메뉴 건너뛰기




Volumn 7, Issue 16, 2007, Pages 2963-2975

Subcellular shotgun proteomics in plants: Looking beyond the usual suspects

Author keywords

Liquid chromatography tandem mass spectrometry; Rice; Sample preparation; Shotgun proteomics; Subcellular fractionation

Indexed keywords

VEGETABLE PROTEIN;

EID: 34548461256     PISSN: 16159853     EISSN: 16159861     Source Type: Journal    
DOI: 10.1002/pmic.200700216     Document Type: Review
Times cited : (52)

References (145)
  • 1
    • 0034649566 scopus 로고    scopus 로고
    • Analysis of the genome sequence of the flowering plant Arabidopsis thaliana
    • AGI
    • AGI, Analysis of the genome sequence of the flowering plant Arabidopsis thaliana. Nature 2000, 408, 796-815.
    • (2000) Nature , vol.408 , pp. 796-815
  • 2
    • 0037023349 scopus 로고    scopus 로고
    • Goff, S. A., Ricke, D., Lan, T. H., Presting, G. et al., A draft sequence of the rice genome (Oryza sativa L. ssp. japonica). Science 2002, 296, 92-100.
    • Goff, S. A., Ricke, D., Lan, T. H., Presting, G. et al., A draft sequence of the rice genome (Oryza sativa L. ssp. japonica). Science 2002, 296, 92-100.
  • 3
    • 0037023384 scopus 로고    scopus 로고
    • A draft sequence of the rice genome (Oryza sativa L. ssp. indica)
    • Yu, J., Hu, S., Wang, J., Wong, G. K. et al., A draft sequence of the rice genome (Oryza sativa L. ssp. indica). Science 2002, 296, 79-92.
    • (2002) Science , vol.296 , pp. 79-92
    • Yu, J.1    Hu, S.2    Wang, J.3    Wong, G.K.4
  • 4
    • 33846111346 scopus 로고    scopus 로고
    • CLE peptide ligands and their roles in establishing meristems
    • Fiers, M., Ku, K. L., Liu, C. M., CLE peptide ligands and their roles in establishing meristems. Curr. Opin. Plant. Biol. 2007, 10, 39-43.
    • (2007) Curr. Opin. Plant. Biol , vol.10 , pp. 39-43
    • Fiers, M.1    Ku, K.L.2    Liu, C.M.3
  • 5
    • 0036482417 scopus 로고    scopus 로고
    • Peptides: New signalling molecules in plants
    • Lindsey, K., Casson, S., Chilley, P., Peptides: New signalling molecules in plants. Trends Plant Sci. 2002, 7, 78-83.
    • (2002) Trends Plant Sci , vol.7 , pp. 78-83
    • Lindsey, K.1    Casson, S.2    Chilley, P.3
  • 6
    • 33745589774 scopus 로고    scopus 로고
    • An endogenous peptide signal in Arabidopsis activates components of the innate immune response
    • Huffaker, A., Pearce, G., Ryan, C. A., An endogenous peptide signal in Arabidopsis activates components of the innate immune response. Proc. Natl. Acad. Sci. USA 2006, 103, 10098-10103.
    • (2006) Proc. Natl. Acad. Sci. USA , vol.103 , pp. 10098-10103
    • Huffaker, A.1    Pearce, G.2    Ryan, C.A.3
  • 7
    • 30044435245 scopus 로고    scopus 로고
    • The Oryza bacterial artificial chromosome library resource: Construction and analysis of 12 deep-coverage large-insert BAC libraries that represent the 10 genome types of the genus Oryza
    • Ammiraju, J. S., Luo, M., Goicoechea, J. L., Wang, W. et al., The Oryza bacterial artificial chromosome library resource: Construction and analysis of 12 deep-coverage large-insert BAC libraries that represent the 10 genome types of the genus Oryza. Genome Res. 2006, 16, 140-147.
    • (2006) Genome Res , vol.16 , pp. 140-147
    • Ammiraju, J.S.1    Luo, M.2    Goicoechea, J.L.3    Wang, W.4
  • 8
    • 0034697980 scopus 로고    scopus 로고
    • Predicting subcellular localization of proteins based on their N-terminal amino acid sequence
    • Emanuelsson, O., Nielsen, H., Brunak, S., von Heijne, G., Predicting subcellular localization of proteins based on their N-terminal amino acid sequence. J. Mol. Biol. 2000, 300, 1005-1016.
    • (2000) J. Mol. Biol , vol.300 , pp. 1005-1016
    • Emanuelsson, O.1    Nielsen, H.2    Brunak, S.3    von Heijne, G.4
  • 9
    • 3242875263 scopus 로고    scopus 로고
    • MITOPRED: A genome-scale method for prediction of nucleus-encoded mitochondrial proteins
    • Guda, C., Fahy, E., Subramaniam, S., MITOPRED: A genome-scale method for prediction of nucleus-encoded mitochondrial proteins. Bioinformatics 2004, 20, 1785-1794.
    • (2004) Bioinformatics , vol.20 , pp. 1785-1794
    • Guda, C.1    Fahy, E.2    Subramaniam, S.3
  • 10
    • 2942589051 scopus 로고    scopus 로고
    • Predotar: A tool for rapidly screening proteomes for N-terminal targeting sequences
    • Small, I., Peeters, N., Legeai, F., Lurin, C., Predotar: A tool for rapidly screening proteomes for N-terminal targeting sequences. Proteomics 2004, 4, 1581-1590.
    • (2004) Proteomics , vol.4 , pp. 1581-1590
    • Small, I.1    Peeters, N.2    Legeai, F.3    Lurin, C.4
  • 11
    • 0032972509 scopus 로고    scopus 로고
    • PSORT: A program for detecting sorting signals in proteins and predicting their subcellular localization
    • Nakai, K., Horton, P., PSORT: A program for detecting sorting signals in proteins and predicting their subcellular localization. Trends Biochem. Sci. 1999, 24, 34-36.
    • (1999) Trends Biochem. Sci , vol.24 , pp. 34-36
    • Nakai, K.1    Horton, P.2
  • 12
    • 33947407688 scopus 로고    scopus 로고
    • Evaluation and comparison of mammalian subcellular localization prediction methods
    • Sprenger, J., Fink, J. L., Teasdale, R. D., Evaluation and comparison of mammalian subcellular localization prediction methods. BMC Bioinformatics 2006, 7, S3.
    • (2006) BMC Bioinformatics , vol.7
    • Sprenger, J.1    Fink, J.L.2    Teasdale, R.D.3
  • 13
    • 0141746356 scopus 로고    scopus 로고
    • LumenP - A neural network predictor for protein localization in the thylakoid lumen
    • Westerlund, I., Von Heijne, G., Emanuelsson, O., LumenP - A neural network predictor for protein localization in the thylakoid lumen. Protein Sci. 2003, 12, 2360-2366.
    • (2003) Protein Sci , vol.12 , pp. 2360-2366
    • Westerlund, I.1    Von Heijne, G.2    Emanuelsson, O.3
  • 14
    • 32144438832 scopus 로고    scopus 로고
    • SubLoc: A server/client suite for protein subcellular location based on SOAP
    • Chen, H., Huang, N., Sun, Z., SubLoc: A server/client suite for protein subcellular location based on SOAP. Bioinformatics 2006, 22, 376-377.
    • (2006) Bioinformatics , vol.22 , pp. 376-377
    • Chen, H.1    Huang, N.2    Sun, Z.3
  • 16
    • 33846611391 scopus 로고    scopus 로고
    • Feature-based reappraisal of the Bacillus subtilis exoproteome
    • Tjalsma, H., Feature-based reappraisal of the Bacillus subtilis exoproteome. Proteomics 2007, 7, 73-81.
    • (2007) Proteomics , vol.7 , pp. 73-81
    • Tjalsma, H.1
  • 17
    • 29144534564 scopus 로고    scopus 로고
    • A genome-wide visual screen reveals a role for sphingolipids and ergosterol in cell surface delivery in yeast
    • Proszynski, T. J., Klemm, R. W., Graven, M., Hsu, P. P. et al., A genome-wide visual screen reveals a role for sphingolipids and ergosterol in cell surface delivery in yeast. Proc. Natl. Acad. Sci. USA 2005, 102, 17981-17986.
    • (2005) Proc. Natl. Acad. Sci. USA , vol.102 , pp. 17981-17986
    • Proszynski, T.J.1    Klemm, R.W.2    Graven, M.3    Hsu, P.P.4
  • 18
    • 0033996303 scopus 로고    scopus 로고
    • Functional, c-myc-tagged Cf-9 resistance gene products are plasma-membrane localized and glycosylated
    • Piedras, P., Rivas, S., Droge, S., Hillmer, S., Jones, J. D., Functional, c-myc-tagged Cf-9 resistance gene products are plasma-membrane localized and glycosylated. Plant J. 2000, 21, 529-536.
