메뉴 건너뛰기




Volumn 9, Issue 10, 2013, Pages

Hsp70-Hsp40 Chaperone Complex Functions in Controlling Polarized Growth by Repressing Hsf1-Driven Heat Stress-Associated Transcription

Author keywords

[No Author keywords available]

Indexed keywords

HEAT SHOCK PROTEIN 40; HEAT SHOCK PROTEIN 70; HEAT SHOCK TRANSCRIPTION FACTOR 1;

EID: 84887283940     PISSN: 15537390     EISSN: 15537404     Source Type: Journal    
DOI: 10.1371/journal.pgen.1003886     Document Type: Article
Times cited : (38)

References (106)
  • 1
    • 78649346692 scopus 로고    scopus 로고
    • The heat shock response: life on the verge of death
    • Richter K, Haslbeck M, Buchner J, (2010) The heat shock response: life on the verge of death. Mol Cell 40: 253-266.
    • (2010) Mol Cell , vol.40 , pp. 253-266
    • Richter, K.1    Haslbeck, M.2    Buchner, J.3
  • 2
    • 0014901006 scopus 로고
    • Patterns of puffing activity in the salivary gland chromosomes of Drosophila. V. Responses to environmental treatments
    • Ashburner M, (1970) Patterns of puffing activity in the salivary gland chromosomes of Drosophila. V. Responses to environmental treatments. Chromosoma 31: 356-376.
    • (1970) Chromosoma , vol.31 , pp. 356-376
    • Ashburner, M.1
  • 3
    • 0018382014 scopus 로고
    • The induction of gene activity in drosophilia by heat shock
    • Ashburner M, Bonner JJ, (1979) The induction of gene activity in drosophilia by heat shock. Cell 17: 241-254.
    • (1979) Cell , vol.17 , pp. 241-254
    • Ashburner, M.1    Bonner, J.J.2
  • 4
    • 0016373748 scopus 로고
    • Protein synthesis in salivary glands of Drosophila melanogaster: relation to chromosome puffs
    • Tissieres A, Mitchell HK, Tracy UM, (1974) Protein synthesis in salivary glands of Drosophila melanogaster: relation to chromosome puffs. J Mol Biol 84: 389-398.
    • (1974) J Mol Biol , vol.84 , pp. 389-398
    • Tissieres, A.1    Mitchell, H.K.2    Tracy, U.M.3
  • 6
    • 0033637153 scopus 로고    scopus 로고
    • Genomic expression programs in the response of yeast cells to environmental changes
    • Gasch AP, Spellman PT, Kao CM, Carmel-Harel O, Eisen MB, et al. (2000) Genomic expression programs in the response of yeast cells to environmental changes. Mol Biol Cell 11: 4241-4257.
    • (2000) Mol Biol Cell , vol.11 , pp. 4241-4257
    • Gasch, A.P.1    Spellman, P.T.2    Kao, C.M.3    Carmel-Harel, O.4    Eisen, M.B.5
  • 7
    • 84866485942 scopus 로고    scopus 로고
    • Cellular response to heat shock studied by multiconfocal fluorescence correlation spectroscopy
    • Kloster-Landsberg M, Herbomel G, Wang I, Derouard J, Vourc'h C, et al. (2012) Cellular response to heat shock studied by multiconfocal fluorescence correlation spectroscopy. Biophys J 103: 1110-1119.
    • (2012) Biophys J , vol.103 , pp. 1110-1119
    • Kloster-Landsberg, M.1    Herbomel, G.2    Wang, I.3    Derouard, J.4    Vourc'h, C.5
  • 8
    • 78650250161 scopus 로고    scopus 로고
    • Recruitment timing and dynamics of transcription factors at the Hsp70 loci in living cells
    • Zobeck KL, Buckley MS, Zipfel WR, Lis JT, (2010) Recruitment timing and dynamics of transcription factors at the Hsp70 loci in living cells. Mol Cell 40: 965-975.
    • (2010) Mol Cell , vol.40 , pp. 965-975
    • Zobeck, K.L.1    Buckley, M.S.2    Zipfel, W.R.3    Lis, J.T.4
  • 9
    • 0027958045 scopus 로고
    • Crystal structure of the DNA binding domain of the heat shock transcription factor
    • Harrison CJ, Bohm AA, Nelson HC, (1994) Crystal structure of the DNA binding domain of the heat shock transcription factor. Science 263: 224-227.
    • (1994) Science , vol.263 , pp. 224-227
    • Harrison, C.J.1    Bohm, A.A.2    Nelson, H.C.3
  • 10
    • 0024282785 scopus 로고
    • Yeast heat shock factor is an essential DNA-binding protein that exhibits temperature-dependent phosphorylation
    • Sorger PK, Pelham HR, (1988) Yeast heat shock factor is an essential DNA-binding protein that exhibits temperature-dependent phosphorylation. Cell 54: 855-864.
    • (1988) Cell , vol.54 , pp. 855-864
    • Sorger, P.K.1    Pelham, H.R.2
  • 11
    • 0027439593 scopus 로고
    • Heat shock factor is required for growth at normal temperatures in the fission yeast Schizosaccharomyces pombe
    • Gallo GJ, Prentice H, Kingston RE, (1993) Heat shock factor is required for growth at normal temperatures in the fission yeast Schizosaccharomyces pombe. Molecular and cellular biology 13: 749-761.
    • (1993) Molecular and Cellular Biology , vol.13 , pp. 749-761
    • Gallo, G.J.1    Prentice, H.2    Kingston, R.E.3
  • 12
    • 51649128089 scopus 로고    scopus 로고
    • Neurospora crassa heat shock factor 1 Is an essential gene; a second heat shock factor-like gene, hsf2, is required for asexual spore formation
    • Thompson S, Croft NJ, Sotiriou A, Piggins HD, Crosthwaite SK, (2008) Neurospora crassa heat shock factor 1 Is an essential gene; a second heat shock factor-like gene, hsf2, is required for asexual spore formation. Eukaryotic cell 7: 1573-1581.
    • (2008) Eukaryotic Cell , vol.7 , pp. 1573-1581
    • Thompson, S.1    Croft, N.J.2    Sotiriou, A.3    Piggins, H.D.4    Crosthwaite, S.K.5
  • 13
    • 0030985251 scopus 로고    scopus 로고
    • Multiple functions of Drosophila heat shock transcription factor in vivo
    • Jedlicka P, Mortin MA, Wu C, (1997) Multiple functions of Drosophila heat shock transcription factor in vivo. The EMBO journal 16: 2452-2462.
