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Volumn 15, Issue 5-6, 2015, Pages 1089-1112

Fourteen years of plant proteomics reflected in Proteomics: Moving from model species and 2DE-based approaches to orphan species and gel-free platforms

Author keywords

Gel based proteomics; Plant proteomics; Shotgun proteomics

Indexed keywords

PROTEOME; VEGETABLE PROTEIN;

EID: 84924722505     PISSN: 16159853     EISSN: 16159861     Source Type: Journal    
DOI: 10.1002/pmic.201400349     Document Type: Review
Times cited : (98)

References (262)
  • 1
    • 79958161133 scopus 로고    scopus 로고
    • Proteomics research on forest trees, the most recalcitrant and orphan plant species
    • Abril, N., Gion, J. M., Kerner, R., Muller-Starck, G. et al., Proteomics research on forest trees, the most recalcitrant and orphan plant species. Phytochemistry 2011, 72, 1219-1242.
    • (2011) Phytochemistry , vol.72 , pp. 1219-1242
    • Abril, N.1    Gion, J.M.2    Kerner, R.3    Muller-Starck, G.4
  • 4
    • 84888030421 scopus 로고    scopus 로고
    • Translational proteomics special issue
    • Jorrín-Novo, J., Valledor, L., Translational proteomics special issue. J. Proteomics 2013, 93, 1-4.
    • (2013) J. Proteomics , vol.93 , pp. 1-4
    • Jorrín-Novo, J.1    Valledor, L.2
  • 5
    • 84934435475 scopus 로고    scopus 로고
    • Plant proteomics methods and protocols
    • Jorrin-Novo, J. V., Plant proteomics methods and protocols. Methods Mol. Biol. 2014, 1072, 3-13.
    • (2014) Methods Mol. Biol. , vol.1072 , pp. 3-13
    • Jorrin-Novo, J.V.1
  • 6
    • 63349097597 scopus 로고    scopus 로고
    • Plant proteomics update (2007-2008): second-generation proteomic techniques, an appropriate experimental design, and data analysis to fulfill MIAPE standards, increase plant proteome coverage and expand biological knowledge
    • Jorrin-Novo, J. V., Maldonado, A. M., Echevarria-Zomeno, S., Valledor, L. et al., Plant proteomics update (2007-2008): second-generation proteomic techniques, an appropriate experimental design, and data analysis to fulfill MIAPE standards, increase plant proteome coverage and expand biological knowledge. J. Proteomics 2009, 72, 285-314.
    • (2009) J. Proteomics , vol.72 , pp. 285-314
    • Jorrin-Novo, J.V.1    Maldonado, A.M.2    Echevarria-Zomeno, S.3    Valledor, L.4
  • 7
    • 33750592138 scopus 로고    scopus 로고
    • Plant proteome analysis: a 2004-2006 update
    • Rossignol, M., Peltier, J. B., Mock, H. P., Matros, A. et al., Plant proteome analysis: a 2004-2006 update. Proteomics 2006, 6, 5529-5548.
    • (2006) Proteomics , vol.6 , pp. 5529-5548
    • Rossignol, M.1    Peltier, J.B.2    Mock, H.P.3    Matros, A.4
  • 8
    • 0029033175 scopus 로고
    • Progress with gene-product mapping of the mollicutes: mycoplasma genitalium
    • Wasinger, V. C., Cordwell, S. J., Cerpa-Poljak, A., Yan, J. X. et al., Progress with gene-product mapping of the mollicutes: mycoplasma genitalium. Electrophoresis 1995, 16, 1090-1094.
    • (1995) Electrophoresis , vol.16 , pp. 1090-1094
    • Wasinger, V.C.1    Cordwell, S.J.2    Cerpa-Poljak, A.3    Yan, J.X.4
  • 9
    • 0030333694 scopus 로고    scopus 로고
    • Progress with proteome projects: why all proteins expressed by a genome should be identified and how to do it
    • Wilkins, M. R., Sanchez, J. C., Gooley, A. A., Appel, R. D. et al., Progress with proteome projects: why all proteins expressed by a genome should be identified and how to do it. Biotechnol. Genet. Eng. Rev. 1996, 13, 19-50.
    • (1996) Biotechnol. Genet. Eng. Rev. , vol.13 , pp. 19-50
    • Wilkins, M.R.1    Sanchez, J.C.2    Gooley, A.A.3    Appel, R.D.4
  • 11
    • 85047683665 scopus 로고    scopus 로고
    • A proteomics approach towards understanding blast fungus infection of rice grown under different levels of nitrogen fertilization
    • Konishi, H., Ishiguro, K., Komatsu, S., A proteomics approach towards understanding blast fungus infection of rice grown under different levels of nitrogen fertilization. Proteomics 2001, 1, 1162-1171.
    • (2001) Proteomics , vol.1 , pp. 1162-1171
    • Konishi, H.1    Ishiguro, K.2    Komatsu, S.3
  • 12
    • 16344375379 scopus 로고    scopus 로고
    • Characterisation of rice anther proteins expressed at the young microspore stage
    • Imin, N., Kerim, T., Weinman, J. J., Rolfe, B. G., Characterisation of rice anther proteins expressed at the young microspore stage. Proteomics 2001, 1, 1149-1161.
    • (2001) Proteomics , vol.1 , pp. 1149-1161
    • Imin, N.1    Kerim, T.2    Weinman, J.J.3    Rolfe, B.G.4
  • 13
    • 84873992298 scopus 로고    scopus 로고
    • Proteomics of nonmodel plant species
    • Champagne, A., Boutry, M., Proteomics of nonmodel plant species. Proteomics 2013, 13, 663-673.
    • (2013) Proteomics , vol.13 , pp. 663-673
    • Champagne, A.1    Boutry, M.2
  • 14
    • 79954991715 scopus 로고    scopus 로고
    • Plant proteomics
    • Plant proteomics. Proteomics 2011, 11, 1557-1558.
    • (2011) Proteomics , vol.11 , pp. 1557-1558
  • 15
    • 84880087479 scopus 로고    scopus 로고
    • Plant proteomics in crop improvement
    • Cramer, R., Bindschedler, L., Agrawal, G., Plant proteomics in crop improvement. Proteomics 2013, 13, 1771-1771.
    • (2013) Proteomics , vol.13 , pp. 1771-1771
    • Cramer, R.1    Bindschedler, L.2    Agrawal, G.3
  • 16
    • 34548442959 scopus 로고    scopus 로고
    • Crop proteomics: aim at sustainable agriculture of tomorrow
    • Salekdeh, G. H., Komatsu, S., Crop proteomics: aim at sustainable agriculture of tomorrow. Proteomics 2007, 7, 2976-2996.
    • (2007) Proteomics , vol.7 , pp. 2976-2996
    • Salekdeh, G.H.1    Komatsu, S.2
  • 17
    • 16344375435 scopus 로고    scopus 로고
    • Rice proteome analysis: a step toward functional analysis of the rice genome
    • Komatsu, S., Tanaka, N., Rice proteome analysis: a step toward functional analysis of the rice genome. Proteomics 2005, 5, 938-949.
    • (2005) Proteomics , vol.5 , pp. 938-949
    • Komatsu, S.1    Tanaka, N.2
  • 18
    • 84896784856 scopus 로고    scopus 로고
    • Rice proteomics: a model system for crop improvement and food security
    • Kim, S. T., Kim, S. G., Agrawal, G. K., Kikuchi, S., Rakwal, R., Rice proteomics: a model system for crop improvement and food security. Proteomics 2014, 14, 593-610.
    • (2014) Proteomics , vol.14 , pp. 593-610
    • Kim, S.T.1    Kim, S.G.2    Agrawal, G.K.3    Kikuchi, S.4    Rakwal, R.5
  • 19
    • 79954997524 scopus 로고    scopus 로고
    • Rice proteomics: a move toward expanded proteome coverage to comparative and functional proteomics uncovers the mysteries of rice and plant biology
    • Agrawal, G. K., Rakwal, R., Rice proteomics: a move toward expanded proteome coverage to comparative and functional proteomics uncovers the mysteries of rice and plant biology. Proteomics 2011, 11, 1630-1649.
    • (2011) Proteomics , vol.11 , pp. 1630-1649
    • Agrawal, G.K.1    Rakwal, R.2
  • 20
    • 61549084035 scopus 로고    scopus 로고
    • Rice proteomics: ending phase I and the beginning of phase II
    • Agrawal, G. K., Jwa, N. S., Rakwal, R., Rice proteomics: ending phase I and the beginning of phase II. Proteomics 2009, 9, 935-963.
    • (2009) Proteomics , vol.9 , pp. 935-963
    • Agrawal, G.K.1    Jwa, N.S.2    Rakwal, R.3
  • 21
    • 33750094060 scopus 로고    scopus 로고
    • Update and challenges on proteomics in rice
    • Komatsu, S., Yano, H., Update and challenges on proteomics in rice. Proteomics 2006, 6, 4057-4068.
    • (2006) Proteomics , vol.6 , pp. 4057-4068
    • Komatsu, S.1    Yano, H.2
  • 22
    • 84880103813 scopus 로고    scopus 로고
    • Use of proteomics to understand seed development in rice
    • Deng, Z. Y., Gong, C. Y., Wang, T., Use of proteomics to understand seed development in rice. Proteomics 2013, 13, 1784-1800.
    • (2013) Proteomics , vol.13 , pp. 1784-1800
    • Deng, Z.Y.1    Gong, C.Y.2    Wang, T.3
  • 23
    • 84880100591 scopus 로고    scopus 로고
    • Proteomics in the fruit tree science arena: new insights into fruit defense, development, and ripening
    • Molassiotis, A., Tanou, G., Filippou, P., Fotopoulos, V., Proteomics in the fruit tree science arena: new insights into fruit defense, development, and ripening. Proteomics 2013, 13, 1871-1884.
    • (2013) Proteomics , vol.13 , pp. 1871-1884
    • Molassiotis, A.1    Tanou, G.2    Filippou, P.3    Fotopoulos, V.4
  • 24
    • 79955018843 scopus 로고    scopus 로고
    • Comparative proteomics of seed maturation in oilseeds reveals differences in intermediary metabolism
    • Hajduch, M., Matusova, R., Houston, N. L., Thelen, J. J., Comparative proteomics of seed maturation in oilseeds reveals differences in intermediary metabolism. Proteomics 2011, 11, 1619-1629.
    • (2011) Proteomics , vol.11 , pp. 1619-1629
    • Hajduch, M.1    Matusova, R.2    Houston, N.L.3    Thelen, J.J.4
  • 26
    • 79955013096 scopus 로고    scopus 로고
    • Reboot the system thanks to protein post-translational modifications and proteome diversity: how quiescent seeds restart their metabolism to prepare seedling establishment
    • Arc, E., Galland, M., Cueff, G., Godin, B. et al., Reboot the system thanks to protein post-translational modifications and proteome diversity: how quiescent seeds restart their metabolism to prepare seedling establishment. Proteomics 2011, 11, 1606-1618.
    • (2011) Proteomics , vol.11 , pp. 1606-1618
    • Arc, E.1    Galland, M.2    Cueff, G.3    Godin, B.4
  • 27
    • 66449129551 scopus 로고    scopus 로고
    • Recent developments in the application of proteomics to the analysis of plant responses to heavy metals
    • Ahsan, N., Renaut, J., Komatsu, S., Recent developments in the application of proteomics to the analysis of plant responses to heavy metals. Proteomics 2009, 9, 2602-2621.
    • (2009) Proteomics , vol.9 , pp. 2602-2621
    • Ahsan, N.1    Renaut, J.2    Komatsu, S.3
  • 28
    • 84873991566 scopus 로고    scopus 로고
    • Proteomics of phosphate use and deprivation in plants
    • Alexova, R., Millar, A. H., Proteomics of phosphate use and deprivation in plants. Proteomics 2013, 13, 609-623.
    • (2013) Proteomics , vol.13 , pp. 609-623
    • Alexova, R.1    Millar, A.H.2
  • 30
    • 84859234253 scopus 로고    scopus 로고
    • Proteomics and plant disease: advances in combating a major threat to the global food supply
    • Rampitsch, C., Bykova, N. V., Proteomics and plant disease: advances in combating a major threat to the global food supply. Proteomics 2012, 12, 673-690.
    • (2012) Proteomics , vol.12 , pp. 673-690
    • Rampitsch, C.1    Bykova, N.V.2
  • 31
    • 79960387002 scopus 로고    scopus 로고
    • Proteome analysis of host-pathogen interactions: investigation of pathogen responses to the host cell environment
    • Schmidt, F., Volker, U., Proteome analysis of host-pathogen interactions: investigation of pathogen responses to the host cell environment. Proteomics 2011, 11, 3203-3211.
    • (2011) Proteomics , vol.11 , pp. 3203-3211
    • Schmidt, F.1    Volker, U.2
  • 32
    • 84880109521 scopus 로고    scopus 로고
    • Nitric oxide-cold stress signalling cross-talk, evolution of a novel regulatory mechanism
    • Sehrawat, A., Gupta, R., Deswal, R., Nitric oxide-cold stress signalling cross-talk, evolution of a novel regulatory mechanism. Proteomics 2013, 13, 1816-1835.
    • (2013) Proteomics , vol.13 , pp. 1816-1835
    • Sehrawat, A.1    Gupta, R.2    Deswal, R.3
  • 33
    • 84880109129 scopus 로고    scopus 로고
    • Proteomic insights into seed germination in response to environmental factors
    • Tan, L., Chen, S., Wang, T., Dai, S., Proteomic insights into seed germination in response to environmental factors. Proteomics 2013, 13, 1850-1870.
    • (2013) Proteomics , vol.13 , pp. 1850-1870
    • Tan, L.1    Chen, S.2    Wang, T.3    Dai, S.4
  • 34
    • 79954992716 scopus 로고    scopus 로고
    • Investigating the plant response to cadmium exposure by proteomic and metabolomic approaches
    • Villiers, F., Ducruix, C., Hugouvieux, V., Jarno, N. et al., Investigating the plant response to cadmium exposure by proteomic and metabolomic approaches. Proteomics 2011, 11, 1650-1663.
    • (2011) Proteomics , vol.11 , pp. 1650-1663
    • Villiers, F.1    Ducruix, C.2    Hugouvieux, V.3    Jarno, N.4
  • 35
    • 84896798870 scopus 로고    scopus 로고
    • Proteomics of aluminum tolerance in plants
    • Zheng, L., Lan, P., Shen, R. F., Li, W. F., Proteomics of aluminum tolerance in plants. Proteomics 2014, 14, 566-578.
    • (2014) Proteomics , vol.14 , pp. 566-578
    • Zheng, L.1    Lan, P.2    Shen, R.F.3    Li, W.F.4
  • 36
    • 84862989345 scopus 로고    scopus 로고
    • Comparative proteomic analysis reveals similar and distinct features of proteins in dry and wet stigmas
    • Sang, Y. L., Xu, M., Ma, F. F., Chen, H. et al., Comparative proteomic analysis reveals similar and distinct features of proteins in dry and wet stigmas. Proteomics 2012, 12, 1983-1998.
