Publications

２０１３年～ | ２００８年～２０１２年 | ２００２年～２００６年 | ２０００年以前

２０１３年～（東北大赴任以降）、２０２３年〜（九州大学とのクロスアポイント）

２０２３年

• Han, B.B.#, Watanabe, S.#, Nomura, N., Liu, K., Uemura, T., Inoue, M., Tsutsumi, A., Fujita, H., KInoshita, K., Kato, Y., Iwata, S., Kikkawa, M. and Inaba, K.* (#contributed equally to this work) “Cryo-EM structures of human zinc transporter ZnT7 reveal the mechanism of Zn2+ uptake into the Golgi apparatus; Nature Communications 14, 4770 (2023)
• Amagai, Y., Yamada, M. , Kowada, T., Watanabe, T., Du, Y., Liu, R., Naramoto, S., Watanabe, S., Kyozuka, J., Aneli, T., Temio, T., Sitia, R., Mizukami, S. and Inaba, K.* “Zinc homeostasis giverned by Golgi-resident ZnT family members regulates ERp44-mediated proteostasis at the ER-Golgi interface; Nature Communications 14, 2683 (2023)
• Chen, Z., Watanabe, S., Hashida, H., Inoue, M., Daigaku, Y., Kikkawa, M., and Inaba, K.* “Cryo-EM structures of human SPCA1a reveal the mechnism of Ca2+/Mn2+ transport into the Golgi apparatus; Science Advances 9, eadd9742 (2023)
• Cai, X., Ito, S., Noi, K., Inoue, M., Ushioda, R., Kato, Y., Nagata, K., and Inaba, K.* “Mechanistic characterization of disulfide bond reduction of an ERAD substrate mediated by cooperation between ERdj5 and BiP; J. Biol. Chem. in press (2023)
• Matsunaga, T., Sano, H., Takita, K., Morita, M., Yamanaka, S., Ichikawa, T., Numakura, T., Ida, T., Jung, M., Ogata, S., Yoon, S., Fujino, N., Kyogoku, Y., Sasaki, Y., Koarai, A., Tamada, T., Toyama, A., Nakabayashi, T., Kageyama, L., Kyuwa, S., Inaba, K., Watanabe, S., Nagy, P., Sawa, T., Oshiumi, H., Ichinose, M., Yamada, M., Sugiura, H., Wei, F.Y., Motohashi, H. and Akaike, T. “Supesulphides provide airway protection in viral and chronic lung diseases; Nature Communications 14, 4476 (2023)
• Uegaki, K., Tokunaga, Y., Inoue, M., Takashima, S., Inaba, K., Takeuchi, K., Ushioda, R. and Nagata, K. “ The oxidative folding of nascent polypeptides provides electrons for reductive reactions in the ER; Cell Reports 42, 112742 (2023)

２０２２年

• Zhang, Y., Kobayashi, C., Cai, X., Watanabe, S., Tsutsumi, A., Kikkawa, M., Sugita, Y. and Inaba, K.* “Multiple sub-state structures of SERCA2b reveal conformational overlap at transition steps during the catalytic cycle; Cell Reports 41, 111760 (2022)
• Zhang, Y. and Inaba, K.* “Machanisms of conformational and functional regulation of SERCA2b, the ubiquitous endoplasmic reticulum calcium pump ; BioEssays e2200052 (2022)
• Isomoto, A., Shoguchi, E., Hisata, K., Inoue, J., Sun, Y. Inaba, K., Sato, N., Ogawa, T. and Shibata, H. “Active expression of genes for protein modification enzymesin Habu Venom Grands; Toxins 14, 300 (2022)
• Liu, R., Kowada, T., Du, Y., Amagai, Y., Matsui, T., Inaba, K., and Mizukami, S. “Organelle-level labile Zn2+ mapping based on targettable fluorescent snsors; ACS sensors 7, 748-757 (2022)

