메뉴 건너뛰기




Volumn 7, Issue 1, 2011, Pages 77-93

Quantitative Neuroproteomics: Classical and Novel Tools for Studying Neural Differentiation and Function

Author keywords

2DE (2D PAGE); Isotopic labeling; Label free; LC MS; MALDI TOF; Mass spectrometry; Neural differentiation; Neurodegeneration; Neuroproteomics; Proteomic profiling

Indexed keywords


EID: 78751643723     PISSN: 15508943     EISSN: 15586804     Source Type: Journal    
DOI: 10.1007/s12015-010-9136-3     Document Type: Review
Times cited : (15)

References (127)
  • 1
    • 11244277000 scopus 로고    scopus 로고
    • Expression of disrupted in schizophrenia 1 (DISC1) protein in the adult and developing mouse brain indicates its role in neurodevelopment
    • Schurov, I. L., Handford, E. J., Brandon, N. J., & Whiting, P. J. (2004). Expression of disrupted in schizophrenia 1 (DISC1) protein in the adult and developing mouse brain indicates its role in neurodevelopment. Molecular Psychiatry, 9, 1100-1110.
    • (2004) Molecular Psychiatry , vol.9 , pp. 1100-1110
    • Schurov, I.L.1    Handford, E.J.2    Brandon, N.J.3    Whiting, P.J.4
  • 2
    • 34548624298 scopus 로고    scopus 로고
    • DISC1 puts the brakes on neurogenesis
    • Dranovsky, A., & Hen, R. (2007). DISC1 puts the brakes on neurogenesis. Cell, 130, 981-983.
    • (2007) Cell , vol.130 , pp. 981-983
    • Dranovsky, A.1    Hen, R.2
  • 4
    • 0242407441 scopus 로고    scopus 로고
    • Altered midbrain dopaminergic neurotransmission during development in an animal model of ADHD
    • Leo, D., Sorrentino, E., Volpicelli, F., et al. (2003). Altered midbrain dopaminergic neurotransmission during development in an animal model of ADHD. Neuroscience and Biobehavioral Reviews, 27, 661-669.
    • (2003) Neuroscience and Biobehavioral Reviews , vol.27 , pp. 661-669
    • Leo, D.1    Sorrentino, E.2    Volpicelli, F.3
  • 5
    • 65349181826 scopus 로고    scopus 로고
    • A fragile balance: Perturbation of GABA mediated circuit in prefrontal cortex generates high intraindividual performance variability
    • Pouget, P., Wattiez, N., Rivaud-Pechoux, S., & Gaymard, B. (2009). A fragile balance: Perturbation of GABA mediated circuit in prefrontal cortex generates high intraindividual performance variability. PLoS ONE, 4, e5208.
    • (2009) PLoS ONE , vol.4
    • Pouget, P.1    Wattiez, N.2    Rivaud-Pechoux, S.3    Gaymard, B.4
  • 6
    • 0348143168 scopus 로고    scopus 로고
    • An inhibition of cyclin-dependent kinases that lengthens, but does not arrest, neuroepithelial cell cycle induces premature neurogenesis
    • Calegari, F., & Huttner, W. B. (2003). An inhibition of cyclin-dependent kinases that lengthens, but does not arrest, neuroepithelial cell cycle induces premature neurogenesis. Journal of Cell Science, 116, 4947-4955.
    • (2003) Journal of Cell Science , vol.116 , pp. 4947-4955
    • Calegari, F.1    Huttner, W.B.2
  • 7
    • 68749118423 scopus 로고    scopus 로고
    • Neural cell cycle dysregulation and central nervous system diseases
    • Wang, W., Bu, B., Xie, M., Zhang, M., Yu, Z., & Tao, D. (2009). Neural cell cycle dysregulation and central nervous system diseases. Progress in Neurobiology, 89, 1-17.
    • (2009) Progress in Neurobiology , vol.89 , pp. 1-17
    • Wang, W.1    Bu, B.2    Xie, M.3    Zhang, M.4    Yu, Z.5    Tao, D.6
  • 9
    • 0034927081 scopus 로고    scopus 로고
    • Neurotrophins: Roles in neuronal development and function
    • Huang, E. J., & Reichardt, L. F. (2001). Neurotrophins: Roles in neuronal development and function. Annual Review of Neuroscience, 24, 677-736.
    • (2001) Annual Review of Neuroscience , vol.24 , pp. 677-736
    • Huang, E.J.1    Reichardt, L.F.2
  • 13
    • 0038392462 scopus 로고    scopus 로고
    • Gene expression profiling of ciliary neurotrophic factor-overexpressing rat striatal progenitor cells (ST14A) indicates improved stress response during the early stage of differentiation
    • Bottcher, T., Mix, E., Koczan, D., et al. (2003). Gene expression profiling of ciliary neurotrophic factor-overexpressing rat striatal progenitor cells (ST14A) indicates improved stress response during the early stage of differentiation. Journal of Neuroscience Research, 73, 42-53.
    • (2003) Journal of Neuroscience Research , vol.73 , pp. 42-53
    • Bottcher, T.1    Mix, E.2    Koczan, D.3
  • 14
    • 33846241742 scopus 로고    scopus 로고
    • Dynamic changes of gangliosides expression during the differentiation of embryonic and mesenchymal stem cells into neural cells
    • Kwak, D. H., Yu, K., Kim, S. M., et al. (2006). Dynamic changes of gangliosides expression during the differentiation of embryonic and mesenchymal stem cells into neural cells. Experimental and Molecular Medicine, 38, 668-676.
    • (2006) Experimental and Molecular Medicine , vol.38 , pp. 668-676
    • Kwak, D.H.1    Yu, K.2    Kim, S.M.3
  • 16
    • 33745938737 scopus 로고    scopus 로고
    • Neuroproteomics- - the tasks lying ahead
    • Becker, M., Schindler, J., & Nothwang, H. G. (2006). Neuroproteomics- - the tasks lying ahead. Electrophoresis, 27, 2819-2829.
    • (2006) Electrophoresis , vol.27 , pp. 2819-2829
    • Becker, M.1    Schindler, J.2    Nothwang, H.G.3
  • 19
    • 34548612001 scopus 로고    scopus 로고
    • Neuroproteomics comes of age
    • Butcher, J. (2007). Neuroproteomics comes of age. Lancet Neurology, 6, 850-851.