    • (2012) Proteomics , vol.12 , pp. 1983-1998
    • Sang, Y.L.1    Xu, M.2    Ma, F.F.3    Chen, H.4
  • 37
    • 77149131806 scopus 로고    scopus 로고
    • Plant secretome: unlocking secrets of the secreted proteins
    • Agrawal, G. K., Jwa, N. S., Lebrun, M. H., Job, D., Rakwal, R., Plant secretome: unlocking secrets of the secreted proteins. Proteomics 2010, 10, 799-827.
    • (2010) Proteomics , vol.10 , pp. 799-827
    • Agrawal, G.K.1    Jwa, N.S.2    Lebrun, M.H.3    Job, D.4    Rakwal, R.5
  • 38
    • 84880083087 scopus 로고    scopus 로고
    • Crop seed oil bodies: from challenges in protein identification to an emerging picture of the oil body proteome
    • Jolivet, P., Acevedo, F., Boulard, C., d'Andrea, S. et al., Crop seed oil bodies: from challenges in protein identification to an emerging picture of the oil body proteome. Proteomics 2013, 13, 1836-1849.
    • (2013) Proteomics , vol.13 , pp. 1836-1849
    • Jolivet, P.1    Acevedo, F.2    Boulard, C.3    d'Andrea, S.4
  • 39
    • 66149173521 scopus 로고    scopus 로고
    • Proteome of plant peroxisomes: new perspectives on the role of these organelles in cell biology
    • Palma, J. M., Corpas, F. J., del Rio, L. A., Proteome of plant peroxisomes: new perspectives on the role of these organelles in cell biology. Proteomics 2009, 9, 2301-2312.
    • (2009) Proteomics , vol.9 , pp. 2301-2312
    • Palma, J.M.1    Corpas, F.J.2    del Rio, L.A.3
  • 40
    • 79955030496 scopus 로고    scopus 로고
    • Toward a definition of the complete proteome of plant peroxisomes: where experimental proteomics must be complemented by bioinformatics
    • Reumann, S., Toward a definition of the complete proteome of plant peroxisomes: where experimental proteomics must be complemented by bioinformatics. Proteomics 2011, 11, 1764-1779.
    • (2011) Proteomics , vol.11 , pp. 1764-1779
    • Reumann, S.1
  • 41
    • 34250372200 scopus 로고    scopus 로고
    • Proteomic analysis of photosystem I components from different plant species
    • Zolla, L., Rinalducci, S., Timperio, A. M., Proteomic analysis of photosystem I components from different plant species. Proteomics 2007, 7, 1866-1876.
    • (2007) Proteomics , vol.7 , pp. 1866-1876
    • Zolla, L.1    Rinalducci, S.2    Timperio, A.M.3
  • 42
    • 40549121251 scopus 로고    scopus 로고
    • Recent advances in plant cell wall proteomics
    • Jamet, E., Albenne, C., Boudart, G., Irshad, M. et al., Recent advances in plant cell wall proteomics. Proteomics 2008, 8, 893-908.
    • (2008) Proteomics , vol.8 , pp. 893-908
    • Jamet, E.1    Albenne, C.2    Boudart, G.3    Irshad, M.4
  • 43
    • 55749085236 scopus 로고    scopus 로고
    • Plasma membrane proteome in Arabidopsis and rice
    • Komatsu, S., Plasma membrane proteome in Arabidopsis and rice. Proteomics 2008, 8, 4137-4145.
    • (2008) Proteomics , vol.8 , pp. 4137-4145
    • Komatsu, S.1
  • 44
    • 79953048692 scopus 로고    scopus 로고
    • Mining the soluble chloroplast proteome by affinity chromatography
    • Bayer, R. G., Stael, S., Csaszar, E., Teige, M., Mining the soluble chloroplast proteome by affinity chromatography. Proteomics 2011, 11, 1287-1299.
    • (2011) Proteomics , vol.11 , pp. 1287-1299
    • Bayer, R.G.1    Stael, S.2    Csaszar, E.3    Teige, M.4
  • 45
    • 84873992560 scopus 로고    scopus 로고
    • Modulating protein function through reversible oxidation: redox-mediated processes in plants revealed through proteomics
    • Bykova, N. V., Rampitsch, C., Modulating protein function through reversible oxidation: redox-mediated processes in plants revealed through proteomics. Proteomics 2013, 13, 579-596.
    • (2013) Proteomics , vol.13 , pp. 579-596
    • Bykova, N.V.1    Rampitsch, C.2
  • 48
    • 84873988073 scopus 로고    scopus 로고
    • Interplay between protein carbonylation and nitrosylation in plants
    • Lounifi, I., Arc, E., Molassiotis, A., Job, D. et al., Interplay between protein carbonylation and nitrosylation in plants. Proteomics 2013, 13, 568-578.
    • (2013) Proteomics , vol.13 , pp. 568-578
    • Lounifi, I.1    Arc, E.2    Molassiotis, A.3    Job, D.4
  • 49
    • 84880136328 scopus 로고    scopus 로고
    • Post-harvest proteomics and food security
    • Pedreschi, R., Lurie, S., Hertog, M., Nicolai, B. et al., Post-harvest proteomics and food security. Proteomics 2013, 13, 1772-1783.
    • (2013) Proteomics , vol.13 , pp. 1772-1783
    • Pedreschi, R.1    Lurie, S.2    Hertog, M.3    Nicolai, B.4
  • 50
    • 84896762078 scopus 로고    scopus 로고
    • Quantitative analysis of protein turnover in plants
    • Nelson, C. J., Li, L., Millar, A. H., Quantitative analysis of protein turnover in plants. Proteomics 2014, 14, 579-592.
    • (2014) Proteomics , vol.14 , pp. 579-592
    • Nelson, C.J.1    Li, L.2    Millar, A.H.3
  • 51
    • 79955032759 scopus 로고    scopus 로고
    • Time to articulate a vision for the future of plant proteomics - a global perspective: an initiative for establishing the International Plant Proteomics Organization (INPPO)
    • Agrawal, G. K., Job, D., Zivy, M., Agrawal, V. P. et al., Time to articulate a vision for the future of plant proteomics - a global perspective: an initiative for establishing the International Plant Proteomics Organization (INPPO). Proteomics 2011, 11, 1559-1568.
    • (2011) Proteomics , vol.11 , pp. 1559-1568
    • Agrawal, G.K.1    Job, D.2    Zivy, M.3    Agrawal, V.P.4
  • 52
    • 33646467046 scopus 로고    scopus 로고
    • Proteomics: a promising approach to study biotic interaction in legumes. A review
    • Jorrín, J. V., Rubiales, D., Dumas-Gaudot, E., Recorbet, G. et al., Proteomics: a promising approach to study biotic interaction in legumes. A review. Euphytica 2006, 147, 37-47.
    • (2006) Euphytica , vol.147 , pp. 37-47
    • Jorrín, J.V.1    Rubiales, D.2    Dumas-Gaudot, E.3    Recorbet, G.4
  • 54
    • 84874625369 scopus 로고    scopus 로고
    • Proteoform: a single term describing protein complexity
    • Smith, L. M., Kelleher, N. L., Proteoform: a single term describing protein complexity. Nat. Methods 2013, 10, 186-187.
    • (2013) Nat. Methods , vol.10 , pp. 186-187
    • Smith, L.M.1    Kelleher, N.L.2
  • 55
    • 0035987406 scopus 로고    scopus 로고
    • Proteomic analysis of amphiphilic proteins of hexaploid wheat kernels
    • Amiour, N., Merlino, M., Leroy, P., Branlard, G., Proteomic analysis of amphiphilic proteins of hexaploid wheat kernels. Proteomics 2002, 2, 632-641.
    • (2002) Proteomics , vol.2 , pp. 632-641
    • Amiour, N.1    Merlino, M.2    Leroy, P.3    Branlard, G.4
  • 57
    • 3042777260 scopus 로고    scopus 로고
    • Proteomics characterization of different bran proteins between aromatic and nonaromatic rice (Oryza sativa L. ssp. indica)
    • Trisiriroj, A., Jeyachok, N., Chen, S. T., Proteomics characterization of different bran proteins between aromatic and nonaromatic rice (Oryza sativa L. ssp. indica). Proteomics 2004, 4, 2047-2057.
    • (2004) Proteomics , vol.4 , pp. 2047-2057
    • Trisiriroj, A.1    Jeyachok, N.2    Chen, S.T.3
  • 58
    • 84858720250 scopus 로고    scopus 로고
    • Facing challenges in Proteomics today and in the coming decade: report of Roundtable Discussions at the 4th EuPA Scientific Meeting, Portugal, Estoril 2010
    • Cox, J., Heeren, R. M., James, P., Jorrin-Novo, J. V. et al., Facing challenges in Proteomics today and in the coming decade: report of Roundtable Discussions at the 4th EuPA Scientific Meeting, Portugal, Estoril 2010. J. Proteomics 2011, 75, 4-17.
    • (2011) J. Proteomics , vol.75 , pp. 4-17
    • Cox, J.1    Heeren, R.M.2    James, P.3    Jorrin-Novo, J.V.4
  • 60
    • 14644391485 scopus 로고    scopus 로고
    • Identification of grass pollen allergens by two-dimensional gel electrophoresis and serological screening
    • Corti, V., Cattaneo, A., Bachi, A., Rossi, R. E. et al., Identification of grass pollen allergens by two-dimensional gel electrophoresis and serological screening. Proteomics 2005, 5, 729-736.
    • (2005) Proteomics , vol.5 , pp. 729-736
    • Corti, V.1    Cattaneo, A.2    Bachi, A.3    Rossi, R.E.4
  • 61
    • 42549123065 scopus 로고    scopus 로고
    • Proteomic analysis of wheat proteins recognized by IgE antibodies of allergic patients
    • Šotkovský, P., Hubálek, M., Hernychová, L., Novák, P. et al., Proteomic analysis of wheat proteins recognized by IgE antibodies of allergic patients. Proteomics 2008, 8, 1677-1691.
    • (2008) Proteomics , vol.8 , pp. 1677-1691
    • Šotkovský, P.1    Hubálek, M.2    Hernychová, L.3    Novák, P.4
  • 62
    • 33645065565 scopus 로고    scopus 로고
    • Down-regulation of the strawberry Bet v 1-homologous allergen in concert with the flavonoid biosynthesis pathway in colorless strawberry mutant
    • Hjernø, K., Alm, R., Canbäck, B., Matthiesen, R. et al., Down-regulation of the strawberry Bet v 1-homologous allergen in concert with the flavonoid biosynthesis pathway in colorless strawberry mutant. Proteomics 2006, 6, 1574-1587.
    • (2006) Proteomics , vol.6 , pp. 1574-1587
    • Hjernø, K.1    Alm, R.2    Canbäck, B.3    Matthiesen, R.4
  • 63
    • 79953687955 scopus 로고    scopus 로고
    • Proteomic profiling of birch (Betula verrucosa) pollen extracts from different origins
    • Erler, A., Hawranek, T., Krückemeier, L., Asam, C. et al., Proteomic profiling of birch (Betula verrucosa) pollen extracts from different origins. Proteomics 2011, 11, 1486-1498.
    • (2011) Proteomics , vol.11 , pp. 1486-1498
    • Erler, A.1    Hawranek, T.2    Krückemeier, L.3    Asam, C.4
  • 64
    • 67651233459 scopus 로고    scopus 로고
    • 2-D DIGE analysis of the proteome of extracts from peanut variants reveals striking differences in major allergen contents
    • Schmidt, H., Gelhaus, C., Latendorf, T., Nebendahl, M. et al., 2-D DIGE analysis of the proteome of extracts from peanut variants reveals striking differences in major allergen contents. Proteomics 2009, 9, 3507-3521.
    • (2009) Proteomics , vol.9 , pp. 3507-3521
    • Schmidt, H.1    Gelhaus, C.2    Latendorf, T.3    Nebendahl, M.4
  • 65
    • 77649159332 scopus 로고    scopus 로고
    • Screening of Ole e 1 polymorphism among olive cultivars by peptide mapping and N-glycopeptide analysis
    • Castro, A. J., Bednarczyk, A., Schaeffer-Reiss, C., Rodríguez-García, M. I. et al., Screening of Ole e 1 polymorphism among olive cultivars by peptide mapping and N-glycopeptide analysis. Proteomics 2010, 10, 953-962.
    • (2010) Proteomics , vol.10 , pp. 953-962
    • Castro, A.J.1    Bednarczyk, A.2    Schaeffer-Reiss, C.3    Rodríguez-García, M.I.4
  • 66
    • 32144459332 scopus 로고    scopus 로고
    • Pedigree analysis of an elite rice hybrid using proteomic approach
    • Xie, Z., Wang, J., Cao, M., Zhao, C. et al., Pedigree analysis of an elite rice hybrid using proteomic approach. Proteomics 2006, 6, 474-486.
    • (2006) Proteomics , vol.6 , pp. 474-486
    • Xie, Z.1    Wang, J.2    Cao, M.3    Zhao, C.4
  • 67
    • 79958131076 scopus 로고    scopus 로고
    • Novel clues on abiotic stress tolerance emerge from embryo proteome analyses of rice varieties with contrasting stress adaptation
    • Farinha, A. P., Irar, S., de Oliveira, E., Oliveira, M. M., Novel clues on abiotic stress tolerance emerge from embryo proteome analyses of rice varieties with contrasting stress adaptation. Proteomics 2011, 11, 2389-2405.
    • (2011) Proteomics , vol.11 , pp. 2389-2405
    • Farinha, A.P.1    Irar, S.2    de Oliveira, E.3    Oliveira, M.M.4
  • 68
    • 27144480404 scopus 로고    scopus 로고
    • Wheat cultivar-specific proteins in grain revealed by 2-DE and their application to cultivar identification of flour
    • Yahata, E., Maruyama-Funatsuki, W., Nishio, Z., Tabiki, T. et al., Wheat cultivar-specific proteins in grain revealed by 2-DE and their application to cultivar identification of flour. Proteomics 2005, 5, 3942-3953.
    • (2005) Proteomics , vol.5 , pp. 3942-3953
    • Yahata, E.1    Maruyama-Funatsuki, W.2    Nishio, Z.3    Tabiki, T.4
  • 69
    • 48949083987 scopus 로고    scopus 로고
    • Comparative proteomic and transcriptional profiling of a bread wheat cultivar and its derived transgenic line overexpressing a low molecular weight glutenin subunit gene in the endosperm
    • Scossa, F., Laudencia-Chingcuanco, D., Anderson, O. D., Vensel, W. H. et al., Comparative proteomic and transcriptional profiling of a bread wheat cultivar and its derived transgenic line overexpressing a low molecular weight glutenin subunit gene in the endosperm. Proteomics 2008, 8, 2948-2966.
    • (2008) Proteomics , vol.8 , pp. 2948-2966
    • Scossa, F.1    Laudencia-Chingcuanco, D.2    Anderson, O.D.3    Vensel, W.H.4
  • 70
    • 33845986694 scopus 로고    scopus 로고
    • Potato tuber proteomics: comparison of two complementary extraction methods designed for 2-DE of acidic proteins
    • Delaplace, P., van der Wal, F., Dierick, J. F., Cordewener, J. H. et al., Potato tuber proteomics: comparison of two complementary extraction methods designed for 2-DE of acidic proteins. Proteomics 2006, 6, 6494-6497.
