Hi, I am Kazufumi Takano, My LiveDNA is 81.3093
 
   
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Dr. Kazufumi Takano
 
Highest Degree: Ph.D. in Environmental Science from Kyoto Prefectural University of Medicine, Kyoto, Japan
 
Institute: Kyoto Prefectural University, Japan
 
Area of Interest: Environmental Sciences
  •   Atmospheric Science
  •   Life Science
  •   Molecular Biology
  •   Biotechnology
 
URL: http://livedna.org/81.3093
 
My SELECTED Publications
1:   Adachi, H., A. Niino, K. Takano, H. Matsumura and S. Murakami et al., 2005. Temperature-screening system for determining protein crystallization conditions. Jpn. J. Appl. Phys., 44: 4080-4083.
CrossRef  |  
2:   Adachi, H., A. Niino, S. Murakami, K. Takano and H. Matsumura et al., 2005. Protein crystallization by combining laser irradiation and solution stirring techniques. Jpn. J. Appl. Phys., 44: 1365-1366.
CrossRef  |  
3:   Adachi, H., A. Niino, T. Kinoshita, M. Warizaya, R. Maruki et al., 2006. Solution-stirring method improves crystal quality of human triosephosphate isomerase. J. Biosci. Bioeng., 101: 83-86.
PubMed  |  
4:   Adachi, H., H. Matsumura, A. Niino, K. Takano and T. Kinoshita et al., 2004. Improving the quality of protein crystals using a stirring crystallization. Jpn. J. Appl. Phys., 43: L522-L525.
Direct Link  |  
5:   Adachi, H., H. Matsumura, K. Takano, A. Niino, T. Inoue, Y. Mori and T. Sasaki, 2004. Two-liquid hanging-drop vapor-diffusion technique of protein crystallization. Jpn. J. Appl. Phys., 43: L79-L81.
CrossRef  |  Direct Link  |  
6:   Adachi, H., H. Matsumura, T. Inoue, A. Niino and K. Takano et al., 2005. Semiautomatic protein crystallization system featuring crystallization solution preparation function. Jpn. J. Appl. Phys., 44: 6302-6303.
CrossRef  |  
7:   Adachi, H., K. Takano, H. Matsumura, T. Inoue, Y. Mori and T. Sasaki, 2004. Protein crystal growth with a two-liquid system and stirring solution. J. Synchrotron Rad., 11: 121-124.
PubMed  |  
8:   Adachi, H., K. Takano, M. Yoshimura, Y. Mori and T. Sasaki, 2003. Application of a stirring method to micro-scale and vapor diffusion protein crystallization. Jpn. J. Appl. Phys., 42: L314-L315.
CrossRef  |  Direct Link  |  
9:   Adachi, H., K. Takano, Y. Hosokawa, T. Inoue and Y. Mori et al., 2003. Laser irradiated growth of protein crystal. Jpn. J. Appl. Phys., 42: L798-L800.
CrossRef  |  Direct Link  |  
10:   Adachi, H., A. Niino, H. Matsumura, K. Takano, T. Inoue, Y. Mori and T. Sasaki, 2004. Novel and simple screening techniques of protein crystallization by vapor diffusion rate control. Jpn. J. Appl. Phys., 43: 6264-6267.
CrossRef  |  
11:   Adachi, H., A. Niino, H. Matsumura, K. Takano, T. Inoue, Y. Mori and T. Sasaki, 2004. Pre-stirring promotes nucleation of protein crystals. Jpn. J. Appl. Phys., 43: L243-L246.
CrossRef  |  Direct Link  |  
12:   Adachi, H., A. Niino, H. Matsumura, K. Takano, T. Kinoshita and M. Warizaya et al., 2004. Generation of protein crystals using a solution-stirring technique. Jpn. J. Appl. Phys., 43: L762-L764.
CrossRef  |  Direct Link  |  
13:   Adachi, H., H. Matsumura, K. Takano, A. Niino, T. Inoue, M. Yoshimura, Y. Mori and T. Sasaki, 2003. New practical technique for protein crystallization with floating and stirring methods. Jpn. J. Appl. Phys., 42: L1161-L1163.
Direct Link  |  
14:   Adachi, H., K. Takano, A. Niino, H. Matsumura and T. Kinoshita et al., 2005. Solution stirring initiates nucleation and improves the quality of adenosine deaminase crystals. Acta. Cryst., D61: 759-762.
PubMed  |  
15:   Adachi, H., K. Takano, H. Matsumura, A. Niino and T. Ishizu et al., 2004. A semiautomatic protein crystallization system with preventing evaporation of drops and surface sensor of solution. Jpn. J. Appl. Phys., 43: L76-L78.
CrossRef  |  Direct Link  |  
16:   Adachi, H., K. Takano, M. Morikawa, S. Kanaya, M. Yoshimura, Y. Mori and T. Sasaki, 2003. Application of a two-liquid system to sitting-drop vapor diffusion protein crystallization. Acta Cryst., D59: 194-196.
CrossRef  |  
17:   Adachi, H., K. Takano, M. Yoshimura, Y. Mori and T. Sasaki, 2003. Effective protein crystallization using crystal hysteresis. Jpn. J. Appl. Phys., 42: L384-L385.
PubMed  |  
18:   Adachi, H., S. Murakami, A. Niino, H. Matsumura and K. Takano et al., 2004. Membrane protein crystallization using laser irradiation. Jpn. J. Appl. Phys., 43: L1376-L1378.
CrossRef  |  Direct Link  |  
19:   Adachi, M., T. Ohhara, K. Kurihara, T. Tamada and E. Honjo et al., 2009. Structure of HIV-1 protease in complex with potent inhibitor KNI-272 determined by high resolution x-ray and neutron crystallography. Proc. Natl. Acad. Sci., 106: 4641-4646.