    • (2007) Lancet Neurology , vol.6 , pp. 850-851
    • Butcher, J.1
  • 21
    • 3142696823 scopus 로고    scopus 로고
    • Comprehensive proteome expression profiling of undifferentiated versus differentiated neural stem cells from adult rat hippocampus
    • Maurer, M. H., Feldmann, R. E., Jr., Futterer, C. D., Butlin, J., & Kuschinsky, W. (2004). Comprehensive proteome expression profiling of undifferentiated versus differentiated neural stem cells from adult rat hippocampus. Neurochemical Research, 29, 1129-1144.
    • (2004) Neurochemical Research , vol.29 , pp. 1129-1144
    • Maurer, M.H.1    Feldmann Jr., R.E.2    Futterer, C.D.3    Butlin, J.4    Kuschinsky, W.5
  • 22
    • 0141680593 scopus 로고    scopus 로고
    • Proteome analysis of conditioned medium from cultured adult hippocampal progenitors
    • Dahl, A., Eriksson, P. S., Persson, A. I., et al. (2003). Proteome analysis of conditioned medium from cultured adult hippocampal progenitors. Rapid Communications in Mass Spectrometry, 17, 2195-2202.
    • (2003) Rapid Communications in Mass Spectrometry , vol.17 , pp. 2195-2202
    • Dahl, A.1    Eriksson, P.S.2    Persson, A.I.3
  • 23
    • 2642558839 scopus 로고    scopus 로고
    • Aldehyde suppression of copepod recruitment in blooms of a ubiquitous planktonic diatom
    • Ianora, A., Miralto, A., Poulet, S. A., et al. (2004). Aldehyde suppression of copepod recruitment in blooms of a ubiquitous planktonic diatom. Nature, 429, 403-407.
    • (2004) Nature , vol.429 , pp. 403-407
    • Ianora, A.1    Miralto, A.2    Poulet, S.A.3
  • 24
    • 33947331255 scopus 로고    scopus 로고
    • FLUOXETINE modifies the expression of serotonergic markers in a differentiation-dependent fashion in the mesencephalic neural cell line A1 mes c-myc
    • Di Lieto, A., Leo, D., Volpicelli, F., di Porzio, U., & Colucci-D'Amato, L. (2007). FLUOXETINE modifies the expression of serotonergic markers in a differentiation-dependent fashion in the mesencephalic neural cell line A1 mes c-myc. Brain Research, 1143, 1-10.
    • (2007) Brain Research , vol.1143 , pp. 1-10
    • Di Lieto, A.1    Leo, D.2    Volpicelli, F.3    di Porzio, U.4    Colucci-D'Amato, L.5
  • 27
    • 33645471321 scopus 로고    scopus 로고
    • 2-DE proteome analysis of a proliferating and differentiating human neuronal stem cell line (ReNcell VM)
    • Hoffrogge, R., Mikkat, S., Scharf, C., et al. (2006). 2-DE proteome analysis of a proliferating and differentiating human neuronal stem cell line (ReNcell VM). Proteomics, 6, 1833-1847.
    • (2006) Proteomics , vol.6 , pp. 1833-1847
    • Hoffrogge, R.1    Mikkat, S.2    Scharf, C.3
  • 28
    • 33846636777 scopus 로고    scopus 로고
    • 2-DE profiling of GDNF overexpression-related proteome changes in differentiating ST14A rat progenitor cells
    • Hoffrogge, R., Beyer, S., Hubner, R., et al. (2007). 2-DE profiling of GDNF overexpression-related proteome changes in differentiating ST14A rat progenitor cells. Proteomics, 7, 33-46.
    • (2007) Proteomics , vol.7 , pp. 33-46
    • Hoffrogge, R.1    Beyer, S.2    Hubner, R.3
  • 29
    • 17844398765 scopus 로고    scopus 로고
    • Differential display of proteins involved in the neural differentiation of mouse embryonic carcinoma P19 cells by comparative proteomic analysis
    • An, J., Yuan, Q., Wang, C., et al. (2005). Differential display of proteins involved in the neural differentiation of mouse embryonic carcinoma P19 cells by comparative proteomic analysis. Proteomics, 5, 1656-1668.
    • (2005) Proteomics , vol.5 , pp. 1656-1668
    • An, J.1    Yuan, Q.2    Wang, C.3
  • 30
    • 33947728056 scopus 로고    scopus 로고
    • Cellular processes underlying maturation of P19 neurons: Changes in protein folding regimen and cytoskeleton organization
    • Inberg, A., Bogoch, Y., Bledi, Y., & Linial, M. (2007). Cellular processes underlying maturation of P19 neurons: Changes in protein folding regimen and cytoskeleton organization. Proteomics, 7, 910-920.
    • (2007) Proteomics , vol.7 , pp. 910-920
    • Inberg, A.1    Bogoch, Y.2    Bledi, Y.3    Linial, M.4
  • 31
    • 60849125760 scopus 로고    scopus 로고
    • Proteomic profiling of proliferating and differentiated neural mes-c-myc A1 cell line from mouse embryonic mesencephalon by LC-MS
    • Chambery, A., Colucci-D'Amato, L., Vissers, J. P., Scarpella, S., Langridge, J. I., & Parente, A. (2009). Proteomic profiling of proliferating and differentiated neural mes-c-myc A1 cell line from mouse embryonic mesencephalon by LC-MS. Journal of Proteome Research, 8, 227-238.
    • (2009) Journal of Proteome Research , vol.8 , pp. 227-238
    • Chambery, A.1    Colucci-D'Amato, L.2    Vissers, J.P.3    Scarpella, S.4    Langridge, J.I.5    Parente, A.6
  • 33
    • 38649096595 scopus 로고    scopus 로고
    • A quantitative proteomic analysis of mitochondrial participation in p19 cell neuronal differentiation
    • Watkins, J., Basu, S., & Bogenhagen, D. F. (2008). A quantitative proteomic analysis of mitochondrial participation in p19 cell neuronal differentiation. Journal of Proteome Research, 7, 328-338.
    • (2008) Journal of Proteome Research , vol.7 , pp. 328-338
    • Watkins, J.1    Basu, S.2    Bogenhagen, D.F.3
  • 35
    • 42549125986 scopus 로고    scopus 로고
    • Subcellular proteomics in neuroscience
    • Li, K. W., & Smit, A. B. (2008). Subcellular proteomics in neuroscience. Frontiers in Bioscience, 13, 4416-4425.
    • (2008) Frontiers in Bioscience , vol.13 , pp. 4416-4425
    • Li, K.W.1    Smit, A.B.2
  • 37
    • 5644302164 scopus 로고    scopus 로고
    • The synaptic vesicle proteome: A comparative study in membrane protein identification
    • Coughenour, H. D., Spaulding, R. S., & Thompson, C. M. (2004). The synaptic vesicle proteome: A comparative study in membrane protein identification. Proteomics, 4, 3141-3155.
