메뉴 건너뛰기




Volumn , Issue , 2007, Pages 1-31

Plant Proteomics: Challenges and Resources

Author keywords

Gene sequencing; Liquid chromatography; Mass spectrometry; Proteome; Two dimensional gel electrophoresis

Indexed keywords

ELECTROPHORESIS; MASS SPECTROMETRY; MOLECULAR BIOLOGY; PROTEINS;

EID: 84948106121     PISSN: None     EISSN: None     Source Type: Book    
DOI: 10.1002/9780470988879.ch1     Document Type: Chapter
Times cited : (4)

References (116)
  • 1
    • 11144273935 scopus 로고    scopus 로고
    • Arabidopsis plasma membrane proteomics identifies components of transport, signal transduction and membrane trafficking
    • Alexandersson, E., Saalbach, G., Larsson, C. and Kjellbom, P. (2004) Arabidopsis plasma membrane proteomics identifies components of transport, signal transduction and membrane trafficking. Plant Cell Physiol., 45, 1543-1556.
    • (2004) Plant Cell Physiol. , vol.45 , pp. 1543-1556
    • Alexandersson, E.1    Saalbach, G.2    Larsson, C.3    Kjellbom, P.4
  • 3
    • 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., Yates III, J.R. and Haynes, P.A. (2002) Proteomic characterization of wheat amyloplasts using identification of proteins by tandem mass spectrometry. Proteomics, 2, 1156-1168.
    • (2002) Proteomics , vol.2 , pp. 1156-1168
    • Andon, N.L.1    Hollingworth, S.2    Koller, A.3    Greenland, A.J.4    Yates, J.R.5    Haynes, P.A.6
  • 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. and Park, O.K. (2003) Analysis of the Arabidopsis nuclear proteome and its response to cold stress. Plant J., 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
  • 5
    • 26844506696 scopus 로고    scopus 로고
    • The Paris consensus
    • Beavis, R. (2005) The Paris consensus. J. Proteome Res., 5, 1475.
    • (2005) J. Proteome Res. , vol.5 , pp. 1475
    • Beavis, R.1
  • 6
    • 0042386232 scopus 로고    scopus 로고
    • Exploiting the complementary nature of LC/MALDI/MS/MS and LC/ESI/MS/MS for increased proteome coverage
    • Bodnar, W.M., Blackburn, R.K., Krise, J.M. and Moseley, M.A. (2003) Exploiting the complementary nature of LC/MALDI/MS/MS and LC/ESI/MS/MS for increased proteome coverage. J. Am. Soc. Mass Spectrom., 14, 971-979.
    • (2003) J. Am. Soc. Mass Spectrom. , vol.14 , pp. 971-979
    • Bodnar, W.M.1    Blackburn, R.K.2    Krise, J.M.3    Moseley, M.A.4
  • 7
    • 0032723313 scopus 로고    scopus 로고
    • Matrix-assisted laser desorption/ionisation time-of-flight mass spectrometry for monitoring alkylation of beta-lactoglobulin B exposed to a series of N-substituted acrylamide monomers
    • Bordini, E., Hamdan, M. and Righetti, P.G. (1999) Matrix-assisted laser desorption/ionisation time-of-flight mass spectrometry for monitoring alkylation of beta-lactoglobulin B exposed to a series of N-substituted acrylamide monomers. Rapid Commun. Mass Spectrom., 13, 2209-2215.
    • (1999) Rapid Commun. Mass Spectrom. , vol.13 , pp. 2209-2215
    • Bordini, E.1    Hamdan, M.2    Righetti, P.G.3
  • 8
    • 24044441882 scopus 로고    scopus 로고
    • Revised draft guidelines for proteomic data publication
    • Bradshaw, R.A. (2005) Revised draft guidelines for proteomic data publication. Mol. Cell. Proteom., 4, 1223-1225.
    • (2005) Mol. Cell. Proteom. , vol.4 , pp. 1223-1225
    • Bradshaw, R.A.1
  • 9
    • 0141529726 scopus 로고    scopus 로고
    • A proteomic study of the Arabidopsis nuclear matrix
    • Calikowski, T.T., Meulia, T. and Meier, I. (2003) A proteomic study of the Arabidopsis nuclear matrix. J. Cell. Biochem., 90, 361-378.
    • (2003) J. Cell. Biochem. , vol.90 , pp. 361-378
    • Calikowski, T.T.1    Meulia, T.2    Meier, I.3
  • 10
    • 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., Swennen, R. and Panis, B. (2005) Preparation of protein extracts from recalcitrant plant tissues: an evaluation of different methods for two-dimensional gel electrophoresis analysis. Proteomics, 5, 2497-2507.
    • (2005) Proteomics , vol.5 , pp. 2497-2507
    • Carpentier, S.C.1    Witters, E.2    Laukens, K.3    Deckers, P.4    Swennen, R.5    Panis, B.6
  • 11
    • 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., Clauser, K. and Nesvizhskii, A. (2004) 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. Proteom., 3, 531-533.
    • (2004) Mol. Cell. Proteom. , vol.3 , pp. 531-533
    • Carr, S.1    Aebersold, R.2    Baldwin, M.3    Burlingame, A.4    Clauser, K.5    Nesvizhskii, A.6
  • 12
    • 15744385479 scopus 로고    scopus 로고
    • The vegetative vacuole proteome of Arabidopsis thaliana reveals predicted and unexpected proteins
    • Carter, C., Pan, S., Zouhar, J., Avila, E.L., Girke, T. and Raikhel, N.V. (2004) The vegetative vacuole proteome of Arabidopsis thaliana reveals predicted and unexpected proteins. Plant Cell, 16, 3285-3303.
