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Volumn 30, Issue 2, 2012, Pages 100-110

Platforms for enrichment of phosphorylated proteins and peptides in proteomics

Author keywords

[No Author keywords available]

Indexed keywords

ABSOLUTE QUANTIFICATION; AFFINITY REAGENTS; DYNAMIC PROCESS; HIGH-THROUGHPUT; MASS SPECTROMETRY ANALYSIS; METABOLIC DISORDERS; PHOSPHORYLATED PROTEINS; PROTEIN FUNCTIONS; PROTEIN PHOSPHORYLATION; PROTEOMIC STUDIES; PROTEOMICS; SIGNALING PATHWAYS; THERAPEUTIC TOOLS; UNDERLYING MECHANISM;

EID: 84856087985     PISSN: 01677799     EISSN: 18793096     Source Type: Journal    
DOI: 10.1016/j.tibtech.2011.07.004     Document Type: Review
Times cited : (81)

References (79)
  • 1
    • 61349179532 scopus 로고    scopus 로고
    • Phosphorylation analysis of primary human T lymphocytes using sequential IMAC and titanium oxide enrichment
    • Carrascal M., et al. Phosphorylation analysis of primary human T lymphocytes using sequential IMAC and titanium oxide enrichment. J. Proteome Res. 2008, 7:5167-5176.
    • (2008) J. Proteome Res. , vol.7 , pp. 5167-5176
    • Carrascal, M.1
  • 2
    • 63049113651 scopus 로고    scopus 로고
    • Analytical strategies for phosphoproteomics
    • Thingholm T.E., et al. Analytical strategies for phosphoproteomics. Proteomics 2009, 9:1451-1468.
    • (2009) Proteomics , vol.9 , pp. 1451-1468
    • Thingholm, T.E.1
  • 3
    • 52049110575 scopus 로고    scopus 로고
    • Advances in the analysis of protein phosphorylation
    • Paradela A., Albar J.P. Advances in the analysis of protein phosphorylation. J. Proteome Res. 2008, 7:1809-1818.
    • (2008) J. Proteome Res. , vol.7 , pp. 1809-1818
    • Paradela, A.1    Albar, J.P.2
  • 4
    • 67649213067 scopus 로고    scopus 로고
    • Phosphopeptide fragmentation and analysis by mass spectrometry
    • Boersema P.J., et al. Phosphopeptide fragmentation and analysis by mass spectrometry. J. Mass Spectrom. 2009, 44:861-878.
    • (2009) J. Mass Spectrom. , vol.44 , pp. 861-878
    • Boersema, P.J.1
  • 5
    • 79955792471 scopus 로고    scopus 로고
    • Tandem mass spectrometry strategies for phosphoproteome analysis
    • Palumbo A.M., et al. Tandem mass spectrometry strategies for phosphoproteome analysis. Mass Spectrom. Rev. 2011, 30:600-625.
    • (2011) Mass Spectrom. Rev. , vol.30 , pp. 600-625
    • Palumbo, A.M.1
  • 6
    • 55849118087 scopus 로고    scopus 로고
    • Quantitative phosphoproteomics by mass spectrometry: past, present, and future
    • Nita-Lazar A., et al. Quantitative phosphoproteomics by mass spectrometry: past, present, and future. Proteomics 2008, 8:4433-4443.
    • (2008) Proteomics , vol.8 , pp. 4433-4443
    • Nita-Lazar, A.1
  • 7
    • 34250641161 scopus 로고    scopus 로고
    • High-throughput phosphotyrosine profi{ligature}ling using SH2 domains
    • Machida K., et al. High-throughput phosphotyrosine profi{ligature}ling using SH2 domains. Mol. Cell 2007, 26:899-915.
    • (2007) Mol. Cell , vol.26 , pp. 899-915
    • Machida, K.1
  • 8
    • 38549086310 scopus 로고    scopus 로고
    • PepCyber:P-PEP: a database of human protein-protein interactions mediated by phosphoprotein-binding domains
    • Gong W.M., et al. PepCyber:P-PEP: a database of human protein-protein interactions mediated by phosphoprotein-binding domains. Nucleic Acids Res. 2008, 36:D679-D683.