    • (2000) Plant J , vol.21 , pp. 529-536
    • Piedras, P.1    Rivas, S.2    Droge, S.3    Hillmer, S.4    Jones, J.D.5
  • 19
    • 0036438898 scopus 로고    scopus 로고
    • The import of ferredoxin-NADP+ reductase precursor into chloroplasts is modulated by the region between the transit peptide and the mature core of the protein
    • Rial, D. V., Lombardo, V. A., Ceccarelli, E. A., Ottado, J., The import of ferredoxin-NADP+ reductase precursor into chloroplasts is modulated by the region between the transit peptide and the mature core of the protein. Eur. J. Biochem. 2002, 269, 5431-5439.
    • (2002) Eur. J. Biochem , vol.269 , pp. 5431-5439
    • Rial, D.V.1    Lombardo, V.A.2    Ceccarelli, E.A.3    Ottado, J.4
  • 20
    • 0034927421 scopus 로고    scopus 로고
    • The N-terminal portion of mature aldehyde dehydrogenase affects protein folding and assembly
    • Zhou, J., Weiner, H., The N-terminal portion of mature aldehyde dehydrogenase affects protein folding and assembly. Protein Sci. 2001, 10, 1490-1497.
    • (2001) Protein Sci , vol.10 , pp. 1490-1497
    • Zhou, J.1    Weiner, H.2
  • 21
    • 0344875538 scopus 로고    scopus 로고
    • Molecular definition of the ascorbate-glutathione cycle in Arabidopsis mitochondria reveals dual targeting of antioxidant defenses in plants
    • Chew, O., Whelan, J., Millar, A. H., Molecular definition of the ascorbate-glutathione cycle in Arabidopsis mitochondria reveals dual targeting of antioxidant defenses in plants. J. Biol. Chem. 2003, 278, 46869-46877.
    • (2003) J. Biol. Chem , vol.278 , pp. 46869-46877
    • Chew, O.1    Whelan, J.2    Millar, A.H.3
  • 22
    • 0035984147 scopus 로고    scopus 로고
    • Intrinsic direct repeats generate consistent post-transcriptional gene silencing in tobacco
    • Ma, C., Mitra, A., Intrinsic direct repeats generate consistent post-transcriptional gene silencing in tobacco. Plant J. 2002, 31, 37-49.
    • (2002) Plant J , vol.31 , pp. 37-49
    • Ma, C.1    Mitra, A.2
  • 23
    • 1842430185 scopus 로고    scopus 로고
    • Improved tandem affinity purification tag and methods for isolation of protein heterocomplexes from plants
    • Rohila, J. S., Chen, M., Cerny, R., Fromm, M. E., Improved tandem affinity purification tag and methods for isolation of protein heterocomplexes from plants. Plant J. 2004, 38, 172-181.
    • (2004) Plant J , vol.38 , pp. 172-181
    • Rohila, J.S.1    Chen, M.2    Cerny, R.3    Fromm, M.E.4
  • 24
    • 0030596214 scopus 로고    scopus 로고
    • Differential glycosylation of epitope-tagged glycoprotein Gp72 during the Trypanosoma cruzi life cycle
    • Haynes, P. A., Cross, G. A., Differential glycosylation of epitope-tagged glycoprotein Gp72 during the Trypanosoma cruzi life cycle. Mol. Biochem. Parasitol. 1996, 83, 253-256.
    • (1996) Mol. Biochem. Parasitol , vol.83 , pp. 253-256
    • Haynes, P.A.1    Cross, G.A.2
  • 25
    • 0037040944 scopus 로고    scopus 로고
    • Proteome map of the chloroplast lumen of Arabidopsis thaliana
    • Schubert, M., Petersson, U. A., Haas, B. J., Funk, C. et al., Proteome map of the chloroplast lumen of Arabidopsis thaliana. J. Biol. Chem. 2002, 277, 8354-8365.
    • (2002) J. Biol. Chem , vol.277 , pp. 8354-8365
    • Schubert, M.1    Petersson, U.A.2    Haas, B.J.3    Funk, C.4
  • 26
    • 0034026047 scopus 로고    scopus 로고
    • Proteomics of the chloroplast: Systematic identification and targeting analysis of lumenal and peripheral thylakoid proteins
    • Peltier, J. B., Friso, G., Kalume, D. E., Roepstorff, P. et al., Proteomics of the chloroplast: Systematic identification and targeting analysis of lumenal and peripheral thylakoid proteins. Plant Cell. 2000, 12, 319-341.
    • (2000) Plant Cell , vol.12 , pp. 319-341
    • Peltier, J.B.1    Friso, G.2    Kalume, D.E.3    Roepstorff, P.4
  • 28
    • 0035231382 scopus 로고    scopus 로고
    • Isolation and subfractionation of mitochondria from plants
    • Millar, A. H., Liddell, A., Leaver, C. J., Isolation and subfractionation of mitochondria from plants. Methods Cell Biol. 2001, 65, 53-74.
    • (2001) Methods Cell Biol , vol.65 , pp. 53-74
    • Millar, A.H.1    Liddell, A.2    Leaver, C.J.3
  • 29
    • 0344668825 scopus 로고    scopus 로고
    • Analysis of the Arabidopsis nuclear proteome and its response to cold stress
    • Bae, M. S., Cho, E. J., Choi, E. Y., Park, O. K., Analysis of the Arabidopsis nuclear proteome and its response to cold stress. Plant J. 2003, 36, 652-663.
    • (2003) Plant J , vol.36 , pp. 652-663
    • Bae, M.S.1    Cho, E.J.2    Choi, E.Y.3    Park, O.K.4
  • 30
    • 0141529726 scopus 로고    scopus 로고
    • A proteomic study of the arabidopsis nuclear matrix
    • Calikowski, T. T., Meulia, T., Meier, I., A proteomic study of the arabidopsis nuclear matrix. J. Cell Biochem. 2003, 90, 361-378.
    • (2003) J. Cell Biochem , vol.90 , pp. 361-378
    • Calikowski, T.T.1    Meulia, T.2    Meier, I.3
  • 31
    • 3242752095 scopus 로고    scopus 로고
    • Rice proteomics: Recent developments and analysis of nuclear proteins
    • Khan, M. M., Komatsu, S., Rice proteomics: Recent developments and analysis of nuclear proteins. Phytochemistry 2004, 65, 1671-1681.
    • (2004) Phytochemistry , vol.65 , pp. 1671-1681
    • Khan, M.M.1    Komatsu, S.2
  • 32
    • 0036346730 scopus 로고    scopus 로고
    • Proteomic analysis of leaf peroxisomal proteins in greening cotyledons of Arabidopsis thaliana
    • Fukao, Y., Hayashi, M., Nishimura, M., Proteomic analysis of leaf peroxisomal proteins in greening cotyledons of Arabidopsis thaliana. Plant Cell Physiol. 2002, 43, 689-696.
    • (2002) Plant Cell Physiol , vol.43 , pp. 689-696
    • Fukao, Y.1    Hayashi, M.2    Nishimura, M.3
  • 33
    • 0036303255 scopus 로고    scopus 로고
    • Proteomic analysis of the Arabidopsis thaliana cell wall
    • Chivasa, S., Ndimba, B. K., Simon, W. J., Robertson, D. et al., Proteomic analysis of the Arabidopsis thaliana cell wall. Electrophoresis 2002, 23, 1754-1765.
    • (2002) Electrophoresis , vol.23 , pp. 1754-1765
    • Chivasa, S.1    Ndimba, B.K.2    Simon, W.J.3    Robertson, D.4
  • 35
    • 3142671423 scopus 로고    scopus 로고
    • Proteomics of the rice cell: Systematic identification of the protein populations in subcellular compartments
    • Tanaka, N., Fujita, M., Handa, H., Murayama, S. et al., Proteomics of the rice cell: Systematic identification of the protein populations in subcellular compartments. Mol. Genet. Genomics 2004, 271, 566-576.
    • (2004) Mol. Genet. Genomics , vol.271 , pp. 566-576
    • Tanaka, N.1    Fujita, M.2    Handa, H.3    Murayama, S.4
  • 36
    • 0034662907 scopus 로고    scopus 로고
    • Evaluation of two-dimensional gel electrophoresis-based proteome analysis technology
    • Gygi, S. P., Corthals, G. L., Zhang, Y., Rochon, Y., Aebersold, R., Evaluation of two-dimensional gel electrophoresis-based proteome analysis technology. Proc. Natl. Acad. Sci. USA 2000, 97, 9390-9395.
    • (2000) Proc. Natl. Acad. Sci. USA , vol.97 , pp. 9390-9395
    • Gygi, S.P.1    Corthals, G.L.2    Zhang, Y.3    Rochon, Y.4    Aebersold, R.5
  • 37
    • 0035346708 scopus 로고    scopus 로고
    • Analysis of the outer membrane proteome of Caulobacter crescentus by two-dimensional electrophoresis and mass spectrometry
    • Phadke, N. D., Molloy, M. P., Steinhoff, S. A., Ulintz, P. J. et al., Analysis of the outer membrane proteome of Caulobacter crescentus by two-dimensional electrophoresis and mass spectrometry. Proteomics 2001, 1, 705-720.