CrossRef  |  
20:   Angkawidjaja, C., K. Kuwahara, K. Omori, Y. Koga, K. Takano and S. Kanaya, 2006. Extracellular secretion of E. coli alkaline phosphatase with a C-terminal tag by type I secretion system: Purification and biochemical characterization. Protein Eng. Des. Sel., 19: 337-343.
CrossRef  |  
21:   Angkawidjaja, C., A. Paul, Y. Koga, K. Takano and S. Kanaya, 2005. Importance of a repetitive nine-residue sequence motif for intracellular stability and functional structure of a family I.3 lipase. FEBS Let., 579: 4707-4712.
CrossRef  |  
22:   Angkawidjaja, C., D.J. You, H. Matsumura, K. Kuwahara, Y. Koga, K. Takano and S. Kanaya, 2007. Crystal structure of a family I.3 lipase from Pseudomonas sp. mIS38 in a closed conformation. FEBS Let., 581: 5060-5064.
PubMed  |  
23:   Angkawidjaja, C., D.J. You, H. Matsumura, Y. Koga, K. Takano and S. Kanaya, 2007. Extracellular overproduction and preliminary crystallographic analysis of a family I.3 lipase. Acta Cryst., F63: 187-189.
PubMed  |  
24:   Angkawidjaja, C., H. Matsumura, Y. Koga, K. Takano and S. Kanaya, 2010. X-ray crystallographic and MD simulation studies on the interfacial activation mechanism of a family I.3 lipase with two lids. J. Mol. Biol., 400: 82-95.
PubMed  |  
25:   Budiman, C., C. Angkawidjaja, H. Motoike, Y. Koga, K. Takano and S. Kanaya, 2011. Crystal structure of N-domain of FKBP22 from Shewanella sp. SIB1: Dimer dissociation by disruption of Val-Leu knot. Protein Sci., 20: 1755-1764.
CrossRef  |  PubMed  |  Direct Link  |  
26:   Budiman, C., K. Bando, C. Angkawidjaja, Y. Koga, K. Takano and S. Kanaya, 2009. Engineering of monomeric FK506-binding protein 22 with peptidyl prolyl cis-trans isomerase. FEBS J., 276: 4091-4101.
CrossRef  |  PubMed  |  Direct Link  |  
27:   Chon, H., H. Matsumura, S. Shimizu, N. Maeda, Y. Koga, K. Takano and S. Kanaya, 2005. Overproduction and preliminary crystallographic study of a human kynurenine aminotransferase II homologue from Pyrococcus horikoshii OT3. Acta Cryst., F61: 319-321.
CrossRef  |  
28:   Chon, H., H. Matsumura, Y. Koga, K. Takano and S. Kanaya, 2006. Crystal structure and structure-based mutational analyses of RNase HIII from Bacillus stearothermophilus: A new type 2 RNase H with TBP-like substrate-binding domain at the N-terminus. J. Mol. Biol., 356: 165-178.
PubMed  |  
29:   Chon, H., R. Nakano, N. Ohtani, M. Haruki, K. Takano, M. Morikawa and S. Kanaya, 2004. Gene cloning and biochemical characterizations of a thermostable ribonuclease hiii from Bacillus stearothermophilus. Biosci. Biotechnol. Biochem., 68: 2138-2147.
CrossRef  |  
30:   Chon, H., T. Tadokoro, N. Ohtani, Y. Koga, K. Takano and S. Kanaya, 2006. Identification of RNase HII from psychrotrophic bacterium, Shewanella sp. SIB1 as a high-activity type RNase H. FEBS J., 273: 2264-2275.
PubMed  |  
31:   Chon, H., H. Matsumura, Y. Koga, K. Takano and S., Kanaya, 2005. Crystal structure of a human kynurenine aminotransferase II homologue from Pyrococcus horikoshii OT3 at 2.20 Å resolution. Proteins, 61: 685-688.
PubMed  |  
32:   Chon, H., H. Matsumura, Y. Koga, K. Takano and S. Kanaya, 2005. Crystallization and preliminary x-ray diffraction study of thermostable RNase HIII from Bacillus stearothermophilus. Acta Cryst., F61: 293-295.
CrossRef  |  
33:   Cornista, J., S. Ikeuchi, M. Haruki, A. Kohara, K. Takano, M. Morikawa and S. Kanaya, 2004. Cleavage of various peptides with pitrilysin from escherichia coli: kinetic analyses using β-endorphin and its derivatives. Biosci. Biotechnol. Biochem., 68: 2128-2137.
PubMed  |  
34:   Cornista, J., Y. Koga, K. Takano and S. Kanaya, 2006. Amyloidogenecity and pitrilysin sensitivity of a lysine-free derivative of amyloid β-peptide cleaved from a recombinant fusion protein. J. Biotechnol., 122: 186-197.
PubMed  |  
35:   Dong, H., A. Mukaiyama, T. Tadokoro, Y. Koga, K. Takano and S. Kanaya, 2008. Hydrophobic effect on the stability and folding of a Hyperthermophilic protein. J. Mol. Biol., 378: 264-272.
PubMed  |  
36:   Foophow, T., S. Tanaka, Y. Koga, K. Takano and S. Kanaya, 2010. Subtilisin-like serine protease from Hyperthermophilic archaeon Thermococcus kodakaraensis with N- and C-terminal propeptides. Protein Eng. Des. Sel., 23: 347-355.
CrossRef  |  
37:   Foophow, T., S. Tanaka, C. Angkawidjaja, Y. Koga, K. Takano and S. Kanaya, 2010. Crystal structure of a subtilisin homologue, Tk-SP, from Thermococcus kodakaraensis: Requirement of a C-terminal beta-jelly roll domain for hyperstability. J. Mol. Biol., 400: 865-877.