    • (1997) The EMBO Journal , vol.16 , pp. 2452-2462
    • Jedlicka, P.1    Mortin, M.A.2    Wu, C.3
  • 14
    • 0033229880 scopus 로고    scopus 로고
    • HSF1 is required for extra-embryonic development, postnatal growth and protection during inflammatory responses in mice
    • Xiao X, Zuo X, Davis AA, McMillan DR, Curry BB, et al. (1999) HSF1 is required for extra-embryonic development, postnatal growth and protection during inflammatory responses in mice. The EMBO journal 18: 5943-5952.
    • (1999) The EMBO Journal , vol.18 , pp. 5943-5952
    • Xiao, X.1    Zuo, X.2    Davis, A.A.3    McMillan, D.R.4    Curry, B.B.5
  • 15
    • 79959463520 scopus 로고    scopus 로고
    • Regulation of HSF1 function in the heat stress response: implications in aging and disease
    • Anckar J, Sistonen L, (2011) Regulation of HSF1 function in the heat stress response: implications in aging and disease. Annu Rev Biochem 80: 1089-1115.
    • (2011) Annu Rev Biochem , vol.80 , pp. 1089-1115
    • Anckar, J.1    Sistonen, L.2
  • 16
    • 0026665975 scopus 로고
    • The human heat shock protein hsp70 interacts with HSF, the transcription factor that regulates heat shock gene expression
    • Abravaya K, Myers MP, Murphy SP, Morimoto RI, (1992) The human heat shock protein hsp70 interacts with HSF, the transcription factor that regulates heat shock gene expression. Genes Dev 6: 1153-1164.
    • (1992) Genes Dev , vol.6 , pp. 1153-1164
    • Abravaya, K.1    Myers, M.P.2    Murphy, S.P.3    Morimoto, R.I.4
  • 17
    • 0026750001 scopus 로고
    • Heat shock gene regulation by nascent polypeptides and denatured proteins: hsp70 as a potential autoregulatory factor
    • Baler R, Welch WJ, Voellmy R, (1992) Heat shock gene regulation by nascent polypeptides and denatured proteins: hsp70 as a potential autoregulatory factor. J Cell Biol 117: 1151-1159.
    • (1992) J Cell Biol , vol.117 , pp. 1151-1159
    • Baler, R.1    Welch, W.J.2    Voellmy, R.3
  • 18
    • 0032555685 scopus 로고    scopus 로고
    • Repression of heat shock transcription factor HSF1 activation by HSP90 (HSP90 complex) that forms a stress-sensitive complex with HSF1
    • Zou J, Guo Y, Guettouche T, Smith DF, Voellmy R, (1998) Repression of heat shock transcription factor HSF1 activation by HSP90 (HSP90 complex) that forms a stress-sensitive complex with HSF1. Cell 94: 471-480.
    • (1998) Cell , vol.94 , pp. 471-480
    • Zou, J.1    Guo, Y.2    Guettouche, T.3    Smith, D.F.4    Voellmy, R.5
  • 19
    • 0035824621 scopus 로고    scopus 로고
    • Evidence for a mechanism of repression of heat shock factor 1 transcriptional activity by a multichaperone complex
    • Guo Y, Guettouche T, Fenna M, Boellmann F, Pratt WB, et al. (2001) Evidence for a mechanism of repression of heat shock factor 1 transcriptional activity by a multichaperone complex. J Biol Chem 276: 45791-45799.
    • (2001) J Biol Chem , vol.276 , pp. 45791-45799
    • Guo, Y.1    Guettouche, T.2    Fenna, M.3    Boellmann, F.4    Pratt, W.B.5
  • 20
    • 0028813131 scopus 로고
    • An efficient method to isolate yeast genes causing overexpression-mediated growth arrest
    • Espinet C, de la Torre MA, Aldea M, Herrero E, (1995) An efficient method to isolate yeast genes causing overexpression-mediated growth arrest. Yeast 11: 25-32.
    • (1995) Yeast , vol.11 , pp. 25-32
    • Espinet, C.1    de la Torre, M.A.2    Aldea, M.3    Herrero, E.4
  • 21
    • 0022042267 scopus 로고
    • Growth in cell length in the fission yeast Schizosaccharomyces pombe
    • Mitchison JM, Nurse P, (1985) Growth in cell length in the fission yeast Schizosaccharomyces pombe. J Cell Sci 75: 357-376.
    • (1985) J Cell Sci , vol.75 , pp. 357-376
    • Mitchison, J.M.1    Nurse, P.2
  • 22
    • 34447550648 scopus 로고    scopus 로고
    • Microtubules offset growth site from the cell centre in fission yeast
    • Castagnetti S, Novak B, Nurse P, (2007) Microtubules offset growth site from the cell centre in fission yeast. Journal of cell science 120: 2205-2213.
    • (2007) Journal of Cell Science , vol.120 , pp. 2205-2213
    • Castagnetti, S.1    Novak, B.2    Nurse, P.3
  • 24
    • 2942668708 scopus 로고    scopus 로고
    • Regulation of a formin complex by the microtubule plus end protein tea1p
    • Feierbach B, Verde F, Chang F, (2004) Regulation of a formin complex by the microtubule plus end protein tea1p. The Journal of cell biology 165: 697-707.
    • (2004) The Journal of Cell Biology , vol.165 , pp. 697-707
    • Feierbach, B.1    Verde, F.2    Chang, F.3
  • 25
    • 0032895191 scopus 로고    scopus 로고
    • Ssp1 promotes actin depolymerization and is involved in stress response and new end take-off control in fission yeast
    • Rupes I, Jia Z, Young PG, (1999) Ssp1 promotes actin depolymerization and is involved in stress response and new end take-off control in fission yeast. Mol Biol Cell 10: 1495-1510.
    • (1999) Mol Biol Cell , vol.10 , pp. 1495-1510
    • Rupes, I.1    Jia, Z.2    Young, P.G.3
  • 26
    • 16244409515 scopus 로고    scopus 로고
    • Tea4p links microtubule plus ends with the formin for3p in the establishment of cell polarity
    • Martin SG, McDonald WH, Yates JR, (2005) Tea4p links microtubule plus ends with the formin for3p in the establishment of cell polarity. Dev Cell 8: 479-491.