    • (2004) Proteomics , vol.4 , pp. 3141-3155
    • Coughenour, H.D.1    Spaulding, R.S.2    Thompson, C.M.3
  • 39
    • 0020955120 scopus 로고
    • Synapsin I (protein I), a nerve terminal-specific phosphoprotein. III. Its association with synaptic vesicles studied in a highly purified synaptic vesicle preparation
    • Huttner, W. B., Schiebler, W., Greengard, P., & De Camilli, P. (1983). Synapsin I (protein I), a nerve terminal-specific phosphoprotein. III. Its association with synaptic vesicles studied in a highly purified synaptic vesicle preparation. Journal of Cell Biology, 96, 1374-1388.
    • (1983) Journal of Cell Biology , vol.96 , pp. 1374-1388
    • Huttner, W.B.1    Schiebler, W.2    Greengard, P.3    de Camilli, P.4
  • 40
    • 0030586426 scopus 로고    scopus 로고
    • 16-BAC/SDS-PAGE: A two-dimensional gel electrophoresis system suitable for the separation of integral membrane proteins
    • Hartinger, J., Stenius, K., Hogemann, D., & Jahn, R. (1996). 16-BAC/SDS-PAGE: A two-dimensional gel electrophoresis system suitable for the separation of integral membrane proteins. Analytical Biochemistry, 240, 126-133.
    • (1996) Analytical Biochemistry , vol.240 , pp. 126-133
    • Hartinger, J.1    Stenius, K.2    Hogemann, D.3    Jahn, R.4
  • 41
    • 33846892783 scopus 로고    scopus 로고
    • Immunoisolation and subfractionation of synaptic vesicle proteins
    • Burre, J., Zimmermann, H., & Volknandt, W. (2007). Immunoisolation and subfractionation of synaptic vesicle proteins. Analytical Biochemistry, 362, 172-181.
    • (2007) Analytical Biochemistry , vol.362 , pp. 172-181
    • Burre, J.1    Zimmermann, H.2    Volknandt, W.3
  • 42
    • 20044371655 scopus 로고    scopus 로고
    • A proteomic survey of rat cerebral cortical synaptosomes
    • Witzmann, F. A., Arnold, R. J., Bai, F., et al. (2005). A proteomic survey of rat cerebral cortical synaptosomes. Proteomics, 5, 2177-2201.
    • (2005) Proteomics , vol.5 , pp. 2177-2201
    • Witzmann, F.A.1    Arnold, R.J.2    Bai, F.3
  • 43
    • 22044446815 scopus 로고    scopus 로고
    • Proteomic analysis of synaptosomes using isotope-coded affinity tags and mass spectrometry
    • Schrimpf, S. P., Meskenaite, V., Brunner, E., et al. (2005). Proteomic analysis of synaptosomes using isotope-coded affinity tags and mass spectrometry. Proteomics, 5, 2531-2541.
    • (2005) Proteomics , vol.5 , pp. 2531-2541
    • Schrimpf, S.P.1    Meskenaite, V.2    Brunner, E.3
  • 44
    • 0035221502 scopus 로고    scopus 로고
    • Perspectives for mass spectrometry and functional proteomics
    • Godovac-Zimmermann, J., & Brown, L. R. (2001). Perspectives for mass spectrometry and functional proteomics. Mass Spectrometry Reviews, 20, 1-57.
    • (2001) Mass Spectrometry Reviews , vol.20 , pp. 1-57
    • Godovac-Zimmermann, J.1    Brown, L.R.2
  • 45
    • 60349101656 scopus 로고    scopus 로고
    • Mapping of signaling pathways by functional interaction proteomics
    • Kriegsheim, A., Preisinger, C., & Kolch, W. (2008). Mapping of signaling pathways by functional interaction proteomics. Methods in Molecular Biology, 484, 177-192.
    • (2008) Methods in Molecular Biology , vol.484 , pp. 177-192
    • Kriegsheim, A.1    Preisinger, C.2    Kolch, W.3
  • 46
    • 0242551370 scopus 로고    scopus 로고
    • Chronic activation of ERK and neurodegenerative diseases
    • Colucci-D'Amato, L., Perrone-Capano, C., & di Porzio, U. (2003). Chronic activation of ERK and neurodegenerative diseases. Bioessays, 25, 1085-1095.
    • (2003) Bioessays , vol.25 , pp. 1085-1095
    • Colucci-D'Amato, L.1    Perrone-Capano, C.2    di Porzio, U.3
  • 47
    • 68549133540 scopus 로고    scopus 로고
    • Identification of astrocyte secreted proteins with a combination of shotgun proteomics and bioinformatics
    • Dowell, J. A., Johnson, J. A., & Li, L. (2009). Identification of astrocyte secreted proteins with a combination of shotgun proteomics and bioinformatics. Journal of Proteome Research, 8, 4135-4143.
    • (2009) Journal of Proteome Research , vol.8 , pp. 4135-4143
    • Dowell, J.A.1    Johnson, J.A.2    Li, L.3
  • 48
    • 62649150690 scopus 로고    scopus 로고
    • Neural cells secrete a unique repertoire of proteins
    • Schubert, D., Herrera, F., Cumming, R., et al. (2009). Neural cells secrete a unique repertoire of proteins. Journal of Neurochemistry, 109, 427-435.
    • (2009) Journal of Neurochemistry , vol.109 , pp. 427-435
    • Schubert, D.1    Herrera, F.2    Cumming, R.3
  • 50
    • 23344453615 scopus 로고    scopus 로고
    • Release of heat shock proteins (Hsps) and the effects of extracellular Hsps on neural cells and tissues
    • Tytell, M. (2005). Release of heat shock proteins (Hsps) and the effects of extracellular Hsps on neural cells and tissues. International Journal of Hyperthermia, 21, 445-455.
    • (2005) International Journal of Hyperthermia , vol.21 , pp. 445-455
    • Tytell, M.1
  • 52
    • 77952412139 scopus 로고    scopus 로고
    • Neuroproteomics: Towards understanding neuronal regeneration and degeneration
    • Sun, F., & Cavalli, V. (2009). Neuroproteomics: Towards understanding neuronal regeneration and degeneration. Molecular & Cellular Proteomics.
