<Publications>

~2013

  • Tani Y, Nakamura K, Sawa R, Nishio M, Saito S, Ito M, Itonori S, Mihara H. (2013) "Novel neogala-series glycosphingolipids with a terminal glucose residue from the fungus Mariannaea elegans" Biosci Biotech Biochem. 77, 754-759.

  • Hidese R, Mihara H, Kurihara T, Esaki N. (2012) "Pseudomonas putida PydR, a RutR-like transcriptional regulator, represses the dihydropyrimidine dehydrogenase gene in the pyrimidine reductive catabolic pathway" J Biochem. 152, 341-6.

  • Mihara H, Esaki N. (2012) "Selenocysteine Lyase: Mechanism, Structure, and Biological Role" Selenium: Its Molecular Biology and Role in Human and Health (Hatfield DL, Berry MJ, Gladyshev VN. eds.), Springer, New York. pp 95-105.

  • Saito S, Yamano K, Ueda H, Tani Y, Hayakawa M, Tsuji A, Mihara H. (2012) "Effects of a supernatant from Aspergillus oryzae culture on the regulation of crassulacean acid metabolism (CAM) and pinitol biosynthesis in the common ice plant, Mesembryanthemum crystallinum L." Trace Nutr Res. 29, 51-57.

  • Mihara H. (2012) 『セレンディピティ』 バイオサイエンスとインダストリー. 70, 144.

  • Mihara H. (2011) "Structure and function of selenocysteine lyase and cysteine desulfurase" Amino Acids. 41, S77-S78.

  • Tamura, T., Sato, K., Komori, K., Imai, T., Kuwahara, M., Okugochi, T., Mihara, H., Esaki, N. & Inagaki, K. (2011) Selenite reduction by the thioredoxin system: kinetics and identification of protein-bound selenide, Biosci Biotechnol Biochem. 75, 1184-7.

  • Omori, T., Honda, A., Mihara, H., Kurihara, T. & Esaki, N. (2011) Identification of novel mammalian phospholipids containing threonine, aspartate, and glutamate as the base moiety, J Chromat B. 879, 3296-3302.

  • Mihara, H. (2011) 鉄硫黄クラスター・セレンタンパク質生合成を司る酵素, 生化学. 83, 1003-1015.

  • Mihara, H. (2011) 硫黄・セレン供給酵素群による含硫・含セレンバイオファクターの生成機構, バイオサイエンスとインダストリー. 69, 471-475.

  • Kurokawa, S., Takehashi, M., Tanaka, H., Mihara, H., Kurihara, T., Tanaka, S., Hill, K., Burk, R. & Esaki, N. (2011) Mammalian selenocysteine lyase is involved in selenoprotein biosynthesis, J Nutr Sci Vitaminol. 57, 298-305.

  • Kawamoto, J., Sato, T., Nakasone, K., Kato, C., Mihara, H., Esaki, N. & Kurihara, T. (2011) Favourable effects of eicosapentaenoic acid on the late step of the cell division in a piezophilic bacterium, Shewanella violacea DSS12, at high-hydrostatic pressures, Environ Microbiol. 13, 2293-2298.

  • Hidese, R., Mihara, H., Kurihara, T. & Esaki, N. (2011) Escherichia coli dihydropyrimidine dehydrogenase is a novel NAD-dependent heterotetramer essential for the production of 5,6-dihydrouracil, J Bacteriol. 193, 989-93.

  • Hidese, R., Mihara, H. & Esaki, N. (2011) Bacterial cysteine desulfurase: versatile key players in biosynthetic pathways of sulfur-containing biofactors, Appl Microbiol Biot. 91, 47-61.

  • Zhang, W. J., Urban, A., Mihara, H., Leimkuhler, S., Kurihara, T. & Esaki, N. (2010) IscS Functions as a Primary Sulfur-donating Enzyme by Interacting Specifically with MoeB and MoaD in the Biosynthesis of Molybdopterin in Escherichia coli, J Biol Chem. 285, 2302-2308.

  • Yoshimura, T., Mihara, H., Ohshima, T. & Tanizawa, K. (2010) Kenji Soda--researching enzymes with the spirit of an alpinist, J Biochem. 148, 371-9.

  • Tobe, R., Mihara, H., Kurihara, T. & Esaki, N. (2010) Specific transfer of selenium in selenoprotein biosynthesis, Biomed Res Trace Elem. 21, 187-193.