    • (2008) Nucleic Acids Res. , vol.36
    • Gong, W.M.1
  • 9
    • 25144501476 scopus 로고    scopus 로고
    • Lessons from nature: on the molecular recognition elements of the phosphoprotein binding-domains
    • Roque A.C.A., Lowe C.R. Lessons from nature: on the molecular recognition elements of the phosphoprotein binding-domains. Biotechnol. Bioeng. 2005, 91:546-555.
    • (2005) Biotechnol. Bioeng. , vol.91 , pp. 546-555
    • Roque, A.C.A.1    Lowe, C.R.2
  • 10
    • 71549166323 scopus 로고    scopus 로고
    • Immobilized-metal affinity chromatography (IMAC): a review
    • Elsevier, R. Burgess, M. Deutscher (Eds.)
    • Block H., et al. Immobilized-metal affinity chromatography (IMAC): a review. Methods in Enzymology - Guide to Protein Purification 2009, 439-473. Elsevier. 2nd edn. R. Burgess, M. Deutscher (Eds.).
    • (2009) Methods in Enzymology - Guide to Protein Purification , pp. 439-473
    • Block, H.1
  • 11
    • 77949293684 scopus 로고    scopus 로고
    • Phosphopeptide enrichment using metal oxide affi{ligature}nity chromatography
    • Leitner A. Phosphopeptide enrichment using metal oxide affi{ligature}nity chromatography. Trends Anal. Chem. 2010, 29:177-185.
    • (2010) Trends Anal. Chem. , vol.29 , pp. 177-185
    • Leitner, A.1
  • 12
    • 0036198435 scopus 로고    scopus 로고
    • Phosphoproteome analysis by mass spectrometry and its application to Saccharomyces cerevisiae
    • Ficarro S.B., et al. Phosphoproteome analysis by mass spectrometry and its application to Saccharomyces cerevisiae. Nat. Biotechnol. 2002, 20:301-305.
    • (2002) Nat. Biotechnol. , vol.20 , pp. 301-305
    • Ficarro, S.B.1
  • 13
    • 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, 3:1630-1638.
    • (2008) Nat. Protoc. , vol.3 , pp. 1630-1638
    • Villen, J.1    Gygi, S.P.2
  • 14
    • 77950373315 scopus 로고    scopus 로고
    • Coupling strong anion-exchange monolithic capillary with MALDI-TOF MS for sensitive detection of phosphopeptides in protein digest
    • Dong M., et al. Coupling strong anion-exchange monolithic capillary with MALDI-TOF MS for sensitive detection of phosphopeptides in protein digest. Anal. Chem. 2010, 82:2907-2915.
    • (2010) Anal. Chem. , vol.82 , pp. 2907-2915
    • Dong, M.1
  • 15
    • 55549131141 scopus 로고    scopus 로고
    • Mass spectrometry analysis of phosphopeptides after peptide carboxy group derivatization
    • Xu Y., et al. Mass spectrometry analysis of phosphopeptides after peptide carboxy group derivatization. Anal. Chem. 2008, 80:8324-8328.
    • (2008) Anal. Chem. , vol.80 , pp. 8324-8328
    • Xu, Y.1
  • 16
    • 60649085411 scopus 로고    scopus 로고
    • Phosphopeptide enrichment on functionalized polymer microspots for MALDI-MS analysis
    • Wang W.-H., Bruening M.L. Phosphopeptide enrichment on functionalized polymer microspots for MALDI-MS analysis. Analyst 2009, 134:512-518.
    • (2009) Analyst , vol.134 , pp. 512-518
    • Wang, W.-H.1    Bruening, M.L.2
  • 17
    • 2642536746 scopus 로고    scopus 로고
    • Use of polymer-modified MALDI-MS probes to improve analyses of protein digests and DNA
    • Xu Y., et al. Use of polymer-modified MALDI-MS probes to improve analyses of protein digests and DNA. Anal. Chem. 2004, 76:3106-3111.
