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Volumn 9, Issue , 2010, Pages

Molecular cloning and biochemical characterization of a novel erythrose reductase from Candida magnoliae JH110

Author keywords

[No Author keywords available]

Indexed keywords

ALCOHOL; ALDEHYDE KETONE REDUCTASE; AMINO ACID; ARGININE; CHAPERONE; ERYTHRITOL; ERYTHROSE REDUCTASE; FUNGAL ENZYME; LYSINE; NUCLEOTIDE; OXIDOREDUCTASE; REDUCED NICOTINAMIDE ADENINE DINUCLEOTIDE PHOSPHATE; THREONINE; UNCLASSIFIED DRUG; ALDEHYDE REDUCTASE; RECOMBINANT PROTEIN;

EID: 77954575962     PISSN: None     EISSN: 14752859     Source Type: Journal    
DOI: 10.1186/1475-2859-9-43     Document Type: Article
Times cited : (34)

References (49)
  • 2
    • 0032411028 scopus 로고    scopus 로고
    • Erythritol: an interpretive summary of biochemical, metabolic, toxicological and clinical data
    • 10.1016/S0278-6915(98)00091-X, 9862657
    • Munro IC, Bernt WO, Borzelleca JF, Flamm G, Lynch BS, Kennepohl E, Bar EA, Modderman J. Erythritol: an interpretive summary of biochemical, metabolic, toxicological and clinical data. Food Chem Toxicol 1998, 36(12):1139-1174. 10.1016/S0278-6915(98)00091-X, 9862657.
    • (1998) Food Chem Toxicol , vol.36 , Issue.12 , pp. 1139-1174
    • Munro, I.C.1    Bernt, W.O.2    Borzelleca, J.F.3    Flamm, G.4    Lynch, B.S.5    Kennepohl, E.6    Bar, E.A.7    Modderman, J.8
  • 3
    • 0027469734 scopus 로고
    • Metabolism of erythritol in humans: comparison with glucose and lactitol
    • 10.1079/BJN19930019, 8457525
    • Hiele M, Ghoos Y, Rutgeerts P, Vantrappen G. Metabolism of erythritol in humans: comparison with glucose and lactitol. Br J Nutr 1993, 69(1):169-176. 10.1079/BJN19930019, 8457525.
    • (1993) Br J Nutr , vol.69 , Issue.1 , pp. 169-176
    • Hiele, M.1    Ghoos, Y.2    Rutgeerts, P.3    Vantrappen, G.4
  • 4
    • 27944455247 scopus 로고    scopus 로고
    • Human gut microbiota does not ferment erythritol
    • 10.1079/BJN20051546, 16277764
    • Arrigoni E, Brouns F, Amado R. Human gut microbiota does not ferment erythritol. Br J Nutr 2005, 94(5):643-646. 10.1079/BJN20051546, 16277764.
    • (2005) Br J Nutr , vol.94 , Issue.5 , pp. 643-646
    • Arrigoni, E.1    Brouns, F.2    Amado, R.3
  • 7
    • 0033760876 scopus 로고    scopus 로고
    • Optimization of erythritol production by Candida magnoliae in fed-batch culture
    • Ryu YW, Park CY, Park JB, Kim SY, Seo JH. Optimization of erythritol production by Candida magnoliae in fed-batch culture. J Ind Microbiol Biotechnol 2000, 25(2):100-103.
    • (2000) J Ind Microbiol Biotechnol , vol.25 , Issue.2 , pp. 100-103
    • Ryu, Y.W.1    Park, C.Y.2    Park, J.B.3    Kim, S.Y.4    Seo, J.H.5
  • 8
    • 0027209897 scopus 로고
    • Pathway and regulation of erythritol formation in Leuconostoc oenos
    • 204821, 8391532
    • Veiga-da-Cunha M, Santos H, Van Schaftingen E. Pathway and regulation of erythritol formation in Leuconostoc oenos. J Bacteriol 1993, 175(13):3941-3948. 204821, 8391532.
