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Volumn 12, Issue , 2012, Pages

NanoUPLC-MSE proteomic data assessment of soybean seeds using the Uniprot database

Author keywords

NanoUPLC MSE; Seed proteomics; Soybean; Uniprot database

Indexed keywords

COMPLEX MIXTURE; DATA ASSESSMENT; DATA BANK; DETECTION RANGE; GENE EXPRESSION PATTERNS; GENETICALLY MODIFIED ORGANISMS; GLYCININ; MASS MEASUREMENTS; NANOUPLC-MSE; PEPTIDE ANALYSIS; PI VALUES; PROTEIN ANALYSIS; PROTEIN CONTENTS; PROTEIN DATABASE; PROTEIN DIGESTION; PROTEIN IDENTIFICATION; PROTEOMIC PROFILES; PROTEOMICS; SEED PROTEIN; SOYBEAN; SOYBEAN SEEDS; TRANSGENIC SOYBEAN; TRYPTIC DIGESTION; UNIPROT;

EID: 84868220534     PISSN: None     EISSN: 14726750     Source Type: Journal    
DOI: 10.1186/1472-6750-12-82     Document Type: Article
Times cited : (55)

References (38)
  • 1
    • 84871778425 scopus 로고    scopus 로고
    • Soystats www.soystats.com.
    • Soystats
  • 3
    • 84255186272 scopus 로고    scopus 로고
    • Genetic modification of low phytic Acid 1-1 maize to enhance iron content and bioavailability
    • 10.1021/jf203485a, 22088162
    • Aluru MR, Rodermel SR, Reddy MB. Genetic modification of low phytic Acid 1-1 maize to enhance iron content and bioavailability. J Agric Food Chem 2011, 59(24):12954-12962. 10.1021/jf203485a, 22088162.
    • (2011) J Agric Food Chem , vol.59 , Issue.24 , pp. 12954-12962
    • Aluru, M.R.1    Rodermel, S.R.2    Reddy, M.B.3
  • 4
    • 27944458471 scopus 로고    scopus 로고
    • Endosperm-specific co-expression of recombinant soybean ferritin and Aspergillus phytase in maize results in significant increases in the levels of bioavailable iron
    • 10.1007/s11103-005-1537-3, 16307363
    • Drakakaki G, Marcel S, Glahn RP, Lund EK, Pariagh S, Fischer R, Christou P, Stoger E. Endosperm-specific co-expression of recombinant soybean ferritin and Aspergillus phytase in maize results in significant increases in the levels of bioavailable iron. Plant Mol Biol 2005, 59(6):869-880. 10.1007/s11103-005-1537-3, 16307363.
    • (2005) Plant Mol Biol , vol.59 , Issue.6 , pp. 869-880
    • Drakakaki, G.1    Marcel, S.2    Glahn, R.P.3    Lund, E.K.4    Pariagh, S.5    Fischer, R.6    Christou, P.7    Stoger, E.8
  • 5
    • 0038523728 scopus 로고    scopus 로고
    • Genetic modification removes an immunodominant allergen from soybean
    • 10.1104/pp.103.021865, 1540313, 12746509
    • Herman EM, Helm RM, Jung R, Kinney AJ. Genetic modification removes an immunodominant allergen from soybean. Plant Physiol 2003, 132(1):36-43. 10.1104/pp.103.021865, 1540313, 12746509.
    • (2003) Plant Physiol , vol.132 , Issue.1 , pp. 36-43
    • Herman, E.M.1    Helm, R.M.2    Jung, R.3    Kinney, A.J.4
  • 9
    • 77954443768 scopus 로고    scopus 로고
    • Correct targeting of proinsulin in protein storage vacuoles of transgenic soybean seeds
    • Cunha NB, Araújo ACG, Leite A, Murad AM, Vianna GR, Rech EL. Correct targeting of proinsulin in protein storage vacuoles of transgenic soybean seeds. Genet Mol Res 2010, 9(2):1163-1170.
    • (2010) Genet Mol Res , vol.9 , Issue.2 , pp. 1163-1170
    • Cunha, N.B.1    Araújo, A.C.G.2    Leite, A.3    Murad, A.M.4    Vianna, G.R.5    Rech, E.L.6
  • 10
    • 27844451115 scopus 로고    scopus 로고
    • Pathways for protein transport to seed storage vacuoles
    • 10.1042/BST20051016, 16246035
    • Jolliffe NA, Craddock CP, Frigerio L. Pathways for protein transport to seed storage vacuoles. Biochem Soc Trans 2005, 33:1016-1018. 10.1042/BST20051016, 16246035.