    • (2005) Dev Cell , vol.8 , pp. 479-491
    • Martin, S.G.1    McDonald, W.H.2    Yates, J.R.3
  • 27
    • 0030773728 scopus 로고    scopus 로고
    • tea1 and the microtubular cytoskeleton are important for generating global spatial order within the fission yeast cell
    • Mata J, Nurse P, (1997) tea1 and the microtubular cytoskeleton are important for generating global spatial order within the fission yeast cell. Cell 89: 939-949.
    • (1997) Cell , vol.89 , pp. 939-949
    • Mata, J.1    Nurse, P.2
  • 28
    • 0030780263 scopus 로고    scopus 로고
    • cps1+, a Schizosaccharomyces pombe gene homolog of Saccharomyces cerevisiae FKS genes whose mutation confers hypersensitivity to cyclosporin A and papulacandin B
    • Ishiguro J, Saitou A, Duran A, Ribas JC, (1997) cps1+, a Schizosaccharomyces pombe gene homolog of Saccharomyces cerevisiae FKS genes whose mutation confers hypersensitivity to cyclosporin A and papulacandin B. Journal of bacteriology 179: 7653-7662.
    • (1997) Journal of Bacteriology , vol.179 , pp. 7653-7662
    • Ishiguro, J.1    Saitou, A.2    Duran, A.3    Ribas, J.C.4
  • 29
    • 78651106804 scopus 로고    scopus 로고
    • Actin cables and the exocyst form two independent morphogenesis pathways in the fission yeast
    • Bendezu FO, Martin SG, (2011) Actin cables and the exocyst form two independent morphogenesis pathways in the fission yeast. Mol Biol Cell 22: 44-53.
    • (2011) Mol Biol Cell , vol.22 , pp. 44-53
    • Bendezu, F.O.1    Martin, S.G.2
  • 30
    • 84863110407 scopus 로고    scopus 로고
    • Fission yeast Sec3 and Exo70 are transported on actin cables and localize the exocyst complex to cell poles
    • Bendezu FO, Vincenzetti V, Martin SG, (2012) Fission yeast Sec3 and Exo70 are transported on actin cables and localize the exocyst complex to cell poles. PLoS One 7: e40248.
    • (2012) PLoS One , vol.7
    • Bendezu, F.O.1    Vincenzetti, V.2    Martin, S.G.3
  • 31
    • 0030932405 scopus 로고    scopus 로고
    • Bni1p, a yeast formin linking cdc42p and the actin cytoskeleton during polarized morphogenesis
    • Evangelista M, Blundell K, Longtine MS, Chow CJ, Adames N, et al. (1997) Bni1p, a yeast formin linking cdc42p and the actin cytoskeleton during polarized morphogenesis. Science 276: 118-122.
    • (1997) Science , vol.276 , pp. 118-122
    • Evangelista, M.1    Blundell, K.2    Longtine, M.S.3    Chow, C.J.4    Adames, N.5
  • 33
    • 70350137227 scopus 로고    scopus 로고
    • Pob1 participates in the Cdc42 regulation of fission yeast actin cytoskeleton
    • Rincon SA, Ye Y, Villar-Tajadura MA, Santos B, Martin SG, et al. (2009) Pob1 participates in the Cdc42 regulation of fission yeast actin cytoskeleton. Mol Biol Cell 20: 4390-4399.
    • (2009) Mol Biol Cell , vol.20 , pp. 4390-4399
    • Rincon, S.A.1    Ye, Y.2    Villar-Tajadura, M.A.3    Santos, B.4    Martin, S.G.5
  • 34
    • 38349030651 scopus 로고    scopus 로고
    • Membrane association and functional regulation of Sec3 by phospholipids and Cdc42
    • Zhang X, Orlando K, He B, Xi F, Zhang J, et al. (2008) Membrane association and functional regulation of Sec3 by phospholipids and Cdc42. J Cell Biol 180: 145-158.
    • (2008) J Cell Biol , vol.180 , pp. 145-158
    • Zhang, X.1    Orlando, K.2    He, B.3    Xi, F.4    Zhang, J.5
  • 35
    • 13444252631 scopus 로고    scopus 로고
    • GEF means go: turning on RHO GTPases with guanine nucleotide-exchange factors
    • Rossman KL, Der CJ, Sondek J, (2005) GEF means go: turning on RHO GTPases with guanine nucleotide-exchange factors. Nature reviews Molecular cell biology 6: 167-180.
    • (2005) Nature Reviews Molecular Cell Biology , vol.6 , pp. 167-180
    • Rossman, K.L.1    Der, C.J.2    Sondek, J.3
  • 36
    • 52149106669 scopus 로고    scopus 로고
    • Cellular signaling for activation of Rho GTPase Cdc42
    • Sinha S, Yang W, (2008) Cellular signaling for activation of Rho GTPase Cdc42. Cell Signal 20: 1927-1934.
    • (2008) Cell Signal , vol.20 , pp. 1927-1934
    • Sinha, S.1    Yang, W.2
  • 37
    • 68149181683 scopus 로고    scopus 로고
    • The conserved NDR kinase Orb6 controls polarized cell growth by spatial regulation of the small GTPase Cdc42
    • Das M, Wiley DJ, Chen X, Shah K, Verde F, (2009) The conserved NDR kinase Orb6 controls polarized cell growth by spatial regulation of the small GTPase Cdc42. Curr Biol 19: 1314-1319.
    • (2009) Curr Biol , vol.19 , pp. 1314-1319
    • Das, M.1    Wiley, D.J.2    Chen, X.3    Shah, K.4    Verde, F.5
  • 38
    • 34548291544 scopus 로고    scopus 로고
    • Spatial regulation of Cdc42 during cytokinesis
    • Rincon S, Coll PM, Perez P, (2007) Spatial regulation of Cdc42 during cytokinesis. Cell cycle 6: 1687-1691.
    • (2007) Cell Cycle , vol.6 , pp. 1687-1691
    • Rincon, S.1    Coll, P.M.2    Perez, P.3
  • 39
    • 40149109750 scopus 로고    scopus 로고
    • Pom1 DYRK regulates localization of the Rga4 GAP to ensure bipolar activation of Cdc42 in fission yeast
    • Tatebe H, Nakano K, Maximo R, Shiozaki K, (2008) Pom1 DYRK regulates localization of the Rga4 GAP to ensure bipolar activation of Cdc42 in fission yeast. Curr Biol 18: 322-330.
