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Original Papers


Otosu, T., Ishii, K., Oikawa, H., Arai, M., Takahashi, S., & Tahara, T.
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 in press (2017)

Kudo, H., Nawa, R., Hayashi, Y., & Arai, M.
Comparison of aldehyde-producing activities of cyanobacterial acyl-(acyl carrier protein) reductases.
Biotechnology for Biofuels 9: 234 (2016)

Haberz, P., Arai, M., Martinez-Yamout, M.A., Dyson, H.J., & Wright, P.E.
Mapping the interactions of adenoviral E1A proteins with the p160 nuclear receptor coactivator binding domain of CBP.
Protein Sci. 25(12), 2256-2267 (2016)

Arai, M., Sugase, K., Dyson, H.J., & Wright, P.E.
Conformational propensities of intrinsically disordered proteins influence the mechanism of binding and folding.
Proc. Natl. Acad. Sci. USA 112(31), 9614-9619 (2015)

Oikawa, H., Kamagata, K., Arai, M., & Takahashi, S.
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 (2015)

Hayashi, Y., Yasugi, F., & Arai, M.
Role of cysteine residues in the structure, stability, and alkane producing activity of cyanobacterial aldehyde deformylating oxygenase.
PLoS ONE 10(4), e0122217 (2015)

Ohori, Y., Okazaki, H., Watanabe, S., Tochio, N., Arai, M., Kigawa, T., & Nishimura, C.
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 (2014)

Oikawa, H., Suzuki, Y., Saito, M., Kamagata, K., Arai, M., & Takahashi, S.
Microsecond dynamics of an unfolded protein by a line confocal tracking of single molecule fluorescence.
Scientific Reports 3, 2151 (2013)

Arai, M., Ferreon, J.C., & Wright, P.E.
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 (2012)

Arai, M., Iwakura, M., Matthews, C.R., & Bilsel, O.
Microsecond subdomain folding in dihydrofolate reductase.
J. Mol. Biol. 410(2), 329-342 (2011)

Arai, M., Dyson, H.J., & Wright, P.E.
Leu628 of the KIX domain of CBP is a key residue for the interaction with the MLL transactivation domain.
FEBS Lett. 584(22), 4500-4504 (2010)

Lee, C.W., Ferreon, J.C., Ferreon, A.C.M, Arai, M., & Wright, P.E.
Graded enhancement of p53 binding to CREB-binding protein (CBP) by multisite phosphorylation.
Proc. Natl. Acad. Sci. USA 107(45), 19290-19295 (2010)
mfeatured article in UCSD-Nature Signaling Gatewayn


Reviews


Munehito Arai
Quantitative analysis of protein-ligand interactions by NMR (Japanese)
Seibutsubutsuri 53(6), 305-308 (2013)


Books


Munehito Arai
Fluctuation and Function of Proteins - Binding and Catalysis - (Japanese)
In "Fluctuation, Dynamics, and Biological Functions" (Ed. Masahide Terajima)
Chapter 17, pp.267-280, Kagaku-dojin (2013)

Before Mar. 2010


Original Papers


Yokota, A., Takahashi, H., Takenawa, T., & Arai, M.
Probing the roles of conserved arginine-44 of Escherichia coli dihydrofolate reductase in its function and stability by systematic sequence perturbation analysis.
Biochem. Biophys. Res. Commun. 391(4), 1703-1707 (2010)

Ferreon, J.C., Lee, C.W., Arai, M., Martinez-Yamout, M.A., Dyson, H.J., & Wright, P.E.
Cooperative regulation of p53 by modulation of ternary complex formation with CBP/p300 and HDM2.
Proc. Natl. Acad. Sci. USA 106(16), 6591-6596 (2009)

Lee, C.W., Arai, M., Martinez-Yamout, M.A., Dyson, H.J., & Wright, P.E.
Mapping the interactions of the p53 transactivation domain with the KIX domain of CBP.
Biochemistry 48(10), 2115-2124 (2009)