    • (2005) Biochem Soc Trans , vol.33 , pp. 1016-1018
    • Jolliffe, N.A.1    Craddock, C.P.2    Frigerio, L.3
  • 11
    • 0141706699 scopus 로고    scopus 로고
    • The production of recombinant pharmaceutical proteins in plants
    • Ma JK-C, Drake PMW, Christou P. The production of recombinant pharmaceutical proteins in plants. Nat Rev Genet 2003, 4:794-805.
    • (2003) Nat Rev Genet , vol.4 , pp. 794-805
    • Ma, J.K.-C.1    Drake, P.M.W.2    Christou, P.3
  • 12
    • 74449089417 scopus 로고    scopus 로고
    • Tobacco, a highly efficient green bioreactor for production of therapeutic proteins
    • 10.1016/j.biotechadv.2009.11.008, 19961918
    • Tremblay R, Wang D, Jevnikar AM, Ma S. Tobacco, a highly efficient green bioreactor for production of therapeutic proteins. Biotechnol Adv 2010, 28:214-221. 10.1016/j.biotechadv.2009.11.008, 19961918.
    • (2010) Biotechnol Adv , vol.28 , pp. 214-221
    • Tremblay, R.1    Wang, D.2    Jevnikar, A.M.3    Ma, S.4
  • 13
    • 32944471888 scopus 로고    scopus 로고
    • Quantitation of CP4 5-Enolpyruvylshikimate-3-Phosphate synthase in soybean by two-dimensional gel electrophoresis
    • Kim Y-H, Choi SJ, Lee H-A, Moon TW. Quantitation of CP4 5-Enolpyruvylshikimate-3-Phosphate synthase in soybean by two-dimensional gel electrophoresis. J Microbiol Biotechnol 2006, 16(1):25-31.
    • (2006) J Microbiol Biotechnol , vol.16 , Issue.1 , pp. 25-31
    • Kim, Y.-H.1    Choi, S.J.2    Lee, H.-A.3    Moon, T.W.4
  • 14
    • 84856225591 scopus 로고    scopus 로고
    • New insights on proteomics of transgenic soybean seeds: evaluation of differential expressions of enzymes and proteins
    • 10.1007/s00216-011-5409-1, 21947011
    • Barbosa HS, Arruda SC, Azevedo RA, Arruda MA. New insights on proteomics of transgenic soybean seeds: evaluation of differential expressions of enzymes and proteins. Anal Bioanal Chem 2012, 402(1):299-314. 10.1007/s00216-011-5409-1, 21947011.
    • (2012) Anal Bioanal Chem , vol.402 , Issue.1 , pp. 299-314
    • Barbosa, H.S.1    Arruda, S.C.2    Azevedo, R.A.3    Arruda, M.A.4
  • 15
    • 33646495734 scopus 로고    scopus 로고
    • Characterization of storage proteins in wild (Glycine soja) and cultivated (Glycine max) soybean seeds using proteomic analysis
    • 10.1021/jf052954k, 16608239
    • Natarajan SS, Xu C, Bae H, Caperna TJ, Garrett WM. Characterization of storage proteins in wild (Glycine soja) and cultivated (Glycine max) soybean seeds using proteomic analysis. J Agric Food Chem 2006, 54(8):3114-3120. 10.1021/jf052954k, 16608239.
    • (2006) J Agric Food Chem , vol.54 , Issue.8 , pp. 3114-3120
    • Natarajan, S.S.1    Xu, C.2    Bae, H.3    Caperna, T.J.4    Garrett, W.M.5
  • 16
    • 58149235243 scopus 로고    scopus 로고
    • Proteome analysis of soybean hypocotyl and root under salt stress
    • 10.1007/s00726-008-0036-7, 18264660
    • Aghaei K, Ehsanpour AA, Shah AH, Komatsu S. Proteome analysis of soybean hypocotyl and root under salt stress. Amino Acids 2009, 36(1):91-98. 10.1007/s00726-008-0036-7, 18264660.
    • (2009) Amino Acids , vol.36 , Issue.1 , pp. 91-98
    • Aghaei, K.1    Ehsanpour, A.A.2    Shah, A.H.3    Komatsu, S.4
  • 17
    • 63349106787 scopus 로고    scopus 로고
    • Soybean proteomics and its application to functional analysis
    • 10.1016/j.jprot.2008.10.001, 19022415
    • Komatsu S, Ahsan N. Soybean proteomics and its application to functional analysis. J Proteomics 2009, 72(3):325-336. 10.1016/j.jprot.2008.10.001, 19022415.