    • (2009) Molecular & Cellular Proteomics
    • Sun, F.1    Cavalli, V.2
  • 53
    • 70350061949 scopus 로고    scopus 로고
    • Multimodal techniques for diagnosis and prognosis of Alzheimer's disease
    • Perrin, R. J., Fagan, A. M., & Holtzman, D. M. (2009). Multimodal techniques for diagnosis and prognosis of Alzheimer's disease. Nature, 461, 916-922.
    • (2009) Nature , vol.461 , pp. 916-922
    • Perrin, R.J.1    Fagan, A.M.2    Holtzman, D.M.3
  • 55
    • 39849101009 scopus 로고    scopus 로고
    • Proteomic analysis of active multiple sclerosis lesions reveals therapeutic targets
    • Han, M. H., Hwang, S. I., Roy, D. B., et al. (2008). Proteomic analysis of active multiple sclerosis lesions reveals therapeutic targets. Nature, 451, 1076-1081.
    • (2008) Nature , vol.451 , pp. 1076-1081
    • Han, M.H.1    Hwang, S.I.2    Roy, D.B.3
  • 56
    • 58949094360 scopus 로고    scopus 로고
    • Deciphering complex mechanisms in neurodegenerative diseases: The advent of systems biology
    • Noorbakhsh, F., Overall, C. M., & Power, C. (2009). Deciphering complex mechanisms in neurodegenerative diseases: The advent of systems biology. Trends in Neurosciences, 32, 88-100.
    • (2009) Trends in Neurosciences , vol.32 , pp. 88-100
    • Noorbakhsh, F.1    Overall, C.M.2    Power, C.3
  • 57
    • 13344269000 scopus 로고    scopus 로고
    • From proteins to proteomes: Large scale protein identification by two-dimensional electrophoresis and amino acid analysis
    • Wilkins, M. R., Pasquali, C., Appel, R. D., et al. (1996). From proteins to proteomes: Large scale protein identification by two-dimensional electrophoresis and amino acid analysis. Biotechnology (N Y), 14, 61-65.
    • (1996) Biotechnology (N Y) , vol.14 , pp. 61-65
    • Wilkins, M.R.1    Pasquali, C.2    Appel, R.D.3
  • 58
    • 0029095434 scopus 로고
    • Two-dimensional polyacrylamide gel electrophoresis with immobilized pH gradients in the first dimension (IPG-Dalt): The state of the art and the controversy of vertical versus horizontal systems
    • Gorg, A., Boguth, G., Obermaier, C., Posch, A., & Weiss, W. (1995). Two-dimensional polyacrylamide gel electrophoresis with immobilized pH gradients in the first dimension (IPG-Dalt): The state of the art and the controversy of vertical versus horizontal systems. Electrophoresis, 16, 1079-1086.
    • (1995) Electrophoresis , vol.16 , pp. 1079-1086
    • Gorg, A.1    Boguth, G.2    Obermaier, C.3    Posch, A.4    Weiss, W.5
  • 60
    • 0023724979 scopus 로고
    • Isoelectric focusing of basic proteins: The problem of oxidation of cysteines
    • Altland, K., Becher, P., Rossmann, U., & Bjellqvist, B. (1988). Isoelectric focusing of basic proteins: The problem of oxidation of cysteines. Electrophoresis, 9, 474-485.
    • (1988) Electrophoresis , vol.9 , pp. 474-485
    • Altland, K.1    Becher, P.2    Rossmann, U.3    Bjellqvist, B.4
  • 62
    • 34548356702 scopus 로고    scopus 로고
    • Applications and current challenges of proteomic approaches, focusing on two-dimensional electrophoresis
    • Vercauteren, F. G., Arckens, L., & Quirion, R. (2007). Applications and current challenges of proteomic approaches, focusing on two-dimensional electrophoresis. Amino Acids, 33, 405-414.
    • (2007) Amino Acids , vol.33 , pp. 405-414
    • Vercauteren, F.G.1    Arckens, L.2    Quirion, R.3
  • 63
    • 0032925313 scopus 로고    scopus 로고
    • Characterisation of stem cell expression using two-dimensional electrophoresis
    • Pearce, A., & Svendsen, C. N. (1999). Characterisation of stem cell expression using two-dimensional electrophoresis. Electrophoresis, 20, 969-970.
    • (1999) Electrophoresis , vol.20 , pp. 969-970
    • Pearce, A.1    Svendsen, C.N.2
  • 65
    • 0343376097 scopus 로고    scopus 로고
    • Difference gel electrophoresis: A single gel method for detecting changes in protein extracts
    • Unlu, M., Morgan, M. E., & Minden, J. S. (1997). Difference gel electrophoresis: A single gel method for detecting changes in protein extracts. Electrophoresis, 18, 2071-2077.
    • (1997) Electrophoresis , vol.18 , pp. 2071-2077
    • Unlu, M.1    Morgan, M.E.2    Minden, J.S.3
  • 66
    • 65549088127 scopus 로고    scopus 로고
    • 2-D DIGE identification of differentially expressed heterogeneous nuclear ribonucleoproteins and transcription factors during neural differentiation of human embryonic stem cells
    • Barthéléry, M., Jaishankar, A., Salli, U., Freeman, W. M., & Vrana, K. E. (2009). 2-D DIGE identification of differentially expressed heterogeneous nuclear ribonucleoproteins and transcription factors during neural differentiation of human embryonic stem cells. Proteomics Clinical Applications, 3, 505-514.
    • (2009) Proteomics Clinical Applications , vol.3 , pp. 505-514
    • Barthéléry, M.1    Jaishankar, A.2    Salli, U.3    Freeman, W.M.4    Vrana, K.E.5
  • 67
    • 1842499791 scopus 로고    scopus 로고
    • Profiling core proteomes of human cell lines by one-dimensional PAGE and liquid chromatography-tandem mass spectrometry
    • Schirle, M., Heurtier, M. A., & Kuster, B. (2003). Profiling core proteomes of human cell lines by one-dimensional PAGE and liquid chromatography-tandem mass spectrometry. Molecular & Cellular Proteomics, 2, 1297-1305.
    • (2003) Molecular & Cellular Proteomics , vol.2 , pp. 1297-1305
    • Schirle, M.1    Heurtier, M.A.2    Kuster, B.3
  • 68
    • 33845585903 scopus 로고    scopus 로고
    • Analysis of the synaptic vesicle proteome using three gel-based protein separation techniques
    • Burre, J., Beckhaus, T., Schagger, H., et al. (2006). Analysis of the synaptic vesicle proteome using three gel-based protein separation techniques. Proteomics, 6, 6250-6262.
