Author

A. Koike

Listed by name: these papers carry no ORCID for this author, so different people with the same name may be mixed together.

Biology Disciplines

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Cell Biology· 2 Biochemistry· 1 Microbiology· 1

Signature Assays, Organisms & Methods

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Approach:experimental assay· 4 Research Focus:drug response / drug discovery· 2 Organism:human· 2 Organism:mouse· 2 Assay:proteomics· 2 Assay:bulk RNA-seq· 1 Research Focus:cell signaling & trafficking· 1 Research Focus:cell type annotation· 1

Frequent Co-Authors

A. Fujimoto· 1 shared C. Chen· 1 shared F. Becker· 1 shared H. Fujimoto· 1 shared I. Fukunaga· 1 shared J. Kim· 1 shared J. Zhang· 1 shared K. Brehm· 1 shared

Activity by Year

2018-2022 · peak 2/yr

Co-Author Collaboration Network

10 top collaborators · 12 mutual co-author links

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1 shared paperCell Biology

A. Fujimoto

Mutual co-authors in cluster

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4 papers

Recent·Most cited

Targeting Echinococcus multilocularis PIM kinase for improving anti-parasitic chemotherapy

A. Koike, F. Becker, P. Sennhenn, J. Kim, J. Zhang, S. Hannus, K. Brehm

This paper identifies EmPIM as a target for anti-AE chemotherapy and demonstrates that in silico-designed compounds can inhibit parasite growth with reduced toxicity to human cells.

bioRxiv · May 12, 2022Microbiology

Statins attenuate antiviral IFN- and ISG expression via inhibiting IRF3/JAK/STAT signaling in poly(I:C)-treated hyperlipidemic mice and macrophages

A. Koike, K. Tsujinaka, K. Fujimori

bioRxiv · Jun 21, 2020Biochemistry

TGF-β inhibitor accelerates BMP4-induced cochlear gap junction formation during in vitro differentiation of embryonic stem cells

I. Fukunaga, C. Chen, Y. Oe, K. Danzaki, S. Ohta, A. Koike, A. Fujimoto, K. Ikeda, K. Kamiya

This study shows that the TGF-β inhibitor SB431542 accelerates BMP4-induced gap junction formation in CX26GJCs derived from mouse iPSCs, improving their yield for therapeutic applications.

bioRxiv · Feb 17, 2020Cell Biology

Acetylation of nuclear localization signal controls importin-mediated nuclear transport of Ku70

H. Fujimoto, T. Ikuta, A. Koike, M. Koike

The paper shows acetylation of specific lysine residues in Ku70's NLS reduces its nuclear localization by impairing importin interaction.

bioRxiv · Aug 29, 2018 · PreprintCell Biology