    • (2004) Plant Cell , vol.16 , pp. 3285-3303
    • Carter, C.1    Pan, S.2    Zouhar, J.3    Avila, E.L.4    Girke, T.5    Raikhel, N.V.6
  • 13
    • 0344305739 scopus 로고    scopus 로고
    • Global protein identification and quantification technology using two-dimensional liquid chromatography nanospray mass spectrometry
    • Chelius, D., Zhang, T., Wang, G. and Shen, R.F. (2003) Global protein identification and quantification technology using two-dimensional liquid chromatography nanospray mass spectrometry. Anal. Chem., 75, 6658-6665.
    • (2003) Anal. Chem. , vol.75 , pp. 6658-6665
    • Chelius, D.1    Zhang, T.2    Wang, G.3    Shen, R.F.4
  • 14
    • 28544435850 scopus 로고    scopus 로고
    • Enhanced characterization of complex proteomic samples using LC-MALDI MS/MS: exclusion of redundant peptides from MS/MS analysis in replicate runs
    • Chen, H.S., Rejtar, T., Andreev, V., Moskovets, E. and Karger, B.L. (2005) Enhanced characterization of complex proteomic samples using LC-MALDI MS/MS: exclusion of redundant peptides from MS/MS analysis in replicate runs. Anal. Chem., 77, 7816-7825.
    • (2005) Anal. Chem , vol.77 , pp. 7816-7825
    • Chen, H.S.1    Rejtar, T.2    Andreev, V.3    Moskovets, E.4    Karger, B.L.5
  • 17
    • 0141786914 scopus 로고    scopus 로고
    • New insights into the respiratory chain of plant mitochondria. Supercomplexes and a unique composition of complex II
    • Eubel, H., Jansch, L. and Braun, H.P. (2003) New insights into the respiratory chain of plant mitochondria. Supercomplexes and a unique composition of complex II. Plant Physiol., 133, 274-286.
    • (2003) Plant Physiol. , vol.133 , pp. 274-286
    • Eubel, H.1    Jansch, L.2    Braun, H.P.3
  • 18
    • 33744901613 scopus 로고    scopus 로고
    • Blue-native PAGE in plants: a tool in analysis of protein-protein interactions
    • Eubel, H., Braun, H.P. and Millar, A.H. (2005) Blue-native PAGE in plants: a tool in analysis of protein-protein interactions. Plant Method., 1, 11.
    • (2005) Plant Method. , vol.1 , pp. 11
    • Eubel, H.1    Braun, H.P.2    Millar, A.H.3
  • 21
    • 1042279117 scopus 로고    scopus 로고
    • In-depth analysis of the thylakoid membrane proteome of Arabidopsis thaliana chloroplasts: new proteins, new functions, and a plastid proteome database
    • Friso, G., Giacomelli, L., Ytterberg, A.J., Peltier, J.B., Rudella, A., Sun, Q. and Wijk, K.J. (2004) In-depth analysis of the thylakoid membrane proteome of Arabidopsis thaliana chloroplasts: new proteins, new functions, and a plastid proteome database. Plant Cell, 16, 478-499.
    • (2004) Plant Cell , vol.16 , pp. 478-499
    • Friso, G.1    Giacomelli, L.2    Ytterberg, A.J.3    Peltier, J.B.4    Rudella, A.5    Sun, Q.6    Wijk, K.J.7
  • 22
    • 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. and Phinney, B.S. (2003) Proteomic study of the Arabidopsis thaliana chloroplastic envelope membrane utilizing alternatives to traditional two-dimensional electrophoresis. J. Proteome Res., 2, 413-425.
    • (2003) J. Proteome Res. , 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
  • 23
    • 0036346730 scopus 로고    scopus 로고
    • Proteomic analysis of leaf peroxisomal proteins in greening cotyledons of Arabidopsis thaliana
    • Fukao, Y., Hayashi, M. and Nishimura, M. (2002) Proteomic analysis of leaf peroxisomal proteins in greening cotyledons of Arabidopsis thaliana. Plant Cell Physiol., 43, 689-696.
    • (2002) Plant Cell Physiol. , vol.43 , pp. 689-696
    • Fukao, Y.1    Hayashi, M.2    Nishimura, M.3
  • 24
    • 0242403025 scopus 로고    scopus 로고
    • Novel glyoxysomal protein kinase, GPK1, identified by proteomic analysis of glyoxysomes in etiolated cotyledons of Arabidopsis thaliana
    • Fukao, Y., Hayashi, M., Hara-Nishimura, I. and Nishimura, M. (2003) Novel glyoxysomal protein kinase, GPK1, identified by proteomic analysis of glyoxysomes in etiolated cotyledons of Arabidopsis thaliana. Plant Cell Physiol., 44, 1002-1012.
    • (2003) Plant Cell Physiol. , vol.44 , pp. 1002-1012
    • Fukao, Y.1    Hayashi, M.2    Hara-Nishimura, I.3    Nishimura, M.4
  • 26
    • 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. and Yates III, J.R. (1998) 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., 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, J.R.5
  • 27
    • 0032935361 scopus 로고    scopus 로고
    • Analysis of the mouse proteome. (I) Brain proteins: separation by two-dimensional electrophoresis and identification by mass spectrometry and genetic variation
    • Gauss, C., Kalkum, M., Lowe, M., Lehrach, H. and Klose, J. (1999) Analysis of the mouse proteome. (I) Brain proteins: separation by two-dimensional electrophoresis and identification by mass spectrometry and genetic variation. Electrophoresis, 20, 575-600.
