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Volumn 10, Issue 12, 2011, Pages 5383-5397

Multidimensional strategy for sensitive phosphoproteomics incorporating protein prefractionation combined with SIMAC, HILIC, and TiO 2 chromatography applied to proximal EGF signaling

Author keywords

EGF signalling; false discovery rate estimation; multidimensional phosphopeptide fractionation; Phosphoproteomics

Indexed keywords

CELL PROTEIN; EPIDERMAL GROWTH FACTOR; PHOSPHOPEPTIDE; PHOSPHOPROTEIN; TITANIUM DIOXIDE;

EID: 82755163993     PISSN: 15353893     EISSN: 15353907     Source Type: Journal    
DOI: 10.1021/pr200641x     Document Type: Article
Times cited : (65)

References (66)
  • 1
    • 0034614490 scopus 로고    scopus 로고
    • Signaling - 2000 and beyond
    • Hunter, T. Signaling - 2000 and beyond Cell 2000, 100 (1) 113-27 (Pubitemid 30046300)
    • (2000) Cell , vol.100 , Issue.1 , pp. 113-127
    • Hunter, T.1
  • 2
    • 63049113651 scopus 로고    scopus 로고
    • Analytical strategies for phosphoproteomics
    • Thingholm, T. E.; Jensen, O. N.; Larsen, M. R. Analytical strategies for phosphoproteomics Proteomics 2009, 9 (6) 1451-68
    • (2009) Proteomics , vol.9 , Issue.6 , pp. 1451-68
    • Thingholm, T.E.1    Jensen, O.N.2    Larsen, M.R.3
  • 4
    • 0022541790 scopus 로고
    • 3+) affinity chromatography
    • Andersson, L.; Porath, J. Isolation of Phosphoproteins by Immobilized Metal (Fe-3+) Affinity-Chromatography Anal. Biochem. 1986, 154 (1) 250-4 (Pubitemid 16063367)
    • (1986) Analytical Biochemistry , vol.154 , Issue.1 , pp. 250-254
    • Andersson, L.1    Porath, J.2
  • 5
    • 0033565503 scopus 로고    scopus 로고
    • Immobilized gallium(III) affinity chromatography of phosphopeptides
    • DOI 10.1021/ac981409y
    • Posewitz, M. C.; Tempst, P. Immobilized gallium(III) affinity chromatography of phosphopeptides Anal. Chem. 1999, 71 (14) 2883-92 (Pubitemid 29340481)
    • (1999) Analytical Chemistry , vol.71 , Issue.14 , pp. 2883-2892
    • Posewitz, M.C.1    Tempst, P.2
  • 6
    • 0030667705 scopus 로고    scopus 로고
    • Evidence for phosphorylation of serine 753 in CFTR using a novel metal- ion affinity resin and matrix-assisted laser desorption mass spectrometry
    • Neville, D. C.; Rozanas, C. R.; Price, E. M.; Gruis, D. B.; Verkman, A. S.; Townsend, R. R. Evidence for phosphorylation of serine 753 in CFTR using a novel metal-ion affinity resin and matrix-assisted laser desorption mass spectrometry Protein Sci. 1997, 6 (11) 2436-45 (Pubitemid 27490754)
    • (1997) Protein Science , vol.6 , Issue.11 , pp. 2436-2445
    • Neville, D.C.A.1    Rozanas, C.R.2    Price, E.M.3    Gruis, D.B.4    Verkman, A.S.5    Townsend, R.R.6
  • 7
    • 0035072715 scopus 로고    scopus 로고
    • A systematic approach to the analysis of protein phosphorylation
    • DOI 10.1038/86777
    • Zhou, H. L.; Watts, J. D.; Aebersold, R. A systematic approach to the analysis of protein phosphorylation Nat. Biotechnol. 2001, 19 (4) 375-8 (Pubitemid 32275349)
    • (2001) Nature Biotechnology , vol.19 , Issue.4 , pp. 375-378
    • Zhou, H.1    Watts, J.D.2    Aebersold, R.3
  • 8
    • 1842427490 scopus 로고    scopus 로고
    • Chemo-affinity of titania for the column-switching HPLC analysis of phosphopeptides
