메뉴 건너뛰기




Volumn 104, Issue 5, 2009, Pages 911-919

Construction of Hansenula polymorpha strains with improved thermotolerance

Author keywords

ATH1; Ethanolic fermentation of xylose; Hansenula polymorpha; High temperature tolerance; HSP104; HSP16

Indexed keywords

ATH1; ETHANOLIC FERMENTATION OF XYLOSE; HANSENULA POLYMORPHA; HIGH-TEMPERATURE TOLERANCE; HSP104; HSP16;

EID: 70350558410     PISSN: 00063592     EISSN: 10970290     Source Type: Journal    
DOI: 10.1002/bit.22457     Document Type: Article
Times cited : (46)

References (50)
  • 1
    • 0034615921 scopus 로고    scopus 로고
    • A stretch of positively charged amino acids at the N terminals of Hansenula polymorpha Pex3p is involved in incorporation of the protein into the peroxisomal membrane
    • DOI 10.1074/jbc.275.14.9986
    • Baerends RJ, Faber KN, Kram AM, Kiel JA, van der Klei IJ, Veenhuis M. 2000. A stretch of positively charged amino acids at the N terminus of Hansenula polymorpha Pex3p is involved in incorporation of the protein into the peroxisomal membrane. J Biol Chem 275(14):9986-9995. (Pubitemid 30202045)
    • (2000) Journal of Biological Chemistry , vol.275 , Issue.14 , pp. 9986-9995
    • Baerends, R.J.S.1    Faber, K.N.2    Kram, A.M.3    Kiel, J.A.K.W.4    Van Der Klei, I.J.5    Veenhuis, M.6
  • 2
    • 37549072150 scopus 로고    scopus 로고
    • Co-purification of glucanase with acid trehalase-invertase aggregate in Saccharomyces cerevisiae
    • Basu A, Chaudhuri P, Malakar D, Ghosh AK. 2008. Co-purification of glucanase with acid trehalase-invertase aggregate in Saccharomyces cerevisiae. Biotechnol Lett 30(2):299-304.
    • (2008) Biotechnol Lett , vol.30 , Issue.2 , pp. 299-304
    • Basu, A.1    Chaudhuri, P.2    Malakar, D.3    Ghosh, A.K.4
  • 3
    • 0028270766 scopus 로고
    • Trehalose-6-P synthase is dispensable for growth on glucose but not for spore germination in Schizosaccharomyces pombe
    • Blázquez MA, Stucka R, Feldmann H, Gancedo C. 1994. Trehalose-6-P synthase is dispensable for growth on glucose but not for spore germination in Schizosaccharomyces pombe. J Bacteriol 176(13): 3895-3902. (Pubitemid 24191272)
    • (1994) Journal of Bacteriology , vol.176 , Issue.13 , pp. 3895-3902
    • Blazquez, M.A.1    Stucka, R.2    Feldmann, H.3    Gancedo, C.4
  • 4
    • 0033037610 scopus 로고    scopus 로고
    • The heat shock response in yeast: Differential regulations and contributions of the Msn2p/Msn4p and Hsf1p regulons
    • DOI 10.1046/j.1365-2958.1999.01467.x
    • Boy-Marcotte E, Lagniel G, Perrot M, Bussereau F, Boudsocq A, Jacquet M, Labarre J. 1999. The heat shock response in yeast: Differential regulations and contributions of the Msn2p/Msn4p and Hsf1p regulons. Mol Microbiol 33(2):274-283. (Pubitemid 29322514)
    • (1999) Molecular Microbiology , vol.33 , Issue.2 , pp. 274-283
    • Boy-Marcotte, E.1    Lagniel, G.2    Perrot, M.3    Bussereau, F.4    Boudsocq, A.5    Jacquet, M.6    Labarre, J.7
  • 5
    • 13944259772 scopus 로고    scopus 로고
    • Role of trehalose and heat in the structure of the C-terminal activation domain of the heat shock transcription factor
    • Bulman AL, Nelson HC. 2005. Role of trehalose and heat in the structure of the C-terminal activation domain of the heat shock transcription factor. Proteins 58(4):826-835.