    • (2001) Proteomics , vol.1 , pp. 705-720
    • Phadke, N.D.1    Molloy, M.P.2    Steinhoff, S.A.3    Ulintz, P.J.4
  • 38
    • 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
  • 39
    • 0041733229 scopus 로고    scopus 로고
    • Proteomic study of the Arabidopsis thaliana chloroplastic envelope membrane utilizing alternatives to traditional two-dimensional electrophoresis
    • Froehlich, J. E., Wilkerson, C. G., Ray, W. K., McAndrew, R. S. et al., Proteomic study of the Arabidopsis thaliana chloroplastic envelope membrane utilizing alternatives to traditional two-dimensional electrophoresis. J. Proteome Res. 2003, 2, 413-425.
    • (2003) J. Proteome Res , vol.2 , pp. 413-425
    • Froehlich, J.E.1    Wilkerson, C.G.2    Ray, W.K.3    McAndrew, R.S.4
  • 40
    • 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
  • 41
    • 0037015065 scopus 로고    scopus 로고
    • Plant proteomics: BLASTing out of a Mud-PIT
    • Whitelegge, J. P., Plant proteomics: BLASTing out of a Mud-PIT. Proc. Natl. Acad. Sci. USA 2002, 99, 11564-11566.
    • (2002) Proc. Natl. Acad. Sci. USA , vol.99 , pp. 11564-11566
    • Whitelegge, J.P.1
  • 42
    • 0035852247 scopus 로고    scopus 로고
    • Dual targeting to mitochondria and chloroplasts
    • Peeters, N., Small, I., Dual targeting to mitochondria and chloroplasts. Biochim. Biophys. Acta 2001, 1541, 54-63.
    • (2001) Biochim. Biophys. Acta , vol.1541 , pp. 54-63
    • Peeters, N.1    Small, I.2
  • 43
    • 0038734441 scopus 로고    scopus 로고
    • Characterization of an ascorbate peroxidase in plastids of tobacco BY-2 cells
    • Madhusudhan, R., Ishikawa, T., Sawa, Y., Shigeoka, S., Shibata, H., Characterization of an ascorbate peroxidase in plastids of tobacco BY-2 cells. Physiol. Plant 2003, 117, 550-557.
    • (2003) Physiol. Plant , vol.117 , pp. 550-557
    • Madhusudhan, R.1    Ishikawa, T.2    Sawa, Y.3    Shigeoka, S.4    Shibata, H.5
  • 44
    • 0032409543 scopus 로고    scopus 로고
    • Use of a proteome strategy for tagging proteins present at the plasma membrane
    • Santoni, V., Rouquie, D., Doumas, P., Mansion, M. et al., Use of a proteome strategy for tagging proteins present at the plasma membrane. Plant J. 1998, 16, 633-641.
    • (1998) Plant J , vol.16 , pp. 633-641
    • Santoni, V.1    Rouquie, D.2    Doumas, P.3    Mansion, M.4
  • 45
    • 0003026156 scopus 로고
    • Presence of host-plasma membrane type H-ATPase in the membrane envelope enclosing the bacteroids in soybean root nodules
    • Blumwald, E., Fortin, M. G., Rea, P. A., Verma, D. P., Poole, R. J., Presence of host-plasma membrane type H-ATPase in the membrane envelope enclosing the bacteroids in soybean root nodules. Plant Physiol. 1985, 78, 665-672.
    • (1985) Plant Physiol , vol.78 , pp. 665-672
    • Blumwald, E.1    Fortin, M.G.2    Rea, P.A.3    Verma, D.P.4    Poole, R.J.5
  • 46
    • 0023354237 scopus 로고
    • Lipid composition of plasma membranes isolated from light-grown barley (Hordeum vulgare) leaves: Identification of cerebroside as a major component
    • Rochester, C. P., Kjellbom, P., Andersson, B., Larsson, C., Lipid composition of plasma membranes isolated from light-grown barley (Hordeum vulgare) leaves: Identification of cerebroside as a major component. Arch. Biochem. Biophys. 1987, 255, 385-391.
    • (1987) Arch. Biochem. Biophys , vol.255 , pp. 385-391
    • Rochester, C.P.1    Kjellbom, P.2    Andersson, B.3    Larsson, C.4
  • 47
    • 0038687192 scopus 로고    scopus 로고
    • Partial purification and characterization of an ascorbate-reducible b-type cytochrome from the plasma membrane of Arabidopsis thaliana leaves
    • Berczi, A., Caubergs, R. J., Asard, H., Partial purification and characterization of an ascorbate-reducible b-type cytochrome from the plasma membrane of Arabidopsis thaliana leaves. Protoplasma 2003, 221, 47-56.
    • (2003) Protoplasma , vol.221 , pp. 47-56
    • Berczi, A.1    Caubergs, R.J.2    Asard, H.3
  • 48
    • 10744226861 scopus 로고    scopus 로고
    • Improved proteome analysis of Saccharomyces cerevisiae mitochondria by free-flow electrophoresis
    • Zischka, H., Weber, G., Weber, P. J., Posch, A. et al., Improved proteome analysis of Saccharomyces cerevisiae mitochondria by free-flow electrophoresis. Proteomics 2003, 3, 906-916.
    • (2003) Proteomics , vol.3 , pp. 906-916
    • Zischka, H.1    Weber, G.2    Weber, P.J.3    Posch, A.4
  • 49
    • 0031836080 scopus 로고    scopus 로고
    • Free-flow electrophoresis for fractionation of Arabidopsis thaliana membranes
    • Bardy, N., Carrasco, A., Galaud, J. P., Pont-Lezica, R., Canut, H., Free-flow electrophoresis for fractionation of Arabidopsis thaliana membranes. Electrophoresis 1998, 19, 1145-1153.
    • (1998) Electrophoresis , vol.19 , pp. 1145-1153
    • Bardy, N.1    Carrasco, A.2    Galaud, J.P.3    Pont-Lezica, R.4    Canut, H.5
  • 50
    • 0014705657 scopus 로고
    • IEF and gradient gel electrophoresis: A two-dimensional technique
    • Kenrick, K. G., Margolis, J., IEF and gradient gel electrophoresis: A two-dimensional technique. Anal. Biochem. 1970, 33, 204-207.
    • (1970) Anal. Biochem , vol.33 , pp. 204-207
    • Kenrick, K.G.1    Margolis, J.2
  • 51
    • 0020185480 scopus 로고
    • Isoelectric focusing in immobilized pH gradients: Principle, methodology and some applications
    • Bjellqvist, B., Ek, K., Righetti, P. G., Gianazza, E. et al., Isoelectric focusing in immobilized pH gradients: Principle, methodology and some applications. J. Biochem. Biophys. Methods 1982, 6, 317-339.
    • (1982) J. Biochem. Biophys. Methods , vol.6 , pp. 317-339
    • Bjellqvist, B.1    Ek, K.2    Righetti, P.G.3    Gianazza, E.4
  • 52
    • 0034095972 scopus 로고    scopus 로고
    • The current state of two-dimensional electrophoresis with immobilized pH gradients
    • Gorg, A., Obermaier, C., Boguth, G., Harder, A. et al., The current state of two-dimensional electrophoresis with immobilized pH gradients. Electrophoresis 2000, 21, 1037-1053.
    • (2000) Electrophoresis , vol.21 , pp. 1037-1053
    • Gorg, A.1    Obermaier, C.2    Boguth, G.3    Harder, A.4
  • 53
    • 0031962612 scopus 로고    scopus 로고
    • Mass spectrometry and the age of the proteome
    • Yates, J. R., III, Mass spectrometry and the age of the proteome. J. Mass Spectrom. 1998, 33, 1-19.
    • (1998) J. Mass Spectrom , vol.33 , pp. 1-19
    • Yates III, J.R.1
  • 54
    • 0032961627 scopus 로고    scopus 로고
    • Mass spectrometric identification of proteins from silver-stained polyacrylamide gel: A method for the removal of silver ions to enhance sensitivity
    • Gharahdaghi, F., Weinberg, C. R., Meagher, D. A., Imai, B. S., Mische, S. M., Mass spectrometric identification of proteins from silver-stained polyacrylamide gel: A method for the removal of silver ions to enhance sensitivity. Electrophoresis 1999, 20, 601-605.
    • (1999) Electrophoresis , vol.20 , pp. 601-605
    • Gharahdaghi, F.1    Weinberg, C.R.2    Meagher, D.A.3    Imai, B.S.4    Mische, S.M.5
  • 55
    • 0029927505 scopus 로고    scopus 로고
    • Mass spectrometric sequencing of proteins from silver stained polyacrylamide gels
    • Shevchenko, A., Wilm, M., Vorm, O., Mann, M., Mass spectrometric sequencing of proteins from silver stained polyacrylamide gels. Anal. Chem. 1996, 68, 850-858.