PubMed  |  
38:   Funahashi, J., K. Takano, K. Ogasahara, Y. Yamagata and K. Yutani, 1996. The Structure, Stability and Folding Process of Amyloidogenic Mutant Human Lysozyme. J. Biochem., 120: 1216-1223.
PubMed  |  
39:   Funahashi, J., K. Takano, Y. Yamagata and K. Yutani, 2002. Positive contribution of hydration structure on the surface of human lysozyme to the conformational stability. J. Biol. Chem., 277: 21792-21800.
CrossRef  |  
40:   Funahashi, J., K. Takano, Y. Yamagata and K. Yutani, 2000. Role of surface hydrophobic residues in the conformational stability of human lysozyme at three different positions. Biochemistry, 39: 14448-14456.
PubMed  |  
41:   Funahashi, J., K. Takano and K. Yutani, 2001. Are the parameters of various stabilization factors estimated from mutant human lysozymes compatible with other proteins? Protein Engng., 14: 127-134.
PubMed  |  
42:   Funahashi, J., K. Takano, Y. Yamagata and K. Yutani, 1999. Contribution of Amino Acid Substitutions at Two Different Interior Positions to the Conformational Stability of Human Lysozyme. Protein Eng., 12: 841-850.
PubMed  |  
43:   Goda, S., K. Takano, Y. Yamagata, R. Nagata and H. Akutsu et al., 2000. Amyloid Protofilament Formation of Hen Egg Lysozyme in Highly Concentrated Ethanol Solution. Protein Sci., 9: 381-387.
PubMed  |  
44:   Goda, S., K. Takano, Y. Yamagata, S. Maki, K. Namba and K. Yutani, 2002. Elongation in a β-structure promotes amyloid-like fibril formation of human lysozyme. J. Biochem., 132: 655-661.
PubMed  |  
45:   Haruki, M., M. Tanaka, T. Motegi, T. Tadokoro, Y. Koga, K. Takano and S. Kanaya, 2007. Structural and thermodynamic analyses of Escherichia coli ribonuclease HI variant with quintuple thermostabilizing mutations. FEBS J., 274: 5815-5825.
PubMed  |  
46:   Hasenaka, H., S. Sugiyama, M. Hirose, N. Shimizu and T. Kitatani et al., 2009. Femtosecond laser processing of protein crystals grown in agarose gel. J. Cryst. Growth, 312: 73-78.
CrossRef  |  
47:   Hirano, S., M. Morikawa, K. Takano, T. Imanaka and S. Kanaya, 2007. Gentisate 1,2-dioxygenase from Xanthobacter polyaromaticivorans 127W. Biosci. Biotechnol. Biochem., 71: 192-199.
Direct Link  |  
48:   Hirano, S., M. Haruki, K. Takano, T. Imanaka, M. Morikawa and S. Kanaya, 2006. Gene cloning and in vivo characterization of a dibenzothiophene dioxygenase from Xanthobacter polyaromaticivorans. Appl. Micobiol. Biotechnol., 69: 672-681.
PubMed  |  
49:   Iefuji, N., R. Murai, M. Maruyama, Y. Takahashi and S. Sugiyama et al., 2011. Laser-induced nucleation in protein crystallization: Local increase in protein concentration induced by femtosecond laser irradiation. J. Cryst. Growth, 318: 741-744.
Direct Link  |  
50:   Jongruja, N., D.J. You, E. Kanaya, Y. Koga, K. Takano and S. Kanaya, 2010. Importance of an N-terminal hybrid binding domain for substrate binding and Mg2+-dependent activity of Rnase HI from Thermotoga maritima. FEBS J., 277: 4474-4489.
CrossRef  |  
51:   Kakinouchi, K., T. Nakamura, T. Tamada, H. Adachi and S. Sugiyama et al., 2010. Growth of large protein crystals by a large-scale hanging drop method. J. Appl. Cryst., 43: 937-939.
CrossRef  |  
52:   Kakinouchi, K., H. Adachi, H. Matsumura, T. Inoue and S. Murakami, 2006. Effect of ultrasonic irradiation on protein crystallization. J. Cryst. Growth, 292: 437-440.
CrossRef  |  
53:   Kanaya, E., T. Sakabe, N. Nguyen, S. Koikeda, Y. Koga, K. Takano and S. Kanaya, 2010. Cloning of the RNase H genes from a metagenomic DNA library: Identification of a new type 1 RNase H without a typical active-site motif. J. Appl. Microbiol., 109: 974-983.
CrossRef  |  PubMed  |  
54:   Kashii, M., H. Kitano, Y. Hosokawa, H. Adachi and Y. Mori et al., 2005. Femtosecond laser processing of protein crystals in crystallization drop. Jpn. J. Appl. Phys., 44: L873-L875.
CrossRef  |  
55:   Kashii, M., R. Fujisawa, H. Adachi, Y. Mori and T. Sasaki et al., 2006. Application of femtosecond laser ablation for detaching grown protein crystals from a glass capillary tube. J. Biosci. Bioeng., 102: 372-374.
PubMed  |  
56:   Kashii, M., Y. Hosokawa, H. Kitano, H. Adachi and Y. Mori et al., 2007. Femtosecond laser-induced cleaving of protein crystal in water solution. Appl. Sur. Sci., 253: 6447-6450.
CrossRef  |  
57:   Katsumi, R., Y. Koga, D.J. You, H. Matsumura, K. Takano and S. Kanaya, 2007. Crystallization and preliminary x-ray diffraction study of glycerol kinase from hyperthermophilic archaeon Thermococcus kodakaraensis. Acta Cryst., F63: 126-129.
PubMed  |  
58:   Kazufumi, T., K. Ogasahara, H. Kaneda, Y. Yamagata and S. Fujii et al., 1995. Contribution of Hydrophobic Residues to the Stability of Human Lysozyme: Calorimetric Studies and X-ray Structural Analysis of the Five Isoleucine to Valine Mutants. J. Mol. Biol. 254: 62-76.