    • (2008) Curr Biol , vol.18 , pp. 322-330
    • Tatebe, H.1    Nakano, K.2    Maximo, R.3    Shiozaki, K.4
  • 40
    • 84863778973 scopus 로고    scopus 로고
    • Oscillatory dynamics of Cdc42 GTPase in the control of polarized growth
    • Das M, Drake T, Wiley DJ, Buchwald P, Vavylonis D, et al. (2012) Oscillatory dynamics of Cdc42 GTPase in the control of polarized growth. Science 337: 239-243.
    • (2012) Science , vol.337 , pp. 239-243
    • Das, M.1    Drake, T.2    Wiley, D.J.3    Buchwald, P.4    Vavylonis, D.5
  • 41
    • 84859760140 scopus 로고    scopus 로고
    • Negative feedback enhances robustness in the yeast polarity establishment circuit
    • Howell AS, Jin M, Wu CF, Zyla TR, Elston TC, et al. (2012) Negative feedback enhances robustness in the yeast polarity establishment circuit. Cell 149: 322-333.
    • (2012) Cell , vol.149 , pp. 322-333
    • Howell, A.S.1    Jin, M.2    Wu, C.F.3    Zyla, T.R.4    Elston, T.C.5
  • 42
    • 56349125826 scopus 로고    scopus 로고
    • Symmetry-breaking polarization driven by a Cdc42p GEF-PAK complex
    • Kozubowski L, Saito K, Johnson JM, Howell AS, Zyla TR, et al. (2008) Symmetry-breaking polarization driven by a Cdc42p GEF-PAK complex. Curr Biol 18: 1719-1726.
    • (2008) Curr Biol , vol.18 , pp. 1719-1726
    • Kozubowski, L.1    Saito, K.2    Johnson, J.M.3    Howell, A.S.4    Zyla, T.R.5
  • 43
    • 0037458909 scopus 로고    scopus 로고
    • Spontaneous cell polarization through actomyosin-based delivery of the Cdc42 GTPase
    • Wedlich-Soldner R, Altschuler S, Wu L, Li R, (2003) Spontaneous cell polarization through actomyosin-based delivery of the Cdc42 GTPase. Science 299: 1231-1235.
    • (2003) Science , vol.299 , pp. 1231-1235
    • Wedlich-Soldner, R.1    Altschuler, S.2    Wu, L.3    Li, R.4
  • 44
    • 0042531556 scopus 로고    scopus 로고
    • The kelch repeat protein, Tea1, is a potential substrate target of the p21-activated kinase, Shk1, in the fission yeast, Schizosaccharomyces pombe
    • Kim H, Yang P, Catanuto P, Verde F, Lai H, et al. (2003) The kelch repeat protein, Tea1, is a potential substrate target of the p21-activated kinase, Shk1, in the fission yeast, Schizosaccharomyces pombe. J Biol Chem 278: 30074-30082.
    • (2003) J Biol Chem , vol.278 , pp. 30074-30082
    • Kim, H.1    Yang, P.2    Catanuto, P.3    Verde, F.4    Lai, H.5
  • 45
    • 45849143261 scopus 로고    scopus 로고
    • Plasticity of polarization: changing dendrites into axons in neurons integrated in neuronal circuits
    • Gomis-Ruth S, Wierenga CJ, Bradke F, (2008) Plasticity of polarization: changing dendrites into axons in neurons integrated in neuronal circuits. Curr Biol 18: 992-1000.
    • (2008) Curr Biol , vol.18 , pp. 992-1000
    • Gomis-Ruth, S.1    Wierenga, C.J.2    Bradke, F.3
  • 46
    • 0022379107 scopus 로고
    • High-frequency switching of colony morphology in Candida albicans
    • Slutsky B, Buffo J, Soll DR, (1985) High-frequency switching of colony morphology in Candida albicans. Science 230: 666-669.
    • (1985) Science , vol.230 , pp. 666-669
    • Slutsky, B.1    Buffo, J.2    Soll, D.R.3
  • 47
    • 84872099448 scopus 로고    scopus 로고
    • Cdc42 explores the cell periphery for mate selection in fission yeast
    • Bendezu FO, Martin SG, (2013) Cdc42 explores the cell periphery for mate selection in fission yeast. Current biology: CB 23: 42-47.
    • (2013) Current Biology: CB , vol.23 , pp. 42-47
    • Bendezu, F.O.1    Martin, S.G.2
  • 48
    • 84872110455 scopus 로고    scopus 로고
    • Tracking shallow chemical gradients by actin-driven wandering of the polarization site
    • Dyer JM, Savage NS, Jin M, Zyla TR, Elston TC, et al. (2013) Tracking shallow chemical gradients by actin-driven wandering of the polarization site. Current biology 23: 32-41.
    • (2013) Current Biology , vol.23 , pp. 32-41
    • Dyer, J.M.1    Savage, N.S.2    Jin, M.3    Zyla, T.R.4    Elston, T.C.5
  • 49
    • 84863615537 scopus 로고    scopus 로고
    • Proteasomal degradation resolves competition between cell polarization and cellular wound healing
    • Kono K, Saeki Y, Yoshida S, Tanaka K, Pellman D, (2012) Proteasomal degradation resolves competition between cell polarization and cellular wound healing. Cell 150: 151-164.
    • (2012) Cell , vol.150 , pp. 151-164
    • Kono, K.1    Saeki, Y.2    Yoshida, S.3    Tanaka, K.4    Pellman, D.5
  • 50
    • 0033523764 scopus 로고    scopus 로고
    • Cell wall stress depolarizes cell growth via hyperactivation of RHO1
    • Delley PA, Hall MN, (1999) Cell wall stress depolarizes cell growth via hyperactivation of RHO1. J Cell Biol 147: 163-174.
    • (1999) J Cell Biol , vol.147 , pp. 163-174
    • Delley, P.A.1    Hall, M.N.2
  • 51
    • 0034749351 scopus 로고    scopus 로고
    • Wsc1 and Mid2 are cell surface sensors for cell wall integrity signaling that act through Rom2, a guanine nucleotide exchange factor for Rho1
    • Philip B, Levin DE, (2001) Wsc1 and Mid2 are cell surface sensors for cell wall integrity signaling that act through Rom2, a guanine nucleotide exchange factor for Rho1. Mol Cell Biol 21: 271-280.
