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Volumn 20, Issue 6, 2009, Pages 915-926

Reactive Landing of Gas-Phase Ions as a Tool for the Fabrication of Metal Oxide Surfaces for In Situ Phosphopeptide Enrichment

Author keywords

[No Author keywords available]

Indexed keywords

ALKOXIDES; COMPLEX PEPTIDE MIXTURES; ELECTROSPRAY DEPOSITIONS; GAS-PHASE IONS; HAFNIUM OXIDES; HIGH THROUGHPUT SCREENINGS; IN-SITU; MATRIX-ASSISTED LASER DESORPTION IONIZATIONS; METAL ALKOXIDES; METAL OXIDE COATINGS; METAL OXIDE LAYERS; METAL OXIDES; METAL SURFACES; METAL-OXIDE SURFACES; MORPHOLOGICAL CHARACTERISTICS; MORPHOLOGICAL CHARACTERIZATIONS; PHOSPHOPEPTIDE ENRICHMENTS; PHOSPHOPEPTIDES; PHOSPHORYLATION SITES; SEM ANALYSIS; SEM IMAGE ANALYSIS; STAINLESS STEEL SURFACES; SURFACE DURABILITIES; TITANIA;

EID: 65549095831     PISSN: 10440305     EISSN: None     Source Type: Journal    
DOI: 10.1016/j.jasms.2009.01.006     Document Type: Article
Times cited : (26)

