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Volumn 18, Issue 2, 2010, Pages 59-73

Separation of biological proteins by liquid chromatography

Author keywords

Chirality; Gene; Liquid chromatography; Nano detection; Preparation; Proteomics

Indexed keywords

PROTEOME; SNAKE VENOM;

EID: 77950502931     PISSN: 13190164     EISSN: None     Source Type: Journal    
DOI: 10.1016/j.jsps.2010.02.001     Document Type: Review
Times cited : (23)

References (77)
  • 3
    • 33846620071 scopus 로고    scopus 로고
    • Native proteomic analysis of protein complexes in murine intestinal brush border membranes
    • Babusiak M., Man P., Petrak J., and Vyoral D. Native proteomic analysis of protein complexes in murine intestinal brush border membranes. Proteomics 7 (2007) 121-129
    • (2007) Proteomics , vol.7 , pp. 121-129
    • Babusiak, M.1    Man, P.2    Petrak, J.3    Vyoral, D.4
  • 5
    • 11144334589 scopus 로고    scopus 로고
    • Definition and characterization of a "Trypsinosome" from specific peptide characteristics by nano-HPLC-MS/MS and in silico analysis of complex protein mixtures
    • Bihan T.L., Robinson M.D., Stewart I.I., and Figeys D. Definition and characterization of a "Trypsinosome" from specific peptide characteristics by nano-HPLC-MS/MS and in silico analysis of complex protein mixtures. J. Proteome Res. 3 (2004) 1138-1148
    • (2004) J. Proteome Res. , vol.3 , pp. 1138-1148
    • Bihan, T.L.1    Robinson, M.D.2    Stewart, I.I.3    Figeys, D.4
  • 8
    • 34547144755 scopus 로고    scopus 로고
    • Snake venomics of Bitis species reveals large intragenus venom toxin composition variation: application to taxonomy of congeneric taxa
    • Calvete J.J., Escolano J., and Sanz L. Snake venomics of Bitis species reveals large intragenus venom toxin composition variation: application to taxonomy of congeneric taxa. J. Proteome Res. 6 (2007) 2732-2745
    • (2007) J. Proteome Res. , vol.6 , pp. 2732-2745
    • Calvete, J.J.1    Escolano, J.2    Sanz, L.3
  • 9
    • 30744432140 scopus 로고    scopus 로고
    • Quantitative phosphoproteomic analysis of the tumor necrosis factor pathway
    • Cantin G.T., Venable J.D., Cociorva D., and Yates III J.R. Quantitative phosphoproteomic analysis of the tumor necrosis factor pathway. J. Proteome Res. 5 (2006) 127-134
    • (2006) J. Proteome Res. , vol.5 , pp. 127-134
    • Cantin, G.T.1    Venable, J.D.2    Cociorva, D.3    Yates III, J.R.4
  • 10
    • 0033810757 scopus 로고    scopus 로고
    • Mapping the phosphorylation sites of proteins using on-line immobilized metal affinity chromatography/capillary electrophoresis/electrospray ionization multiple stage tandem mass spectrometry
    • Cao P., and Stults J.T. Mapping the phosphorylation sites of proteins using on-line immobilized metal affinity chromatography/capillary electrophoresis/electrospray ionization multiple stage tandem mass spectrometry. Rapid Commun. Mass Spectrom. 14 (2000) 1600-1606
    • (2000) Rapid Commun. Mass Spectrom. , vol.14 , pp. 1600-1606
    • Cao, P.1    Stults, J.T.2
  • 11
    • 33750970827 scopus 로고    scopus 로고
    • Characterization of the outer membrane protein profile from disease-related Helicobactor pylori isolates by subcellular fractionation and nano-LCFT-ICR MS analysis
    • Carlsohn E., Nystrom J., Karlsson H., Svennerholm A.M., and Nilsson C.L. Characterization of the outer membrane protein profile from disease-related Helicobactor pylori isolates by subcellular fractionation and nano-LCFT-ICR MS analysis. J. Proteome Res. 5 (2006) 3197-3204