    • (2005) Proteins , vol.58 , Issue.4 , pp. 826-835
    • Bulman, A.L.1    Nelson, H.C.2
  • 6
    • 0021346412 scopus 로고
    • Temperature relations of yield, growth and thermal death in the yeast Hansenula polymorpha
    • Cabeca-Silva C, Madiera-Lopes A. 1984. Temperature relations of yield, growth and thermal death in the yeast Hansenula polymorpha. Z Allg Mikrobiol 24:129-132. (Pubitemid 14142173)
    • (1984) Zeitschrift fur Allgemeine Mikrobiologie , vol.24 , Issue.2 , pp. 129-132
    • Cabeca-Silva, C.1    Madeira-Lopes, A.2
  • 7
    • 21244466032 scopus 로고    scopus 로고
    • A chaperone pathway in protein disaggregation: HSP26 alteks the nature of protein aggregates to facilitate reactivation by HSP104
    • DOI 10.1074/jbc.M502854200
    • Cashikar AG, Duennwald M, Lindquist SL. 2005. A chaperone pathway in protein disaggregation. Hsp26 alters the nature of protein aggregates to facilitate reactivation by Hsp104. J Biol Chem 280(25):23869-23875. (Pubitemid 40884874)
    • (2005) Journal of Biological Chemistry , vol.280 , Issue.25 , pp. 23869-23875
    • Cashikar, A.G.1    Duennwald, M.2    Lindquist, S.L.3
  • 8
    • 33846909430 scopus 로고    scopus 로고
    • The natural osmolyte trehalose is a positive regulator of the heat-induced activity of yeast heat shock transcription factor
    • Conlin LK, Nelson HC. 2007. The natural osmolyte trehalose is a positive regulator of the heat-induced activity of yeast heat shock transcription factor. Mol Cell Biol 27(4):1505-1515.
    • (2007) Mol Cell Biol , vol.27 , Issue.4 , pp. 1505-1515
    • Conlin, L.K.1    Nelson, H.C.2
  • 9
    • 38349193136 scopus 로고    scopus 로고
    • Overexpression of bacterial xylose isomerase and yeast host xylulokinase improves xylose alcoholic fermentation in the thermotolerant yeast Hansenula polymorpha
    • Dmytruk OV, Voronovsky AY, Abbas CA, Dmytruk KV, Ishchuk OP, Sibirny AA. 2008a. Overexpression of bacterial xylose isomerase and yeast host xylulokinase improves xylose alcoholic fermentation in the thermotolerant yeast Hansenula polymorpha. FEMS Yeast Res 8:165-173.
    • (2008) FEMS Yeast Res , vol.8 , pp. 165-173
    • Dmytruk, O.V.1    Voronovsky, A.Y.2    Abbas, C.A.3    Dmytruk, K.V.4    Ishchuk, O.P.5    Sibirny, A.A.6
  • 10
    • 49749098829 scopus 로고    scopus 로고
    • Engineering of xylose reductase and overexpression of xylitol dehydrogenase and xylulokinase improves xylose alcoholic fermentation in the thermotolerant yeast Hansenula polymorpha
    • 10.1186/1475-2859-7-21
    • Dmytruk OV, Dmytruk KV, Abbas CA, Voronovsky AY, Sibirny AA. 2008b. Engineering of xylose reductase and overexpression of xylitol dehydrogenase and xylulokinase improves xylose alcoholic fermentation in the thermotolerant yeast Hansenula polymorpha. Microb Cell Fact 7:21. 10.1186/1475-2859-7-21.
    • (2008) Microb Cell Fact , vol.7 , pp. 21
    • Dmytruk, O.V.1    Dmytruk, K.V.2    Abbas, C.A.3    Voronovsky, A.Y.4    Sibirny, A.A.5
  • 11
    • 33845925240 scopus 로고    scopus 로고
    • Genome-wide analysis reveals new roles for the activation domains of the Saccharomyces cerevisiae heat shock transcription factor (Hsf1) during the transient heat shock response
    • Eastmond DL, Nelson HC. 2006. Genome-wide analysis reveals new roles for the activation domains of the Saccharomyces cerevisiae heat shock transcription factor (Hsf1) during the transient heat shock response. J Biol Chem 281(43):32909-32921.