    • (2006) Proteomics , vol.6 , pp. 6250-6262
    • Burre, J.1    Beckhaus, T.2    Schagger, H.3
  • 69
    • 33750805030 scopus 로고    scopus 로고
    • Molecular anatomy of a trafficking organelle
    • Takamori, S., Holt, M., Stenius, K., et al. (2006). Molecular anatomy of a trafficking organelle. Cell, 127, 831-846.
    • (2006) Cell , vol.127 , pp. 831-846
    • Takamori, S.1    Holt, M.2    Stenius, K.3
  • 71
    • 0018198549 scopus 로고
    • Studies of microhigh-performance liquid chromatography. IV. Application of the micro pre-column method to the analysis of corticosteroids in serum
    • Ishii, D., Hibi, K., Asai, K., Nagaya, M., Mochizuki, K., & Mochida, Y. (1978). Studies of microhigh-performance liquid chromatography. IV. Application of the micro pre-column method to the analysis of corticosteroids in serum. Journal of Chromatography, 156, 173-180.
    • (1978) Journal of Chromatography , vol.156 , pp. 173-180
    • Ishii, D.1    Hibi, K.2    Asai, K.3    Nagaya, M.4    Mochizuki, K.5    Mochida, Y.6
  • 72
    • 0017935859 scopus 로고
    • Packed microcapillary columns in high performance liquid chromatography
    • Tsuda, T., & Novotny, M. V. (1978). Packed microcapillary columns in high performance liquid chromatography. Analytical Chemistry, 50, 271-275.
    • (1978) Analytical Chemistry , vol.50 , pp. 271-275
    • Tsuda, T.1    Novotny, M.V.2
  • 73
    • 0018797498 scopus 로고
    • Use of microbore columns for the separation of substances of biological origin
    • Scott, R. P., & Kucera, P. (1979). Use of microbore columns for the separation of substances of biological origin. Journal of Chromatography, 185, 27-41.
    • (1979) Journal of Chromatography , vol.185 , pp. 27-41
    • Scott, R.P.1    Kucera, P.2
  • 75
    • 0032859642 scopus 로고    scopus 로고
    • Recent developments in microcolumn liquid chromatography
    • Vissers, J. P. (1999). Recent developments in microcolumn liquid chromatography. Journal of Chromatography A, 856, 117-143.
    • (1999) Journal of Chromatography A , vol.856 , pp. 117-143
    • Vissers, J.P.1
  • 76
    • 0037102411 scopus 로고    scopus 로고
    • High-efficiency nanoscale liquid chromatography coupled on-line with mass spectrometry using nanoelectrospray ionization for proteomics
    • Shen, Y., Zhao, R., Berger, S. J., Anderson, G. A., Rodriguez, N., & Smith, R. D. (2002). High-efficiency nanoscale liquid chromatography coupled on-line with mass spectrometry using nanoelectrospray ionization for proteomics. Analytical Chemistry, 74, 4235-4249.
    • (2002) Analytical Chemistry , vol.74 , pp. 4235-4249
    • Shen, Y.1    Zhao, R.2    Berger, S.J.3    Anderson, G.A.4    Rodriguez, N.5    Smith, R.D.6
  • 77
    • 0032190378 scopus 로고    scopus 로고
    • Protein identification at the low femtomole level from silver-stained gels using a new fritless electrospray interface for liquid chromatography-microspray and nanospray mass spectrometry
    • Gatlin, C. L., Kleemann, G. R., Hays, L. G., Link, A. J., & Yates, J. R., 3rd. (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. Analytical Biochemistry, 263, 93-101.
    • (1998) Analytical Biochemistry , vol.263 , pp. 93-101
    • Gatlin, C.L.1    Kleemann, G.R.2    Hays, L.G.3    Link, A.J.4    Yates 3rd, J.R.5
  • 78
    • 0034665968 scopus 로고    scopus 로고
    • Subfemtomole MS and MS/MS peptide sequence analysis using nano-HPLC micro-ESI fourier transform ion cyclotron resonance mass spectrometry
    • Martin, S. E., Shabanowitz, J., Hunt, D. F., & Marto, J. A. (2000). Subfemtomole MS and MS/MS peptide sequence analysis using nano-HPLC micro-ESI fourier transform ion cyclotron resonance mass spectrometry. Analytical Chemistry, 72, 4266-4274.
    • (2000) Analytical Chemistry , vol.72 , pp. 4266-4274
    • Martin, S.E.1    Shabanowitz, J.2    Hunt, D.F.3    Marto, J.A.4
  • 79
    • 33645813378 scopus 로고    scopus 로고
    • Mass spectrometry and protein analysis
    • Domon, B., & Aebersold, R. (2006). Mass spectrometry and protein analysis. Science, 312, 212-217.
    • (2006) Science , vol.312 , pp. 212-217
    • Domon, B.1    Aebersold, R.2
  • 81
    • 40549107755 scopus 로고    scopus 로고
    • Comparative LC-MS: A landscape of peaks and valleys
    • America, A. H., & Cordewener, J. H. (2008). Comparative LC-MS: A landscape of peaks and valleys. Proteomics, 8, 731-749.
    • (2008) Proteomics , vol.8 , pp. 731-749
    • America, A.H.1    Cordewener, J.H.2
  • 84
    • 0036583926 scopus 로고    scopus 로고
    • Stable isotope labeling by amino acids in cell culture, SILAC, as a simple and accurate approach to expression proteomics
    • Ong, S. E., Blagoev, B., Kratchmarova, I., et al. (2002). Stable isotope labeling by amino acids in cell culture, SILAC, as a simple and accurate approach to expression proteomics. Molecular & Cellular Proteomics, 1, 376-386.
    • (2002) Molecular & Cellular Proteomics , vol.1 , pp. 376-386
    • Ong, S.E.1    Blagoev, B.2    Kratchmarova, I.3
  • 86
    • 67449107495 scopus 로고    scopus 로고
    • Stable isotope labeling by amino acids in cell culture (SILAC) and quantitative comparison of the membrane proteomes of self-renewing and differentiating human embryonic stem cells
    • Prokhorova, T. A., Rigbolt, K. T., Johansen, P. T., et al. (2009). Stable isotope labeling by amino acids in cell culture (SILAC) and quantitative comparison of the membrane proteomes of self-renewing and differentiating human embryonic stem cells. Molecular & Cellular Proteomics, 8, 959-970.