２０２１年

• Zhang, Y., Watanabe, S., Tsutsumi, A., Kadokura, H., Kikkawa, M. and Inaba, K.* “Cryo-EM analysis provides new mechanistic insight into ATP binding to Ca2+-ATPase SERCA2b; EMBO Journal 40, e108482 (2021)
• Okumura, M.*, Kanemura, S., Matsusaki, M., Kinoshita, M., saio, T., Ito, D., Hirayama, C., Kumuta, H., Watabe, M., Amagai, Y., Lee, Y.-H., Akiyama, S., and Inaba, K.* “A unique leucine-valine adhesive motif supports structure and function of protein disulfide isomerase P5 via dimerization; Structure 29, 1357-1370 (2021)
• Hirayama, C., Machida, K., Noi, K., Murakawa, T., Okumura, M., Ogura, T., Imataka, H. and Inaba, K.* “Distinct roles and actions of protein disulfide isomerase family enzymes in catalysis of nascent-chain disulfide bond formation; iScience 4, 102296 (2021)
• Okumura, M., Noi, K. and Inaba, K.* “Visualization of structura dynamics of protein disulfide isomerase enzymes in catalysis of oxidative folding and reductive unfolding; Curr. Opin. Struct. Biol. 66, 49-57 (2021)
• Matsusaki, M., Okada, R., Tanikawa, Y., Kanemura, S., Ito, D., Lin, Y., Watabe, M., Yamaguchi, H., Saio, T., Lee, Y.H., Inaba, K., and Okumura, M. “ Functional interplay between P5 and PDI/ERp72 to drive protein folding; Biology 10, 1112 (2021)
• Tanikawa, Y., Kanemura, S., Ito, D., Lin, Y., Matsusaki, M., Kuroki, K., Yamaguchi, H., Maenaka, K., Lee, Y.H., Inaba, K., and Okumura, M. “ Ca2+ regulates ERp57-Calnexin complex formation; Molecules 26, 2853 (2021)

２０２０年

• Zhang, Y., Inoue, M., Tsutsumi, A., Watanabe, S., Nishizawa, T., Nagata, K., Kikkawa, M. and Inaba, K.* “Cryo-EM structures of SERCA2b reveal the mechanism of regulation by the luminal extension tail; Science Advances 6, eabb0147 (2020)
• Kadokura, H.*, Dazai, Y., Fukuda, Y., Hirai, N., Nakamura, O. and Inaba, K. “Observing the nonvectrorial yet cotranslational folding of a multidomain protein, LDL, receptor, in the ER of mammalian cells; Proc. Natl. Acad. Sci. USA 117, 16401-16408 (2020)
• Kanemura, S., Elza, F. S., Hirai, N., Okumura, M., Kadokura, H. and Inaba, K.* “Characterization of the ER-resident peroxidases GPx7 and GPx8 shows the higher oxidative activity of GPx7 and its linkage to oxidative protein folding; J. Biol. Chem. 295, 12772-12785 (2020)
• Kowada, T., Watanabe, T., Amagai, Y., Liu, R., Yamada, M., Takahashi, H. Inaba, K., and Mizukami, S. “Quantitative imaging of labile Zn2+ in the Golgi apparatus using a localizable small-molecule fluorescent probe; Cell Chem. Biol. 27, 1521-1531 (2020)
• Ninagawa, S., Tada, S., Okumura, M., Inoguchi, K., Kinoshita, M., Kanemura, S., Imami, K., Umezawa, H., Ishikawa, T., Mackin, R., Torii, S., Ishihama, Y., Inaba, K., Anazawa, T., Nagamine, T. and Mori, K. “ Antipsychotic olanzapine-induced misfolding of proinsulin in the endoplasmic reticulum accounts for atypical development of diabetes; eLife 66, 49-57 (2020)
• Kanemura, S., Matsusaki, M., Inaba, K., Okumura, M.* “PDI family members as guides for client folding and assembly; Int. J. Mol. Sci. 21, E9351 (2020)
• Matsusaki, M.#, Kanemura, S.#, Kinoshita, M.#, Lee, Y.H., Inaba, K.* and Okumura, M.* (#contributed equally to this work) “The protein disulfide isomerase family: from proteostasis to pathogenesis; BBA General Subjects 1864, 129338 (2020)