    • Sano, A.; Nakamura, H. Chemo-affinity of titania for the column-switching HPLC analysis of phosphopeptides Anal. Sci. 2004, 20 (3) 565-6
    • (2004) Anal. Sci. , vol.20 , Issue.3 , pp. 565-6
    • Sano, A.1    Nakamura, H.2
  • 9
    • 5644259649 scopus 로고    scopus 로고
    • Phosphopeptide-selective column-switching RP-HPLC with a titania precolumn
    • Kuroda, I.; Shintani, Y.; Motokawa, M.; Abe, S.; Furuno, M. Phosphopeptide-selective column-switching RP-HPLC with a titania precolumn Anal. Sci. 2004, 20 (9) 1313-9
    • (2004) Anal. Sci. , vol.20 , Issue.9 , pp. 1313-9
    • Kuroda, I.1    Shintani, Y.2    Motokawa, M.3    Abe, S.4    Furuno, M.5
  • 10
    • 24944519450 scopus 로고    scopus 로고
    • Highly selective enrichment of phosphorylated peptides from peptide mixtures using titanium dioxide microcolumns
    • DOI 10.1074/mcp.T500007-MCP200
    • Larsen, M. R.; Thingholm, T. E.; Jensen, O. N.; Roepstorff, P.; Jorgensen, T. J. Highly selective enrichment of phosphorylated peptides from peptide mixtures using titanium dioxide microcolumns Mol. Cell. Proteomics 2005, 4 (7) 873-86 (Pubitemid 41309146)
    • (2005) Molecular and Cellular Proteomics , vol.4 , Issue.7 , pp. 873-886
    • Larsen, M.R.1    Thingholm, T.E.2    Jensen, O.N.3    Roepstorff, P.4    Jorgensen, T.J.D.5
  • 11
    • 3242688830 scopus 로고    scopus 로고
    • Selective isolation at the femtomole level of phosphopeptides from proteolytic digests using 2D-NanoLC-ESI-MS/MS and titanium oxide precolumns
    • DOI 10.1021/ac0498617
    • Pinkse, M. W.; Uitto, P. M.; Hilhorst, M. J.; Ooms, B.; Heck, A. J. Selective isolation at the femtomole level of phosphopeptides from proteolytic digests using 2D-NanoLC-ESI-MS/MS and titanium oxide precolumns Anal. Chem. 2004, 76 (14) 3935-43 (Pubitemid 38943662)
    • (2004) Analytical Chemistry , vol.76 , Issue.14 , pp. 3935-3943
    • Pinkse, M.W.H.1    Uitto, P.M.2    Hilhorst, M.J.3    Ooms, B.4    Heck, A.J.R.5
  • 15
    • 33750456519 scopus 로고    scopus 로고
    • Global, In Vivo, and Site-Specific Phosphorylation Dynamics in Signaling Networks
    • DOI 10.1016/j.cell.2006.09.026, PII S0092867406012748
    • Olsen, J. V.; Blagoev, B.; Gnad, F.; Macek, B.; Kumar, C.; Mortensen, P.; Mann, M. Global, in vivo, and site-specific phosphorylation dynamics in signaling networks Cell 2006, 127 (3) 635-48 (Pubitemid 44647421)
    • (2006) Cell , vol.127 , Issue.3 , pp. 635-648
    • Olsen, J.V.1    Blagoev, B.2    Gnad, F.3    Macek, B.4    Kumar, C.5    Mortensen, P.6    Mann, M.7
  • 16
    • 0035106351 scopus 로고    scopus 로고
    • Large-scale analysis of the yeast proteome by multidimensional protein identification technology
    • DOI 10.1038/85686
    • Washburn, M. P.; Wolters, D.; Yates, J. R., 3rd Large-scale analysis of the yeast proteome by multidimensional protein identification technology Nat. Biotechnol. 2001, 19 (3) 242-7 (Pubitemid 32220565)
    • (2001) Nature Biotechnology , vol.19 , Issue.3 , pp. 242-247
    • Washburn, M.P.1    Wolters, D.2    Yates, J.R.3
  • 18
    • 9744270734 scopus 로고    scopus 로고
    • Implications of column peak capacity on the separation of complex peptide mixtures in single- and two-dimensional high-performance liquid chromatography