Inobe, T., Takahashi, K., Maki, K., Enoki, S., Kamagata, K., Kadooka, A., Arai, M., & Kuwajima, K.
Asymmetry of the GroEL-GroES complex under physiological conditions as revealed by small-angle x-ray scattering.
Biophys. J. 94(4), 1392-1402 (2008)

Arai, M., Kondrashkina, E., Kayatekin, C., Matthews, C.R., Iwakura, M., & Bilsel, O.
Microsecond hydrophobic collapse in the folding of Escherichia coli dihydrofolate deductase, an α/β-type protein.
J. Mol. Biol. 368(1), 219-229 (2007)

Takahashi, H., Arai, M., Takenawa, T., Sota, H., Xie, Q.H., & Iwakura, M.
Stabilization of hyperactive dihydrofolate reductase by cyanocysteine-mediated backbone cyclization.
J. Biol. Chem. 282(13), 9420-9429 (2007)

Arai, M., & Iwakura, M.
Peptide fragment studies on the folding elements of dihydrofolate reductase from Escherichia coli
Proteins: Structure, Function and Bioinformatics 62(2), 399-410 (2006)

Yamada, Y., Yajima, T., Fujiwara, K., Arai, M., Ito, K., Shimizu, A., Kihara, H., Kuwajima, K., Amemiya, Y., & Ikeguchi, M.
Helical and expanded conformation of equine β-lactoglobulin in the cold-denatured state.
J. Mol. Biol. 350(2), 338-348 (2005)

Nakao, M., Maki, K., Arai, M., Koshiba, T., Nitta, K., & Kuwajima, K.
Characterization of kinetic folding intermediates of recombinant canine milk lysozyme by stopped-flow circular dichroism.
Biochemistry 44(17), 6685-6692 (2005)

Arai, M., & Iwakura, M.
Probing the interactions between the folding elements early in the folding of Escherichia coli dihydrofolate reductase by systematic sequence perturbation analysis.
J. Mol. Biol. 347(2), 337-353 (2005)

Akhtar, M. W., Srinivas, V., Raman, B., Ramakrishna, T., Inobe, T., Maki, K., Arai, M., Kuwajima, K., & Rao, C. M.
Oligomeric Hsp33 with enhanced chaperone activity: gel-filtration, cross-linking and SAXS analysis.
J. Biol. Chem. 279(53), 55760-55769 (2004)

Saeki#, K., Arai#, M., Yoda, T., Nakao, M., & Kuwajima, K. (# equal contribution)
Localized nature of the transition-state structure in goat α-lactalbumin folding.
J. Mol. Biol. 341(2), 589-604 (2004)

Kamagata, K., Arai, M., & Kuwajima, K.
Unification of the folding mechanisms of non-two-state and two-state proteins.
J. Mol. Biol. 339(4), 951-965 (2004) [erratum]

Ali, S.A., Iwabuchi, N., Matsui, T., Hirota, K., Kidokoro, S., Arai, M., Kuwajima, K., Schuck, P., & Arisaka, F.
Reversible and fast association equilibria of a molecular chaperone, gp57A, of bacteriophage T4.
Biophys. J. 85(4), 2606-2618 (2003)

Arai, M., Kataoka, M., Kuwajima, K., Matthews, C.R., & Iwakura, M.
Effects of the difference in the unfolded-state ensemble on the folding of Escherichia coli dihydrofolate reductase.
J. Mol. Biol. 329(4), 779-791 (2003)

Inobe, T., Kikushima, K., Makio, T., Arai, M., & Kuwajima, K.
The allosteric transition of GroEL induced by metal fluoride-ADP complexes.
J. Mol. Biol. 329(1), 121-134 (2003)

Nakao, M., Arai, M., Koshiba, T., Nitta, K., & Kuwajima, K.
Folding mechanism of canine milk lysozyme studied by circular dichroism and fluorescence spectroscopy.
Spectroscopy 17(2-3), 183-193 (2003)

