現在の構成員による研究成果

• Mori Y., Mizukami T., Suzuki, I., Fukazawa, S., Miki, K., Roder, H., Maki K. (2025)
  "Direct Comparison of the Structural Dynamics between Spontaneous and Ligand-induced Folding of Staphylococcal Nuclease."
  Protein Science accepted.
  
  

• Mori Y., Mizukami T., Segawa, S., Roder, H., Maki K. (2023)
  "Folding of Staphylococcal Nuclease Induced by Binding of Chemically Modified Substrate Analogues Sheds Light on Mechanisms of Coupled Folding/Binding Reactions."
  Biochemistry 62, (11) 1670-1678.
  
  

• Mizukami T., Furuzawa, S., Itoh, S.G., Segawa, S., Ikura, T., Ihara, K., Okumura, H., Roder, H., Maki K. (2020)
  "Energetics and kinetics of substrate analog-coupled staphylococcal nuclease folding revealed by a statistical mechanical approach."
  Proceedings of the National Academy of Sciences of the United States of America 117, (33) 19953-19962.
  
  

• Narita, K., Suzuki, N., Himi, N., Murayama, T., Nakagawa, T., Okabe, N., Nakamura-Maruyama, E., Hayashi, N., Sakamoto, I., Miyamoto, O., Kuba, K. (2019)
  "Effects of intravesicular loading of a Ca²⁺ chelator and depolymerization of actin fibers on neurotransmitter release in frog motor nerve terminals."
  Europian Journal of Neuroscience 50, (1) 1700-1711.
  
  

• Kouyama, T., Ihara, K., Maki K., Chan S.K. (2018)
  "Three-Step Isomerization of the Retinal Chromophore during the Anion Pumping Cycle of Halorhodopsin."
  Biochemistry 57, (41) 6013-6026.
  
  

• 水上琢也, 槇亙介 (2008)
  「統計力学モデルを用いて捉えなおす蛋白質の酸変性・フォールディング」
  日本物理学会誌, 73 (2) 91-96
  
  

• Mizukami, T., Sakuma, Y., Maki K. (2016)
  "Statistical Mechanical Model for pH-Induced Protein Folding: Application to Apomyoglobin."
  Journal of Physical Chemistry B 120 (34) 8970-8986.
  
  
• Chan, SK., Kawaguchi, H., Kubo, H., Murakami, M., Ihara, K., Maki, K., Kouyama, T. (2016)
  "Crystal Structure of the 11-cis Isomer of Pharaonis Halorhodopsin: Structural Constraints on Interconversions among Different Isomeric States."
  Biochemistry 55 (29) 4092-4104.
  
  

• Mizukami, T., Abe, Y., Maki K. (2015)
  "Evidence for a Shared Mechanism in the Formation of Urea-Induced Kinetic and Equilibrium Intermediates of Horse Apomyoglobin from Ultrarapid Mixing Experiments."
  PLoS One 10 (8) e0134238.
  
  

• Ishii, K., Terauchi, S., Murakami, R., Valencia, S. J,, Mutoh, R., Mino, H., Maki K., Arata, T., Ishiura, M. (2014)
  "Site-directed spin labeling-electron spin resonance mapping of the residues of cyanobacterial clock protein KaiA that are affected by KaiA-KaiC interaction."
  Genes to Cells 19 (10) 297-324.
  
  

• Mizukami, T., Xu, M., Cheng, H., Roder, H. and Maki, K. (2013)
  "Nonuniform chain collapse during early stages of staphylococcal nuclease folding detected by fluorescence resonance energy transfer and ultrarapid mixing methods."
  Protein Science 22 (10) 1336-1348.
  
  
• Mukaiyama, A., Nakamura, T., Makabe, K., Maki, K., Goto, Y. and Kuwajima, K. (2013)
  "The molten globule of beta2-microglobulin accumulated at pH 4 and its role in protein folding."
  Journal of Molecular Biology 425 (2) 273-291.
  
  
• Mukaiyama, A., Nakamura, T., Makabe, K., Maki, K., Goto, Y. and Kuwajima, K. (2013)
  "Native-state heterogeneity of beta2-microglobulin as revealed by kinetic folding and real-time NMR experiments."
  Journal of Molecular Biology 425 (2) 257-272.
  