    • DOI 10.1016/j.chroma.2004.10.092, PII S0021967304019697
    • Gilar, M.; Daly, A. E.; Kele, M.; Neue, U. D.; Gebler, J. C. Implications of column peak capacity on the separation of complex peptide mixtures in single- and two-dimensional high-performance liquid chromatography J. Chromatogr., A 2004, 1061 (2) 183-92 (Pubitemid 39586746)
    • (2004) Journal of Chromatography A , vol.1061 , Issue.2 , pp. 183-192
    • Gilar, M.1    Daly, A.E.2    Kele, M.3    Neue, U.D.4    Gebler, J.C.5
  • 19
    • 0025173758 scopus 로고
    • Hydrophilic-interaction chromatography for the separation of peptides, nucleic acids and other polar compounds
    • DOI 10.1016/S0021-9673(00)96972-3
    • Alpert, A. J. Hydrophilic-interaction chromatography for the separation of peptides, nucleic acids and other polar compounds J. Chromatogr. 1990, 499, 177-96 (Pubitemid 20044236)
    • (1990) Journal of Chromatography , vol.499 , pp. 177-196
    • Alpert, A.J.1
  • 20
    • 43849091451 scopus 로고    scopus 로고
    • Hydrophilic interaction chromatography reduces the complexity of the phosphoproteome and improves global phosphopeptide isolation and detection
    • DOI 10.1074/mcp.M700543-MCP200
    • McNulty, D. E.; Annan, R. S. Hydrophilic interaction chromatography reduces the complexity of the phosphoproteome and improves global phosphopeptide isolation and detection Mol. Cell. Proteomics 2008, 7 (5) 971-80 (Pubitemid 351737096)
    • (2008) Molecular and Cellular Proteomics , vol.7 , Issue.5 , pp. 971-980
    • McNulty, D.E.1    Annan, R.S.2
  • 21
    • 26444539668 scopus 로고    scopus 로고
    • Orthogonality of separation in two-dimensional liquid chromatography
    • DOI 10.1021/ac050923i
    • Gilar, M.; Olivova, P.; Daly, A. E.; Gebler, J. C. Orthogonality of separation in two-dimensional liquid chromatography Anal. Chem. 2005, 77 (19) 6426-34 (Pubitemid 41436983)
    • (2005) Analytical Chemistry , vol.77 , Issue.19 , pp. 6426-6434
    • Gilar, M.1    Olivova, P.2    Daly, A.E.3    Gebler, J.C.4
  • 22
    • 42649139982 scopus 로고    scopus 로고
    • SIMAC (Sequential Elution from IMAC), a phosphoproteomics strategy for the rapid separation of monophosphorylated from multiply phosphorylated peptides
    • DOI 10.1074/mcp.M700362-MCP200
    • Thingholm, T. E.; Jensen, O. N.; Robinson, P. J.; Larsen, M. R. SIMAC-A phosphoproteomic strategy for the rapid separation of mono-phosphorylated from multiply phosphorylated peptides Mol. Cell. Proteomics 2007, 7 (4) 661-71 (Pubitemid 351597478)
    • (2008) Molecular and Cellular Proteomics , vol.7 , Issue.4 , pp. 661-671
    • Thingholm, T.E.1    Jensen, O.N.2    Robinson, P.J.3    Larsen, M.R.4
  • 23
    • 33749853607 scopus 로고    scopus 로고
    • A probability-based approach for high-throughput protein phosphorylation analysis and site localization
    • DOI 10.1038/nbt1240, PII NBT1240
    • Beausoleil, S. A.; Villen, J.; Gerber, S. A.; Rush, J.; Gygi, S. P. A probability-based approach for high-throughput protein phosphorylation analysis and site localization Nat. Biotechnol. 2006, 24 (10) 1285-92 (Pubitemid 44564776)
    • (2006) Nature Biotechnology , vol.24 , Issue.10 , pp. 1285-1292
    • Beausoleil, S.A.1    Villen, J.2    Gerber, S.A.3    Rush, J.4    Gygi, S.P.5
