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Volumn 65, Issue 11, 2004, Pages 1517-1530

Untangling multi-gene families in plants by integrating proteomics into functional genomics

Author keywords

Arabidopsis; Gene families; Organelles; Proteomics

Indexed keywords

CYTOCHROME P450; F BOX PROTEIN; LEUCINE; PROTEIN KINASE; PROTEIN SERINE THREONINE KINASE; VEGETABLE PROTEIN; ZINC FINGER PROTEIN;

EID: 3242763941     PISSN: 00319422     EISSN: None     Source Type: Journal    
DOI: 10.1016/j.phytochem.2004.04.021     Document Type: Review
Times cited : (31)

References (93)
  • 1
    • 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. 3rd, Haynes P.A. High-throughput functional affinity purification of mannose binding proteins from Oryza sativa. Proteomics. 3:2003;1270-1278
    • (2003) Proteomics , vol.3 , pp. 1270-1278
    • Andon, N.L.1    Eckert, D.2    Yates III, J.R.3    Haynes, P.A.4
  • 2
    • 0034518604 scopus 로고    scopus 로고
    • Gene discovery using computational and microarray analysis of transcription in the Drosophila melanogaster testis
    • Andrews J., Bouffard G.G., Cheadle C., Lu J.N., Becker K.G., Oliver B. Gene discovery using computational and microarray analysis of transcription in the Drosophila melanogaster testis. Genome Research. 10:2000;2030-2043
    • (2000) Genome Research , vol.10 , pp. 2030-2043
    • Andrews, J.1    Bouffard, G.G.2    Cheadle, C.3    Lu, J.N.4    Becker, K.G.5    Oliver, B.6
  • 3
    • 0012830439 scopus 로고    scopus 로고
    • The plasma membrane proton pump ATPase: The significance of gene subfamilies
    • Arango M., Gevaudant F., Oufattole M., Boutry M. The plasma membrane proton pump ATPase: the significance of gene subfamilies. Planta. 216:2003;355-365
    • (2003) Planta , vol.216 , pp. 355-365
    • Arango, M.1    Gevaudant, F.2    Oufattole, M.3    Boutry, M.4
  • 4
    • 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 Journal. 36:2003;652-663
    • (2003) Plant Journal , vol.36 , pp. 652-663
    • Bae, M.S.1    Cho, E.J.2    Choi, E.Y.3    Park, O.K.4
  • 6
    • 0037294003 scopus 로고    scopus 로고
    • Affinity purification-mass spectrometry. Powerful tools for the characterization of protein complexes
    • Bauer A., Kuster B. Affinity purification-mass spectrometry. Powerful tools for the characterization of protein complexes. European Journal of Biochemistry. 270:2003;570-578
    • (2003) European Journal of Biochemistry , vol.270 , pp. 570-578
    • Bauer, A.1    Kuster, B.2
  • 8
    • 0037866868 scopus 로고    scopus 로고
    • Proteomic identification of plant proteins probed by mammalian nitric oxide synthase antibodies
    • Butt Y.K., Lum J.H., Lo S.C. Proteomic identification of plant proteins probed by mammalian nitric oxide synthase antibodies. Planta. 216:2003;762-771
    • (2003) Planta , vol.216 , pp. 762-771
    • Butt, Y.K.1    Lum, J.H.2    Lo, S.C.3
  • 10
    • 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. Journal of Biological Chemistry. 278:2003;46869-46877
    • (2003) Journal of Biological Chemistry , vol.278 , pp. 46869-46877
    • Chew, O.1    Whelan, J.2    Millar, A.H.3
  • 11
    • 1642532372 scopus 로고    scopus 로고
    • A plant outer mitochondrial membrane protein with high amino acid sequence identity to a chloroplast protein import receptor
    • Chew O., Lister R., Qbadou S., Heazlewood J.L., Soll J., Schleiff E., Millar A.H., Whelan J. A plant outer mitochondrial membrane protein with high amino acid sequence identity to a chloroplast protein import receptor. FEBS Letters. 557:2004;109-114
    • (2004) FEBS Letters , vol.557 , pp. 109-114