  

• Tomoyori, K., Nakamura, T., Makabe, K., Maki, K., Saeki, K., Kuwajima, K. (2012)
  "Sequential four-state folding/unfolding of goat α-lactalbumin and its N-terminal variants."
  Proteins 80 (9) 2191-2206.
  
  

• Sasamori, E., Kato, M., Maki, K., Tagawa, Y. and Hanyu, Y. (2011)
  "Salt bridges in prion proteins are necessary for high-affinity binding to the monoclonal antibody T2."
  Biophysical Chemistry 156 (2-3) 140-145.
  
  

• Nakamura, T., Makabe, K., Tomoyori, K., Maki, K., Mukaiyama, A. and Kuwajima K. (2010)
  "Different folding pathways taken by highly homologous proteins, goat alpha-lactalbumin and canine milk lysozyme."
  Journal of Molecular Biology 396 (5) 1361-1378.
  
  

• 水上琢也, 槇亙介 (2008)
  「ストップト・フロー法を用いた速度論測定」
  蛋白質科学会アーカイブ, 3 e058.
  
  

• Tsukamoto, S., Yamashita, T., Yamada, Y., Fujiwara, K., Maki, K., Kuwajima, K., Matsumura, Y., Kihara, H., Tsuge, H. and Ikeguchi, M.. (2009)
  "Non-native alpha-helix formation is not necessary for folding of lipocalin: Comparison of burst-phase folding between tear lipocalin and beta-lactoglobulin."
  Proteins, 76 (1) 226-236.
  
  

• Kanzaki, T., Iizuka, R., Takahashi, K., Maki, K., Masuda, R., Sahlan, M., Yebene, H., Valpuesta, J. M., Oka, T., Furutani, M., Ishii, N., Kuwajima, K. and Yohda, M. (2008)
  "Sequential action of ATP dependent subunit conformational change and interaction between helical protrusions in the closure of the built-in lid of group II chaperonins."
  Journal of Biological Chemistry 283 (50) 34773 - 34784.
  
  
• Ishii, T., Murayama, Y., Katano, A., Maki, K., Kuwajima, K. and Sano, M. (2008)
  "Probing force-induced unfolding intermediates of a single staphylococcal nuclease molecule and the effect of ligand binding."
  Biochemical and Biophysical Research Communications. 375 (4) 586 - 591.
  
  
• Latypov, R. F., Maki, K., Cheng, H., Luck, S. D. and Roder, H. (2008)
  "Folding mechanism of reduced cytochrome c: Equilibrium and kinetic properties in the presence of carbon monoxide."
  Journal of Molecular Biology 383 (2) 437-453.
  
  
• Inobe, T., Takahashi, K., Maki, K., Enoki, S., Kamagata, K., Kadooka, A., Arai, M. and Kuwajima, K. (2008)
  "Asymmetry of the GroEL-GroES Complex under Physiological Conditions as Revealed by Small-angle X-ray Scattering."
  Biophysical Journal, 94 (4) 1392-1402.
  
  

• Maki, K., Cheng, H., Dolgikh, D. A. and Roder, H. (2007)
  "Folding Kinetics of Staphylococcal Nuclease Studied by Tryptophan Engineering and Rapid Mixing Methods."
  Journal of Molecular Biology, 368 (1) 244-255.
  
  
• Nakatani, H., Maki, K., Saeki, K., Aizawa, T., Demura, M., Kawano, K., Tomoda, S., Kuwajima, K. (2007)
  "Equilibrium and Kinetics of the Folding and Unfolding of Canine Milk Lysozyme."
  Biochemistry, 46 (17) 5238-5251.
  
  
• Kato, A., Maki, K., Ebina, T., Kuwajima, K., Soda, K. and Kuroda, Y. (2007)
  "Mutational analysis of protein solubility enhancement using short peptide tags."
  Biopolymers, 85(1) 12-18.
  
  

• Aprtri, A. C., Maki, K., Roder, H. and Surewicz, W. K. (2006)
  "Early intermediate in human prion protein folding as evidenced ultrarapid mixing experiments."
  Journal of American Chemical Society, 128(35) 11673-11678.
  
  
• Roder, H., Maki, K., and Cheng, H. (2006)
  "Early events in protein folding explored by rapid mixing methods."
  Chemical Reviews, 106(5) 1836-1861.
  