    • (2001) Mol Cell Biol , vol.21 , pp. 271-280
    • Philip, B.1    Levin, D.E.2
  • 52
    • 67650529807 scopus 로고    scopus 로고
    • A MAP kinase dependent feedback mechanism controls Rho1 GTPase and actin distribution in yeast
    • Guo S, Shen X, Yan G, Ma D, Bai X, et al. (2009) A MAP kinase dependent feedback mechanism controls Rho1 GTPase and actin distribution in yeast. PLoS One 4: e6089.
    • (2009) PLoS One , vol.4
    • Guo, S.1    Shen, X.2    Yan, G.3    Ma, D.4    Bai, X.5
  • 53
    • 0035805617 scopus 로고    scopus 로고
    • The highly conserved protein methyltransferase, Skb1, is a mediator of hyperosmotic stress response in the fission yeast Schizosaccharomyces pombe
    • Bao S, Qyang Y, Yang P, Kim H, Du H, et al. (2001) The highly conserved protein methyltransferase, Skb1, is a mediator of hyperosmotic stress response in the fission yeast Schizosaccharomyces pombe. J Biol Chem 276: 14549-14552.
    • (2001) J Biol Chem , vol.276 , pp. 14549-14552
    • Bao, S.1    Qyang, Y.2    Yang, P.3    Kim, H.4    Du, H.5
  • 54
    • 27144473638 scopus 로고    scopus 로고
    • Fission yeast MO25 protein is localized at SPB and septum and is essential for cell morphogenesis
    • Kanai M, Kume K, Miyahara K, Sakai K, Nakamura K, et al. (2005) Fission yeast MO25 protein is localized at SPB and septum and is essential for cell morphogenesis. EMBO J 24: 3012-3025.
    • (2005) EMBO J , vol.24 , pp. 3012-3025
    • Kanai, M.1    Kume, K.2    Miyahara, K.3    Sakai, K.4    Nakamura, K.5
  • 55
    • 19544370361 scopus 로고    scopus 로고
    • Polo kinase links the stress pathway to cell cycle control and tip growth in fission yeast
    • Petersen J, Hagan IM, (2005) Polo kinase links the stress pathway to cell cycle control and tip growth in fission yeast. Nature 435: 507-512.
    • (2005) Nature , vol.435 , pp. 507-512
    • Petersen, J.1    Hagan, I.M.2
  • 56
    • 59349091875 scopus 로고    scopus 로고
    • Stress-regulated kinase pathways in the recovery of tip growth and microtubule dynamics following osmotic stress in S. pombe
    • Robertson AM, Hagan IM, (2008) Stress-regulated kinase pathways in the recovery of tip growth and microtubule dynamics following osmotic stress in S. pombe. J Cell Sci 121: 4055-4068.
    • (2008) J Cell Sci , vol.121 , pp. 4055-4068
    • Robertson, A.M.1    Hagan, I.M.2
  • 57
    • 61949321279 scopus 로고    scopus 로고
    • The Rho1p exchange factor Rgf1p signals upstream from the Pmk1 mitogen-activated protein kinase pathway in fission yeast
    • Garcia P, Tajadura V, Sanchez Y, (2009) The Rho1p exchange factor Rgf1p signals upstream from the Pmk1 mitogen-activated protein kinase pathway in fission yeast. Mol Biol Cell 20: 721-731.
    • (2009) Mol Biol Cell , vol.20 , pp. 721-731
    • Garcia, P.1    Tajadura, V.2    Sanchez, Y.3
  • 58
    • 33845429658 scopus 로고    scopus 로고
    • Rho2 is a target of the farnesyltransferase Cpp1 and acts upstream of Pmk1 mitogen-activated protein kinase signaling in fission yeast
    • Ma Y, Kuno T, Kita A, Asayama Y, Sugiura R, (2006) Rho2 is a target of the farnesyltransferase Cpp1 and acts upstream of Pmk1 mitogen-activated protein kinase signaling in fission yeast. Mol Biol Cell 17: 5028-5037.
    • (2006) Mol Biol Cell , vol.17 , pp. 5028-5037
    • Ma, Y.1    Kuno, T.2    Kita, A.3    Asayama, Y.4    Sugiura, R.5
  • 59
    • 0031844293 scopus 로고    scopus 로고
    • Heat stress activates fission yeast Spc1/StyI MAPK by a MEKK-independent mechanism
    • Shiozaki K, Shiozaki M, Russell P, (1998) Heat stress activates fission yeast Spc1/StyI MAPK by a MEKK-independent mechanism. Molecular biology of the cell 9: 1339-1349.
    • (1998) Molecular Biology of the Cell , vol.9 , pp. 1339-1349
    • Shiozaki, K.1    Shiozaki, M.2    Russell, P.3
  • 60
    • 0016374195 scopus 로고
    • An alpha-D-galactosyl-binding lectin from Bandeiraea simplicifolia seeds. Isolation by affinity chromatography and characterization
    • Hayes CE, Goldstein IJ, (1974) An alpha-D-galactosyl-binding lectin from Bandeiraea simplicifolia seeds. Isolation by affinity chromatography and characterization. J Biol Chem 249: 1904-1914.
    • (1974) J Biol Chem , vol.249 , pp. 1904-1914
    • Hayes, C.E.1    Goldstein, I.J.2
  • 61
    • 0022504212 scopus 로고
    • Length growth in fission yeast cells measured by two novel techniques
    • May JW, Mitchison JM, (1986) Length growth in fission yeast cells measured by two novel techniques. Nature 322: 752-754.
    • (1986) Nature , vol.322 , pp. 752-754
    • May, J.W.1    Mitchison, J.M.2
  • 62
    • 12244267727 scopus 로고    scopus 로고
    • Global transcriptional responses of fission yeast to environmental stress
    • Chen D, Toone WM, Mata J, Lyne R, Burns G, et al. (2003) Global transcriptional responses of fission yeast to environmental stress. Mol Biol Cell 14: 214-229.
    • (2003) Mol Biol Cell , vol.14 , pp. 214-229
    • Chen, D.1    Toone, W.M.2    Mata, J.3    Lyne, R.4    Burns, G.5
  • 63
    • 77954955686 scopus 로고    scopus 로고
    • Heat shock factors: integrators of cell stress, development and lifespan
    • Akerfelt M, Morimoto RI, Sistonen L, (2010) Heat shock factors: integrators of cell stress, development and lifespan. Nat Rev Mol Cell Biol 11: 545-555.