PubMed  |  
59:   Kim, J.J., H.M. Jin, H.J. Lee, C.O. Jeon and E. Kanaya et al., 2010. Flavobacterium banpakuense sp. nov. Isolated from leaf-and-branch compost. Int. J. Syst. Evol. Microbiol., 61: 1595-1600.
PubMed  |  
60:   Kinoshita, T., I. Nakanishi, T. Terasaka, M. Kuno and N. Seki et al., 2005. Structural basis of compound recognition by adenosine deaminase. Biochemistry, 44: 10562-10569.
PubMed  |  
61:   Kitano, H., H. Adachi, A. Murakami, H. Matsumura and K. Takano et al., 2004. New approach to improve x-ray diffraction pattern of protein crystal using uv-laser ablative processing. Jpn. J. Appl. Phys., 43: L297-L299.
Direct Link  |  
62:   Kitano, H., H. Adachi, A. Sato, A. Murakami and H. Matsumura et al., 2004. Application of uv-laser ablation to detaching protein crystal from growth vessel. Jpn. J. Appl. Phys., 43: L1271-L1274.
Direct Link  |  
63:   Kitano, H., S. Murakami, H. Adachi, H. Matsumura and K. Takano et al., 2005. Processing of membrane protein crystal using UV laser irradiation. J. Biosci. Bioeng., 100: 50-53.
PubMed  |  
64:   Kitano, H., H. Adachi, A. Murakami, H. Matsumura, K. Takano, T. Inoue, Y. Mori, S. Owa and T. Sasaki, 2004. Protein crystal processing using a deep-uv laser. Jpn. J. Appl. Phys., 43: L73-L75.
Direct Link  |  
65:   Kitano, H., H. Matsumura, H. Adachi, S. Murakami and K. Takano et al., 2005. Protein cryocrystallography using laser-processed crystal. Jpn. J. Appl. Phys., 44: L54-L56.
CrossRef  |  Direct Link  |  
66:   Kitatani, T., H. Adachi, S. Sugiyama, H. Matsumura and R. Murai et al., 2009. A manipulating tool for protein microcrystals in solution using adhesive materials. Jpn. J. Appl. Phys., Vol. 48 http://jjap.jsap.jp/link?JJAP/48/118001/pdf.
67:   Kitatani, T., S. Sugiyama, H. Matsumura, H. Adachi and H. Yoshikawa et al., 2008. New technique of manipulating a protein crystal using adhesive material. Appl. Phys. Express, Vol. 1 .
Direct Link  |  
68:   Kitatani, T., H. Adachi, S. Sugiyama, H. Matsumura and R. Murai et al., 2008. Evaluation and improvement of a technique to manipulate protein crystals in solution. Jpn. J. Appl. Phys., 47: 8995-8997.
CrossRef  |  
69:   Koga, Y., R. Katsumi, D.J. You, H. Matsumura, K. Takano and S. Kanaya, 2008. Crystal Structure of Highly Thermostable glycerol kinase from a hyperthermophilic archaeon in a dimeric form. FEBS J., 275: 2632-2643.
PubMed  |  
70:   Kunihiro, N., M. Haruki, K. Takano, M. Morikawa and S. Kanaya, 2005. Isolation and characterization of rhodococcus sp. Tmp2 and t12 that degrade 2,6,10,14-tetramethylpentadecane (pristane) at moderately low temperatures. J. Biotechnol., 115: 129-136.
CrossRef  |  
71:   Kuwahara, K., C. Angkawidjaja, H. Matsumura, Y. Koga, K. Takano and S. Kanaya, 2008. Importance of the Ca2+-binding sites in the N-catalytic domain of a family I.3 lipase for activity and stability. Protein Eng. Des. Sel., 21: 737-744.
PubMed  |  
72:   Kuwahara, K., C. Angkawidjaja, Y. Koga, K. Takano and S. Kanaya, 2011. Importance of an extreme C-terminal motif of a family I.3 lipase for stability. Protein Eng. Des. Sel., 24: 411-418.
CrossRef  |  
73:   Maki, S., R. Murai, H. Yoshikawa, T. Kitatani and S. Nakata et al., 2008. Protein crystallization in a 100 nl solution with new stirring equipment. J. Synchrotron Rad., 15: 269-272.
CrossRef  |  
74:   Maruyama, M., N. Shimizu, S. Sugiyama, Y. Takahashi and H. Adachi et al., 2010. Estimated effects of silicone glue on protein crystal growth. J. Cryst. Growth, 312: 2771-2774.
Direct Link  |  
75:   Matsumura, H., K. Kakinouchi, T. Nakamura, S. Sugiyama and M. Maruyama et al., 2011. Growth of Protein Crystals by Syringe-Type Top-Seeded Solution Growth. Cryst. Growth Des., 11: 1486-1492.
76:   Matsumura, H., M. Adachi, S. Sugiyama, S. Okada and M. Yamakami et al., 2008. Crystallization and preliminary neutron diffraction studies of HIV-1 protease cocrystallized with inhibitor KNI-272. Acta Cryst., F64: 1003-1006.
CrossRef  |  
77:   Matsumura, H., S. Sugiyama, M. Hirose, K. Kakinouchi and M. Maruyama et al., 2010. Approach for growth of high-quality and large protein crystals. J. Synchrotron Rad., 18: 16-19.
CrossRef  |  
78:   Mima, M., C. Kawai, K. Paku, K. Tomoo and T. Ishida, 2008. Crystallization and preliminary x-ray crystallographic analysis of Ca2+-free primary Ca2+-sensor of Na+/Ca2+ exchanger. Acta Cryst., F64: 1125-1127.