    • (1993) J Bacteriol , vol.175 , Issue.13 , pp. 3941-3948
    • Veiga-da-Cunha, M.1    Santos, H.2    Van Schaftingen, E.3
  • 9
    • 0013595670 scopus 로고
    • Breeding of a mutant of Aureobasidium sp. with high erythritol production
    • Ishizuka H, Wako K, Kasumi T, Sasaki T. Breeding of a mutant of Aureobasidium sp. with high erythritol production. J Ferment Bioeng 1989, 68(5):310-314.
    • (1989) J Ferment Bioeng , vol.68 , Issue.5 , pp. 310-314
    • Ishizuka, H.1    Wako, K.2    Kasumi, T.3    Sasaki, T.4
  • 10
    • 0002496761 scopus 로고    scopus 로고
    • Analysis of fermentation characteristics for production of erythritol by Candida sp
    • Kim SY, Park SS, Jeon YJ, Seo JH. Analysis of fermentation characteristics for production of erythritol by Candida sp. Kor J Food Sci Technol 1996, 28(5):935-939.
    • (1996) Kor J Food Sci Technol , vol.28 , Issue.5 , pp. 935-939
    • Kim, S.Y.1    Park, S.S.2    Jeon, Y.J.3    Seo, J.H.4
  • 11
    • 77954593119 scopus 로고    scopus 로고
    • Two-stage fed-batch culture of Candida magnoliae for the production of erythritol using an industrial medium
    • Park SY, Seo JH, Ryu YW. Two-stage fed-batch culture of Candida magnoliae for the production of erythritol using an industrial medium. Kor J Biotechnol Bioeng 2003, 18(4):249-254.
    • (2003) Kor J Biotechnol Bioeng , vol.18 , Issue.4 , pp. 249-254
    • Park, S.Y.1    Seo, J.H.2    Ryu, Y.W.3
  • 12
    • 0032824740 scopus 로고    scopus 로고
    • Production of erythritol from glucose by an osmophilic mutant of Candida magnoliae
    • Yang SW, Park JB, Han NS, Ryu YW, Seo JH. Production of erythritol from glucose by an osmophilic mutant of Candida magnoliae. Biotechnol Lett 1999, 21:887-890.
    • (1999) Biotechnol Lett , vol.21 , pp. 887-890
    • Yang, S.W.1    Park, J.B.2    Han, N.S.3    Ryu, Y.W.4    Seo, J.H.5
  • 13
    • 0346463113 scopus 로고    scopus 로고
    • Scale-up of erythritol production by an osmophilic mutant of Candida magnoliae
    • 10.1023/B:BILE.0000007076.64338.ce, 14969417
    • Koh ES, Leet TH, Lee DY, Kim HJ, Ryu YW, Seo JH. Scale-up of erythritol production by an osmophilic mutant of Candida magnoliae. Biotechnol Lett 2003, 25(24):2103-2105. 10.1023/B:BILE.0000007076.64338.ce, 14969417.
    • (2003) Biotechnol Lett , vol.25 , Issue.24 , pp. 2103-2105
    • Koh, E.S.1    Leet, T.H.2    Lee, D.Y.3    Kim, H.J.4    Ryu, Y.W.5    Seo, J.H.6
  • 14
    • 0001763246 scopus 로고
    • Purification and some properties of an erythrose reductase from an Aureobasidium sp. mutant
    • Isuizuka H, Tokuoka K, Sasaki T, Taniguchi H. Purification and some properties of an erythrose reductase from an Aureobasidium sp. mutant. Biosci Biotechnol Biochem 1992, 56(6):941-945.
    • (1992) Biosci Biotechnol Biochem , vol.56 , Issue.6 , pp. 941-945
    • Isuizuka, H.1    Tokuoka, K.2    Sasaki, T.3    Taniguchi, H.4
  • 15
    • 0026784835 scopus 로고
    • Comparison of three-forms of erythrose reductase from an Aureobasidium sp. mutant
    • Tokuoka K, Ishizuka H, Wako K, Taniguchi H. Comparison of three-forms of erythrose reductase from an Aureobasidium sp. mutant. J Gen Appl Microbiol 1992, 38(22):145-155.