    • Chew, O.1    Lister, R.2    Qbadou, S.3    Heazlewood, J.L.4    Soll, J.5    Schleiff, E.6    Millar, A.H.7    Whelan, J.8
  • 14
    • 0016990971 scopus 로고
    • The origin and evolution of protein superfamilies
    • Dayoff M.O. The origin and evolution of protein superfamilies. Federation Proceedings. 35:1976;2132-2138
    • (1976) Federation Proceedings , vol.35 , pp. 2132-2138
    • Dayoff, M.O.1
  • 15
    • 0035983618 scopus 로고    scopus 로고
    • The branched-chain amino acid transaminase gene family in Arabidopsis encodes plastid and mitochondrial proteins
    • Diebold R., Schuster J., Daschner K., Binder S. The branched-chain amino acid transaminase gene family in Arabidopsis encodes plastid and mitochondrial proteins. Plant Physiology. 129:2002;540-550
    • (2002) Plant Physiology , vol.129 , pp. 540-550
    • Diebold, R.1    Schuster, J.2    Daschner, K.3    Binder, S.4
  • 16
    • 0036202462 scopus 로고    scopus 로고
    • Plant glutathione transferases
    • reviews3004.1-3004.10
    • Dixon D.P., Lapthorn A., Edwards R. Plant glutathione transferases. Genome Biology. 3:2002;. reviews3004.1-3004.10
    • (2002) Genome Biology , vol.3
    • Dixon, D.P.1    Lapthorn, A.2    Edwards, R.3
  • 18
    • 0037092969 scopus 로고    scopus 로고
    • Identification of polysaccharide binding proteins by affinity electrophoresis in inhomogeneous polyacrylamide gels and subsequent SDS-PAGE/matrix-assisted laser desorption ionization-time of flight analysis
    • Eckermann N., Fettke J., Steup M. Identification of polysaccharide binding proteins by affinity electrophoresis in inhomogeneous polyacrylamide gels and subsequent SDS-PAGE/matrix-assisted laser desorption ionization-time of flight analysis. Analytical Biochemistry. 304:2002;180-192
    • (2002) Analytical Biochemistry , vol.304 , pp. 180-192
    • Eckermann, N.1    Fettke, J.2    Steup, M.3
  • 20
    • 0347925092 scopus 로고    scopus 로고
    • Tandemly duplicated Arabidopsis genes that encode polygalacturonase- inhibiting proteins are regulated coordinately by different signal transduction pathways in response to fungal infection
    • Ferrari S., Vairo D., Ausubel F.M., Cervone F., De Lorenzo G. Tandemly duplicated Arabidopsis genes that encode polygalacturonase-inhibiting proteins are regulated coordinately by different signal transduction pathways in response to fungal infection. Plant Cell. 15:2003;93-106
    • (2003) Plant Cell , vol.15 , pp. 93-106
    • Ferrari, S.1    Vairo, D.2    Ausubel, F.M.3    Cervone, F.4    De Lorenzo, G.5
  • 22
    • 1042279117 scopus 로고    scopus 로고
    • In-depth analysis of the thylakoid membrane proteome of Arabidopsis thaliana chloroplasts; New proteins, functions and a plastid proteome database
    • Friso G., Ytterberg A.J., Giacomelli L., Peltier J.B., Rudella A., Sun Q., van Wijk K.J. In-depth analysis of the thylakoid membrane proteome of Arabidopsis thaliana chloroplasts; new proteins, functions and a plastid proteome database. The Plant Cell. 16:2004;478-499
    • (2004) The Plant Cell , vol.16 , pp. 478-499
    • Friso, G.1    Ytterberg, A.J.2    Giacomelli, L.3    Peltier, J.B.4    Rudella, A.5    Sun, Q.6    Van Wijk, K.J.7
  • 23
    • 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 K., McAndrew R.S., Osteryoung K.W., Gage D.A., Phinney B.S. Proteomic study of the Arabidopsis thaliana chloroplastic envelope membrane utilizing alternatives to traditional two-dimensional electrophoresis. Journal of Proteome Research. 2:2003;413-425
    • (2003) Journal of Proteome Research , vol.2 , pp. 413-425
    • Froehlich, J.E.1    Wilkerson, C.G.2    Ray, K.3    McAndrew, R.S.4    Osteryoung, K.W.5    Gage, D.A.6    Phinney, B.S.7
  • 24
