>Japanese

Publication

(* = corresponding author)

[Selected research
 articles]

Nanaura H., Kawamukai H., Fujiwara A., Uehara T., Aiba Y., Nakanishi M., Shiota T., Hibino M., Wiriyasermkul P., Kikuchi S., Nagata R., Matsubayashi M., Shinkai Y., Niwa T., Mannen T., Morikawa N., Iguchi N., Kiriyama T., Morishima K., Inoue R., Sugiyama M., Oda T., Kodera N., Toma-Fukai S., Sato M., Taguchi H., Nagamori S., Shoji O., Ishimori K., Matsumura H., Sugie K., Saio T. , Yoshizawa T., Mori E. C9orf72-derived arginine-rich poly-dipeptides impede phase modifiers. Nat Commun. 2021 Sep 6;12(1):5301. doi: 10.1038/s41467-021-25560-0.

Saio T. , Hiramatsu S., Asada M., Nakagawa H., Shimizu K., Kumeta H., Nakamura T., Ishimori K. Conformational ensemble of a multidomain protein explored by Gd3+ electron paramagnetic resonance. Biophys J. 2021 Aug 3;120(15):2943-2951. doi: 10.1016/j.bpj.2021.06.033.

Kawagoe, S., Nakagawa, H., Kumeta, H., Ishimori, K., *Saio, T.. Structural insight into proline cis/trans isomerization of unfolded proteins catalyzed by the trigger factor chaperone. J Biol Chem. 2018, 293, 15095. DOI: 10.1074/jbc.RA118.003579

*Saio, T., Kawagoe, S., Ishimori, K., *Kalodimos, C.G. Oligomerization of a molecular chaperone modulates its activity. eLife 2018, 7, e35731. DOI: 10.7554/eLife.35731

Huang, C., Rossi, P., Saio, T., *Kalodimos, C.G. Structural basis for the antifolding activity of a molecular chaperone. Nature 2016, 537, 202. DOI: 10.1038/nature18965

Saio, T., Ogura, K., Kumeta, H., Kobashigawa, Y., Shimizu, K., Yokochi, M., Kodama, K., Yamaguchi, H., Tsujishita, H., *Inagaki, F. Ligand-driven conformational changes of MurD visualized by paramagnetic NMR. Sci. Rep. 2015, 5, 16685. DOI: 10.1038/srep16685

Saio, T., Guan, X., Rossi, P., Economou, A., *Kalodimos, CG. Structural basis for protein anti-aggregation activity of the trigger factor chaperone. Science 2014, 344, 1250494. DOI: 10.1126/science.1250494

[Research articles]

< 2022 >

Kawagoe S, Ishimori K, Saio T.
Structural and Kinetic Views of Molecular Chaperones in Multidomain Protein Folding.
Int J Mol Sci. 2022, 23, 2485. DOI: 10.3390/ijms23052485

Miyake M, Sobajima M, Kurahashi K, Shigenaga A, Denda M, Otaka A, Saio T, Sakane N, Kosako H, Oyadomari S.
Identification of an endoplasmic reticulum proteostasis modulator that enhances insulin production in pancreatic β cells.
Cell Chem Biol. 2022, S2451-9456(22)00002-2. DOI: 10.1016/j.chembiol.2022.01.002

< 2021 >

Zhu H, Matsusaki M , Sugawara T, Ishimori K, Saio T.
Zinc-Dependent Oligomerization of Thermus thermophilus Trigger Factor Chaperone.
Biology. 2021, 10, 1106. DOI: 10.3390/biology10111106

Matsusaki M , Okada R, Tanikawa Y, Kanemura S, Ito D, Lin Y, Watabe M, Yamaguchi H, Saio T, Lee YH, Inaba K, Okumura M.
Functional Interplay between P5 and PDI/ERp72 to Drive Protein Folding.
Biology. 2021, 10, 1112. DOI: 10.3390/biology10111112

Nanaura H., Kawamukai H., Fujiwara A., Uehara T., Aiba Y., Nakanishi M., Shiota T., Hibino M., Wiriyasermkul P., Kikuchi S., Nagata R., Matsubayashi M., Shinkai Y., Niwa T., Mannen T., Morikawa N., Iguchi N., Kiriyama T., Morishima K., Inoue R., Sugiyama M., Oda T., Kodera N., Toma-Fukai S., Sato M., Taguchi H., Nagamori S., Shoji O., Ishimori K., Matsumura H., Sugie K., Saio T. , Yoshizawa T., Mori E.
C9orf72-derived arginine-rich poly-dipeptides impede phase modifiers.
Nat Commun. 2021,12, 5301. DOI: 10.1038/s41467-021-25560-0.