  • 24
    • 4544370533 scopus 로고    scopus 로고
    • Improved peptide identification in proteomics by two consecutive stages of mass spectrometric fragmentation
    • DOI 10.1073/pnas.0405549101
    • Olsen, J. V.; Mann, M. Improved peptide identification in proteomics by two consecutive stages of mass spectrometric fragmentation Proc. Natl. Acad. Sci. U.S.A. 2004, 101 (37) 13417-22 (Pubitemid 39238417)
    • (2004) Proceedings of the National Academy of Sciences of the United States of America , vol.101 , Issue.37 , pp. 13417-13422
    • Olsen, J.V.1    Mann, M.2
  • 25
    • 77958000048 scopus 로고    scopus 로고
    • Comparative assessment of site assignments in CID and electron transfer dissociation spectra of phosphopeptides discloses limited relocation of phosphate groups
    • Mischerikow, N.; Altelaar, A. F.; Navarro, J. D.; Mohammed, S.; Heck, A. J. Comparative assessment of site assignments in CID and electron transfer dissociation spectra of phosphopeptides discloses limited relocation of phosphate groups Mol. Cell. Proteomics 2010, 9 (10) 2140-8
    • (2010) Mol. Cell. Proteomics , vol.9 , Issue.10 , pp. 2140-8
    • Mischerikow, N.1    Altelaar, A.F.2    Navarro, J.D.3    Mohammed, S.4    Heck, A.J.5
  • 26
    • 58149116970 scopus 로고    scopus 로고
    • Evaluation of gas-phase rearrangement and competing fragmentation reactions on protein phosphorylation site assignment using collision induced dissociation-MS/MS and MS3
    • Palumbo, A. M.; Reid, G. E. Evaluation of gas-phase rearrangement and competing fragmentation reactions on protein phosphorylation site assignment using collision induced dissociation-MS/MS and MS3 Anal. Chem. 2008, 80 (24) 9735-47
    • (2008) Anal. Chem. , vol.80 , Issue.24 , pp. 9735-47
    • Palumbo, A.M.1    Reid, G.E.2
  • 28
    • 0033434080 scopus 로고    scopus 로고
    • Probability-based protein identification by searching sequence databases using mass spectrometry data
    • Perkins, D. N.; Pappin, D. J.; Creasy, D. M.; Cottrell, J. S. Probability-based protein identification by searching sequence databases using mass spectrometry data Electrophoresis 1999, 20 (18) 3551-67 (Pubitemid 30007252)
    • (1999) Electrophoresis , vol.20 , Issue.18 , pp. 3551-3567
    • Perkins, D.N.1    Pappin, D.J.C.2    Creasy, D.M.3    Cottrell, J.S.4
  • 29
    • 0000857494 scopus 로고
    • An Approach to Correlate Tandem Mass-Spectral Data of Peptides with Amino-Acid-Sequences in a Protein Database
    • Eng, J. K.; Mccormack, A. L.; Yates, J. R. An Approach to Correlate Tandem Mass-Spectral Data of Peptides with Amino-Acid-Sequences in a Protein Database J. Am. Soc. Mass Spectrom. 1994, 5 (11) 976-89
    • (1994) J. Am. Soc. Mass Spectrom. , vol.5 , Issue.11 , pp. 976-89
    • Eng, J.K.1    McCormack, A.L.2    Yates, J.R.3
  • 30
    • 3142702204 scopus 로고    scopus 로고
    • TANDEM: Matching proteins with tandem mass spectra
    • DOI 10.1093/bioinformatics/bth092
    • Craig, R.; Beavis, R. C. TANDEM: matching proteins with tandem mass spectra Bioinformatics 2004, 20 (9) 1466-7 (Pubitemid 38931421)
    • (2004) Bioinformatics , vol.20 , Issue.9 , pp. 1466-1467
    • Craig, R.1    Beavis, R.C.2
  • 32
    • 24044491542 scopus 로고    scopus 로고