    • 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 Physiology. 43:2002;689-696
    • (2002) Plant & Cell Physiology , vol.43 , pp. 689-696
    • Fukao, Y.1    Hayashi, M.2    Nishimura, M.3
  • 27
    • 0036051481 scopus 로고    scopus 로고
    • The chloroplast grana proteome defined by intact mass measurements from liquid chromatography mass spectrometry
    • Gomez S.M., Nishio J.N., Faull K.F., Whitelegge J.P. The chloroplast grana proteome defined by intact mass measurements from liquid chromatography mass spectrometry. Molecular & Cellular Proteomics. 1:2002;46-59
    • (2002) Molecular & Cellular Proteomics , vol.1 , pp. 46-59
    • Gomez, S.M.1    Nishio, J.N.2    Faull, K.F.3    Whitelegge, J.P.4
  • 32
    • 0036391454 scopus 로고    scopus 로고
    • Proteome analysis of low-abundance proteins using multidimensional chromatography and isotope-coded affinity tags
    • Gygi S.P., Rist B., Griffin T.J., Eng J., Aebersold R. Proteome analysis of low-abundance proteins using multidimensional chromatography and isotope-coded affinity tags. Journal of Proteome Research. 1:2002;47-54
    • (2002) Journal of Proteome Research , vol.1 , pp. 47-54
    • Gygi, S.P.1    Rist, B.2    Griffin, T.J.3    Eng, J.4    Aebersold, R.5
  • 33
    • 1842546738 scopus 로고    scopus 로고
    • Identification of three previously unknown in vivo protein phosphorylation sites in thylakoid membranes of Arabidopsis thaliana
    • Hansson M., Vener A.V. Identification of three previously unknown in vivo protein phosphorylation sites in thylakoid membranes of Arabidopsis thaliana. Molecular & Cellular Proteomics. 2:2003;550-559
    • (2003) Molecular & Cellular Proteomics , vol.2 , pp. 550-559
    • Hansson, M.1    Vener, A.V.2
  • 34
    • 0842270043 scopus 로고    scopus 로고
    • Experimental analysis of the Arabidopsis mitochondrial proteome highlights signalling and regulatory components, provides assessment of targeting prediction programs and points to plant specific mitochondrial proteins
    • Heazlewood J.L., Tonti-Filippini J.S., Gout A.M., Day D.A., Whelan J., Millar A.H. Experimental analysis of the Arabidopsis mitochondrial proteome highlights signalling and regulatory components, provides assessment of targeting prediction programs and points to plant specific mitochondrial proteins. Plant Cell. 16:2004;241-256
    • (2004) Plant Cell , vol.16 , pp. 241-256
    • Heazlewood, J.L.1    Tonti-Filippini, J.S.2    Gout, A.M.3    Day, D.A.4    Whelan, J.5    Millar, A.H.6
  • 35
    • 0032924894 scopus 로고    scopus 로고
    • Advances in protein solubilisation for two-dimensional electrophoresis
    • Herbert B. Advances in protein solubilisation for two-dimensional electrophoresis. Electrophoresis. 20:1999;660-663
    • (1999) Electrophoresis , vol.20 , pp. 660-663
    • Herbert, B.1
  • 36
    • 0033672478 scopus 로고    scopus 로고
    • A turning point in proteome analysis: Sample prefractionation via multicompartment electrolyzers with isoelectric membranes
    • Herbert B., Righetti P.G. A turning point in proteome analysis: sample prefractionation via multicompartment electrolyzers with isoelectric membranes. Electrophoresis. 21:2000;3639-3648
    • (2000) Electrophoresis , vol.21 , pp. 3639-3648
    • Herbert, B.1    Righetti, P.G.2
  • 37
    • 0141502037 scopus 로고    scopus 로고
    • European consortia building integrated resources for Arabidopsis functional genomics
    • Hilson P., Small I., Kuiper M.T. European consortia building integrated resources for Arabidopsis functional genomics. Current Opinion in Plant Biology. 6:2003;426-429
    • (2003) Current Opinion in Plant Biology , vol.6 , pp. 426-429
    • Hilson, P.1    Small, I.2    Kuiper, M.T.3
