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

Suzuki K, Nojiri R, Matsusaki M, Mabuchi T, Kanemura S, Ishii K, Kumeta H, Okumura M, Saio T, Muraoka T.
Redox-active chemical chaperones exhibiting promiscuous binding promote oxidative protein folding under condensed sub-millimolar conditions.
Chem Sci, 2024. DOI: 10.1039/D4SC02123A.

Yoshimura S, Shimada R, Kikuchi K, Kawagoe S, Abe H, Iisaka S, Fujimura S, Yasunaga K, Usuki S, Tani N, Ohba T, Kondoh E, Saio T, Araki K, Ishiguro K.
Atypical heat shock transcription factor HSF5 is critical for male meiotic prophase under non-stress conditions.
Nat Commun, 2024, 3330. DOI: 10.1038/s41467-024-47601-0.

Muraoka T, Okumura M, Saio T.
Enzymatic and synthetic regulation of polypeptide folding.
Chem Sci, 2024, 15, 2282-2299. DOI: 10.1039/d3sc05781j.

Kawamukai H, Takishita S, Shimizu K, Kohda D, Ishimori K, Saio T.
Conformational Distribution of a Multidomain Protein Measured by Single-Pair Small-Angle X-ray Scattering.
J Phys Chem Lett, 2024, 15, 744-750. DOI: 10.1021/acs.jpclett.3c02600.

Taniguchi S, Ono Y, Doi Y, Taniguchi S, Matsuura Y, Iwasaki A, Hirata N, Fukuda R, Inoue K, Yamaguchi M, Tashiro A, Egami D, Aoki S, Kondoh Y, Honda K, Osada H, Kumeta H, Saio T, Okiyoneda T.
Identification of α-Tocopherol succinate as an RFFL-substrate interaction inhibitor inducing peripheral CFTR stabilization and apoptosis
Biochem Pharmacol. 2023, 215, 115730. DOI: 10.1016/j.bcp.2023.115730.

Kawagoe S, Kumashiro M, Mabuchi T, Kumeta H, Ishimori K, Saio T.
Heat-Induced Conformational Transition Mechanism of Heat Shock Factor 1 Investigated by Tryptophan Probe.
Biochemistry 2022, 64, 24, 2897. DOI: 10.1021/acs.biochem.2c00492

Muraoka T, Saio T, Okumura M.
Biophysical elucidation of neural network and chemical regeneration of neural tissue.
Biophys Physicobiol. 2022, 19, e190024. DOI: 10.2142/biophysico.bppb-v19.0024

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

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

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

*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

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

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

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

*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

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

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

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.

*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.

*小田 隆， 齋尾 智英, 検出技術：天然変性タンパク質の構造生物学, In: 特集 相分離生物学：相分離メガネのススメ, 生物工学会誌, 98, 228-254, 2020.

*斉尾 智英, 石森 浩一郎. 立体構造から明らかにする分子シャペロンの作用機序. 生物物理, 59, 197-201, 2019.

*児玉 耕太, 斉尾 智英, 前仲 勝実, 金城 政孝. WetとDryのコミュニケーションによるアカデミア創薬. バイオサイエンスとインダストリー, 75, 323-325, 2017.

*斉尾 智英トリガーファクターシャペロンによる動的基質認識の構造基盤． 生化学, 88, 406-610, 2016.

*斉尾 智英, Charalampos G. Kalodimos. トリガー因子は変性状態のタンパク質とのダイナミックな相互作用により凝集を抑制する. ライフサイエンス 新着論文レビュー, 10.7875/first.author.2014.065, 2014.