CrossRef  |  
79:   Miyashita, S., T. Tadokoro, C. Angkawidjaja, D.J. You, Y. Koga, K. Takano and S. Kanaya, 2011. Identification of the substrate binding site in the N-terminal TBP-like domain of RNase H3. FEBS Let., 585: 2313-2327.
PubMed  |  
80:   Morikawa, M., S. Kagihiro, M. Haruki, K. Takano, S. Branda, R. Kolter and S. Kanaya, 2006. Biofilm formation by Bacillus subtilis that produces and gamma;-polyglutamate. Microbiol.-SGM, 152: 2801-2807.
PubMed  |  
81:   Mukaiyama, A. and K. Takano, 2009. Slow unfolding of monomeric proteins from hyperthermophiles with reversible unfolding. Int. J. Mol. Sci., 10: 1369-1385.
CrossRef  |  
82:   Mukaiyama, A., K. Takano, M. Haruki, M. Morikawa and S. Kanaya, 2004. Kinetically robust monomeric protein from a hyperthermophile. Biochemistry, 43: 13859-13866.
PubMed  |  
83:   Mukaiyama, A., M. Haruki, M. Ota, Y. Koga, K. Takano and S. Kanaya, 2006. A hyperthermophilic protein acquires function at the cost of stability. Biochemistry, 45: 12673-12679.
CrossRef  |  
84:   Mukaiyama, A., Y. Koga, K. Takano and S. Kanaya, 2008. Osmolyte effect on the stability and folding of a hyperthermophilic protein. Proteins, 71: 110-118.
PubMed  |  
85:   Murai, R., H.Y. Yoshikawa, Y. Takahashi, M. Maruyama and S. Sugiyama et al., 2010. Enhancement of femtosecond laser-induced nucleation of protein in a gel solution. Appl. Phys. Let., 96: 043702-043702.
CrossRef  |  
86:   Murai, R., H. Yoshikawa, H. Kawahara, S. Maki and S. Sugiyama et al., 2008. Effect of solution flow produced by rotary shaker on protein crystallization. J. Cryst. Growth, 310: 2168-2172.
CrossRef  |  
87:   Murai, R., H.Y. Yoshikawa, H. Hasenaka, Y. Takahashi and M. Maruyama et al., 2011. Influence of energy and wavelength on femtosecond laser-induced nucleation of protein. Chem. Phys. Let., 510: 139-142.
Direct Link  |  
88:   Murai, R., S. Nakata, M. Kashii, H. Adachi and A. Niino et al., 2006. Cooling-rate screening system for determining protein crystal growth conditions. J. Cryst. Growth, 292: 433-436.
CrossRef  |  
89:   Murakami, A., H. Kitano, H. Adachi, H. Matsumura and K. Takano, 2004. Universal processing technique for protein crystals using a pulsed uv laser. Jpn. J. Appl. Phys., 43: L873-L876.
CrossRef  |  Direct Link  |  
90:   Murakami, S., M. Kashii, H. Kitano, H. Adachi and K. Takano et al., 2005. Effect of laser irradiation on enzyme activity. Jpn. J. Appl. Phys., 44: 8216-8218.
CrossRef  |  
91:   Nagashima, K., M. Abe, S. Morita, N. Oyabu and K. Kobayashi et al., 2010. Molecular resolution investigation of tetragonal lysozyme (110) face in liquid by FM-AFM. J. Vac. Sci. Technol., B28: C4C11-C4C14.
CrossRef  |  
92:   Nick, P.C., B.M.H. Despointes, H. Fu, K. Takano, J.M. Scholtz and G.R. Grimsley, 2010. Urea denatured state ensembles contain extensive secondary structure that is increased in hydrophobic proteins. Protein Sci., 19: 929-943.
PubMed  |  
93:   Niino, A., H. Adachi, K. Takano, H. Matsumura and T. Kinoshita et al., 2004. Control of protein crystal nucleation and growth using stirring solution. Jpn. J. Appl. Phys., 43: L1442-L1444.
Direct Link  |  
94:   Nomura, Y., S. Sugiyama, T. Sakamoto, S. Miyakawa and H. Adachi et al., 2010. Conformational plasticity of RNA for target recognition as revealed by the 2.15 A crystal structure of a human IgG-aptamer complex. Nucleic. Acids Res., 38: 7822-7829.
CrossRef  |  
95:   Numata, T., Y. Ikeuchi, S. Fukai, H. Adachi and H. Matsumura et al., 2006. Crystallization and preliminary X-ray analysis of the tRNA thiolation enzyme MnmA from Escherichia coli complexed with tRNAGlu. Acta. Cryst., F62: 368-371.
PubMed  |  
96:   Ohnishi S., and K. Takano, 2004. Amyloidfibrils from the viewpoint of protein folding. Cell. Mol. Life Sci., 61: 511-524.
PubMed  |  
97:   Okada, J., T. Okamoto, A. Mukaiyama, T. Tadokoro and D.J. You et al., 2010. Evolution and thermodynamics of slow unfolding of hyperstable monomeric proteins. BMC Evol. Biol., 10: 207-207.
PubMed  |  
98:   Pulido, M., Y. Koga, K. Takano and S. Kanaya, 2007. Directed evolution of Tk-subtilisin from Hyperthermophilic archaeon: Identification of single amino acid substitution responsible for low-temperature adaptation. Protein Eng. Des. Sel., 20: 143-153.
PubMed  |  
99:   Pulido, M., K. Saito, S. Tanaka, Y. Koga, M. Morikawa, K. Takano and S. Kanaya, 2006. Ca2+-dependent maturation of Tk-subtilisin from a hyperthermophilic archaeon: Propeptide is a potent inhibitor of the mature domain but is not required for Its folding. Appl. Environ. Microbiol., 72: 4154-4162.