References (40)
  • 1
    • 0034614490 scopus 로고    scopus 로고
    • Signaling: 2000 and Beyond
    • Hunter T. Signaling: 2000 and Beyond. Cell 100 (2000) 113-127
    • (2000) Cell , vol.100 , pp. 113-127
    • Hunter, T.1
  • 4
    • 52049110575 scopus 로고    scopus 로고
    • Advances in the Analysis of Protein Phosphorylation
    • Paradela A., and Albar J.P. Advances in the Analysis of Protein Phosphorylation. J. Proteome Res. 7 (2008) 1809-1818
    • (2008) J. Proteome Res. , vol.7 , pp. 1809-1818
    • Paradela, A.1    Albar, J.P.2
  • 5
    • 33745960413 scopus 로고    scopus 로고
    • Proteomics Technology in Systems Biology
    • Smith J.C., and Figeys D. Proteomics Technology in Systems Biology. Mol. BioSyst. 2 (2006) 364-370
    • (2006) Mol. BioSyst. , vol.2 , pp. 364-370
    • Smith, J.C.1    Figeys, D.2
  • 6
    • 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., and Mann M. Stable Isotope Labeling by Amino Acids in Cell Culture, SILAC, as a Simple and Accurate Approach to Expression Proteomics. Mol. Cell Proteomics 1 (2002) 376-386
    • (2002) Mol. Cell Proteomics , vol.1 , pp. 376-386
    • Ong, S.E.1    Blagoev, B.2    Kratchmarova, I.3    Kristensen, D.B.4    Steen, H.5    Pandey, A.6    Mann, M.7
  • 7
    • 0032875697 scopus 로고    scopus 로고
    • Quantitative Analysis of Complex Protein Mixtures Using Isotope Coded Affinity Tags
    • Gygi S.P., Rist B., Gerber S.A., Tureček F., Gelb M.H., and Aebersold R. Quantitative Analysis of Complex Protein Mixtures Using Isotope Coded Affinity Tags. Nat. Biotechnol. 17 (1999) 994-999
    • (1999) Nat. Biotechnol. , vol.17 , pp. 994-999
    • Gygi, S.P.1    Rist, B.2    Gerber, S.A.3    Tureček, F.4    Gelb, M.H.5    Aebersold, R.6
  • 8
    • 0035356565 scopus 로고    scopus 로고
    • Phosphoprotein Isotope-Coded Affinity Tag Approach for Isolating and Quantitating Phosphopeptides in Proteome-Wide Analyses
    • Goshe M.B., Conrads T.P., Panisko E.A., Angell N.H., Veenstra T.D., and Smith R.D. Phosphoprotein Isotope-Coded Affinity Tag Approach for Isolating and Quantitating Phosphopeptides in Proteome-Wide Analyses. Anal. Chem. 73 (2001) 2578-2586
    • (2001) Anal. Chem. , vol.73 , pp. 2578-2586
    • Goshe, M.B.1    Conrads, T.P.2    Panisko, E.A.3    Angell, N.H.4    Veenstra, T.D.5    Smith, R.D.6
  • 9
    • 33748483856 scopus 로고    scopus 로고
    • Metal Affinity Capture Tandem Mass Spectrometry for the Selective Detection of Phosphopeptides
    • Blacken G.B., Gelb M.H., and Tureček F. Metal Affinity Capture Tandem Mass Spectrometry for the Selective Detection of Phosphopeptides. Anal. Chem. 78 (2006) 6065-6073
    • (2006) Anal. Chem. , vol.78 , pp. 6065-6073
    • Blacken, G.B.1    Gelb, M.H.2    Tureček, F.3
  • 10
    • 49549102686 scopus 로고    scopus 로고
    • Gallium Metal Affinity Capture Tandem Mass Spectrometry for the Selective Detection of Phosphopeptides in Complex Mixtures
    • Blacken G.R., Sadilek M., and Tureček F. Gallium Metal Affinity Capture Tandem Mass Spectrometry for the Selective Detection of Phosphopeptides in Complex Mixtures. J. Mass Spectrom. 43 (2008) 1072-1080
    • (2008) J. Mass Spectrom. , vol.43 , pp. 1072-1080
    • Blacken, G.R.1    Sadilek, M.2    Tureček, F.3
  • 11
    • 0030218817 scopus 로고    scopus 로고
    • Selective Detection and Sequencing of Phosphopeptides at the Femtomole Level by Mass Spectrometry
    • Carr S.A., Huddleston M.J., and Annan R.S. Selective Detection and Sequencing of Phosphopeptides at the Femtomole Level by Mass Spectrometry. Anal. Biochem. 239 (1996) 180-192
    • (1996) Anal. Biochem. , vol.239 , pp. 180-192
    • Carr, S.A.1    Huddleston, M.J.2    Annan, R.S.3
  • 12
    • 3042824849 scopus 로고    scopus 로고
    • A Neutral Loss Activation Method for Improved Phosphopeptide Sequence Analysis by Quadrupole Ion Trap Mass Spectrometry
    • Schroeder M.J., Shabanowitz J., Schwartz J.C., Hunt D.F., and Coon J.C. A Neutral Loss Activation Method for Improved Phosphopeptide Sequence Analysis by Quadrupole Ion Trap Mass Spectrometry. Anal. Chem. 76 (2004) 3590-3598
    • (2004) Anal. Chem. , vol.76 , pp. 3590-3598
    • Schroeder, M.J.1    Shabanowitz, J.2    Schwartz, J.C.3    Hunt, D.F.4    Coon, J.C.5
  • 13
    • 2942692932 scopus 로고    scopus 로고
    • Analysis of Protein Phosphorylation by Hypothesis-Driven Multiple-Stage Mass sSectrometry