  
• Iwakura, M., Maki, K., Takahashi, T., Takenawa, T., Yokota, A., Katayanagi, K., Kamiyama, T., and Gekko, K. (2006)
  "Evolutional design of a hyper-active cysteine-and methionine-free mutant of Escherichia coli dihydrofolate reductase."
  Journal of Biological Chemistry, 281(19) 13234-13246.
  
  
• Enoki, S., Maki, K., Inobe, T., Takahashi, K., Kamagata, K., Oroguchi, T., Nakatani, H., Tomoyori, K. and Kuwajima, K. (2006)
  "The equilibrium unfolding intermediate observed at pH 4 and its relationship with the kinetic folding intermediates in Green fluorescent protein."
  Journal of Molecular Biology, 361(5) 969-982.
  
  

• 鈴木直哉. (2006)
  第６章　「共焦点レーザー走査蛍光顕微鏡によるイメージング」
  「蛍光分光とイメージングの手法」　御橋廣眞　編,　日本分光学会　測定法シリーズ 42, 学会出版センター, 211-237.

• Nakao, M., Maki, K., Arai, M., Koshiba, T., Nitta, K. and Kuwajima, K. (2005)
  "Characterization of kinetic folding intermediates of recombinant canine milk lysozyme by stopped-flow circular dichroism."
  Biochemistry, 44(17) 6685-6692.
  
  
• Iizuka, R., Yoshida, T., Ishii, N., Zako, T., Takahashi, K., Maki, K., Inobe, T., Kuwajima K. and Yohda, M. (2005)
  "Characterization of archeal group II chaperonin-ADP-metal fluoride complexes: Implications that group II chaperonins operate as a "two-stroke engine."
  Journal of Biological Chemistry, 280(48) 40375-40383.
  
  
• Maki, K., Kamagata, K. and Kuwajima, K. (2005)
  "Equilibrium and kinetically observed molten globule states."
  Protein Folding Handbook (Buchner, J. and Kiefhaber, T. eds., WILEY-VCH), 852-879.
  
  
• Roder, H., Maki, K., Latypov, R. F., Cheng, H. and Shastry, M. C. R. (2005)
  "Early events in protein folding explored by rapid mixing methods."
  Protein Folding Handbook (Buchner, J. and Kiefhaber, T. eds., WILEY-VCH), 491-535.
  
  

• Maki, K., Cheng, H., Dolgikh, D. A., Shastry, M. C. R. and Roder, H. (2004)
  "Early events during folding of wild type staphylococcal nuclease and a single-tryptophan variant studied by ultrarapid mixing."
  Journal of Molecular Biology, 338(2) 383-400.
  
  
• Welker, E., Maki, K., Shastry, M. C. R., Juminaga, D., Bhat, R., Roder, H. and Scheraga, H. A. (2004)
  "Ultra-rapid mixing experiments shed new light on the characteristics of the initial conformational ensemble during the folding of ribonuclease A."
  Proceedings of the National Academy of Sciences of the United States of America, 101(51), 17681-17686.
  
  
• Roder, H., Maki, K., Cheng, H. and Shastry, M. C. R. (2004)
  "Rapid mixing methods for exploring the kinetics of protein folding."
  Methods, 34(1), 15-27.
  
  
• Enoki, S., Saeki, K., Maki, K. and Kuwajima, K. (2004)
  "Acid denaturation and refolding of green fluorescent protein."
  Biochemistry, 43(44), 14238-14248.
  
  
• Akhtar, M. W., Srinivas, V., Raman, B., Ramakrishna, T., Inobe, T., Maki, K., Arai, M., Kuwajima, K., and Rao, C. M. (2004)
  "Oligomeric Hsp33 with enhanced chaperone activity: gel filtration, cross-linking, and small angle x-ray scattering analysis."
  Journal of Biological Chemistry, 279(53), 55760-55769.
  
  

• Zhu, Y., Alonso, D. O. V., Maki, K., Huang, C-Y, Lahr, S. J., Daggett, V., Roder, H., DeGrado, W. F. and Gai, F. (2003)
  "Ultrafast Folding of α₃D, A De Novo Designed Three-Helix Bundle Protein."
  Proceedings of the National Academy of Sciences of the United States of America, 100(26), 15486-15491.
  