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100:   Pulido, M., S. Tanaka, C. Sringiew, D.J. You and H. Matsumura et al., 2007. Requirement of left-handed glycine residue for high stability of the Tk-subtilisin propeptide as revealed by mutational and crystallographic analyses. J. Mol. Biol., 374: 1359-1373.
PubMed  |  
101:   Rohman, M.S., Y. Koga, K. Takano, H. Chon, R.J. Crouch and S. Kanaya, 2008. Effect of the disease-causing mutations identified in human RNase H2 on the activities and stabilities of yeast RNase H2 and archaeal Rnase HII. FEBS J., 275: 4836-4849.
PubMed  |  
102:   Rohman, M.S., T. Tadokoro, C. Angkawidjaja, Y. Abe and H. Matsumura et al., 2009. Destabilization of psychrotrophic RNase HI in a localized fashion as revealed by mutational and x-ray crystallographic analyses. FEBS J., 276: 603-613.
PubMed  |  
103:   Roongsawang, N., S.P. Lim, K. Washio, K. Takano, S. Kanaya and M. Morikawa, 2005. Phylogenetic Analysis of condensation domain in the nonribosomal peptide synthetases. FEMS Microbiol. Lett., 252: 143-151.
PubMed  |  
104:   Sato, A., S. Yokotani, T. Tadokoro, S. Tanaka and C. Angkawidjaja et al., 2011. Crystal structure of stable protein, cutA1, from psychrotrophic bacterium Shewanella sp. SIB1. J. Synchrotron Rad., 18: 6-10.
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105:   Shimizu, N., S. Sugiyama, M. Maruyama, Y. Takahashi and M. Adachi et al., 2010. Crystal growth procedure of HIV-1 protease-inhibitor KNI-272 complex for neutron structural analysis at 1.9A resolution. Cryst. Growth Des., 10: 2990-2994.
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106:   Shimizu, N., S. Sugiyama, M. Maruyama, H.Y. Yoshikawa and Y. Takahashi et al., 2009. Growth of large protein crystals by top-seeded solution growth together with floating and solution-stirring technique. Cryst. Growth Des., 9: 5227-5232.
Direct Link  |  
107:   Sinsereekul, N., T. Foophow, M. Yamanouchi, Y. Koga, K. Takano and S. Kanaya, 2011. An alternative mature form of subtilisin homologue, Tk-SP, from Thermococcus kodakaraensis identified in the presence of Ca2+. FEBS J., 278: 1901-1911.
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108:   Sogabe, Y., T. Kitatani, A. Yamaguchi, T. Kinoshita and H. Adachi et al., 2011. High-resolution structure of exo-arabinanase from Penicillium chrysogenum. Acta Cryst., D67: 415-422.
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109:   Sudaratana R. Krungkrai, K. Tokuoka, Y. Kusakari and T. Inoue et al., 2006. Crystallization and preliminary crystallographic analysis of orotidine 5-monophosphate decarboxylase from the human malaria parasite Plasmodium falciparum. Acta. Cryst., F62: 542-545.
PubMed  |  
110:   Sugiyama, S., Y. Nomura, T. Sakamoto, T. Kitatani and A. Kobayashi et al., 2008. Crystallization and preliminary x-ray diffraction studies of an RNA aptamer in complex with the human IgG Fc fragment. Acta Cryst., F64: 942-944.
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111:   Sugiyama, S., H. Hasenaka, M. Hirose, N. Shimizu and T. Kitatani et al., 2009. Femtosecond laser processing of agarose gel surrounding protein crystals for the development of an automated crystal capturing system. Jpn. J. Appl. Phys., 48: 105502-105502.
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112:   Sugiyama, S., K. Tanabe, M. Hirose, T. Kitatani and H. Hasenaka et al., 2009. Protein crystallization in agarose gel with high strength: Developing an automated system for protein crystallographic processes. Jpn. J. Appl. Phys., 48: 075502-075502.
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113:   Sugiyama, S., M. Hirose, N. Shimizu, M. Niiyama and M. Maruyama et al., 2011. Effect of evaporation on protein crystals grown in semi-solid agarose hydrogel. Jpn. J. Appl. Phys., 50: 025502-025504.
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114:   Suzuki, Y., K. Takano and S. Kanaya, 2005. Stabilities and activitiesof the n- and c-domains of FKBP22 from a psychrotrophic bacterium overproduced in E. coli. FEBS J., 272: 632-642.
PubMed  |  
115:   Suzuki, Y., M. Haruki, K. Takano, M. Morikawa and S. Kanaya, 2004. Possible involvement of a FKBP family protein from a psychrotrophic bacterium shewanella sp. sib1 in cold-adaptation. Eur. J. Biochem., 271: 1372-1381.
PubMed  |  
116:   Suzuki, Y., O.Y. Win, Y. Koga, K. Takano and S. Kanaya, 2005. Binding analysis of a psychrotrophic FKBP22 to a folding intermediate of protein using surface plasmon resonance. FEBS Let., 579: 5781-5784.
CrossRef  |  PubMed  |  Direct Link  |  
117:   Suzuki, Y., Y. Mizutani, T. Tsuji, N. Ohtani and K. Takano et al., 2005. Gene cloning, overproduction, and characterizations of thermolabile alkaline phosphatase from a psychrotrophic bacterium. Biosci. Biotechnol. Biochem., 69: 364-373.
PubMed  |  
118:   Tadokoro, T., H. Chon, Y. Koga, K. Takano and S. Kanaya, 2007. Identification of the gene encoding a type 1 RNase H with an N-terminal double-stranded RNA binding domain from a psychrotrophic bacterium. FEBS J., 274: 3715-3727.
PubMed  |  
119:   Tadokoro, T., K. Matsushita, Y. Abe, M.S. Rohman, Y. Koga, K. Takano and S. Kanaya, 2008. Remarkable stabilization of a psychrotrophic RNase HI by combination of thermostabilizing mutations identified by suppressor mutation method. Biochemistry, 47: 8040-8047.