    • (2009) Molecular & Cellular Proteomics , vol.8 , pp. 959-970
    • Prokhorova, T.A.1    Rigbolt, K.T.2    Johansen, P.T.3
  • 87
    • 42649132889 scopus 로고    scopus 로고
    • Stable isotope labeling by amino acids in cell culture (SILAC) and proteome quantitation of mouse embryonic stem cells to a depth of 5, 111 proteins
    • Graumann, J., Hubner, N. C., Kim, J. B., et al. (2008). Stable isotope labeling by amino acids in cell culture (SILAC) and proteome quantitation of mouse embryonic stem cells to a depth of 5, 111 proteins. Molecular & Cellular Proteomics, 7, 672-683.
    • (2008) Molecular & Cellular Proteomics , vol.7 , pp. 672-683
    • Graumann, J.1    Hubner, N.C.2    Kim, J.B.3
  • 88
    • 58049195459 scopus 로고    scopus 로고
    • Quantitative mass spectrometry identifies drug targets in cancer stem cell-containing side population
    • Steiniger, S. C., Coppinger, J. A., Kruger, J. A., Yates, J., 3rd, & Janda, K. D. (2008). Quantitative mass spectrometry identifies drug targets in cancer stem cell-containing side population. Stem Cells, 26, 3037-3046.
    • (2008) Stem Cells , vol.26 , pp. 3037-3046
    • Steiniger, S.C.1    Coppinger, J.A.2    Kruger, J.A.3    Yates 3rd, J.4    Janda, K.D.5
  • 89
    • 68549133585 scopus 로고    scopus 로고
    • IDAWG: Metabolic incorporation of stable isotope labels for quantitative glycomics of cultured cells
    • Orlando, R., Lim, J. M., Atwood, J. A., 3rd, et al. (2009). IDAWG: Metabolic incorporation of stable isotope labels for quantitative glycomics of cultured cells. Journal of Proteome Research, 8, 3816-3823.
    • (2009) Journal of Proteome Research , vol.8 , pp. 3816-3823
    • Orlando, R.1    Lim, J.M.2    Atwood 3rd, J.A.3
  • 90
    • 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., & Aebersold, R. (1999). Quantitative analysis of complex protein mixtures using isotope-coded affinity tags. Nature Biotechnology, 17, 994-999.
    • (1999) Nature Biotechnology , 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
  • 91
    • 13244260803 scopus 로고    scopus 로고
    • A novel strategy for quantitative proteomics using isotope-coded protein labels
    • Schmidt, A., Kellermann, J., & Lottspeich, F. (2005). A novel strategy for quantitative proteomics using isotope-coded protein labels. Proteomics, 5, 4-15.
    • (2005) Proteomics , vol.5 , pp. 4-15
    • Schmidt, A.1    Kellermann, J.2    Lottspeich, F.3
  • 93
    • 20144368638 scopus 로고    scopus 로고
    • Integrated genomic and proteomic analyses of gene expression in Mammalian cells
    • Tian, Q., Stepaniants, S. B., Mao, M., et al. (2004). Integrated genomic and proteomic analyses of gene expression in Mammalian cells. Molecular & Cellular Proteomics, 3, 960-969.
    • (2004) Molecular & Cellular Proteomics , vol.3 , pp. 960-969
    • Tian, Q.1    Stepaniants, S.B.2    Mao, M.3
  • 94
    • 65249112733 scopus 로고    scopus 로고
    • Proteomic characteristics of ex vivo-enriched adult human bone marrow mononuclear cells in continuous perfusion cultures
    • Prahalad, A. K., & Hock, J. M. (2009). Proteomic characteristics of ex vivo-enriched adult human bone marrow mononuclear cells in continuous perfusion cultures. Journal of Proteome Research, 8, 2079-2089.
    • (2009) Journal of Proteome Research , vol.8 , pp. 2079-2089
    • Prahalad, A.K.1    Hock, J.M.2
  • 95
    • 19944432197 scopus 로고    scopus 로고
    • Multiplexed protein quantitation in Saccharomyces cerevisiae using amine-reactive isobaric tagging reagents
    • Ross, P. L., Huang, Y. N., Marchese, J. N., et al. (2004). Multiplexed protein quantitation in Saccharomyces cerevisiae using amine-reactive isobaric tagging reagents. Molecular & Cellular Proteomics, 3, 1154-1169.
    • (2004) Molecular & Cellular Proteomics , vol.3 , pp. 1154-1169
    • Ross, P.L.1    Huang, Y.N.2    Marchese, J.N.3
  • 96
    • 70449412362 scopus 로고    scopus 로고
    • iTRAQ underestimation in simple and complex mixtures: The good, the bad and the ugly
    • Ow, S. Y., Salim, M., Noirel, J., Evans, C., Rehman, I., & Wright, P. C. (2009). iTRAQ underestimation in simple and complex mixtures: "The good, the bad and the ugly". Journal of Proteome Research, 8, 5347-5355.
    • (2009) Journal of Proteome Research , vol.8 , pp. 5347-5355
    • Ow, S.Y.1    Salim, M.2    Noirel, J.3    Evans, C.4    Rehman, I.5    Wright, P.C.6
  • 98
    • 12444345515 scopus 로고    scopus 로고
    • Tandem mass tags: A novel quantification strategy for comparative analysis of complex protein mixtures by MS/MS
    • Thompson, A., Schafer, J., Kuhn, K., et al. (2003). Tandem mass tags: A novel quantification strategy for comparative analysis of complex protein mixtures by MS/MS. Analytical Chemistry, 75, 1895-1904.
    • (2003) Analytical Chemistry , vol.75 , pp. 1895-1904
    • Thompson, A.1    Schafer, J.2    Kuhn, K.3
  • 99
    • 33744926266 scopus 로고    scopus 로고
    • Quantitative proteomics reveals posttranslational control as a regulatory factor in primary hematopoietic stem cells
    • Unwin, R. D., Smith, D. L., Blinco, D., et al. (2006). Quantitative proteomics reveals posttranslational control as a regulatory factor in primary hematopoietic stem cells. Blood, 107, 4687-4694.
    • (2006) Blood , vol.107 , pp. 4687-4694
    • Unwin, R.D.1    Smith, D.L.2    Blinco, D.3
  • 100
    • 35848931437 scopus 로고    scopus 로고
    • The use of isobaric tag peptide labeling (iTRAQ) and mass spectrometry to examine rare, primitive hematopoietic cells from patients with chronic myeloid leukemia
    • Griffiths, S. D., Burthem, J., Unwin, R. D., et al. (2007). The use of isobaric tag peptide labeling (iTRAQ) and mass spectrometry to examine rare, primitive hematopoietic cells from patients with chronic myeloid leukemia. Molecular Biotechnology, 36, 81-89.