    • (2004) Anal. Chem. , vol.76 , pp. 3106-3111
    • Xu, Y.1
  • 18
    • 33644779778 scopus 로고    scopus 로고
    • Detection of phosphopeptides using Fe(III) nitrilotriacetate complexes immobilized on a MALDI plate
    • Dunn J.D., et al. Detection of phosphopeptides using Fe(III) nitrilotriacetate complexes immobilized on a MALDI plate. Anal. Chem. 2006, 78:1574-1580.
    • (2006) Anal. Chem. , vol.78 , pp. 1574-1580
    • Dunn, J.D.1
  • 19
    • 1442348860 scopus 로고    scopus 로고
    • Enhanced ionization of phosphorylated peptides during MALDI TOF mass spectrometry
    • Yang X., et al. Enhanced ionization of phosphorylated peptides during MALDI TOF mass spectrometry. Anal. Chem. 2004, 76:1532-1536.
    • (2004) Anal. Chem. , vol.76 , pp. 1532-1536
    • Yang, X.1
  • 20
    • 25444449827 scopus 로고    scopus 로고
    • Preparation and characterization of nitrilotriacetic-acid-terminated self-assembled monolayers on gold surfaces for matrix-assisted laser desorption ionization-time of flight-mass spectrometry analysis of proteins and peptides
    • Shen J., et al. Preparation and characterization of nitrilotriacetic-acid-terminated self-assembled monolayers on gold surfaces for matrix-assisted laser desorption ionization-time of flight-mass spectrometry analysis of proteins and peptides. Anal. Biochem. 2005, 345:258-269.
    • (2005) Anal. Biochem. , vol.345 , pp. 258-269
    • Shen, J.1
  • 21
    • 34948905273 scopus 로고    scopus 로고
    • Metal-chelating plastic MALDI (pMALDI) chips for the enhancement of phosphorylated-peptide/protein signals
    • Ibáñez A.J., et al. Metal-chelating plastic MALDI (pMALDI) chips for the enhancement of phosphorylated-peptide/protein signals. J. Proteome Res. 2007, 6:3842-3848.
    • (2007) J. Proteome Res. , vol.6 , pp. 3842-3848
    • Ibáñez, A.J.1
  • 22
    • 33646904825 scopus 로고    scopus 로고
    • Iminodiacetic acid derivatized porous silicon as a matrix support for sample pretreatment and matrix-assisted laser desorption/ionization time-of-fl{ligature}ight mass spectrometry analysis
    • Xu S., et al. Iminodiacetic acid derivatized porous silicon as a matrix support for sample pretreatment and matrix-assisted laser desorption/ionization time-of-fl{ligature}ight mass spectrometry analysis. Rapid Commun. Mass Spectrom. 2006, 20:1769-1775.
    • (2006) Rapid Commun. Mass Spectrom. , vol.20 , pp. 1769-1775
    • Xu, S.1
  • 23
    • 49449107225 scopus 로고    scopus 로고
    • Phosphopeptide enrichment using MALDI plates modifi{ligature}ed with high-capacity polymer brushes
    • Dunn J.D., et al. Phosphopeptide enrichment using MALDI plates modifi{ligature}ed with high-capacity polymer brushes. Anal. Chem. 2008, 80:5727-5735.
    • (2008) Anal. Chem. , vol.80 , pp. 5727-5735
    • Dunn, J.D.1
  • 24
    • 33748328051 scopus 로고    scopus 로고
    • Zirconium phosphonate-modified porous silicon for highly specific capture of phosphopeptides and MALDI-TOF MS analysis
    • Zhou H., et al. Zirconium phosphonate-modified porous silicon for highly specific capture of phosphopeptides and MALDI-TOF MS analysis. J. Proteome Res. 2006, 5:2431-2437.
    • (2006) J. Proteome Res. , vol.5 , pp. 2431-2437
    • Zhou, H.1
  • 25
    • 77956402498 scopus 로고    scopus 로고
    • Gum Arabic coated magnetic nanoparticles with affinity for antibodies
    • Batalha I.L., et al. Gum Arabic coated magnetic nanoparticles with affinity for antibodies. J. Mol. Recognit. 2010, 23:462-471.