    • (1996) Anal. Chem , vol.68 , pp. 850-858
    • Shevchenko, A.1    Wilm, M.2    Vorm, O.3    Mann, M.4
  • 56
    • 0038488182 scopus 로고    scopus 로고
    • Mass spectrometric analysis of the editosome and other multiprotein complexes in Trypanosoma brucei
    • Panigrahi, A. K., Allen, T. E., Stuart, K., Haynes, P. A., Gygi, S. P., Mass spectrometric analysis of the editosome and other multiprotein complexes in Trypanosoma brucei. J. Am. Soc. Mass. Spectrom. 2003, 14, 728-735.
    • (2003) J. Am. Soc. Mass. Spectrom , vol.14 , pp. 728-735
    • Panigrahi, A.K.1    Allen, T.E.2    Stuart, K.3    Haynes, P.A.4    Gygi, S.P.5
  • 57
    • 0038488181 scopus 로고    scopus 로고
    • Investigative proteomics: Identification of an unknown plant virus from infected plants using mass spectrometry
    • Cooper, B., Eckert, D., Andon, N. L., Yates, J. R., III, Haynes, P. A., Investigative proteomics: Identification of an unknown plant virus from infected plants using mass spectrometry. J. Am. Soc. Mass Spectrom. 2003, 14, 736-741.
    • (2003) J. Am. Soc. Mass Spectrom , vol.14 , pp. 736-741
    • Cooper, B.1    Eckert, D.2    Andon, N.L.3    Yates III, J.R.4    Haynes, P.A.5
  • 58
    • 0024289037 scopus 로고
    • Laser desorption ionization of proteins with molecular masses exceeding 10,000 daltons
    • Karas, M., Hillenkamp, F., Laser desorption ionization of proteins with molecular masses exceeding 10,000 daltons. Anal. Chem. 1988, 60, 2299-2301.
    • (1988) Anal. Chem , vol.60 , pp. 2299-2301
    • Karas, M.1    Hillenkamp, F.2
  • 59
    • 0024438708 scopus 로고
    • Electrospray ionization for mass spectrometry of large biomolecules
    • Fenn, J. B., Mann, M., Meng, C. K., Wong, S. F., Whitehouse, C. M., Electrospray ionization for mass spectrometry of large biomolecules. Science 1989, 246, 64-71.
    • (1989) Science , vol.246 , pp. 64-71
    • Fenn, J.B.1    Mann, M.2    Meng, C.K.3    Wong, S.F.4    Whitehouse, C.M.5
  • 60
    • 0000857494 scopus 로고
    • An approach to correlate tandem mass spectral data of peptides with amino acid sequences in a protein database
    • Eng, J., McCormack, A. L., Yates, J. R., III, An approach to correlate tandem mass spectral data of peptides with amino acid sequences in a protein database. J. Am. Mass Spectrom. 1994, 5, 976-989.
    • (1994) J. Am. Mass Spectrom , vol.5 , pp. 976-989
    • Eng, J.1    McCormack, A.L.2    Yates III, J.R.3
  • 61
    • 0033434080 scopus 로고    scopus 로고
    • Probability-based protein identification by searching sequence databases using mass spectrometry data
    • Perkins, D. N., Pappin, D. J., Creasy, D. M., Cottrell, J. S., Probability-based protein identification by searching sequence databases using mass spectrometry data. Electrophoresis 1999, 20, 3551-3567.
    • (1999) Electrophoresis , vol.20 , pp. 3551-3567
    • Perkins, D.N.1    Pappin, D.J.2    Creasy, D.M.3    Cottrell, J.S.4
  • 62
    • 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, R et al., Quantitative analysis of complex protein mixtures using isotope-coded affinity tags. Nat. Biotechnol. 1999, 17, 994-999.
    • (1999) Nat. Biotechnol , vol.17 , pp. 994-999
    • Gygi, S.P.1    Rist, B.2    Gerber, S.A.3    Turecek, R.4
  • 63
    • 32344434974 scopus 로고    scopus 로고
    • Comparison of two proteomics techniques used to identify proteins regulated by gibberellin in rice
    • Komatsu, S., Zang, X., Tanaka, N., Comparison of two proteomics techniques used to identify proteins regulated by gibberellin in rice. J. Proteome Res. 2006, 5, 270-276.
    • (2006) J. Proteome Res , vol.5 , pp. 270-276
    • Komatsu, S.1    Zang, X.2    Tanaka, N.3
  • 64
    • 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
  • 65
    • 85047683107 scopus 로고    scopus 로고
    • Proteomic approach to identify novel mitochondrial proteins in Arabidopsis
    • Kruft, V., Eubel, H., Jansch, L., Werhahn, W., Braun, H. P., Proteomic approach to identify novel mitochondrial proteins in Arabidopsis. Plant Physiol. 2001, 127, 1694-1710.
    • (2001) Plant Physiol , vol.127 , pp. 1694-1710
    • Kruft, V.1    Eubel, H.2    Jansch, L.3    Werhahn, W.4    Braun, H.P.5
  • 66
    • 0037321898 scopus 로고    scopus 로고
    • Genomic and proteomic analysis of mitochondrial carrier proteins in Arabidopsis
    • Millar, A. H., Heazlewood, J. L., Genomic and proteomic analysis of mitochondrial carrier proteins in Arabidopsis. Plant Physiol. 2003, 131, 443-453.
    • (2003) Plant Physiol , vol.131 , pp. 443-453
    • Millar, A.H.1    Heazlewood, J.L.2
  • 67
    • 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
  • 68
    • 0347755545 scopus 로고    scopus 로고
    • Rice Proteome Database based on two-dimensional polyacrylamide gel electrophoresis: Its status in 2003
    • Komatsu, S., Kojima, K., Suzuki, K., Ozaki, K., Higo, K., Rice Proteome Database based on two-dimensional polyacrylamide gel electrophoresis: Its status in 2003. Nucleic Acids Res. 2004, 32, D388-D392.
    • (2004) Nucleic Acids Res , vol.32
    • Komatsu, S.1    Kojima, K.2    Suzuki, K.3    Ozaki, K.4    Higo, K.5
  • 69
    • 0000608625 scopus 로고
    • Analysis of leaf proteins by two-dimensional gel electrophoresis: Protease action as exemplified by ribulose bisphosphate carboxylase/oxygenase degradation and procedure to avoid proteolysis during extraction
    • des Francs, C. C., Thiellement, H., de Vienne, D., Analysis of leaf proteins by two-dimensional gel electrophoresis: Protease action as exemplified by ribulose bisphosphate carboxylase/oxygenase degradation and procedure to avoid proteolysis during extraction. Plant Physiol. 1985, 78, 178-182.
    • (1985) Plant Physiol , vol.78 , pp. 178-182
    • des Francs, C.C.1    Thiellement, H.2    de Vienne, D.3
  • 70
    • 0034931862 scopus 로고    scopus 로고
    • Two-dimensional electrophoretic analysis of rice proteins by polyethylene glycol fractionation for protein arrays
    • Kim, S. T., Cho, K. S., Jang, Y. S., Kang, K. Y., Two-dimensional electrophoretic analysis of rice proteins by polyethylene glycol fractionation for protein arrays. Electrophoresis 2001, 22, 2103-2109.
    • (2001) Electrophoresis , vol.22 , pp. 2103-2109
    • Kim, S.T.1    Cho, K.S.2    Jang, Y.S.3    Kang, K.Y.4
  • 71
    • 0033838003 scopus 로고    scopus 로고
    • Towards high performance two-dimensional gel electrophoresis using ultrazoom gels
    • Hoving, S., Voshol, H., van Oostrum, J., Towards high performance two-dimensional gel electrophoresis using ultrazoom gels. Electrophoresis 2000, 21, 2617-2621.
    • (2000) Electrophoresis , vol.21 , pp. 2617-2621
    • Hoving, S.1    Voshol, H.2    van Oostrum, J.3
  • 72
    • 0033849339 scopus 로고    scopus 로고
    • Towards higher resolution: Two-dimensional electrophoresis of Saccharomyces cerevisiae proteins using overlapping narrow immobilized pH gradients
    • Wildgruber, R., Harder, A., Obermaier, C., Boguth, G. et al., Towards higher resolution: Two-dimensional electrophoresis of Saccharomyces cerevisiae proteins using overlapping narrow immobilized pH gradients. Electrophoresis 2000, 21, 2610-2616.
    • (2000) Electrophoresis , vol.21 , pp. 2610-2616
    • Wildgruber, R.1    Harder, A.2    Obermaier, C.3    Boguth, G.4
  • 73
    • 0034066471 scopus 로고    scopus 로고
    • Membrane proteins and proteomics: Un amour impossible?