  • Omori, T., Mihara, H., Kurihara, T. & Esaki, N. (2010) Distribution of phosphatidyl-D-serine in rat, Biosci Biotechnol Biochem. 74, 1953-1955.

  • Omi, R., Kurokawa, S., Mihara, H., Hayashi, H., Goto, M., Miyahara, I., Kurihara, T., Hirotsu, K. & Esaki, N. (2010) Reaction mechanism and molecular basis for selenium/sulfur discrimination of selenocysteine lyase, J Biol Chem. 285, 12133-9.

  • Kotera, M., Bayashi, T., Hattori, M., Tokimatsu, T., Goto, S., Mihara, H. & Kanehisa, M. (2010) Comprehensive genomic analysis of sulfur-relay pathway genes, Genome Inform. 24, 104-15.

  • Mihara, H. & Esaki, N. (2010) Synthesis of L-Pipecolic Acid with D1-Piperidine-2-carboxylate Reductase from Pseudomonas putida in Practical Methods for Biocatalysis and Biotransformations (Whittall, J. & Sutton, P. W., eds) pp. 310-313, Wiley, Chichester, UK.

  • Yasuda, M. H., Ueda, M., Okano, K., Mihara, H. & Esaki, N. (2009) Enzymatic Synthesis of Unnatural Amino Acids in Asymmetric Synthesis and Application of α-Amino Acids (Soloshonok, V. A. & Izawa, K., eds), ACS Publications, Washington, DC.

  • Yamauchi, T., Goto, M., Wu, H. Y., Uo, T., Yoshimura, T., Mihara, H., Kurihara, T., Miyahara, I., Hirotsu, K. & Esaki, N. (2009) Serine racemase with catalytically active lysinoalanyl residue, J Biochem. 145, 421-4.

  • Tobe, R., Mihara, H., Kurihara, T. & Esaki, N. (2009) Identification of proteins interacting with selenocysteine lyase, Biosci Biotechnol Biochem. 73, 1230-2.

  • Omori, T., Mihara, H., Kurihara, T. & Esaki, N. (2009) Occurrence of phosphatidyl-D-serine in the rat cerebrum, Biochem Biophys Res Commun. 382, 415-8.

  • Mihara, H. (2009) Discrimination between selenium and sulfur by enzymes [Japanese], Biomed Res Trace Elem. 20, 218-225.

  • Kawamoto, J., Kurihara, T., Yamamoto, K., Nagayasu, M., Tani, Y., Mihara, H., Hosokawa, M., Baba, T., Sato, S. B. & Esaki, N. (2009) Eicosapentaenoic acid plays a beneficial role in membrane organization and cell division of a cold-adapted bacterium, Shewanella livingstonensis Ac10, J Bacteriol. 191, 632-40.

  • Jitsumori, K., Omi, R., Kurihara, T., Kurata, A., Mihara, H., Miyahara, I., Hirotsu, K. & Esaki, N. (2009) X-Ray Crystallographic and Mutational Studies of Fluoroacetate Dehalogenase from Burkholderia sp Strain FA1, J Bacteriol. 191, 2630-2637.

  • Imai, T., Mihara, H., Kurihara, T. & Esaki, N. (2009) Selenocysteine is selectively taken up by red blood cells, Biosci Biotechnol Biochem. 73, 2746-8.

  • Imai, T., Mihara, H., Kurihara, T. & Esaki, N. (2009) Possible Role of Red Blood Cells in Selenocysteine Metabolism Trace Nutri Res. 26, 22-25.

  • Hidese R, Mihara H, Esaki N. (2009) 『大腸菌由来新規 NADH 依存性ジヒドロピリミジンデヒドロゲナーゼの機能解析』ビタミン. 83, 528-532.

  • Goto, M., Yamauchi, T., Kamiya, N., Miyahara, I., Yoshimura, T., Mihara, H., Kurihara, T., Hirotsu, K. & Esaki, N. (2009) Crystal Structure of a Homolog of Mammalian Serine Racemase from Schizosaccharomyces pombe, J Biol Chem. 284, 25944-25952.

  • Zhang W, Mihara H, Kurihara T, Esaki N. (2008) 『モリブドプテリン生合成におけるシステインデスルフラーゼ IscS の役割』ビタミン. 82, 645-650.