    • (2006) J Biol Chem , vol.281 , Issue.43 , pp. 32909-32921
    • Eastmond, D.L.1    Nelson, H.C.2
  • 12
    • 0038056150 scopus 로고    scopus 로고
    • New insights on trehalose: A multifunctional molecule
    • DOI 10.1093/glycob/cwg047
    • Elbein AD, Pan YT, Pastuszak I, Carroll D. 2003. New insights on trehalose: A multifunctional molecule. Glycobiology 13(4):17R-27R. (Pubitemid 36592310)
    • (2003) Glycobiology , vol.13 , Issue.4
    • Elbein, A.D.1    Pan, Y.T.2    Pastuszak, I.3    Carroll, D.4
  • 13
    • 0028217090 scopus 로고
    • Highly-efficient electrotransformation of the yeast Hansenula polymorpha
    • Faber KN, Haima P, Harder W, Veenhuis M, Ab G. 1994. Highly-efficient electrotransformation of the yeast Hansenula polymorpha. Curr Genet 25(4):305-310. (Pubitemid 24078028)
    • (1994) Current Genetics , vol.25 , Issue.4 , pp. 305-310
    • Faber, K.N.1    Haima, P.2    Harder, W.3    Veenhuis, M.4    Geert, A.B.5
  • 14
    • 58149333407 scopus 로고    scopus 로고
    • Acid trehalase is involved in intracellular trehalose mobilization during postdiauxic growth and severe saline stress in Saccharomyces cerevisiae
    • Garre E, Pérez-Torrado R, Gimeno-Alcañiz JV, Matallana E. 2009. Acid trehalase is involved in intracellular trehalose mobilization during postdiauxic growth and severe saline stress in Saccharomyces cerevisiae. FEMS Yeast Res 9(1):52-62.
    • (2009) FEMS Yeast Res , vol.9 , Issue.1 , pp. 52-62
    • Garre, E.1    Pérez-Torrado, R.2    Gimeno-Alcañiz, J.V.3    Matallana, E.4
  • 15
    • 0034537455 scopus 로고    scopus 로고
    • Heterologous protein production in methylotrophic yeasts
    • DOI 10.1007/s002530000464
    • Gellissen G. 2000. Heterologous protein production in methylotrophic yeasts. Appl Microbiol Biotechnol 54:741-750. (Pubitemid 32009733)
    • (2000) Applied Microbiology and Biotechnology , vol.54 , Issue.6 , pp. 741-750
    • Gellissen, G.1
  • 17
    • 84990723635 scopus 로고
    • Genetic analysis in the methylotrophic yeast Hansenula polymorpha
    • Gleeson MAG, Sudbery PE. 1988. Genetic analysis in the methylotrophic yeast Hansenula polymorpha. Yeast 4:293-303.
    • (1988) Yeast , vol.4 , pp. 293-303
    • Gleeson, M.A.G.1    Sudbery, P.E.2
  • 18
    • 0032503968 scopus 로고    scopus 로고
    • Hsp104, Hsp70, and Hsp40: A novel chaperone system that rescues previously aggregated proteins
    • DOI 10.1016/S0092-8674(00)81223-4
    • Glover JR, Lindquist S. 1998. Hsp104, Hsp70, and Hsp40: A novel chaperone system that rescues previously aggregated proteins. Cell 94(1):73-82. (Pubitemid 28347471)
    • (1998) Cell , vol.94 , Issue.1 , pp. 73-82
    • Glover, J.R.1    Lindquist, S.2
  • 19
    • 0348133457 scopus 로고    scopus 로고
    • Sensitive method for quantitative determination of hydrogen peroxide and oxidase substrates in biological samples
    • Gonchar MV. 1998. Sensitive method for quantitative determination of hydrogen peroxide and oxidase substrates in biological samples. Ukr Biokhim Zh 70:157-163.