    • (1999) Electrophoresis , vol.20 , pp. 575-600
    • Gauss, C.1    Kalkum, M.2    Lowe, M.3    Lehrach, H.4    Klose, J.5
  • 28
    • 0037265724 scopus 로고    scopus 로고
    • Extraction of proteins from plant tissues for two-dimensional electrophoresis analysis
    • Giavalisco, P., Nordhoff, E., Lehrach, H., Gobom, J. and Klose, J. (2003) Extraction of proteins from plant tissues for two-dimensional electrophoresis analysis. Electrophoresis, 24, 207-216.
    • (2003) Electrophoresis , vol.24 , pp. 207-216
    • Giavalisco, P.1    Nordhoff, E.2    Lehrach, H.3    Gobom, J.4    Klose, J.5
  • 29
    • 0023768475 scopus 로고
    • The current state of two-dimensional electrophoresis with immobilized pH gradients
    • Görg, A., Postel, W. and Günther, S. (1988) The current state of two-dimensional electrophoresis with immobilized pH gradients. Electrophoresis, 9, 531-546.
    • (1988) Electrophoresis , vol.9 , pp. 531-546
    • Görg, A.1    Postel, W.2    Günther, S.3
  • 30
    • 0024118527 scopus 로고
    • Extraction of plant proteins for two-dimensional electrophoresis
    • Granier, F. (1988) Extraction of plant proteins for two-dimensional electrophoresis. Electrophoresis, 9, 712-718.
    • (1988) Electrophoresis , vol.9 , pp. 712-718
    • Granier, F.1
  • 32
    • 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., Gelb, M.H. and Aebersold, R. (1999) Quantitative analysis of complex protein mixtures using isotope-coded affinity tags. Nat. Biotechnol., 17, 994-999.
    • (1999) Nat. Biotechnol. , vol.17 , pp. 994-999
    • Gygi, S.P.1    Rist, B.2    Gerber, S.A.3    Turecek, F.4    Gelb, M.H.5    Aebersold, R.6
  • 33
    • 0033885949 scopus 로고    scopus 로고
    • Measuring gene expression by quantitative proteome analysis
    • Gygi, S.P., Rist, B. and Aebersold, R. (2000) Measuring gene expression by quantitative proteome analysis. Curr. Opin. Biotechnol., 11, 396-401.
    • (2000) Curr. Opin. Biotechnol. , vol.11 , pp. 396-401
    • Gygi, S.P.1    Rist, B.2    Aebersold, R.3
  • 34
    • 0034789979 scopus 로고    scopus 로고
    • Quantitative profiling of differentiation-induced microsomal proteins using isotope-coded affinity tags and mass spectrometry
    • Han, D.K., Eng, J., Zhou, H. and Aebersold, R. (2001) Quantitative profiling of differentiation-induced microsomal proteins using isotope-coded affinity tags and mass spectrometry. Nat. Biotechnol., 19, 946-951.
    • (2001) Nat. Biotechnol. , vol.19 , pp. 946-951
    • Han, D.K.1    Eng, J.2    Zhou, H.3    Aebersold, R.4
  • 36
    • 0037444512 scopus 로고    scopus 로고
    • Fast-response proteomics by accelerated in-gel digestion of proteins
    • Havlis, J., Thomas, H., Sebela, M. and Shevchenko, A. (2003) Fast-response proteomics by accelerated in-gel digestion of proteins. Anal. Chem., 75, 1300-1306.
    • (2003) Anal. Chem. , vol.75 , pp. 1300-1306
    • Havlis, J.1    Thomas, H.2    Sebela, M.3    Shevchenko, A.4
  • 37
    • 0037626984 scopus 로고    scopus 로고
    • Integrated plant proteomics - putting the green genomes to work
    • Heazlewood, J.L. and Millar, A.H. (2003) Integrated plant proteomics - putting the green genomes to work. Funct. Plant Biol., 30, 471-482.
    • (2003) Funct. Plant Biol. , vol.30 , pp. 471-482
    • Heazlewood, J.L.1    Millar, A.H.2
  • 38
    • 0038433229 scopus 로고    scopus 로고
    • Mitochondrial complex I form Arabidopsis and rice: orthologs of mammalian and fungal components coupled with plant-specific subunits
    • Heazlewood, J.L., Howell, K.A. and Millar, A.H. (2003a) Mitochondrial complex I form Arabidopsis and rice: orthologs of mammalian and fungal components coupled with plant-specific subunits. Biochim. Biophys. Acta, 1604, 159-169.
    • (2003) Biochim. Biophys. Acta , vol.1604 , pp. 159-169
    • Heazlewood, J.L.1    Howell, K.A.2    Millar, A.H.3
  • 39
    • 0037430978 scopus 로고    scopus 로고
    • The products of the mitochondrial orf25 and orfB genes are F0 components in the plant F1F0 ATP synthase
    • Heazlewood, J.L., Whelan, J. and Millar, A.H. (2003b) The products of the mitochondrial orf25 and orfB genes are F0 components in the plant F1F0 ATP synthase. FEBS Lett., 540, 201-205.
    • (2003) FEBS Lett. , vol.540 , pp. 201-205
    • Heazlewood, J.L.1    Whelan, J.2    Millar, A.H.3
  • 40
    • 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. and Millar, A.H. (2004) 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, 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
  • 41
    • 33644649331 scopus 로고    scopus 로고
    • Combining experimental and predicted datasets for determination of the subcellular location of proteins in Arabidopsis
    • Heazlewood, J.L., Tonti-Filippini, J., Verboom, R.E. and Millar, A.H. (2005) Combining experimental and predicted datasets for determination of the subcellular location of proteins in Arabidopsis. Plant Physiol., 139, 598-609.