  • 39
    • 0034947503 scopus 로고    scopus 로고
    • Mass spectrometry for protein and peptide characterisation
    • Jonsson A.P. Mass spectrometry for protein and peptide characterisation. Cellular & Molecular Life Sciences. 58:2001;868-884
    • (2001) Cellular & Molecular Life Sciences , vol.58 , pp. 868-884
    • Jonsson, A.P.1
  • 40
    • 0033773392 scopus 로고    scopus 로고
    • Proteomics meets cell biology: The establishment of subcellular proteomes
    • Jung E., Heller M., Sanchez J.C., Hochstrasser D.F. Proteomics meets cell biology: the establishment of subcellular proteomes. Electrophoresis. 21:2000;3369-3377
    • (2000) Electrophoresis , vol.21 , pp. 3369-3377
    • Jung, E.1    Heller, M.2    Sanchez, J.C.3    Hochstrasser, D.F.4
  • 42
    • 0037108887 scopus 로고    scopus 로고
    • Empirical statistical model to estimate the accuracy of peptide identifications made by MS/MS and database search
    • Keller A., Nesvizhskii A.I., Kolker E., Aebersold R. Empirical statistical model to estimate the accuracy of peptide identifications made by MS/MS and database search. Analytical Chemistry. 74:2002;5383-5392
    • (2002) Analytical Chemistry , vol.74 , pp. 5383-5392
    • Keller, A.1    Nesvizhskii, A.I.2    Kolker, E.3    Aebersold, R.4
  • 44
    • 0036835070 scopus 로고    scopus 로고
    • Family business: The multidrug-resistance related protein (MRP) ABC transporter genes in Arabidopsis thaliana
    • Kolukisaoglu H.U., Bovet L., Klein M., Eggmann T., Geisler M., Wanke D., Martinoia E., Schulz B. Family business: the multidrug-resistance related protein (MRP) ABC transporter genes in Arabidopsis thaliana. Planta. 216:2002;107-119
    • (2002) Planta , vol.216 , pp. 107-119
    • Kolukisaoglu, H.U.1    Bovet, L.2    Klein, M.3    Eggmann, T.4    Geisler, M.5    Wanke, D.6    Martinoia, E.7    Schulz, B.8
  • 47
    • 0002574663 scopus 로고    scopus 로고
    • The Dictionary of Cell & Molecular Biology
    • London: Academic Press
    • Lackie J.M., Dow J.A.T. The Dictionary of Cell & Molecular Biology. third ed.:1999;Academic Press, London
    • (1999) Third Ed.
    • Lackie, J.M.1    Dow, J.A.T.2
  • 50
    • 0035260225 scopus 로고    scopus 로고
    • Strategy for protein isoform identification from expressed sequence tags and its application to peptide mass fingerprinting
    • Lisacek F.C., Traini M.D., Sexton D., Harry J.L., Wilkins M.R. Strategy for protein isoform identification from expressed sequence tags and its application to peptide mass fingerprinting. Proteomics. 1:2001;186-193
    • (2001) Proteomics , vol.1 , pp. 186-193
    • Lisacek, F.C.1    Traini, M.D.2    Sexton, D.3    Harry, J.L.4    Wilkins, M.R.5
  • 51
    • 1342265924 scopus 로고    scopus 로고
    • A transcriptomic and proteomic characterisation of the Arabidopsis mitochondrial protein import apparatus and its response to mitochondrial dysfunction
    • Lister R., Chew O., Lee M.-N., Heazlewood J., Clifton R., Parker K., Millar A., Whelan J. A transcriptomic and proteomic characterisation of the Arabidopsis mitochondrial protein import apparatus and its response to mitochondrial dysfunction. Plant Physiology. 134:2004;777-789
    • (2004) Plant Physiology , vol.134 , pp. 777-789
    • Lister, R.1    Chew, O.2    Lee, M.-N.3    Heazlewood, J.4    Clifton, R.5    Parker, K.6    Millar, A.7    Whelan, J.8
  • 53
    • 0037636244 scopus 로고    scopus 로고
    • Identification, cloning and characterization of two thioredoxin h isoforms, HvTrxh1 and HvTrxh2, from the barley seed proteome
    • Maeda K., Finnie C., Stergaard O.S., Svensson B. Identification, cloning and characterization of two thioredoxin h isoforms, HvTrxh1 and HvTrxh2, from the barley seed proteome. European Journal of Biochemistry. 270:2003;2633-2643