    • (2007) Molecular Biotechnology , vol.36 , pp. 81-89
    • Griffiths, S.D.1    Burthem, J.2    Unwin, R.D.3
  • 101
    • 33847371618 scopus 로고    scopus 로고
    • iTRAQ is a useful method to screen for membrane-bound proteins differentially expressed in human natural killer cell types
    • Lund, T. C., Anderson, L. B., McCullar, V., et al. (2007). iTRAQ is a useful method to screen for membrane-bound proteins differentially expressed in human natural killer cell types. Journal of Proteome Research, 6, 644-653.
    • (2007) Journal of Proteome Research , vol.6 , pp. 644-653
    • Lund, T.C.1    Anderson, L.B.2    McCullar, V.3
  • 102
    • 33749630783 scopus 로고    scopus 로고
    • An integrated approach to mapping the proteome of the human bone marrow stromal cell
    • Seshi, B. (2006). An integrated approach to mapping the proteome of the human bone marrow stromal cell. Proteomics, 6, 5169-5182.
    • (2006) Proteomics , vol.6 , pp. 5169-5182
    • Seshi, B.1
  • 103
    • 33746255981 scopus 로고    scopus 로고
    • Identification of differentiating neural progenitor cell markers using shotgun isobaric tagging mass spectrometry
    • Salim, K., Kehoe, L., Minkoff, M. S., Bilsland, J. G., Munoz-Sanjuan, I., & Guest, P. C. (2006). Identification of differentiating neural progenitor cell markers using shotgun isobaric tagging mass spectrometry. Stem Cells and Development, 15, 461-470.
    • (2006) Stem Cells and Development , vol.15 , pp. 461-470
    • Salim, K.1    Kehoe, L.2    Minkoff, M.S.3    Bilsland, J.G.4    Munoz-Sanjuan, I.5    Guest, P.C.6
  • 104
    • 0037106398 scopus 로고    scopus 로고
    • Identification and relative quantitation of protein mixtures by enzymatic digestion followed by capillary reversed-phase liquid chromatography-tandem mass spectrometry
    • Bondarenko, P. V., Chelius, D., & Shaler, T. A. (2002). Identification and relative quantitation of protein mixtures by enzymatic digestion followed by capillary reversed-phase liquid chromatography-tandem mass spectrometry. Analytical Chemistry, 74, 4741-4749.
    • (2002) Analytical Chemistry , vol.74 , pp. 4741-4749
    • Bondarenko, P.V.1    Chelius, D.2    Shaler, T.A.3
  • 105
    • 0036665581 scopus 로고    scopus 로고
    • Quantitative profiling of proteins in complex mixtures using liquid chromatography and mass spectrometry
    • Chelius, D., & Bondarenko, P. V. (2002). Quantitative profiling of proteins in complex mixtures using liquid chromatography and mass spectrometry. Journal of Proteome Research, 1, 317-323.
    • (2002) Journal of Proteome Research , vol.1 , pp. 317-323
    • Chelius, D.1    Bondarenko, P.V.2
  • 106
    • 10744233766 scopus 로고    scopus 로고
    • Quantification of proteins and metabolites by mass spectrometry without isotopic labeling or spiked standards
    • Wang, W., Zhou, H., Lin, H., et al. (2003). Quantification of proteins and metabolites by mass spectrometry without isotopic labeling or spiked standards. Analytical Chemistry, 75, 4818-4826.
    • (2003) Analytical Chemistry , vol.75 , pp. 4818-4826
    • Wang, W.1    Zhou, H.2    Lin, H.3
  • 107
    • 20144388265 scopus 로고    scopus 로고
    • Quantitative proteomic analysis by accurate mass retention time pairs
    • Silva, J. C., Denny, R., Dorschel, C. A., et al. (2005). Quantitative proteomic analysis by accurate mass retention time pairs. Analytical Chemistry, 77, 2187-2200.
    • (2005) Analytical Chemistry , vol.77 , pp. 2187-2200
    • Silva, J.C.1    Denny, R.2    Dorschel, C.A.3
  • 108
    • 26844559000 scopus 로고    scopus 로고
    • Exponentially modified protein abundance index (emPAI) for estimation of absolute protein amount in proteomics by the number of sequenced peptides per protein
    • Ishihama, Y., Oda, Y., Tabata, T., et al. (2005). Exponentially modified protein abundance index (emPAI) for estimation of absolute protein amount in proteomics by the number of sequenced peptides per protein. Molecular & Cellular Proteomics, 4, 1265-1272.
    • (2005) Molecular & Cellular Proteomics , vol.4 , pp. 1265-1272
    • Ishihama, Y.1    Oda, Y.2    Tabata, T.3
  • 109
    • 33846165487 scopus 로고    scopus 로고
    • Absolute protein expression profiling estimates the relative contributions of transcriptional and translational regulation
    • Lu, P., Vogel, C., Wang, R., Yao, X., & Marcotte, E. M. (2007). Absolute protein expression profiling estimates the relative contributions of transcriptional and translational regulation. Nature Biotechnology, 25, 117-124.
    • (2007) Nature Biotechnology , vol.25 , pp. 117-124
    • Lu, P.1    Vogel, C.2    Wang, R.3    Yao, X.4    Marcotte, E.M.5
  • 111
    • 34249657456 scopus 로고    scopus 로고
    • Analysis and quantification of diagnostic serum markers and protein signatures for Gaucher disease
    • Vissers, J. P., Langridge, J. I., & Aerts, J. M. (2007). Analysis and quantification of diagnostic serum markers and protein signatures for Gaucher disease. Molecular & Cellular Proteomics, 6, 755-766.
    • (2007) Molecular & Cellular Proteomics , vol.6 , pp. 755-766
    • Vissers, J.P.1    Langridge, J.I.2    Aerts, J.M.3
  • 112
    • 71449100011 scopus 로고    scopus 로고
    • Towards a proteome signature for invasive ductal breast carcinoma derived from label-free nanoscale LC-MS protein expression profiling of tumorous and glandular tissue
    • Rower, C., Vissers, J. P., Koy, C., et al. (2009). Towards a proteome signature for invasive ductal breast carcinoma derived from label-free nanoscale LC-MS protein expression profiling of tumorous and glandular tissue. Analytical and Bioanalytical Chemistry, 395, 2443-2456.
    • (2009) Analytical and Bioanalytical Chemistry , vol.395 , pp. 2443-2456
    • Rower, C.1    Vissers, J.P.2    Koy, C.3
  • 113
    • 68449102172 scopus 로고    scopus 로고
    • Proteome-wide cellular protein concentrations of the human pathogen Leptospira interrogans
    • Malmstrom, J., Beck, M., Schmidt, A., Lange, V., Deutsch, E. W., & Aebersold, R. (2009). Proteome-wide cellular protein concentrations of the human pathogen Leptospira interrogans. Nature, 460, 762-765.