    • (2005) Plant Physiol. , vol.139 , pp. 598-609
    • Heazlewood, J.L.1    Tonti-Filippini, J.2    Verboom, R.E.3    Millar, A.H.4
  • 42
    • 3242754429 scopus 로고    scopus 로고
    • Proteomic approach to characterize the supramolecular organization of photosystems in higher plants
    • Heinemeyer, J., Eubel, H., Wehmhoner, D., Jansch, L. and Braun, H.P. (2004) Proteomic approach to characterize the supramolecular organization of photosystems in higher plants. Phytochemistry, 65, 1683-1692.
    • (2004) Phytochemistry , vol.65 , pp. 1683-1692
    • Heinemeyer, J.1    Eubel, H.2    Wehmhoner, D.3    Jansch, L.4    Braun, H.P.5
  • 43
    • 0032924894 scopus 로고    scopus 로고
    • Advances in protein solubilisation for two-dimensional electrophoresis
    • Herbert, B. (1999) Advances in protein solubilisation for two-dimensional electrophoresis. Electrophoresis, 20, 660-663.
    • (1999) Electrophoresis , vol.20 , pp. 660-663
    • Herbert, B.1
  • 44
    • 0031861787 scopus 로고    scopus 로고
    • Improved protein solubility in two-dimensional electrophoresis using tributyl phosphine as reducing agent
    • Herbert, B.R., Molloy, M.P., Gooley, A.A., Walsh, B.J., Bryson, W.G. and Williams, K.L. (1998) Improved protein solubility in two-dimensional electrophoresis using tributyl phosphine as reducing agent. Electrophoresis, 19, 845-851.
    • (1998) Electrophoresis , vol.19 , pp. 845-851
    • Herbert, B.R.1    Molloy, M.P.2    Gooley, A.A.3    Walsh, B.J.4    Bryson, W.G.5    Williams, K.L.6
  • 45
    • 0034940957 scopus 로고    scopus 로고
    • Reduction and alkylation of proteins in preparation of two-dimensional map analysis:Why, when, and how?
    • Herbert, B., Galvani, M., Hamdan, M., Olivieri, E., MacCarthy, J., Pedersen, S. and Righetti, P.G. (2001a) Reduction and alkylation of proteins in preparation of two-dimensional map analysis:Why, when, and how? Electrophoresis, 22, 2046-2057.
    • (2001) Electrophoresis , vol.22 , pp. 2046-2057
    • Herbert, B.1    Galvani, M.2    Hamdan, M.3    Olivieri, E.4    MacCarthy, J.5    Pedersen, S.6    Righetti, P.G.7
  • 47
    • 0001510436 scopus 로고
    • Solubilization of plant membrane proteins for analysis by twodimensional gel electrophoresis
    • Hurkman, W.J. and Tanaka, C.K. (1986) Solubilization of plant membrane proteins for analysis by twodimensional gel electrophoresis. Plant Physiol., 81, 802-806.
    • (1986) Plant Physiol. , vol.81 , pp. 802-806
    • Hurkman, W.J.1    Tanaka, C.K.2
  • 48
    • 0028060306 scopus 로고
    • Protein identification in DNA databases by peptide mass fingerprinting
    • James, P., Quadroni, M., Carafoli, E. and Gonnet, G. (1994) Protein identification in DNA databases by peptide mass fingerprinting. Protein Sci., 3, 1347-1350.
    • (1994) Protein Sci. , vol.3 , pp. 1347-1350
    • James, P.1    Quadroni, M.2    Carafoli, E.3    Gonnet, G.4
  • 49
    • 0030111226 scopus 로고    scopus 로고
    • New insights into the composition, molecular mass and stoichiometry of the protein complexes of plant mitochondria
    • Jänsch, L., Kruft, V., Schmitz, U.K. and Braun, H.P. (1996) New insights into the composition, molecular mass and stoichiometry of the protein complexes of plant mitochondria. Plant J., 9, 357-368.
    • (1996) Plant J. , vol.9 , pp. 357-368
    • Jänsch, L.1    Kruft, V.2    Schmitz, U.K.3    Braun, H.P.4
  • 52
    • 0032956095 scopus 로고    scopus 로고
    • Separation and characterization of proteins from green and etiolated shoots of rice (Oryza sativa L.): towards a rice proteome
    • Komatsu, S., Muhammad, A. and Rakwal, R. (1999) Separation and characterization of proteins from green and etiolated shoots of rice (Oryza sativa L.): towards a rice proteome. Electrophoresis, 20, 630-636.
    • (1999) Electrophoresis , vol.20 , pp. 630-636
    • Komatsu, S.1    Muhammad, A.2    Rakwal, R.3
  • 53
    • 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. and Higo, K. (2004) Rice proteome database based on two-dimensional polyacrylamide gel electrophoresis: its status in 2003. Nucleic Acid. Res., 32, D388-D392.
    • (2004) Nucleic Acid. Res. , vol.32 , pp. D388-D392
    • Komatsu, S.1    Kojima, K.2    Suzuki, K.3    Ozaki, K.4    Higo, K.5
  • 54
    • 85047683107 scopus 로고    scopus 로고
    • Proteomic approach to identify novel mitochondrial proteins in Arabidopsis
    • Kruft, V., Eubel, H., Jansch, L., Werhahn, W. and Braun, H.P. (2001) Proteomic approach to identify novel mitochondrial proteins in Arabidopsis. Plant Physiol., 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
  • 57
    • 0037253223 scopus 로고    scopus 로고
    • Expanding the organismal scope of proteomics: cross-species protein identification by mass spectrometry and its implications
    • Liska, A.J. and Shevchenko, A. (2003) Expanding the organismal scope of proteomics: cross-species protein identification by mass spectrometry and its implications. Proteomics, 3, 19-28.