    • (2003) European Journal of Biochemistry , vol.270 , pp. 2633-2643
    • Maeda, K.1    Finnie, C.2    Stergaard, O.S.3    Svensson, B.4
  • 55
    • 0344237365 scopus 로고    scopus 로고
    • Glutathione peroxidase genes in Arabidopsis are ubiquitous and regulated by abiotic stresses through diverse signaling pathways
    • Milla M.A., Maurer A., Huete A.R., Gustafson J.P. Glutathione peroxidase genes in Arabidopsis are ubiquitous and regulated by abiotic stresses through diverse signaling pathways. Plant Journal. 36:2003;602-615
    • (2003) Plant Journal , vol.36 , pp. 602-615
    • Milla, M.A.1    Maurer, A.2    Huete, A.R.3    Gustafson, J.P.4
  • 56
    • 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 Physiology. 131:2003;443-453
    • (2003) Plant Physiology , vol.131 , pp. 443-453
    • Millar, A.H.1    Heazlewood, J.L.2
  • 59
    • 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. Analytical Chemistry. 75:2003;4646-4658
    • (2003) Analytical Chemistry , vol.75 , pp. 4646-4658
    • Nesvizhskii, A.I.1    Keller, A.2    Kolker, E.3    Aebersold, R.4
  • 60
    • 0034002980 scopus 로고    scopus 로고
    • Five geranylgeranyl diphosphate synthases expressed in different organs are localized into three subcellular compartments in Arabidopsis
    • Okada K., Saito T., Nakagawa T., Kawamukai M., Kamiya Y. Five geranylgeranyl diphosphate synthases expressed in different organs are localized into three subcellular compartments in Arabidopsis. Plant Physiology. 122:2000;1045-1056
    • (2000) Plant Physiology , vol.122 , pp. 1045-1056
    • Okada, K.1    Saito, T.2    Nakagawa, T.3    Kawamukai, M.4    Kamiya, Y.5
  • 61
    • 0034954952 scopus 로고    scopus 로고
    • Directed proteomics identifies a plant-specific protein rapidly phosphorylated in response to bacterial and fungal elicitors
    • Peck S.C., Nuhse T.S., Hess D., Iglesias A., Meins F., Boller T. Directed proteomics identifies a plant-specific protein rapidly phosphorylated in response to bacterial and fungal elicitors. Plant Cell. 13:2001;1467-1475
    • (2001) Plant Cell , vol.13 , pp. 1467-1475
    • Peck, S.C.1    Nuhse, T.S.2    Hess, D.3    Iglesias, A.4    Meins, F.5    Boller, T.6
  • 63
    • 0027652967 scopus 로고
    • Comparison of four grass pollen species concerning their allergens of grass group V by 2D immunoblotting and microsequencing
    • Petersen A., Schramm G., Becker W.M., Schlaak M. Comparison of four grass pollen species concerning their allergens of grass group V by 2D immunoblotting and microsequencing. Biol Chem Hoppe Seyler. 374:1993;855-861
    • (1993) Biol Chem Hoppe Seyler , vol.374 , pp. 855-861
    • Petersen, A.1    Schramm, G.2    Becker, W.M.3    Schlaak, M.4
  • 67
    • 0034865417 scopus 로고    scopus 로고
    • Protein kinases in the plant defence response
    • Romeis T. Protein kinases in the plant defence response. Current Opinion in Plant Biology. 4:2001;407-414
    • (2001) Current Opinion in Plant Biology , vol.4 , pp. 407-414
    • Romeis, T.1
  • 69
    • 0035056535 scopus 로고    scopus 로고
    • Disruption of individual members of Arabidopsis syntaxin gene families indicates each has essential functions
    • Sanderfoot A.A., Pilgrim M., Adam L., Raikhel N.V. Disruption of individual members of Arabidopsis syntaxin gene families indicates each has essential functions. Plant Cell. 13:2001;659-666
    • (2001) Plant Cell , vol.13 , pp. 659-666
    • Sanderfoot, A.A.1    Pilgrim, M.2    Adam, L.3    Raikhel, N.V.4
  • 71
    • 3242773787 scopus 로고    scopus 로고
