>English

Publication

研究実績

(* = corresponding author)

【代表論文】

Kawagoe S, Matsusaki M, Mabuchi Y, Ogasawara Y, Watanabe K, Ishimori K, *Saio T. Mechanistic Insights Into Oxidative Response of Heat Shock Factor 1 Condensates. JACS Au, 2025, 5, 606–617. DOI: 10.1021/jacsau.4c00578.

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.

*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., 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

【主要論文】

< 2025 >

Lee YH, Saio T, Watabe M, Matsusaki M, Kanemura S, Lin Y, Mannen T, Kuramochi T, Kamada Y, Iuchi K, Tajiri M, Suzuki K, Li Y, Heo Y, Ishii K, Arai K, Ban K, Hashimoto M, Oshita S, Ninagawa S, Hattori Y, Kumeta H, Takeuchi A, Kajimoto S, Abe H, Mori E, Muraoka T, Nakabayashi T, Akashi S, Okiyoneda T, Vendruscolo M, Inaba K, Okumura M
Ca2+-driven PDIA6 biomolecular condensation ensures proinsulin folding
Nat. Cell Biol. 2025, 27, 1952–1964. DOI: 10.1038/s41556-025-01794-8

Iguchi N, Isozumi N, Hattori Y, Imamura T, Yokoyama T, So M, Nanaura H, Kiriyama T, Eura N, Yamaoka M, Iwasa N, Shiota T, Nakanishi M, Konishi N, Ito H, Takeuchi A, Mori M, Ohki S, Kumeta H, Koga H, Watabe M, Mabuchi T, Kanemura S, Okumura M, Tanaka Y, Morishima K, Sugiyama M, Ide F, Matsumura H, Yoshizawa T, Ota I, Suzuki N, Aoki M, Yamashiro Y, Saio T, Sugie K, Mori E
Zinc finger domains bind low-complexity domain polymers
Nat. Commun. 2025, 16, 8922. DOI: 10.1038/s41467-025-64382-2

Kawagoe S, Kumeta H, Saio T
19F NMR-based solvent accessibility profiling reveals tryptophan ring-flip dynamics in a protein
Protein Sci. 2025, 34, e70307. DOI: 10.1002/pro.70307

Ali H, Yamanishi M, Tsuchiya M, Hasi RY, Matsusaki M, Saio T, Aihara M, Kawakami R, Tanaka T
Solubilization of Saturated Fatty Acids and Its Lysophosphatidylcholine by Complexation With Bovine Serum Albumin
Lipids 2025, Early View. DOI: 10.1002/lipd.70005

Mori K, Kuramochi T, Matsusaki M, Hashiguchi Y, Okumura M, Saio T, Furukawa Y, Arai K, Muraoka T
Metal-Responsive Up-Regulation of Bifunctional Disulfides for Suppressing Protein Misfolding and Promoting Oxidative Folding
Angew. Chem. Int. Ed. 2025, 64, e202502187. DOI: 10.1002/anie.202502187

Hattori Y, Kumashiro M, Kumeta Y, Kyo T, Kawagoe S, Matsusaki M, Saio T
A Disease-Associated Mutation Impedes PPIA through Allosteric Dynamics Modulation
Biochemistry 2025, 64, 2971–2975. DOI: 10.1021/acs.biochem.5c00260

Park NY, Heo Y, Yang JW, Yoo JM, Jang HJ, Jo JH, Park SJ, Lin Y, Choi J, Jeon H, Cha SJ, Bae G, Kim D, Kim J, Zeno W, Park JB, Isozumi N, Saio T, Kim SH, Lee H, Hong BH, Nahm M, Lee YH, Hong YB
Graphene Quantum Dots Attenuate TDP-43 Proteinopathy in Amyotrophic Lateral Sclerosis
ACS Nano 2025, 19, 8692-8710. DOI: 10.1021/acsnano.4c15283

Kawagoe S, Matsusaki M, Mabuchi Y, Ogasawara Y, Watanabe K, Ishimori K, Saio T
Mechanistic Insights Into Oxidative Response of Heat Shock Factor 1 Condensates
JACS Au 2025, 5, 606–617. DOI: 10.1021/jacsau.4c00578

< 2024 >

Sato S, Miyano S, Nakane K, Liu Z, Kumashiro M, Saio T, Tanaka Y, Shigenaga A, Fujimura C, Koyanagi E, Nishi H, Tomoshige A, Ishikawa M
Tyrosine bioconjugation using stably preparable urazole radicals
Tetrahedron Chem. 2024, 12, 100111. DOI: 10.1016/j.tchem.2024.100111

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, 15, 12676-12685. 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, 15, 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

< 2023 >

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

< 2022 >

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, 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, 16, 996-1009.e9. 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.
Nat. 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

< 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.

【書籍】

*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.

【主要な和文総説】

*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.