    • (2009) Nature , vol.460 , pp. 762-765
    • Malmstrom, J.1    Beck, M.2    Schmidt, A.3    Lange, V.4    Deutsch, E.W.5    Aebersold, R.6
  • 115
    • 61849119027 scopus 로고    scopus 로고
    • Qualitative and quantitative proteomic profiling of cripto(-/-) embryonic stem cells by means of accurate mass LC-MS analysis
    • Chambery, A., Vissers, J. P., Langridge, J. I., et al. (2009). Qualitative and quantitative proteomic profiling of cripto(-/-) embryonic stem cells by means of accurate mass LC-MS analysis. Journal of Proteome Research, 8, 1047-1058.
    • (2009) Journal of Proteome Research , vol.8 , pp. 1047-1058
    • Chambery, A.1    Vissers, J.P.2    Langridge, J.I.3
  • 116
    • 33645721632 scopus 로고    scopus 로고
    • Quantitative mass spectrometric multiple reaction monitoring assays for major plasma proteins
    • Anderson, L., & Hunter, C. L. (2006). Quantitative mass spectrometric multiple reaction monitoring assays for major plasma proteins. Molecular & Cellular Proteomics, 5, 573-588.
    • (2006) Molecular & Cellular Proteomics , vol.5 , pp. 573-588
    • Anderson, L.1    Hunter, C.L.2
  • 117
    • 38349068918 scopus 로고    scopus 로고
    • Quantitative, multiplexed assays for low abundance proteins in plasma by targeted mass spectrometry and stable isotope dilution
    • Keshishian, H., Addona, T., Burgess, M., Kuhn, E., & Carr, S. A. (2007). Quantitative, multiplexed assays for low abundance proteins in plasma by targeted mass spectrometry and stable isotope dilution. Molecular & Cellular Proteomics, 6, 2212-2229.
    • (2007) Molecular & Cellular Proteomics , vol.6 , pp. 2212-2229
    • Keshishian, H.1    Addona, T.2    Burgess, M.3    Kuhn, E.4    Carr, S.A.5
  • 118
    • 1842528125 scopus 로고    scopus 로고
    • Quantification of C-reactive protein in the serum of patients with rheumatoid arthritis using multiple reaction monitoring mass spectrometry and 13C-labeled peptide standards
    • Kuhn, E., Wu, J., Karl, J., Liao, H., Zolg, W., & Guild, B. (2004). Quantification of C-reactive protein in the serum of patients with rheumatoid arthritis using multiple reaction monitoring mass spectrometry and 13C-labeled peptide standards. Proteomics, 4, 1175-1186.
    • (2004) Proteomics , vol.4 , pp. 1175-1186
    • Kuhn, E.1    Wu, J.2    Karl, J.3    Liao, H.4    Zolg, W.5    Guild, B.6
  • 120
    • 33847179916 scopus 로고    scopus 로고
    • Multiplexed absolute quantification for proteomics using concatenated signature peptides encoded by QconCAT genes
    • Pratt, J. M., Simpson, D. M., Doherty, M. K., Rivers, J., Gaskell, S. J., & Beynon, R. J. (2006). Multiplexed absolute quantification for proteomics using concatenated signature peptides encoded by QconCAT genes. Nature Protocols, 1, 1029-1043.
    • (2006) Nature Protocols , vol.1 , pp. 1029-1043
    • Pratt, J.M.1    Simpson, D.M.2    Doherty, M.K.3    Rivers, J.4    Gaskell, S.J.5    Beynon, R.J.6
  • 122
    • 63049107227 scopus 로고    scopus 로고
    • Quantifying proteins by mass spectrometry: The selectivity of SRM is only part of the problem
    • Duncan, M. W., Yergey, A. L., & Patterson, S. D. (2009). Quantifying proteins by mass spectrometry: The selectivity of SRM is only part of the problem. Proteomics, 9, 1124-1127.
    • (2009) Proteomics , vol.9 , pp. 1124-1127
    • Duncan, M.W.1    Yergey, A.L.2    Patterson, S.D.3
  • 123
    • 63049090914 scopus 로고    scopus 로고
    • How specific is my SRM? The issue of precursor and product ion redundancy
    • Sherman, J., McKay, M. J., Ashman, K., & Molloy, M. P. (2009). How specific is my SRM? The issue of precursor and product ion redundancy. Proteomics, 9, 1120-1123.
    • (2009) Proteomics , vol.9 , pp. 1120-1123
    • Sherman, J.1    McKay, M.J.2    Ashman, K.3    Molloy, M.P.4
  • 124
    • 34547727671 scopus 로고    scopus 로고
    • High-speed data reduction, feature detection, and MS/MS spectrum quality assessment of shotgun proteomics data sets using high-resolution mass spectrometry
    • Hoopmann, M. R., Finney, G. L., & MacCoss, M. J. (2007). High-speed data reduction, feature detection, and MS/MS spectrum quality assessment of shotgun proteomics data sets using high-resolution mass spectrometry. Analytical Chemistry, 79, 5620-5632.
    • (2007) Analytical Chemistry , vol.79 , pp. 5620-5632
    • Hoopmann, M.R.1    Finney, G.L.2    Maccoss, M.J.3
  • 125
    • 55249111329 scopus 로고    scopus 로고
    • Precursor-ion mass re-estimation improves peptide identification on hybrid instruments
    • Luethy, R., Kessner, D. E., Katz, J. E., et al. (2008). Precursor-ion mass re-estimation improves peptide identification on hybrid instruments. Journal of Proteome Research, 7, 4031-4039.
    • (2008) Journal of Proteome Research , vol.7 , pp. 4031-4039
    • Luethy, R.1    Kessner, D.E.2    Katz, J.E.3
  • 126
    • 63049084861 scopus 로고    scopus 로고
    • The detection, correlation, and comparison of peptide precursor and product ions from data independent LC-MS with data dependant LC-MS/MS
    • Geromanos, S. J., Vissers, J. P., Silva, J. C., et al. (2009). The detection, correlation, and comparison of peptide precursor and product ions from data independent LC-MS with data dependant LC-MS/MS. Proteomics, 9, 1683-1695.
    • (2009) Proteomics , vol.9 , pp. 1683-1695
    • Geromanos, S.J.1    Vissers, J.P.2    Silva, J.C.3


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.