메뉴 건너뛰기




Volumn 39, Issue 8, 2012, Pages 8447-8456

Comparative proteomic and phosphoproteomic analysis of the silkworm (Bombyx mori) posterior silk gland under high temperature treatment

Author keywords

2D electrophoresis; Bombyx mori; MALDI TOF TOF MS; Phosphoproteomic; Posterior silk gland

Indexed keywords

ADENOSINE KINASE; ALPHA CRYSTALLIN; ELONGATION FACTOR; ELONGATION FACTOR 1BETA; ELONGATION FACTOR 1DELTA; FIBROIN; FIBROIN LIGHT CHAIN; HEAT SHOCK PROTEIN; PROHIBITIN; RIBOSOME PROTEIN; RIBOSOME PROTEIN P0; RIBOSOME PROTEIN P1; RIBOSOME PROTEIN P2; UNCLASSIFIED DRUG; INSECT PROTEIN; PROTEOME; SILK;

EID: 84868644058     PISSN: 03014851     EISSN: 15734978     Source Type: Journal    
DOI: 10.1007/s11033-012-1698-5     Document Type: Article
Times cited : (37)

References (44)
  • 1
    • 85007940210 scopus 로고
    • Effect of high temperature on the resistance of silkworm, Bombyx mori L., to flacherie-virus disease
    • Aruga H, Tanaka S (1968) Effect of high temperature on the resistance of silkworm, Bombyx mori L., to flacherie-virus disease. J Sericult Sci Jpn 37:441-444
    • (1968) J Sericult Sci Jpn , vol.37 , pp. 441-444
    • Aruga, H.1    Tanaka, S.2
  • 2
    • 0028883292 scopus 로고
    • Stathmin is a major substrate for MAP-kinase activated during heat-shock and chemical stress in HeLa cells
    • 7851413 10.1111/j.1432-1033.1995.tb20401.x 1:CAS:528:DyaK2MXktVSjtb4%3D
    • Beretta L, Dubois M, Sobel A, Bensaude O (1995) Stathmin is a major substrate for MAP-kinase activated during heat-shock and chemical stress in HeLa cells. Eur J Biochem 227:388-395
    • (1995) Eur J Biochem , vol.227 , pp. 388-395
    • Beretta, L.1    Dubois, M.2    Sobel, A.3    Bensaude, O.4
  • 3
    • 0007434361 scopus 로고
    • Combining ability of seven silk technological characters in mulberry silkworm, Bombyx mori
    • Bhargava S, Majumdar M, Datta R (1995) Combining ability of seven silk technological characters in mulberry silkworm, Bombyx mori. Ital J Zool 62:359-362
    • (1995) Ital J Zool , vol.62 , pp. 359-362
    • Bhargava, S.1    Majumdar, M.2    Datta, R.3
  • 4
    • 76649126399 scopus 로고    scopus 로고
    • Silk cocoon of Bombyx mori: Proteins and posttranslational modifications heavy phosphorylation and evidence for lysine-mediated cross links
    • 20029844 10.1002/pmic.200900624 1:CAS:528:DC%2BC3cXhvFGhsbk%3D
    • Chen WQ, Priewalder H, Pradeep John JP, Lubec G (2010) Silk cocoon of Bombyx mori: proteins and posttranslational modifications heavy phosphorylation and evidence for lysine-mediated cross links. Proteomics 10:369-379
    • (2010) Proteomics , vol.10 , pp. 369-379
    • Chen, W.Q.1    Priewalder, H.2    Pradeep John, J.P.3    Lubec, G.4
  • 5
    • 0000422766 scopus 로고
    • Alternative hypotheses of hybrid vigor
    • Crow JF (1948) Alternative hypotheses of hybrid vigor. Genetics 33:477-487
    • (1948) Genetics , vol.33 , pp. 477-487
    • Crow, J.F.1
  • 6
    • 34548459741 scopus 로고    scopus 로고
    • Using phosphoproteomics to reveal signalling dynamics in plants
    • 17765599 10.1016/j.tplants.2007.08.007
    • de la Fuente van Bentem S, Hirt H (2007) Using phosphoproteomics to reveal signalling dynamics in plants. Trends Plant Sci 12:404-411
    • (2007) Trends Plant Sci , vol.12 , pp. 404-411
    • De La Fuente Van Bentem, S.1    Hirt, H.2
  • 7
    • 5644243395 scopus 로고    scopus 로고
    • Proteomics of the Drosophila immune response
    • 10.1016/j.tibtech.2004.09.002