    • Proteomic analysis of glutathione S-transferases of Arabidopsis thaliana reveals differential salicylic acid induced expression of the plant specific Phi and Tau classes
    • in press
    • Sappl, P.G., Onãte-Sanchez, L., Singh, K., Millar, A.H., 2004. Proteomic analysis of glutathione S-transferases of Arabidopsis thaliana reveals differential salicylic acid induced expression of the plant specific Phi and Tau classes. Plant Molecular Biology, in press
    • (2004) Plant Molecular Biology
    • Sappl, P.G.1    Onãte-Sanchez, L.2    Singh, K.3    Millar, A.H.4
  • 75
    • 0031466276 scopus 로고    scopus 로고
    • Purification and determination of intact molecular mass by electrospray ionization mass spectrometry of the photosystem II reaction center subunits
    • Sharma J., Panico M., Barber J., Morris H.R. Purification and determination of intact molecular mass by electrospray ionization mass spectrometry of the photosystem II reaction center subunits. Journal of Biological Chemistry. 272:1997;33153-33157
    • (1997) Journal of Biological Chemistry , vol.272 , pp. 33153-33157
    • Sharma, J.1    Panico, M.2    Barber, J.3    Morris, H.R.4
  • 76
    • 0036702419 scopus 로고    scopus 로고
    • Identification of modified proteins by mass spectrometry
    • Sickmann A., Mreyen M., Meyer H.E. Identification of modified proteins by mass spectrometry. IUBMB Life. 54:2002;51-57
    • (2002) IUBMB Life , vol.54 , pp. 51-57
    • Sickmann, A.1    Mreyen, M.2    Meyer, H.E.3
  • 79
    • 0037401446 scopus 로고    scopus 로고
    • Preferential induction of 20S proteasome subunits during elicitation of plant defense reactions: Towards the characterization of plant defense proteasomes
    • Suty L., Lequeu J., Lancon A., Etienne P., Petitot A.S., Blein J.P. Preferential induction of 20S proteasome subunits during elicitation of plant defense reactions: towards the characterization of plant defense proteasomes. International Journal of Biochemistry & Cell Biology. 35:2003;637-650
    • (2003) International Journal of Biochemistry & Cell Biology , vol.35 , pp. 637-650
    • Suty, L.1    Lequeu, J.2    Lancon, A.3    Etienne, P.4    Petitot, A.S.5    Blein, J.P.6
  • 80
    • 0031812471 scopus 로고    scopus 로고
    • The identification of peptide modifications derived from gel-separated proteins using electrospray triple quadrupole and ion trap analyses
    • Swiderek K.M., Davis M.T., Lee T.D. The identification of peptide modifications derived from gel-separated proteins using electrospray triple quadrupole and ion trap analyses. Electrophoresis. 19:1998;989-997
    • (1998) Electrophoresis , vol.19 , pp. 989-997
    • Swiderek, K.M.1    Davis, M.T.2    Lee, T.D.3
  • 82
    • 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. 3rd DTASelect and Contrast: tools for assembling and comparing protein identifications from shotgun proteomics. Journal of Proteome Research. 1:2002;21-26
    • (2002) Journal of Proteome Research , vol.1 , pp. 21-26
    • Tabb, D.L.1    McDonald, W.H.2    Yates III, J.R.3
  • 83
    • 0027968068 scopus 로고
    • CLUSTAL W: Improving the sensitivity of progressive multiple sequence alignment through sequence weighting, positions-specific gap penalties and weight matrix choice
    • Thompson J.D., Higgins D.G., Gibson T.J. CLUSTAL W: improving the sensitivity of progressive multiple sequence alignment through sequence weighting, positions-specific gap penalties and weight matrix choice. Nucleic Acids Research. 22:1994;4673-4680
    • (1994) Nucleic Acids Research , vol.22 , pp. 4673-4680
    • Thompson, J.D.1    Higgins, D.G.2    Gibson, T.J.3
  • 84
    • 0037123359 scopus 로고    scopus 로고
    • Analysis and expression of the class III peroxidase large gene family in Arabidopsis thaliana