    • (2003) Proteomics , vol.3 , pp. 19-28
    • Liska, A.J.1    Shevchenko, A.2
  • 58
    • 3242731195 scopus 로고    scopus 로고
    • A model for random sampling and estimation of relative protein abundance in shotgun proteomics
    • Liu, H., Sadygov, R.G. and Yates III, J.R. (2004) A model for random sampling and estimation of relative protein abundance in shotgun proteomics. Anal. Chem., 76, 4193-4201.
    • (2004) Anal. Chem. , vol.76 , pp. 4193-4201
    • Liu, H.1    Sadygov, R.G.2    Yates, J.R.3
  • 59
    • 0033667456 scopus 로고    scopus 로고
    • A comparison of silver stain and SYPRO Ruby Protein Gel Stain with respect to protein detection in twodimensional gels and identification by peptide mass profiling
    • Lopez, M.F., Berggren, K., Chernokalskaya, E., Lazarev, A., Robinson, M. and Patton, W.F. (2000) A comparison of silver stain and SYPRO Ruby Protein Gel Stain with respect to protein detection in twodimensional gels and identification by peptide mass profiling. Electrophoresis, 21, 3673-3683.
    • (2000) Electrophoresis , vol.21 , pp. 3673-3683
    • Lopez, M.F.1    Berggren, K.2    Chernokalskaya, E.3    Lazarev, A.4    Robinson, M.5    Patton, W.F.6
  • 60
    • 0037338365 scopus 로고    scopus 로고
    • Proteomic analysis of post-translational modifications
    • Mann, M. and Jensen, O.N. (2003) Proteomic analysis of post-translational modifications. Nat. Biotechnol., 21, 255-261.
    • (2003) Nat. Biotechnol. , vol.21 , pp. 255-261
    • Mann, M.1    Jensen, O.N.2
  • 61
    • 0035525061 scopus 로고    scopus 로고
    • Establishment of a root proteome reference map for the model legume Medicago truncatula using the expressed sequence tag database for peptide mass fingerprinting
    • Mathesius, U., Keijzers, G., Natera, S.H., Weinman, J.J., Djordjevic, M.A. and Rolfe, B.G. (2001) Establishment of a root proteome reference map for the model legume Medicago truncatula using the expressed sequence tag database for peptide mass fingerprinting. Proteomics, 1, 1424-1440.
    • (2001) Proteomics , vol.1 , pp. 1424-1440
    • Mathesius, U.1    Keijzers, G.2    Natera, S.H.3    Weinman, J.J.4    Djordjevic, M.A.5    Rolfe, B.G.6
  • 63
    • 0036684101 scopus 로고    scopus 로고
    • Comparison of three directly coupled HPLC MS/MS strategies for identification of proteins from complex mixtures:single-dimension LC-MS/MS, 2-phase MudPIT, and 3-phase MudPIT
    • McDonald, W.H., Ohi, R., Miyamoto, D.T., Mitchison, T.J. and Yates III, J.R. (2002) Comparison of three directly coupled HPLC MS/MS strategies for identification of proteins from complex mixtures:single-dimension LC-MS/MS, 2-phase MudPIT, and 3-phase MudPIT. Int. J. Mass. Spectrom., 219, 245-251.
    • (2002) Int. J. Mass. Spectrom. , vol.219 , pp. 245-251
    • McDonald, W.H.1    Ohi, R.2    Miyamoto, D.T.3    Mitchison, T.J.4    Yates, J.R.5
  • 64
    • 3342890632 scopus 로고    scopus 로고
    • Location, location, location: surveying the intracellular real estate through proteomics in plants
    • Millar, A.H. (2004) Location, location, location: surveying the intracellular real estate through proteomics in plants. Funct. Plant. Biol., 31, 563-571.
    • (2004) Funct. Plant. Biol. , vol.31 , pp. 563-571
    • Millar, A.H.1
  • 65
    • 0037321898 scopus 로고    scopus 로고
    • Genomic and proteomic analysis of mitochondrial carrier proteins in Arabidopsis
    • Millar, A.H. and Heazlewood, J.L. (2003) Genomic and proteomic analysis of mitochondrial carrier proteins in Arabidopsis. Plant. Physiol., 131, 443-453.
    • (2003) Plant. Physiol. , vol.131 , pp. 443-453
    • Millar, A.H.1    Heazlewood, J.L.2
  • 66
    • 67651108027 scopus 로고    scopus 로고
    • Analysis of the Arabidopsis mitochondrial proteome
    • Millar, A.H., Sweetlove, L.J., Giege, P. and Leaver, C.J. (2001) Analysis of the Arabidopsis mitochondrial proteome. Plant Physiol, 127, 1711-1727.
    • (2001) Plant Physiol , vol.127 , pp. 1711-1727
    • Millar, A.H.1    Sweetlove, L.J.2    Giege, P.3    Leaver, C.J.4
  • 67
    • 0036107468 scopus 로고    scopus 로고
    • Identification of defence-related cell wall proteins in Phytophthora sojae-infected soybean roots by ESI-MS/MS
    • Mithoefer, A., Mueller, B., Wanner, G. and Eichacker, L.A. (2002) Identification of defence-related cell wall proteins in Phytophthora sojae-infected soybean roots by ESI-MS/MS. Mol. Plant Pathol., 3, 163-166.
    • (2002) Mol. Plant Pathol. , vol.3 , pp. 163-166
    • Mithoefer, A.1    Mueller, B.2    Wanner, G.3    Eichacker, L.A.4
  • 68
    • 0031711073 scopus 로고    scopus 로고
    • Mass spectrometry and EST-database searching allows characterization of the multi-protein spliceosome complex
    • Neubauer, G., King, A., Rappsilber, J., Calvio, C., Watson, M., Ajuh, P., Sleeman, J., Lamond, A. and Mann, M. (1998) Mass spectrometry and EST-database searching allows characterization of the multi-protein spliceosome complex. Nat. Genet., 20, 46-50.