  • Zhang, W., Mihara, H., Kurihara, T. & Esaki, N. (2008) Investigation of the Roles of Cysteine Desulfurases in the Molybdopterin Synthesis in Escherichia coli, Trace Nutri Res. 25, 152-157

  • Takahata, M., Tamura, T., Abe, K., Mihara, H., Kurokawa, S., Yamamoto, Y., Nakano, R., Esaki, N. & Inagaki, K. (2008) Selenite Assimilation into Formate Dehydrogenase H Depends on Thioredoxin Reductase in Escherichia coli, J Biochem. 143, 467-473.

  • Muramatsu, H., Mihara, H., Kurihara, T. & Esaki, N. (2008) N-アルキルアミノ酸と環状イミノ酸の不斉合成に利用できる酵素, ファインケミカル. 37, 12-21.

  • Mihara H, Hidese R, Yamane M, Kurihara T, Esaki N. (2008) "The iscS gene deficiency affects the expression of pyrimidine metabolism genes" Biochem Biophys Res Commun. 372, 407-411.

  • Kurokawa, S., Mihara, H., Yokoyama, I., Mochizuki, M., Yodoi, J., Tamura, T., Kurihara, T. & Esaki, N. (2008) Thioredoxin Reductase 1 Is Important for Selenoprotein Biosynthesis in HeLa Cells, Biomed Res Trace Elem. 19, 84-87.

  • Esaki, N. & Mihara, H. (2008) Function and biosynthesis of selenoproteins [Japanese], Biomed Res Trace Elem. 19, 308-316.

  • Abe, K., Mihara, H., Tobe, R. & Esaki, N. (2008) Characterization of human selenocysteine synthase involved in selenoprotein biosynthesis, Biomed Res Trace Elem. 19, 80-83.

  • Abe, K., Mihara, H., Nishijima, Y., Kurokawa, S. & Esaki, N. (2008) Functional analysis of two homologous mouse selenophosphate synthetases, Biomed Res Trace Elem. 19, 76-79.

  • Yoshida, M., Oikawa, T., Obata, H., Abe, K., Mihara, H. & Esaki, N. (2007) Biochemical and genetic analysis of the γ-resorcylate (2,6-dihydroxybenzoate) catabolic pathway in Rhizobium sp strain MTP-10005: Identification and functional analysis of its gene cluster, J Bacteriol. 189, 1573-1581.

  • Yamanishi, Y., Mihara, H., Osaki, M., Muramatsu, H., Esaki, N., Sato, T., Hizukuri, Y., Goto, S. & Kanehisa, M. (2007) Prediction of missing enzyme genes in a bacterial metabolic network - Reconstruction of the lysine-degradation pathway of Pseudomonas aeruginosa, FEBS J. 274, 2262-2273.

  • Mihara H, Esaki N. (2007) 『シュードモナスのリジン分解経路におけるミッシング酵素の同定と解析』ビタミン. 81, 595-600.

  • Mihara H, Esaki N. (2007) 『Selenoproteins [セレンタンパク質]』 Kinzoku [金属]. 77, 262-268.

  • Fujita, M., Mihara, H., Goto, S., Esaki, N. & Kanehisa, M. (2007) Mining prokaryotic genomes for unknown amino acids: a stop-codon-based approach, BMC Bioinformatics. 8, 225.

  • Yasuda, M., Ueda, M., Muramatsu, H., Mihara, H. & Esaki, N. (2006) Enzymatic synthesis of cyclic amino acids by N-methyl-L-amino acid dehydrogenase from Pseudomonas putida, Tetrahedron Asymmet. 17, 1775-1779.

  • Muramatsu, H., Mihara, H., Yasuda, M., Ueda, M., Kurihara, T. & Esaki, N. (2006) Enzymatic synthesis of L-pipecolic acid by Δ1-piperideine-2-carboxylate reductase from Pseudomonas putida, Biosci Biotechnol Biochem. 70, 2296-2298.

  • Mihara, H., Kurokawa, S., Omi, R., Kurihara, T., Hirotsu, K. & Esaki, N. (2006) Selenoprotein biosynthesis and selenium-specific enzymes, Biomed Res Trace Elem. 17, 355-359.

  • Mihara H, Esaki N. (2006) 『セレン化合物とピリドキサール5´-リン酸酵素の生化学』 ビタミン. 80, 587-595.

  • Mihara H,  Esaki N. (2006)『代謝経路データベース上のミッシング酵素の同定 -Identification of missing enzymes in metabolic pathway databases-』 バイオサイエンスとインダストリー. 64, 553-557.