    • (2010) J. Mol. Recognit. , vol.23 , pp. 462-471
    • Batalha, I.L.1
  • 26
    • 33846643023 scopus 로고    scopus 로고
    • Rapid enrichment of phosphopeptides and phosphoproteins from complex samples using magnetic particles coated with alumina as the concentrating probes for MALDI MS analysis
    • Chen C.-T., et al. Rapid enrichment of phosphopeptides and phosphoproteins from complex samples using magnetic particles coated with alumina as the concentrating probes for MALDI MS analysis. J. Proteome Res. 2007, 6:316-325.
    • (2007) J. Proteome Res. , vol.6 , pp. 316-325
    • Chen, C.-T.1
  • 27
    • 35648951727 scopus 로고    scopus 로고
    • Fe3O4@Al2O3 magnetic core-shell microspheres for rapid and highly specifi{ligature}c capture of phosphopeptides with mass spectrometry analysis
    • Li Y., et al. Fe3O4@Al2O3 magnetic core-shell microspheres for rapid and highly specifi{ligature}c capture of phosphopeptides with mass spectrometry analysis. J. Chromatogr. A 2007, 1172:57-71.
    • (2007) J. Chromatogr. A , vol.1172 , pp. 57-71
    • Li, Y.1
  • 28
    • 34247235764 scopus 로고    scopus 로고
    • Analysis of peptides and proteins affinity-bound to iron oxide nanoparticles by MALDI MS
    • Chang S.Y., et al. Analysis of peptides and proteins affinity-bound to iron oxide nanoparticles by MALDI MS. J. Am. Soc. Mass Spectrom. 2007, 18:910-918.
    • (2007) J. Am. Soc. Mass Spectrom. , vol.18 , pp. 910-918
    • Chang, S.Y.1
  • 29
    • 33847374660 scopus 로고    scopus 로고
    • Rapid enrichment of phosphopeptides from tryptic digests of proteins using iron oxide nanocomposites of magnetic particles coated with zirconia as the concentrating probes
    • Lo C.-Y., et al. Rapid enrichment of phosphopeptides from tryptic digests of proteins using iron oxide nanocomposites of magnetic particles coated with zirconia as the concentrating probes. J. Proteome Res. 2007, 887:893.
    • (2007) J. Proteome Res. , vol.887 , pp. 893
    • Lo, C.-Y.1
  • 30
    • 24944442458 scopus 로고    scopus 로고
    • Fe3O4/TiO2 Core/shell nanoparticles as affinity probes for the analysis of phosphopeptides using TiO2 surface-assisted laser desorption/ionization mass spectrometry
    • Chen C.-T., Chen Y.-C. Fe3O4/TiO2 Core/shell nanoparticles as affinity probes for the analysis of phosphopeptides using TiO2 surface-assisted laser desorption/ionization mass spectrometry. Anal. Chem. 2005, 77:5912-5919.
    • (2005) Anal. Chem. , vol.77 , pp. 5912-5919
    • Chen, C.-T.1    Chen, Y.-C.2
  • 31
    • 38949105850 scopus 로고    scopus 로고
    • Highly selective and rapid enrichment of phosphorylated peptides using gallium oxide-coated magnetic microspheres for MALDI-TOF-MS and nano-LC-ESI-MS/MS/MS analysis
    • Li Y., et al. Highly selective and rapid enrichment of phosphorylated peptides using gallium oxide-coated magnetic microspheres for MALDI-TOF-MS and nano-LC-ESI-MS/MS/MS analysis. Proteomics 2008, 8:238-249.
    • (2008) Proteomics , vol.8 , pp. 238-249
    • Li, Y.1
  • 32
    • 70349135032 scopus 로고    scopus 로고
    • Magnetically responsive Fe3O4@C@SnO2 core shell microspheres: synthesis, characterization and application in phosphoproteomics
    • Qi D., et al. Magnetically responsive Fe3O4@C@SnO2 core shell microspheres: synthesis, characterization and application in phosphoproteomics. J. Phys. Chem. C 2009, 113:15854-15861.