    • (2006) J. Proteome Res. , vol.5 , pp. 3197-3204
    • Carlsohn, E.1    Nystrom, J.2    Karlsson, H.3    Svennerholm, A.M.4    Nilsson, C.L.5
  • 12
    • 23044465186 scopus 로고    scopus 로고
    • Identification of human nasal mucous proteins using proteomics
    • Casado B., Pannell L.K., Iadarola P., and Baraniuk J.N. Identification of human nasal mucous proteins using proteomics. Proteomics 5 (2005) 2949-2959
    • (2005) Proteomics , vol.5 , pp. 2949-2959
    • Casado, B.1    Pannell, L.K.2    Iadarola, P.3    Baraniuk, J.N.4
  • 13
    • 17444361957 scopus 로고    scopus 로고
    • Quantitative proteomic analysis of the secretory proteins from rat adipose cells using a-2D liquid chromatography MS/MS approach
    • Chen X., Cushman S.W., Pannel L.K., and Hess S. Quantitative proteomic analysis of the secretory proteins from rat adipose cells using a-2D liquid chromatography MS/MS approach. J. Proteome Res. 4 (2005) 570-577
    • (2005) J. Proteome Res. , vol.4 , pp. 570-577
    • Chen, X.1    Cushman, S.W.2    Pannel, L.K.3    Hess, S.4
  • 17
    • 33645795446 scopus 로고    scopus 로고
    • Modification-specific proteomics of plasma membrane proteins: identification and characterization of glycosylphosphatidylinositol-anchored proteins released upon phospholipase D treatment
    • Elortza F., Mohammed S., Bunkenborg J., Foster L.J., Nuhse T.S., Brodbeck Urs., Peck S.C., and Jensen O.N. Modification-specific proteomics of plasma membrane proteins: identification and characterization of glycosylphosphatidylinositol-anchored proteins released upon phospholipase D treatment. J. Proteome Res. 5 (2006) 935-943
    • (2006) J. Proteome Res. , vol.5 , pp. 935-943
    • Elortza, F.1    Mohammed, S.2    Bunkenborg, J.3    Foster, L.J.4    Nuhse, T.S.5    Brodbeck, Urs.6    Peck, S.C.7    Jensen, O.N.8
  • 18
    • 10644242580 scopus 로고    scopus 로고
    • Characterization of the in vivo forms of lacrimal-specific proline-rich proteins in human tear fluid
    • Fung K.Y., Morris C., Sathe S., Sack R., and Duncan M.W. Characterization of the in vivo forms of lacrimal-specific proline-rich proteins in human tear fluid. Proteomics 4 (2004) 3953-3959
    • (2004) Proteomics , vol.4 , pp. 3953-3959
    • Fung, K.Y.1    Morris, C.2    Sathe, S.3    Sack, R.4    Duncan, M.W.5
  • 19
    • 33646077891 scopus 로고    scopus 로고
    • Several glutathione S-transferase isozymes that protect against oxidative injury are expressed in human liver mitochondria
    • Gallagher E.P., Gardner J.L., and Barber D.S. Several glutathione S-transferase isozymes that protect against oxidative injury are expressed in human liver mitochondria. Biochem. Pharmacol. 71 (2006) 1619-1628
    • (2006) Biochem. Pharmacol. , vol.71 , pp. 1619-1628
    • Gallagher, E.P.1    Gardner, J.L.2    Barber, D.S.3
  • 23
    • 33644896212 scopus 로고    scopus 로고
    • The role of mass spectrometry in plant systems biology
    • Glinski M., and Weckwerth W. The role of mass spectrometry in plant systems biology. Mass Spectrom. Rev. 25 (2006) 173-214
    • (2006) Mass Spectrom. Rev. , vol.25 , pp. 173-214
    • Glinski, M.1    Weckwerth, W.2
  • 24
    • 34948851348 scopus 로고    scopus 로고
    • An automated platform for analysis of phosphoproteomic datasets: application to kidney collecting duct phosphoproteins