２０１９年

• Watanabe, S.#, Amagai, Y.#, Sannino, S.#, Tempio, T., Anelli, T., Harayama, M., Masui, S., Sorrentino, I., Yamada, M., Sitia, R.* and Inaba, K.* (#contributed equally to this work) “Zinc regulates ERp44-dependent protein quaility control in the early secretory pathway; Nature Communications 10, 603 (2019)
• Okumura, M.#*, Noi, K.#, Kanemura, S., Kinoshita, M., Saio, T., Inoue, Y., Hikima, T., Akiyama, S., Ogura, T.* and Inaba, K.* (#contributed equally to this work) “Dynamic assembly of protein disulfide isomerase in catalysis of oxidative folding; Nature Chemical Biology 15, 499-509 (2019) ★Faculty of 1000に選ばれました！
• Inoue, M., Sakuta, N., Watanabe, S., Zhang, Y., Yoshikaie, K., Tanaka, Y., Ushioda, R., Kato, Y., Takagi, J., Tsukazaki, T., Nagata, K. and Inaba, K.* “Structural basis of sarco/endoplasmic reticulum Ca2+-ATPase 2b regulation; Cell Reports 27, 1221-1230 (2019)
• Nakamura, Y.*, Lin, Y.-C.#, Watanabe, S.#, Liu, Y.C., Katsuyama, K., Kanehara, K. and Inaba, K.* (#contributed equally to this work) “ High-resolution crystal structure of Arabidopsis FLOWERING LOCUS T illuminates its phospholipid-binding site in flowering iScience (Cell Press) 21, 577-586 (2019)
• Fujimoto, T., Inaba, K., and Kadokura, H.* “Methods to identify the substrates of thiol-disulfide oxidoreductases; Protein Science 28, 30-40 (2019)
• Okada, S.#, Matsusaki, M.#, Araki, K., Hidaka, Y., Inaba, K., Okumura, M.*, and Muraoka, T.* (#contributed equally to this work) “Coupling effects of thiol and urea-type groups for promotion of oxidative protein folding; Chem. Commun. 55, 759-762 (2019)★雑誌のバックカバーを飾りました！

２０１８年

• Fujimoto, T., Nakamura, O., Saito, M., Tsuru, A., Matsumoto, M., Kohno, K., Inaba, K. and Kadokura, H.* “Identification of the physiological substrates of PDIp, a pancreas-specific protein disulfide isomerase family member; J. Biol. Chem. 293, 18421-18433 (2018)
• O'Brien, H., Kanemura, S., Okumura, M., Baskin, P., Bandyopadhyay, P., Ellgaard, L., Inaba, K., and Safavi-Hemami, H. “Ero1-mediated reoxidation of PDI accelerates the folding of cone-snail toxins; Int. J. Mol. Sci. 19, E3418 (2018)
• Arai, K., Takei, T., Shinozaki, R., Noguchi, M., Fujisawa, S., Katayama, H., Moroder, M., Ando, S., Okumura, M., Inaba, K., Hojo, H. and Iwaoka, M. “Characterization and optimization of two-chain folding pathways of insulin via native chain assembly; Communications Chemistry (Nature Research) 26,(2018)★国内外の多くのメディアに紹介されました！

２０１７年

• Watanabe, S., Harayama, M., Kanemura, S., Sitia, R. and Inaba, K.* “Structural basis of pH-dependent client binding by ERp44, a key regulator of protein secretion at the ER-Golgi interface” Proc. Natl. Acad. Sci. USA 114, 3224-3232 (2017)
• Maegawa, K., Watanabe, S., Noi, K., Okumura, M., Amagai, Y., Inoue, M., Ushioda, R., Nagata, K., Ogura, T. and Inaba, K.* “The highly dynamic nature of ERdj5 is key to efficient elimination of aberrant protein oligomers through ER-associated degradation; Structure 6, 846-857 (2017)★雑誌の表紙を飾りました！
• Arai, K.#, Takei, T.#, Okumura, M.#, Watanabe, S.#, Amagai, Y., Hojo, H.*, Inaba, K.* and Iwaoka, M.* (#contributed equally to this work; *co-corresponding authors) “Preparation of selenoinsulin as a long-lasting insulin analog; Angewandte Chemie 56, 5522-5526 (2017)
• Akaike, T., Ida, T., Wei, F.Y., Nishida, M., Kumagai, Y., Alam, M.M., Ihara, H., Sawa, T., Matsunaga, T., Kasamatsu, S., Nishimura, A., Morita, M., Tomizawa, K., Nishimiura, A., Watanabe, S., Inaba, K., Shima, H., Tanuma, N., Jung, M., Fujii, S., Watanabe, Y., Ohmuraya, M., Nagy, P., Feelish, M, Fukuto, M. and Motohashi, H. “Cysteinyl-tRNA synthetase governs cysteine polysulfidation and mitochondrial bioenergetics; Nature Communications 8, 1177- (2017)