    • (2010) Nat Rev Mol Cell Biol , vol.11 , pp. 545-555
    • Akerfelt, M.1    Morimoto, R.I.2    Sistonen, L.3
  • 64
    • 0026060759 scopus 로고
    • Regulation of heat shock factor in Schizosaccharomyces pombe more closely resembles regulation in mammals than in Saccharomyces cerevisiae
    • Gallo GJ, Schuetz TJ, Kingston RE, (1991) Regulation of heat shock factor in Schizosaccharomyces pombe more closely resembles regulation in mammals than in Saccharomyces cerevisiae. Molecular and cellular biology 11: 281-288.
    • (1991) Molecular and Cellular Biology , vol.11 , pp. 281-288
    • Gallo, G.J.1    Schuetz, T.J.2    Kingston, R.E.3
  • 65
    • 67650681847 scopus 로고    scopus 로고
    • An atlas of chaperone-protein interactions in Saccharomyces cerevisiae: implications to protein folding pathways in the cell
    • Gong Y, Kakihara Y, Krogan N, Greenblatt J, Emili A, et al. (2009) An atlas of chaperone-protein interactions in Saccharomyces cerevisiae: implications to protein folding pathways in the cell. Mol Syst Biol 5: 275.
    • (2009) Mol Syst Biol , vol.5 , pp. 275
    • Gong, Y.1    Kakihara, Y.2    Krogan, N.3    Greenblatt, J.4    Emili, A.5
  • 66
    • 0020130877 scopus 로고
    • Correlation between synthesis of heat shock proteins and development of thermotolerance in Chinese hamster fibroblasts
    • Li GC, Werb Z, (1982) Correlation between synthesis of heat shock proteins and development of thermotolerance in Chinese hamster fibroblasts. Proc Natl Acad Sci U S A 79: 3218-3222.
    • (1982) Proc Natl Acad Sci U S A , vol.79 , pp. 3218-3222
    • Li, G.C.1    Werb, Z.2
  • 68
    • 83455179434 scopus 로고    scopus 로고
    • Regulation of cell wall biogenesis in Saccharomyces cerevisiae: the cell wall integrity signaling pathway
    • Levin DE, (2011) Regulation of cell wall biogenesis in Saccharomyces cerevisiae: the cell wall integrity signaling pathway. Genetics 189: 1145-1175.
    • (2011) Genetics , vol.189 , pp. 1145-1175
    • Levin, D.E.1
  • 69
    • 0029923979 scopus 로고    scopus 로고
    • The fission yeast pmk1+ gene encodes a novel mitogen-activated protein kinase homolog which regulates cell integrity and functions coordinately with the protein kinase C pathway
    • Toda T, Dhut S, Superti-Furga G, Gotoh Y, Nishida E, et al. (1996) The fission yeast pmk1+ gene encodes a novel mitogen-activated protein kinase homolog which regulates cell integrity and functions coordinately with the protein kinase C pathway. Molecular and cellular biology 16: 6752-6764.
    • (1996) Molecular and Cellular Biology , vol.16 , pp. 6752-6764
    • Toda, T.1    Dhut, S.2    Superti-Furga, G.3    Gotoh, Y.4    Nishida, E.5
  • 70
    • 0029563651 scopus 로고
    • Cell-cycle control linked to extracellular environment by MAP kinase pathway in fission yeast
    • Shiozaki K, Russell P, (1995) Cell-cycle control linked to extracellular environment by MAP kinase pathway in fission yeast. Nature 378: 739-743.
    • (1995) Nature , vol.378 , pp. 739-743
    • Shiozaki, K.1    Russell, P.2
  • 71
    • 39049140674 scopus 로고    scopus 로고
    • urg1: a uracil-regulatable promoter system for fission yeast with short induction and repression times
    • Watt S, Mata J, Lopez-Maury L, Marguerat S, Burns G, et al. (2008) urg1: a uracil-regulatable promoter system for fission yeast with short induction and repression times. PLoS One 3: e1428.
    • (2008) PLoS One , vol.3
    • Watt, S.1    Mata, J.2    Lopez-Maury, L.3    Marguerat, S.4    Burns, G.5
  • 72
    • 77951888185 scopus 로고    scopus 로고
    • Rho GTPases: regulation of cell polarity and growth in yeasts
    • Perez P, Rincon SA, (2010) Rho GTPases: regulation of cell polarity and growth in yeasts. The Biochemical journal 426: 243-253.
    • (2010) The Biochemical Journal , vol.426 , pp. 243-253
    • Perez, P.1    Rincon, S.A.2
  • 73
    • 11944273348 scopus 로고
    • The protein kinase C-activated MAP kinase pathway of Saccharomyces cerevisiae mediates a novel aspect of the heat shock response
    • Kamada Y, Jung US, Piotrowski J, Levin DE, (1995) The protein kinase C-activated MAP kinase pathway of Saccharomyces cerevisiae mediates a novel aspect of the heat shock response. Genes & development 9: 1559-1571.
    • (1995) Genes & Development , vol.9 , pp. 1559-1571
    • Kamada, Y.1    Jung, U.S.2    Piotrowski, J.3    Levin, D.E.4
  • 74
    • 20544432791 scopus 로고    scopus 로고
    • Cell wall integrity signaling in Saccharomyces cerevisiae
    • Levin DE, (2005) Cell wall integrity signaling in Saccharomyces cerevisiae. Microbiology and molecular biology reviews 69: 262-291.
    • (2005) Microbiology and Molecular Biology Reviews , vol.69 , pp. 262-291
    • Levin, D.E.1
  • 75
    • 34147175165 scopus 로고    scopus 로고
    • Endocytosis optimizes the dynamic localization of membrane proteins that regulate cortical polarity
    • Marco E, Wedlich-Soldner R, Li R, Altschuler SJ, Wu LF, (2007) Endocytosis optimizes the dynamic localization of membrane proteins that regulate cortical polarity. Cell 129: 411-422.
    • (2007) Cell , vol.129 , pp. 411-422
    • Marco, E.1    Wedlich-Soldner, R.2    Li, R.3    Altschuler, S.J.4    Wu, L.F.5
  • 76
    • 0037241470 scopus 로고    scopus 로고
    • Gef1p, a new guanine nucleotide exchange factor for Cdc42p, regulates polarity in Schizosaccharomyces pombe
    • Coll PM, Trillo Y, Ametzazurra A, Perez P, (2003) Gef1p, a new guanine nucleotide exchange factor for Cdc42p, regulates polarity in Schizosaccharomyces pombe. Mol Biol Cell 14: 313-323.