    • Santoni, V., Molloy, M., Rabilloud, T., Membrane proteins and proteomics: Un amour impossible? Electrophoresis 2000, 21, 1054-1070.
    • (2000) Electrophoresis , vol.21 , pp. 1054-1070
    • Santoni, V.1    Molloy, M.2    Rabilloud, T.3
  • 74
    • 0025224152 scopus 로고
    • Biochemistry and function of the plastid envelope
    • Douce, R., Joyard, J., Biochemistry and function of the plastid envelope. Annu. Rev. Cell Biol. 1990, 6, 173-216.
    • (1990) Annu. Rev. Cell Biol , vol.6 , pp. 173-216
    • Douce, R.1    Joyard, J.2
  • 75
    • 0031807041 scopus 로고    scopus 로고
    • Proteins of rat serum: I. Establishing a reference two-dimensional electrophoresis map by immunodetection and microbore high performance liquid chromatography-electrospray mass spectrometry
    • Haynes, P., Miller, I., Aebersold, R., Gemeiner, M. et al., Proteins of rat serum: I. Establishing a reference two-dimensional electrophoresis map by immunodetection and microbore high performance liquid chromatography-electrospray mass spectrometry. Electrophoresis 1998, 19, 1484-1492.
    • (1998) Electrophoresis , vol.19 , pp. 1484-1492
    • Haynes, P.1    Miller, I.2    Aebersold, R.3    Gemeiner, M.4
  • 77
    • 3042771394 scopus 로고    scopus 로고
    • Effect of early cold stress on the maturation of rice anthers
    • Imin, N., Kerim, T., Rolfe, B. G., Weinman, J. J., Effect of early cold stress on the maturation of rice anthers. Proteomics 2004, 4, 1873-1882.
    • (2004) Proteomics , vol.4 , pp. 1873-1882
    • Imin, N.1    Kerim, T.2    Rolfe, B.G.3    Weinman, J.J.4
  • 78
    • 0034714532 scopus 로고    scopus 로고
    • Four years of post-genomic life with 6,000 yeast genes
    • Goffeau, A., Four years of post-genomic life with 6,000 yeast genes. FEBS Lett. 2000, 480, 37-41.
    • (2000) FEBS Lett , vol.480 , pp. 37-41
    • Goffeau, A.1
  • 80
    • 0035130163 scopus 로고    scopus 로고
    • Genomic divergences between humans and other hominoids and the effective population size of the common ancestor of humans and chimpanzees
    • Chen, F. C., Li, W. H., Genomic divergences between humans and other hominoids and the effective population size of the common ancestor of humans and chimpanzees. Am. J. Hum. Genet. 2001, 68, 444-456.
    • (2001) Am. J. Hum. Genet , vol.68 , pp. 444-456
    • Chen, F.C.1    Li, W.H.2
  • 81
    • 34250815069 scopus 로고    scopus 로고
    • Phylogenetic and expression analysis of sucrose phosphate synthase isozymes in plants
    • in press, DOI: 10.1016/j.jplph.2006.04.014
    • Lutfiyya, L. L., Xu, N., DÓrdine, R. L., Morrell, J. A. et al., Phylogenetic and expression analysis of sucrose phosphate synthase isozymes in plants. J. Plant Physiol., in press, DOI: 10.1016/j.jplph.2006.04.014.
    • J. Plant Physiol
    • Lutfiyya, L.L.1    Xu, N.2    DÓrdine, R.L.3    Morrell, J.A.4
  • 82
    • 8444247483 scopus 로고    scopus 로고
    • Evolution of vertebrate genes related to prion and Shadoo proteins-Clues from comparative genomic analysis
    • Premzl, M., Gready, J. E., Jermiin, L. S., Simonic, T., Marshall Graves, J. A., Evolution of vertebrate genes related to prion and Shadoo proteins-Clues from comparative genomic analysis. Mol. Biol. Evol. 2004, 21, 2210-2231.
    • (2004) Mol. Biol. Evol , vol.21 , pp. 2210-2231
    • Premzl, M.1    Gready, J.E.2    Jermiin, L.S.3    Simonic, T.4    Marshall Graves, J.A.5
  • 83
    • 0032033458 scopus 로고    scopus 로고
    • A high-resolution metric HAPPY map of human chromosome 14
    • Dear, P. H., Bankier, A. T., Piper, M. B., A high-resolution metric HAPPY map of human chromosome 14. Genomics 1998, 48, 232-241.
    • (1998) Genomics , vol.48 , pp. 232-241
    • Dear, P.H.1    Bankier, A.T.2    Piper, M.B.3
  • 85
    • 26844545468 scopus 로고    scopus 로고
    • Characterization of the Drosophila melanogaster mitochondrial proteome
    • Alonso, J., Rodriguez, J. M., Baena-Lopez, L. A., Santaren, J. F., Characterization of the Drosophila melanogaster mitochondrial proteome. J. Proteome Res. 2005, 4, 1636-1645.
    • (2005) J. Proteome Res , vol.4 , pp. 1636-1645
    • Alonso, J.1    Rodriguez, J.M.2    Baena-Lopez, L.A.3    Santaren, J.F.4
  • 86
    • 19944429644 scopus 로고    scopus 로고
    • A comprehensive survey of the Plasmodium life cycle by genomic, transcriptomic, and proteomic analyses
    • Hall, N., Karras, M., Raine, J. D., Carlton, J. M. et al., A comprehensive survey of the Plasmodium life cycle by genomic, transcriptomic, and proteomic analyses. Science 2005, 307, 82-86.
    • (2005) Science , vol.307 , pp. 82-86
    • Hall, N.1    Karras, M.2    Raine, J.D.3    Carlton, J.M.4
  • 87
    • 0041358756 scopus 로고    scopus 로고
    • Mass spectrometric proteome analysis for profiling temperature-dependent changes of protein expression in wild-type Caenorhabditis elegans
    • Madi, A., Mikkat, S., Ringel, B., Ulbrich, M. et al., Mass spectrometric proteome analysis for profiling temperature-dependent changes of protein expression in wild-type Caenorhabditis elegans. Proteomics 2003, 3, 1526-1534.
    • (2003) Proteomics , vol.3 , pp. 1526-1534
    • Madi, A.1    Mikkat, S.2    Ringel, B.3    Ulbrich, M.4
  • 91
    • 0035106351 scopus 로고    scopus 로고
    • Large-scale analysis of the yeast proteome by multidimensional protein identification technology
    • Washburn, M. P., Wolters, D., Yates, J. R., III, 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 III, J.R.3
  • 92
    • 0035582244 scopus 로고    scopus 로고
    • An automated multidimensional protein identification technology for shotgun proteomics
    • Wolters, D. A., Washburn, M. P., Yates, J. R., III, An automated multidimensional protein identification technology for shotgun proteomics. Anal. Chem. 2001, 73, 5683-5690.
    • (2001) Anal. Chem , vol.73 , pp. 5683-5690
    • Wolters, D.A.1    Washburn, M.P.2    Yates III, J.R.3
  • 93
    • 33748319353 scopus 로고    scopus 로고
    • Statistical analysis of membrane proteome expression changes in Saccharomyces cerevisiae
    • Zybailov, B., Mosley, A. L., Sardiu, M. E., Coleman, M. K. et al., Statistical analysis of membrane proteome expression changes in Saccharomyces cerevisiae. J. Proteome Res. 2006, 5, 2339-2347.
    • (2006) J. Proteome Res , vol.5 , pp. 2339-2347
    • Zybailov, B.1    Mosley, A.L.2    Sardiu, M.E.3    Coleman, M.K.4
  • 95
    • 0032848549 scopus 로고    scopus 로고
    • Two-dimensional gel protein database of Saccharomyces cerevisiae (update 1999)
    • Perrot, M., Sagliocco, F., Mini, T., Monribot, C. et al., Two-dimensional gel protein database of Saccharomyces cerevisiae (update 1999). Electrophoresis 1999, 20, 2280-2298.
    • (1999) Electrophoresis , vol.20 , pp. 2280-2298
    • Perrot, M.1    Sagliocco, F.2    Mini, T.3    Monribot, C.4
  • 96
    • 33644683776 scopus 로고    scopus 로고
    • Development of an on-line automated sample clean-up method and liquid chromatography-tandem mass spectrometry analysis: Application in an in vitro proteolytic assay
    • Drexler, D., Barlow, D. J., Falk, P., Cantone, J. et al., Development of an on-line automated sample clean-up method and liquid chromatography-tandem mass spectrometry analysis: Application in an in vitro proteolytic assay. Anal. Bioanal. Chem. 2006, 384, 1145-1154.
    • (2006) Anal. Bioanal. Chem , vol.384 , pp. 1145-1154
    • Drexler, D.1    Barlow, D.J.2    Falk, P.3    Cantone, J.4
  • 97
    • 0034669677 scopus 로고    scopus 로고
    • A robust, detergent-friendly method for mass spectrometric analysis of integral membrane proteins
    • Cadene, M., Chait, B. T., A robust, detergent-friendly method for mass spectrometric analysis of integral membrane proteins. Anal. Chem. 2000, 72, 5655-5658.
