Author

E. Chatani

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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Biochemistry· 3 Biophysics· 2

Signature Assays, Organisms & Methods

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Research Focus:cell type annotation· 3 Approach:experimental assay· 3 Assay:imaging· 2 Approach:statistical model· 2 Research Focus:host-pathogen & immune response· 1 Organism:human· 1 Approach:microscopy & imaging analysis· 1 Research Focus:protein folding & dynamics· 1

Frequent Co-Authors

K. Yuzu· 3 shared N. Yamamoto· 3 shared M. Ishigaki· 2 shared M. Sugiyama· 2 shared R. Inoue· 2 shared Y. Ozaki· 2 shared A. Naito· 1 shared A. Okuda· 1 shared

Activity by Year

2019-2023 · peak 2/yr

Co-Author Collaboration Network

10 top collaborators · 23 mutual co-author links

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3 shared papersBiochemistry

K. Yuzu

Mutual co-authors in cluster

Author profile →

5 papers

Recent·Most cited

Mechanistic modeling of amyloid oligomer and protofibril formation

K. Yuzu, H. Imamura, T. Nozaki, Y. Fujii, S. M. M. Badawy, K. Morishima, A. Okuda, R. Inoue, M. Sugiyama, E. Chatani

This study establishes a mechanistic model of amyloid oligomer and protofibril formation in bovine insulin using light scattering and kinetic analysis, revealing end-to-end association as the rate-limiting step.

bioRxiv · Sep 2, 2023 · PreprintBiophysics

Structural development of amyloid precursors in insulin B chain and the inhibition effect by fibrinogen

N. Yamamoto, R. Inoue, Y. Makino, N. Shibayama, A. Naito, M. Sugiyama, E. Chatani

This study investigates the structural development of insulin B chain prefibrillar intermediates and how fibrinogen inhibits their fibril formation using multiple biophysical techniques.

bioRxiv · Dec 26, 2021 · PreprintBiochemistry

Multistep changes in amyloid structure that are induced by cross-seeding on a rugged energy landscape

K. Yuzu, N. Yamamoto, M. Noji, M. So, Y. Goto, T. Iwasaki, M. Tsubaki, E. Chatani

This study investigates how cross-seeding of insulin amyloid fibrils from different species leads to structural changes and new amyloid forms with distinct properties.

bioRxiv · Jul 19, 2020Biochemistry

Iodine staining as a useful probe for distinguishing amyloid fibril polymorphs

T. Hiramatsu, N. Yamamoto, S. Ha, Y. Masuda, M. Yasuda, M. Ishigaki, K. Yuzu, Y. Ozaki, E. Chatani

The paper demonstrates that iodine staining can distinguish amyloid fibril polymorphs by color differences, linked to specific iodine binding sites and surface structures.

bioRxiv · Mar 21, 2020Biochemistry

Exploration of insulin amyloid polymorphism using Raman spectroscopy and imaging

M. Ishigaki, K. Morimoto, E. Chatani, Y. Ozaki

This paper uses Raman spectroscopy to analyze insulin amyloid polymorphism under different salt and temperature conditions, identifying structural markers that distinguish fibril forms.

bioRxiv · Sep 25, 2019Biophysics