    • (2009) J. Phys. Chem. C , vol.113 , pp. 15854-15861
    • Qi, D.1
  • 33
    • 68549136509 scopus 로고    scopus 로고
    • Iron oxide/tantalum oxide core-shell magnetic nanoparticle-based microwave-assisted extraction for phosphopeptide enrichment from complex samples for MALDI MS analysis
    • Lin H.-Y., et al. Iron oxide/tantalum oxide core-shell magnetic nanoparticle-based microwave-assisted extraction for phosphopeptide enrichment from complex samples for MALDI MS analysis. Anal. Bioanal.Chem. 2009, 394:2129-2136.
    • (2009) Anal. Bioanal.Chem. , vol.394 , pp. 2129-2136
    • Lin, H.-Y.1
  • 34
    • 67649364169 scopus 로고    scopus 로고
    • Iron oxide/niobium oxide core-shell magnetic nanoparticle-based phosphopeptide enrichment from biological samples for MALDI MS analysis
    • Lin H., et al. Iron oxide/niobium oxide core-shell magnetic nanoparticle-based phosphopeptide enrichment from biological samples for MALDI MS analysis. J. Biomed. Nanotechnol. 2009, 5:215-223.
    • (2009) J. Biomed. Nanotechnol. , vol.5 , pp. 215-223
    • Lin, H.1
  • 35
    • 78049326007 scopus 로고    scopus 로고
    • Functional Fe3O4@ZnO magnetic nanoparticle-assisted enrichment and enzymatic digestion of phosphoproteins from saliva
    • Chen W.-Y., Chen Y.-C. Functional Fe3O4@ZnO magnetic nanoparticle-assisted enrichment and enzymatic digestion of phosphoproteins from saliva. Anal. Bioanal.Chem. 2010, 398:2049-2057.
    • (2010) Anal. Bioanal.Chem. , vol.398 , pp. 2049-2057
    • Chen, W.-Y.1    Chen, Y.-C.2
  • 36
    • 41549135248 scopus 로고    scopus 로고
    • Highly effi{ligature}cient enrichment of phosphopeptides by magnetic nanoparticles coated with zirconium phosphonate for phosphoproteome analysis
    • Wei J., et al. Highly effi{ligature}cient enrichment of phosphopeptides by magnetic nanoparticles coated with zirconium phosphonate for phosphoproteome analysis. Rapid Commun. Mass Spectrom. 2008, 22:1069-1080.
    • (2008) Rapid Commun. Mass Spectrom. , vol.22 , pp. 1069-1080
    • Wei, J.1
  • 37
    • 48349098876 scopus 로고    scopus 로고
    • The highly selective capture of phosphopeptides by zirconium phosphonate-modified magnetic nanoparticles for phosphoproteome analysis
    • Zhao L., et al. The highly selective capture of phosphopeptides by zirconium phosphonate-modified magnetic nanoparticles for phosphoproteome analysis. J. Am. Soc. Mass Spectrom. 2008, 19:1176-1186.
    • (2008) J. Am. Soc. Mass Spectrom. , vol.19 , pp. 1176-1186
    • Zhao, L.1
  • 38
    • 45549094497 scopus 로고    scopus 로고
    • Cerium ion-chelated magnetic silica microspheres for enrichment and direct determination of phosphopeptides by matrix-assisted laser desorption ionization mass spectrometry
    • Li Y., et al. Cerium ion-chelated magnetic silica microspheres for enrichment and direct determination of phosphopeptides by matrix-assisted laser desorption ionization mass spectrometry. J. Proteome Res. 2008, 7:1767-1777.
    • (2008) J. Proteome Res. , vol.7 , pp. 1767-1777
    • Li, Y.1
  • 39
    • 44449123735 scopus 로고    scopus 로고
    • Enrichment of phosphopeptides by Fe3+-immobilized magnetic nanoparticles for phosphoproteome analysis of the plasma membrane of mouse liver
    • Tan F., et al. Enrichment of phosphopeptides by Fe3+-immobilized magnetic nanoparticles for phosphoproteome analysis of the plasma membrane of mouse liver. J. Proteome Res. 2008, 7:1078-1087.