PubMed  |  
120:   Tadokoro, T., D.J. You, Y. Abe, H. Chon and H. Matsumura et al., 2007. Structural, thermodynamic and mutational analyses of a psychrotrophic RNase HI. Biochemistry, 46: 7460-7468.
PubMed  |  
121:   Takano K. and K. Yutani, 2001. Stability and structure of a series of mutant human lysozymes. Curr. Topics Peptide Protein Res., 4: 1-16.
122:   Takano K. and Katsuhide Yutani, 2001. A new scale for side chain contribution to protein stability based on the empirical stability analysis of mutant proteins. Protein Engng., 14: 525-528.
PubMed  |  
123:   Takano K., 2008. Amyloid β conformation in aqueous environment. Curr. Alzheimer Res., 5: 540-547.
PubMed  |  
124:   Takano, K., K. Tsuchimori, Y. Yamagata and K. Yutani, 2000. Contribution of salt bridges near the surface of a protein to the conformational stability. Biochemistry, 39: 12375-12381.
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125:   Takano, K., Y. Yamagata and K. Yutani, 2001. Contribution of polar groups in the interior of a protein to the conformational stability. Biochemistry, 40: 4853-4858.
PubMed  |  
126:   Takano, K., H.Y. Yoshikawa, T. Kitatani, S. Sugiyama and Y. Takahashi et al., 2009. Protein crystallization using femtosecond laser irradiation and solution stirring. Curr. Topics Peptide Protein Res., 9: 1-9.
127:   Takano, K., J. Funahashi and K. Yutani, 2001. The stability and folding process of amyloidogenic mutant human lysozymes. Eur. J. Biochem., 268: 155-159.
PubMed  |  
128:   Takano, K., J. Funahashi, Y. Yamagata, S. Fujii and K. Yutani, 1997. Contribution of Water Molecules in the Interior of a Protein to the Conformational Stability. J. Mol. Biol., 274: 132-142.
PubMed  |  
129:   Takano, K., J.M. Scholtz, C.J. Sacchettini and C.N. Pace, 2003. The contribution of polar group burial to protein stability is strongly context dependent. J. Biol. Chem., 278: 31790-31795.
PubMed  |  
130:   Takano, K., R. Higashi, J. Okada, A. Mukaiyama, T. Tadokoro, Y. Koga and S. Kanaya, 2009. Proline effect on the thermostability and slow unfolding of a hyperthermophilic protein. J. Biochem., 145: 79-85.
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131:   Takano, K., S. Endo, A. Mukaiyama, H. Chon, H. Matsumura, Y. Koga and S. Kanaya, 2006. Structure of amyloid β fragments in aqueous environments. FEBS J., 273: 150-158.
PubMed  |  
132:   Takano, K., Y. Yamagata and K. Yutani, 2000. Role of Amino Acid Residues at Turns in the Conformational Stability and Folding of Human Lysozyme. Biochemistry, 39: 8655-8665.
PubMed  |  
133:   Takano, K., Y. Yamagata, S. Fujii and K. Yutani, 1997. Contribution of the Hydrophobic Effect to the Stability of Human Lysozyme: Calorimetric Studies and X-ray Structural Analyses of the Nine Valine to Alanine Mutants. Biochemistry, 36: 688-698.
PubMed  |  
134:   Takano, K., K. Tsuchimori, Y. Yamagata and K. Yutani, 1999. Effect of Foreign N-terminal Residues on the Conformational Stability of Human Lysozyme. Eur. J. Biochem., 266: 675-682.
PubMed  |  
135:   Takano, K., M. Ota, K. Ogasahara, Y. Yamagata, K. Nishikawa and K. Yutani, 1999. Experimental Verification of the Stability Profile of Mutant Protein (SPMP) Data Using Mutant Human Lysozymes. Protein Eng., 12: 663-672.
PubMed  |  
136:   Takano, K., M. Saito, M. Morikawa and S. Kanaya, 2004. Mutational and structural-based analyses of the osmolyte effect on protein stability. J. Biochem., 135: 701-708.
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137:   Takano, K., T. Okamoto, J. Okada, S. Tanaka, C. Angkawidjaja, Y. Koga and S. Kanaya, 2011. Stabilization by fusion to the C-terminus of hyperthermophile Sulfolobus tokodaii RNase HI: A possibility of protein stabilization tag. PLoS ONE, 6: e16226-e16226.
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138:   Takano, K., Y. Katagiri, A. Mukaiyama, H. Chon, H. Matsumura, Y. Koga and S. Kanaya, 2007. Conformational contagion in a protein: Structural properties of a chameleon sequence. Proteins, 68: 617-625.
PubMed  |  
139:   Takano, K., Y. Yamagata and K. Yutani, 1998. A general rule for the relationship between hydrophobic effect and conformational stability of a protein: Stability and structure of a series of hydrophobic mutants of human lysozyme. J. Mol. Biol., 280: 749-761.
PubMed  |  
140:   Takano, K., Y. Yamagata and K. Yutani, 2001. Role of amino acid residues in left-handed helical conformation for the conformational stability of a protein. Proteins, 45: 274-280.
PubMed  |  
141:   Takano, K., Y. Yamagata and K. Yutani, 2001. Role of non-glycine residues in left-handed helical conformation for the conformational stability of human lysozyme. Proteins, 44: 233-243.
PubMed  |  
142:   Takano, K., Y. Yamagata and K. Yutani, 2003. Takano, K., Y. Yamagata and K. Yutani, 2003. Buried water molecules contribute to the conformational stability of a protein. Protein Eng., 16: 5-9.