    • (1998) Ukr Biokhim Zh , vol.70 , pp. 157-163
    • Gonchar, M.V.1
  • 21
    • 15844365815 scopus 로고    scopus 로고
    • Hypoxia abolishes transience of the heat-shock response in the methylotrophic yeast Hansenula polymorpha
    • DOI 10.1099/mic.0.27272-0
    • Guerra E, Chye PP, Berardi E, Piper PW. 2005. Hypoxia abolishes transience of the heat-shock response in the methylotrophic yeast Hansenula polymorpha. Microbiology 151(Pt 3):805-811. (Pubitemid 40425015)
    • (2005) Microbiology , vol.151 , Issue.3 , pp. 805-811
    • Guerra, E.1    Chye, P.P.2    Berardi, E.3    Piper, P.W.4
  • 22
    • 28444437367 scopus 로고    scopus 로고
    • Responses of Saccharomyces cerevisiae to thermal stress
    • DOI 10.1002/bit.20600
    • Guyot S, Ferret E, Gervais P. 2005. Responses of Saccharomyces cerevisiae to thermal stress. Biotechnol Bioeng 92(4):403-409. (Pubitemid 41737230)
    • (2005) Biotechnology and Bioengineering , vol.92 , Issue.4 , pp. 403-409
    • Guyot, S.1    Ferret, E.2    Gervais, P.3
  • 23
    • 8844219685 scopus 로고    scopus 로고
    • Roles and applications of small heat shock proteins in the production of recombinant proteins in Escherichia coli
    • DOI 10.1002/bit.20227
    • Han MJ, Park SJ, Park TJ, Lee SY. 2004. Roles and applications of small heat shock proteins in the production of recombinant proteins in Escherichia coli. Biotechnol Bioeng 88(4):426-436. (Pubitemid 39536545)
    • (2004) Biotechnology and Bioengineering , vol.88 , Issue.4 , pp. 426-436
    • Han, M.-J.1    Park, S.J.2    Park, T.J.3    Lee, S.Y.4
  • 25
    • 1442289304 scopus 로고    scopus 로고
    • Hsp42 is the general small heat shock protein in the cytosol of Saccharomyces cerevisiae
    • DOI 10.1038/sj.emboj.7600080
    • Haslbeck M, Braun N, Stromer T, Richter B, Model N, Weinkauf S, Buchner J. 2004. Hsp42 is the general small heat shock protein in the cytosol of Saccharomyces cerevisiae. EMBO J 23(3):638-649. (Pubitemid 38282395)
    • (2004) EMBO Journal , vol.23 , Issue.3 , pp. 638-649
    • Haslbeck, M.1    Braun, N.2    Stromer, T.3    Richter, B.4    Model, N.5    Weinkauf, S.6    Buchner, J.7
  • 27
    • 54049094405 scopus 로고    scopus 로고
    • Overexpression of pyruvate decarboxylase in the yeast Hansenula polymorpha results in increased ethanol yield in high-temperature fermentation of xylose
    • Ishchuk OP, Voronovsky AY, Stasyk OV, Gayda GZ, Gonchar MV, Abbas CA, Sibirny AA. 2008. Overexpression of pyruvate decarboxylase in the yeast Hansenula polymorpha results in increased ethanol yield in high-temperature fermentation of xylose. FEMS Yeast Res 8(7):1167-1174.
    • (2008) FEMS Yeast Res , vol.8 , Issue.7 , pp. 1167-1174
    • Ishchuk, O.P.1    Voronovsky, A.Y.2    Stasyk, O.V.3    Gayda, G.Z.4    Gonchar, M.V.5    Abbas, C.A.6    Sibirny, A.A.7
  • 28
    • 0033769895 scopus 로고    scopus 로고
    • Ethanol and thermotolerance in the bioconversion of xylose by yeasts
    • Jeffries TW, Jin YS. 2000. Ethanol and thermotolerance in the bioconversion of xylose by yeasts. Adv Appl Microbiol 47:221-268.
    • (2000) Adv Appl Microbiol , vol.47 , pp. 221-268
    • Jeffries, T.W.1    Jin, Y.S.2
  • 29
    • 28444455642 scopus 로고    scopus 로고
    • Antisense-mediated inhibition of acid trehalase (ATH1) gene expression promotes ethanol fermentation and tolerance in Saccharomyces cerevisiae
    • Jung YJ, Park HD. 2005. Antisense-mediated inhibition of acid trehalase (ATH1) gene expression promotes ethanol fermentation and tolerance in Saccharomyces cerevisiae. Biotechnol Lett 27(23-24):1855-1859.
    • (2005) Biotechnol Lett , vol.27 , Issue.23-24 , pp. 1855-1859
    • Jung, Y.J.1    Park, H.D.2
  • 30
    • 0019959287 scopus 로고
    • Localization of trehalase in vacuoles and of trehalose in the cytosol of yeast (Saccharomyces cerevisiae)
    • Keller F, Schellenberg M, Wiemken A. 1982. Localization of trehalase in vacuoles and of trehalose in the cytosol of yeast (Saccharomyces cerevisiae). Arch Microbiol 131:298-301.