    • (1992) J Gen Appl Microbiol , vol.38 , Issue.22 , pp. 145-155
    • Tokuoka, K.1    Ishizuka, H.2    Wako, K.3    Taniguchi, H.4
  • 16
    • 22444438054 scopus 로고    scopus 로고
    • Primary structure analysis and functional expression of erythrose reductases from erythritol-producing fungi (Trichosporonoides megachiliensis SNG-42)
    • 10.1271/bbb.69.944, 15914914
    • Ookura T, Azuma K, Isshiki K, Taniguchi H, Kasumi T, Kawamura Y. Primary structure analysis and functional expression of erythrose reductases from erythritol-producing fungi (Trichosporonoides megachiliensis SNG-42). Biosci Biotechnol Biochem 2005, 69(5):944-951. 10.1271/bbb.69.944, 15914914.
    • (2005) Biosci Biotechnol Biochem , vol.69 , Issue.5 , pp. 944-951
    • Ookura, T.1    Azuma, K.2    Isshiki, K.3    Taniguchi, H.4    Kasumi, T.5    Kawamura, Y.6
  • 17
    • 0037357735 scopus 로고    scopus 로고
    • Purification and properties of a NADPH-dependent erythrose reductase from the newly isolated Troula corallina
    • 10.1021/bp025680j, 12675593
    • Lee JK, Hong KW, Kim SY. Purification and properties of a NADPH-dependent erythrose reductase from the newly isolated Troula corallina. Biotechnol Prog 2003, 19:495-500. 10.1021/bp025680j, 12675593.
    • (2003) Biotechnol Prog , vol.19 , pp. 495-500
    • Lee, J.K.1    Hong, K.W.2    Kim, S.Y.3
  • 18
    • 0038493652 scopus 로고    scopus 로고
    • Purification and characterization of a novel erythrose reductase from Candida magnoliae
    • 10.1128/AEM.69.7.3710-3718.2003, 165123, 12839736
    • Lee JK, Kim SY, Ryu YW, Seo JH, Kim JH. Purification and characterization of a novel erythrose reductase from Candida magnoliae. Appl Environ Microbiol 2003, 69(7):3710-3718. 10.1128/AEM.69.7.3710-3718.2003, 165123, 12839736.
    • (2003) Appl Environ Microbiol , vol.69 , Issue.7 , pp. 3710-3718
    • Lee, J.K.1    Kim, S.Y.2    Ryu, Y.W.3    Seo, J.H.4    Kim, J.H.5
  • 19
    • 0023375195 scopus 로고
    • The neighbor-joining method: a new method for reconstructing phylogenetic trees
    • Saitou N, Nei M. The neighbor-joining method: a new method for reconstructing phylogenetic trees. Mol Biol Evol 1987, 4(4):406-425.
    • (1987) Mol Biol Evol , vol.4 , Issue.4 , pp. 406-425
    • Saitou, N.1    Nei, M.2
  • 20
    • 0037465661 scopus 로고    scopus 로고
    • High-level expression and rapid purification of rare-codon genes from hyperthermophilic archaea by the GST gene fusion system
    • 10.1016/S1570-0232(02)00810-3, 12651013
    • Wu X, Oppermann U. High-level expression and rapid purification of rare-codon genes from hyperthermophilic archaea by the GST gene fusion system. J Chromatogr B Analyt Technol Biomed Life Sci 2003, 786(1-2):177-185. 10.1016/S1570-0232(02)00810-3, 12651013.
    • (2003) J Chromatogr B Analyt Technol Biomed Life Sci , vol.786 , Issue.1-2 , pp. 177-185
    • Wu, X.1    Oppermann, U.2
  • 21
    • 1242309283 scopus 로고    scopus 로고
    • Consortium of fold-catalyzing proteins increases soluble expression of cyclohexanone monooxygenase in recombinant Escherichia coli
    • 10.1007/s00253-003-1370-z, 12827321
    • Lee DH, Kim MD, Lee WH, Kweon DH, Seo JH. Consortium of fold-catalyzing proteins increases soluble expression of cyclohexanone monooxygenase in recombinant Escherichia coli. Appl Microbiol Biotechnol 2004, 63(5):549-552. 10.1007/s00253-003-1370-z, 12827321.