    • (2009) J Proteomics , vol.72 , Issue.3 , pp. 325-336
    • Komatsu, S.1    Ahsan, N.2
  • 18
    • 34548178909 scopus 로고    scopus 로고
    • In-gel digestion for mass spectrometric characterization of proteins and proteomes
    • Shevchenko A, Tomas H, Havlis J, Olsen JV, Mann M. In-gel digestion for mass spectrometric characterization of proteins and proteomes. Nat Protoc 2006, 1(6):2856-2860.
    • (2006) Nat Protoc , vol.1 , Issue.6 , pp. 2856-2860
    • Shevchenko, A.1    Tomas, H.2    Havlis, J.3    Olsen, J.V.4    Mann, M.5
  • 19
    • 36049014914 scopus 로고    scopus 로고
    • A comparison of nLC-ESI-MS/MS and nLC-MALDI-MS/MS for GeLC-based protein identification and iTRAQ-based shotgun quantitative proteomics
    • 2062563, 17916795
    • Yang Y, Zhang S, Howe K, Wilson DB, Moser F, Irwin D, Thannhauser TW. A comparison of nLC-ESI-MS/MS and nLC-MALDI-MS/MS for GeLC-based protein identification and iTRAQ-based shotgun quantitative proteomics. J Biomol Tech 2007, 18:226-237. 2062563, 17916795.
    • (2007) J Biomol Tech , vol.18 , pp. 226-237
    • Yang, Y.1    Zhang, S.2    Howe, K.3    Wilson, D.B.4    Moser, F.5    Irwin, D.6    Thannhauser, T.W.7
  • 20
    • 3242774747 scopus 로고    scopus 로고
    • High-throughput peptide mass fingerprinting of soybean seed proteins: automated workflow and utility of UniGene expressed sequence tag databases for protein identification
    • 10.1016/j.phytochem.2004.04.011, 15276434
    • Mooney BP, Krishnan HB, Thelen JJ. High-throughput peptide mass fingerprinting of soybean seed proteins: automated workflow and utility of UniGene expressed sequence tag databases for protein identification. Phytochemistry 2004, 65(12):1733-1744. 10.1016/j.phytochem.2004.04.011, 15276434.
    • (2004) Phytochemistry , vol.65 , Issue.12 , pp. 1733-1744
    • Mooney, B.P.1    Krishnan, H.B.2    Thelen, J.J.3
  • 22
    • 77953120293 scopus 로고    scopus 로고
    • Image analysis of two-dimensional gel electrophoresis for comparative proteomics of transgenic and non-transgenic soybean seeds
    • 10.1016/j.jprot.2010.01.009, 20123049
    • Brandao AR, Barbosa HS, Arruda MA. Image analysis of two-dimensional gel electrophoresis for comparative proteomics of transgenic and non-transgenic soybean seeds. J Proteomics 2010, 73(8):1433-1440. 10.1016/j.jprot.2010.01.009, 20123049.
    • (2010) J Proteomics , vol.73 , Issue.8 , pp. 1433-1440
    • Brandao, A.R.1    Barbosa, H.S.2    Arruda, M.A.3
  • 23
    • 80053209141 scopus 로고    scopus 로고
    • Detection and expression analysis of recombinant proteins in plant-derived complex mixtures using nanoUPLC-MS(E)
    • 10.1002/jssc.201100238, 21898799
    • Murad AM, Souza GH, Garcia JS, Rech EL. Detection and expression analysis of recombinant proteins in plant-derived complex mixtures using nanoUPLC-MS(E). J Sep Sci 2011, 34(19):2618-2630. 10.1002/jssc.201100238, 21898799.
    • (2011) J Sep Sci , vol.34 , Issue.19 , pp. 2618-2630
    • Murad, A.M.1    Souza, G.H.2    Garcia, J.S.3    Rech, E.L.4
  • 24
    • 0037102411 scopus 로고    scopus 로고
    • High-efficiency nanoscale liquid chromatography coupled on-line with mass spectrometry using nanoelectrospray ionization for proteomics
    • 10.1021/ac0202280, 12199598
    • Shen Y, Zhao R, Berger SJ, Anderson GA, Rodriguez N, Smith RD. High-efficiency nanoscale liquid chromatography coupled on-line with mass spectrometry using nanoelectrospray ionization for proteomics. Anal Chem 2002, 74:4235-4249. 10.1021/ac0202280, 12199598.