    • Hoffert J.D., Wang G., Pisitkun T., Shen R.F., and Knepper M.A. An automated platform for analysis of phosphoproteomic datasets: application to kidney collecting duct phosphoproteins. J. Proteome Res. 6 (2007) 3501-3508
    • (2007) J. Proteome Res. , vol.6 , pp. 3501-3508
    • Hoffert, J.D.1    Wang, G.2    Pisitkun, T.3    Shen, R.F.4    Knepper, M.A.5
  • 26
    • 25144489182 scopus 로고    scopus 로고
    • Discovering neuropeptides in Caenorhabditis elegans by two dimensional liquid chromatography and mass spectrometry
    • Husson S.J., Clynen E., Baggerman G., De Loof A., and Schoofs L. Discovering neuropeptides in Caenorhabditis elegans by two dimensional liquid chromatography and mass spectrometry. Biochem. Biophys. Res. Commun. 335 (2005) 76-86
    • (2005) Biochem. Biophys. Res. Commun. , vol.335 , pp. 76-86
    • Husson, S.J.1    Clynen, E.2    Baggerman, G.3    De Loof, A.4    Schoofs, L.5
  • 27
    • 33748036746 scopus 로고    scopus 로고
    • Defective processing of neuropeptide precursors in Caenorhabditis elegans lacking proprotein convertase 2 (KPC-2/EGL-3): mutant analysis by mass spectrometry
    • Husson S.J., Clynen E., Baggerman G., Janssen T., and Schoofs L. Defective processing of neuropeptide precursors in Caenorhabditis elegans lacking proprotein convertase 2 (KPC-2/EGL-3): mutant analysis by mass spectrometry. J. Neurochem. 98 (2006) 1999-2012
    • (2006) J. Neurochem. , vol.98 , pp. 1999-2012
    • Husson, S.J.1    Clynen, E.2    Baggerman, G.3    Janssen, T.4    Schoofs, L.5
  • 28
    • 21844464043 scopus 로고    scopus 로고
    • Protein fishing with chiral molecular baits
    • Kawamura A., and Hindi S. Protein fishing with chiral molecular baits. Chirality 17 (2005) 332-337
    • (2005) Chirality , vol.17 , pp. 332-337
    • Kawamura, A.1    Hindi, S.2
  • 29
    • 0345791524 scopus 로고    scopus 로고
    • Proteomic analysis of rat liver peroxisome: presence of peroxisome-specific isozyme of Lon protease
    • Kikuchi M., Hatano N., Yokota S., Shimozawa N., Imanaka T., and Taniguchi H. Proteomic analysis of rat liver peroxisome: presence of peroxisome-specific isozyme of Lon protease. J. Biol. Chem. 279 (2004) 421-428
    • (2004) J. Biol. Chem. , vol.279 , pp. 421-428
    • Kikuchi, M.1    Hatano, N.2    Yokota, S.3    Shimozawa, N.4    Imanaka, T.5    Taniguchi, H.6
  • 33
    • 33750140109 scopus 로고    scopus 로고
    • Quantification of membrane and membrane-bound proteins in normal and malignant breast cancer cells isolated from the same patient with primary breast carcinoma
    • Liang X., Zhao J., Hajivandi M., Wu R., Tao J., Amshey J.W., and Pope R.M. Quantification of membrane and membrane-bound proteins in normal and malignant breast cancer cells isolated from the same patient with primary breast carcinoma. J. Proteome Res. 5 (2006) 2632-2641
    • (2006) J. Proteome Res. , vol.5 , pp. 2632-2641
    • Liang, X.1    Zhao, J.2    Hajivandi, M.3    Wu, R.4    Tao, J.5    Amshey, J.W.6    Pope, R.M.7
  • 35
    • 0012573999 scopus 로고    scopus 로고
    • Multidimensional peptide separations in proteomics
    • Link A.J. Multidimensional peptide separations in proteomics. Trends Biotechnol. 20 (2002) S8-S13
    • (2002) Trends Biotechnol. , vol.20
    • Link, A.J.1
  • 37
    • 0034329604 scopus 로고    scopus 로고