  
• Arai, M.#, Maki, K.#, Takahashi, H. and Iwakura, M. (2003)
  "Testing the Relationship Between Foldability and the Early Folding Events of Dihydrofolate Reductase from Escherichia coli."
  Journal of Molecular Biology, 328(1), 273-288. (#M. A. and K. M. equally contributed to the paper.)
  
  
• Arai, M., Inobe, T., Maki, K., Ikura, T., Kihara, H., Amemiya, Y., and Kuwajima, K. (2003)
  "Denaturation and Reassembly of Chaperonin GroEL Studied by Solution X-ray Scattering."
  Protein Science, 12(4), 672-680.
  
  

• Teilum, K., Maki, K., Kragelund, B. B., Poulsen, F. M., and Roder, H. (2002)
  "Early kinetic intermediate in the folding of acyl-CoA binding protein detected by fluorescence labeling and ultrarapid mixing."
  Proceedings of the National Academy of Sciences of the United States of America, 99(15), 9807-9812.
  
  
• Arai, M., Ito, K., Inobe, T., Nakao, M., Maki, K., Kamagata, K., Kihara, H., Amemiya, Y. and Kuwajima, K. (2002)
  "Fast Compaction of α-Lactalbumin During Folding Studied by Stopped-flow X-ray Scattering."
  Journal of Molecular Biology, 321(1), 121-132.
  
  
• Kuwajima, K., Arai, M., Inobe, T., Ito, K., Nakao, M., Maki, K., Kamagata, K., Kihara, H. and Amemiya, Y. (2002)
  "The use of the time-resolved X-ray solution scattering for studies of globular proteins."
  Spectroscopy, 16(3-4), 127-138.

• 槙 亙介、巖倉正寛. (2001)
  「円順列変異(サーキュラーパーミューテーション)解析からわかるタンパク質立体構造単位」
  日本生化学会機関誌・生化学, 73(1), 42-46.

• 木島博正、村瀬雅樹、鈴木直哉. (2001)
  「シナプスの短期可塑性と残存Ca²⁺仮説」
  脳の科学, 23(8), 691-695.

• 鈴木直哉、河西春郎. (2001)
  「伝達物質放出におけるCa²⁺の作用とCa²⁺緩衝能による調節」
  脳の科学, 23(4), 287–295.

• Iwakura, M., Nakamura, T., Yamane, C. and Maki, K. (2000)
  "Systematic circular permutation of and entire protein reveals essential folding elements."
  Nature Structural Biology, 7 (7), 580-585.
  

• Suzuki, S., Osanai, M., Murase, M., Suzuki, N., Ito, K., Shirasaki, T., Narita, K., Ohnuma, K., Kuba, K. and Kijima, H. (2000)
  "Ca²⁺ dynamics at the frog motor nerve terminal."
  Pflugers Arch - Eur. J. Physiol., 440, 351-365.
  

• Ogawa, S., Takeuchi, T., Ohnuma, K., Suzuki, N., Miwa, A., Kawai, N. and Kijima, H. (2000)
  "Facilitation of neurotranmitter release at the spiny lobster neuromuscular junction."
  Neuroscience Research, 37, 33-48.
  

• 槙 亙介. (2000)
  「感染性及び遺伝性プリオン病の発症機構に於ける関連性」
  日本薬学会・ファルマシア, 36(10), 885-886.

• Maki, K., Ikura, T., Hayano, H., Takahashi, N. and Kuwajima, K. (1999)
  "Effects of Proline Mutations on the Folding of Staphylococcal nuclease."
  Biochemistry, 38(7), 2213-2223.
  
  
• Maki, K., Ikura, T., Mohs, A., and Kuwajima, K. (1999)
  "Equilibrium and kinetics of foldng of staphylococcal nuclease."
  Old and New Views of Protein Folding (Elsevier Science, Amsterdam), 271-278.
  
  
• Arai, M., Ito, K., Maki, K., Ikura, T., Inobe, T., Kihara, H., Amemiya, Y. and Kuwajima, K. (1999)
  "Structural analysis of protein folding intermediates by solution X-ray scattering."
  Old and New Views of Protein Folding (Elsevier Science, Amsterdam), 31-40.
  

• Ohnuma, K., Kazawa, T., Ogawa, S., Suzuki, N., Miwa, A., and Kijima, H. (1999)
  "Cooperative Ca²⁺ removal from presynaptic terminals of the spiny lobster neuromuscular junction."
  Biophysical Journal, 76, 1819-1834.