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143:   Takano, K., Y. Yamagata, M. Kubota, J. Funahashi, S. Fujii and K. Yutani, 1999. Contribution of Hydrogen Bonds to the Conformational Stability of Human Lysozyme: Calorimetry and X-ray Analysis of Six Ser --> Ala Mutants. Biochemistry, 38: 6623-6629.
PubMed  |  
144:   Takeuchi, K., H. Kitano, H. Adachi, Y. Mori and T. Sasaki et al., 2005. Protein crystal growth using laser-processed seed crystals. Jpn. J. Appl. Phys., 44: 3177-3179.
CrossRef  |  
145:   Takeuchi, Y., S. Tanaka, H. Matsumura, Y. Koga, K. Takano and S. Kanaya, 2009. Requirement of a unique Ca2+-binding loop for folding of Tk-subtilisin from a hyperthermophilic archaeon. Biochemistry, 48: 10637-10643.
PubMed  |  
146:   Tanabe, K., M. Hirose, R. Murai, S. Sugiyama and N. Shimizu et al., 2009. Promotion of crystal nucleation of protein by semi-solid agarose gel. Appl. Phys. Express, 2: 125501-125501.
Direct Link  |  
147:   Tanaka, M., H. Chon, C. Angkawidjaja, Y. Koga, K. Takano and S. Kanaya, 2010. Protein core adaptability: Crystal structures of the cavity-filling variants of Escherichia coli RNase HI. Protein Pept. Lett., 17: 1163-1169.
PubMed  |  
148:   Tanaka, S., H. Matsumura, Y. Koga, K. Takano and S. Kanaya, 2007. Four new crystal structures of Tk-subtilisin in unautoprocessed, autoprocessed and mature forms: Insight in structural changes during maturation process. J. Mol. Biol., 372: 1055-1069.
PubMed  |  
149:   Tanaka, S., K. Saito, H. Chon, H. Matsumura, Y. Koga, K. Takano and S. Kanaya, 2006. Crystallization and preliminary X-ray diffraction study of active-site mutant of pro-Tk-subtilisin from a hyperthermophilic archaeon. Acta. Cryst., F62: 902-905.
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150:   Tanaka, S., H. Matsumura, Y. Koga, K. Takano and S. Kanaya, 2009. Identification of the interactions critical for propeptide-catalyzed folding of Tk-subtilisin. J. Mol. Biol., 394: 306-319.
PubMed  |  
151:   Tanaka, S., K. Saito, H. Chon, H. Matsumura, Y. Koga, K. Takano and S. Kanaya, 2007. Crystal structure of unautoprocessed precursor of subtilisin from a Hyperthermophilic archaeon: Evidence for Ca2+-induced folding. J. Biol. Chem., 282: 8246-8255.
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152:   Tanaka, S., Y. Takeuchi, H. Matsumura, Y. Koga, K. Takano and S. Kanaya, 2008. Crystal structure of Tk-subtilisin folded without propeptide: Requirement of propeptide for acceleration of folding. FEBS Let., 582: 3875-3878.
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153:   Tsukazaki, T., H. Mori, S. Fukai, T. Numata and A. Perederina et al., 2006. Purification, crystallization and preliminary X-ray diffraction of secDF, a translocon-associated membrane protein, from Thermus thermophilus. Acta. Cryst., F62: 376-380.
PubMed  |  
154:   Tsunaka, Y., K. Takano, H. Matsumura, Y. Yamagata and S. Kanaya, 2005. Identification of single Mn2+ binding sites required for activation of the mutant proteins of E. coli rnase HI at glu48 and/or asp134 by X-ray crystallography. J. Mol. Biol., 345: 1171-1183.
Direct Link  |  
155:   Yamagata, Y., M. Kubota, Y. Sumikawa, J. Funahashi, K. Takano, S. Fujii and K. Yutani, 1998. Contribution of Hydrogen Bonds to the Conformational Stability of Human Lysozyme: Calorimetry and X-ray Analysis of Six Tyr --> Phe Mutants. Biochemistry, 37: 9355-9362.
PubMed  |  
156:   Yaoi, M., H. Adachi, K. Takano, H. Matsumura, T. Inoue, Y. Mori and T. Sasaki, 2004. The effects of solution stirring on protein crystal growth. Jpn. J. Appl. Phys., 43: L686-L688.
CrossRef  |  Direct Link  |  
157:   Yaoi, M., H. Adachi, K. Takano, H. Matsumura, T. Inoue, Y. Mori and T. Sasaki, 2004. Effect of stirring method on protein crystallization. Jpn. J. Appl. Phys., 43: L1318-L1319.
CrossRef  |  Direct Link  |  
158:   Yoshikawa, H.Y., R. Murai, S. Maki, T. Kitatani and S. Sugiyama et al., 2008. Laser energy dependence on femtosecond laser-induced nucleation of protein. Appl. Phys., A93: 911-915.
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159:   Yoshikawa, H.Y., R. Murai, S. Sugiyama, G. Sazaki and T. Kitatani et al., 2009. Femtosecond laser-induced nucleation of protein in agarose gel. J. Cryst. Growth, 311: 956-959.
160:   You, D.J., H. Chon, Y. Koga, K. Takano and S. Kanaya, 2006. Crystallization and preliminary crystallographic analysis of type 1 RNase H from hyperthermophilic archaeon Sulfolobus tokodaii 7. Acta. Cryst., F62: 781-784.
PubMed  |  
161:   You, D.J., S. Fukuchi, K. Nishikawa, Y. Koga, K. Takano and S. Kanaya, 2007. Protein thermostabilization requires a fine-tuned placement of surface charged residues. J. Biochem., 142: 507-516.
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162:   You, D.J., H. Chon, Y. Koga, K. Takano and S. Kanaya, 2007. Crystal structure of type 1 RNase H from Hyperthermophilic archaeon sulfolobus tokodaii: Role of arg118 and C-terminal anchoring. Biochemistry, 46: 11494-11503.
PubMed  |