A. Nakano

Structural snapshots of V/A-ATPase reveal the rotary catalytic mechanism of rotary ATPases

K. Yokoyama, J. Kishikawa, A. Furuta, 2022, Nature Communications.

Structural snapshots of V/A-ATPase reveal a new paradigm for rotary catalysis

K. Yokoyama, S. Saeki, J. Kishikawa, 2021, bioRxiv.

Proton nuclear magnetic resonance study on the roles of histidine residues in the binding of polypeptide chain elongation factor Tu from Thermus thermophilus with aminoacyl transfer ribonucleic acid and guanine nucleotides.

Y. Kaziro, S. Nakamura, T. Miyazawa, 1980, Biochemistry.

31P NMR study on the guanine nucleotide binding of elongation factor Tu from Thermus thermophilus

Y. Kaziro, S. Nakamura, T. Miyazawa, 1980, FEBS Letters.

Involvement of histidine residues in the substrate binding of elongation factor Tu from Thermus thermophilus: proton nuclear magnetic resonance and photooxidation study.

Y. Kaziro, S. Nakamura, T. Miyazawa, 1979, Archives of biochemistry and biophysics.

Molecular structure of a gene, VMA1, encoding the catalytic subunit of H(+)-translocating adenosine triphosphatase from vacuolar membranes of Saccharomyces cerevisiae.

R. Hirata, Y. Ohsumk, A. Nakano, 1990, The Journal of biological chemistry.