    • (2000) Anal. Chem , vol.72 , pp. 5655-5658
    • Cadene, M.1    Chait, B.T.2
  • 98
    • 3142702204 scopus 로고    scopus 로고
    • TANDEM: Matching proteins with tandem mass spectra
    • Craig, R., Beavis, R. C., TANDEM: Matching proteins with tandem mass spectra. Bioinformatics 2004, 20, 1466-1467.
    • (2004) Bioinformatics , vol.20 , pp. 1466-1467
    • Craig, R.1    Beavis, R.C.2
  • 99
    • 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
  • 100
    • 0035326344 scopus 로고    scopus 로고
    • Charting the proteomes of organisms with unsequenced genomes by MALDI-quadrupole time-of-flight mass spectrometry and BLAST homology searching
    • Shevchenko, A., Sunyaev, S., Loboda, A., Shevchenko, A. et al., Charting the proteomes of organisms with unsequenced genomes by MALDI-quadrupole time-of-flight mass spectrometry and BLAST homology searching. Anal. Chem. 2001, 73, 1917-1926.
    • (2001) Anal. Chem , vol.73 , pp. 1917-1926
    • Shevchenko, A.1    Sunyaev, S.2    Loboda, A.3    Shevchenko, A.4
  • 101
    • 3042735127 scopus 로고    scopus 로고
    • The need for guidelines in publication of peptide and protein identification data: Working group on publication guidelines for peptide and protein identification data
    • Carr, S., Aebersold, R., Baldwin, M., Burlingame, A. et al., The need for guidelines in publication of peptide and protein identification data: Working group on publication guidelines for peptide and protein identification data. Mol. Cell Proteomics 2004, 3, 531-533.
    • (2004) Mol. Cell Proteomics , vol.3 , pp. 531-533
    • Carr, S.1    Aebersold, R.2    Baldwin, M.3    Burlingame, A.4
  • 102
    • 27644555055 scopus 로고    scopus 로고
    • Interpretation of shotgun proteomic data: The protein inference problem
    • Nesvizhskii, A. I., Aebersold, R., Interpretation of shotgun proteomic data: The protein inference problem. Mol. Cell Proteomics 2005, 4, 1419-1440.
    • (2005) Mol. Cell Proteomics , vol.4 , pp. 1419-1440
    • Nesvizhskii, A.I.1    Aebersold, R.2
  • 103
    • 0036393898 scopus 로고    scopus 로고
    • DTASelect and Contrast: Tools for assembling and comparing protein identifications from shotgun proteomics
    • Tabb, D. L., McDonald, W. H., Yates, J. R., III, DTASelect and Contrast: Tools for assembling and comparing protein identifications from shotgun proteomics. J. Proteome Res. 2002, 1, 21-26.
    • (2002) J. Proteome Res , vol.1 , pp. 21-26
    • Tabb, D.L.1    McDonald, W.H.2    Yates III, J.R.3
  • 104
    • 7044241344 scopus 로고    scopus 로고
    • DBParser: Web-based software for shotgun proteomic data analyses
    • Yang, X., Dondeti, V., Dezube, R., Maynard, D. M. et al., DBParser: Web-based software for shotgun proteomic data analyses. J. Proteome Res. 2004, 3, 1002-1008.
    • (2004) J. Proteome Res , vol.3 , pp. 1002-1008
    • Yang, X.1    Dondeti, V.2    Dezube, R.3    Maynard, D.M.4
  • 105
    • 0042338362 scopus 로고    scopus 로고
    • A statistical model for identifying proteins by tandem mass spectrometry
    • Nesvizhskii, A. I., Keller, A., Kolker, E., Aebersold, R., A statistical model for identifying proteins by tandem mass spectrometry. Anal. Chem. 2003, 15, 4646-4658.
    • (2003) Anal. Chem , vol.15 , pp. 4646-4658
    • Nesvizhskii, A.I.1    Keller, A.2    Kolker, E.3    Aebersold, R.4
  • 106
    • 0033051101 scopus 로고    scopus 로고
    • Direct analysis of protein complexes using mass spectrometry
    • Link, A. J., Eng, J., Schieltz, D. M., Carmack, E. et al., Direct analysis of protein complexes using mass spectrometry. Nat. Biotechnol. 1999, 17, 676-682.
    • (1999) Nat. Biotechnol , vol.17 , pp. 676-682
    • Link, A.J.1    Eng, J.2    Schieltz, D.M.3    Carmack, E.4
  • 107
    • 0032190378 scopus 로고    scopus 로고
    • Protein identification at the low femtomole level from silver-stained gels using a new fritless electrospray interface for liquid chromatography-microspray and nanospray mass spectrometry
    • Gatlin, C. L., Kleemann, G. R., Hays, L. G., Link, A. J., Yates, J. R., III, Protein identification at the low femtomole level from silver-stained gels using a new fritless electrospray interface for liquid chromatography-microspray and nanospray mass spectrometry. Anal. Biochem. 1998, 263, 93-101.
    • (1998) Anal. Biochem , vol.263 , pp. 93-101
    • Gatlin, C.L.1    Kleemann, G.R.2    Hays, L.G.3    Link, A.J.4    Yates III, J.R.5
  • 108
    • 31344434715 scopus 로고    scopus 로고
    • Host cell factor and an uncharacterized SANT domain protein are stable components of ATAC, a novel dAda2A/dGcn5-containing histone acetyltransferase complex in Drosophila
    • Guelman, S., Suganuma, T., Florens, L., Swanson, S. K. et al., Host cell factor and an uncharacterized SANT domain protein are stable components of ATAC, a novel dAda2A/dGcn5-containing histone acetyltransferase complex in Drosophila. Mol. Cell Biol. 2006, 26, 871-882.
    • (2006) Mol. Cell Biol , vol.26 , pp. 871-882
    • Guelman, S.1    Suganuma, T.2    Florens, L.3    Swanson, S.K.4
  • 109
    • 28144460300 scopus 로고    scopus 로고
    • A mammalian chromatin remodeling complex with similarities to the yeast INO80 complex
    • Jin, J., Cai, Y., Yao, T., Gottschalk, A. J. et al., A mammalian chromatin remodeling complex with similarities to the yeast INO80 complex. J. Biol. Chem. 2005, 280, 41207-41212.
    • (2005) J. Biol. Chem , vol.280 , pp. 41207-41212
    • Jin, J.1    Cai, Y.2    Yao, T.3    Gottschalk, A.J.4
  • 110
    • 0038561131 scopus 로고    scopus 로고
    • A method for the comprehensive proteomic analysis of membrane proteins
    • Wu, C. C., MacCoss, M. J., Howell, K. E., Yates, J. R., III, A method for the comprehensive proteomic analysis of membrane proteins. Nat. Biotechnol. 2003, 21, 532-538.
    • (2003) Nat. Biotechnol , vol.21 , pp. 532-538
    • Wu, C.C.1    MacCoss, M.J.2    Howell, K.E.3    Yates III, J.R.4
  • 111
    • 2542485409 scopus 로고    scopus 로고
    • Organellar proteomics reveals golgi arginine dimethylation
    • Wu, C. C., MacCoss, M. J., Mardones, G., Finnigan, C. et al., Organellar proteomics reveals golgi arginine dimethylation. Mol. Biol. Cell 2004, 15, 2907-2919.
    • (2004) Mol. Biol. Cell , vol.15 , pp. 2907-2919
    • Wu, C.C.1    MacCoss, M.J.2    Mardones, G.3    Finnigan, C.4
  • 112
    • 33745711870 scopus 로고    scopus 로고
    • Identification of new Golgi complex specific proteins by direct organelle proteomic analysis
    • Takatalo, M. S., Kouvonen, P., Corthals, G., Nyman, T. A., Ronnholm, R. H., Identification of new Golgi complex specific proteins by direct organelle proteomic analysis. Proteomics 2006, 6, 3502-3508.
    • (2006) Proteomics , vol.6 , pp. 3502-3508
    • Takatalo, M.S.1    Kouvonen, P.2    Corthals, G.3    Nyman, T.A.4    Ronnholm, R.H.5
  • 113
    • 1842585612 scopus 로고    scopus 로고
    • Linking protein fractionation with multidimensional monolithic reversed-phase peptide chromatography/mass spectrometry enhances protein identification from complex mixtures even in the presence of abundant proteins
    • Wienkoop, S., Glinski, M., Tanaka, N., Tolstikov, V. et al., Linking protein fractionation with multidimensional monolithic reversed-phase peptide chromatography/mass spectrometry enhances protein identification from complex mixtures even in the presence of abundant proteins. Rapid. Commun. Mass Spectrom. 2004, 18, 643-650.