    • (1998) Nat. Genet. , vol.20 , pp. 46-50
    • Neubauer, G.1    King, A.2    Rappsilber, J.3    Calvio, C.4    Watson, M.5    Ajuh, P.6    Sleeman, J.7    Lamond, A.8    Mann, M.9
  • 69
    • 0023931883 scopus 로고
    • Improved staining of proteins in polyacrylamide gels including isoelectric focusing gels with clear background at nanogram sensitivity using Coomassie Brilliant Blue G-250 and R-250
    • Neuhoff, V., Arold, N., Taube, D. and Ehrhardt, W. (1988) Improved staining of proteins in polyacrylamide gels including isoelectric focusing gels with clear background at nanogram sensitivity using Coomassie Brilliant Blue G-250 and R-250. Electrophoresis, 9, 255-262.
    • (1988) Electrophoresis , vol.9 , pp. 255-262
    • Neuhoff, V.1    Arold, N.2    Taube, D.3    Ehrhardt, W.4
  • 70
    • 3242755176 scopus 로고    scopus 로고
    • Plant proteome analysis by mass spectrometry:principles, problems, pitfalls and recent developments
    • Newton, R.P., Brenton, A.G., Smith, C.J. and Dudley, E. (2004) Plant proteome analysis by mass spectrometry:principles, problems, pitfalls and recent developments. Phytochemistry, 65, 1449-1485.
    • (2004) Phytochemistry , vol.65 , pp. 1449-1485
    • Newton, R.P.1    Brenton, A.G.2    Smith, C.J.3    Dudley, E.4
  • 71
    • 0033535961 scopus 로고    scopus 로고
    • Accurate quantitation of protein expression and site-specific phosphorylation
    • Oda, Y., Huang, K., Cross, F.R., Cowburn, D. and Chait, B.T. (1999) Accurate quantitation of protein expression and site-specific phosphorylation. Proc. Natl Acad. Sci. USA, 96, 6591-6596.
    • (1999) Proc. Natl Acad. Sci. USA , vol.96 , pp. 6591-6596
    • Oda, Y.1    Huang, K.2    Cross, F.R.3    Cowburn, D.4    Chait, B.T.5
  • 72
    • 0016711037 scopus 로고
    • High resolution two-dimensional electrophoresis of proteins
    • O'Farrell, P.H. (1975) High resolution two-dimensional electrophoresis of proteins. J. Biol. Chem., 250, 4007-4021.
    • (1975) J. Biol. Chem. , vol.250 , pp. 4007-4021
    • O'Farrell, P.H.1
  • 74
    • 0035987498 scopus 로고    scopus 로고
    • Initial proteome analysis of mature barley seeds and malt
    • Østergaard, O., Melchior, S., Roepstorff, P. and Svensson, B. (2002) Initial proteome analysis of mature barley seeds and malt. Proteomics, 2, 733-739.
    • (2002) Proteomics , vol.2 , pp. 733-739
    • Østergaard, O.1    Melchior, S.2    Roepstorff, P.3    Svensson, B.4
  • 75
    • 4544347338 scopus 로고    scopus 로고
    • How much of the proteome do we see with discovery-based proteomics methods and how much do we need to see?
    • Patterson, S.D. (2004) How much of the proteome do we see with discovery-based proteomics methods and how much do we need to see? Curr. Proteom., 1, 3-12.
    • (2004) Curr. Proteom. , vol.1 , pp. 3-12
    • Patterson, S.D.1
  • 76
    • 0030028209 scopus 로고    scopus 로고
    • Application of combined mass spectrometry and partial amino acid sequence to the identification of gel-separated proteins
    • Patterson, S.D., Thomas, D. and Bradshaw, R.A. (1996) Application of combined mass spectrometry and partial amino acid sequence to the identification of gel-separated proteins. Electrophoresis, 17, 877-891.
    • (1996) Electrophoresis , vol.17 , pp. 877-891
    • Patterson, S.D.1    Thomas, D.2    Bradshaw, R.A.3
  • 77
    • 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. and Boller, T. (2001) Directed proteomics identifies a plant-specific protein rapidly phosphorylated in response to bacterial and fungal elicitors. Plant Cell, 13, 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
  • 80
    • 0020997304 scopus 로고
    • The use of a zwitterionic detergent in twodimensional gel electrophoresis of trout liver microsomes
    • Perdew, G.H., Schaup, H.W. and Selivonchick, D.P. (1983) The use of a zwitterionic detergent in twodimensional gel electrophoresis of trout liver microsomes. Anal. Biochem., 135, 453-455.
    • (1983) Anal. Biochem. , vol.135 , pp. 453-455
    • Perdew, G.H.1    Schaup, H.W.2    Selivonchick, D.P.3
  • 81
    • 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. and Cottrell, J.S. (1999) Probability-based protein identification by searching sequence databases using mass spectrometry data. Electrophoresis, 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
  • 82
    • 1842830433 scopus 로고    scopus 로고
    • Cutler, P. (ed.), Humana Press Inc., Totowa, NJ
    • Pierpoint, W.S. (2004) In: Cutler, P. (ed.) Methods in Molecular Biology, Vol. 244. Humana Press Inc., Totowa, NJ, pp. 65-74.
    • (2004) Methods in Molecular Biology , vol.244 , pp. 65-74
    • Pierpoint, W.S.1
  • 86
    • 0031807109 scopus 로고    scopus 로고
    • Use of thiourea to increase the solubility of membrane proteins in two-dimensional electrophoresis
    • Rabilloud, T. (1998) Use of thiourea to increase the solubility of membrane proteins in two-dimensional electrophoresis. Electrophoresis, 19, 758-760.