    • (2002) Anal Chem , vol.74 , pp. 4235-4249
    • Shen, Y.1    Zhao, R.2    Berger, S.J.3    Anderson, G.A.4    Rodriguez, N.5    Smith, R.D.6
  • 25
    • 33947202203 scopus 로고    scopus 로고
    • Effects of column length, particle size, gradient length and flow rate on peak capacity of nano-scale liquid chromatography for peptide separations
    • 10.1016/j.chroma.2007.02.016, 17320886
    • Liu H, Finch JW, Lavallee MJ, Collamati RA, Benevides CC, Gebler JC. Effects of column length, particle size, gradient length and flow rate on peak capacity of nano-scale liquid chromatography for peptide separations. J Chromatogr A 2007, 1147(1):30-36. 10.1016/j.chroma.2007.02.016, 17320886.
    • (2007) J Chromatogr A , vol.1147 , Issue.1 , pp. 30-36
    • Liu, H.1    Finch, J.W.2    Lavallee, M.J.3    Collamati, R.A.4    Benevides, C.C.5    Gebler, J.C.6
  • 26
    • 64549139332 scopus 로고    scopus 로고
    • Real-time evaluation of experimental variation in large-scale LC-MS/MS-based quantitative proteomics of complex samples
    • Levin Y, Wang L, Ingudomnukul E, Schwarz E, Baron-Cohen S, Palotás A, Bahn S. Real-time evaluation of experimental variation in large-scale LC-MS/MS-based quantitative proteomics of complex samples. J Chromatogr B 2009, 877:1299-1305.
    • (2009) J Chromatogr B , vol.877 , pp. 1299-1305
    • Levin, Y.1    Wang, L.2    Ingudomnukul, E.3    Schwarz, E.4    Baron-Cohen, S.5    Palotás, A.6    Bahn, S.7
  • 27
    • 63049084861 scopus 로고    scopus 로고
    • The detection, correlation, and comparison of peptide precursor and product ions from data independent LC-MS with data dependant LC-MS/MS
    • 10.1002/pmic.200800562, 19294628
    • Geromanos SJ, Vissers JPC, Silva JC, Dorschel CA, Li G-Z, Gorenstein MV, Bateman RH, Langridge JI. The detection, correlation, and comparison of peptide precursor and product ions from data independent LC-MS with data dependant LC-MS/MS. Proteomics 2009, 9(6):1683-1695. 10.1002/pmic.200800562, 19294628.
    • (2009) Proteomics , vol.9 , Issue.6 , pp. 1683-1695
    • Geromanos, S.J.1    Vissers, J.P.C.2    Silva, J.C.3    Dorschel, C.A.4    Li, G.-Z.5    Gorenstein, M.V.6    Bateman, R.H.7    Langridge, J.I.8
  • 28
    • 31644446949 scopus 로고    scopus 로고
    • Absolute quantification of proteins by LCMSE: a virtue of parallel MS acquisition
    • 10.1074/mcp.M500230-MCP200, 16219938
    • Silva JC, Gorenstein MV, Li G-Z, Vissers JPC, Geromanos SJ. Absolute quantification of proteins by LCMSE: a virtue of parallel MS acquisition. Mol Cell Proteomics 2005, 5(1):144-156. 10.1074/mcp.M500230-MCP200, 16219938.
    • (2005) Mol Cell Proteomics , vol.5 , Issue.1 , pp. 144-156
    • Silva, J.C.1    Gorenstein, M.V.2    Li, G.-Z.3    Vissers, J.P.C.4    Geromanos, S.J.5
  • 31
    • 63049138916 scopus 로고    scopus 로고
    • Database searching and accounting of multiplexed precursor and product ion spectra from the data independent analysis of simple and complex peptide mixtures
    • 10.1002/pmic.200800564, 19294629
    • Li G-Z, Vissers JPC, Silva JC, Golick D, Gorenstein MV, Geromanos SJ. Database searching and accounting of multiplexed precursor and product ion spectra from the data independent analysis of simple and complex peptide mixtures. Proteomics 2009, 9:1696-1719. 10.1002/pmic.200800564, 19294629.