２０１６年

• Kanemura, S., Okumura, M., Yutani, K., Ramming, T., Hikima, T., Appenzeller-Herzog, C., Akiyama, S., and Inaba, K.* “Human ER Oxidereductin-1a (Ero1a) undergoes dual regulation through complementary redox interactions with Protein Disulfide Isomerase ” J. Biol. Chem. 291, 23952-23964 (2016)
• Ramming, T.#, Kanemura, S.#, Okumura, M., Inaba, K.* and Appenzeller-Herzog, C.* (#contributed equally to this work; *co-corresponding authors) “Cysteines 208 and 241 in Ero1α are required for maximal catalytic turnover”, Redox Biology 7, 14-20 (2016)
• Ushioda, R., Miyamoto, A., Inoue, M., Watanabe, S., Okumura, M., Maegawa, K., Uegaki, K., Fujii, S., Fukuda, Y., Umitsu, M., Takagi, J., Inaba, K., Mikoshiba, K., Nagata, K.“Redox-assisted regulation of Ca2+ homeostasis in the endoplasmic reticulum by ERdj5” Proc. Natl. Acad. Sci. USA 113, 6055-6063 (2016)
• Cao, Z, van Lith, M., Mitchell, L. J., Pringle, M. A., Inaba, K. and Bulleid, N. J. “The membrane topology of Vitamin K Epoxide Reductase is conserved between human isoforms and the bacterial enzyme” Biochem. J 473, 851-858 (2016)

２０１５年

• Okumura, M.^†, Kadokura, K.^†and Inaba, K.* (^†contributed equally to this work) "The structures and functions of protein disulfide isomerase family members involved in proteostasis in the endoplasmic reticulum. "Free Rad. Biol. Med. 83, 314-322 (2015)
• Watanabe, S., Kawashima, T., Nishitani, Y., Kanai, T., Wada, T., Inaba, K., Atomi, H., Imanaka, T. and Miki, K. “Structural basis of a Ni acquisition cycle for [NiFe]-hydrogenase by HypA and its enhancer.” Proc. Natl. Acad. Sci. USA112, 7701-7706 (2015)
• Ramming, T., Okumura, M., Kanemura, S., Baday, S., Birk, J., Moes, S., Spiess, M., Jeno, P., Berneche, S., Inaba, K. and Appenzeller- Herzog, C. "A PDI-catalyzed thiol/disulfide switch regulates the production of hydrogen peroxide by human Ero1" Free Rad. Biol. Med. 83, 361-372 (2015)
• Murata, A., Ito, Y., Kashima, R., Kanbayashi1, S., Nanatani, K., Igarashi, C., Okumura, M., Inaba, K., Tokino, T., Takahashi, S. and Kamagata, K. “One-dimensional sliding of p53 along DNA is accelerated in the presence of Ca2+ or Mg2+ at millimolar concentrations.” J. Mol. Biol. 427, 2663-2678 (2015)

２０１４年

• Kojima, R.^†, Okumura, M.^†, Masui, S., Kanemura, S., Inoue, M., Saiki, M., Yamaguchi, H., Hikima, T., Suzuki, M., Akiyama, S. and Inaba, K.* (^†contributed equally to this work) "Radically different thioredoxin domain arrangement of ERp46, an efficient disulfide-bond introducer of the mammalian PDI family" Structure 22, 431-443 (2014)
• Okumura, M.*, Kadokura, K., Hashimot, S., Yutani, K., Kanemura, S., Hikima, T., Hidaka, Y., Ito, L., Shiba, K., Masui, S., Imai, D., Imaoka, S., Yamaguchi, H.* and Inaba, K.* "Inhibition of the functional interplay between ER oxidoreduclin-1a(Ero1a) and protein disulfide isomerase (PDI) by the endocrine disruptor bisphenol A. "J. Biol. Chem. 289, 27004-27018 (2014)
• Sannino, S., Anelli, T., Cortini, M., Masui, S., Degano, M., Fagioli, C, Inaba, K., Sitia, R. "Progressive quality control of secretory proteins in the early secretory compartment by ERp44" J. Cell. Sci. 127, 4260-4269 (2014)
• Appenzeller-Herzog, C., Inaba, K., Delaunay-Moisan, A. “Cell biology of cysteine-based molecular switches.” Int. J. Cell Biol. 2014, 157038-039 (2014)