    • (2006) Proteomics , vol.6 , pp. 6494-6497
    • Delaplace, P.1    van der Wal, F.2    Dierick, J.F.3    Cordewener, J.H.4
  • 71
    • 33746030032 scopus 로고    scopus 로고
    • Proteomic analysis of tomato fruits from two ecotypes during ripening
    • Rocco, M., D'Ambrosio, C., Arena, S., Faurobert, M. et al., Proteomic analysis of tomato fruits from two ecotypes during ripening. Proteomics 2006, 6, 3781-3791.
    • (2006) Proteomics , vol.6 , pp. 3781-3791
    • Rocco, M.1    D'Ambrosio, C.2    Arena, S.3    Faurobert, M.4
  • 72
    • 74049115774 scopus 로고    scopus 로고
    • Mass spectrometry-based label-free quantitative proteomics
    • Zhu, W., Smith, J. W., Huang, C.-M., Mass spectrometry-based label-free quantitative proteomics. J. Biomed. Biotechnol. 2010, 6, 1-6.
    • (2010) J. Biomed. Biotechnol. , vol.6 , pp. 1-6
    • Zhu, W.1    Smith, J.W.2    Huang, C.-M.3
  • 73
    • 84885406397 scopus 로고    scopus 로고
    • An extensive proteome map of tomato (Solanum lycopersicum) fruit pericarp
    • Xu, J., Pascual, L., Aurand, R., Bouchet, J. P. et al., An extensive proteome map of tomato (Solanum lycopersicum) fruit pericarp. Proteomics 2013, 13, 3059-3063.
    • (2013) Proteomics , vol.13 , pp. 3059-3063
    • Xu, J.1    Pascual, L.2    Aurand, R.3    Bouchet, J.P.4
  • 74
    • 60349108930 scopus 로고    scopus 로고
    • Dissecting the proteome of pea mature seeds reveals the phenotypic plasticity of seed protein composition
    • Bourgeois, M., Jacquin, F., Savois, V., Sommerer, N. et al., Dissecting the proteome of pea mature seeds reveals the phenotypic plasticity of seed protein composition. Proteomics 2009, 9, 254-271.
    • (2009) Proteomics , vol.9 , pp. 254-271
    • Bourgeois, M.1    Jacquin, F.2    Savois, V.3    Sommerer, N.4
  • 75
    • 79955033759 scopus 로고    scopus 로고
    • A PQL (protein quantity loci) analysis of mature pea seed proteins identifies loci determining seed protein composition
    • Bourgeois, M., Jacquin, F., Cassecuelle, F., Savois, V. et al., A PQL (protein quantity loci) analysis of mature pea seed proteins identifies loci determining seed protein composition. Proteomics 2011, 11, 1581-1594.
    • (2011) Proteomics , vol.11 , pp. 1581-1594
    • Bourgeois, M.1    Jacquin, F.2    Cassecuelle, F.3    Savois, V.4
  • 76
    • 84866154557 scopus 로고    scopus 로고
    • Identification of proteins associated with malting quality in a subset of wild barley introgression lines
    • March, T. J., Richter, D., Colby, T., Harzen, A. et al., Identification of proteins associated with malting quality in a subset of wild barley introgression lines. Proteomics 2012, 12, 2843-2851.
    • (2012) Proteomics , vol.12 , pp. 2843-2851
    • March, T.J.1    Richter, D.2    Colby, T.3    Harzen, A.4
  • 77
    • 84880136328 scopus 로고    scopus 로고
    • Post-harvest proteomics and food security
    • Pedreschi, R., Lurie, S., Hertog, M., Nicolaï, B. et al., Post-harvest proteomics and food security. Proteomics 2013, 13, 1772-1783.
    • (2013) Proteomics , vol.13 , pp. 1772-1783
    • Pedreschi, R.1    Lurie, S.2    Hertog, M.3    Nicolaï, B.4
  • 78
    • 0942287050 scopus 로고    scopus 로고
    • Proteomics as a tool to improve investigation of substantial equivalence in genetically modified organisms: the case of a virus-resistant tomato
    • Corpillo, D., Gardini, G., Vaira, A. M., Basso, M. et al., Proteomics as a tool to improve investigation of substantial equivalence in genetically modified organisms: the case of a virus-resistant tomato. Proteomics 2004, 4, 193-200.
    • (2004) Proteomics , vol.4 , pp. 193-200
    • Corpillo, D.1    Gardini, G.2    Vaira, A.M.3    Basso, M.4
  • 79
    • 23944475619 scopus 로고    scopus 로고
    • Differences among techniques for high-abundant protein depletion
    • Zolotarjova, N., Martosella, J., Nicol, G., Bailey, J. et al., Differences among techniques for high-abundant protein depletion. Proteomics 2005, 5, 3304-3313.
    • (2005) Proteomics , vol.5 , pp. 3304-3313
    • Zolotarjova, N.1    Martosella, J.2    Nicol, G.3    Bailey, J.4
  • 80
    • 66149160362 scopus 로고    scopus 로고
    • The cell wall and secretory proteome of a tobacco cell line synthesising secondary wall
    • Millar, D. J., Whitelegge, J. P., Bindschedler, L. V., Rayon, C. et al., The cell wall and secretory proteome of a tobacco cell line synthesising secondary wall. Proteomics 2009, 9, 2355-2372.
    • (2009) Proteomics , vol.9 , pp. 2355-2372
    • Millar, D.J.1    Whitelegge, J.P.2    Bindschedler, L.V.3    Rayon, C.4
  • 81
    • 70349149839 scopus 로고    scopus 로고
    • Unintended changes in protein expression revealed by proteomic analysis of seeds from transgenic pea expressing a bean α-amylase inhibitor gene
    • Chen, H., Bodulovic, G., Hall, P. J., Moore, A. et al., Unintended changes in protein expression revealed by proteomic analysis of seeds from transgenic pea expressing a bean α-amylase inhibitor gene. Proteomics 2009, 9, 4406-4415.
    • (2009) Proteomics , vol.9 , pp. 4406-4415
    • Chen, H.1    Bodulovic, G.2    Hall, P.J.3    Moore, A.4
  • 82
    • 84897378696 scopus 로고    scopus 로고
    • Comparative proteomics and metallomics studies in Arabidopsis thaliana leaf tissues: evaluation of the selenium addition in transgenic and nontransgenic plants using two-dimensional difference gel electrophoresis and laser ablation imaging
    • Maciel, B., Barbosa, H. S., Pessoa, G. S., Salazar, M. M. et al., Comparative proteomics and metallomics studies in Arabidopsis thaliana leaf tissues: evaluation of the selenium addition in transgenic and nontransgenic plants using two-dimensional difference gel electrophoresis and laser ablation imaging. Proteomics 2014, 14, 904-912.
    • (2014) Proteomics , vol.14 , pp. 904-912
    • Maciel, B.1    Barbosa, H.S.2    Pessoa, G.S.3    Salazar, M.M.4
  • 83
    • 55849143642 scopus 로고    scopus 로고
    • Proteomic profiling of rice embryos from a hybrid rice cultivar and its parental lines
    • Wang, W., Meng, B., Ge, X., Song, S. et al., Proteomic profiling of rice embryos from a hybrid rice cultivar and its parental lines. Proteomics 2008, 8, 4808-4821.
    • (2008) Proteomics , vol.8 , pp. 4808-4821
    • Wang, W.1    Meng, B.2    Ge, X.3    Song, S.4
  • 84
    • 84898615501 scopus 로고    scopus 로고
    • Maize (Zea mays L.) seedling leaf nuclear proteome and differentially expressed proteins between a hybrid and its parental lines
    • Guo, B., Chen, Y., Li, C., Wang, T. et al., Maize (Zea mays L.) seedling leaf nuclear proteome and differentially expressed proteins between a hybrid and its parental lines. Proteomics 2014, 14, 1071-1087.
    • (2014) Proteomics , vol.14 , pp. 1071-1087
    • Guo, B.1    Chen, Y.2    Li, C.3    Wang, T.4
  • 85
    • 20044363321 scopus 로고    scopus 로고
    • Autopolyploidy in cabbage (Brassica oleracea L.) does not alter significantly the proteomes of green tissues
    • Albertin, W., Brabant, P., Catrice, O., Eber, F. et al., Autopolyploidy in cabbage (Brassica oleracea L.) does not alter significantly the proteomes of green tissues. Proteomics 2005, 5, 2131-2139.
    • (2005) Proteomics , vol.5 , pp. 2131-2139
    • Albertin, W.1    Brabant, P.2    Catrice, O.3    Eber, F.4
  • 86
    • 33847652913 scopus 로고    scopus 로고
    • Effects of agricultural production systems and their components on protein profiles of potato tubers
    • Lehesranta, S. J., Koistinen, K. M., Massat, N., Davies, H. V. et al., Effects of agricultural production systems and their components on protein profiles of potato tubers. Proteomics 2007, 7, 597-604.
    • (2007) Proteomics , vol.7 , pp. 597-604
    • Lehesranta, S.J.1    Koistinen, K.M.2    Massat, N.3    Davies, H.V.4
  • 87
    • 84908634901 scopus 로고    scopus 로고
    • Proteomic approaches to sexual development mediated by antheridiogen in the fern Blechnum spicant L
    • Valledor, L., Menéndez, V., Cañal, M., Revilla, M., Fernández, H., Proteomic approaches to sexual development mediated by antheridiogen in the fern Blechnum spicant L. Proteomics 2014, 14, 2061-2071.
    • (2014) Proteomics , vol.14 , pp. 2061-2071
    • Valledor, L.1    Menéndez, V.2    Cañal, M.3    Revilla, M.4    Fernández, H.5
  • 88
    • 3042818014 scopus 로고    scopus 로고
    • Proteomic characterization of herbicide safener-induced proteins in the coleoptile of Triticum tauschii seedlings
    • Zhang, Q., Riechers, D. E., Proteomic characterization of herbicide safener-induced proteins in the coleoptile of Triticum tauschii seedlings. Proteomics 2004, 4, 2058-2071.
    • (2004) Proteomics , vol.4 , pp. 2058-2071
    • Zhang, Q.1    Riechers, D.E.2
  • 89
    • 34248363651 scopus 로고    scopus 로고
    • Differential binding of calmodulin-related proteins to their targets revealed through high-density Arabidopsis protein microarrays
    • Popescu, S. C., Popescu, G. V., Bachan, S., Zhang, Z. et al., Differential binding of calmodulin-related proteins to their targets revealed through high-density Arabidopsis protein microarrays. Proc. Natl. Acad. Sci. USA 2007, 104, 4730-4735.
    • (2007) Proc. Natl. Acad. Sci. USA , vol.104 , pp. 4730-4735
    • Popescu, S.C.1    Popescu, G.V.2    Bachan, S.3    Zhang, Z.4
  • 91
    • 33750117539 scopus 로고    scopus 로고
    • Analysis of the defence phosphoproteome of Arabidopsis thaliana using differential mass tagging
    • Jones, A. M., Bennett, M. H., Mansfield, J. W., Grant, M., Analysis of the defence phosphoproteome of Arabidopsis thaliana using differential mass tagging. Proteomics 2006, 6, 4155-4165.
    • (2006) Proteomics , vol.6 , pp. 4155-4165
    • Jones, A.M.1    Bennett, M.H.2    Mansfield, J.W.3    Grant, M.4
  • 92
    • 84866169135 scopus 로고    scopus 로고
    • Differential phosphorylation of thylakoid proteins in mesophyll and bundle sheath chloroplasts from maize plants grown under low or high light
    • Fristedt, R., Wasilewska, W., Romanowska, E., Vener, A. V., Differential phosphorylation of thylakoid proteins in mesophyll and bundle sheath chloroplasts from maize plants grown under low or high light. Proteomics 2012, 12, 2852-2861.
    • (2012) Proteomics , vol.12 , pp. 2852-2861
    • Fristedt, R.1    Wasilewska, W.2    Romanowska, E.3    Vener, A.V.4
  • 93
    • 60349118495 scopus 로고    scopus 로고
    • In vivo phosphorylation sites of barley tonoplast proteins identified by a phosphoproteomic approach
    • Endler, A., Reiland, S., Gerrits, B., Schmidt, U. G. et al., In vivo phosphorylation sites of barley tonoplast proteins identified by a phosphoproteomic approach. Proteomics 2009, 9, 310-321.
    • (2009) Proteomics , vol.9 , pp. 310-321
    • Endler, A.1    Reiland, S.2    Gerrits, B.3    Schmidt, U.G.4
  • 94
    • 84892406978 scopus 로고    scopus 로고
    • Phosphoproteome analysis of Lotus japonicus seeds
    • Ino, Y., Ishikawa, A., Nomura, A., Kajiwara, H. et al., Phosphoproteome analysis of Lotus japonicus seeds. Proteomics 2014, 14, 116-120.
    • (2014) Proteomics , vol.14 , pp. 116-120
    • Ino, Y.1    Ishikawa, A.2    Nomura, A.3    Kajiwara, H.4
  • 95
    • 84868151706 scopus 로고    scopus 로고
    • Revealing phosphoproteins playing role in tobacco pollen activated in vitro
    • Fíla, J., Matros, A., Radau, S., Zahedi, R. P. et al., Revealing phosphoproteins playing role in tobacco pollen activated in vitro. Proteomics 2012, 12, 3229-3250.
    • (2012) Proteomics , vol.12 , pp. 3229-3250
    • Fíla, J.1    Matros, A.2    Radau, S.3    Zahedi, R.P.4
  • 96
    • 84895766026 scopus 로고    scopus 로고
    • Identification of redox-sensitive cysteines in the Arabidopsis proteome using OxiTRAQ, a quantitative redox proteomics method
    • Liu, P., Zhang, H., Wang, H., Xia, Y., Identification of redox-sensitive cysteines in the Arabidopsis proteome using OxiTRAQ, a quantitative redox proteomics method. Proteomics 2014, 14, 750-762.
    • (2014) Proteomics , vol.14 , pp. 750-762
    • Liu, P.1    Zhang, H.2    Wang, H.3    Xia, Y.4
  • 97
    • 39149095741 scopus 로고    scopus 로고
    • Proteomic analysis of S-nitrosylated proteins in Arabidopsis thaliana undergoing hypersensitive response
    • Romero-Puertas, M. C., Campostrini, N., Mattè, A., Righetti, P. G. et al., Proteomic analysis of S-nitrosylated proteins in Arabidopsis thaliana undergoing hypersensitive response. Proteomics 2008, 8, 1459-1469.
    • (2008) Proteomics , vol.8 , pp. 1459-1469
    • Romero-Puertas, M.C.1    Campostrini, N.2    Mattè, A.3    Righetti, P.G.4
  • 98
    • 79953703697 scopus 로고    scopus 로고
    • Towards characterization of the glycoproteome of tomato (Solanum lycopersicum) fruit using Concanavalin A lectin affinity chromatography and LC-MALDI-MS/MS analysis
    • Catalá, C., Howe, K. J., Hucko, S., Rose, J. K., Thannhauser, T. W., Towards characterization of the glycoproteome of tomato (Solanum lycopersicum) fruit using Concanavalin A lectin affinity chromatography and LC-MALDI-MS/MS analysis. Proteomics 2011, 11, 1530-1544.