    • (2004) Rapid. Commun. Mass Spectrom , vol.18 , pp. 643-650
    • Wienkoop, S.1    Glinski, M.2    Tanaka, N.3    Tolstikov, V.4
  • 115
    • 0141817918 scopus 로고    scopus 로고
    • Proteomic characterization of the Chlamydomonas reinhardtii chloroplast ribosome. Identification of proteins unique to th e70 S ribosome
    • Yamaguchi, K., Beligni, M. V., Prieto, S., Haynes, P. A. et al., Proteomic characterization of the Chlamydomonas reinhardtii chloroplast ribosome. Identification of proteins unique to th e70 S ribosome. J. Biol. Chem. 2003, 278, 33774-33785.
    • (2003) J. Biol. Chem , vol.278 , pp. 33774-33785
    • Yamaguchi, K.1    Beligni, M.V.2    Prieto, S.3    Haynes, P.A.4
  • 116
    • 26444506068 scopus 로고    scopus 로고
    • Correlation of relative abundance ratios derived from peptide ion chromatograms and spectrum counting for quantitative proteomic analysis using stable isotope labeling
    • Zybailov, B., Coleman, M. K., Florens, L., Washburn, M. P., Correlation of relative abundance ratios derived from peptide ion chromatograms and spectrum counting for quantitative proteomic analysis using stable isotope labeling. Anal. Chem. 2005, 77, 6218-6224.
    • (2005) Anal. Chem , vol.77 , pp. 6218-6224
    • Zybailov, B.1    Coleman, M.K.2    Florens, L.3    Washburn, M.P.4
  • 117
    • 0041706161 scopus 로고    scopus 로고
    • Metabolic labeling of C. elegans and D. melanogaster for quantitative proteomics
    • Krijgsveld, J., Ketting, R. F., Mahmoudi, T., Johansen, J. et al., Metabolic labeling of C. elegans and D. melanogaster for quantitative proteomics. Nat. Biotechnol. 2003, 21, 927-931.
    • (2003) Nat. Biotechnol , vol.21 , pp. 927-931
    • Krijgsveld, J.1    Ketting, R.F.2    Mahmoudi, T.3    Johansen, J.4
  • 118
    • 25844518423 scopus 로고    scopus 로고
    • A proteomic method for the analysis of changes in protein concentrations in response to systemic perturbations using metabolic incorporation of stable isotopes and mass spectrometry
    • Gustavsson, N., Greber, B., Kreitler, T., Himmelbauer, H. et al., A proteomic method for the analysis of changes in protein concentrations in response to systemic perturbations using metabolic incorporation of stable isotopes and mass spectrometry. Proteomics 2005, 5, 3563-3570.
    • (2005) Proteomics , vol.5 , pp. 3563-3570
    • Gustavsson, N.1    Greber, B.2    Kreitler, T.3    Himmelbauer, H.4
  • 119
    • 4444346217 scopus 로고    scopus 로고
    • Metabolic labeling of mammalian organisms with stable isotopes for quantitative proteomic analysis
    • Wu, C. C., MacCoss, M. J., Howell, K. E., Matthews, D. E., Yates, J. R., III, Metabolic labeling of mammalian organisms with stable isotopes for quantitative proteomic analysis. Anal. Chem. 2004, 76, 4951-4959.
    • (2004) Anal. Chem , vol.76 , pp. 4951-4959
    • Wu, C.C.1    MacCoss, M.J.2    Howell, K.E.3    Matthews, D.E.4    Yates III, J.R.5
  • 120
    • 33745591083 scopus 로고    scopus 로고
    • Status of complete proteome analysis by mass spectrometry: SILAC labeled yeast as a model system
    • de Godoy, L. M., Olsen, J. V., de Souza, G. A., Li, G. et al., Status of complete proteome analysis by mass spectrometry: SILAC labeled yeast as a model system. Genome Biol. 2006, 7, R50.
    • (2006) Genome Biol , vol.7
    • de Godoy, L.M.1    Olsen, J.V.2    de Souza, G.A.3    Li, G.4
  • 121
    • 3242747629 scopus 로고    scopus 로고
    • Subtle modification of isotope ratio proteomics; an integrated strategy for expression proteomics
    • Whitelegge, J. P., Katz, J. E., Pihakari, K. A., Hale, R. et al., Subtle modification of isotope ratio proteomics; an integrated strategy for expression proteomics. Phytochemistry 2004, 65, 1507-1515.
    • (2004) Phytochemistry , vol.65 , pp. 1507-1515
    • Whitelegge, J.P.1    Katz, J.E.2    Pihakari, K.A.3    Hale, R.4
  • 122
    • 33745993022 scopus 로고    scopus 로고
    • Quantitative proteomic profiling of pancreatic cancer juice
    • Chen, R., Pan, S., Yi, E. C., Donohoe, S. et al., Quantitative proteomic profiling of pancreatic cancer juice. Proteomics 2006, 6, 3871-3879.
    • (2006) Proteomics , vol.6 , pp. 3871-3879
    • Chen, R.1    Pan, S.2    Yi, E.C.3    Donohoe, S.4
  • 123
    • 26844576371 scopus 로고    scopus 로고
    • Time-resolved mass spectrometry of tyrosine phosphorylation sites in the epidermal growth factor receptor signaling network reveals dynamic modules
    • Zhang, Y., Wolf-Yadlin, A., Ross, P. L., Pappin, D. J. et al., Time-resolved mass spectrometry of tyrosine phosphorylation sites in the epidermal growth factor receptor signaling network reveals dynamic modules. Mol. Cell Proteomics 2005, 4, 1240-1250.
    • (2005) Mol. Cell Proteomics , vol.4 , pp. 1240-1250
    • Zhang, Y.1    Wolf-Yadlin, A.2    Ross, P.L.3    Pappin, D.J.4
  • 124
    • 33747791792 scopus 로고    scopus 로고
    • Optimized proteomic analysis of a mouse model of cerebellar dysfunction using amine-specific isobaric tags
    • Hu, J., Qian, J., Borisov, O., Pan, S. et al., Optimized proteomic analysis of a mouse model of cerebellar dysfunction using amine-specific isobaric tags. Proteomics 2006, 6, 4321-4334.
    • (2006) Proteomics , vol.6 , pp. 4321-4334
    • Hu, J.1    Qian, J.2    Borisov, O.3    Pan, S.4
  • 125
    • 33646590920 scopus 로고    scopus 로고
    • Differential protein expression profiling by iTRAQ-2DLC-MS/MS of lung cancer cells undergoing epithelial-mesenchymal transition reveals a migratory/invasive phenotype
    • Keshamouni, V. G., Michailidis, G., Grasso, C. S., Anthwal, S. et al., Differential protein expression profiling by iTRAQ-2DLC-MS/MS of lung cancer cells undergoing epithelial-mesenchymal transition reveals a migratory/invasive phenotype. J. Proteome Res. 2006, 5, 1143-1154.
    • (2006) J. Proteome Res , vol.5 , pp. 1143-1154
    • Keshamouni, V.G.1    Michailidis, G.2    Grasso, C.S.3    Anthwal, S.4
  • 126
    • 33748364356 scopus 로고    scopus 로고
    • High-coverage quantitative proteomics using amine-specific isotopic labeling
    • Melanson, J. E., Avery, S. L., Pinto, D. M., High-coverage quantitative proteomics using amine-specific isotopic labeling. Proteomics 2006, 6, 4466-4474.
    • (2006) Proteomics , vol.6 , pp. 4466-4474
    • Melanson, J.E.1    Avery, S.L.2    Pinto, D.M.3
  • 127
    • 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
  • 128
    • 27644543078 scopus 로고    scopus 로고
    • Comparison of label-free methods for quantifying human proteins by shotgun proteomics
    • Old, W., Meyer-Arendt, K., Aveline-Wolf, L., Pierce, K. 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.1    Meyer-Arendt, K.2    Aveline-Wolf, L.3    Pierce, K.4
  • 129
    • 33947586766 scopus 로고    scopus 로고
    • BDNF induces widespread changes in synaptic protein content and upregulates components of the translation machinery: An analysis using high-throughput proteomics
    • Liao, L., Pilotte, J., Xu, T., Wong, C. C., et al., BDNF induces widespread changes in synaptic protein content and upregulates components of the translation machinery: An analysis using high-throughput proteomics. J. Proteome Res. 2007, 6, 1059-1071.
    • (2007) J. Proteome Res , vol.6 , pp. 1059-1071
    • Liao, L.1    Pilotte, J.2    Xu, T.3    Wong, C.C.4
  • 130
    • 34248148090 scopus 로고    scopus 로고
    • Proteomic analysis of maternal serum in down syndrome: Identification of novel protein biomarkers
    • Nagalla, S. R., Canick, J. A., Jacob, T., Schneider, K. A. et al., Proteomic analysis of maternal serum in down syndrome: Identification of novel protein biomarkers. J. Proteome Res. 2007, 6, 1245-1257.