  • Mihara H,  Esaki N. (2006) 『遺伝子と微量元素』 治療. 88, 1859-1864.

  • Mihara H. (2006) 『N-メチル-L-アミノ酸とL-ピペコリン酸の合成酵素 -An enzyme synthesizing N-methyl-L-amino acid and pipecolic acid-』バイオサイエンスとインダストリー. 64, 31-32.

  • Muramatsu, H., Mihara, H., Kakutani, R., Yasuda, M., Ueda, M., Kurihara, T. & Esaki, N. (2005) The putative malate/lactate dehydrogenase from Pseudomonas putida is an NADPH-dependent Δ1-piperideine-2-carboxylate/Δ1-pyrroline-2-carboxylate reductase involved in the catabolism of D-lysine and D-proline, J Biol Chem. 280, 5329-5335.

  • Muramatsu, H., Mihara, H., Goto, M., Miyahara, I., Hirotsu, K., Kurihara, T. & Esaki, N. (2005) A new family of NAD(P)H-dependent oxidoreductases distinct from conventional Rossmann-fold proteins, J Biosci Bioeng. 99, 541-547.

  • Mihara, H., Muramatsu, H., Kakutani, R., Yasuda, M., Ueda, M., Kurihara, T. & Esaki, N. (2005) N-Methyl-L-amino acid dehydrogenase from Pseudomonas putida - A novel member of an unusual NAD(P)-dependent oxidoreductase superfamily, FEBS J. 272, 1117-1123.

  • Kurokawa, S., Mihara, H., Takehashi, M., Tanaka, S., Kurihara, T. & Esaki, N. (2005) RNAi-mediated knock down of mammalian selenocysteine lyase, Biomed Res Trace Elem. 16, 321-324.

  • Goto, M., Muramatsu, H., Mihara, H., Kurihara, T., Esaki, N., Omi, R., Miyahara, I. & Hirotsu, K. (2005) Crystal structures of Δ1-piperideine-2-carboxylate/Δ1-pyrroline-2-carboxylate reductase belonging to a new family of NAD(P)H-dependent oxidoreductases - Conformational change, substrate recognition, and stereochemistry of the reaction, J Biol Chem. 280, 40875-40884.

  • Esaki, N., Mihara, H., Hara, M. & Ueda, M. (2005) Manufacture of optically active cyclic amino acids with N-methyl-L-amino acid dehydrogenase in Jpn Kokai Tokkyo Koho (Koho, J. K. T., ed)Japan.

  • Abe, K., Ebata, I., Kazuoka, T., Mihara, H., Kurihara, T. & Esaki, N. (2005) Protein interaction between selenophosphate synthetase and IscS, Biomed Res Trace Elem. 16, 325-327.

  • Muramatsu, H., Mihara, H., Kakutani, R., Yasuda, M., Ueda, M., Kurihara, T. & Esaki, N. (2004) Enzymatic synthesis of N-methyl-L-phenylalanine by a novel enzyme, N-methyl-L-amino acid dehydrogenase, from Pseudomonas putida, Tetrahedron Asymmet. 15, 2841-2843.

  • Kurokawa, S., Mihara, H., Kurihara, T. & Esaki, N. (2004) Expression analysis of mammalian selenocysteine lyase, Biomed Res Trace Elem. 15, 278-280.

  • Pilon-Smits, E. A. H., Garifullina, G. F., Abdel-Ghany, S., Kato, S. I., Mihara, H., Hale, K. L., Burkhead, J. L., Esaki, N., Kurihara, T. & Pilon, M. (2003) Characterization of a NifS-like chloroplast protein from Arabidopsis. Implications for its role in sulfur and selenium metabolism (vol 130, pg 1309, 2002), Plant Physiol. 131, 379-379.

  • Pilon, M., Owen, J. D., Garifullina, G. F., Kurihara, T., Mihara, H., Esaki, N. & Pilon-Smits, E. A. H. (2003) Enhanced selenium tolerance and accumulation in transgenic Arabidopsis expressing a mouse selenocysteine lyase, Plant Physiol. 131, 1250-1257.

  • Mihara, H. (2003) まだまだ謎の多いビオチン生合成, 生物工学会誌. 81, 164.

  • Kwak, M. S., Mihara, H. & Esaki, N. (2003) A novel regulatory function of selenocysteine lyase, a unique catalyst to modulate major urinary protein, J Mol Catal B-Enzym. 23, 367-372.