    • (2008) J. Proteome Res. , vol.7 , pp. 1078-1087
    • Tan, F.1
  • 40
    • 35348990994 scopus 로고    scopus 로고
    • Nitrilotriacetic acid-coated magnetic nanoparticles as affinity probes for enrichment of histidine-tagged proteins and phosphorylated peptides
    • Li Y.-C., et al. Nitrilotriacetic acid-coated magnetic nanoparticles as affinity probes for enrichment of histidine-tagged proteins and phosphorylated peptides. Anal. Chem. 2007, 79:7519-7525.
    • (2007) Anal. Chem. , vol.79 , pp. 7519-7525
    • Li, Y.-C.1
  • 41
    • 77249148900 scopus 로고    scopus 로고
    • Rapid enrichment and determination of phosphopeptides using bacterial magnetic particles via both strong and weak interactions
    • Huang J., et al. Rapid enrichment and determination of phosphopeptides using bacterial magnetic particles via both strong and weak interactions. Analyst 2010, 135:559-563.
    • (2010) Analyst , vol.135 , pp. 559-563
    • Huang, J.1
  • 42
    • 0042861519 scopus 로고    scopus 로고
    • Phosphospecific proteolysis for mapping sites of protein phosphorylation
    • Knight Z.A., et al. Phosphospecific proteolysis for mapping sites of protein phosphorylation. Nat. Biotechnol. 2003, 21:1047-1054.
    • (2003) Nat. Biotechnol. , vol.21 , pp. 1047-1054
    • Knight, Z.A.1
  • 43
    • 0032875697 scopus 로고    scopus 로고
    • Quantitative analysis of complex protein mixtures using isotope-coded affinity tags
    • Gygi S.P., et al. Quantitative analysis of complex protein mixtures using isotope-coded affinity tags. Nat. Biotechnol. 1999, 17:994-999.
    • (1999) Nat. Biotechnol. , vol.17 , pp. 994-999
    • Gygi, S.P.1
  • 44
    • 0036468952 scopus 로고    scopus 로고
    • Phosphoprotein isotope-coded affinity tags: application to the enrichment and identification of low-abundance phosphoproteins
    • Goshe M.B., et al. Phosphoprotein isotope-coded affinity tags: application to the enrichment and identification of low-abundance phosphoproteins. Anal. Chem. 2002, 74:607-616.
    • (2002) Anal. Chem. , vol.74 , pp. 607-616
    • Goshe, M.B.1
  • 45
    • 0036246088 scopus 로고    scopus 로고
    • Quantitive proteome analysis by solid-phase isotope tagging and mass spectrometry
    • Zhou H., et al. Quantitive proteome analysis by solid-phase isotope tagging and mass spectrometry. Nat. Biotechnol. 2002, 19:512-515.
    • (2002) Nat. Biotechnol. , vol.19 , pp. 512-515
    • Zhou, H.1
  • 46
    • 0142040631 scopus 로고    scopus 로고
    • Phosphoprotein isotope-coded solid-phase tag approach for enrichment and quantitative analysis of phosphopeptides from complex mixtures
    • Qian W.-J., et al. Phosphoprotein isotope-coded solid-phase tag approach for enrichment and quantitative analysis of phosphopeptides from complex mixtures. Anal. Chem. 2003, 75:5441-5450.
    • (2003) Anal. Chem. , vol.75 , pp. 5441-5450
    • Qian, W.-J.1
  • 47
    • 34548611179 scopus 로고    scopus 로고
    • Protein phosphorylation analysis by site-specifi{ligature}c arginine-mimic labeling in gel electrophoresis and matrix-assisted laser desorption/ionization time-of-fl{ligature}ight mass spectrometry
    • Ahn Y.H., et al. Protein phosphorylation analysis by site-specifi{ligature}c arginine-mimic labeling in gel electrophoresis and matrix-assisted laser desorption/ionization time-of-fl{ligature}ight mass spectrometry. Anal. Biochem. 2007, 370:77-86.