    • Engström M, Loseva O, Theopold U (2004) Proteomics of the Drosophila immune response. Trend Biotechnol 22:600-605
    • (2004) Trend Biotechnol , vol.22 , pp. 600-605
    • Engström, M.1    Loseva, O.2    Theopold, U.3
  • 8
    • 10644230916 scopus 로고    scopus 로고
    • Current two-dimensional electrophoresis technology for proteomics
    • 15543535 10.1002/pmic.200401031
    • Gorg A, Weiss W, Dunn M (2004) Current two-dimensional electrophoresis technology for proteomics. Proteomics 4(12):3665-3685
    • (2004) Proteomics , vol.4 , Issue.12 , pp. 3665-3685
    • Gorg, A.1    Weiss, W.2    Dunn, M.3
  • 9
    • 0002312476 scopus 로고
    • Genetics of the silkworm: Revisiting an ancient model system
    • M.R. Goldsmith A.S. Wilkins (eds) Cambridge University Press New York 10.1017/CBO9780511529931.003
    • Goldsmith MR (1995) Genetics of the silkworm: revisiting an ancient model system. In: Goldsmith MR, Wilkins AS (eds) Molecular model systems in the lepidoptera. Cambridge University Press, New York, pp 21-76
    • (1995) Molecular Model Systems in the Lepidoptera , pp. 21-76
    • Goldsmith, M.R.1
  • 10
    • 0025777354 scopus 로고
    • Heat shock, stress proteins, chaperones, and proteotoxicity
    • 1855252 10.1016/0092-8674(91)90611-2 1:STN:280:DyaK3MzgvFWgtg%3D%3D
    • Hightower L (1991) Heat shock, stress proteins, chaperones, and proteotoxicity. Cell 66:191-197
    • (1991) Cell , vol.66 , pp. 191-197
    • Hightower, L.1
  • 11
    • 56849085740 scopus 로고    scopus 로고
    • Proteome analysis on differentially expressed proteins of the fat body of two silkworm breeds, Bombyx mori, exposed to heat shock exposure
    • 10.1007/s12257-008-0049-9
    • Hossein Hosseini Moghaddam S, Du X, Li J, Cao J, Zhong B, Chen Y (2008) Proteome analysis on differentially expressed proteins of the fat body of two silkworm breeds, Bombyx mori, exposed to heat shock exposure. Biotechnol Bioprocess Eng 13:624-631
    • (2008) Biotechnol Bioprocess Eng , vol.13 , pp. 624-631
    • Hossein Hosseini Moghaddam, S.1    Du, X.2    Li, J.3    Cao, J.4    Zhong, B.5    Chen, Y.6
  • 12
    • 0037305895 scopus 로고    scopus 로고
    • Tackling the phosphoproteome: Tools and strategies
    • 12547428 10.1016/S1367-5931(02)00009-1 1:CAS:528:DC%2BD3sXltlaqtQ%3D%3D
    • Kalume D, Molina H, Pandey A (2003) Tackling the phosphoproteome: tools and strategies. Curr Opin Chem Biol 7:64-69
    • (2003) Curr Opin Chem Biol , vol.7 , pp. 64-69
    • Kalume, D.1    Molina, H.2    Pandey, A.3
  • 13
    • 0033111657 scopus 로고    scopus 로고
    • Expression of elongation factor 1β' in Escherichia coli and its interaction with elongation factor 1α from silk gland
    • 10361679 10.1271/bbb.63.666 1:CAS:528:DyaK1MXjtFeqsbc%3D
    • Kamiie K, Taira H, Kobayashi K, Yamashita T, Kidou S, Ejiri S (1999) Expression of elongation factor 1β' in Escherichia coli and its interaction with elongation factor 1α from silk gland. Biosci Biotechnol Biochem 63:666-671
    • (1999) Biosci Biotechnol Biochem , vol.63 , pp. 666-671
    • Kamiie, K.1    Taira, H.2    Kobayashi, K.3    Yamashita, T.4    Kidou, S.5    Ejiri, S.6
  • 14
    • 0011837802 scopus 로고
    • Effect of high temperature on the development of nuclear polyhedrosis virus in the silkworm, Bombyx mori
    • 10.1016/0022-2011(81)90106-3
    • Kobayashi M, Inagaki S, Kawase S (1981) Effect of high temperature on the development of nuclear polyhedrosis virus in the silkworm, Bombyx mori. J Invertebr Pathol 38:386-394