    • (2011) Proteomics , vol.11 , pp. 1530-1544
    • Catalá, C.1    Howe, K.J.2    Hucko, S.3    Rose, J.K.4    Thannhauser, T.W.5
  • 99
    • 4444327673 scopus 로고    scopus 로고
    • New targets of Arabidopsis thioredoxins revealed by proteomic analysis
    • Marchand, C., Le Maréchal, P., Meyer, Y., Miginiac-Maslow, M. et al., New targets of Arabidopsis thioredoxins revealed by proteomic analysis. Proteomics 2004, 4, 2696-2706.
    • (2004) Proteomics , vol.4 , pp. 2696-2706
    • Marchand, C.1    Le Maréchal, P.2    Meyer, Y.3    Miginiac-Maslow, M.4
  • 100
    • 33845968455 scopus 로고    scopus 로고
    • Comparative proteomic approaches for the isolation of proteins interacting with thioredoxin
    • Marchand, C., Le Maréchal, P., Meyer, Y., Decottignies, P., Comparative proteomic approaches for the isolation of proteins interacting with thioredoxin. Proteomics 2006, 6, 6528-6537.
    • (2006) Proteomics , vol.6 , pp. 6528-6537
    • Marchand, C.1    Le Maréchal, P.2    Meyer, Y.3    Decottignies, P.4
  • 102
    • 17844411493 scopus 로고    scopus 로고
    • Identification of thioredoxin h-reducible disulphides in proteomes by differential labelling of cysteines: insight into recognition and regulation of proteins in barley seeds by thioredoxin h
    • Maeda, K., Finnie, C., Svensson, B., Identification of thioredoxin h-reducible disulphides in proteomes by differential labelling of cysteines: insight into recognition and regulation of proteins in barley seeds by thioredoxin h. Proteomics 2005, 5, 1634-1644.
    • (2005) Proteomics , vol.5 , pp. 1634-1644
    • Maeda, K.1    Finnie, C.2    Svensson, B.3
  • 103
    • 33745711847 scopus 로고    scopus 로고
    • Identification of phytochrome-interacting protein candidates in Arabidopsis thaliana by co-immunoprecipitation coupled with MALDI-TOF MS
    • Phee, B. K., Shin, D. H., Cho, J. H., Kim, S. H. et al., Identification of phytochrome-interacting protein candidates in Arabidopsis thaliana by co-immunoprecipitation coupled with MALDI-TOF MS. Proteomics 2006, 6, 3671-3680.
    • (2006) Proteomics , vol.6 , pp. 3671-3680
    • Phee, B.K.1    Shin, D.H.2    Cho, J.H.3    Kim, S.H.4
  • 104
    • 67649235671 scopus 로고    scopus 로고
    • Proteomic profiling of tandem affinity purified 14-3-3 protein complexes in Arabidopsis thaliana
    • Chang, I. F., Curran, A., Woolsey, R., Quilici, D. et al., Proteomic profiling of tandem affinity purified 14-3-3 protein complexes in Arabidopsis thaliana. Proteomics 2009, 9, 2967-2985.
    • (2009) Proteomics , vol.9 , pp. 2967-2985
    • Chang, I.F.1    Curran, A.2    Woolsey, R.3    Quilici, D.4
  • 105
    • 33645474438 scopus 로고    scopus 로고
    • A proteomic analysis of 14-3-3 binding proteins from developing barley grains
    • Alexander, R. D., Morris, P. C., A proteomic analysis of 14-3-3 binding proteins from developing barley grains. Proteomics 2006, 6, 1886-1896.
    • (2006) Proteomics , vol.6 , pp. 1886-1896
    • Alexander, R.D.1    Morris, P.C.2
  • 106
    • 0042665868 scopus 로고    scopus 로고
    • High-throughput functional affinity purification of mannose binding proteins from Oryza sativa
    • Andon, N. L., Eckert, D., Yates, J. R., Haynes, P. A., High-throughput functional affinity purification of mannose binding proteins from Oryza sativa. Proteomics 2003, 3, 1270-1278.
    • (2003) Proteomics , vol.3 , pp. 1270-1278
    • Andon, N.L.1    Eckert, D.2    Yates, J.R.3    Haynes, P.A.4
  • 107
    • 33646739506 scopus 로고    scopus 로고
    • Proteomic survey of copper-binding proteins in Arabidopsis roots by immobilized metal affinity chromatography and mass spectrometry
    • Kung, C. C. S., Huang, W. N., Huang, Y. C., Yeh, K. C., Proteomic survey of copper-binding proteins in Arabidopsis roots by immobilized metal affinity chromatography and mass spectrometry. Proteomics 2006, 6, 2746-2758.
    • (2006) Proteomics , vol.6 , pp. 2746-2758
    • Kung, C.C.S.1    Huang, W.N.2    Huang, Y.C.3    Yeh, K.C.4
  • 109
    • 84873988073 scopus 로고    scopus 로고
    • Interplay between protein carbonylation and nitrosylation in plants
    • Lounifi, I., Arc, E., Molassiotis, A., Job, D. et al., Interplay between protein carbonylation and nitrosylation in plants. Proteomics 2013, 13, 568-578.
    • (2013) Proteomics , vol.13 , pp. 568-578
    • Lounifi, I.1    Arc, E.2    Molassiotis, A.3    Job, D.4
  • 110
    • 29544453143 scopus 로고    scopus 로고
    • Development of a simplified, economical polyacrylamide gel staining protocol for phosphoproteins
    • Agrawal, G. K., Thelen, J. J., Development of a simplified, economical polyacrylamide gel staining protocol for phosphoproteins. Proteomics 2005, 5, 4684-4688.
    • (2005) Proteomics , vol.5 , pp. 4684-4688
    • Agrawal, G.K.1    Thelen, J.J.2
  • 111
    • 79551475593 scopus 로고    scopus 로고
    • The good, the bad, the ugly: validating the mass spectrometric analysis of modified peptides
    • Beck, F., Lewandrowski, U., Wiltfang, M., Feldmann, I. et al., The good, the bad, the ugly: validating the mass spectrometric analysis of modified peptides. Proteomics 2011, 11, 1099-1109.
    • (2011) Proteomics , vol.11 , pp. 1099-1109
    • Beck, F.1    Lewandrowski, U.2    Wiltfang, M.3    Feldmann, I.4
  • 112
    • 70350247861 scopus 로고    scopus 로고
    • Modification-specific proteomics: strategies for characterization of post-translational modifications using enrichment techniques
    • Zhao, Y., Jensen, O. N., Modification-specific proteomics: strategies for characterization of post-translational modifications using enrichment techniques. Proteomics 2009, 9, 4632-4641.
    • (2009) Proteomics , vol.9 , pp. 4632-4641
    • Zhao, Y.1    Jensen, O.N.2
  • 113
    • 84873990418 scopus 로고    scopus 로고
    • Integration of phosphoproteomic, chemical, and biological strategies for the functional analysis of targeted protein phosphorylation
    • Guo, M., Huang, B. X., Integration of phosphoproteomic, chemical, and biological strategies for the functional analysis of targeted protein phosphorylation. Proteomics 2013, 13, 424-437.
    • (2013) Proteomics , vol.13 , pp. 424-437
    • Guo, M.1    Huang, B.X.2
  • 114
    • 63049113651 scopus 로고    scopus 로고
    • Analytical strategies for phosphoproteomics
    • Thingholm, T. E., Jensen, O. N., Larsen, M. R., Analytical strategies for phosphoproteomics. Proteomics 2009, 9, 1451-1468.
    • (2009) Proteomics , vol.9 , pp. 1451-1468
    • Thingholm, T.E.1    Jensen, O.N.2    Larsen, M.R.3
  • 115
    • 81855166733 scopus 로고    scopus 로고
    • IMAC/TiO2 enrich for peptide modifications other than phosphorylation: implications for chromatographic choice and database searching in phosphoproteomics
    • Worthington, J., Cutillas, P. R., Timms, J. F., IMAC/TiO2 enrich for peptide modifications other than phosphorylation: implications for chromatographic choice and database searching in phosphoproteomics. Proteomics 2011, 11, 4583-4587.
    • (2011) Proteomics , vol.11 , pp. 4583-4587
    • Worthington, J.1    Cutillas, P.R.2    Timms, J.F.3
  • 116
    • 33846590457 scopus 로고    scopus 로고
    • Effect of glycosylation on the protein pattern in 2-D-gel electrophoresis
    • Kleinert, P., Kuster, T., Arnold, D., Jaeken, J. et al., Effect of glycosylation on the protein pattern in 2-D-gel electrophoresis. Proteomics 2007, 7, 15-22.
    • (2007) Proteomics , vol.7 , pp. 15-22
    • Kleinert, P.1    Kuster, T.2    Arnold, D.3    Jaeken, J.4
  • 117
    • 84874967213 scopus 로고    scopus 로고
    • Protein carbamylation: in vivo modification or in vitro artefact
    • Kollipara, L., Zahedi, R. P., Protein carbamylation: in vivo modification or in vitro artefact? Proteomics 2013, 13, 941-944.
    • (2013) Proteomics , vol.13 , pp. 941-944
    • Kollipara, L.1    Zahedi, R.P.2
  • 118
    • 84862642360 scopus 로고    scopus 로고
    • Molecular interaction databases
    • Orchard, S., Molecular interaction databases. Proteomics 2012, 12, 1656-1662.
    • (2012) Proteomics , vol.12 , pp. 1656-1662
    • Orchard, S.1
  • 119
    • 79955007479 scopus 로고    scopus 로고
    • Isolation and characterization of plant protein complexes by mass spectrometry
    • Pflieger, D., Bigeard, J., Hirt, H., Isolation and characterization of plant protein complexes by mass spectrometry. Proteomics 2011, 11, 1824-1833.
    • (2011) Proteomics , vol.11 , pp. 1824-1833
    • Pflieger, D.1    Bigeard, J.2    Hirt, H.3
  • 120
    • 60549105863 scopus 로고    scopus 로고
    • A bioanalytical method for the proteome wide display and analysis of protein complexes from whole plant cell lysates
    • Remmerie, N., Roef, L., van de Slijke, E., van Leene, J. et al., A bioanalytical method for the proteome wide display and analysis of protein complexes from whole plant cell lysates. Proteomics 2009, 9, 598-609.
    • (2009) Proteomics , vol.9 , pp. 598-609
    • Remmerie, N.1    Roef, L.2    van de Slijke, E.3    van Leene, J.4
  • 121
    • 84887063785 scopus 로고    scopus 로고
    • Back to the future-the value of single protein species investigations
    • Jungblut, P. R., Back to the future-the value of single protein species investigations. Proteomics 2013, 13, 3103-3105.
    • (2013) Proteomics , vol.13 , pp. 3103-3105
    • Jungblut, P.R.1
  • 122
    • 84867800367 scopus 로고    scopus 로고
    • Analysis of protein isoforms: can we do it better
    • Stastna, M., van Eyk, J. E., Analysis of protein isoforms: can we do it better? Proteomics 2012, 12, 2937-2948.
    • (2012) Proteomics , vol.12 , pp. 2937-2948
    • Stastna, M.1    van Eyk, J.E.2
  • 123
    • 77949670309 scopus 로고    scopus 로고
    • Investigating protein isoforms via proteomics: a feasibility study
    • Blakeley, P., Siepen, J. A., Lawless, C., Hubbard, S. J., Investigating protein isoforms via proteomics: a feasibility study. Proteomics 2010, 10, 1127-1140.
    • (2010) Proteomics , vol.10 , pp. 1127-1140
    • Blakeley, P.1    Siepen, J.A.2    Lawless, C.3    Hubbard, S.J.4
  • 124
    • 84860848068 scopus 로고    scopus 로고
    • Mass spectrometry-based targeted quantitative proteomics: achieving sensitive and reproducible detection of proteins
    • Boja, E. S., Rodriguez, H., Mass spectrometry-based targeted quantitative proteomics: achieving sensitive and reproducible detection of proteins. Proteomics 2012, 12, 1093-1110.
    • (2012) Proteomics , vol.12 , pp. 1093-1110
    • Boja, E.S.1    Rodriguez, H.2
  • 125
    • 0000264243 scopus 로고
    • Our present knowledge of plant proteins
    • Osborne, T. B., Our present knowledge of plant proteins. Science 1908, 28, 417-427.
    • (1908) Science , vol.28 , pp. 417-427
    • Osborne, T.B.1
  • 126
    • 23044444710 scopus 로고    scopus 로고
    • Characterization of wheat gliadin proteins by combined two-dimensional gel electrophoresis and tandem mass spectrometry
    • Mamone, G., Addeo, F., Chianese, L., di Luccia, A. et al., Characterization of wheat gliadin proteins by combined two-dimensional gel electrophoresis and tandem mass spectrometry. Proteomics 2005, 5, 2859-2865.
    • (2005) Proteomics , vol.5 , pp. 2859-2865
    • Mamone, G.1    Addeo, F.2    Chianese, L.3    di Luccia, A.4
  • 127
    • 84934438382 scopus 로고    scopus 로고
    • Back to Osborne. Sequential protein extraction and LC-MS analysis for the characterization of the holm oak seed proteome
    • in: Jorrín-Novo, J. V., Komatsu, S., Weckwerth, W., Wienkoop, S., Eds.), Humana Press
    • Romero-Rodriguez, M. C., Maldonado-Alconada, A. M., Valledor, L., Jorrin-Novo, J. V., Back to Osborne. Sequential protein extraction and LC-MS analysis for the characterization of the holm oak seed proteome, in: Jorrín-Novo, J. V., Komatsu, S., Weckwerth, W., Wienkoop, S., (Eds.), Plant Proteomics, Humana Press 2014, pp. 379-389.
    • (2014) Plant Proteomics , pp. 379-389
    • Romero-Rodriguez, M.C.1    Maldonado-Alconada, A.M.2    Valledor, L.3    Jorrin-Novo, J.V.4
  • 128
    • 33747886382 scopus 로고    scopus 로고
    • Towards the identification of late-embryogenic-abundant phosphoproteome in Arabidopsis by 2-DE and MS
    • Irar, S., Oliveira, E., Goday, A., Towards the identification of late-embryogenic-abundant phosphoproteome in Arabidopsis by 2-DE and MS. Proteomics 2006, 6, S175-S185.
    • (2006) Proteomics , vol.6 , pp. S175-S185
    • Irar, S.1    Oliveira, E.2    Goday, A.3
  • 129
    • 33744482032 scopus 로고    scopus 로고
    • Proteomic analysis of the 14-3-3 family in Arabidopsis
    • Fuller, B., Stevens, S. M., Sehnke, P. C., Ferl, R. J., Proteomic analysis of the 14-3-3 family in Arabidopsis. Proteomics 2006, 6, 3050-3059.
    • (2006) Proteomics , vol.6 , pp. 3050-3059
    • Fuller, B.1    Stevens, S.M.2    Sehnke, P.C.3    Ferl, R.J.4
  • 130
    • 35648954540 scopus 로고    scopus 로고
    • A novel late embryogenesis abundant protein and peroxidase associated with black point in barley grains
    • March, T. J., Able, J. A., Schultz, C. J., Able, A. J., A novel late embryogenesis abundant protein and peroxidase associated with black point in barley grains. Proteomics 2007, 7, 3800-3808.