    • (1982) Arch Microbiol , vol.131 , pp. 298-301
    • Keller, F.1    Schellenberg, M.2    Wiemken, A.3
  • 31
    • 0030002467 scopus 로고    scopus 로고
    • Disruption of the yeast ATH1 gene confers better survival after dehydration, freezing, and ethanol shock: Potential commercial applications
    • Kim J, Alizadeh P, Harding T, Hefner-Gravink A, Klionsky DJ. 1996. Disruption of the yeast ATH1 gene confers better survival after dehydration, freezing, and ethanol shock: Potential commercial applications. Appl Environ Microbiol 62:1563-1569. (Pubitemid 26143424)
    • (1996) Applied and Environmental Microbiology , vol.62 , Issue.5 , pp. 1563-1569
    • Kim, J.1    Alizadeh, P.2    Harding, T.3    Hefner-Gravink, A.4    Klionsky, D.J.5
  • 32
    • 0036315595 scopus 로고    scopus 로고
    • Escherichia coli small heat shock proteins, IbpA and IbpB, protect enzymes from inactivation by heat and oxidants
    • DOI 10.1046/j.1432-1033.2002.02958.x
    • Kitagawa M, Miyakawa M, Matsumura Y, Tsuchido T. 2002. Escherichia coli small heat shock proteins, IbpA and IbpB, protect enzymes from inactivation by heat and oxidants. Eur J Biochem 269(12):2907-2917. (Pubitemid 34754019)
    • (2002) European Journal of Biochemistry , vol.269 , Issue.12 , pp. 2907-2917
    • Kitagawa, M.1    Miyakawa, M.2    Matsumura, Y.3    Tsuchido, T.4
  • 33
    • 0036173641 scopus 로고    scopus 로고
    • Isolation and properties of genetically defined strains of the methylotrophic yeast Hansenula polymorpha CBS4732
    • DOI 10.1007/s00203-001-0370-6
    • Lahtchev KL, Semenova VD, Tolstorukov II, van der Klei I, Veenhuis M. 2002. Isolation and properties of genetically defined strains of the methylotrophic yeast Hansenula polymorpha CBS4732. Arch Microbiol 177:150-158. (Pubitemid 34143414)
    • (2002) Archives of Microbiology , vol.177 , Issue.2 , pp. 150-158
    • Lahtchev, K.L.1    Semenova, V.D.2    Tolstorukov, I.I.3    Van Der Klei, I.4    Veenhuis, M.5
  • 35
    • 0021763252 scopus 로고
    • Characterization of two trehalases in baker's yeast
    • Londesborough J, Varimo K. 1984. Characterization of two trehalases in baker's yeast. Biochem J 219:511-518.
    • (1984) Biochem J , vol.219 , pp. 511-518
    • Londesborough, J.1    Varimo, K.2
  • 37
    • 0029879360 scopus 로고    scopus 로고
    • The Saccharomyces cerevisiae zinc finger proteins Msn2p and Msn4p are required for transcriptional induction through the stress-response element (STRE)
    • Martínez-Pastor MT, Marchler G, Schüller C, Marchler-Bauer A, Ruis H, Estruch F. 1996. The Saccharomyces cerevisiae zinc finger proteins Msn2p and Msn4p are required for transcriptional induction through the stress response element (STRE). EMBO J 15(9):2227-2235. (Pubitemid 26141139)
    • (1996) EMBO Journal , vol.15 , Issue.9 , pp. 2227-2235
    • Martinez-Pastor, M.T.1    Marchler, G.2    Schuller, C.3    Marchler-Bauer, A.4    Ruis, H.5    Estruch, F.6
  • 38
    • 0030008819 scopus 로고    scopus 로고
    • Deletion of the ATH1 gene in Saccharomyces cerevisiae prevents growth on trehalose
    • DOI 10.1016/0014-5793(96)00450-4
    • Nwaka S, Mechler B, Holzer H. 1996. Deletion of the ATH1 gene in Saccharomyces cerevisiae prevents growth on trehalose. FEBS Lett 386(2-3):235-238. (Pubitemid 26170145)
    • (1996) FEBS Letters , vol.386 , Issue.2-3 , pp. 235-238
    • Nwaka, S.1    Mechler, B.2    Holzer, H.3
  • 39
    • 15044352160 scopus 로고    scopus 로고
    • Acid trehalase in yeasts and filamentous fungi: Localization, regulation and physiological function
    • DOI 10.1016/j.femsyr.2005.01.002, Fungal Physiology, Moving Towards Fungal Physionomics
    • Parrou JL, Jules M, Beltran G, Francois J. 2005. Acid trehalase in yeasts and filamentous fungi: Localization, regulation and physiological function. FEMS Yeast Res 5:503-511. (Pubitemid 40380693)
    • (2005) FEMS Yeast Research , vol.5 , Issue.6-7 , pp. 503-511