Arai, M., Maki, K., Takahashi, H., & Iwakura, M.
Testing the relationship between foldability and the early folding events of dihydrofolate reductase from Escherichia coli.
J. Mol. Biol. 328(1), 273-288 (2003)

Arai, M., Inobe, T., Maki, K., Ikura, T., Kihara, H., Amemiya, Y., & Kuwajima, K.
Denaturation and reassembly of chaperonin GroEL studied by solution X-ray scattering.
Protein Sci. 12(4), 672-680 (2003)

Inobe, T., Arai, M., Nakao, M., Ito, K., Kamagata, K., Makio, T., Amemiya, Y., Kihara, H., & Kuwajima, K.
Equilibrium and kinetics of the allosteric transition of GroEL studied by solution X-ray scattering and fluorescence spectroscopy.
J. Mol. Biol. 327(1), 183-191 (2003)

Kuwajima, K., Arai, M., Inobe, T., Ito, K., Nakao, M., Maki, K., Kamagata, K., Kihara, H., & Amemiya, Y.
The use of the time-resolved X-ray solution scattering for studies of globular proteins.
Spectroscopy 16(3-4), 127-138 (2002)

Arai, M., Ito, K., Inobe, T., Nakao, M., Maki, K., Kamagata, K., Kihara, H., Amemiya, Y., & Kuwajima, K.
Fast compaction of α-lactalbumin during folding studied by stopped-flow X-ray scattering.
J. Mol. Biol. 321(1), 121-132 (2002)

Qin, Z., Hu, D., Shimada, L., Nakagawa, T., Arai, M., Zhou, J.M., & Kihara, H.
Refolding of β-lactoglobulin studied by stopped-flow circular dichroism at subzero temperatures.
FEBS Lett. 507(3), 299-302 (2001)

Yoda, T., Saito, M., Arai, M., Horii, K., Tsumoto, K., Matsushima, M., Kumagai, I., & Kuwajima, K.
Folding-unfolding of goat α-lactalbumin studied by stopped-flow circular dichroism and molecular dynamics simulations.
Proteins: Structure, Function and Genetics 42(1), 49-65 (2001)

Chaudhuri, T.K., Arai, M., Terada, T.P., Ikura, T., & Kuwajima, K.
Equilibrium and kinetic studies on folding of the authentic and recombinant forms of human α-lactalbumin by circular dichroism spectroscopy.
Biochemistry 39(50), 15643-15651 (2000)

Fukuda, H., Arai, M., & Kuwajima, K.
The folding of green fluorescent protein and the Cycle3 mutant.
Biochemistry 39(39), 12025-12032 (2000)

Arai, M., Hamel, P., Kanaya, E., Inaka, K., Miki, K., Kikuchi, M., & Kuwajima, K.
Effect of an alternative disulfide bond on the structure, stability, and folding of human lysozyme.
Biochemistry 39(12), 3472-3479 (2000)

Forge, V., Hoshino, M., Kuwata, K., Arai, M., Kuwajima, K., & Goto, Y.
Is folding of β-lactglobulin non-hierarchic? Intermediate with native-like β-sheet and non-native α-helix.
J. Mol. Biol. 296(4), 1039-1051 (2000)

Makio, T., Arai, M., & Kuwajima, K.
Chaperonin-affected refolding of α-lactalbumin. Effects of nucleotides and the co-chaperonin GroES.
J. Mol. Biol. 293(1), 125-137 (1999)

Fujiwara, K., Arai, M., Shimizu, A., Ikeguchi, M., Kuwajima, K., & Sugai, S.
Folding-unfolding equilibrium and kinetics of equine β-lactoglobulin: equivalence between the equilibrium molten globule state and a burst phase folding intermediate.
Biochemistry 38(14), 4455-4463 (1999)