    • (2004) Appl Microbiol Biotechnol , vol.63 , Issue.5 , pp. 549-552
    • Lee, D.H.1    Kim, M.D.2    Lee, W.H.3    Kweon, D.H.4    Seo, J.H.5
  • 22
    • 18144376288 scopus 로고    scopus 로고
    • Coexpression of folding accessory proteins for production of active cyclodextrin glycosyltransferase of Bacillus macerans in recombinant Escherichia coli
    • Kim SG, Kweon DH, Lee DH, Park YC, Seo JH. Coexpression of folding accessory proteins for production of active cyclodextrin glycosyltransferase of Bacillus macerans in recombinant Escherichia coli. Protein Expres Pur 2005, 41(2):426-432.
    • (2005) Protein Expres Pur , vol.41 , Issue.2 , pp. 426-432
    • Kim, S.G.1    Kweon, D.H.2    Lee, D.H.3    Park, Y.C.4    Seo, J.H.5
  • 23
    • 0031860811 scopus 로고    scopus 로고
    • Chaperone coexpression plasmids: differential and synergistic roles of DnaK-DnaJ-GrpE and GroEL-GroES in assisting folding of an allergen of Japanese cedar pollen, Cryj2, in Escherichia coli
    • 106217, 9572938
    • Nishihara K, Kanemori M, Kitagawa M, Yanagi H, Yura T. Chaperone coexpression plasmids: differential and synergistic roles of DnaK-DnaJ-GrpE and GroEL-GroES in assisting folding of an allergen of Japanese cedar pollen, Cryj2, in Escherichia coli. Appl Environ Microbiol 1998, 64(5):1694-1699. 106217, 9572938.
    • (1998) Appl Environ Microbiol , vol.64 , Issue.5 , pp. 1694-1699
    • Nishihara, K.1    Kanemori, M.2    Kitagawa, M.3    Yanagi, H.4    Yura, T.5
  • 24
    • 0029294528 scopus 로고
    • An aldose reductase homologous gene from barley: regulation and function
    • 10.1046/j.1365-313X.1995.07050809.x, 7773309
    • Renza R, Francesco S, Dorothea B. An aldose reductase homologous gene from barley: regulation and function. Plant J 1995, 7(5):809-822. 10.1046/j.1365-313X.1995.07050809.x, 7773309.
    • (1995) Plant J , vol.7 , Issue.5 , pp. 809-822
    • Renza, R.1    Francesco, S.2    Dorothea, B.3
  • 25
    • 0030821699 scopus 로고    scopus 로고
    • Comparative anatomy of the aldo-keto reductase superfamily
    • 1218714, 9307009
    • Jez JM, Bennett MJ, Schlegel BP, Lewis M, Penning TM. Comparative anatomy of the aldo-keto reductase superfamily. Biochem J 1997, 326(3):625-636. 1218714, 9307009.
    • (1997) Biochem J , vol.326 , Issue.3 , pp. 625-636
    • Jez, J.M.1    Bennett, M.J.2    Schlegel, B.P.3    Lewis, M.4    Penning, T.M.5
  • 26
    • 0031989518 scopus 로고    scopus 로고
    • Purification and characterization of NADPH-dependent carbonyl reductase, involved in stereoselective reduction of ethyl 4-chloro-3-oxobutanoate, from Candida magnoliae
    • 10.1271/bbb.62.280, 9532783
    • Wada M, Kataoka M, Kawabata H, Yasohara Y, Kizaki N, Hasegawa J, Shimizu S. Purification and characterization of NADPH-dependent carbonyl reductase, involved in stereoselective reduction of ethyl 4-chloro-3-oxobutanoate, from Candida magnoliae. Biosci Biotechnol Biochem 1998, 62(2):280-285. 10.1271/bbb.62.280, 9532783.
    • (1998) Biosci Biotechnol Biochem , vol.62 , Issue.2 , pp. 280-285
    • Wada, M.1    Kataoka, M.2    Kawabata, H.3    Yasohara, Y.4    Kizaki, N.5    Hasegawa, J.6    Shimizu, S.7
  • 28
    • 0036731755 scopus 로고    scopus 로고
    • Fumarate-mediated inhibition of erythrose reductase, a key enzyme for erythritol production by Torula corallina
    • 10.1128/AEM.68.9.4534-4538.2002, 124133, 12200310
    • Lee JK, Koo BS, Kim SY. Fumarate-mediated inhibition of erythrose reductase, a key enzyme for erythritol production by Torula corallina. Appl Environ Microbiol 2002, 68(9):4534-4538. 10.1128/AEM.68.9.4534-4538.2002, 124133, 12200310.