    • (2007) Proteomics , vol.7 , pp. 3800-3808
    • March, T.J.1    Able, J.A.2    Schultz, C.J.3    Able, A.J.4
  • 131
    • 46049101277 scopus 로고    scopus 로고
    • Identification of peptidases in Nicotiana tabacum leaf intercellular fluid
    • Delannoy, M., Alves, G., Vertommen, D., Ma, J. et al., Identification of peptidases in Nicotiana tabacum leaf intercellular fluid. Proteomics 2008, 8, 2285-2298.
    • (2008) Proteomics , vol.8 , pp. 2285-2298
    • Delannoy, M.1    Alves, G.2    Vertommen, D.3    Ma, J.4
  • 132
  • 133
    • 0036744503 scopus 로고    scopus 로고
    • Proteome of oriental ginseng Panax ginseng CA Meyer and the potential to use it as an identification tool
    • Lum, J. H. K., Fung, K. L., Cheung, P. Y., Wong, M. S. et al., Proteome of oriental ginseng Panax ginseng CA Meyer and the potential to use it as an identification tool. Proteomics 2002, 2, 1123-1130.
    • (2002) Proteomics , vol.2 , pp. 1123-1130
    • Lum, J.H.K.1    Fung, K.L.2    Cheung, P.Y.3    Wong, M.S.4
  • 134
    • 0036746362 scopus 로고    scopus 로고
    • Evaluation of proteome reference maps for cross-species identification of proteins by peptide mass fingerprinting
    • Mathesius, U., Imin, N., Chen, H., Djordjevic, M. A. et al., Evaluation of proteome reference maps for cross-species identification of proteins by peptide mass fingerprinting. Proteomics 2002, 2, 1288-1303.
    • (2002) Proteomics , vol.2 , pp. 1288-1303
    • Mathesius, U.1    Imin, N.2    Chen, H.3    Djordjevic, M.A.4
  • 135
    • 77149143194 scopus 로고    scopus 로고
    • Fish proteome analysis: model organisms and non-sequenced species
    • Forne, I., Abian, J., Cerda, J., Fish proteome analysis: model organisms and non-sequenced species. Proteomics 2010, 10, 858-872.
    • (2010) Proteomics , vol.10 , pp. 858-872
    • Forne, I.1    Abian, J.2    Cerda, J.3
  • 137
    • 84901846391 scopus 로고    scopus 로고
    • Improving the quality of protein identification in non-model species. Characterization of Quercus ilex seed and Pinus radiata needle proteomes by using SEQUEST and custom databases
    • Romero-Rodríguez, M. C., Pascual, J., Valledor, L., Jorrín-Novo, J., Improving the quality of protein identification in non-model species. Characterization of Quercus ilex seed and Pinus radiata needle proteomes by using SEQUEST and custom databases. J. Proteomics 2014, 105, 85-91.
    • (2014) J. Proteomics , vol.105 , pp. 85-91
    • Romero-Rodríguez, M.C.1    Pascual, J.2    Valledor, L.3    Jorrín-Novo, J.4
  • 138
    • 18844427007 scopus 로고    scopus 로고
    • Proteome analysis of Arabidopsis thaliana by two-dimensional gel electrophoresis and matrix-assisted laser desorption/ionisation-time of flight mass spectrometry
    • Giavalisco, P., Nordhoff, E., Kreitler, T., Klöppel, K. D. et al., Proteome analysis of Arabidopsis thaliana by two-dimensional gel electrophoresis and matrix-assisted laser desorption/ionisation-time of flight mass spectrometry. Proteomics 2005, 5, 1902-1913.
    • (2005) Proteomics , vol.5 , pp. 1902-1913
    • Giavalisco, P.1    Nordhoff, E.2    Kreitler, T.3    Klöppel, K.D.4
  • 139
    • 60549109457 scopus 로고    scopus 로고
    • Comparative proteomics of leaf, stem, and root tissues of synthetic Brassica napus
    • Albertin, W., Langella, O., Joets, J., Négroni, L. et al., Comparative proteomics of leaf, stem, and root tissues of synthetic Brassica napus. Proteomics 2009, 9, 793-799.
    • (2009) Proteomics , vol.9 , pp. 793-799
    • Albertin, W.1    Langella, O.2    Joets, J.3    Négroni, L.4
  • 140
    • 79955037355 scopus 로고    scopus 로고
    • Comparative proteomic profiles of the soybean (Glycine max) root apex and differentiated root zone
    • Mathesius, U., Djordjevic, M. A., Oakes, M., Goffard, N. et al., Comparative proteomic profiles of the soybean (Glycine max) root apex and differentiated root zone. Proteomics 2011, 11, 1707-1719.
    • (2011) Proteomics , vol.11 , pp. 1707-1719
    • Mathesius, U.1    Djordjevic, M.A.2    Oakes, M.3    Goffard, N.4
  • 141
    • 84892843619 scopus 로고    scopus 로고
    • Proteomic mapping for legume nodule organogenesis
    • Ahsan, N., Stevenson, S. E., Proteomic mapping for legume nodule organogenesis. Proteomics 2014, 14, 153-154.
    • (2014) Proteomics , vol.14 , pp. 153-154
    • Ahsan, N.1    Stevenson, S.E.2
  • 142
    • 34748853919 scopus 로고    scopus 로고
    • Analyses of intricate kinetics of the serum proteome during and after colon surgery by protein expression time series
    • Roelofsen, H., Alvarez-Llamas, G., Dijkstra, M., Breitling, R. et al., Analyses of intricate kinetics of the serum proteome during and after colon surgery by protein expression time series. Proteomics 2007, 7, 3219-3228.
    • (2007) Proteomics , vol.7 , pp. 3219-3228
    • Roelofsen, H.1    Alvarez-Llamas, G.2    Dijkstra, M.3    Breitling, R.4
  • 143
    • 79955000178 scopus 로고    scopus 로고
    • Analysis of the xylem sap proteome of Brassica oleracea reveals a high content in secreted proteins
    • Ligat, L., Lauber, E., Albenne, C., Clemente, H. S. et al., Analysis of the xylem sap proteome of Brassica oleracea reveals a high content in secreted proteins. Proteomics 2011, 11, 1798-1813.
    • (2011) Proteomics , vol.11 , pp. 1798-1813
    • Ligat, L.1    Lauber, E.2    Albenne, C.3    Clemente, H.S.4
  • 145
    • 14644433039 scopus 로고    scopus 로고
    • Changes in the tobacco leaf apoplast proteome in response to salt stress
    • Dani, V., Simon, W. J., Duranti, M., Croy, R. R., Changes in the tobacco leaf apoplast proteome in response to salt stress. Proteomics 2005, 5, 737-745.
    • (2005) Proteomics , vol.5 , pp. 737-745
    • Dani, V.1    Simon, W.J.2    Duranti, M.3    Croy, R.R.4
  • 146
    • 38949120694 scopus 로고    scopus 로고
    • Identification by 2-D DIGE of apoplastic proteins regulated by oligogalacturonides in Arabidopsis thaliana
    • Casasoli, M., Spadoni, S., Lilley, K. S., Cervone, F. et al., Identification by 2-D DIGE of apoplastic proteins regulated by oligogalacturonides in Arabidopsis thaliana. Proteomics 2008, 8, 1042-1054.
    • (2008) Proteomics , vol.8 , pp. 1042-1054
    • Casasoli, M.1    Spadoni, S.2    Lilley, K.S.3    Cervone, F.4
  • 147
    • 0036668514 scopus 로고    scopus 로고
    • Analytical and biological variances associated with proteomic studies of Medicago truncatula by two-dimensional polyacrylamide gel electrophoresis
    • Asirvatham, V. S., Watson, B. S., Sumner, L. W., Analytical and biological variances associated with proteomic studies of Medicago truncatula by two-dimensional polyacrylamide gel electrophoresis. Proteomics 2002, 2, 960-968.
    • (2002) Proteomics , vol.2 , pp. 960-968
    • Asirvatham, V.S.1    Watson, B.S.2    Sumner, L.W.3
  • 148
    • 13244252296 scopus 로고    scopus 로고
    • The holm oak leaf proteome: analytical and biological variability in the protein expression level assessed by 2-DE and protein identification tandem mass spectrometry de novo sequencing and sequence similarity searching
    • Jorge, I., Navarro, R. M., Lenz, C., Ariza, D. et al., The holm oak leaf proteome: analytical and biological variability in the protein expression level assessed by 2-DE and protein identification tandem mass spectrometry de novo sequencing and sequence similarity searching. Proteomics 2005, 5, 222-234.
    • (2005) Proteomics , vol.5 , pp. 222-234
    • Jorge, I.1    Navarro, R.M.2    Lenz, C.3    Ariza, D.4
  • 149
    • 22044453401 scopus 로고    scopus 로고
    • A proteome approach defines protective functions of tobacco leaf trichomes
    • Amme, S., Rutten, T., Melzer, M., Sonsmann, G. et al., A proteome approach defines protective functions of tobacco leaf trichomes. Proteomics 2005, 5, 2508-2518.
    • (2005) Proteomics , vol.5 , pp. 2508-2518
    • Amme, S.1    Rutten, T.2    Melzer, M.3    Sonsmann, G.4
  • 150
    • 79251479735 scopus 로고    scopus 로고
    • Gel-based and gel-free proteomic analysis of Nicotiana tabacum trichomes identifies proteins involved in secondary metabolism and in the (a) biotic stress response
    • van Cutsem, E., Simonart, G., Degand, H., Faber, A. M. et al., Gel-based and gel-free proteomic analysis of Nicotiana tabacum trichomes identifies proteins involved in secondary metabolism and in the (a) biotic stress response. Proteomics 2011, 11, 440-454.
    • (2011) Proteomics , vol.11 , pp. 440-454
    • van Cutsem, E.1    Simonart, G.2    Degand, H.3    Faber, A.M.4
  • 151
    • 84888023062 scopus 로고    scopus 로고
    • Proteomic snapshot of spearmint (Mentha spicata L.) leaf trichomes: a genuine terpenoid factory
    • Champagne, A., Boutry, M., Proteomic snapshot of spearmint (Mentha spicata L.) leaf trichomes: a genuine terpenoid factory. Proteomics 2013, 13, 3327-3332.
    • (2013) Proteomics , vol.13 , pp. 3327-3332
    • Champagne, A.1    Boutry, M.2
  • 152
    • 84870196515 scopus 로고    scopus 로고
    • Identification of soybean proteins from a single cell type: the root hair
    • Brechenmacher, L., Nguyen, T. H. N., Hixson, K., Libault, M. et al., Identification of soybean proteins from a single cell type: the root hair. Proteomics 2012, 12, 3365-3373.
    • (2012) Proteomics , vol.12 , pp. 3365-3373
    • Brechenmacher, L.1    Nguyen, T.H.N.2    Hixson, K.3    Libault, M.4
  • 153
    • 0035523361 scopus 로고    scopus 로고
    • Sequential solubilization of proteins precipitated with trichloroacetic acid in acetone from cultured Catharanthus roseus cells yields 52% more spots after two-dimensional electrophoresis
    • Jacobs, D. I., van Rijssen, M. S., van der Heijden, R., Verpoorte, R., Sequential solubilization of proteins precipitated with trichloroacetic acid in acetone from cultured Catharanthus roseus cells yields 52% more spots after two-dimensional electrophoresis. Proteomics 2001, 1, 1345-1350.
    • (2001) Proteomics , vol.1 , pp. 1345-1350
    • Jacobs, D.I.1    van Rijssen, M.S.2    van der Heijden, R.3    Verpoorte, R.4
  • 154
    • 79960770457 scopus 로고    scopus 로고
    • New protein isoforms identified within Arabidopsis thaliana seed oil bodies combining chymotrypsin/trypsin digestion and peptide fragmentation analysis
    • Vermachova, M., Purkrtova, Z., Santrucek, J., Jolivet, P. et al., New protein isoforms identified within Arabidopsis thaliana seed oil bodies combining chymotrypsin/trypsin digestion and peptide fragmentation analysis. Proteomics 2011, 11, 3430-3434.
    • (2011) Proteomics , vol.11 , pp. 3430-3434
    • Vermachova, M.1    Purkrtova, Z.2    Santrucek, J.3    Jolivet, P.4
  • 155
    • 34447110006 scopus 로고    scopus 로고
    • Sample extraction techniques for enhanced proteomic analysis of plant tissues
    • Isaacson, T., Damasceno, C. M., Saravanan, R. S., He, Y. et al., Sample extraction techniques for enhanced proteomic analysis of plant tissues. Nat. Protoc. 2006, 1, 769-774.
    • (2006) Nat. Protoc. , vol.1 , pp. 769-774
    • Isaacson, T.1    Damasceno, C.M.2    Saravanan, R.S.3    He, Y.4
  • 156
    • 35649013698 scopus 로고    scopus 로고
    • Alternative and effective proteomic analysis in Arabidopsis
    • Espagne, C., Martinez, A., Valot, B., Meinnel, T., Giglione, C., Alternative and effective proteomic analysis in Arabidopsis. Proteomics 2007, 7, 3788-3799.
    • (2007) Proteomics , vol.7 , pp. 3788-3799
    • Espagne, C.1    Martinez, A.2    Valot, B.3    Meinnel, T.4    Giglione, C.5
  • 157
    • 68049087901 scopus 로고    scopus 로고
    • BiomarkerDigger: a versatile disease proteome database and analysis platform for the identification of plasma cancer biomarkers
    • Jeong, S. K., Kwon, M. S., Lee, E. Y., Lee, H. J. et al., BiomarkerDigger: a versatile disease proteome database and analysis platform for the identification of plasma cancer biomarkers. Proteomics 2009, 9, 3729-3740.
    • (2009) Proteomics , vol.9 , pp. 3729-3740
    • Jeong, S.K.1    Kwon, M.S.2    Lee, E.Y.3    Lee, H.J.4
  • 158
    • 84895750134 scopus 로고    scopus 로고
    • Protein extraction from plant tissues for 2DE and its application in proteomic analysis
    • Wu, X., Gong, F., Wang, W., Protein extraction from plant tissues for 2DE and its application in proteomic analysis. Proteomics 2014, 14, 645-658.
    • (2014) Proteomics , vol.14 , pp. 645-658
    • Wu, X.1    Gong, F.2    Wang, W.3
  • 160
    • 51649124682 scopus 로고    scopus 로고
    • Evaluation of three different protocols of protein extraction for Arabidopsis thaliana leaf proteome analysis by two-dimensional electrophoresis
    • Maldonado, A. M., Echevarria-Zomeno, S., Jean-Baptiste, S., Hernandez, M., Jorrin-Novo, J. V., Evaluation of three different protocols of protein extraction for Arabidopsis thaliana leaf proteome analysis by two-dimensional electrophoresis. J. Proteomics 2008, 71, 461-472.
    • (2008) J. Proteomics , vol.71 , pp. 461-472
    • Maldonado, A.M.1    Echevarria-Zomeno, S.2    Jean-Baptiste, S.3    Hernandez, M.4    Jorrin-Novo, J.V.5
  • 161
    • 0028049137 scopus 로고
    • Leaf protein contents and nitrogen-to-protein conversion factors for 90 plant species
    • Yeoh, H.-H., Wee, Y.-C., Leaf protein contents and nitrogen-to-protein conversion factors for 90 plant species. Food Chem. 1994, 49, 245-250.