    • Tognolli M., Penel C., Greppin H., Simon P. Analysis and expression of the class III peroxidase large gene family in Arabidopsis thaliana. Gene. 288:2002;129-138
    • (2002) Gene , vol.288 , pp. 129-138
    • Tognolli, M.1    Penel, C.2    Greppin, H.3    Simon, P.4
  • 86
    • 0035983888 scopus 로고    scopus 로고
    • Probing the diversity of the Arabidopsis glutathione S-transferase gene family
    • Wagner U., Edwards R., Dixon D.P., Mauch F. Probing the diversity of the Arabidopsis glutathione S-transferase gene family. Plant Molecular Biology. 49:2002;515-532
    • (2002) Plant Molecular Biology , vol.49 , pp. 515-532
    • Wagner, U.1    Edwards, R.2    Dixon, D.P.3    Mauch, F.4
  • 87
    • 0036119404 scopus 로고    scopus 로고
    • Biochemical dissection of the mitochondrial proteome from Arabidopsis thaliana by three-dimensional gel electrophoresis
    • Werhahn W., Braun H.P. Biochemical dissection of the mitochondrial proteome from Arabidopsis thaliana by three-dimensional gel electrophoresis. Electrophoresis. 23:2002;640-646
    • (2002) Electrophoresis , vol.23 , pp. 640-646
    • Werhahn, W.1    Braun, H.P.2
  • 88
    • 0031776931 scopus 로고    scopus 로고
    • Electrospray-ionization mass spectrometry of intact intrinsic membrane proteins
    • Whitelegge J.P., Gundersen C.B., Faull K.F. Electrospray-ionization mass spectrometry of intact intrinsic membrane proteins. Protein Science. 7:1998;1423-1430
    • (1998) Protein Science , vol.7 , pp. 1423-1430
    • Whitelegge, J.P.1    Gundersen, C.B.2    Faull, K.F.3
  • 89
    • 0012252011 scopus 로고    scopus 로고
    • Full subunit coverage liquid chromatography electrospray ionization mass spectrometry (LCMS+) of an oligomeric membrane protein: Cytochrome b(6)f complex from spinach and the cyanobacterium Mastigocladus laminosus
    • Whitelegge J.P., Zhang H., Aguilera R., Taylor R.M., Cramer W.A. Full subunit coverage liquid chromatography electrospray ionization mass spectrometry (LCMS+) of an oligomeric membrane protein: cytochrome b(6)f complex from spinach and the cyanobacterium Mastigocladus laminosus. Molecular & Cellular Proteomics. 1:2002;816-827
    • (2002) Molecular & Cellular Proteomics , vol.1 , pp. 816-827
    • Whitelegge, J.P.1    Zhang, H.2    Aguilera, R.3    Taylor, R.M.4    Cramer, W.A.5
  • 92
    • 0034760628 scopus 로고    scopus 로고
    • A comprehensive expression analysis of all members of a gene family encoding cell-wall enzymes allowed us to predict cis-regulatory regions involved in cell-wall construction in specific organs of Arabidopsis
    • Yokoyama R., Nishitani K. A comprehensive expression analysis of all members of a gene family encoding cell-wall enzymes allowed us to predict cis-regulatory regions involved in cell-wall construction in specific organs of Arabidopsis. Plant & Cell Physiology. 42:2001;1025-1033
    • (2001) Plant & Cell Physiology , vol.42 , pp. 1025-1033
    • Yokoyama, R.1    Nishitani, K.2
  • 93
    • 0036929475 scopus 로고    scopus 로고
    • Proteomics of light-harvesting proteins in different plant species. Analysis and comparison by liquid chromatography-electrospray ionization mass spectrometry
    • Zolla L., Rinalducci S., Timperio A.M., Huber C.G. Proteomics of light-harvesting proteins in different plant species. Analysis and comparison by liquid chromatography-electrospray ionization mass spectrometry. Photosystem I. Plant Physiology. 130:2002;1938-1950
    • (2002) Photosystem I. Plant Physiology , vol.130 , pp. 1938-1950
    • Zolla, L.1    Rinalducci, S.2    Timperio, A.M.3    Huber, C.G.4


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