    • (2007) Anal. Biochem. , vol.370 , pp. 77-86
    • Ahn, Y.H.1
  • 48
    • 37649025660 scopus 로고    scopus 로고
    • Coupling of TiO2-mediated enrichment and on-bead guanidinoethanethiol labeling for effective phosphopeptide analysis by matrix-assisted laser desorption/ionization mass spectrometry
    • Ahn Y.H., et al. Coupling of TiO2-mediated enrichment and on-bead guanidinoethanethiol labeling for effective phosphopeptide analysis by matrix-assisted laser desorption/ionization mass spectrometry. Rapid Commun. Mass Spectrom. 2007, 21:3987-3994.
    • (2007) Rapid Commun. Mass Spectrom. , vol.21 , pp. 3987-3994
    • Ahn, Y.H.1
  • 49
    • 23044472346 scopus 로고    scopus 로고
    • Enhancement of phosphoprotein analysis using a fl{ligature}uorescent affi{ligature}nity tag and mass spectrometry
    • Stevens S.M., et al. Enhancement of phosphoprotein analysis using a fl{ligature}uorescent affi{ligature}nity tag and mass spectrometry. Rapid Commun. Mass Spectrom. 2005, 19:2157-2162.
    • (2005) Rapid Commun. Mass Spectrom. , vol.19 , pp. 2157-2162
    • Stevens, S.M.1
  • 50
    • 0035072715 scopus 로고    scopus 로고
    • A systematic approach to the analysis of protein phosphorylation
    • Zhou H., et al. A systematic approach to the analysis of protein phosphorylation. Nat. Biotechnol. 2001, 19:375-378.
    • (2001) Nat. Biotechnol. , vol.19 , pp. 375-378
    • Zhou, H.1
  • 51
    • 23144441172 scopus 로고    scopus 로고
    • Quantitive phosphoproteome analysis using a dendrimer conjugation chemistry and tandem mass spectrometry
    • Tao W.A., et al. Quantitive phosphoproteome analysis using a dendrimer conjugation chemistry and tandem mass spectrometry. Nat. Methods 2005, 2:591-598.
    • (2005) Nat. Methods , vol.2 , pp. 591-598
    • Tao, W.A.1
  • 52
    • 77955342864 scopus 로고    scopus 로고
    • A Phos-tag-based approach reveals the extent of physiological endoplasmic reticulum stress
    • Yang L., et al. A Phos-tag-based approach reveals the extent of physiological endoplasmic reticulum stress. PLoS ONE 2010, 5:e11621.
    • (2010) PLoS ONE , vol.5
    • Yang, L.1
  • 53
    • 0042836937 scopus 로고    scopus 로고
    • Matrix-assisted laser desorption/ionization time-of-fl{ligature}ight mass spectrometry of phosphorylated compounds using a novel phosphate capture molecule
    • Takeda H., et al. Matrix-assisted laser desorption/ionization time-of-fl{ligature}ight mass spectrometry of phosphorylated compounds using a novel phosphate capture molecule. Rapid Commun. Mass Spectrom. 2003, 17:2075-2081.
    • (2003) Rapid Commun. Mass Spectrom. , vol.17 , pp. 2075-2081
    • Takeda, H.1
  • 54
    • 2342589413 scopus 로고    scopus 로고
    • Recognition of phosphate monoester dianion by an alkoxide-bridged dinuclear zinc(II) complex
    • Kinoshita E., et al. Recognition of phosphate monoester dianion by an alkoxide-bridged dinuclear zinc(II) complex. Dalton Trans. 2004, 1189-1193.
    • (2004) Dalton Trans. , pp. 1189-1193
    • Kinoshita, E.1
  • 55
    • 33645714857 scopus 로고    scopus 로고
    • Phosphate-binding tag, a new tool to visualize phosphorylated proteins
    • Kinoshita E., et al. Phosphate-binding tag, a new tool to visualize phosphorylated proteins. Mol. Cell. Proteomics 2006, 5:749-757.