    • (1994) Food Chem. , vol.49 , pp. 245-250
    • Yeoh, H.-H.1    Wee, Y.-C.2
  • 163
    • 79955018843 scopus 로고    scopus 로고
    • Comparative proteomics of seed maturation in oilseeds reveals differences in intermediary metabolism
    • Hajduch, M., Matusova, R., Houston, N. L., Thelen, J. J., Comparative proteomics of seed maturation in oilseeds reveals differences in intermediary metabolism. Proteomics 2011, 11, 1619-1629.
    • (2011) Proteomics , vol.11 , pp. 1619-1629
    • Hajduch, M.1    Matusova, R.2    Houston, N.L.3    Thelen, J.J.4
  • 164
    • 33645082204 scopus 로고    scopus 로고
    • Changes in cod muscle proteins during frozen storage revealed by proteome analysis and multivariate data analysis
    • Kjærsgård, I. V., Nørrelykke, M. R., Jessen, F., Changes in cod muscle proteins during frozen storage revealed by proteome analysis and multivariate data analysis. Proteomics 2006, 6, 1606-1618.
    • (2006) Proteomics , vol.6 , pp. 1606-1618
    • Kjærsgård, I.V.1    Nørrelykke, M.R.2    Jessen, F.3
  • 166
    • 34447575648 scopus 로고    scopus 로고
    • Proteomics of European beech (Fagus sylvatica L.) seed dormancy breaking: influence of abscisic and gibberellic acids
    • Pawłowski, T. A., Proteomics of European beech (Fagus sylvatica L.) seed dormancy breaking: influence of abscisic and gibberellic acids. Proteomics 2007, 7, 2246-2257.
    • (2007) Proteomics , vol.7 , pp. 2246-2257
    • Pawłowski, T.A.1
  • 167
    • 20944441193 scopus 로고    scopus 로고
    • Proteome analysis of early somatic embryogenesis in Picea glauca
    • Lippert, D., Zhuang, J., Ralph, S., Ellis, D. E. et al., Proteome analysis of early somatic embryogenesis in Picea glauca. Proteomics 2005, 5, 461-473.
    • (2005) Proteomics , vol.5 , pp. 461-473
    • Lippert, D.1    Zhuang, J.2    Ralph, S.3    Ellis, D.E.4
  • 168
    • 70349119507 scopus 로고    scopus 로고
    • Proteomic analysis from haploid and diploid embryos of Quercus suber L. identifies qualitative and quantitative differential expression patterns
    • Gómez, A., López, J. A., Pintos, B., Camafeita, E., Bueno, M. Á., Proteomic analysis from haploid and diploid embryos of Quercus suber L. identifies qualitative and quantitative differential expression patterns. Proteomics 2009, 9, 4355-4367.
    • (2009) Proteomics , vol.9 , pp. 4355-4367
    • Gómez, A.1    López, J.A.2    Pintos, B.3    Camafeita, E.4    Bueno, M.A.5
  • 169
    • 84890267953 scopus 로고    scopus 로고
    • The use of 2D-DIGE to understand the regeneration of somatic embryos in avocado
    • Guzmán-García, E., Sánchez-Romero, C., Panis, B., Carpentier, S. C., The use of 2D-DIGE to understand the regeneration of somatic embryos in avocado. Proteomics 2013, 13, 3498-3507.
    • (2013) Proteomics , vol.13 , pp. 3498-3507
    • Guzmán-García, E.1    Sánchez-Romero, C.2    Panis, B.3    Carpentier, S.C.4
  • 170
    • 66249138826 scopus 로고    scopus 로고
    • Proteomic analysis of the development and germination of date palm (Phoenix dactylifera L.) zygotic embryos
    • Sghaier-Hammami, B., Valledor, L., Drira, N., Jorrin-Novo, J. V., Proteomic analysis of the development and germination of date palm (Phoenix dactylifera L.) zygotic embryos. Proteomics 2009, 9, 2543-2554.
    • (2009) Proteomics , vol.9 , pp. 2543-2554
    • Sghaier-Hammami, B.1    Valledor, L.2    Drira, N.3    Jorrin-Novo, J.V.4
  • 171
    • 79954988552 scopus 로고    scopus 로고
    • Proteomics reveals potential biomarkers of seed vigor in sugarbeet
    • Catusse, J., Meinhard, J., Job, C., Strub, J. M. et al., Proteomics reveals potential biomarkers of seed vigor in sugarbeet. Proteomics 2011, 11, 1569-1580.
    • (2011) Proteomics , vol.11 , pp. 1569-1580
    • Catusse, J.1    Meinhard, J.2    Job, C.3    Strub, J.M.4
  • 172
    • 34447555622 scopus 로고    scopus 로고
    • Proteomic analysis of the cambial region in juvenile Eucalyptus grandis at three ages
    • Celedon, P. A. F., de Andrade, A., Meireles, K. G. X., da Cruz Gallo de Carvalho, M. et al., Proteomic analysis of the cambial region in juvenile Eucalyptus grandis at three ages. Proteomics 2007, 7, 2258-2274.
    • (2007) Proteomics , vol.7 , pp. 2258-2274
    • Celedon, P.A.F.1    de Andrade, A.2    Meireles, K.G.X.3    da Cruz Gallo de Carvalho, M.4
  • 173
    • 32944473420 scopus 로고    scopus 로고
    • Regeneration of the secondary vascular system in poplar as a novel system to investigate gene expression by a proteomic approach
    • Juan, D., Hong-Li, X., De-Qiang, Z., Xin-Qiang, H. et al., Regeneration of the secondary vascular system in poplar as a novel system to investigate gene expression by a proteomic approach. Proteomics 2006, 6, 881-895.
    • (2006) Proteomics , vol.6 , pp. 881-895
    • Juan, D.1    Hong-Li, X.2    De-Qiang, Z.3    Xin-Qiang, H.4
  • 174
  • 175
    • 84880085784 scopus 로고    scopus 로고
    • Progress and challenges for abiotic stress proteomics of crop plants
    • Barkla, B. J., Vera-Estrella, R., Pantoja, O., Progress and challenges for abiotic stress proteomics of crop plants. Proteomics 2013, 13, 1801-1815.
    • (2013) Proteomics , vol.13 , pp. 1801-1815
    • Barkla, B.J.1    Vera-Estrella, R.2    Pantoja, O.3
  • 176
    • 34548442959 scopus 로고    scopus 로고
    • Crop proteomics: aim at sustainable agriculture of tomorrow
    • Salekdeh, G. H., Komatsu, S., Crop proteomics: aim at sustainable agriculture of tomorrow. Proteomics 2007, 7, 2976-2996.
    • (2007) Proteomics , vol.7 , pp. 2976-2996
    • Salekdeh, G.H.1    Komatsu, S.2
  • 178
    • 84873996440 scopus 로고    scopus 로고
    • Proteomics dissection of plant responses to mineral nutrient deficiency
    • Liang, C., Tian, J., Liao, H., Proteomics dissection of plant responses to mineral nutrient deficiency. Proteomics 2013, 13, 624-636.
    • (2013) Proteomics , vol.13 , pp. 624-636
    • Liang, C.1    Tian, J.2    Liao, H.3
  • 179
    • 84873991566 scopus 로고    scopus 로고
    • Proteomics of phosphate use and deprivation in plants
    • Alexova, R., Millar, A. H., Proteomics of phosphate use and deprivation in plants. Proteomics 2013, 13, 609-623.
    • (2013) Proteomics , vol.13 , pp. 609-623
    • Alexova, R.1    Millar, A.H.2
  • 180
    • 66449129551 scopus 로고    scopus 로고
    • Recent developments in the application of proteomics to the analysis of plant responses to heavy metals
    • Ahsan, N., Renaut, J., Komatsu, S., Recent developments in the application of proteomics to the analysis of plant responses to heavy metals. Proteomics 2009, 9, 2602-2621.
    • (2009) Proteomics , vol.9 , pp. 2602-2621
    • Ahsan, N.1    Renaut, J.2    Komatsu, S.3
  • 181
    • 79954992716 scopus 로고    scopus 로고
    • Investigating the plant response to cadmium exposure by proteomic and metabolomic approaches
    • Villiers, F., Ducruix, C., Hugouvieux, V., Jarno, N. et al., Investigating the plant response to cadmium exposure by proteomic and metabolomic approaches. Proteomics 2011, 11, 1650-1663.
    • (2011) Proteomics , vol.11 , pp. 1650-1663
    • Villiers, F.1    Ducruix, C.2    Hugouvieux, V.3    Jarno, N.4
  • 182
    • 79960387002 scopus 로고    scopus 로고
    • Proteome analysis of host-pathogen interactions: investigation of pathogen responses to the host cell environment
    • Schmidt, F., Völker, U., Proteome analysis of host-pathogen interactions: investigation of pathogen responses to the host cell environment. Proteomics 2011, 11, 3203-3211.
    • (2011) Proteomics , vol.11 , pp. 3203-3211
    • Schmidt, F.1    Völker, U.2
  • 184
    • 67649184787 scopus 로고    scopus 로고
    • Generally detected proteins in comparative proteomics-a matter of cellular stress response
    • Wang, P., Bouwman, F. G., Mariman, E., Generally detected proteins in comparative proteomics-a matter of cellular stress response? Proteomics 2009, 9, 2955-2966.
    • (2009) Proteomics , vol.9 , pp. 2955-2966
    • Wang, P.1    Bouwman, F.G.2    Mariman, E.3
  • 185
    • 78649841084 scopus 로고    scopus 로고
    • Back to the basics: maximizing the information obtained by quantitative two dimensional gel electrophoresis analyses by an appropriate experimental design and statistical analyses
    • Valledor, L., Jorrín, J., Back to the basics: maximizing the information obtained by quantitative two dimensional gel electrophoresis analyses by an appropriate experimental design and statistical analyses. J. Proteomics 2011, 74, 1-18.
    • (2011) J. Proteomics , vol.74 , pp. 1-18
    • Valledor, L.1    Jorrín, J.2
  • 186
    • 79952310105 scopus 로고    scopus 로고
    • Statistical issues in quality control of proteomic analyses: good experimental design and planning
    • Cairns, D. A., Statistical issues in quality control of proteomic analyses: good experimental design and planning. Proteomics 2011, 11, 1037-1048.
    • (2011) Proteomics , vol.11 , pp. 1037-1048
    • Cairns, D.A.1
  • 187
    • 33750362838 scopus 로고    scopus 로고
    • Statistics for proteomics: a review of tools for analyzing experimental data
    • Urfer, W., Grzegorczyk, M., Jung, K., Statistics for proteomics: a review of tools for analyzing experimental data. Proteomics 2006, 6, 48-55.
    • (2006) Proteomics , vol.6 , pp. 48-55
    • Urfer, W.1    Grzegorczyk, M.2    Jung, K.3
  • 188
    • 79958118891 scopus 로고    scopus 로고
    • The role of statistical power analysis in quantitative proteomics
    • Levin, Y., The role of statistical power analysis in quantitative proteomics. Proteomics 2011, 11, 2565-2567.
    • (2011) Proteomics , vol.11 , pp. 2565-2567
    • Levin, Y.1
  • 189
    • 77951046988 scopus 로고    scopus 로고
    • Using a cross-model loadings plot to identify protein spots causing 2-DE gels to become outliers in PCA
    • Kristiansen, L. C., Jacobsen, S., Jessen, F., Jørgensen, B. M., Using a cross-model loadings plot to identify protein spots causing 2-DE gels to become outliers in PCA. Proteomics 2010, 10, 1721-1723.
    • (2010) Proteomics , vol.10 , pp. 1721-1723
    • Kristiansen, L.C.1    Jacobsen, S.2    Jessen, F.3    Jørgensen, B.M.4
  • 190
    • 84896771417 scopus 로고    scopus 로고
    • Distributed computing and data storage in proteomics: many hands make light work, and a stronger memory
    • Verheggen, K., Barsnes, H., Martens, L., Distributed computing and data storage in proteomics: many hands make light work, and a stronger memory. Proteomics 2014, 14, 367-377.
    • (2014) Proteomics , vol.14 , pp. 367-377
    • Verheggen, K.1    Barsnes, H.2    Martens, L.3
  • 191
    • 22044456721 scopus 로고    scopus 로고
    • Preparation of protein extracts from recalcitrant plant tissues: an evaluation of different methods for two-dimensional gel electrophoresis analysis
    • Carpentier, S. C., Witters, E., Laukens, K., Deckers, P. et al., Preparation of protein extracts from recalcitrant plant tissues: an evaluation of different methods for two-dimensional gel electrophoresis analysis. Proteomics 2005, 5, 2497-2507.
    • (2005) Proteomics , vol.5 , pp. 2497-2507
    • Carpentier, S.C.1    Witters, E.2    Laukens, K.3    Deckers, P.4
  • 192
    • 0037347236 scopus 로고    scopus 로고
    • Evaluation of nonionic and zwitterionic detergents as membrane protein solubilizers in two-dimensional electrophoresis
    • Luche, S., Santoni, V., Rabilloud, T., Evaluation of nonionic and zwitterionic detergents as membrane protein solubilizers in two-dimensional electrophoresis. Proteomics 2003, 3, 249-253.
    • (2003) Proteomics , vol.3 , pp. 249-253
    • Luche, S.1    Santoni, V.2    Rabilloud, T.3
  • 193
    • 10644268451 scopus 로고    scopus 로고
    • Zooming in: fractionation strategies in proteomics
    • Stasyk, T., Huber, L. A., Zooming in: fractionation strategies in proteomics. Proteomics 2004, 4, 3704-3716.
    • (2004) Proteomics , vol.4 , pp. 3704-3716
    • Stasyk, T.1    Huber, L.A.2
  • 194
    • 84901832799 scopus 로고    scopus 로고
    • Identification of proteins associated with ion homeostasis and salt tolerance in barley
    • Wu, D., Shen, Q., Qiu, L., Han, Y. et al., Identification of proteins associated with ion homeostasis and salt tolerance in barley. Proteomics 2014, 14, 1381-1392.
    • (2014) Proteomics , vol.14 , pp. 1381-1392
    • Wu, D.1    Shen, Q.2    Qiu, L.3    Han, Y.4
  • 195
    • 84887070144 scopus 로고    scopus 로고
    • Sample preparation for two-dimensional gel electrophoresis: considering the composition of biological material
    • 3106-2108
    • Knigge, T., Letendre, J., Monsinjon, T., Sample preparation for two-dimensional gel electrophoresis: considering the composition of biological material. Proteomics 2013, 13, 3106-2108.
    • (2013) Proteomics , vol.13
    • Knigge, T.1    Letendre, J.2    Monsinjon, T.3
  • 196
    • 4444237731 scopus 로고    scopus 로고
    • A critical evaluation of sample extraction techniques for enhanced proteomic analysis of recalcitrant plant tissues
    • Saravanan, R. S., Rose, J. K., A critical evaluation of sample extraction techniques for enhanced proteomic analysis of recalcitrant plant tissues. Proteomics 2004, 4, 2522-2532.
