitive to ketoconazole-induced hepatotoxicity and adrenal dysfunction

DOI: 10.22541/au.162763451.13052487/v1

Year: 2021

Evaluation of lens opacity due to inhibition of cholesterol biosynthesis using rat lens explant cultures.

DOI: 10.1016/j.tox.2021.153064

Year: 2021

Arylacetamide deacetylase as a determinant of the hydrolysis and activation of abiraterone acetate in mice and humans.

DOI: 10.1016/j.lfs.2021.119896

Year: 2021