    • Comprehensive analysis of a multidimensional liquid chromatography mass spectrometry dataset acquired on a quadrupole selecting, quadrupole collision cells, time-of-flight mass spectrometer: II New developments in protein prospector allow for reliable and comprehensive automatic analysis of large datasets
    • DOI 10.1074/mcp.D500002-MCP200
    • Chalkley, R. J.; Baker, P. R.; Huang, L.; Hansen, K. C.; Allen, N. P.; Rexach, M.; Burlingame, A. L. Comprehensive analysis of a multidimensional liquid chromatography mass spectrometry dataset acquired on a quadrupole selecting, quadrupole collision cell, time-of-flight mass spectrometer: II. New developments in Protein Prospector allow for reliable and comprehensive automatic analysis of large datasets Mol. Cell. Proteomics 2005, 4 (8) 1194-204 (Pubitemid 41223378)
    • (2005) Molecular and Cellular Proteomics , vol.4 , Issue.8 , pp. 1194-1204
    • Chalkley, R.J.1    Baker, P.R.2    Huang, L.3    Hansen, K.C.4    Allen, N.P.5    Rexach, M.6    Burlingame, A.L.7
  • 34
    • 84984933087 scopus 로고    scopus 로고
    • The SCX/IMAC enrichment approach for global phosphorylation analysis by mass spectrometry
    • Villen, J.; Gygi, S. P. The SCX/IMAC enrichment approach for global phosphorylation analysis by mass spectrometry Nat. Protoc. 2008, 3 (10) 1630-8
    • (2008) Nat. Protoc. , vol.3 , Issue.10 , pp. 1630-8
    • Villen, J.1    Gygi, S.P.2
  • 35
    • 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.; Kristensen, D. B.; Steen, H.; Pandey, A.; Mann, M. Stable isotope labeling by amino acids in cell culture, SILAC, as a simple and accurate approach to expression proteomics Mol. Cell. Proteomics 2002, 1 (5) 376-86
    • (2002) Mol. Cell. Proteomics , vol.1 , Issue.5 , pp. 376-86
    • Ong, S.E.1    Blagoev, B.2    Kratchmarova, I.3    Kristensen, D.B.4    Steen, H.5    Pandey, A.6    Mann, M.7
  • 36
    • 0036428393 scopus 로고    scopus 로고
    • Amino acid residue specific stable isotope labeling for quantitative proteomics
    • DOI 10.1002/rcm.831
    • Zhu, H.; Pan, S.; Gu, S.; Bradbury, E. M.; Chen, X. Amino acid residue specific stable isotope labeling for quantitative proteomics Rapid Commun. Mass Spectrom. 2002, 16 (22) 2115-23 (Pubitemid 35340078)
    • (2002) Rapid Communications in Mass Spectrometry , vol.16 , Issue.22 , pp. 2115-2123
    • Zhu, H.1    Pan, S.2    Gu, S.3    Morton Bradbury, E.4    Chen, X.5
  • 37
    • 57449099865 scopus 로고    scopus 로고
    • MaxQuant enables high peptide identification rates, individualized p.p.b.-range mass accuracies and proteome-wide protein quantification
    • Cox, J.; Mann, M. MaxQuant enables high peptide identification rates, individualized p.p.b.-range mass accuracies and proteome-wide protein quantification Nat. Biotechnol. 2008, 26 (12) 1367-72
    • (2008) Nat. Biotechnol. , vol.26 , Issue.12 , pp. 1367-72
    • Cox, J.1    Mann, M.2
  • 38
    • 35649011957 scopus 로고    scopus 로고
    • Exploring the sialiome using titanium dioxide chromatography and mass spectrometry
    • DOI 10.1074/mcp.M700086-MCP200
    • Larsen, M. R.; Jensen, S. S.; Jakobsen, L. A.; Heegaard, N. H. Exploring the sialiome using titanium dioxide chromatography and mass spectrometry Mol. Cell. Proteomics 2007, 6 (10) 1778-87 (Pubitemid 350031679)