    • (1981) J Invertebr Pathol , vol.38 , pp. 386-394
    • Kobayashi, M.1    Inagaki, S.2    Kawase, S.3
  • 15
    • 0002289905 scopus 로고
    • Diseases caused by bacteria and other prokaryotes
    • J.R. Fuxa Y. Tanada (eds) 8 John Wiley and Sons New York
    • Krieg A (1987) Diseases caused by bacteria and other prokaryotes. In: Fuxa JR, Tanada Y (eds) Epizootiology of insect diseases., 8John Wiley and Sons, New York, pp 323-355
    • (1987) Epizootiology of Insect Diseases , pp. 323-355
    • Krieg, A.1
  • 16
    • 0034851443 scopus 로고    scopus 로고
    • Overdominant epistatic loci are the primary genetic basis of inbreeding depression and heterosis in rice I. Biomass and grain yield
    • 11514459 1:CAS:528:DC%2BD3MXmvFKgsbg%3D
    • Li ZK, Luo LJ, Mei HW, Wang DL, Shu QY, Tabien R, Zhong DB, Ying CS, Stansel JW, Khush GS, Paterson AH (2001) Overdominant epistatic loci are the primary genetic basis of inbreeding depression and heterosis in rice I. Biomass and grain yield. Genetics 158:1737-1753
    • (2001) Genetics , vol.158 , pp. 1737-1753
    • Li, Z.K.1    Luo, L.J.2    Mei, H.W.3    Wang, D.L.4    Shu, Q.Y.5    Tabien, R.6    Zhong, D.B.7    Ying, C.S.8    Stansel, J.W.9    Khush, G.S.10    Paterson, A.H.11
  • 17
    • 0034845083 scopus 로고    scopus 로고
    • Overdominant epistatic loci are the primary genetic basis of inbreeding depression and heterosis in rice. II. Grain yield components
    • 11514460 1:CAS:528:DC%2BD3MXmvFKgsbk%3D
    • Luo LJ, Li ZK, Mei HW, Shu QY, Tabien R, Zhong DB, Ying CS, Stansel JW, Khush GS, Paterson AH (2001) Overdominant epistatic loci are the primary genetic basis of inbreeding depression and heterosis in rice. II. Grain yield components. Genetics 158:1755-1771
    • (2001) Genetics , vol.158 , pp. 1755-1771
    • Luo, L.J.1    Li, Z.K.2    Mei, H.W.3    Shu, Q.Y.4    Tabien, R.5    Zhong, D.B.6    Ying, C.S.7    Stansel, J.W.8    Khush, G.S.9    Paterson, A.H.10
  • 18
    • 0027493838 scopus 로고
    • Multiple signal transduction pathways induce phosphorylation of serines 16, 25, and 38 of oncoprotein 18 in T lymphocytes
    • 8245003 1:CAS:528:DyaK2cXlt1Gksw%3D%3D
    • Marklund U, Brattsand G, Osterman O, Ohlsson P, Gullberg M (1993) Multiple signal transduction pathways induce phosphorylation of serines 16, 25, and 38 of oncoprotein 18 in T lymphocytes. J Biol Chem 268:25671-25680
    • (1993) J Biol Chem , vol.268 , pp. 25671-25680
    • Marklund, U.1    Brattsand, G.2    Osterman, O.3    Ohlsson, P.4    Gullberg, M.5
  • 19
    • 0027522356 scopus 로고
    • Cells in stress: Transcriptional activation of heat shock genes
    • 8451637 10.1126/science.8451637 1:CAS:528:DyaK3sXhvVCnt7Y%3D
    • Morimoto R (1993) Cells in stress: transcriptional activation of heat shock genes. Science 259:1409-1410
    • (1993) Science , vol.259 , pp. 1409-1410
    • Morimoto, R.1
  • 20
    • 0001313256 scopus 로고    scopus 로고
    • Recent advances in molecular genetics of the silk moth, Bombyx mori
    • 1:CAS:528:DC%2BD3cXhtV2gs7s%3D
    • Nagaraju J (2000) Recent advances in molecular genetics of the silk moth, Bombyx mori. Curr Sci India 78:151-161
    • (2000) Curr Sci India , vol.78 , pp. 151-161
    • Nagaraju, J.1
  • 22
    • 0025733603 scopus 로고
    • Ribosomal RNA and translation
    • 1883196 10.1146/annurev.bi.60.070191.001203 1:CAS:528:DyaK3MXmtVWitbg%3D
    • Noller H (1991) Ribosomal RNA and translation. Annu Rev Biochem 60:191-227