    • (1998) Electrophoresis , vol.19 , pp. 758-760
    • Rabilloud, T.1
  • 87
    • 0036208433 scopus 로고    scopus 로고
    • Two-dimensional gel electrophoresis in proteomics: old, old fashioned, but it still climbs up the mountains
    • Rabilloud, T. (2002) Two-dimensional gel electrophoresis in proteomics: old, old fashioned, but it still climbs up the mountains. Proteomics, 2, 3-10.
    • (2002) Proteomics , vol.2 , pp. 3-10
    • Rabilloud, T.1
  • 88
    • 0030957650 scopus 로고    scopus 로고
    • Improvement of the solubilization of proteins in two-dimensional electrophoresis with immobilized pH gradients
    • Rabilloud, T., Adessi, C., Giraudel, A. and Lunardi, J. (1997) Improvement of the solubilization of proteins in two-dimensional electrophoresis with immobilized pH gradients. Electrophoresis, 18, 307-316.
    • (1997) Electrophoresis , vol.18 , pp. 307-316
    • Rabilloud, T.1    Adessi, C.2    Giraudel, A.3    Lunardi, J.4
  • 89
    • 0036470450 scopus 로고    scopus 로고
    • What does it mean to identify a protein in proteomics?
    • Rappsilber, J. and Mann, M. (2002) What does it mean to identify a protein in proteomics? Trends. Biochem. Sci., 27, 74-78.
    • (2002) Trends. Biochem. Sci. , vol.27 , pp. 74-78
    • Rappsilber, J.1    Mann, M.2
  • 90
    • 4544265213 scopus 로고    scopus 로고
    • Tackling the plant proteome:practical approaches, hurdles and experimental tools
    • Rose, J.K., Bashir, S., Giovannoni, J.J., Jahn, M.M. and Saravanan, R.S. (2004) Tackling the plant proteome:practical approaches, hurdles and experimental tools. Plant J., 39, 715-733.
    • (2004) Plant J. , vol.39 , pp. 715-733
    • Rose, J.K.1    Bashir, S.2    Giovannoni, J.J.3    Jahn, M.M.4    Saravanan, R.S.5
  • 91
  • 93
    • 0035356739 scopus 로고    scopus 로고
    • Proteolysis in mixed organic-aqueous solvent systems:applications for peptide mass mapping using mass spectrometry
    • Russell, W.K., Park, Z.Y. and Russell, D.H. (2001) Proteolysis in mixed organic-aqueous solvent systems:applications for peptide mass mapping using mass spectrometry. Anal. Chem., 73, 2682-2685.
    • (2001) Anal. Chem. , vol.73 , pp. 2682-2685
    • Russell, W.K.1    Park, Z.Y.2    Russell, D.H.3
  • 96
    • 0033778077 scopus 로고    scopus 로고
    • Membrane proteomics: use of additive main effects with multiplicative interaction model to classify plasma membrane proteins according to their solubility and electrophoretic properties
    • Santoni, V., Kieffer, S., Desclaux, D., Masson, F. and Rabilloud, T. (2000) Membrane proteomics: use of additive main effects with multiplicative interaction model to classify plasma membrane proteins according to their solubility and electrophoretic properties. Electrophoresis, 21, 3329-3344.
    • (2000) Electrophoresis , vol.21 , pp. 3329-3344
    • Santoni, V.1    Kieffer, S.2    Desclaux, D.3    Masson, F.4    Rabilloud, T.5
  • 97
    • 0026409298 scopus 로고
    • Blue native electrophoresis for isolation of membrane protein complexes in enzymatically active form
    • Schägger, H. and von Jagow, G. (1991) Blue native electrophoresis for isolation of membrane protein complexes in enzymatically active form. Anal. Biochem., 199, 223-231.
    • (1991) Anal. Biochem. , vol.199 , pp. 223-231
    • Schägger, H.1    von Jagow, G.2
  • 100
    • 0029927505 scopus 로고    scopus 로고
    • Mass spectrometric sequencing of proteins silver-stained polyacrylamide gels
    • Shevchenko, A., Wilm, M., Vorm, O. and Mann, M. (1996b) Mass spectrometric sequencing of proteins silver-stained polyacrylamide gels. Anal. Chem., 68, 850-858.
    • (1996) Anal. Chem. , vol.68 , pp. 850-858
    • Shevchenko, A.1    Wilm, M.2    Vorm, O.3    Mann, M.4
  • 102
    • 0024186788 scopus 로고
    • Fingerprinting of proteins cleaved in solution by cyanogen bromide
    • Skopp, R.N. and Lane, L.C. (1989) Fingerprinting of proteins cleaved in solution by cyanogen bromide. Appl. Theor. Electrophor., 1, 61-64.
    • (1989) Appl. Theor. Electrophor. , vol.1 , pp. 61-64
    • Skopp, R.N.1    Lane, L.C.2
  • 103
    • 0030218803 scopus 로고    scopus 로고
    • SYPRO orange and SYPRO red protein gel stains: one-step fluorescent staining of denaturing gels for detection of nanogram levels of protein
    • Steinberg, T.H., Jones, L.J., Haugland, R.P. and Singer, V.L. (1996) SYPRO orange and SYPRO red protein gel stains: one-step fluorescent staining of denaturing gels for detection of nanogram levels of protein. Anal. Biochem., 239, 223-237.
    • (1996) Anal. Biochem. , vol.239 , pp. 223-237
    • Steinberg, T.H.1    Jones, L.J.2    Haugland, R.P.3    Singer, V.L.4
  • 104
    • 1242294379 scopus 로고    scopus 로고
    • Large-scale characterization of integral proteins from Arabidopsis vacuolar membrane by two-dimensional liquid chromatography
    • Szponarski, W., Sommerer, N., Boyer, J.C., Rossignol, M. and Gibrat, R. (2004) Large-scale characterization of integral proteins from Arabidopsis vacuolar membrane by two-dimensional liquid chromatography. Proteomics, 4, 397-406.