    • (2007) Molecular and Cellular Proteomics , vol.6 , Issue.10 , pp. 1778-1787
    • Larsen, M.R.1    Jensen, S.S.2    Jakobsen, L.A.3    Heegaard, N.H.H.4
  • 39
    • 36248934589 scopus 로고    scopus 로고
    • Evaluation of the impact of some experimental procedures on different phosphopeptide enrichment techniques
    • DOI 10.1002/rcm.3254
    • Jensen, S. S.; Larsen, M. R. Evaluation of the impact of some experimental procedures on different phosphopeptide enrichment techniques Rapid Commun. Mass Spectrom. 2007, 21 (22) 3635-45 (Pubitemid 350124632)
    • (2007) Rapid Communications in Mass Spectrometry , vol.21 , Issue.22 , pp. 3635-3645
    • Jensen, S.S.1    Larsen, M.R.2
  • 40
    • 3042824849 scopus 로고    scopus 로고
    • A neutral loss activation method for improved phosphopeptide sequence analysis by quadrupole ion trap mass spectrometry
    • DOI 10.1021/ac0497104
    • Schroeder, M. J.; Shabanowitz, J.; Schwartz, J. C.; Hunt, D. F.; Coon, J. J. A neutral loss activation method for improved phosphopeptide sequence analysis by quadrupole ion trap mass spectrometry Anal. Chem. 2004, 76 (13) 3590-8 (Pubitemid 38868819)
    • (2004) Analytical Chemistry , vol.76 , Issue.13 , pp. 3590-3598
    • Schroeder, M.J.1    Shabanowitz, J.2    Schwartz, J.C.3    Hunt, D.F.4    Coon, J.J.5
  • 42
    • 67649400942 scopus 로고    scopus 로고
    • A practical guide to the MaxQuant computational platform for SILAC-based quantitative proteomics
    • Cox, J.; Matic, I.; Hilger, M.; Nagaraj, N.; Selbach, M.; Olsen, J. V.; Mann, M. A practical guide to the MaxQuant computational platform for SILAC-based quantitative proteomics Nat. Protoc. 2009, 4 (5) 698-705
    • (2009) Nat. Protoc. , vol.4 , Issue.5 , pp. 698-705
    • Cox, J.1    Matic, I.2    Hilger, M.3    Nagaraj, N.4    Selbach, M.5    Olsen, J.V.6    Mann, M.7
  • 43
    • 33847630405 scopus 로고    scopus 로고
    • Target-decoy search strategy for increased confidence in large-scale protein identifications by mass spectrometry
    • DOI 10.1038/nmeth1019, PII NMETH1019
    • Elias, J. E.; Gygi, S. P. Target-decoy search strategy for increased confidence in large-scale protein identifications by mass spectrometry Nat. Methods 2007, 4 (3) 207-14 (Pubitemid 46358868)
    • (2007) Nature Methods , vol.4 , Issue.3 , pp. 207-214
    • Elias, J.E.1    Gygi, S.P.2
  • 44
    • 0020039866 scopus 로고
    • Isolation of intracellular membranes by means of sodium carbonate treatment: Application to endoplasmic reticulum
    • DOI 10.1083/jcb.93.1.97
    • Fujiki, Y.; Hubbard, A. L.; Fowler, S.; Lazarow, P. B. Isolation of intracellular membranes by means of sodium carbonate treatment: application to endoplasmic reticulum J. Cell Biol. 1982, 93 (1) 97-102 (Pubitemid 12117045)
    • (1982) Journal of Cell Biology , vol.93 , Issue.1 , pp. 97-102
    • Fujiki, Y.1    Hubbard, A.L.2    Fowler, S.3    Lazarow, P.B.4
  • 45
    • 33947603651 scopus 로고    scopus 로고
    • Evaluation and optimization of ZIC-HILIC-RP as an alternative MudPIT strategy
    • DOI 10.1021/pr060589m
    • Boersema, P. J.; Divecha, N.; Heck, A. J.; Mohammed, S. Evaluation and optimization of ZIC-HILIC-RP as an alternative MudPIT strategy J. Proteome Res. 2007, 6 (3) 937-46 (Pubitemid 46480458)