Saio T. , Hiramatsu S., Asada M., Nakagawa H., Shimizu K., Kumeta H., Nakamura T., Ishimori K. Conformational ensemble of a multidomain protein explored by Gd3+ electron paramagnetic resonance.
Biophys J. 2021, 120, 2943-2951. DOI: 10.1016/j.bpj.2021.06.033

Nakagawa H., Saio T., Nagao M., Inoue R., Sugiyama M., Ajito S., Tominaga T., Kawakita Y. Conformational dynamics of a multidomain protein by neutron scattering and computational analysis.
Biophys J. 2021, 120, 3341-3354. DOI: 10.1016/j.bpj.2021.07.001

Okuda A, Inoue R., Morishima K., Saio T., Yunoki Y., Yagi-Utsumi M., Yagi H, Shimizu M., Sato N., Urade R., Kato K., Sugiyama M. Deuteration Aiming for Neutron Scattering.
Biophys Physicobiol. 2021, 18, 16-27. DOI: 10.2142/biophysico.bppb-v18.003 eCollection 2021

Mimura M., Tomita S., Shinkai Y., Hosokai T., Kumeta H., Saio T., Shiraki K., Kurita R. Quadruplex Folding Promotes the Condensation of Linker Histones and DNAs via Liquid-Liquid Phase Separation.
J Am Chem Soc. 2021, 143, 9849-9857. DOI: 10.1021/jacs.1c03447

Okumura M., Kanemura S., Matsusaki M., Kinoshita M., Saio T., Ito D., Hirayama C., Kumeta H., Watabe M., Amagai Y., Lee Y.H., Akiyama S., Inaba K. A unique leucine-valine adhesive motif supports structure and function of protein disulfide isomerase P5 via dimerization.
Structure. 2021, 29, 1357-1370. DOI: 10.1016/j.str.2021.03.016

Kamran Rizzolo, Angela Yeou Hsiung Yu, Adedeji Ologbenla, Sa-Rang Kim, Haojie Zhu, Koichiro Ishimori, Guillaume Thibault, Elisa Leung, Yi Wen Zhang, Mona Teng, Marta Haniszewski, Noha Miah, Sadhna Phanse, Zoran Minic, Sukyeong Lee, Julio Diaz Caballero, Mohan Babu, Francis T. F. Tsai, Tomohide Saio & Walid A. Houry. Functional cooperativity between the trigger factor chaperone and the ClpXP proteolytic complex.
Nature Commun. 2021, 12, 281. DOI: 10.1038/s41467-020-20553-x

< 2020 >

Saio, T., Ishimori, K. Accelerating structural life science by paramagnetic lanthanide probe methods.
Biochim. Biophys. Acta. Gen. Subj. 2020, 1864, 129332. DOI: 10.1016/j.bbagen.2019.03.018

Taguchi, Y., Saio, T., *Kohda, D. Distance Distribution between Two Iodine Atoms Derived from Small-Angle X-ray Scattering Interferometry for Analyzing a Conformational Ensemble of Heavy Atom-Labeled Small Molecules.
J. Phys. Chem. Lett. 2020, 11, 5451-5456. DOI: 10.1021/acs.jpclett.0c01107

Yoshizawa, T., Nozawa, R.S., Jia, T.Z., Saio, T., *Mori, E. Biological phase separation: cell biology meets biophysics.
Biophys. Rev. 2020, 12, 519-539. DOI: 10.1007/s12551-020-00680-x

< 2019 >

*Okumura, M., Noi, K., Kanemura, S., Kinoshita, M., Saio, T., Inoue, Y., Hikima, T., Akiyama, S., *Ogura, T., *Inaba, K. Dynamic assembly of protein disulfide isomerase in catalysis of oxidative folding.
Nat. Chem. Biol. 2019, 15, 499-509. DOI: 10.1038/s41589-019-0268-8

Nanaura, H., Kawamukai, H., Fujiwara, A., Uehara, T., Nakanishi, M., Shiota, T., Hibino, M., Aiba, Y., Wiriyasermkul, P., Kikuchi, S., Nagata, R., Matsubayashi, M., Nagamori, S., Shoji, O., Ishimori, K., Matsumura, H., Sugie, K., *Saio, T., *Yoshizawa, T., *Mori, E.. Toxic PR poly-dipeptides encoded by the C9orf72 repeat expansion target Kapβ2 and dysregulate phase separation of low-complexity domains.
bioRxiv 2019. DOI: 10.1101/812099

< 2018 >

Kawagoe, S., Nakagawa, H., Kumeta, H., Ishimori, K., *Saio, T. Structural insight into proline cis/trans isomerization of unfolded proteins catalyzed by the trigger factor chaperone.
J. Biol. Chem. 2018, 293, 15905-15106. DOI: 10.1074/jbc.RA118.003579

*Saio, T., Kawagoe, S., Ishimori, K., *Kalodimos, C.G. Oligomerization of a molecular chaperone modulates its activity.
eLife 2018, 7, e35731. DOI: 10.7554/eLife.35731

Sato, W., Uchida, T., Saio, T., *Ishimori K. Polyethylene glycol promotes autoxidation of cytochrome c.
Biochim. Biophys. Acta. Gen. Subj. 2018, 1862, 1339-1349. DOI: 10.1016/j.bbagen.2018.03.010

< 2016 >

Huang, C., Rossi, P., Saio, T., *Kalodimos, C.G. Structural basis for the antifolding activity of a molecular chaperone.
Nature 2016, 537, 202-206. DOI: 10.1038/nature18965