    • (2003) Mol Biol Cell , vol.14 , pp. 313-323
    • Coll, P.M.1    Trillo, Y.2    Ametzazurra, A.3    Perez, P.4
  • 77
    • 0037428460 scopus 로고    scopus 로고
    • The Cdc42 binding and scaffolding activities of the fission yeast adaptor protein Scd2
    • Endo M, Shirouzu M, Yokoyama S, (2003) The Cdc42 binding and scaffolding activities of the fission yeast adaptor protein Scd2. The Journal of biological chemistry 278: 843-852.
    • (2003) The Journal of Biological Chemistry , vol.278 , pp. 843-852
    • Endo, M.1    Shirouzu, M.2    Yokoyama, S.3
  • 79
    • 0029610382 scopus 로고
    • Fission yeast cell morphogenesis: identification of new genes and analysis of their role during the cell cycle
    • Verde F, Mata J, Nurse P, (1995) Fission yeast cell morphogenesis: identification of new genes and analysis of their role during the cell cycle. J Cell Biol 131: 1529-1538.
    • (1995) J Cell Biol , vol.131 , pp. 1529-1538
    • Verde, F.1    Mata, J.2    Nurse, P.3
  • 80
    • 0030802287 scopus 로고    scopus 로고
    • Molecular chaperones and the cytoskeleton
    • Liang P, MacRae TH, (1997) Molecular chaperones and the cytoskeleton. Journal of cell science 110 (Pt 13) (): 1431-1440.
    • (1997) Journal of Cell Science , vol.110 , Issue.Pt 13 , pp. 1431-1440
    • Liang, P.1    MacRae, T.H.2
  • 81
    • 0036556697 scopus 로고    scopus 로고
    • Actin cytoskeleton and small heat shock proteins: how do they interact?
    • Mounier N, Arrigo AP, (2002) Actin cytoskeleton and small heat shock proteins: how do they interact? Cell stress & chaperones 7: 167-176.
    • (2002) Cell Stress & Chaperones , vol.7 , pp. 167-176
    • Mounier, N.1    Arrigo, A.P.2
  • 82
    • 79956300350 scopus 로고    scopus 로고
    • Understanding systems-level properties: timely stories from the study of clocks
    • Hogenesch JB, Ueda HR, (2011) Understanding systems-level properties: timely stories from the study of clocks. Nat Rev Genet 12: 407-416.
    • (2011) Nat Rev Genet , vol.12 , pp. 407-416
    • Hogenesch, J.B.1    Ueda, H.R.2
  • 83
    • 65549088967 scopus 로고    scopus 로고
    • A role for casein kinase 2 in the mechanism underlying circadian temperature compensation
    • Mehra A, Shi M, Baker CL, Colot HV, Loros JJ, et al. (2009) A role for casein kinase 2 in the mechanism underlying circadian temperature compensation. Cell 137: 749-760.
    • (2009) Cell , vol.137 , pp. 749-760
    • Mehra, A.1    Shi, M.2    Baker, C.L.3    Colot, H.V.4    Loros, J.J.5
  • 84
    • 0028285110 scopus 로고
    • Genetic analysis of cell morphogenesis in fission yeast-a role for casein kinase II in the establishment of polarized growth
    • Snell V, Nurse P, (1994) Genetic analysis of cell morphogenesis in fission yeast-a role for casein kinase II in the establishment of polarized growth. EMBO J 13: 2066-2074.
    • (1994) EMBO J , vol.13 , pp. 2066-2074
    • Snell, V.1    Nurse, P.2
  • 85
    • 77957960061 scopus 로고    scopus 로고
    • Temperature as a universal resetting cue for mammalian circadian oscillators
    • Buhr ED, Yoo SH, Takahashi JS, (2010) Temperature as a universal resetting cue for mammalian circadian oscillators. Science 330: 379-385.
    • (2010) Science , vol.330 , pp. 379-385
    • Buhr, E.D.1    Yoo, S.H.2    Takahashi, J.S.3
  • 86
    • 84872047018 scopus 로고    scopus 로고
    • Hsp90 Orchestrates Transcriptional Regulation by Hsf1 and Cell Wall Remodelling by MAPK Signalling during Thermal Adaptation in a Pathogenic Yeast
    • Leach MD, Budge S, Walker L, Munro C, Cowen LE, et al. (2012) Hsp90 Orchestrates Transcriptional Regulation by Hsf1 and Cell Wall Remodelling by MAPK Signalling during Thermal Adaptation in a Pathogenic Yeast. PLoS pathogens 8: e1003069.
    • (2012) PLoS Pathogens , vol.8
    • Leach, M.D.1    Budge, S.2    Walker, L.3    Munro, C.4    Cowen, L.E.5
  • 87
    • 0029095916 scopus 로고
    • A heat shock transcription factor with reduced activity suppresses a yeast HSP70 mutant
    • Halladay JT, Craig EA, (1995) A heat shock transcription factor with reduced activity suppresses a yeast HSP70 mutant. Mol Cell Biol 15: 4890-4897.
    • (1995) Mol Cell Biol , vol.15 , pp. 4890-4897
    • Halladay, J.T.1    Craig, E.A.2
  • 88
    • 84865804550 scopus 로고    scopus 로고
    • The yeast Hsp70 Ssa1 is a sensor for activation of the heat shock response by thiol-reactive compounds
    • Wang Y, Gibney PA, West JD, Morano KA, (2012) The yeast Hsp70 Ssa1 is a sensor for activation of the heat shock response by thiol-reactive compounds. Mol Biol Cell 23: 3290-3298.
    • (2012) Mol Biol Cell , vol.23 , pp. 3290-3298
    • Wang, Y.1    Gibney, P.A.2    West, J.D.3    Morano, K.A.4
  • 89
    • 0032031725 scopus 로고    scopus 로고
    • Molecular chaperones as HSF1-specific transcriptional repressors
    • Shi Y, Mosser DD, Morimoto RI, (1998) Molecular chaperones as HSF1-specific transcriptional repressors. Genes & development 12: 654-666.