    • Separation and detection of intact noncovalent protein complexes from mixtures by on-line capillary isoelectric focusing-mass spectrometry
    • Martinovic S., Berger S.J., Pasa-Tolic L., and Smith R.D. Separation and detection of intact noncovalent protein complexes from mixtures by on-line capillary isoelectric focusing-mass spectrometry. Anal. Chem. 72 (2000) 5356-5360
    • (2000) Anal. Chem. , vol.72 , pp. 5356-5360
    • Martinovic, S.1    Berger, S.J.2    Pasa-Tolic, L.3    Smith, R.D.4
  • 39
    • 3543035767 scopus 로고    scopus 로고
    • Comprehensive proteomic analysis of interphase and mitotic 14-3-3-binding proteins
    • Meek S.E., Lane W.S., and Piwnica-Worms H.J. Comprehensive proteomic analysis of interphase and mitotic 14-3-3-binding proteins. Biol. Chem. 279 (2004) 32046-32054
    • (2004) Biol. Chem. , vol.279 , pp. 32046-32054
    • Meek, S.E.1    Lane, W.S.2    Piwnica-Worms, H.J.3
  • 40
    • 2442471739 scopus 로고    scopus 로고
    • Differential phosphoproteome profiling by affinity capture and tandem matrix-assisted laser desorption/ionization mass spectrometry
    • Metodiev M.V., Timanova A., and Stone D.E. Differential phosphoproteome profiling by affinity capture and tandem matrix-assisted laser desorption/ionization mass spectrometry. Proteomics 4 (2004) 1433-1438
    • (2004) Proteomics , vol.4 , pp. 1433-1438
    • Metodiev, M.V.1    Timanova, A.2    Stone, D.E.3
  • 42
    • 17644385255 scopus 로고    scopus 로고
    • Monitoring food quality by microfluidic electrophoresis, gas chromatography, and mass spectrometry techniques: effects of aquaculture on the sea bass (Dicentrarchus labrax)
    • Monti G., Napoli L.D., Mainolfi P., Barone R., Guida M., Marino G., and Amoresano A. Monitoring food quality by microfluidic electrophoresis, gas chromatography, and mass spectrometry techniques: effects of aquaculture on the sea bass (Dicentrarchus labrax). Anal. Chem. 77 (2005) 2587-2594
    • (2005) Anal. Chem. , vol.77 , pp. 2587-2594
    • Monti, G.1    Napoli, L.D.2    Mainolfi, P.3    Barone, R.4    Guida, M.5    Marino, G.6    Amoresano, A.7
  • 43
    • 33745393068 scopus 로고    scopus 로고
    • Liquid chromatography with tandem mass spectrometry-based proteomic discovery in aging and Alzheimer's disease
    • Montine T.J., Woltjer R.L., Pan C., Montine K.S., and Zhang J. Liquid chromatography with tandem mass spectrometry-based proteomic discovery in aging and Alzheimer's disease. Neuro. Rx 3 (2006) 336-343
    • (2006) Neuro. Rx , vol.3 , pp. 336-343
    • Montine, T.J.1    Woltjer, R.L.2    Pan, C.3    Montine, K.S.4    Zhang, J.5
  • 44
    • 0242418236 scopus 로고    scopus 로고
    • Dual electrospray ionization source for confident generation of accurate mass tags using liquid chromatography Fourier transform ion cyclotron resonance mass spectrometry
    • Nepomuceno A.I., Muddiman D.C., Bergen III H.R., Craighead J.R., Burke M.J., Caskey P.E., and Allan J.A. Dual electrospray ionization source for confident generation of accurate mass tags using liquid chromatography Fourier transform ion cyclotron resonance mass spectrometry. Anal. Chem. 75 (2003) 3411-3418
    • (2003) Anal. Chem. , vol.75 , pp. 3411-3418
    • Nepomuceno, A.I.1    Muddiman, D.C.2    Bergen III, H.R.3    Craighead, J.R.4    Burke, M.J.5    Caskey, P.E.6    Allan, J.A.7
  • 45
    • 12344330739 scopus 로고    scopus 로고
    • Role of chromatographic techniques in proteomic analysis