    • (2004) Proteomics , vol.4 , pp. 397-406
    • Szponarski, W.1    Sommerer, N.2    Boyer, J.C.3    Rossignol, M.4    Gibrat, R.5
  • 106
    • 23944457745 scopus 로고    scopus 로고
    • Identification and functional analysis of in vivo phosphorylation sites of the Arabidopsis BRASSINOSTEROID-INSENSITIVE1 receptor kinase
    • Wang, X., Goshe, M.B., Soderblom, E.J., Phinney, B.S., Kuchar, J.A., Li, J., Asami, T., Yoshida, S., Huber, S.C. and Clouse, S.D. (2005) Identification and functional analysis of in vivo phosphorylation sites of the Arabidopsis BRASSINOSTEROID-INSENSITIVE1 receptor kinase. Plant Cell, 17, 1685-1703.
    • (2005) Plant Cell , vol.17 , pp. 1685-1703
    • Wang, X.1    Goshe, M.B.2    Soderblom, E.J.3    Phinney, B.S.4    Kuchar, J.A.5    Li, J.6    Asami, T.7    Yoshida, S.8    Huber, S.C.9    Clouse, S.D.10
  • 107
    • 0035106351 scopus 로고    scopus 로고
    • Large-scale analysis of the yeast proteome by multidimensional protein identification technology
    • Washburn, M.P., Wolters, D. and Yates III, J.R. (2001) Large-scale analysis of the yeast proteome by multidimensional protein identification technology. Nat. Biotechnol., 19, 242-247.
    • (2001) Nat. Biotechnol. , vol.19 , pp. 242-247
    • Washburn, M.P.1    Wolters, D.2    Yates, J.R.3
  • 108
    • 0031776931 scopus 로고    scopus 로고
    • Electrospray-ionization mass spectrometry of intact intrinsic membrane proteins
    • Whitelegge, J.P., Gundersen, C.B. and Faull, K.F. (1998) Electrospray-ionization mass spectrometry of intact intrinsic membrane proteins. Protein Sci., 7, 1423-1430.
    • (1998) Protein Sci. , vol.7 , pp. 1423-1430
    • Whitelegge, J.P.1    Gundersen, C.B.2    Faull, K.F.3
  • 110
    • 0035582244 scopus 로고    scopus 로고
    • An automated multidimensional protein identification technology for shotgun proteomics
    • Wolters, D.A., Washburn, M.P. and Yates III, J.R. (2001) An automated multidimensional protein identification technology for shotgun proteomics. Anal. Chem., 73, 5683-5690.
    • (2001) Anal. Chem. , vol.73 , pp. 5683-5690
    • Wolters, D.A.1    Washburn, M.P.2    Yates, J.R.3
  • 111
    • 0037337308 scopus 로고    scopus 로고
    • The application of mass spectrometry to membrane proteomics
    • Wu, C.C. and Yates III, J.R. (2003) The application of mass spectrometry to membrane proteomics. Nat. Biotechnol., 21, 262-267.
    • (2003) Nat. Biotechnol. , vol.21 , pp. 262-267
    • Wu, C.C.1    Yates, J.R.2
  • 112
    • 0036907867 scopus 로고    scopus 로고
    • Fluorescence 2-D difference gel electrophoresis and mass spectrometry based proteomic analysis of Escherichia coli
    • Yan, J.X., Devenish, A.T., Wait, R., Stone, T., Lewis, S. and Fowler, S. (2002) Fluorescence 2-D difference gel electrophoresis and mass spectrometry based proteomic analysis of Escherichia coli. Proteomics, 2, 1682-1698.
    • (2002) Proteomics , vol.2 , pp. 1682-1698
    • Yan, J.X.1    Devenish, A.T.2    Wait, R.3    Stone, T.4    Lewis, S.5    Fowler, S.6
  • 113
    • 0031814022 scopus 로고    scopus 로고
    • Database searching using mass spectrometry data
    • Yates III, J.R. (1998) Database searching using mass spectrometry data. Electrophoresis, 19, 893-900.
    • (1998) Electrophoresis , vol.19 , pp. 893-900
    • Yates, J.R.1
  • 114
    • 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. and Schieltz, D. (1995) Method to correlate tandem mass spectra of modified peptides to amino acid sequences in the protein database. Anal. Chem., 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
  • 115
    • 2342422227 scopus 로고    scopus 로고
    • GelScape: a web-based server for interactively annotating, manipulating, comparing and archiving 1D and 2D gel images
    • Young, N., Chang, Z. and Wishart, D.S. (2004) GelScape: a web-based server for interactively annotating, manipulating, comparing and archiving 1D and 2D gel images. Bioinformatics, 20, 976-978.
    • (2004) Bioinformatics , vol.20 , pp. 976-978
    • Young, N.1    Chang, Z.2    Wishart, D.S.3
  • 116
    • 18144420373 scopus 로고    scopus 로고
    • Protein pI shifts due to posttranslational modifications in the separation and characterization of proteins
    • Zhu, K., Zhao, J., Lubman, D.M., Miller, F.R. and Barder, T.J. (2005) Protein pI shifts due to posttranslational modifications in the separation and characterization of proteins. Anal. Chem., 77, 2745-2755.
    • (2005) Anal. Chem. , vol.77 , pp. 2745-2755
    • Zhu, K.1    Zhao, J.2    Lubman, D.M.3    Miller, F.R.4    Barder, T.J.5


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.