    • Chang E.J., Archambault V., McLachlin D.T., Krutchinsky A.N., and Chait B.T. Analysis of Protein Phosphorylation by Hypothesis-Driven Multiple-Stage Mass sSectrometry. Anal. Chem. 76 (2004) 4472-4483
    • (2004) Anal. Chem. , vol.76 , pp. 4472-4483
    • Chang, E.J.1    Archambault, V.2    McLachlin, D.T.3    Krutchinsky, A.N.4    Chait, B.T.5
  • 14
    • 0037067094 scopus 로고    scopus 로고
    • Gas-Phase Ion Unimolecular Dissociation for Rapid Phosphopeptide Mapping by IRMPD in a Penning Ion Trap: An Energetically Favored Process
    • Flora F.W., and Muddiman D.C. Gas-Phase Ion Unimolecular Dissociation for Rapid Phosphopeptide Mapping by IRMPD in a Penning Ion Trap: An Energetically Favored Process. J. Am. Chem. Soc. 124 (2002) 6546-6547
    • (2002) J. Am. Chem. Soc. , vol.124 , pp. 6546-6547
    • Flora, F.W.1    Muddiman, D.C.2
  • 15
    • 24644456406 scopus 로고    scopus 로고
    • Differentiation of Phosphorylated and Unphosphorylated Peptides by High-Performance Liquid Chromatography-Electrospray Ionization-Infrared Multiphoton Dissociation in a Quadrupole Ion Trap
    • Crowe M.C., and Brodbelt J.S. Differentiation of Phosphorylated and Unphosphorylated Peptides by High-Performance Liquid Chromatography-Electrospray Ionization-Infrared Multiphoton Dissociation in a Quadrupole Ion Trap. Anal. Chem. 77 (2005) 5726-5734
    • (2005) Anal. Chem. , vol.77 , pp. 5726-5734
    • Crowe, M.C.1    Brodbelt, J.S.2
  • 18
    • 0033565503 scopus 로고    scopus 로고
    • Immobilized Gallium(III) Affinity Chromatography of Phosphopeptides
    • Posewitz M.C., and Tempst P. Immobilized Gallium(III) Affinity Chromatography of Phosphopeptides. Anal. Chem. 71 (1999) 2883-2892
    • (1999) Anal. Chem. , vol.71 , pp. 2883-2892
    • Posewitz, M.C.1    Tempst, P.2
  • 19
    • 33645566839 scopus 로고    scopus 로고
    • Characterizing Phosphoproteins and Phosphoproteomes Using Mass Spectroscopy
    • Goshe M.B. Characterizing Phosphoproteins and Phosphoproteomes Using Mass Spectroscopy. Brief. Funct. Genomic. Proteomic. 4 (2006) 363-376
    • (2006) Brief. Funct. Genomic. Proteomic. , vol.4 , pp. 363-376
    • Goshe, M.B.1
  • 20
    • 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
    • Pinkse M.W., Uitto P.M., Hilhorst M.J., Ooms B., and 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. 76 (2004) 3935-3943
    • (2004) Anal. Chem. , vol.76 , pp. 3935-3943
    • Pinkse, M.W.1    Uitto, P.M.2    Hilhorst, M.J.3    Ooms, B.4    Heck, A.J.5
  • 22
    • 33645217942 scopus 로고    scopus 로고
    • Selective Zirconium Dioxide-Based Enrichment of Phosphorylated Peptides for Mass Spectrometric Analysis
    • Kweon H.K., and Håkansson K. Selective Zirconium Dioxide-Based Enrichment of Phosphorylated Peptides for Mass Spectrometric Analysis. Anal. Chem. 78 (2006) 1743-1749
    • (2006) Anal. Chem. , vol.78 , pp. 1743-1749
    • Kweon, H.K.1    Håkansson, K.2
  • 23
    • 24944519450 scopus 로고    scopus 로고
    • Highly Selective Enrichment of Phosphorylated Peptides from Peptide Mixtures Using Titanium Dioxide Microcolumns
    • Larsen M.R., Thinghom T.E., Jensen O.N., Roepstorff P., and Jorgensen T.J.D. Highly Selective Enrichment of Phosphorylated Peptides from Peptide Mixtures Using Titanium Dioxide Microcolumns. Mol. Cell Proteomics 4 (2005) 873-886
    • (2005) Mol. Cell Proteomics , vol.4 , pp. 873-886
    • Larsen, M.R.1    Thinghom, T.E.2    Jensen, O.N.3    Roepstorff, P.4    Jorgensen, T.J.D.5
  • 24
    • 33847616949 scopus 로고    scopus 로고
    • Reproducible Isolation of Distinct, Overlapping Segments of the Phosphoproteome
    • Bodenmiller B., Mueller L.N., Mueller M., Domon B., and Aebersold R. Reproducible Isolation of Distinct, Overlapping Segments of the Phosphoproteome. Nat. Methods 4 (2007) 231-237
    • (2007) Nat. Methods , vol.4 , pp. 231-237
    • Bodenmiller, B.1    Mueller, L.N.2    Mueller, M.3    Domon, B.4    Aebersold, R.5
  • 25
    • 36248934589 scopus 로고    scopus 로고
    • Evaluation of the Impact of Some Experimental Procedures on Different Phosphopeptide Enrichment Techniques
    • Jensen S.S., and Larsen M.R. Evaluation of the Impact of Some Experimental Procedures on Different Phosphopeptide Enrichment Techniques. Rapid Commun. Mass Spectrom. 21 (2007) 3635-3645
    • (2007) Rapid Commun. Mass Spectrom. , vol.21 , pp. 3635-3645
    • Jensen, S.S.1    Larsen, M.R.2
  • 26
    • 34547164417 scopus 로고    scopus 로고