    • (2002) Appl Environ Microbiol , vol.68 , Issue.9 , pp. 4534-4538
    • Lee, J.K.1    Koo, B.S.2    Kim, S.Y.3
  • 29
    • 0030881429 scopus 로고    scopus 로고
    • NAD(P)H-dependent aldose reductase from the xylose-assimilating yeast Candida tenuis. Isolation, characterization and biochemical properties of the enzyme
    • 1218722, 9307017
    • Neuhauser W, Haltrich D, Kulbe K, Nidetzky B. NAD(P)H-dependent aldose reductase from the xylose-assimilating yeast Candida tenuis. Isolation, characterization and biochemical properties of the enzyme. Biochem J 1997, 326(Pt 3):683-692. 1218722, 9307017.
    • (1997) Biochem J , vol.326 , Issue.PART 3 , pp. 683-692
    • Neuhauser, W.1    Haltrich, D.2    Kulbe, K.3    Nidetzky, B.4
  • 30
    • 0021959310 scopus 로고
    • Properties of the NAD(P)H-dependent xylose reductase from the xylose-fermenting yeast Pichia stipitis
    • 1144764, 3921014
    • Verduyn C, Van Kleef R, Frank J, Schreuder H, Van Dijken J, Scheffers W. Properties of the NAD(P)H-dependent xylose reductase from the xylose-fermenting yeast Pichia stipitis. Biochem J 1985, 226(3):669-677. 1144764, 3921014.
    • (1985) Biochem J , vol.226 , Issue.3 , pp. 669-677
    • Verduyn, C.1    Van Kleef, R.2    Frank, J.3    Schreuder, H.4    Van Dijken, J.5    Scheffers, W.6
  • 31
    • 0020461029 scopus 로고
    • Purification and characterization of human-brain aldose reductase
    • 10.1111/j.1432-1033.1982.tb06867.x, 6814912
    • Bendicht W, Hanspeter B, Kurt B, Jean-Pierre W. Purification and characterization of human-brain aldose reductase. Eur J Biochem 1982, 127(2):279-284. 10.1111/j.1432-1033.1982.tb06867.x, 6814912.
    • (1982) Eur J Biochem , vol.127 , Issue.2 , pp. 279-284
    • Bendicht, W.1    Hanspeter, B.2    Kurt, B.3    Jean-Pierre, W.4
  • 32
    • 0014599195 scopus 로고
    • Erythritol metabolism in wild-type and mutant strains of Schizophyllum commune
    • 250136, 4390964
    • Braun ML, Niederpruem DJ. Erythritol metabolism in wild-type and mutant strains of Schizophyllum commune. J Bacteriol 1969, 100(2):625-634. 250136, 4390964.
    • (1969) J Bacteriol , vol.100 , Issue.2 , pp. 625-634
    • Braun, M.L.1    Niederpruem, D.J.2
  • 33
    • 0028222097 scopus 로고
    • Tyrosine-48 is the proton donor and histidine-110 directs substrate stereochemical selectivity in the reduction reaction of human aldose reductase: enzyme kinetics and crystal structure of the Y48H mutant enzyme
    • 10.1021/bi00174a007, 8117659
    • Bohren K, Grimshaw C, Lai C, Harrison D, Ringe D, Petsko G, Gabbay K. Tyrosine-48 is the proton donor and histidine-110 directs substrate stereochemical selectivity in the reduction reaction of human aldose reductase: enzyme kinetics and crystal structure of the Y48H mutant enzyme. Biochemistry 1994, 33(8):2021-2032. 10.1021/bi00174a007, 8117659.
    • (1994) Biochemistry , vol.33 , Issue.8 , pp. 2021-2032
    • Bohren, K.1    Grimshaw, C.2    Lai, C.3    Harrison, D.4    Ringe, D.5    Petsko, G.6    Gabbay, K.7
  • 34
    • 0027431819 scopus 로고
    • Probing the active site of human aldose reductase. Site-directed mutagenesis of Asp-43, Tyr-48, Lys-77, and His-110
    • Tarle I, Borhani DW, Wilson DK, Quiocho FA, Petrash JM. Probing the active site of human aldose reductase. Site-directed mutagenesis of Asp-43, Tyr-48, Lys-77, and His-110. J Biol Chem 1993, 268(34):25687-25693.
