Author

J.-i. Inoue

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

Biology Disciplines

Click to filter author papers

Microbiology· 4 Cancer Biology· 1

Signature Assays, Organisms & Methods

Click to filter · or open tag

Approach:experimental assay· 5 Research Focus:host-pathogen & immune response· 4 Organism:human· 4 Assay:bulk RNA-seq· 2 Research Focus:cancer & tumor microenvironment· 1 Organism:virus· 1

Frequent Co-Authors

M. Yamamoto· 4 shared Y. Kawaguchi· 4 shared J. Gohda· 3 shared K. Semba· 3 shared K. Tomita· 2 shared Y. Hirayama· 2 shared Z. Matsuda· 2 shared A. Kobayashi· 1 shared

Activity by Year

2020-2022 · peak 2/yr

Co-Author Collaboration Network

10 top collaborators · 29 mutual co-author links

Click any collaborator node to inspect or filter shared papers

Focal author (center)Selected co-authorORCID co-authorUnlinked name

Curved chords = mutual co-authorship

4 shared papersMicrobiology

M. Yamamoto

Mutual co-authors in cluster

Author profile →

5 papers

Recent·Most cited

SARS-CoV-2 Omicron spike H655Y mutation is responsible for enhancement of the endosomal entry pathway and reduction of cell surface entry pathway

M. Yamamoto, K. Tomita, Y. Hirayama, J.-i. Inoue, Y. Kawaguchi, J. Gohda

This paper investigates how the H655Y mutation in the Omicron SARS-CoV-2 spike protein enhances endosomal entry and reduces cell surface entry, altering viral tropism and fusogenicity.

bioRxiv · Mar 21, 2022 · PreprintMicrobiology

Metalloproteinase-dependent and TMPRSS2-independnt cell surface entry pathway of SARS-CoV-2 requires the furin-cleavage site and the S2 domain of spike protein

M. Yamamoto, J. Gohda, A. Kobayashi, K. Tomita, Y. Hirayama, N. Koshikawa, M. Seiki, K. Semba, T. Akiyama, Y. Kawaguchi, J.-i. Inoue

This study identifies a TMPRSS2-independent metalloproteinase-dependent entry pathway for SARS-CoV-2 that requires the furin cleavage site and S2 domain of the spike protein, highlighting new therapeutic targets.

bioRxiv · Dec 14, 2021 · PreprintMicrobiology

Aberrant accumulation of NIK promotes tumorigenicity by dysregulating post-translational modifications in breast cancer

Y. Hayashi, J. Nakayama, M. Yamamoto, M. Maekawa, S. Watanabe, S. Higashiyama, J.-i. Inoue, Y. Yamamoto, K. Semba

This study identifies NIK upregulation in breast cancer due to translational dysregulation, which promotes tumorigenicity by activating the non-canonical NF-κB pathway.

bioRxiv · Aug 27, 2021 · PreprintCancer Biology

The anticoagulant nafamostat potently inhibits SARS-CoV-2 infection in vitro: an existing drug with multiple possible therapeutic effects

M. Yamamoto, M. Kiso, Y. Sakai-Tagawa, K. Iwatsuki-Horimoto, M. Imai, M. Takeda, N. Kinoshita, N. Ohmagari, J. Gohda, K. Semba, Z. Matsuda, Y. Kawaguchi, Y. Kawaoka, J.-i. Inoue

This study shows nafamostat inhibits SARS-CoV-2 infection in vitro by blocking TMPRSS2-mediated fusion, with potency exceeding its blood concentration, suggesting it as a potential COVID-19 treatment.

bioRxiv · Apr 22, 2020 · PreprintMicrobiology

Analysis of insertion mutants in distal α9 portion of C-terminal heptad repeat (CHR) of HIV-1 gp41 subunit

H. Wang, J. Song, Y. Kawaguchi, J.-i. Inoue, Z. Matsuda

The paper analyzes insertion mutants in the HIV-1 gp41 C-terminal heptad repeat, finding that alanine insertion (653+A) attenuates membrane fusion due to slower 6HB formation kinetics, not 6HB stability.

bioRxiv · Mar 30, 2020 · PreprintMicrobiology