    • (1998) Genes & Development , vol.12 , pp. 654-666
    • Shi, Y.1    Mosser, D.D.2    Morimoto, R.I.3
  • 90
    • 14544290988 scopus 로고    scopus 로고
    • Constitutive nuclear import and stress-regulated nucleocytoplasmic shuttling of mammalian heat-shock factor 1
    • Vujanac M, Fenaroli A, Zimarino V, (2005) Constitutive nuclear import and stress-regulated nucleocytoplasmic shuttling of mammalian heat-shock factor 1. Traffic 6: 214-229.
    • (2005) Traffic , vol.6 , pp. 214-229
    • Vujanac, M.1    Fenaroli, A.2    Zimarino, V.3
  • 91
    • 21244495733 scopus 로고    scopus 로고
    • Mathematical modeling of the eukaryotic heat-shock response: dynamics of the hsp70 promoter
    • Rieger TR, Morimoto RI, Hatzimanikatis V, (2005) Mathematical modeling of the eukaryotic heat-shock response: dynamics of the hsp70 promoter. Biophys J 88: 1646-1658.
    • (2005) Biophys J , vol.88 , pp. 1646-1658
    • Rieger, T.R.1    Morimoto, R.I.2    Hatzimanikatis, V.3
  • 92
    • 84866125053 scopus 로고    scopus 로고
    • The critical size is set at a single-cell level by growth rate to attain homeostasis and adaptation
    • Ferrezuelo F, Colomina N, Palmisano A, Gari E, Gallego C, et al. (2012) The critical size is set at a single-cell level by growth rate to attain homeostasis and adaptation. Nat Commun 3: 1012.
    • (2012) Nat Commun , vol.3 , pp. 1012
    • Ferrezuelo, F.1    Colomina, N.2    Palmisano, A.3    Gari, E.4    Gallego, C.5
  • 93
    • 34249828941 scopus 로고    scopus 로고
    • Cyclin Cln3 is retained at the ER and released by the J chaperone Ydj1 in late G1 to trigger cell cycle entry
    • Verges E, Colomina N, Gari E, Gallego C, Aldea M, (2007) Cyclin Cln3 is retained at the ER and released by the J chaperone Ydj1 in late G1 to trigger cell cycle entry. Mol Cell 26: 649-662.
    • (2007) Mol Cell , vol.26 , pp. 649-662
    • Verges, E.1    Colomina, N.2    Gari, E.3    Gallego, C.4    Aldea, M.5
  • 94
    • 64049092699 scopus 로고    scopus 로고
    • Slow growth induces heat-shock resistance in normal and respiratory-deficient yeast
    • Lu C, Brauer MJ, Botstein D, (2009) Slow growth induces heat-shock resistance in normal and respiratory-deficient yeast. Mol Biol Cell 20: 891-903.
    • (2009) Mol Biol Cell , vol.20 , pp. 891-903
    • Lu, C.1    Brauer, M.J.2    Botstein, D.3
  • 95
    • 2442442719 scopus 로고    scopus 로고
    • Protocols for experimentation with Schizosaccharomyces pombe
    • Gould KL, (2004) Protocols for experimentation with Schizosaccharomyces pombe. Methods 33: 187-188.
    • (2004) Methods , vol.33 , pp. 187-188
    • Gould, K.L.1
  • 96
    • 68349159309 scopus 로고    scopus 로고
    • Measuring DNA content by flow cytometry in fission yeast
    • Sabatinos SA, Forsburg SL, (2009) Measuring DNA content by flow cytometry in fission yeast. Methods Mol Biol 521: 449-461.
    • (2009) Methods Mol Biol , vol.521 , pp. 449-461
    • Sabatinos, S.A.1    Forsburg, S.L.2
  • 97
    • 77955801615 scopus 로고    scopus 로고
    • Galaxy: a comprehensive approach for supporting accessible, reproducible, and transparent computational research in the life sciences
    • Goecks J, Nekrutenko A, Taylor J, (2010) Galaxy: a comprehensive approach for supporting accessible, reproducible, and transparent computational research in the life sciences. Genome biology 11: R86.
    • (2010) Genome Biology , vol.11
    • Goecks, J.1    Nekrutenko, A.2    Taylor, J.3
  • 101
    • 65449136284 scopus 로고    scopus 로고
    • TopHat: discovering splice junctions with RNA-Seq
    • Trapnell C, Pachter L, Salzberg SL, (2009) TopHat: discovering splice junctions with RNA-Seq. Bioinformatics 25: 1105-1111.
    • (2009) Bioinformatics , vol.25 , pp. 1105-1111
    • Trapnell, C.1    Pachter, L.2    Salzberg, S.L.3
  • 102
    • 77952123055 scopus 로고    scopus 로고
    • Transcript assembly and quantification by RNA-Seq reveals unannotated transcripts and isoform switching during cell differentiation
    • Trapnell C, Williams BA, Pertea G, Mortazavi A, Kwan G, et al. (2010) Transcript assembly and quantification by RNA-Seq reveals unannotated transcripts and isoform switching during cell differentiation. Nature biotechnology 28: 511-515.
    • (2010) Nature Biotechnology , vol.28 , pp. 511-515
    • Trapnell, C.1    Williams, B.A.2    Pertea, G.3    Mortazavi, A.4    Kwan, G.5
  • 103
    • 0036081355 scopus 로고    scopus 로고
    • Gene Expression Omnibus: NCBI gene expression and hybridization array data repository
    • Edgar R, Domrachev M, Lash AE, (2002) Gene Expression Omnibus: NCBI gene expression and hybridization array data repository. Nucleic Acids Res 30: 207-210.
    • (2002) Nucleic Acids Res , vol.30 , pp. 207-210
    • Edgar, R.1    Domrachev, M.2    Lash, A.E.3
  • 104
    • 20044366888 scopus 로고    scopus 로고
    • Identification of cell cycle-regulated genes in fission yeast
    • Peng X, Karuturi RK, Miller LD, Lin K, Jia Y, et al. (2005) Identification of cell cycle-regulated genes in fission yeast. Mol Biol Cell 16: 1026-1042.
    • (2005) Mol Biol Cell , vol.16 , pp. 1026-1042
    • Peng, X.1    Karuturi, R.K.2    Miller, L.D.3    Lin, K.4    Jia, Y.5
  • 105
    • 9444225935 scopus 로고    scopus 로고
    • Java Treeview-extensible visualization of microarray data
    • Saldanha AJ, (2004) Java Treeview-extensible visualization of microarray data. Bioinformatics 20: 3246-3248.
    • (2004) Bioinformatics , vol.20 , pp. 3246-3248
    • Saldanha, A.J.1


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.