Chaudhuri, T.K., Horii, K., Yoda, T., Arai, M., Nagata, S., Terada, T.P., Ikura, T., Uchiyama, H., Tsumoto, K., Kataoka, H., Matsushima, M., Kuwajima, K., & Kumagai, I.
Effect of the extra N-terminal methionine residue on the stability and folding of recombinant α-lactalbumin expressed in Escherichia coli.
J. Mol. Biol. 285(3), 1179-1194 (1999)

Mizuguchi, M., Arai, M., Ke, Y., Nitta, K., & Kuwajima, K.
Equilibrium and kinetics of the folding of equine lysozyme studied by circular dichroism spectroscopy.
J. Mol. Biol. 283(1), 265-277 (1998)

Arai, M., Ikura, T., Semisotnov, G.V., Amemiya, Y., Kihara, H., & Kuwajima, K.
Kinetic refolding of β-lactoglobulin. Studies by synchrotron X-ray scattering, and circular dichroism, absorption and fluorescence spectroscopy.
J. Mol. Biol. 275(1), 149-162 (1998)

Arai, M., & Kuwajima, K.
Rapid formation of a molten globule intermediate in refolding of α-lactalbumin.
Folding & Design 1(4), 275-287 (1996)


Reviews


Kuwajima, K., Inobe, T., & Arai, M.
The allosteric transition of the chaperonin GroEL from Escherichia coli studied by solution X-ray scattering.
Macromolecular Res. 14(2), 166-172 (2006)

Arai, M., & Iwakura, M.
Protein Folding Elements (Japanese)
Seibutsubutsuri 45(3), 140-144 (2005)

Kuwajima, K., & Arai, M.
[Two views of protein folding: what is the universal view? ] (Japanese)
Tanpakushitsu Kakusan Koso 47(6), 657-662 (2002)

Kuwajima, K., & Arai, M.
The molten globule state: the physical picture and biological significance.
In Mechanisms of Protein Folding (Second Edition) (Pain, R.H. ed), (2000) Oxford University Press, New York.

Arai, M., & Kuwajima, K.
Role of the molten globule state in protein folding.
Adv. Protein Chem. 53, 209-282 (2000)


Books


Munehito Arai
Protein denaturation by solvent changes (denaturants, pH, and temperature)
In Protein Science" (Eds. Yuji Goto, Kunihiro Kuwajima, Katsuyuki Tanizaki), pp. 185-195 (2005) Kagaku-dojin

Arai, M., Ito, K., Maki, K., Ikura, T., Inobe, T., Kihara, H., Amemiya, Y., & Kuwajima, K.
Structural analysis of protein folding intermediates by solution X-ray scattering.
In Old and New Views of Protein Folding (Kuwajima, K. & Arai, M. eds) pp. 31-40 (1999) Elsevier Science, Amsterdam.

Kuwajima, K., Arai, M., Mizuguchi, M., Koshiba, T., & Nitta, K.
The folding mechanisms of α-lactalbumin and Ca2+-binding lysozyme.
In Old and New Views of Protein Folding (Kuwajima, K. & Arai, M. eds) pp. 135-144 (1999) Elsevier Science, Amsterdam.

Yoda, T., Saito, M., Arai, M., Horii, K., Tsumoto, K., Matsushima, M., Kumagai, I., Chaudhuri, T.K., & Kuwajima, K.
Kinetic folding reactions and molecular dynamics simulations of α-lactalbumin.
In Old and New Views of Protein Folding (Kuwajima, K., Arai, M. eds) pp. 155-162 (1999) Elsevier Science, Amsterdam.


Editor, Translation, etc.


"Principles of Physical Biochemistry" (Kensal E. Van Holde, et al.)
(translation for the Japanese version)
Eds. Masaru Tanokura & Fumio Arisaka
Translation by Masaru Tanokura, Fumio Arisaka, Munehito Arai, et al. (2003) Igaku-shuppan

"Old and New Views of Protein Folding"
Kuwajima, K., & Arai, M. (Editors)
Elsevier Science Ltd ; ISBN-10: 0444502912 ; (1999/11/30)


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