    • (1991) Annu Rev Biochem , vol.60 , pp. 191-227
    • Noller, H.1
  • 24
    • 27744563093 scopus 로고    scopus 로고
    • State-of-the-art in phosphoproteomics
    • 16196093 10.1002/pmic.200401289 1:CAS:528:DC%2BD2MXht1GrtbzI
    • Reinders J, Sickmann A (2005) State-of-the-art in phosphoproteomics. Proteomics 5:4052-4061
    • (2005) Proteomics , vol.5 , pp. 4052-4061
    • Reinders, J.1    Sickmann, A.2
  • 26
    • 0023445178 scopus 로고
    • Human acidic ribosomal phosphoproteins P0, P1, and P2: Analysis of cDNA clones, in vitro synthesis, and assembly
    • 3323886 1:CAS:528:DyaL1cXhtVOhtLw%3D
    • Rich B, Steitz J (1987) Human acidic ribosomal phosphoproteins P0, P1, and P2: analysis of cDNA clones, in vitro synthesis, and assembly. Mol Cell Biol 7:4065-4074
    • (1987) Mol Cell Biol , vol.7 , pp. 4065-4074
    • Rich, B.1    Steitz, J.2
  • 27
    • 4444305698 scopus 로고    scopus 로고
    • Characterization of dynamic and steady-state protein phosphorylation using a fluorescent phosphoprotein gel stain and mass spectrometry
    • 15300772 10.1002/elps.200406007 1:CAS:528:DC%2BD2cXmvFOjtL0%3D
    • Schulenberg B, Goodman TN, Aggeler R, Capaldi RA, Patton WF (2004) Characterization of dynamic and steady-state protein phosphorylation using a fluorescent phosphoprotein gel stain and mass spectrometry. Electrophoresis 25:2526-2532
    • (2004) Electrophoresis , vol.25 , pp. 2526-2532
    • Schulenberg, B.1    Goodman, T.N.2    Aggeler, R.3    Capaldi, R.A.4    Patton, W.F.5
  • 28
    • 33646529110 scopus 로고    scopus 로고
    • Small heat shock proteins and adaptation of various Drosophila species to hyperthermia
    • 10.1134/S0026893306020087 1:CAS:528:DC%2BD28XjvVWntb4%3D
    • Shilova V, Garbuz D, Evgen'ev M, Zatsepina O (2006) Small heat shock proteins and adaptation of various Drosophila species to hyperthermia. Mol Biol 40:235-239
    • (2006) Mol Biol , vol.40 , pp. 235-239
    • Shilova, V.1    Garbuz, D.2    Evgen'Ev, M.3    Zatsepina, O.4
  • 29
    • 0037096782 scopus 로고    scopus 로고
    • Interaction among silkworm ribosomal proteins P1, P2 and P0 required for functional protein binding to the GTPase-associated domain of 28S rRNA
    • 12060678 10.1093/nar/gkf379 1:CAS:528:DC%2BD38XltF2lsL0%3D
    • Shimizu T, Nakagaki M, Nishi Y, Kobayashi Y, Hachimori A, Uchiumi T (2002) Interaction among silkworm ribosomal proteins P1, P2 and P0 required for functional protein binding to the GTPase-associated domain of 28S rRNA. Nucleic Acids Res 30:2620-2627
    • (2002) Nucleic Acids Res , vol.30 , pp. 2620-2627
    • Shimizu, T.1    Nakagaki, M.2    Nishi, Y.3    Kobayashi, Y.4    Hachimori, A.5    Uchiumi, T.6
  • 30
    • 1642524277 scopus 로고    scopus 로고
    • Analysis of the regulation of the molecular chaperone Hsp26 by temperature-induced dissociation: The N-terminal domail is important for oligomer assembly and the binding of unfolding proteins
    • 14722093 10.1074/jbc.M310149200 1:CAS:528:DC%2BD2cXitFyhsLs%3D
    • Stromer T, Fischer E, Richter K, Haslbeck M, Buchner J (2004) Analysis of the regulation of the molecular chaperone Hsp26 by temperature-induced dissociation: the N-terminal domail is important for oligomer assembly and the binding of unfolding proteins. J Biol Chem 279:11222-11228
    • (2004) J Biol Chem , vol.279 , pp. 11222-11228
    • Stromer, T.1    Fischer, E.2    Richter, K.3    Haslbeck, M.4    Buchner, J.5
  • 32
    • 0037040229 scopus 로고    scopus 로고
