Author

N. Miyazaki

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· 5 Immunology· 1 Microbiology· 1 Pathology· 1 Plant Biology· 1

Signature Assays, Organisms & Methods

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Assay:cryo-EM· 7 Approach:experimental assay· 6 Research Focus:protein structure prediction· 6 Approach:microscopy & imaging analysis· 3 Organism:bacteria (other)· 2 Research Focus:cell type annotation· 2 Research Focus:protein folding & dynamics· 2 Approach:biophysical modeling· 1

Frequent Co-Authors

K. Murata· 4 shared K. Iwasaki· 3 shared C. Song· 2 shared F. Akita· 2 shared J.-R. Shen· 2 shared K. Kato· 2 shared K. Murakami· 2 shared K. Okamoto· 2 shared

Activity by Year

2017-2023 · peak 3/yr

Co-Author Collaboration Network

10 top collaborators · 20 mutual co-author links

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4 shared papersBiophysics

K. Murata

Mutual co-authors in cluster

Author profile →

9 papers

Recent·Most cited

Structure and its transformation of elliptical nege-like virus Tanay virus

K. Okamoto, C. Song, M. Sakaguchi, C. Chalkiadaki, N. Miyazaki, T. Nabeshima, K. Morita, S. Inoue, K. Murata

This study determines the cryo-EM structure of Tanay virus and reveals its dynamic shape changes under different conditions, suggesting structural roles in infection and assembly.

bioRxiv · Jan 20, 2023Biophysics

Three-dimensional motions of GroEL during substrate protein recognition

K. Stapleton, T. Mizobata, N. Miyazaki, T. Takatsuji, T. Kato, K. Iwasaki, D. M. Standley, T. Kawamura, T. Nakane, J. Takagi, E. Mizohata

The paper uses cryo-EM to study the 3D motions of GroEL during substrate recognition, revealing asymmetric binding and conformational dynamics at near-atomic resolution.

bioRxiv · Sep 15, 2022 · PreprintBiophysics

An actin-like filament from Clostridium botulinum exhibits a novel mechanism of filament dynamics

A. Koh, S. Ali, D. Popp, K. Tanaka, Y. Kitaoku, N. Miyazaki, I. Kenji, K. Mitsuoka, R. C. Robinson, A. Narita

The paper identifies a ParM protein from Clostridium botulinum that forms a double-stranded filament with unique dynamics involving Pi-induced lateral shifts and distinct interactions with ParR.

bioRxiv · Mar 7, 2022 · PreprintBiophysics

Structural insights into an evolutionary turning-point of photosystem I from prokaryotes to eukaryotes

K. Kato, R. Nagao, Y. Ueno, M. Yokono, T. Suzuki, T.-Y. Jiang, N. Dohmae, F. Akita, S. Akimoto, N. Miyazaki, J.-R. Shen

The paper presents a cryo-EM structure of tetrameric PSI from Cyanophora paradoxa, revealing structural differences from cyanobacterial PSI that suggest evolutionary changes in PSI organization.

bioRxiv · Jan 3, 2022 · PreprintPlant Biology

Prediction of antigen-responding VHH antibodies by tracking evolution of antibody along time course of immunization

T. Matsuda, Y. Akazawa-Ogawa, L.-K. Komaba, N. Kiyose, N. Miyazaki, Y. Mizuguchi, T. Fukuta, Y. Ito, Y. Hagihara

The paper predicts antigen-reactive VHH antibodies by analyzing sequence evolution during immunization, achieving 75% accuracy in identifying antigen-responding clusters.

bioRxiv · Jun 29, 2021Immunology

Atomic structure of human sapovirus capsid by single particle cryo-electron microscopy

N. Miyazaki, K. Murakami, T. Oka, M. Miki, K. Iwasaki, K. Murata

The paper reports the atomic structure of human sapovirus capsid using cryo-EM, revealing domain interactions and hypervariable regions important for immune response and receptor binding.

bioRxiv · Feb 9, 2021 · PreprintMicrobiology

High-resolution cryo-EM structure of photosystem II: Effects of electron beam damage

K. Kato, N. Miyazaki, T. Hamaguchi, Y. Nakajima, F. Akita, K. Yonekura, J.-R. Shen

This study presents a high-resolution cryo-EM structure of photosystem II in solution, revealing its physiological state and effects of electron beam damage.

bioRxiv · Oct 18, 2020 · PreprintBiophysics

Dynamic rotation of the protruding domain enhances the infectivity of norovirus

C. Song, R. Takai-Todaka, M. Miki, K. Haga, A. Fujimoto, R. Ishiyama, K. Oikawa, M. Yokoyama, N. Miyazaki, K. Iwasaki, K. Murakami, K. Katayama, K. Murata

This study shows that the protruding domain of norovirus capsids dynamically rotates between rising and resting conformations in response to pH and metal ions, enhancing infection efficiency.

bioRxiv · Dec 16, 2019Pathology

Cryo-EM Of A Marseilleviridae Virus Particle Reveals A Large Internal Microassembly

K. Okamoto, N. Miyazaki, H. K. N. Reddy, M. F. Hantke, F. R. N. C. Maia, D. S. D. Larsson, C. Abergel, J.-M. Claverie, J. Hajdu, K. Murata, M. Svenda

The paper presents a cryo-EM structure of the Marseilleviridae virus Melbournevirus, revealing a large internal microassembly and structural complexity.

bioRxiv · May 17, 2017Biophysics