    • In Situ Enrichment of Phosphopeptides on MALDI Plates Functionalized by Reactive Landing of Zirconium(IV)-n-Propoxide Ions
    • Blacken G.R., Volny M.E., Vaisar T., Sadilek M., and Tureček F. In Situ Enrichment of Phosphopeptides on MALDI Plates Functionalized by Reactive Landing of Zirconium(IV)-n-Propoxide Ions. Anal. Chem. 79 (2007) 5449-5456
    • (2007) Anal. Chem. , vol.79 , pp. 5449-5456
    • Blacken, G.R.1    Volny, M.E.2    Vaisar, T.3    Sadilek, M.4    Tureček, F.5
  • 29
    • 44449124267 scopus 로고    scopus 로고
    • Combining Protein-Based IMAC, Peptide-Based IMAC, and MudPIT for Efficient Phosphoproteomic Analysis
    • Cantin G.T., Yi W., Lu B., Park S.K., Xu T., Lee J.-D., and Yates III J.R. Combining Protein-Based IMAC, Peptide-Based IMAC, and MudPIT for Efficient Phosphoproteomic Analysis. J. Proteome Res. 7 (2008) 1346-1351
    • (2008) J. Proteome Res. , vol.7 , pp. 1346-1351
    • Cantin, G.T.1    Yi, W.2    Lu, B.3    Park, S.K.4    Xu, T.5    Lee, J.-D.6    Yates III, J.R.7
  • 31
    • 23044496367 scopus 로고    scopus 로고
    • Preparative Soft and Reactive Landing of Gas-Phase Ions on Plasma-Treated Metal Surfaces
    • Volny M., Elam W.T., Ratner B.D., and Tureček F. Preparative Soft and Reactive Landing of Gas-Phase Ions on Plasma-Treated Metal Surfaces. Anal. Chem. 77 (2005) 4846-4853
    • (2005) Anal. Chem. , vol.77 , pp. 4846-4853
    • Volny, M.1    Elam, W.T.2    Ratner, B.D.3    Tureček, F.4
  • 32
    • 23044506207 scopus 로고    scopus 로고
    • Preparative Soft and Reactive Landing of Multiply Charged Protein Ions on a Plasma-Treated Metal Surface
    • Volny M., Elam W.T., Branca A., Ratner B.D., and Tureček F. Preparative Soft and Reactive Landing of Multiply Charged Protein Ions on a Plasma-Treated Metal Surface. Anal. Chem. 77 (2005) 4890-4896
    • (2005) Anal. Chem. , vol.77 , pp. 4890-4896
    • Volny, M.1    Elam, W.T.2    Branca, A.3    Ratner, B.D.4    Tureček, F.5
  • 33
    • 33846953198 scopus 로고    scopus 로고
    • Enhanced In-Vitro Blood Compatibility of 316L Stainless Steel Surfaces by Reactive Landing of Hyaluronan Ions
    • Volny M., Elam W.T., Ratner B.D., and Tureček F.J. Enhanced In-Vitro Blood Compatibility of 316L Stainless Steel Surfaces by Reactive Landing of Hyaluronan Ions. J. Biomed. Mater. Res. B 80B (2007) 505-510
    • (2007) J. Biomed. Mater. Res. B , vol.80 B , pp. 505-510
    • Volny, M.1    Elam, W.T.2    Ratner, B.D.3    Tureček, F.J.4
  • 34
    • 0344131157 scopus 로고    scopus 로고
    • Salamone J.C. (Ed), Chemical Rubber Corp, Boca Raton, FL
    • Ratner B.D. In: Salamone J.C. (Ed). Polymeric Materials Encyclopedia Vol. 11 (1996), Chemical Rubber Corp, Boca Raton, FL 1006
    • (1996) Polymeric Materials Encyclopedia , vol.11 , pp. 1006
    • Ratner, B.D.1
  • 35
    • 0026568155 scopus 로고
    • Molecular Cloning and Expression of Chicken c-Src Kinase: Lack of Stable Association with c-Src Protein
    • Sabe H., Knudsen B., Okada M., Nada S., Nakagawa H., and Hanafusa H. Molecular Cloning and Expression of Chicken c-Src Kinase: Lack of Stable Association with c-Src Protein. Proc. Natl. Acad. Sci. U. S. A. 89 (1992) 2190-2194
    • (1992) Proc. Natl. Acad. Sci. U. S. A. , vol.89 , pp. 2190-2194
    • Sabe, H.1    Knudsen, B.2    Okada, M.3    Nada, S.4    Nakagawa, H.5    Hanafusa, H.6
  • 38
    • 0028828950 scopus 로고
    • Autophosphorylation of Purified c-Src at its Primary Negative Regulation Site
    • Osusky M., Taylor S.J., and Shalloway D. Autophosphorylation of Purified c-Src at its Primary Negative Regulation Site. J. Biol. Chem. 270 (1995) 25729-25734
    • (1995) J. Biol. Chem. , vol.270 , pp. 25729-25734
    • Osusky, M.1    Taylor, S.J.2    Shalloway, D.3
  • 39
    • 0032563970 scopus 로고    scopus 로고
    • Autophosphorylation of Src and Yes Blocks Their Inactivation by Csk Phosphorylation
    • Sun G., Sharma A.K., and Budde R.J.A. Autophosphorylation of Src and Yes Blocks Their Inactivation by Csk Phosphorylation. Oncogene 17 (1998) 1587-1595
    • (1998) Oncogene , vol.17 , pp. 1587-1595
    • Sun, G.1    Sharma, A.K.2    Budde, R.J.A.3
  • 40
    • 65549142013 scopus 로고    scopus 로고
    • For example, see Applied Biosystems application note 114AP20-01 and ABS technical note 114TN49-02 at www.appliedbiosystems.com.
    • For example, see Applied Biosystems application note 114AP20-01 and ABS technical note 114TN49-02 at www.appliedbiosystems.com.


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