Monneau, Y.R., Ishida, Y., Rossi, P., Saio, T., Tzeng, S.R., Inouye, M., *Kalodimos, C.G.
Exploiting E. coli auxotrophs for leucine, valine, and threonine specific methyl labeling of large proteins for NMR applications.
J. Biomol. NMR 2016, 65, 99-108. DOI: 10.1007/s10858-016-0041-1

Imai, M., Saio, T., Kumeta, H., Uchida, T., Inagaki, F., Ishimori, K. Investigation of the redox-dependent modulation of structure and dynamics in human cytochrome c.
Biochem. Biophys. Res. Commun. 2016, 469, 978-984. DOI: 10.1016/j.bbrc.2015.12.079

Sato, W., Hitaoka, S., Inoue, K., Imai, M., Saio, T., Uchida, T., Shinzawa-Itoh, K., Yoshikawa, S., Yoshizawa, K., *Ishimori, K. Energetic Mechanism of Cytochrome c-Cytochrome c Oxidase Electron Transfer Complex Formation under Turnover Conditions Revealed by Mutational Effects and Docking Simulation.
J. Biol. Chem. 2016, 291, 15320-15331. DOI: 10.1074/jbc.M115.708065

*Furukawa, Y., Anzai, I., Akiyama, S., Imai, M., Cruz, F.J., Saio, T., Nagasawa, K., Nomura, T., Ishimori, K. Conformational Disorder of the Most Immature Cu, Zn-Superoxide Dismutase Leading to Amyotrophic Lateral Sclerosis.
J. Biol. Chem. 2016, 291, 4144-4155. DOI: 10.1074/jbc.M115.683763

< 2015 >

Saio, T., Ogura, K., Kumeta, H., Kobashigawa, Y., Shimizu, K., Yokochi, M., Kodama, K., Yamaguchi, H., Tsujishita, H., *Inagaki, F. Ligand-driven conformational changes of MurD visualized by paramagnetic NMR.
Sci. Rep. 2015, 5, 16685. DOI: 10.1038/srep16685

< 2014 >

Saio, T., Guan, X., Rossi, P., Economou, A., *Kalodimos, CG. Structural basis for protein anti-aggregation activity of the trigger factor chaperone.
Science 2014, 344, 1250494. DOI: 10.1126/science.1250494

< 2013 >

*Ogura, K., Kobashigawa, Y., Saio, T., Kumeta H, Torikai S, Inagaki F. Practical applications of hydrostatic pressure to refold proteins from inclusion bodies for NMR structural studies.
Protein. Eng. Des. Sel. 2013, 26, 409-416. DOI: 10.1093/protein/gzt012

Saio, T., *Kalodimos, C.G. NMR disentangles a dynamic disaggregase machinery.
Nat. Struct. Mol. Biol. 2013, 20, 409-410. DOI: 10.1038/nsmb.2551

< 2012 >

Kobashigawa, Y. †, Saio, T. †, Ushio, M. †, Sekiguchi, M., Yokochi, M., Ogura, K., *Inagaki, F. (†Equal contribution)
Convenient method for resolving degeneracies due to symmetry of the magnetic susceptibility tensor and its application to pseudo contact shift-based protein-protein complex structure determination.
J. Biomol. NMR 2012, 53, 53-63. DOI: 10.1007/s10858-012-9623-8

< 2011 >

Saio, T., Ogura, K., Shimizu, K., Yokochi, M., Burke, T.R. Jr., *Inagaki, F. An NMR strategy for fragment-based ligand screening utilizing a paramagnetic lanthanide probe.
J. Biomol. NMR 2011, 51, 395-408. DOI: 10.1007/s10858-011-9566-5

< 2010 >

Saio, T., Yokochi, M., Kumeta, H., *Inagaki, F. PCS-based structure determination of protein-protein complexes.
J. Biomol. NMR 2010, 46, 271-280. DOI: 10.1007/s10858-010-9401-4.

[Books]

*Saio, T., Fuyuhiko Inagaki. Structural Study of Proteins by Paramagnetic Lanthanide Probe Methods. Springer, In: Experimental approaches of NMR spectroscopy -Methodology and application to life science and materials science-, Chapter 8, 227-252, 2017.

Saio, T., *Inagaki, F.. Structural biology with advanced NMR technique. Springer, In: Advanced Methods in Structural Biology, Chapter 17, 315-340, 2016.

[Japanese Review
 Articles]

Takashi Oda, Tomohide Saio, Detection Technology: Structural Biology of Intrinsically Disordered Proteins, In: Special Feature Phase Separation Biology: Recommendation of Phase Separation Glasses, Journal of Biotechnology

Tomohide Saio, Koichiro Ishimori. Mechanism of action of molecular chaperones revealed from three-dimensional structure. Biophysics

Kota Kodama, Tomohide Saio, Katsumi Maenaka, Masataka Kaneshiro. Academia drug discovery through communication between Wet and Dry. Bioscience and industry

Tomohide Saio Trigger factor Structural basis of dynamic substrate recognition by chaperone. Biochemistry

Tomohide Saio, Charalampos G. Kalodimos. Trigger factors suppress aggregation by dynamic interaction with denatured proteins. Life Science New Paper Review