    • (1993) J Biol Chem , vol.268 , Issue.34 , pp. 25687-25693
    • Tarle, I.1    Borhani, D.W.2    Wilson, D.K.3    Quiocho, F.A.4    Petrash, J.M.5
  • 35
    • 0026344829 scopus 로고
    • Expression of human aldose and aldehyde reductases. Site-directed mutagenesis of a critical lysine 262
    • Bohren KM, Page JL, Shankar R, Henry SP, Gabbay KH. Expression of human aldose and aldehyde reductases. Site-directed mutagenesis of a critical lysine 262. J Biol Chem 1991, 266(35):24031-24037.
    • (1991) J Biol Chem , vol.266 , Issue.35 , pp. 24031-24037
    • Bohren, K.M.1    Page, J.L.2    Shankar, R.3    Henry, S.P.4    Gabbay, K.H.5
  • 36
    • 0026443085 scopus 로고
    • The crystal structure of the aldose reductase. NADPH binary complex
    • Borhani DW, Harter TM, Petrash JM. The crystal structure of the aldose reductase. NADPH binary complex. J Biol Chem 1992, 267(34):24841-24847.
    • (1992) J Biol Chem , vol.267 , Issue.34 , pp. 24841-24847
    • Borhani, D.W.1    Harter, T.M.2    Petrash, J.M.3
  • 37
    • 0026531024 scopus 로고
    • Novel NADPH-binding domain revealed by the crystal structure of aldose reductase
    • 10.1038/355469a0, 1734286
    • Rondeau J, Tete-Favier F, Podjarny A, Reymann J, Barth P, Biellmann J, Moras D. Novel NADPH-binding domain revealed by the crystal structure of aldose reductase. Nature 1992, 355(6359):469-472. 10.1038/355469a0, 1734286.
    • (1992) Nature , vol.355 , Issue.6359 , pp. 469-472
    • Rondeau, J.1    Tete-Favier, F.2    Podjarny, A.3    Reymann, J.4    Barth, P.5    Biellmann, J.6    Moras, D.7
  • 38
    • 0017406572 scopus 로고
    • Purification and properties of NADPH-dependent aldehyde reductase from human liver
    • Wermuth B, Munch J, von Wartburg J. Purification and properties of NADPH-dependent aldehyde reductase from human liver. J Biol Chem 1977, 252(11):3821-3828.
    • (1977) J Biol Chem , vol.252 , Issue.11 , pp. 3821-3828
    • Wermuth, B.1    Munch, J.2    von Wartburg, J.3
  • 40
    • 0036213581 scopus 로고    scopus 로고
    • Alteration of the specificity of the cofactor-binding pocket of Corynebacterium 2,5-diketo-D-gluconic acid reductase A
    • 10.1093/protein/15.2.131, 11917149
    • Banta S, Swanson BA, Wu S, Jarnagin A, Anderson S. Alteration of the specificity of the cofactor-binding pocket of Corynebacterium 2,5-diketo-D-gluconic acid reductase A. Protein Eng 2002, 15(2):131-140. 10.1093/protein/15.2.131, 11917149.
    • (2002) Protein Eng , vol.15 , Issue.2 , pp. 131-140
    • Banta, S.1    Swanson, B.A.2    Wu, S.3    Jarnagin, A.4    Anderson, S.5
  • 41
    • 0029017363 scopus 로고
    • Studies on human aldose reductase
    • 10.1074/jbc.270.28.16911, 7622508
    • Kubiseski TJ, Flynn TG. Studies on human aldose reductase. J Biol Chem 1995, 270(28):16911-16917. 10.1074/jbc.270.28.16911, 7622508.