２０１３年

• Sato, Y.^†,Kojima, R.^†,Okumura, M.^†,Hagiwara, M^†., Masui S., Maegawa, K., Saiki, M., Horibe, T., Suzuki, M. and Inaba, K.* (^†contributed equally to this work) “Synergistic cooperation of PDI family member proteins in peroxiredoxin 4-driven oxidative protein folding” Scientific Reports 3: 2456 (2013)
• Kojima, R.^†, Okumura, M.^†and Inaba, K.* (^†contributed equally to this work) "Structural basis of disulfide bond formation in the bacterial periplasm and mammalian ER" Encyclopedia of Life Science DOI: 10.1002 (2013)
• Walden, P. M., Halili, M. A., Archbold, J. K., Lindahl, F., Fairlie, D. P., Inaba, K.* and Martin, J. L.*(*co-corresponding authors) "The a-ProteobacteriaWolbachia pipientisprotein disulfide machinery has a regulartory mechanism absent in g-Proteobacteria" PLoS One 8, e81440 (2013)
• Kadokura, H.*, Saito, M., Tsuru, A., Hosoda, A., Iwawaki, T., Inaba, K. and Kohno, K.* "Identification of the redox parners of ERdj5/JPDI, a PDI family member, from an animal tissue. Biochem. Biophys. Res. Comm. 440, 245-250 (2013)
• Vavassori, S.^†, Cortini, M.^†, Masui, S.^†, Sannino, S.^†, Anelli, T., Caserta, I., Fagioli, C., Mossuto, M., Fornili, A., van Anken, E., Degano, M., Inaba, K. and Sitia, R. (^†contributed equally to this work) “A pH-Regulated Quality Control Cycle for Surveillance of Secretory Protein Assembly” Mol. Cell 50, 783-792 (2013) ★同雑誌のPreviewとNat. Chem. Biol.のHighlightで紹介され、またFaculty of 1000にも選ばれました！

２００８年～２０１２年（九州大学生体防御医学研究所・独立准教授時代）

２０１２年

• Sato, Y. and Inaba, K.* “Disulfide bond formation network in the biological kingdoms” FEBS J 279, 2262-2271 (2012) ★One of the top10 most cited FEBS journal papers two years from publicationに選ばれました！
• Araki, K. and Inaba, K.* “Structure, mechanism and evolution of Ero1 family enzymes” Antioxid. Redox Signal. 16, 790-799 (2012) ★雑誌の表紙を飾りました！

２０１１年

• Hagiwara, M.^†, Maegawa, K.^†, Suzuki, M.^†, Ushioda, R., Araki, K., Matsimoto, Y., Hoseki, J., Nagata, K.* and Inaba, K.* (^†contributed equally to this work) “Structural basis of an ERAD pathway mediated by the ER-resident disulfide reductasse ERdj5” Mol. Cell 41, 432-444 (2011) ★雑誌の表紙を飾りました！
• Masui, S., Vavassori, S., Fagioli, C., Sitia, R. and Inaba, K.* "Molecular bases of cyclic and specific disulfide interchange between human Ero1a protein and protein-disulfide isomerase (PDI)" J. Biol. Chem. 286, 16262-16271 (2011)
  
• Ishitani, S., Inaba, K.,  Matsumoto, K. and Ishitani, T.“Homo-dimerization of Nemo-like kinase is essential for activation and nuclear localization” Mol. Biol. Cell 22, 266-277 (2011)

２０１０年

• Inaba, K.*, Masui, S., Iida, H. Vavassori, S., Sitia, R. and Suzuki, M. “Crystal structures of human Ero1a reveal the mechanisms of regulated and targeted oxidation of PDI” EMBO J 29, 3330-3343 (2010)
• Inaba, K.* Structural basis of protein disulfide bond generation in the cell. Genes to Cells 15, 935-943 (2010)
• Serve, O., Kamiya, Y., Meano, A., Nakano, M., Murakami, C., Sasakawa, H., Yamaguchi, Y., Harada, T., Kurimoto, E., Yagi-Utsumi, M., Iguchi, T., Inaba, K., Kikuchi, J., Asami, O., Kajino, T., Oka, T., Nakasako, M. and Kato, K. Redox-dependent intramolecular domain rearrangement of protein disulfide isomerase coupled with exposure of its substrate-binding hydrophobic surface. J. Mol. Biol. 396, 361-374 (2010)

２００９年

• Inaba, K.*, Murakami, S., Nakagawa, A.,Iida, H.,Kinjo, H., Ito, K. and Suzuki, M. “Dynamic nature of disulfide bond formation catalysts revealed by crystal structures of DsbB” EMBO J 28, 779-791 (2009)
• Inaba, K.* “Disulfide bond formation system in Eschericia coli” J. Biochem. 146, 591-597 (2009)

