Author

H. Shigematsu

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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Biophysics· 2 Bioengineering· 1 Cell Biology· 1 Microbiology· 1

Signature Assays, Organisms & Methods

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Approach:experimental assay· 5 Research Focus:cell signaling & trafficking· 2 Organism:C. elegans· 1 Research Focus:host-pathogen & immune response· 1 Organism:human· 1 Research Focus:protein folding & dynamics· 1 Assay:proteomics· 1 Assay:structural biology· 1

Frequent Co-Authors

E. Nitta· 2 shared N. Sakai· 2 shared R. Nitta· 2 shared S. Iwata· 2 shared S. Kikkawa· 2 shared S. Niwa· 2 shared S. Taguchi· 2 shared T. Imasaki· 2 shared

Activity by Year

2021-2022 · peak 3/yr

Co-Author Collaboration Network

10 top collaborators · 36 mutual co-author links

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2 shared papersBiophysics

E. Nitta

Mutual co-authors in cluster

Author profile →

5 papers

Recent·Most cited

Novel monoclonal antibodies showing broad neutralizing activity for SARS-CoV-2 variants including Omicrons BA.5 and BA.2.75

H. Ishimaru, M. Nishimura, L. H. Tjan, S. Sutandhio, M. I. Marini, G. B. Effendi, H. Shigematsu, K. Kato, N. Hasegawa, K. Aoki, Y. Kurahashi, K. Furukawa, M. Shinohara, T. Nakamura, J. Arii, , Y. Mori

bioRxiv · Sep 2, 2022 · PreprintMicrobiology

Structural model of microtubule dynamics inhibition by Kinesin-4 from the crystal structure of KLP-12 - tubulin complex

S. Taguchi, J. Nakano, T. Imasaki, T. Kita, Y. Saijo-Hamano, N. Sakai, H. Shigematsu, H. Okuma, T. Shimizu, E. Nitta, S. Kikkawa, S. Mizobuchi, S. Niwa, R. Nitta

The paper reports the crystal structure of KLP-12-tubulin complex, revealing how KLP-12 inhibits microtubule dynamics by altering tubulin curvature.

bioRxiv · Feb 14, 2022Biophysics

Generation of stable microtubule superstructures by binding of peptide-fused tetrameric proteins to inside and outside

H. Inaba, Y. Sueki, M. Ichikawa, A. M. R. Kabir, T. Iwasaki, H. Shigematsu, A. Kakugo, K. Sada, K. Matsuura

This study develops a tetrameric protein that binds to microtubules to generate stable superstructures, offering insights for nanomaterial design.

bioRxiv · Jan 27, 2022Bioengineering

CAMSAP2 organizes a γ-tubulin-independent microtubule nucleation centre

T. Imasaki, S. Kikkawa, S. Niwa, Y. Saijo-Hamano, H. Shigematsu, K. Aoyama, K. Mitsuoka, M. Aoki, A. Sakamot, Y. Tomabechi, N. Sakai, M. Shirouz, S. Taguchi, Y. Yamagish, T. Setsu, , R. Nitta

The paper shows CAMSAP2 nucleates microtubules from soluble β-tubulin without γ-tubulin, reducing the nucleation barrier and forming aster-like structures.

bioRxiv · Mar 1, 2021 · PreprintCell Biology

GTP-dependent formation of straight oligomers leads to nucleation of microtubules

R. Ayukawa, S. Iwata, H. Imai, S. Kamimura, M. Hayashi, K. X. Ngo, I. Minoura, S. Uchimura, T. Makino, M. Shirouzu, H. Shigematsu, K. Sekimoto, B. Gigant, E. Muto

The paper shows that GTP-dependent formation of straight oligomers is essential for microtubule nucleation, with a mutation increasing straight oligomers and accelerating nucleation.

Journal of Cell Biology · Feb 5, 2021Peer-reviewedBiophysics