Author

Y. Yamagata

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 Microbiology· 2

Signature Assays, Organisms & Methods

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Approach:experimental assay· 3 Research Focus:cell type annotation· 2 Research Focus:development & morphogenesis· 2 Research Focus:chromatin & epigenetic regulation· 1 Research Focus:database / resource· 1 Organism:fungi (other)· 1 Research Focus:host-pathogen & immune response· 1 Organism:human· 1

Frequent Co-Authors

A. Koizumi· 1 shared A. Takeuchi· 1 shared A. Yoshimi· 1 shared H. Masuya· 1 shared H. Miyoshi· 1 shared H. Nakata· 1 shared K. Abe· 1 shared K. Kato· 1 shared

Activity by Year

2019-2023 · peak 2/yr

Co-Author Collaboration Network

10 top collaborators · 12 mutual co-author links

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1 shared paperMicrobiology

A. Koizumi

Mutual co-authors in cluster

Author profile →

4 papers

Recent·Most cited

Ontology for Cellular Senescence Mechanisms

Y. Yamagata, T. Fukuyama, S. Onami, H. Masuya

This paper proposes an ontological model to organize knowledge of cellular senescence mechanisms for computer-readable integration and analysis.

bioRxiv · Mar 9, 2023 · PreprintCell Biology

A glycosylphosphatidylinositol-anchored α-amylase encoded by amyD contributes to a decrease in the molecular mass of cell wall α-1,3-glucan in Aspergillus nidulans

K. Miyazawa, T. Yamashita, A. Takeuchi, Y. Kamachi, A. Yoshimi, Y. Tashiro, A. Koizumi, S. Yano, S. Kasahara, M. Sano, Y. Yamagata, T. Nakajima, K. Abe

The paper investigates the role of AmyD, a GPI-anchored α-amylase, in regulating the molecular mass of -1,3-glucan in Aspergillus nidulans cell walls.

bioRxiv · Nov 24, 2021Microbiology

Appropriate tension sensitivity of α-catenin ensures rounding morphogenesis of epithelial spheroids

R. Nishimura, K. Kato, M. Saida, Y. Kamei, M. Takeda, H. Miyoshi, Y. Yamagata, Y. Amano, S. Yonemura

This study shows that appropriate tension sensitivity of α-catenin is essential for epithelial cells to form round spheroids through multicellular rearrangement.

bioRxiv · Oct 27, 2021Cell Biology

A unique conformational escape reaction of HIV-1 against an allosteric integrase inhibitor

T. Nakamura, T. Nakamura, M. Amano, T. Miyakawa, Y. Yamagata, M. Matsuoka, H. Nakata

The paper identifies a novel conformational escape mechanism of HIV-1 integrase against NCINIs through under-multimerization of the IN protein.

bioRxiv · Nov 9, 2019Microbiology