    • Neverova I., and Van Eyk J.E. Role of chromatographic techniques in proteomic analysis. J. Chromatogr. B 815 (2005) 51-63
    • (2005) J. Chromatogr. B , vol.815 , pp. 51-63
    • Neverova, I.1    Van Eyk, J.E.2
  • 47
    • 0032079807 scopus 로고    scopus 로고
    • Comprehensive two-dimensional high-performance liquid chromatography for the isolation of overexpressed proteins and proteome mapping
    • Opiteck G.J., Ramirez S.M., Jorgenson J.W., and Moseley M.A. Comprehensive two-dimensional high-performance liquid chromatography for the isolation of overexpressed proteins and proteome mapping. Anal. Biochem. 258 (1998) 349-361
    • (1998) Anal. Biochem. , vol.258 , pp. 349-361
    • Opiteck, G.J.1    Ramirez, S.M.2    Jorgenson, J.W.3    Moseley, M.A.4
  • 48
    • 33748051433 scopus 로고    scopus 로고
    • The role of prohormone convertase-2 in hypothalamic neuropeptide processing: a quantitative neuropeptidomic study
    • Pan H., Che F.Y., Peng B., Steiner D.F., Pintar J.E., and Fricker L.D. The role of prohormone convertase-2 in hypothalamic neuropeptide processing: a quantitative neuropeptidomic study. J. Neurochem. 98 (2006) 1763-1777
    • (2006) J. Neurochem. , vol.98 , pp. 1763-1777
    • Pan, H.1    Che, F.Y.2    Peng, B.3    Steiner, D.F.4    Pintar, J.E.5    Fricker, L.D.6
  • 49
    • 33751217992 scopus 로고    scopus 로고
    • Evaluation of stationary phases for 2-dimensional HPLC of proteins part 1. Validation of commercial RP-columns
    • Reh E., Hahn B., and Lamotte S. Evaluation of stationary phases for 2-dimensional HPLC of proteins part 1. Validation of commercial RP-columns. J. Chromatogr. B 844 (2006) 204-212
    • (2006) J. Chromatogr. B , vol.844 , pp. 204-212
    • Reh, E.1    Hahn, B.2    Lamotte, S.3
  • 50
    • 33750362923 scopus 로고    scopus 로고
    • Bovine milk fat globule membrane proteome
    • Reinhardt T.A., and Lippolis J.D. Bovine milk fat globule membrane proteome. J. Dairy Res. 73 (2006) 406-416
    • (2006) J. Dairy Res. , vol.73 , pp. 406-416
    • Reinhardt, T.A.1    Lippolis, J.D.2
  • 53
    • 27744473495 scopus 로고    scopus 로고
    • Proteomic identification of the TRAF6 regulation of vacuolar ATPase for osteoclast function
    • Ryu J., Kim H., Lee S.K., Chang E.J., Kim H.J., and Kim H.H. Proteomic identification of the TRAF6 regulation of vacuolar ATPase for osteoclast function. Proteomics 5 (2005) 4152-4160
    • (2005) Proteomics , vol.5 , pp. 4152-4160
    • Ryu, J.1    Kim, H.2    Lee, S.K.3    Chang, E.J.4    Kim, H.J.5    Kim, H.H.6
  • 55
  • 56
    • 34748891107 scopus 로고    scopus 로고
    • Evaluation of two proteomics technologies used to screen the membrane proteomes of wild-type Corynebacterium glutamicum and an l-lysine producing strain
    • Schluesener D., Rogner M., and Poetsch A. Evaluation of two proteomics technologies used to screen the membrane proteomes of wild-type Corynebacterium glutamicum and an l-lysine producing strain. Anal. Bioanal. Chem. 389 (2007) 1055-1064
    • (2007) Anal. Bioanal. Chem. , vol.389 , pp. 1055-1064
    • Schluesener, D.1    Rogner, M.2    Poetsch, A.3
  • 58
    • 33749630783 scopus 로고    scopus 로고
    • An integrated approach to mapping the proteome of the human bone marrow stromal cell
    • Seshi B. An integrated approach to mapping the proteome of the human bone marrow stromal cell. Proteomics 6 (2006) 5169-5182
    • (2006) Proteomics , vol.6 , pp. 5169-5182
    • Seshi, B.1