    • (2007) J. Proteome Res , vol.6 , pp. 1245-1257
    • Nagalla, S.R.1    Canick, J.A.2    Jacob, T.3    Schneider, K.A.4
  • 131
    • 34248196045 scopus 로고    scopus 로고
    • Identification of novel protein biomarkers of preterm birth in human cervical-vaginal fluid
    • Pereira, L., Reddy, A. P., Jacob, T., Thomas, A. et al., Identification of novel protein biomarkers of preterm birth in human cervical-vaginal fluid. J. Proteome Res. 2007, 6, 1269-1276.
    • (2007) J. Proteome Res , vol.6 , pp. 1269-1276
    • Pereira, L.1    Reddy, A.P.2    Jacob, T.3    Thomas, A.4
  • 132
    • 23044439399 scopus 로고    scopus 로고
    • Multidimensional protein identification technology (Mud-PIT): Technical overview of a profiling method optimized for the comprehensive proteomic investigation of normal and diseased heart tissue
    • Kislinger, T., Gramolini, A. O., MacLennan, D. H., Emili, A., Multidimensional protein identification technology (Mud-PIT): Technical overview of a profiling method optimized for the comprehensive proteomic investigation of normal and diseased heart tissue. J. Am. Soc. Mass Spectrom. 2005, 16, 1207-1220.
    • (2005) J. Am. Soc. Mass Spectrom , vol.16 , pp. 1207-1220
    • Kislinger, T.1    Gramolini, A.O.2    MacLennan, D.H.3    Emili, A.4
  • 133
    • 3543023287 scopus 로고    scopus 로고
    • Direct proteomic mapping of the lung microvascular endothelial cell surface in vivo and in cell culture
    • Durr, E., Yu, J., Krasinska, K. M., Carver, L. A. et al., Direct proteomic mapping of the lung microvascular endothelial cell surface in vivo and in cell culture. Nat. Biotechnol. 2004, 22, 985-992.
    • (2004) Nat. Biotechnol , vol.22 , pp. 985-992
    • Durr, E.1    Yu, J.2    Krasinska, K.M.3    Carver, L.A.4
  • 134
    • 3242731195 scopus 로고    scopus 로고
    • Liu, H., Sadygov, R. G., Yates, J. R., III, A model for random sampling and estimation of relative protein abundance in shotgun proteomics. Anal. Chem. 2004, 76, 41934201.
    • Liu, H., Sadygov, R. G., Yates, J. R., III, A model for random sampling and estimation of relative protein abundance in shotgun proteomics. Anal. Chem. 2004, 76, 41934201.
  • 135
    • 0036746523 scopus 로고    scopus 로고
    • Proteomic characterization of wheat amyloplasts using identification of proteins by tandem mass spectrometry
    • Andon, N. L., Hollingworth, S., Koller, A., Greenland, A. J. et al., Proteomic characterization of wheat amyloplasts using identification of proteins by tandem mass spectrometry. Proteomics 2002, 2, 1156-1168.
    • (2002) Proteomics , vol.2 , pp. 1156-1168
    • Andon, N.L.1    Hollingworth, S.2    Koller, A.3    Greenland, A.J.4
  • 136
    • 20044372385 scopus 로고    scopus 로고
    • Comprehensive proteomics in yeast using chromatographic fractionation, gas phase fractionation, protein gel electrophoresis, and isoelectric focusing
    • Breci, L., Hattrup, E., Keeler, M., Letarte, J. et al., Comprehensive proteomics in yeast using chromatographic fractionation, gas phase fractionation, protein gel electrophoresis, and isoelectric focusing. Proteomics 2005, 5, 2018-2028.
    • (2005) Proteomics , vol.5 , pp. 2018-2028
    • Breci, L.1    Hattrup, E.2    Keeler, M.3    Letarte, J.4
  • 137
    • 0037143630 scopus 로고    scopus 로고
    • Integral membrane proteins of the chloroplast envelope: Identification and subcellular localization of new transporters
    • Ferro, M., Salvi, D., Riviere-Rolland, H., Vermat, T. et al., Integral membrane proteins of the chloroplast envelope: Identification and subcellular localization of new transporters. Proc. Natl. Acad. Sci. USA 2002, 99, 11487-11492.
    • (2002) Proc. Natl. Acad. Sci. USA , vol.99 , pp. 11487-11492
    • Ferro, M.1    Salvi, D.2    Riviere-Rolland, H.3    Vermat, T.4
  • 138
    • 0036120467 scopus 로고    scopus 로고
    • Proteomic analysis of the ER from developing and germinating seed of castor (Ricinus communis)
    • Maltman, D. J., Simon, W. J., Wheeler, C. H., Dunn, M. J. et al., Proteomic analysis of the ER from developing and germinating seed of castor (Ricinus communis). Electrophoresis 2002, 23, 626-639.
    • (2002) Electrophoresis , vol.23 , pp. 626-639
    • Maltman, D.J.1    Simon, W.J.2    Wheeler, C.H.3    Dunn, M.J.4
  • 139
    • 4143128922 scopus 로고    scopus 로고
    • Identification of new intrinsic proteins in Arabidopsis plasma membrane proteome
    • Marmagne, A., Rouet, M. A., Ferro, M., Rolland, N. et al., Identification of new intrinsic proteins in Arabidopsis plasma membrane proteome. Mol. Cell Proteomics 2004, 3, 675-691.
    • (2004) Mol. Cell Proteomics , vol.3 , pp. 675-691
    • Marmagne, A.1    Rouet, M.A.2    Ferro, M.3    Rolland, N.4
  • 140
    • 33751089055 scopus 로고    scopus 로고
    • Alternative workflows for plant proteomic analysis
    • Lee, J., Cooper, B., Alternative workflows for plant proteomic analysis. Mol. Biosyst. 2006, 2, 621-626.
    • (2006) Mol. Biosyst , vol.2 , pp. 621-626
    • Lee, J.1    Cooper, B.2
  • 141
    • 1242329500 scopus 로고    scopus 로고
    • Gel based isoelectric focusing of peptides and the utility of isoelectric point in protein identification
    • Cargile, B. J., Bundy, J. L., Freeman, T. W., Stephenson, J. L., Gel based isoelectric focusing of peptides and the utility of isoelectric point in protein identification. J. Proteome Res. 2004, 3, 112-119.
    • (2004) J. Proteome Res , vol.3 , pp. 112-119
    • Cargile, B.J.1    Bundy, J.L.2    Freeman, T.W.3    Stephenson, J.L.4
  • 142
    • 33745857712 scopus 로고    scopus 로고
    • In-gel isoelectric focusing of peptides as a tool for improved protein identification
    • Krijgsveld, J., Gauci, S., Dormeyer, W., Heck, A. J., In-gel isoelectric focusing of peptides as a tool for improved protein identification. J. Proteome Res. 2006, 5, 1721-1730.
    • (2006) J. Proteome Res , vol.5 , pp. 1721-1730
    • Krijgsveld, J.1    Gauci, S.2    Dormeyer, W.3    Heck, A.J.4
  • 143
    • 1642485152 scopus 로고    scopus 로고
    • Immobilized pH gradients as a first dimension in shotgun proteomics and analysis of the accuracy of p/ predictability of peptides
    • Cargile, B. J., Talley, D. L., Stephenson, J. L., Immobilized pH gradients as a first dimension in shotgun proteomics and analysis of the accuracy of p/ predictability of peptides. Electrophoresis 2004, 25, 936-945.
    • (2004) Electrophoresis , vol.25 , pp. 936-945
    • Cargile, B.J.1    Talley, D.L.2    Stephenson, J.L.3
  • 144
    • 33745264884 scopus 로고    scopus 로고
    • Dynamic range of mass accuracy in LTQ Orbitrap hybrid mass spectrometer
    • Makarov, A., Denisov, E., Lange, O., Horning, S., Dynamic range of mass accuracy in LTQ Orbitrap hybrid mass spectrometer. J. Am. Soc. Mass Spectrom. 2006, 17, 977-982.
    • (2006) J. Am. Soc. Mass Spectrom , vol.17 , pp. 977-982
    • Makarov, A.1    Denisov, E.2    Lange, O.3    Horning, S.4
  • 145
    • 3042789073 scopus 로고    scopus 로고
    • Peptide and protein sequence analysis by electron transfer dissociation mass spectrometry
    • Syka, J. E., Coon, J. J., Schroeder, M. J., Shabanowitz, J., Hunt, D. F., Peptide and protein sequence analysis by electron transfer dissociation mass spectrometry. Proc. Natl. Acad. Sci. USA 2004, 101, 9528-9533.
    • (2004) Proc. Natl. Acad. Sci. USA , vol.101 , pp. 9528-9533
    • Syka, J.E.1    Coon, J.J.2    Schroeder, M.J.3    Shabanowitz, J.4    Hunt, D.F.5


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.