    • (1995) J Biol Chem , vol.270 , Issue.28 , pp. 16911-16917
    • Kubiseski, T.J.1    Flynn, T.G.2
  • 42
    • 12844287005 scopus 로고    scopus 로고
    • The coenzyme specificity of Candida tenuis xylose reductase (AKR2B5) explored by site-directed mutagenesis and X-ray crystallography
    • 1134675, 15320875
    • Petschacher B, Leitgeb S, Kavanagh KL, Wilson DK, B N. The coenzyme specificity of Candida tenuis xylose reductase (AKR2B5) explored by site-directed mutagenesis and X-ray crystallography. Biochem J 2005, 385(Pt 1):75-83. 1134675, 15320875.
    • (2005) Biochem J , vol.385 , Issue.PART 1 , pp. 75-83
    • Petschacher, B.1    Leitgeb, S.2    Kavanagh, K.L.3    Wilson, D.K.4    B, N.5
  • 43
    • 65549138558 scopus 로고    scopus 로고
    • Folding machineries displayed on a cation-exchanger for the concerted refolding of cysteine- or proline-rich proteins
    • 10.1186/1472-6750-9-27, 2676282, 19323835
    • Lee DH, Kim SG, Kweon DH, Seo JH. Folding machineries displayed on a cation-exchanger for the concerted refolding of cysteine- or proline-rich proteins. BMC Biotechnol 2009, 9(1):27-36. 10.1186/1472-6750-9-27, 2676282, 19323835.
    • (2009) BMC Biotechnol , vol.9 , Issue.1 , pp. 27-36
    • Lee, D.H.1    Kim, S.G.2    Kweon, D.H.3    Seo, J.H.4
  • 44
    • 0032568655 scopus 로고    scopus 로고
    • SMART, a simple modular architecture research tool: Identification of signaling domains
    • 10.1073/pnas.95.11.5857, 34487, 9600884
    • Schultz J, Milpetz F, Bork P, Ponting CP. SMART, a simple modular architecture research tool: Identification of signaling domains. Proc Natl Acad Sci 1998, 95(11):5857-5864. 10.1073/pnas.95.11.5857, 34487, 9600884.
    • (1998) Proc Natl Acad Sci , vol.95 , Issue.11 , pp. 5857-5864
    • Schultz, J.1    Milpetz, F.2    Bork, P.3    Ponting, C.P.4
  • 45
  • 46
    • 3242810318 scopus 로고    scopus 로고
    • MEGA3: integrated software for molecular evolutionary genetics analysis and sequence alignment
    • 10.1093/bib/5.2.150, 15260895
    • Kumar S, Tamura K, Nei M. MEGA3: integrated software for molecular evolutionary genetics analysis and sequence alignment. Brief Bioinform 2004, 5(2):150-163. 10.1093/bib/5.2.150, 15260895.
    • (2004) Brief Bioinform , vol.5 , Issue.2 , pp. 150-163
    • Kumar, S.1    Tamura, K.2    Nei, M.3
  • 47
    • 0034818755 scopus 로고    scopus 로고
    • Taking variation of evolutionary rates between sites into account in inferring phylogenies
    • 10.1007/s002390010234, 11675604
    • Felsenstein J. Taking variation of evolutionary rates between sites into account in inferring phylogenies. J Mol Evol 2001, 53(4-5):447-455. 10.1007/s002390010234, 11675604.
    • (2001) J Mol Evol , vol.53 , Issue.4-5 , pp. 447-455
    • Felsenstein, J.1
  • 48
    • 0014949207 scopus 로고
    • Cleavage of structural proteins during the assembly of the head of bacteriophage T4
    • 10.1038/227680a0, 5432063
    • Laemmli UK. Cleavage of structural proteins during the assembly of the head of bacteriophage T4. Nature 1970, 227(5259):680-685. 10.1038/227680a0, 5432063.
    • (1970) Nature , vol.227 , Issue.5259 , pp. 680-685
    • Laemmli, U.K.1
  • 49
    • 84962865167 scopus 로고    scopus 로고
    • Yeast Gcy1p reduces erythrose and erythrose-4-phosphate
    • Ookura T, Kasumi T. Yeast Gcy1p reduces erythrose and erythrose-4-phosphate. Rep Natl Food Res Inst 2007, 71:57-60.
    • (2007) Rep Natl Food Res Inst , vol.71 , pp. 57-60
    • Ookura, T.1    Kasumi, T.2


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.