  • 59
    • 0036749343 scopus 로고    scopus 로고
    • Proteomics based on high-efficiency capillary separations
    • Shen Y., and Smith R.D. Proteomics based on high-efficiency capillary separations. Electrophoresis 23 (2002) 3106-3124
    • (2002) Electrophoresis , vol.23 , pp. 3106-3124
    • Shen, Y.1    Smith, R.D.2
  • 60
    • 0347361594 scopus 로고    scopus 로고
    • Ultrasensitive proteomics using high-efficiency on-line micro-SPE-nano LC-nanoESI MS and MS/MS
    • Shen Y., Tolic N., Masselon C., Pasa-Tolic L., Camp II D.G., Hixson K.K., and Zhao R. Ultrasensitive proteomics using high-efficiency on-line micro-SPE-nano LC-nanoESI MS and MS/MS. Anal. Chem. 76 (2004) 144-154
    • (2004) Anal. Chem. , vol.76 , pp. 144-154
    • Shen, Y.1    Tolic, N.2    Masselon, C.3    Pasa-Tolic, L.4    Camp II, D.G.5    Hixson, K.K.6    Zhao, R.7
  • 62
    • 0344084088 scopus 로고    scopus 로고
    • High-throughput proteomic-based identification of oxidatively induced protein carbonylation in mouse brain
    • Soreghan B.A., Yang F., Thomas S.N., Hsu J., and Yang A. High-throughput proteomic-based identification of oxidatively induced protein carbonylation in mouse brain. J. Pharm. Res. 20 (2003) 1713-1720
    • (2003) J. Pharm. Res. , vol.20 , pp. 1713-1720
    • Soreghan, B.A.1    Yang, F.2    Thomas, S.N.3    Hsu, J.4    Yang, A.5
  • 63
    • 0035258256 scopus 로고    scopus 로고
    • Characterization of phosphoproteins from electrophoretic gels by nanoscale Fe(III) affinity chromatography with off-line mass spectrometry analysis
    • Stensballe A., Andersen S., and Jensen O.N. Characterization of phosphoproteins from electrophoretic gels by nanoscale Fe(III) affinity chromatography with off-line mass spectrometry analysis. Proteomics 1 (2001) 207-222
    • (2001) Proteomics , vol.1 , pp. 207-222
    • Stensballe, A.1    Andersen, S.2    Jensen, O.N.3
  • 64
    • 2642511406 scopus 로고    scopus 로고
    • Proteomic characterization of protein phosphatase complexes of the mammalian nucleus
    • Tran H.T., Ulke A., Morrice N., Johannes C.J., and Moorhead G.B. Proteomic characterization of protein phosphatase complexes of the mammalian nucleus. Mol. Cell Proteomics 3 (2004) 257-265
    • (2004) Mol. Cell Proteomics , vol.3 , pp. 257-265
    • Tran, H.T.1    Ulke, A.2    Morrice, N.3    Johannes, C.J.4    Moorhead, G.B.5
  • 65
    • 33749264369 scopus 로고    scopus 로고
    • Proteomic profiling of human urinary proteome using nano-high performance liquid chromatography/electrospray ionization tandem mass spectrometry
    • Tyan Y.C., Guo H.R., Liu C.Y., and Liao P.C. Proteomic profiling of human urinary proteome using nano-high performance liquid chromatography/electrospray ionization tandem mass spectrometry. Anal. Chem. Acta 579 (2006) 158-176
    • (2006) Anal. Chem. Acta , vol.579 , pp. 158-176
    • Tyan, Y.C.1    Guo, H.R.2    Liu, C.Y.3    Liao, P.C.4
  • 66
    • 29144500411 scopus 로고    scopus 로고
    • Profiling of myelin proteins by 2D-gel electrophoresis and multidimensional liquid chromatography coupled to MALDI-TOF-TOF mass spectrometry
    • Vanrobaeys F., Van Coster R., Dhondt G., Devreese B., and Van Beeumen J. Profiling of myelin proteins by 2D-gel electrophoresis and multidimensional liquid chromatography coupled to MALDI-TOF-TOF mass spectrometry. J. Proteome Res. 4 (2005) 2283-2293
    • (2005) J. Proteome Res. , vol.4 , pp. 2283-2293