    • (2004) Proteomics , vol.4 , pp. 2522-2532
    • Saravanan, R.S.1    Rose, J.K.2
  • 197
    • 84859995893 scopus 로고    scopus 로고
    • Improving gel-based proteome analysis of soluble protein extracts by heat prefractionation
    • Wang, W., Wu, X., Xiong, E., Tai, F., Improving gel-based proteome analysis of soluble protein extracts by heat prefractionation. Proteomics 2012, 12, 938-943.
    • (2012) Proteomics , vol.12 , pp. 938-943
    • Wang, W.1    Wu, X.2    Xiong, E.3    Tai, F.4
  • 198
    • 59449111124 scopus 로고    scopus 로고
    • Combining subproteome enrichment and Rubisco depletion enables identification of low abundance proteins differentially regulated during plant defense
    • Widjaja, I., Naumann, K., Roth, U., Wolf, N. et al., Combining subproteome enrichment and Rubisco depletion enables identification of low abundance proteins differentially regulated during plant defense. Proteomics 2009, 9, 138-147.
    • (2009) Proteomics , vol.9 , pp. 138-147
    • Widjaja, I.1    Naumann, K.2    Roth, U.3    Wolf, N.4
  • 199
    • 84880628089 scopus 로고    scopus 로고
    • Depletion of abundant plant RuBisCO protein using the protamine sulfate precipitation method
    • Kim, Y. J., Lee, H. M., Wang, Y., Wu, J. et al., Depletion of abundant plant RuBisCO protein using the protamine sulfate precipitation method. Proteomics 2013, 13, 2176-2179.
    • (2013) Proteomics , vol.13 , pp. 2176-2179
    • Kim, Y.J.1    Lee, H.M.2    Wang, Y.3    Wu, J.4
  • 200
    • 67649184776 scopus 로고    scopus 로고
    • A rapid and simple procedure for the depletion of abundant storage proteins from legume seeds to advance proteome analysis: a case study using Glycine max
    • Krishnan, H. B., Oehrle, N. W., Natarajan, S. S., A rapid and simple procedure for the depletion of abundant storage proteins from legume seeds to advance proteome analysis: a case study using Glycine max. Proteomics 2009, 9, 3174-3188.
    • (2009) Proteomics , vol.9 , pp. 3174-3188
    • Krishnan, H.B.1    Oehrle, N.W.2    Natarajan, S.S.3
  • 201
    • 48849086000 scopus 로고    scopus 로고
    • The ProteoMiner and the FortyNiners: searching for gold nuggets in the proteomic arena
    • Righetti, P. G., Boschetti, E., The ProteoMiner and the FortyNiners: searching for gold nuggets in the proteomic arena. Mass Spectrom. Rev. 2008, 27, 596-608.
    • (2008) Mass Spectrom. Rev. , vol.27 , pp. 596-608
    • Righetti, P.G.1    Boschetti, E.2
  • 202
    • 0035106351 scopus 로고    scopus 로고
    • Large-scale analysis of the yeast proteome by multidimensional protein identification technology
    • Washburn, M. P., Wolters, D., Yates 3rd, J. R., Large-scale analysis of the yeast proteome by multidimensional protein identification technology. Nat. Biotechnol. 2001, 19, 242-247.
    • (2001) Nat. Biotechnol. , vol.19 , pp. 242-247
    • Washburn, M.P.1    Wolters, D.2    Yates 3rd, J.R.3
  • 203
    • 31344473515 scopus 로고    scopus 로고
    • Arabidopsis cell wall proteome defined using multidimensional protein identification technology
    • Bayer, E. M., Bottrill, A. R., Walshaw, J., Vigouroux, M. et al., Arabidopsis cell wall proteome defined using multidimensional protein identification technology. Proteomics 2006, 6, 301-311.
    • (2006) Proteomics , vol.6 , pp. 301-311
    • Bayer, E.M.1    Bottrill, A.R.2    Walshaw, J.3    Vigouroux, M.4
  • 204
    • 33645466243 scopus 로고    scopus 로고
    • Toward the complete membrane proteome high coverage of integral membrane proteins through transmembrane peptide detection
    • Fischer, F., Wolters, D., Rögner, M., Poetsch, A., Toward the complete membrane proteome high coverage of integral membrane proteins through transmembrane peptide detection. Mol. Cell. Proteomics 2006, 5, 444-453.
    • (2006) Mol. Cell. Proteomics , vol.5 , pp. 444-453
    • Fischer, F.1    Wolters, D.2    Rögner, M.3    Poetsch, A.4
  • 205
    • 0034649566 scopus 로고    scopus 로고
    • Analysis of the genome sequence of the flowering plant Arabidopsis thaliana
    • Analysis of the genome sequence of the flowering plant Arabidopsis thaliana. Nature 2000, 408, 796-815.
    • (2000) Nature , vol.408 , pp. 796-815
  • 206
    • 79955765369 scopus 로고    scopus 로고
    • Protein spot detection and quantification in 2-DE gel images using machine-learning methods
    • Tsakanikas, P., Manolakos, E. S., Protein spot detection and quantification in 2-DE gel images using machine-learning methods. Proteomics 2011, 11, 2038-2050.
    • (2011) Proteomics , vol.11 , pp. 2038-2050
    • Tsakanikas, P.1    Manolakos, E.S.2
  • 207
    • 37049006551 scopus 로고    scopus 로고
    • A workflow to increase the detection rate of proteins from unsequenced organisms in high-throughput proteomics experiments
    • Grossmann, J., Fischer, B., Baerenfaller, K., Owiti, J. et al., A workflow to increase the detection rate of proteins from unsequenced organisms in high-throughput proteomics experiments. Proteomics 2007, 7, 4245-4254.
    • (2007) Proteomics , vol.7 , pp. 4245-4254
    • Grossmann, J.1    Fischer, B.2    Baerenfaller, K.3    Owiti, J.4
  • 208
    • 77949768663 scopus 로고    scopus 로고
    • Maximizing the sensitivity and reliability of peptide identification in large-scale proteomic experiments by harnessing multiple search engines
    • Yu, W., Taylor, J. A., Davis, M. T., Bonilla, L. E. et al., Maximizing the sensitivity and reliability of peptide identification in large-scale proteomic experiments by harnessing multiple search engines. Proteomics 2010, 10, 1172-1189.
    • (2010) Proteomics , vol.10 , pp. 1172-1189
    • Yu, W.1    Taylor, J.A.2    Davis, M.T.3    Bonilla, L.E.4
  • 210
    • 79952309827 scopus 로고    scopus 로고
    • Quality meets quantity-quality control, data standards and repositories
    • Eisenacher, M., Schnabel, A., Stephan, C., Quality meets quantity-quality control, data standards and repositories. Proteomics 2011, 11, 1031-1036.
    • (2011) Proteomics , vol.11 , pp. 1031-1036
    • Eisenacher, M.1    Schnabel, A.2    Stephan, C.3
  • 211
    • 0343376097 scopus 로고    scopus 로고
    • Difference gel electrophoresis: a single gel method for detecting changes in protein extracts
    • Unlu, M., Morgan, M. E., Minden, J. S., Difference gel electrophoresis: a single gel method for detecting changes in protein extracts. Electrophoresis 1997, 18, 2071-2077.
    • (1997) Electrophoresis , vol.18 , pp. 2071-2077
    • Unlu, M.1    Morgan, M.E.2    Minden, J.S.3
  • 212
    • 82955170647 scopus 로고    scopus 로고
    • Preventing and troubleshooting artefacts in saturation labelled fluorescence 2-D difference gel electrophoresis (saturation DiGE)
    • McNamara, L. E., Kantawong, F. A., Dalby, M. J., Riehle, M. O., Burchmore, R., Preventing and troubleshooting artefacts in saturation labelled fluorescence 2-D difference gel electrophoresis (saturation DiGE). Proteomics 2011, 11, 4610-4621.
    • (2011) Proteomics , vol.11 , pp. 4610-4621
    • McNamara, L.E.1    Kantawong, F.A.2    Dalby, M.J.3    Riehle, M.O.4    Burchmore, R.5
  • 213
    • 0033535961 scopus 로고    scopus 로고
    • Accurate quantitation of protein expression and site-specific phosphorylation
    • Oda, Y., Huang, K., Cross, F. R., Cowburn, D., Chait, B. T., Accurate quantitation of protein expression and site-specific phosphorylation. Proc. Natl. Acad. Sci. 1999, 96, 6591-6596.
    • (1999) Proc. Natl. Acad. Sci. , vol.96 , pp. 6591-6596
    • Oda, Y.1    Huang, K.2    Cross, F.R.3    Cowburn, D.4    Chait, B.T.5
  • 214
    • 84896762078 scopus 로고    scopus 로고
    • Quantitative analysis of protein turnover in plants
    • Nelson, C. J., Li, L., Millar, A. H., Quantitative analysis of protein turnover in plants. Proteomics 2014, 14, 579-592.
    • (2014) Proteomics , vol.14 , pp. 579-592
    • Nelson, C.J.1    Li, L.2    Millar, A.H.3
  • 215
    • 34548725468 scopus 로고    scopus 로고
    • Proteomics technologies and challenges
    • Cho, W., Proteomics technologies and challenges. Genomics Proteomics Bioinformatics 2007, 5, 77-85.
    • (2007) Genomics Proteomics Bioinformatics , vol.5 , pp. 77-85
    • Cho, W.1
  • 217
    • 0032875697 scopus 로고    scopus 로고
    • Quantitative analysis of complex protein mixtures using isotope-coded affinity tags
    • Gygi, S. P., Rist, B., Gerber, S. A., Turecek, F. et al., Quantitative analysis of complex protein mixtures using isotope-coded affinity tags. Nat. Biotech. 1999, 17, 994-999.
    • (1999) Nat. Biotech. , vol.17 , pp. 994-999
    • Gygi, S.P.1    Rist, B.2    Gerber, S.A.3    Turecek, F.4
  • 218
    • 3042581458 scopus 로고    scopus 로고
    • Analysis of curated and predicted plastid subproteomes of Arabidopsis. Subcellular compartmentalization leads to distinctive proteome properties
    • Sun, Q., Emanuelsson, O., van Wijk, K. J., Analysis of curated and predicted plastid subproteomes of Arabidopsis. Subcellular compartmentalization leads to distinctive proteome properties. Plant Physiol. 2004, 135, 723-734.
    • (2004) Plant Physiol. , vol.135 , pp. 723-734
    • Sun, Q.1    Emanuelsson, O.2    van Wijk, K.J.3
  • 220
    • 79952293306 scopus 로고    scopus 로고
    • Challenges for proteomics core facilities
    • Lilley, K. S., Deery, M. J., Gatto, L., Challenges for proteomics core facilities. Proteomics 2011, 11, 1017-1025.
    • (2011) Proteomics , vol.11 , pp. 1017-1025
    • Lilley, K.S.1    Deery, M.J.2    Gatto, L.3
  • 221
    • 63349084973 scopus 로고    scopus 로고
    • Advancements in plant proteomics using quantitative mass spectrometry
    • Oeljeklaus, S., Meyer, H. E., Warscheid, B., Advancements in plant proteomics using quantitative mass spectrometry. J. Proteomics 2009, 72, 545-554.
    • (2009) J. Proteomics , vol.72 , pp. 545-554
    • Oeljeklaus, S.1    Meyer, H.E.2    Warscheid, B.3
  • 222
    • 0036898579 scopus 로고    scopus 로고
    • Protein microarrays and proteomics
    • MacBeath, G., Protein microarrays and proteomics. Nat. Genet. 2002, 32, 526-532.
    • (2002) Nat. Genet. , vol.32 , pp. 526-532
    • MacBeath, G.1
  • 224
    • 0041408938 scopus 로고    scopus 로고
    • Electrostatic axially harmonic orbital trapping: a high-performance technique of mass analysis
    • Makarov, A., Electrostatic axially harmonic orbital trapping: a high-performance technique of mass analysis. Anal. Chem. 2000, 72, 1156-1162.
    • (2000) Anal. Chem. , vol.72 , pp. 1156-1162
    • Makarov, A.1
  • 225
    • 0037398266 scopus 로고    scopus 로고
    • Interfacing the orbitrap mass analyzer to an electrospray ion source
    • Hardman, M., Makarov, A. A., Interfacing the orbitrap mass analyzer to an electrospray ion source. Anal. Chem. 2003, 75, 1699-1705.
    • (2003) Anal. Chem. , vol.75 , pp. 1699-1705
    • Hardman, M.1    Makarov, A.A.2
  • 226
    • 67651173106 scopus 로고    scopus 로고
    • Proteomics by mass spectrometry: approaches, advances, and applications
    • Yates, J. R., Ruse, C. I., Nakorchevsky, A., Proteomics by mass spectrometry: approaches, advances, and applications. Annu. Rev. Biomed. Eng. 2009, 11, 49-79.
    • (2009) Annu. Rev. Biomed. Eng. , vol.11 , pp. 49-79
    • Yates, J.R.1    Ruse, C.I.2    Nakorchevsky, A.3
  • 227
    • 33750364830 scopus 로고    scopus 로고
    • The human urinary proteome contains more than 1500 proteins, including a large proportion of membrane proteins
    • R80
    • Adachi, J., Kumar, C., Zhang, Y., Olsen, J. V., Mann, M., The human urinary proteome contains more than 1500 proteins, including a large proportion of membrane proteins. Genome Biol. 2006, 7, R80.
    • (2006) Genome Biol. , vol.7
    • Adachi, J.1    Kumar, C.2    Zhang, Y.3    Olsen, J.V.4    Mann, M.5
  • 228
    • 33748754288 scopus 로고    scopus 로고
    • Identification of 491 proteins in the tear fluid proteome reveals a large number of proteases and protease inhibitors
    • R72
    • de Souza, G. A., Godoy, L. M., Mann, M., Identification of 491 proteins in the tear fluid proteome reveals a large number of proteases and protease inhibitors. Genome Biol. 2006, 7, R72.
    • (2006) Genome Biol. , vol.7
    • de Souza, G.A.1    Godoy, L.M.2    Mann, M.3
  • 229
    • 44349099751 scopus 로고    scopus 로고
    • Sorting signals, N-terminal modifications and abundance of the chloroplast proteome
    • Zybailov, B., Rutschow, H., Friso, G., Rudella, A. et al., Sorting signals, N-terminal modifications and abundance of the chloroplast proteome. PLoS One 2008, 3, e1994.
    • (2008) PLoS One , vol.3 , pp. e1994
    • Zybailov, B.1    Rutschow, H.2    Friso, G.3    Rudella, A.4
  • 230
    • 84855549488 scopus 로고    scopus 로고
    • System-wide perturbation analysis with nearly complete coverage of the yeast proteome by single-shot ultra HPLC runs on a bench top Orbitrap
    • M111.013722.
    • Nagaraj, N., Kulak, N. A., Cox, J., Neuhauser, N. et al., System-wide perturbation analysis with nearly complete coverage of the yeast proteome by single-shot ultra HPLC runs on a bench top Orbitrap. Mol. Cell. Proteomics 2012, 11, M111.013722.