    • (2009) Proteomics , vol.9 , pp. 1696-1719
    • Li, G.-Z.1    Vissers, J.P.C.2    Silva, J.C.3    Golick, D.4    Gorenstein, M.V.5    Geromanos, S.J.6
  • 33
    • 0029844186 scopus 로고    scopus 로고
    • Limited proteolysis of beta-conglycinin and glycinin, the 7S and 11S storage globulins from soybean [Glycine max (L.) Merr.]. Structural and evolutionary implications
    • 10.1111/j.1432-1033.1996.0221t.x, 8898910
    • Shutov AD, Kakhovskaya IA, Bastrygina AS, Bulmaga VP, Horstmann C, Muntz K. Limited proteolysis of beta-conglycinin and glycinin, the 7S and 11S storage globulins from soybean [Glycine max (L.) Merr.]. Structural and evolutionary implications. Eur J Biochem 1996, 241(1):221-228. 10.1111/j.1432-1033.1996.0221t.x, 8898910.
    • (1996) Eur J Biochem , vol.241 , Issue.1 , pp. 221-228
    • Shutov, A.D.1    Kakhovskaya, I.A.2    Bastrygina, A.S.3    Bulmaga, V.P.4    Horstmann, C.5    Muntz, K.6
  • 34
    • 84862756887 scopus 로고    scopus 로고
    • Proteomic characterization of Kunitz trypsin inhibitor variants, Tia and Tib, in soybean [Glycine max (L.) Merrill]
    • Lee KJ, Kim JB, Ha BK, Kim SH, Kang SY, Lee BM, Kim DS. Proteomic characterization of Kunitz trypsin inhibitor variants, Tia and Tib, in soybean [Glycine max (L.) Merrill]. Amino Acids 2011, 43(1):379-388.
    • (2011) Amino Acids , vol.43 , Issue.1 , pp. 379-388
    • Lee, K.J.1    Kim, J.B.2    Ha, B.K.3    Kim, S.H.4    Kang, S.Y.5    Lee, B.M.6    Kim, D.S.7
  • 35
    • 0347300280 scopus 로고    scopus 로고
    • Plant responses to drought, salinity and extreme temperatures: towards genetic engineering for stress tolerance
    • 10.1007/s00425-003-1105-5, 14513379
    • Wang W, Vinocur B, Altman A. Plant responses to drought, salinity and extreme temperatures: towards genetic engineering for stress tolerance. Planta 2003, 218(1):1-14. 10.1007/s00425-003-1105-5, 14513379.
    • (2003) Planta , vol.218 , Issue.1 , pp. 1-14
    • Wang, W.1    Vinocur, B.2    Altman, A.3
  • 36
    • 0000514965 scopus 로고
    • Proteins of soybean seeds: II. Accumulation of the major protein components during seed development and maturation
    • 10.1104/pp.53.5.747, 541438, 16658782
    • Hill JE, Breidenbach RW. Proteins of soybean seeds: II. Accumulation of the major protein components during seed development and maturation. Plant Physiol 1974, 53(5):747-751. 10.1104/pp.53.5.747, 541438, 16658782.
    • (1974) Plant Physiol , vol.53 , Issue.5 , pp. 747-751
    • Hill, J.E.1    Breidenbach, R.W.2
  • 37
    • 0032190302 scopus 로고    scopus 로고
    • Tissue- and stage-specific expression of a soybean (Glycine max L.) seed-maturation, biotinylated protein
    • 10.1023/A:1006079926339, 9747855
    • Hsing YC, Tsou CH, Hsu TF, Chen ZY, Hsieh KL, Hsieh JS, Chow TY. Tissue- and stage-specific expression of a soybean (Glycine max L.) seed-maturation, biotinylated protein. Plant Mol Biol 1998, 38(3):481-490. 10.1023/A:1006079926339, 9747855.
    • (1998) Plant Mol Biol , vol.38 , Issue.3 , pp. 481-490
    • Hsing, Y.C.1    Tsou, C.H.2    Hsu, T.F.3    Chen, Z.Y.4    Hsieh, K.L.5    Hsieh, J.S.6    Chow, T.Y.7
  • 38
    • 77949294118 scopus 로고    scopus 로고
    • Transgenic soybean seed as protein expression system: aqueous extraction of recombinant beta-glucuronidase
    • 10.1007/s12010-009-8637-5, 19412577
    • Robic G, Farinas CS, Rech EL, Miranda EA. Transgenic soybean seed as protein expression system: aqueous extraction of recombinant beta-glucuronidase. Appl Biochem Biotechnol 2010, 160(4):1157-1167. 10.1007/s12010-009-8637-5, 19412577.
    • (2010) Appl Biochem Biotechnol , vol.160 , Issue.4 , pp. 1157-1167
    • Robic, G.1    Farinas, C.S.2    Rech, E.L.3    Miranda, E.A.4


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