２００８年

• Inaba, K., Suzuki, M. Maegawa, K., Akiyama, S., Ito, K. and Akiyama, Y. “A pair of circularly permutated PDZ domains control RseP, the S2P family intramembrane protease of E. coli” J. Biol. Chem. 283, 35042-35052 (2008)
• Ito, K. and Inaba, K. “The disulfide bond formation (Dsb) system” Curr. Opin. Struct. Biol. 18, 450-458 (2008)
• Inaba, K. and Ito, K. “Structure and mechanisms of the DsbB-DsbA disulfide bond generation machine” Biochem. Biophys. Acta. Mol. Cell Res. 1783, 520-529 (2008)
• Inaba, K.* “Protein disulfide bond generation inEscherichia coli DsbB-DsbA” J. Synchr. Rad. 15, 199-201 (2008) ★雑誌の表紙を飾りました！

２００２年～２００６年（京都大学ウイルス研究所・さきがけ２１研究員時代）

２００６年

• Inaba, K.*, Murakami, S., Suzuki, M., Nakagawa, A., Yamashita, E., Okada, K. and Ito, K.*
  “Crystal structure of the DsbB-DsbA complex reveals a mechanism of disulfide bond generation”
  Cell 127, 789-801 (2006) ★Faculty of 1000に選ばれ、EXCEPTIONALの評価を受けました！
• Inaba, K., Takahashi, Y.-H., Ito, K. and Hayashi, S. “Critical role of a thiolate-quinone charge transfer complex and its adduct form in de novo disulfide bond generation by DsbB” Proc. Natl. Acad. Sci. USA.103, 287-292 (2006)
• Takahashi, Y.-H., Inaba, K. and Ito, K. “Role of the cytosolic loop of DsbB in catalytic turnover of the ubiquinone-DsbB complex” Antioxid. Redox Signal. 8, 743-752, (2006)

２００５年

• Inaba, K., Takahashi, Y.-H. and Ito, K. “Reactivities of quinone-free DsbB from Escherichia coli” J. Biol. Chem. 280, 33035-33044, (2005)

２００４年

• Takahashi, Y.-H., Inaba, K. and Ito, K. “Characterization of menaquinone -dependent disulfide bond formation pathway of Escherichia coli” J. Biol. Chem. 279, 47057-47065, (2004)
• Inaba, K., Takahashi, Y.-H. and Ito, K. “DsbB elicits a red-shift of bound ubiquinone during the catalysis of DsbA oxidation” J. Biol. Chem. 279, 6761-6768, (2004)

２００２年

• Inaba, K. and Ito, K. “Paradoxical redox properties of DsbB and DsbA in the protein disulfide-introducing reaction cascade” EMBO J 21, 2646-2654 (2002) ★Science誌Editor’s Choiceに掲載されました（Vol. 296, p1767, 2002)！

２０００年以前（京都大学工学研究科在学＆英国留学時代）

Selected papersのみ

• Inaba, K., Kobayashi, N. and Fersht, A. R.“Conversion of two-state to multi-state folding kinetics on fusion of two protein foldons” J. Mol. Biol. 302, 219-233, (2000)
• Inaba, K., Ishimori, K. and Morishima, I.“Substitution of the heme binding module in hemoglobin a- and b-subunits- Implication for different regulation mechanism of the heme proximal structure between hemoglobin and myoglobin” J. Biol. Chem. 275, 12438-12445, (2000)
• Shirai, T., Fujikake, M., Yamane, T., Inaba, K., Ishimori, K. and Morishima, I. “Crystal structure of a protein with an artificial exon-shuffling, module M4-substituted chimera hemoglobin ba, at 2.5 A resolution.” J. Mol. Biol. 287, 369-382, (1999)
• Inaba, K., Ishimori, K., Imai, K. and Morishima, I. “Structural and functional roles of heme binding module in globin proteins: Identification of the segment regulating the heme binding structure” J. Mol. Biol. 283, 311-327, (1998)
• Inaba, K., Ishimori, K., Imai, K. and Morishima, I. “Structural and functional effects of pseudo-module substitution in hemoglobin subunits- New structural and functional units in globin structure” J. Biol. Chem. 273, 8080-8087, (1998)
• Inaba, K., Wakasugi, K., Ishimori, K., Konno, T., Kataoka, M. and Morishima, I. “Structural and functional roles of modules in hemoglobin subunits-Substitution of module M4 in hemoglobin subunits” J. Biol. Chem. 272, 30054-30060, (1997)