    • (2012) Mol. Cell. Proteomics , vol.11
    • Nagaraj, N.1    Kulak, N.A.2    Cox, J.3    Neuhauser, N.4
  • 231
    • 84901846221 scopus 로고    scopus 로고
    • An improved detergent-compatible gel-fractionation LC-LTQ-Orbitrap-MS workflow for plant and microbial proteomics
    • Jorrín-Novo, J. V., Komatsu, S., Weckwerth, W., Wienkoop, S., Eds.), Humana Press
    • Valledor, L., Weckwerth, W., An improved detergent-compatible gel-fractionation LC-LTQ-Orbitrap-MS workflow for plant and microbial proteomics, Jorrín-Novo, J. V., Komatsu, S., Weckwerth, W., Wienkoop, S., (Eds.), Plant Proteomics Humana Press 2014, pp. 379-389.
    • (2014) Plant Proteomics , pp. 379-389
    • Valledor, L.1    Weckwerth, W.2
  • 232
    • 35848949043 scopus 로고    scopus 로고
    • Decoding protein modifications using top-down mass spectrometry
    • Siuti, N., Kelleher, N. L., Decoding protein modifications using top-down mass spectrometry. Nat. Methods 2007, 4, 817-821.
    • (2007) Nat. Methods , vol.4 , pp. 817-821
    • Siuti, N.1    Kelleher, N.L.2
  • 233
    • 33749606981 scopus 로고    scopus 로고
    • Extending top-down mass spectrometry to proteins with masses greater than 200 kilodaltons
    • Han, X., Jin, M., Breuker, K., McLafferty, F. W., Extending top-down mass spectrometry to proteins with masses greater than 200 kilodaltons. Science 2006, 314, 109-112.
    • (2006) Science , vol.314 , pp. 109-112
    • Han, X.1    Jin, M.2    Breuker, K.3    McLafferty, F.W.4
  • 234
    • 2642578319 scopus 로고    scopus 로고
    • A new approach for plant proteomics characterization of chloroplast proteins of arabidopsis thaliana by top-down mass spectrometry
    • Zabrouskov, V., Giacomelli, L., van Wijk, K. J., McLafferty, F. W., A new approach for plant proteomics characterization of chloroplast proteins of arabidopsis thaliana by top-down mass spectrometry. Mol. Cell. Proteomics 2003, 2, 1253-1260.
    • (2003) Mol. Cell. Proteomics , vol.2 , pp. 1253-1260
    • Zabrouskov, V.1    Giacomelli, L.2    van Wijk, K.J.3    McLafferty, F.W.4
  • 235
    • 63749117839 scopus 로고    scopus 로고
    • A top-down approach to infer and compare domain-domain interactions across eight model organisms
    • Guda, C., King, B. R., Pal, L. R., Guda, P., A top-down approach to infer and compare domain-domain interactions across eight model organisms. PloS One 2009, 4, e5096.
    • (2009) PloS One , vol.4 , pp. e5096
    • Guda, C.1    King, B.R.2    Pal, L.R.3    Guda, P.4
  • 236
    • 84860866702 scopus 로고    scopus 로고
    • Highly multiplexed targeted proteomics using precise control of peptide retention time
    • Gallien, S., Peterman, S., Kiyonami, R., Souady, J. et al., Highly multiplexed targeted proteomics using precise control of peptide retention time. Proteomics 2012, 12, 1122-1133.
    • (2012) Proteomics , vol.12 , pp. 1122-1133
    • Gallien, S.1    Peterman, S.2    Kiyonami, R.3    Souady, J.4
  • 237
    • 84860872156 scopus 로고    scopus 로고
    • The development of selected reaction monitoring methods for targeted proteomics via empirical refinement
    • Bereman, M. S., MacLean, B., Tomazela, D. M., Liebler, D. C., MacCoss, M. J., The development of selected reaction monitoring methods for targeted proteomics via empirical refinement. Proteomics 2012, 12, 1134-1141.
    • (2012) Proteomics , vol.12 , pp. 1134-1141
    • Bereman, M.S.1    MacLean, B.2    Tomazela, D.M.3    Liebler, D.C.4    MacCoss, M.J.5
  • 238
    • 51249117296 scopus 로고    scopus 로고
    • If the antibody fails - a mass Western approach
    • Lehmann, U., Wienkoop, S., Tschoep, H., Weckwerth, W., If the antibody fails - a mass Western approach. Plant J. 2008, 55, 1039-1046.
    • (2008) Plant J. , vol.55 , pp. 1039-1046
    • Lehmann, U.1    Wienkoop, S.2    Tschoep, H.3    Weckwerth, W.4
  • 239
    • 84908388827 scopus 로고    scopus 로고
    • Targeted quantitative analysis of a diurnal RuBisCO subunit expression and translation profile in Chlamydomonas reinhardtii introducing a novel mass Western approach
    • Recuenco-Muñoz, L., Offre, P., Valledor, L., Lyon, D. et al., Targeted quantitative analysis of a diurnal RuBisCO subunit expression and translation profile in Chlamydomonas reinhardtii introducing a novel mass Western approach. J. Proteomics 2014, 113, 143-153.
    • (2014) J. Proteomics , vol.113 , pp. 143-153
    • Recuenco-Muñoz, L.1    Offre, P.2    Valledor, L.3    Lyon, D.4
  • 240
    • 84896757081 scopus 로고    scopus 로고
    • The next level of complexity: crosstalk of posttranslational modifications
    • Venne, A. S., Kollipara, L., Zahedi, R. P., The next level of complexity: crosstalk of posttranslational modifications. Proteomics 2014, 14, 513-524.
    • (2014) Proteomics , vol.14 , pp. 513-524
    • Venne, A.S.1    Kollipara, L.2    Zahedi, R.P.3
  • 241
    • 84880611990 scopus 로고    scopus 로고
    • When 2D is not enough, go for an extra dimension
    • Rabilloud, T., When 2D is not enough, go for an extra dimension. Proteomics 2013, 13, 2065-2068.
    • (2013) Proteomics , vol.13 , pp. 2065-2068
    • Rabilloud, T.1
  • 242
    • 84880623873 scopus 로고    scopus 로고
    • Evaluation of three-dimensional gel electrophoresis to improve quantitative profiling of complex proteomes
    • Colignon, B., Raes, M., Dieu, M., Delaive, E., Mauro, S., Evaluation of three-dimensional gel electrophoresis to improve quantitative profiling of complex proteomes. Proteomics 2013, 13, 2077-2082.
    • (2013) Proteomics , vol.13 , pp. 2077-2082
    • Colignon, B.1    Raes, M.2    Dieu, M.3    Delaive, E.4    Mauro, S.5
  • 243
    • 84858718127 scopus 로고    scopus 로고
    • Green systems biology - from single genomes, proteomes and metabolomes to ecosystems research and biotechnology
    • Weckwerth, W., Green systems biology - from single genomes, proteomes and metabolomes to ecosystems research and biotechnology. J. Proteomics 2011, 75, 284-305.
    • (2011) J. Proteomics , vol.75 , pp. 284-305
    • Weckwerth, W.1
  • 245
    • 79959258968 scopus 로고    scopus 로고
    • Sparse PLS discriminant analysis: biologically relevant feature selection and graphical displays for multiclass problems
    • Le Cao, K.-A., Boitard, S., Besse, P., Sparse PLS discriminant analysis: biologically relevant feature selection and graphical displays for multiclass problems. BMC Bioinformatics 2011, 12, 253.
    • (2011) BMC Bioinformatics , vol.12 , pp. 253
    • Le Cao, K.-A.1    Boitard, S.2    Besse, P.3
  • 246
    • 0034069495 scopus 로고    scopus 로고
    • Gene ontology: tool for the unification of biology
    • Ashburner, M., Ball, C. A., Blake, J. A., Botstein, D. et al., Gene ontology: tool for the unification of biology. Nat. Genet. 2000, 25, 25-29.
    • (2000) Nat. Genet. , vol.25 , pp. 25-29
    • Ashburner, M.1    Ball, C.A.2    Blake, J.A.3    Botstein, D.4
  • 247
    • 12144291195 scopus 로고    scopus 로고
    • Mapman: a user-driven tool to display genomics data sets onto diagrams of metabolic pathways and other biological processes
    • Thimm, O., Bläsing, O., Gibon, Y., Nagel, A. et al., Mapman: a user-driven tool to display genomics data sets onto diagrams of metabolic pathways and other biological processes. Plant J. 2004, 37, 914-939.
    • (2004) Plant J. , vol.37 , pp. 914-939
    • Thimm, O.1    Bläsing, O.2    Gibon, Y.3    Nagel, A.4
  • 248
    • 84892788440 scopus 로고    scopus 로고
    • Constraint-based models predict metabolic and associated cellular functions
    • Bordbar, A., Monk, J. M., King, Z. A., Palsson, B. O., Constraint-based models predict metabolic and associated cellular functions. Nat. Rev. Genet. 2014, 15, 107-120.
    • (2014) Nat. Rev. Genet. , vol.15 , pp. 107-120
    • Bordbar, A.1    Monk, J.M.2    King, Z.A.3    Palsson, B.O.4
  • 250
    • 27644543078 scopus 로고    scopus 로고
    • Comparison of label-free methods for quantifying human proteins by shotgun proteomics
    • Old, W. M., Meyer-Arendt, K., Aveline-Wolf, L., Pierce, K. G. et al., Comparison of label-free methods for quantifying human proteins by shotgun proteomics. Mol. Cell. Proteomics 2005, 4, 1487-1502.
    • (2005) Mol. Cell. Proteomics , vol.4 , pp. 1487-1502
    • Old, W.M.1    Meyer-Arendt, K.2    Aveline-Wolf, L.3    Pierce, K.G.4
  • 251
    • 79551500036 scopus 로고    scopus 로고
    • Less label, more free: approaches in label-free quantitative mass spectrometry
    • Neilson, K. A., Ali, N. A., Muralidharan, S., Mirzaei, M. et al., Less label, more free: approaches in label-free quantitative mass spectrometry. Proteomics 2011, 11, 535-553.
    • (2011) Proteomics , vol.11 , pp. 535-553
    • Neilson, K.A.1    Ali, N.A.2    Muralidharan, S.3    Mirzaei, M.4
  • 252
    • 84865576726 scopus 로고    scopus 로고
    • Quantitative mass spectrometry in proteomics: critical review update from 2007 to the present
    • Bantscheff, M., Lemeer, S., Savitski, M. M., Kuster, B., Quantitative mass spectrometry in proteomics: critical review update from 2007 to the present. Anal. Bioanal. Chem. 2012, 404, 939-965.
    • (2012) Anal. Bioanal. Chem. , vol.404 , pp. 939-965
    • Bantscheff, M.1    Lemeer, S.2    Savitski, M.M.3    Kuster, B.4
  • 253
    • 84860854049 scopus 로고    scopus 로고
    • Advancing the sensitivity of selected reaction monitoring-based targeted quantitative proteomics
    • Shi, T., Su, D., Liu, T., Tang, K. et al., Advancing the sensitivity of selected reaction monitoring-based targeted quantitative proteomics. Proteomics 2012, 12, 1074-1092.
    • (2012) Proteomics , vol.12 , pp. 1074-1092
    • Shi, T.1    Su, D.2    Liu, T.3    Tang, K.4
  • 254
    • 34548183872 scopus 로고    scopus 로고
    • Protocol for micro-purification, enrichment, pre-fractionation and storage of peptides for proteomics using StageTips
    • Rappsilber, J., Mann, M., Ishihama, Y., Protocol for micro-purification, enrichment, pre-fractionation and storage of peptides for proteomics using StageTips. Nat. Protoc. 2007, 2, 1896-1906.
    • (2007) Nat. Protoc. , vol.2 , pp. 1896-1906
    • Rappsilber, J.1    Mann, M.2    Ishihama, Y.3
  • 255
    • 0029644596 scopus 로고
    • Method to correlate tandem mass spectra of modified peptides to amino acid sequences in the protein database
    • Yates III, J. R., Eng, J. K., McCormack, A. L., Schieltz, D., Method to correlate tandem mass spectra of modified peptides to amino acid sequences in the protein database. Anal. Chem. 1995, 67, 1426-1436.
    • (1995) Anal. Chem. , vol.67 , pp. 1426-1436
    • Yates, J.R.1    Eng, J.K.2    McCormack, A.L.3    Schieltz, D.4
  • 256
    • 0036828724 scopus 로고    scopus 로고
    • Probability-based validation of protein identifications using a modified SEQUEST algorithm
    • MacCoss, M. J., Wu, C. C., Yates, J. R., Probability-based validation of protein identifications using a modified SEQUEST algorithm. Anal. Chem. 2002, 74, 5593-5599.
    • (2002) Anal. Chem. , vol.74 , pp. 5593-5599
    • MacCoss, M.J.1    Wu, C.C.2    Yates, J.R.3
  • 257
    • 0027286502 scopus 로고
    • MASCOT: multiple alignment system for protein sequences based on three-way dynamic programming
    • Hirosawa, M., Hoshida, M., Ishikawa, M., Toya, T., MASCOT: multiple alignment system for protein sequences based on three-way dynamic programming. Comp. Appl. Biosci. 1993, 9, 161-167.
    • (1993) Comp. Appl. Biosci. , vol.9 , pp. 161-167
    • Hirosawa, M.1    Hoshida, M.2    Ishikawa, M.3    Toya, T.4
  • 259
    • 34848889259 scopus 로고    scopus 로고
    • The paragon algorithm, a next generation search engine that uses sequence temperature values and feature probabilities to identify peptides from tandem mass spectra
    • Shilov, I. V., Seymour, S. L., Patel, A. A., Loboda, A. et al., The paragon algorithm, a next generation search engine that uses sequence temperature values and feature probabilities to identify peptides from tandem mass spectra. Mol. Cell. Proteomics 2007, 6, 1638-1655.
    • (2007) Mol. Cell. Proteomics , vol.6 , pp. 1638-1655
    • Shilov, I.V.1    Seymour, S.L.2    Patel, A.A.3    Loboda, A.4
  • 260
    • 84893824425 scopus 로고    scopus 로고
    • DeNovoGUI: an open source graphical user interface for de novo sequencing of tandem mass spectra
    • Muth, T., Weilnboöck, L., Rapp, E., Huber, C. G. et al., DeNovoGUI: an open source graphical user interface for de novo sequencing of tandem mass spectra. J. Proteome Res. 2014, 13, 1143-1146.
    • (2014) J. Proteome Res. , vol.13 , pp. 1143-1146
    • Muth, T.1    Weilnboöck, L.2    Rapp, E.3    Huber, C.G.4
  • 261
    • 0141989734 scopus 로고    scopus 로고
    • PEAKS: powerful software for peptide de novo sequencing by tandem mass spectrometry
    • Ma, B., Zhang, K., Hendrie, C., Liang, C. et al., PEAKS: powerful software for peptide de novo sequencing by tandem mass spectrometry. Rapid Commun. Mass Spectrom. 2003, 17, 2337-2342.
    • (2003) Rapid Commun. Mass Spectrom. , vol.17 , pp. 2337-2342
    • Ma, B.1    Zhang, K.2    Hendrie, C.3    Liang, C.4
  • 262
    • 84901773142 scopus 로고    scopus 로고
    • Non-model organisms, a species endangered by proteogenomics
    • Armengaud, J., Trapp, J., Pible, O., Geffard, O. et al., Non-model organisms, a species endangered by proteogenomics. J. Proteomics 2014, 105, 5-18.
    • (2014) J. Proteomics , vol.105 , pp. 5-18
    • Armengaud, J.1    Trapp, J.2    Pible, O.3    Geffard, O.4


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