    • (2007) Journal of Proteome Research , vol.6 , Issue.3 , pp. 937-946
    • Boersema, P.J.1    Divecha, N.2    Heck, A.J.R.3    Mohammed, S.4
  • 46
    • 0028279520 scopus 로고
    • Prediction of transmembrane segments in proteins utilising multiple sequence alignments
    • DOI 10.1006/jmbi.1994.1220
    • Persson, B.; Argos, P. Prediction of transmembrane segments in proteins utilising multiple sequence alignments J. Mol. Biol. 1994, 237 (2) 182-92 (Pubitemid 24182232)
    • (1994) Journal of Molecular Biology , vol.237 , Issue.2 , pp. 182-192
    • Persson, B.1    Argos, P.2
  • 47
    • 84859469968 scopus 로고    scopus 로고
    • According to the protocol: "Filter Aided Sample Preparation (FASP) Method"
    • According to the protocol: "Filter Aided Sample Preparation (FASP) Method". http://www.biochem.mpg.de/mann/approaches/fasp/index.html
  • 49
    • 77952379073 scopus 로고    scopus 로고
    • An integrated global strategy for cell lysis, fractionation, enrichment and mass spectrometric analysis of phosphorylated peptides
    • Rogers, L. D.; Fang, Y.; Foster, L. J. An integrated global strategy for cell lysis, fractionation, enrichment and mass spectrometric analysis of phosphorylated peptides Mol. Biosyst. 2010, 6 (5) 822-9
    • (2010) Mol. Biosyst. , vol.6 , Issue.5 , pp. 822-9
    • Rogers, L.D.1    Fang, Y.2    Foster, L.J.3
  • 50
    • 33847616949 scopus 로고    scopus 로고
    • Reproducible isolation of distinct, overlapping segments of the phosphoproteome
    • DOI 10.1038/nmeth1005, PII NMETH1005
    • Bodenmiller, B.; Mueller, L. N.; Mueller, M.; Domon, B.; Aebersold, R. Reproducible isolation of distinct, overlapping segments of the phosphoproteome Nat. Methods 2007, 4 (3) 231-7 (Pubitemid 46358873)
    • (2007) Nature Methods , vol.4 , Issue.3 , pp. 231-237
    • Bodenmiller, B.1    Mueller, L.N.2    Mueller, M.3    Domon, B.4    Aebersold, R.5
  • 51
    • 79952431239 scopus 로고    scopus 로고
    • The problem with Peptide presumption and low mascot scoring
    • Cooper, B. The problem with Peptide presumption and low mascot scoring J. Proteome Res. 2011, 10 (3) 1432-5
    • (2011) J. Proteome Res. , vol.10 , Issue.3 , pp. 1432-5
    • Cooper, B.1
  • 52
    • 79951925573 scopus 로고    scopus 로고
    • The potential cost of high-throughput proteomics
    • White, F. M. The potential cost of high-throughput proteomics Sci. Signal. 2011, 4, 160
    • (2011) Sci. Signal. , vol.4 , pp. 160
    • White, F.M.1
  • 53
    • 78649715058 scopus 로고    scopus 로고
    • Evaluation of data analysis strategies for improved mass spectrometry-based phosphoproteomics
    • Savitski, M. M.; Scholten, A.; Sweetman, G.; Mathieson, T.; Bantscheff, M. Evaluation of data analysis strategies for improved mass spectrometry-based phosphoproteomics Anal. Chem. 2010, 82 (23) 9843-9
    • (2010) Anal. Chem. , vol.82 , Issue.23 , pp. 9843-9
    • Savitski, M.M.1    Scholten, A.2    Sweetman, G.3    Mathieson, T.4    Bantscheff, M.5
  • 54
    • 67650725988 scopus 로고    scopus 로고
    • Computational principles of determining and improving mass precision and accuracy for proteome measurements in an Orbitrap