  • Kuwana, E., Kurokawa, S., Mihara, H., Kurihara, T., Yoshimura, T. & Esaki, N. (2003) Effects of selenium deficiency on the expression of selenoprotein mRNAs in mouse brain, Biomed Res Trace Elem. 14, 293-296.

  • Kurihara, T., Mihara, H., Kato, S., Yoshimura, T. & Esaki, N. (2003) Assembly of iron-sulfur clusters mediated by cysteine desulfarases, IscS, CsdB and CSD, from Escherichia coli, Biochim Biophys Acta. 1647, 303-309.

  • Esaki, N., Mihara, H., Hara, M. & Ueda, M. (2003) Novel Pseudomonas putida dehydrogenase catalyzing synthesis of N-alkyl amino acid from pyruvate and alkylamine, encoding gene, and biosynthetic uses. in WO2003072770

  • Esaki, N. & Mihara, H. (2003) 鉄硫黄クラスター形成にかかわるピリドキサル酵素の機能、構造、触媒機構, ビタミン. 77, 285-295.

  • Tokumoto, U., Nomura, S., Minami, Y., Mihara, H., Kato, S., Kurihara, T., Esaki, N., Kanazawa, H., Matsubara, H. & Takahashi, Y. (2002) Network of protein-protein interactions among iron-sulfur cluster assembly proteins in Escherichia coli, J Biochem. 131, 713-719.

  • Pilon-Smits, E. A. H., Garifullina, G. F., Abdel-Ghany, S., Kato, S. I., Mihara, H., Hale, K. L., Burkhead, J. L., Esaki, N., Kurihara, T. & Pilon, M. (2002) Characterization of a NifS-Like chloroplast protein from Arabidopsis. Implications for its role in sulfur and selenium metabolism, Plant Physiol. 130, 1309-1318.

  • Mihara, H., Kato, S., Lacourciere, G. M., Stadtman, T. C., Kurihara, T., Tokumoto, U., Takahashi, Y. & Esaki, N. (2002). Role of NifS homologs in selenium metabolism. Paper presented at the The 19th Symposium on Trace Nutrients Research.

  • Mihara, H., Kato, S., Lacourciere, G. M., Stadtman, T. C., Kennedy, R. A. J. D., Kurihara, T., Tokumoto, U., Takahashi, Y. & Esaki, N. (2002) The iscS gene is essential for the biosynthesis of 2-selenouridine in tRNA and the selenocysteine-containing formate dehydrogenase H, P Natl Acad Sci USA. 99, 6679-6683.

  • Mihara, H., Fujii, T., Kato, S., Kurihara, T., Hata, Y. & Esaki, N. (2002) Structure of external aldimine of Escherichia coli CsdB, an IscS/NifS homolog: Implications for its specificity toward selenocysteine, J Biochem. 131, 679-685.

  • Mihara, H. & Esaki, N. (2002) セレンの生化学, ビタミン. 76, 7-9.

  • Mihara, H. & Esaki, N. (2002) Selenocysteine lyase from mouse liver, Methods Enzymol. 347, 198-203.

  • Mihara, H. & Esaki, N. (2002) Bacterial cysteine desulfurases: their function and mechanisms, Appl Microbiol Biot. 60, 12-23.

  • Kwak, M. S., Mihara, H. & Esaki, N. (2002) Protein Interaction between Selenocysteine Lyase and MUP-I, Biomed Res Trace Elem. 13, 238-239.

  • Kato, S., Mihara, H., Kurihara, T., Takahashi, Y., Tokumoto, U., Yoshimura, T. & Esaki, N. (2002) Cys-328 of IscS and Cys-63 of IscU are the sites of disulfide bridge formation in a covalently bound IscS/IscU complex: Implications for the mechanism of iron-sulfur cluster assembly, P Natl Acad Sci USA. 99, 5948-5952.

  • Mihara, H., Kato, S., Kurihara, T., Yoshimura, T., Esaki, N., Lacourciere, G. M. & Stadtman, T. C. (2001) Role of Cysteine Desulfurase in the Biosynthesis of Formate Dehydrogenase H Containing Mo, Molybdopterin, Selenocysteine, and Fe4S4 Cluster, Biomed Res Trace Elem. 12, 261-262.

