Author

J. Gohda

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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Microbiology· 4

Signature Assays, Organisms & Methods

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Approach:experimental assay· 4 Research Focus:host-pathogen & immune response· 4 Organism:human· 4 Assay:bulk RNA-seq· 2

Frequent Co-Authors

Y. Kawaguchi· 4 shared J.-i. Inoue· 3 shared M. Yamamoto· 3 shared K. Semba· 2 shared K. Tomita· 2 shared Y. Hirayama· 2 shared A. Kobayashi· 1 shared D. Xu· 1 shared

Activity by Year

2020-2022 · peak 2/yr

Co-Author Collaboration Network

10 top collaborators · 27 mutual co-author links

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4 shared papersMicrobiology

Y. Kawaguchi

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4 papers

Recent·Most cited

Antiviral roles of interferon regulatory factor (IRF)-1, 3 and 7 against human coronavirus infection

D. Xu, J. K. S. Duncan, M. Licursi, J. Gohda, Y. Kawaguchi, K. Hirasawa

This study investigates the antiviral roles of IRF1, IRF3, and IRF7 against human coronavirus infection, finding that IRF3 is critical for restricting 229E and OC43 infections.

bioRxiv · Mar 24, 2022 · PreprintMicrobiology

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

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