    • Parrou, J.L.1    Jules, M.2    Beltran, G.3    Francois, J.4
  • 40
    • 0027135501 scopus 로고
    • The function of heat-shock proteins in stress tolerance: Degradation and reactivation of damaged proteins
    • Parsell DA, Lindquist S. 1993. The function of heat-shock proteins in stress tolerance: Degradation and reactivation of damaged proteins. Annu Rev Genet 27:437-496. (Pubitemid 24011359)
    • (1993) Annual Review of Genetics , vol.27 , pp. 437-496
    • Parsell, D.A.1    Lindquist, S.2
  • 41
    • 0032770738 scopus 로고    scopus 로고
    • The thermophilic yeast Hansenula polymorpha does not require trehalose synthesis for growth at high temperatures but does for normal acquisition of thermotolerance
    • Reinders A, Romano I, Wiemken A, De Virgilio C. 1999. The thermophilic yeast Hansenula polymorpha does not require trehalose synthesis for growth at high temperatures but does for normal acquisition of thermotolerance. J Bacteriol 181(15):4665-4668. (Pubitemid 29357951)
    • (1999) Journal of Bacteriology , vol.181 , Issue.15 , pp. 4665-4668
    • Reinders, A.1    Romano, I.2    Wiemken, A.3    De Virgilio, C.4
  • 42
    • 0242576754 scopus 로고    scopus 로고
    • Xylose and cellobiose fermentation to ethanol by the thermotolerant methylotrophic yeast Hansenula polymorpha
    • DOI 10.1016/S1567-1356(03)00146-6
    • Ryabova OB, Chmil OM, Sibirny AA. 2003. Xylose and cellobiose fermentation to ethanol by the thermotolerant methylotrophic yeast Hansenula polymorpha. FEMS Yeast Res 4:157-164. (Pubitemid 37419954)
    • (2003) FEMS Yeast Research , vol.4 , Issue.2 , pp. 157-164
    • Ryabova, O.B.1    Chmil, O.M.2    Sibirny, A.A.3
  • 44
    • 0033537845 scopus 로고    scopus 로고
    • Biochemical characterization of the small heat shock protein IbpB from Escherichia coli
    • Shearstone JR, Baneyx F. 1999. Biochemical characterization of the small heat shock protein IbpB from Escherichia coli. J Biol Chem 274(15):9937-9945. (Pubitemid 129518273)
    • (1999) Journal of Biological Chemistry , vol.274 , Issue.15 , pp. 9937-9945
    • Shearstone, J.R.1    Baneyx, F.2
  • 48
    • 27644527016 scopus 로고    scopus 로고
    • Expression of xylA genes encoding xylose isomerases from Escherichia coli and Streptomyces coelicolor in the methylotrophic yeast Hansenula polymorpha
    • Voronovsky AY, Ryabova OB, Verba OV, Ishchuk OP, Dmytruk KV, Sibirny AA. 2005. Expression of xylA genes encoding xylose isomerases from Escherichia coli and Streptomyces coelicolor in the methylotrophic yeast Hansenula polymorpha. FEMS Yeast Res 5(11):1055-1062.
    • (2005) FEMS Yeast Res , vol.5 , Issue.11 , pp. 1055-1062
    • Voronovsky, A.Y.1    Ryabova, O.B.2    Verba, O.V.3    Ishchuk, O.P.4    Dmytruk, K.V.5    Sibirny, A.A.6
  • 49
    • 0033199810 scopus 로고    scopus 로고
    • Process design and costing of bioethanol technology: A tool for determining the status and direction of research and development
    • DOI 10.1021/bp990107u
    • Wooley R, Ruth M, Glassner D, Sheehan J. 1999. Process design and costing of bioethanol technology: A tool for determining the status and direction of research and development. Biotechnol Prog 15:794-803. (Pubitemid 29475618)
    • (1999) Biotechnology Progress , vol.15 , Issue.5 , pp. 794-803
    • Wooley, R.1    Ruth, M.2    Glassner, D.3    Sheehan, J.4
  • 50
    • 17844389629 scopus 로고    scopus 로고
    • Hsp16p is required for thermotolerance in nuclear mRNA export in fission yeast Schizosaccharomyces pombe
    • DOI 10.1247/csf.29.125
    • Yoshida J, Tani T. 2005. Hsp16p is required for thermotolerance in nuclear mRNA export in fission yeast Schizosaccharomyces pombe. Cell Struct Funct 29(5-6):125-138. (Pubitemid 40584969)
    • (2005) Cell Structure and Function , vol.29 , Issue.5-6 , pp. 125-138
    • Yoshida, J.-I.1    Tani, T.2


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.