  • Kato, S., Mihara, H., Kurihara, T., Yoshimura, T. & Esaki, N. (2001). Screening and Identification of a Protein Interacting with IscU. Paper presented at the The 18th Symposium on Trace Nutrients Research.

  • Kashiwa, M., Ike, M., Mihara, H., Esaki, N. & Fujita, M. (2001) Removal of soluble selenium by a selenate-reducing bacterium Bacillus sp. SF-1, Biofactors. 14, 261-265.

  • Mihara, H., Kurihara, T., Yoshimura, T. & Esaki, N. (2000) Kinetic and mutational studies of three NifS homologs from Escherichia coli: Mechanistic difference between L-cysteine desulfurase and L-selenocysteine lyase reaction, J Biochem. 127, 559-567.

  • Mihara, H., Kurihara, T., Watanabe, T., Yoshimura, T. & Esaki, N. (2000) cDNA cloning, purification, and characterization of mouse liver selenocysteine lyase - Candidate for selenium delivery protein in selenoprotein synthesis, J Biol Chem. 275, 6195-6200.

  • Lacourciere, G. M., Mihara, H., Kurihara, T., Esaki, N. & Stadtman, T. C. (2000) Escherichia coli NifS-like proteins provide selenium in the pathway for the biosynthesis of selenophosphate, J Biol Chem. 275, 23769-23773.

  • Kato, S., Mihara, H., Kurihara, T., Yoshimura, T. & Esaki, N. (2000). A NifS homolog operating the biogenesis of elemental sulfur and elemental selemium: Analysis of their ability to form iron-sulfur cluster [元素状硫黄と元素状セレンのバイオジェネシスを司るNifS相同タンパク質: 鉄-硫黄クラスター形成能の解明]. Paper presented at the The 17th Symposium on Trace Nutrients Research.

  • Kato, S., Mihara, H., Kurihara, T., Yoshimura, T. & Esaki, N. (2000) Gene cloning, purification, and characterization of two cyanobacterial NifS homologs driving iron-sulfur cluster formation, Biosci Biotechnol Biochem. 64, 2412-2419.

  • Fujii, T., Maeda, M., Mihara, H., Kurihara, T., Esaki, N. & Hata, Y. (2000) Structure of a NifS homologue: X-ray structure analysis of CsdB, an Escherichia coli counterpart of mammalian selenocysteine lyase, Biochemistry. 39, 1263-1273.

  • Mihara, H., Maeda, M., Fujii, T., Kurihara, T., Hata, Y. & Esaki, N. (1999) A nifS-like gene, csdB, encodes an Escherichia coli counterpart of mammalian selenocysteine lyase - Gene cloning, purification, characterization and preliminary x-ray crystallographic studies, J Biol Chem. 274, 14768-14772.

  • Mihara, H. (1999) Enzymological studies of cysteine desulfurase and selenocysteine lyase, Kyoto University.

  • Esaki, N., Mihara, H., Kurihara, T., Yoshimura, T. & Soda, K. (1999). Structure and function of an E. coli NifS homolog with selenocysteine lyase activity [セレノシステインリアーゼ活性を持つ大腸菌NifSホモログの構造と機能]. Paper presented at the The 16th Symposium on Trace Nutrients Research.

  • Mihara H, Kurihara T, Yoshimura T, Soda K, Esaki N. (1997) "Cysteine sulfinate desulfinase, a NIFS-like protein of Escherichia coli with selenocysteine lyase and cysteine desulfurase activities - Gene cloning, purification, and characterization of a novel pyridoxal enzyme" J Biol Chem. 272, 22417-22424.

  • Mihara H. (1995) 『セレンによるAIDS治療の可能性』 ビタミン. 69, 226-228.

  • Watanabe K, Masuda T, Ohashi H, Mihara H, Suzuki Y. (1994) "Multiple proline substitutions cumulatively thermostabilize Bacillus cereus ATCC7064 oligo-1,6-glucosidase - irrefragable proof supporting the proline rule" Eur J Biochem. 226, 277-283.

<Contact>

Bio Link 7F,

Biwako-Kusatsu Campus (BKC),

Ritsumeikan University

 

1-1-1 Nojihigashi,

Kusatsu, Shiga 525-8577, Japan

Tel.: +81-77-561-2732

Fax: +81-77-561-2659

E-mail: mihara* (* = @fc.ritsumei.ac.jp)

This site was designed with the
.com
website builder. Create your website today.
Start Now