    • Translation elongation by a hybrid ribosome in which proteins at the GTPase center of the Escherichia coli ribosome are replaced with rat counterparts
    • 11729183 10.1074/jbc.M107730200
    • Uchiumi T, Honma S, Nomura T, Dabbs ER, Hachimori A (2002) Translation elongation by a hybrid ribosome in which proteins at the GTPase center of the Escherichia coli ribosome are replaced with rat counterparts. J Biol Chem 277:3857-3862
    • (2002) J Biol Chem , vol.277 , pp. 3857-3862
    • Uchiumi, T.1    Honma, S.2    Nomura, T.3    Dabbs, E.R.4    Hachimori, A.5
  • 33
    • 0031021942 scopus 로고    scopus 로고
    • Binding of mammalian ribosomal protein complex P0. P1. P2 and protein L12 to the GTPase-associated domain of 28 S ribosomal RNA and effect on the accessibility to anti-28 S RNA Autoantibody
    • 9013569 10.1074/jbc.272.6.3302 1:CAS:528:DyaK2sXhtFemu7s%3D
    • Uchiumi T, Kominami R (1997) Binding of mammalian ribosomal protein complex P0. P1. P2 and protein L12 to the GTPase-associated domain of 28 S ribosomal RNA and effect on the accessibility to anti-28 S RNA Autoantibody. J Biol Chem 272:3302-3308
    • (1997) J Biol Chem , vol.272 , pp. 3302-3308
    • Uchiumi, T.1    Kominami, R.2
  • 34
    • 0023393132 scopus 로고
    • Topography and stoichiometry of acidic proteins in large ribosomal subunits from Artemia salina as determined by crosslinking
    • 3475694 10.1073/pnas.84.16.5580 1:CAS:528:DyaL1cXit1yn
    • Uchiumi T, Wahba A, Traut R (1987) Topography and stoichiometry of acidic proteins in large ribosomal subunits from Artemia salina as determined by crosslinking. Proc Natl Acad Sci USA 84:5580-5584
    • (1987) Proc Natl Acad Sci USA , vol.84 , pp. 5580-5584
    • Uchiumi, T.1    Wahba, A.2    Traut, R.3
  • 35
    • 77953284896 scopus 로고    scopus 로고
    • Prohibitins: Mitochondrial partners in development and stress response
    • 20226718 10.1016/j.tplants.2010.02.002
    • Van Aken O, Whelan J, Van Breusegem F (2010) Prohibitins: mitochondrial partners in development and stress response. Trends Plant Sci 15:275-282
    • (2010) Trends Plant Sci , vol.15 , pp. 275-282
    • Van Aken, O.1    Whelan, J.2    Van Breusegem, F.3
  • 36
    • 0035718677 scopus 로고    scopus 로고
    • Structure and function of the small heat shock protein/alpha-crystallin family of molecular chaperones
    • 11868270 10.1016/S0065-3233(01)59004-X
    • Van Montfort R, Slingsby C, Vierling E (2001) Structure and function of the small heat shock protein/alpha-crystallin family of molecular chaperones. Adv Protein Chem 59:105-156
    • (2001) Adv Protein Chem , vol.59 , pp. 105-156
    • Van Montfort, R.1    Slingsby, C.2    Vierling, E.3
  • 37
    • 19944380791 scopus 로고    scopus 로고
    • Adenosine kinase inhibition and suppression of RNA silencing by geminivirus AL2 and L2 proteins
    • 15919897 10.1128/JVI.79.12.7410-7418.2005 1:CAS:528:DC%2BD2MXkvFCnu7k%3D
    • Wang H, Buckley K, Yang X, Buchmann R, Bisaro D (2005) Adenosine kinase inhibition and suppression of RNA silencing by geminivirus AL2 and L2 proteins. J Virol 79:7410-7418
    • (2005) J Virol , vol.79 , pp. 7410-7418
    • Wang, H.1    Buckley, K.2    Yang, X.3    Buchmann, R.4    Bisaro, D.5
  • 38
    • 0346234414 scopus 로고    scopus 로고
    • Adenosine kinase is inactivated by geminivirus AL2 and L2 proteins
    • 1:CAS:528:DC%2BD2cXhtVSgsA%3D%3D
    • Wang H, Hao L, Shung C, Sunter G, Bisaro D (2003) Adenosine kinase is inactivated by geminivirus AL2 and L2 proteins. Plant Cell Online 15:3020-3032
