Yang, K., Arai, M., & Wright, P.E. (2020) Determining binding kinetics of intrinsically disordered proteins by NMR spectroscopy. Methods Mol. Biol. in press.
Kunihara, T., Hayashi, Y., & Arai, M. (2019) Conformational diversity in the intrinsically disordered HIV-1 Tat protein induced by zinc and pH. Biochem. Biophys. Res. Commun. 509(2), 564-569.
Kenri, T., Kawakita, Y., Kudo, H., Matsumoto, U., Mori, S., Furukawa, Y., Tahara, Y.O., Shibayama, K., Hayashi, Y., Arai, M., & Miyata, M. (2019) Production and characterization of recombinant P1 adhesin essential for adhesion, gliding, and antigenic variation in the human pathogenic bacterium, Mycoplasma pneumoniae. Biochem. Biophys. Res. Commun. 508(4), 1050-1055.
Kujirai, J., Nanba, S., Kadowaki, T., Oka, Y., Nishiyama, Y., Hayashi, Y., Arai, M., & Hihara, Y. (2018) Interaction of the GntR-family transcription factor Sll1961 with thioredoxin in the cyanobacterium Synechocystis sp. PCC 6803. Scientific Reports 8, 6666.
Takenaka, T., Nakamura, T., Yanaka, S., Yagi-Utsumi, M., Chandak, M.S., Takahashi, K., Paul, S., Makabe, K., Arai, M., Kato, K., & Kuwajima, K. (2017) Formation of the chaperonin complex studied by 2D NMR spectroscopy. PLoS ONE 12(10), e0187022.
Otosu, T., Ishii, K., Oikawa, H., Arai, M., Takahashi, S., & Tahara, T. (2017) Highly heterogeneous nature of the native and unfolded states of B domain of protein A revealed by two-dimensional fluorescence lifetime correlation spectroscopy. J. Phys. Chem. B 121(22), 5463-5473.
Haberz, P., Arai, M., Martinez-Yamout, M.A., Dyson, H.J., & Wright, P.E. (2016) Mapping the interactions of adenoviral E1A proteins with the p160 nuclear receptor coactivator binding domain of CBP. Protein Sci. 25(12), 2256-2267.
Arai, M., Sugase, K., Dyson, H.J., & Wright, P.E. (2015) Conformational propensities of intrinsically disordered proteins influence the mechanism of binding and folding. Proc. Natl. Acad. Sci. USA 112(31), 9614-9619.
Oikawa, H., Kamagata, K., Arai, M., & Takahashi, S. (2015) Complexity of the folding transition of the B domain of protein A revealed by the high-speed tracking of single-molecule fluorescence time series. J. Phys. Chem. B 119(20), 6081-6091.
Ohori, Y., Okazaki, H., Watanabe, S., Tochio, N., Arai, M., Kigawa, T., & Nishimura, C. (2014) Flexible and rigid structures in HIV-1 p17 matrix protein monitored by relaxation and amide proton exchange with NMR. Biochim. Biophys. Acta 1844(3), 520-526.
Oikawa, H., Suzuki, Y., Saito, M., Kamagata, K., Arai, M., & Takahashi, S. (2013) Microsecond dynamics of an unfolded protein by a line confocal tracking of single molecule fluorescence. Scientific Reports 3, 2151.
新井宗仁(2013)「タンパク質の揺らぎと機能 〜結合と触媒〜」『揺らぎ・ダイナミクスと生体機能 〜物理化学的視点から見た生体分子〜』(寺嶋正秀 編)第17章 pp.267-280, 化学同人(ISBN-10: 9784759815108)Arai, M., Ferreon, J.C., & Wright, P.E. (2012) Quantitative analysis of multisite protein ligand interactions by NMR: binding of intrinsically disordered p53 transactivation subdomains with the TAZ2 domain of CBP. J. Am. Chem. Soc. 134(8), 3792-3803.
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Lee, C.W., Ferreon, J.C., Ferreon, A.C.M, Arai, M., & Wright, P.E. (2010) Graded enhancement of p53 binding to CREB-binding protein (CBP) by multisite phosphorylation. Proc. Natl. Acad. Sci. USA 107(45), 19290-19295.
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