Author

Y. Fujiyoshi

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· 2 Bioengineering· 1 Biophysics· 1

Signature Assays, Organisms & Methods

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Approach:experimental assay· 3 Organism:human· 2 Research Focus:protein structure prediction· 2 Approach:statistical model· 2 Assay:structural biology· 2 Approach:deep learning· 1 Research Focus:drug response / drug discovery· 1 Research Focus:perturbation response prediction· 1

Frequent Co-Authors

K. Irie· 3 shared H. Nakanishi· 2 shared K. Abe· 2 shared H. Khandelia· 1 shared H. Nagura· 1 shared H. Yamaguchi· 1 shared K. Hasegawa· 1 shared K. Segawa· 1 shared

Activity by Year

2019-2026 · peak 3/yr

Co-Author Collaboration Network

10 top collaborators · 19 mutual co-author links

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3 shared papersBiochemistry

K. Irie

Mutual co-authors in cluster

Author profile →

4 papers

Recent·Most cited

De novo design of mini-proteins as specific binders to PACAP-38, a key mediator of migraine

H. Yamaguchi, S. Suzuki, Y. Fujiyoshi, M. Isalan

This study designs mini-proteins that bind PACAP-38 with high affinity, showing improved potency and stability compared to earlier versions.

bioRxiv · Nov 2, 2026 · PreprintBioengineering

Crystal structure of a human plasma membrane phospholipid flippase

H. Nakanishi, K. Irie, K. Segawa, K. Hasegawa, Y. Fujiyoshi, S. Nagata, K. Abe

The paper determines the crystal structure of the ATP11C-CDC50A complex and proposes a model for phosphatidylserine translocation across the plasma membrane.

bioRxiv · Dec 23, 2019Biochemistry

A native prokaryotic voltage-dependent calcium channel with a novel selectivity filter sequence

T. Shimomura, Y. Yonekawa, H. Nagura, M. Tateyama, Y. Fujiyoshi, K. Irie

The paper identifies a native prokaryotic Cav channel, CavMr, and shows that a glycine residue in its selectivity filter determines Ca2+ selectivity, conserved in eukaryotic Cavs.

bioRxiv · Oct 17, 2019Biophysics

A single K+-binding site in the crystal structure of the gastric proton pump

K. Yamamoto, V. Dubey, K. Irie, H. Nakanishi, H. Khandelia, Y. Fujiyoshi, K. Abe

The paper determines the crystal structure of the gastric proton pump, revealing a single K+-binding site and confirming a 1H+/1K+ exchange per ATP hydrolysis.

bioRxiv · Apr 15, 2019Biochemistry