    • Vanrobaeys, F.1    Van Coster, R.2    Dhondt, G.3    Devreese, B.4    Van Beeumen, J.5
  • 67
    • 29144505073 scopus 로고    scopus 로고
    • Proteomic analysis of ubiquitinated proteins from human MCF-7 breast cancer cells by immunoaffinity purification and mass spectrometry
    • Vasilescu J., Smith J.C., Ethier M., and Figeys D. Proteomic analysis of ubiquitinated proteins from human MCF-7 breast cancer cells by immunoaffinity purification and mass spectrometry. J. Proteome Res. 4 (2005) 2192-2200
    • (2005) J. Proteome Res. , vol.4 , pp. 2192-2200
    • Vasilescu, J.1    Smith, J.C.2    Ethier, M.3    Figeys, D.4
  • 68
    • 0037084079 scopus 로고    scopus 로고
    • An automated on-line multidimensional HPLC system for protein and peptide mapping with integrated sample preparation
    • Wagner K., Miliotis T., Marko-Varga G., Bischoff R., and Unger K.K. An automated on-line multidimensional HPLC system for protein and peptide mapping with integrated sample preparation. Anal. Chem. 74 (2002) 809-820
    • (2002) Anal. Chem. , vol.74 , pp. 809-820
    • Wagner, K.1    Miliotis, T.2    Marko-Varga, G.3    Bischoff, R.4    Unger, K.K.5
  • 69
    • 17444413879 scopus 로고    scopus 로고
    • Effects of chromatography conditions on intact protein separations for top-down proteomics
    • Wang Y., Balgley B.M., Rudnick P.A., and Lee C.S. Effects of chromatography conditions on intact protein separations for top-down proteomics. J. Chromatogr. A 1073 (2005) 35-41
    • (2005) J. Chromatogr. A , vol.1073 , pp. 35-41
    • Wang, Y.1    Balgley, B.M.2    Rudnick, P.A.3    Lee, C.S.4
  • 71
    • 11144310571 scopus 로고    scopus 로고
    • 2D LC/MS analysis of membrane proteins from breast cancer cell lines MCF7 and BT 474
    • Xiang R., Shi Y., Dillon D.A., Negin B., Horvath C., and Wilkins J.A. 2D LC/MS analysis of membrane proteins from breast cancer cell lines MCF7 and BT 474. J. Proteome Res. 3 (2004) 1278-1283
    • (2004) J. Proteome Res. , vol.3 , pp. 1278-1283
    • Xiang, R.1    Shi, Y.2    Dillon, D.A.3    Negin, B.4    Horvath, C.5    Wilkins, J.A.6
  • 73
    • 14744274048 scopus 로고    scopus 로고
    • Human cerebrospinal fluid peptidomics
    • Yuan X., and Desiderio D.M. Human cerebrospinal fluid peptidomics. J. Mass Spectrom. 40 (2005) 176-181
    • (2005) J. Mass Spectrom. , vol.40 , pp. 176-181
    • Yuan, X.1    Desiderio, D.M.2
  • 75
    • 0038699625 scopus 로고    scopus 로고
    • Identification and quantification of N-linked glycoproteins using hydrazide chemistry, stable isotope labeling and mass spectrometry
    • Zhang H., Li X.J., Martin D.B., and Aebersold R. Identification and quantification of N-linked glycoproteins using hydrazide chemistry, stable isotope labeling and mass spectrometry. Nat. Biotechnol. 21 (2003) 660-666
    • (2003) Nat. Biotechnol. , vol.21 , pp. 660-666
    • Zhang, H.1    Li, X.J.2    Martin, D.B.3    Aebersold, R.4
  • 77
    • 0037249679 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., Timperio A.M., Walcher W., and Huber C.G. Proteomics of light-harvesting proteins in different plant species. Analysis and comparison by liquid chromatography-electrospray ionization mass spectrometry. Plant Physiol. 131 (2003) 198-214
    • (2003) Plant Physiol. , vol.131 , pp. 198-214
    • Zolla, L.1    Timperio, A.M.2    Walcher, W.3    Huber, C.G.4


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