    • Cox, J.; Mann, M. Computational principles of determining and improving mass precision and accuracy for proteome measurements in an Orbitrap J. Am. Soc. Mass Spectrom. 2009, 20 (8) 1477-85
    • (2009) J. Am. Soc. Mass Spectrom. , vol.20 , Issue.8 , pp. 1477-85
    • Cox, J.1    Mann, M.2
  • 58
    • 0034644537 scopus 로고    scopus 로고
    • Ras and Rho GTPases: A family reunion
    • Bar-Sagi, D.; Hall, A. Ras and Rho GTPases: a family reunion Cell 2000, 103 (2) 227-38
    • (2000) Cell , vol.103 , Issue.2 , pp. 227-38
    • Bar-Sagi, D.1    Hall, A.2
  • 59
    • 0029791452 scopus 로고    scopus 로고
    • Identification of the mitogen-activated protein kinase phosphorylation sites on human Sos1 that regulate interaction with Grb2
    • Corbalan-Garcia, S.; Yang, S. S.; Degenhardt, K. R.; Bar-Sagi, D. Identification of the mitogen-activated protein kinase phosphorylation sites on human Sos1 that regulate interaction with Grb2 Mol. Cell. Biol. 1996, 16 (10) 5674-82 (Pubitemid 26315087)
    • (1996) Molecular and Cellular Biology , vol.16 , Issue.10 , pp. 5674-5682
    • Corbalan-Garcia, S.1    Yang, S.-S.2    Degenhardt, K.R.3    Bar-Sagi, D.4
  • 60
    • 0024023873 scopus 로고
    • Egf binding to its receptor triggers a rapid tyrosine phosphorylation of the erbB-2 protein in the mammary tumor cell line SK-BR-3
    • King, C. R.; Borrello, I.; Bellot, F.; Comoglio, P.; Schlessinger, J. Egf binding to its receptor triggers a rapid tyrosine phosphorylation of the erbB-2 protein in the mammary tumor cell line SK-BR-3 Embo J. 1988, 7 (6) 1647-51
    • (1988) Embo J. , vol.7 , Issue.6 , pp. 1647-51
    • King, C.R.1    Borrello, I.2    Bellot, F.3    Comoglio, P.4    Schlessinger, J.5
  • 61
    • 0028021566 scopus 로고
    • The mechanism by which epidermal growth factor inhibits glycogen synthase kinase 3 in A431 cells
    • Saito, Y.; Vandenheede, J. R.; Cohen, P. The mechanism by which epidermal growth factor inhibits glycogen synthase kinase 3 in A431 cells Biochem. J. 1994, 303 (Pt 1) 27-31 (Pubitemid 24302894)
    • (1994) Biochemical Journal , vol.303 , Issue.1 , pp. 27-31
    • Saito, Y.1    Vandenheede, J.R.2    Cohen, P.3
  • 63
    • 0033634977 scopus 로고    scopus 로고
    • TAB2, a novel adaptor protein, mediates activation of TAK1MAPKKK by linking TAK1 to TRAF6 in the IL-1 signal transduction pathway
    • Takaesu, G.; Kishida, S.; Hiyama, A.; Yamaguchi, K.; Shibuya, H.; Irie, K.; Ninomiya-Tsuji, J.; Matsumoto, K. TAB2, a novel adaptor protein, mediates activation of TAK1MAPKKK by linking TAK1 to TRAF6 in the IL-1 signal transduction pathway Mol. Cell 2000, 5 (4) 649-58
    • (2000) Mol. Cell , vol.5 , Issue.4 , pp. 649-58
    • Takaesu, G.1    Kishida, S.2    Hiyama, A.3    Yamaguchi, K.4    Shibuya, H.5    Irie, K.6    Ninomiya-Tsuji, J.7    Matsumoto, K.8
  • 66
    • 77955373300 scopus 로고    scopus 로고
    • 14-3-3gamma induces oncogenic transformation by stimulating MAP kinase and PI3K signaling
    • Radhakrishnan, V. M.; Martinez, J. D. 14-3-3gamma induces oncogenic transformation by stimulating MAP kinase and PI3K signaling PLoS One 2010, 5 (7) e11433
    • (2010) PLoS One , vol.5 , Issue.7 , pp. 11433
    • Radhakrishnan, V.M.1    Martinez, J.D.2


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