    • (2003) Plant Cell Online , vol.15 , pp. 3020-3032
    • Wang, H.1    Hao, L.2    Shung, C.3    Sunter, G.4    Bisaro, D.5
  • 39
    • 38249042331 scopus 로고
    • Resistance of the silkworm, Bombyx mori, to viral infections
    • 10.1016/0167-8809(86)90086-1
    • Watanabe H (1986) Resistance of the silkworm, Bombyx mori, to viral infections. Agric Ecosyst Environ 15:131-139
    • (1986) Agric Ecosyst Environ , vol.15 , pp. 131-139
    • Watanabe, H.1
  • 40
    • 0025988131 scopus 로고
    • The primary structure of rat ribosomal proteins P0, P1, and P2 and a proposal for a uniform nomenclature for mammalian and yeast ribosomal proteins
    • 1742361 10.1016/0300-9084(91)90127-M 1:CAS:528:DyaK38XlsVGmsbs%3D
    • Wool I, Chan Y, Glück A, Suzuki K (1991) The primary structure of rat ribosomal proteins P0, P1, and P2 and a proposal for a uniform nomenclature for mammalian and yeast ribosomal proteins. Biochimie 73:861-870
    • (1991) Biochimie , vol.73 , pp. 861-870
    • Wool, I.1    Chan, Y.2    Glück, A.3    Suzuki, K.4
  • 41
    • 13844284345 scopus 로고    scopus 로고
    • Up-regulation of acidic ribosomal phosphoprotein P0 in response to freezing or anoxia in the freeze tolerant wood frog, Rana sylvatica
    • 15710371 10.1016/j.cryobiol.2004.11.001 1:CAS:528:DC%2BD2MXhtlGjtrw%3D
    • Wu S, Storey K (2005) Up-regulation of acidic ribosomal phosphoprotein P0 in response to freezing or anoxia in the freeze tolerant wood frog, Rana sylvatica. Cryobiology 50:71-82
    • (2005) Cryobiology , vol.50 , pp. 71-82
    • Wu, S.1    Storey, K.2
  • 42
    • 0029035408 scopus 로고
    • Dominance is the major genetic-basis of heterosis in rice as revealed by QTL analysis using molecular markers
    • 7498751 1:CAS:528:DyaK28Xht1CgsLo%3D
    • Xiao JH, Li JM, Yuan LP, Tanksley SD (1995) Dominance is the major genetic-basis of heterosis in rice as revealed by QTL analysis using molecular markers. Genetics 140:745-754
    • (1995) Genetics , vol.140 , pp. 745-754
    • Xiao, J.H.1    Li, J.M.2    Yuan, L.P.3    Tanksley, S.D.4
  • 43
    • 33646236906 scopus 로고    scopus 로고
    • Proteome analysis of silk gland proteins from the silkworm, Bombyx mori
    • 16548058 10.1002/pmic.200500348 1:CAS:528:DC%2BD28XkslCgtr4%3D
    • Zhang P, Aso Y, Yamamoto K, Banno Y, Wang Y, Tsuchida K, Kawaguchi Y, Fujii H (2006) Proteome analysis of silk gland proteins from the silkworm, Bombyx mori. Proteomics 6:2586-2599
    • (2006) Proteomics , vol.6 , pp. 2586-2599
    • Zhang, P.1    Aso, Y.2    Yamamoto, K.3    Banno, Y.4    Wang, Y.5    Tsuchida, K.6    Kawaguchi, Y.7    Fujii, H.8
  • 44
    • 61349125577 scopus 로고    scopus 로고
    • Comparative proteomic analysis between the domesticated silkworm (Bombyx mori) reared on fresh mulberry leaves and on artificial diet
    • 18998723 10.1021/pr800383r 1:CAS:528:DC%2BD1cXhtlGrs7vK
    • Zhou ZH, Yang HJ, Chen M, Lou CF, Zhang YZ, Chen KP, Wang Y, Yu ML, Yu F, Li JY, Zhong BX (2008) Comparative proteomic analysis between the domesticated silkworm (Bombyx mori) reared on fresh mulberry leaves and on artificial diet. J Proteome Res 7:5103-5111
    • (2008) J Proteome Res , vol.7 , pp. 5103-5111
    • Zhou, Z.H.1    Yang, H.J.2    Chen, M.3    Lou, C.F.4    Zhang, Y.Z.5    Chen, K.P.6    Wang, Y.7    Yu, M.L.8    Yu, F.9    Li, J.Y.10    Zhong, B.X.11


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.