    • (2006) Mol. Cell. Proteomics , vol.5 , pp. 749-757
    • Kinoshita, E.1
  • 56
    • 14944345703 scopus 로고    scopus 로고
    • Novel immobilized zinc(II) affinity chromatography for phosphopeptides and phosphorylated proteins
    • Kinoshita E., et al. Novel immobilized zinc(II) affinity chromatography for phosphopeptides and phosphorylated proteins. J. Sep. Sci. 2005, 28:155-162.
    • (2005) J. Sep. Sci. , vol.28 , pp. 155-162
    • Kinoshita, E.1
  • 57
    • 65049086456 scopus 로고    scopus 로고
    • Phos-tag beads as an immunoblotting enhancer for selective detection of phosphoproteins in cell lysates
    • Kinoshita-Kikuta E., et al. Phos-tag beads as an immunoblotting enhancer for selective detection of phosphoproteins in cell lysates. Anal. Biochem. 2009, 389:83-85.
    • (2009) Anal. Biochem. , vol.389 , pp. 83-85
    • Kinoshita-Kikuta, E.1
  • 58
    • 73349138284 scopus 로고    scopus 로고
    • Separation and detection of large phosphoproteins using Phos-tag SDS-PAGE
    • Kinoshita E., et al. Separation and detection of large phosphoproteins using Phos-tag SDS-PAGE. Nat. Protoc. 2009, 4:1513-1521.
    • (2009) Nat. Protoc. , vol.4 , pp. 1513-1521
    • Kinoshita, E.1
  • 59
    • 57749117453 scopus 로고    scopus 로고
    • Enhancing the separation of phosphorylated proteins in gel electrophoresis with dinuclear bispyridylmethylamine-tyrosine-acrylamide complexes
    • Dirscherl G., et al. Enhancing the separation of phosphorylated proteins in gel electrophoresis with dinuclear bispyridylmethylamine-tyrosine-acrylamide complexes. Inorg. Chim. Acta 2009, 362:537-542.
    • (2009) Inorg. Chim. Acta , vol.362 , pp. 537-542
    • Dirscherl, G.1
  • 60
    • 0037024162 scopus 로고    scopus 로고
    • First artificial receptors and chemosensors toward phosphorylated peptide in aqueous solution
    • Ojida A., et al. First artificial receptors and chemosensors toward phosphorylated peptide in aqueous solution. J. Am. Chem. Soc. 2002, 124:6256-6258.
    • (2002) J. Am. Chem. Soc. , vol.124 , pp. 6256-6258
    • Ojida, A.1
  • 61
    • 69949123361 scopus 로고    scopus 로고
    • Fluorescent BODIPY-based Zn(II) complex as a molecular probe for selective detection of neurofibrillary tangles in the brains of Alzheimer's disease patients
    • Ojida A., et al. Fluorescent BODIPY-based Zn(II) complex as a molecular probe for selective detection of neurofibrillary tangles in the brains of Alzheimer's disease patients. J. Am. Chem. Soc. 2009, 131:6543-6548.
    • (2009) J. Am. Chem. Soc. , vol.131 , pp. 6543-6548
    • Ojida, A.1
  • 62
    • 0041429638 scopus 로고    scopus 로고
    • Cross-linking strategy for molecular recognition and fluorescent sensing of a multi-phosphorylated peptide in aqueous solution
    • Ojida A., et al. Cross-linking strategy for molecular recognition and fluorescent sensing of a multi-phosphorylated peptide in aqueous solution. J. Am. Chem. Soc. 2003, 125:10184-10185.
    • (2003) J. Am. Chem. Soc. , vol.125 , pp. 10184-10185
    • Ojida, A.1
  • 63
    • 33847712279 scopus 로고    scopus 로고
    • Two-dimensional arrays of amphiphilic Zn2+-cyclens for guided molecular recognition at interfaces
    • Turygin D.S., et al. Two-dimensional arrays of amphiphilic Zn2+-cyclens for guided molecular recognition at interfaces. Langmuir 2007, 23:2517-2524.
    • (2007) Langmuir , vol.23 , pp. 2517-2524
    • Turygin, D.S.1
  • 64
    • 77950687929 scopus 로고    scopus 로고
    • Binding of phosphorylated peptides and inhibition of their interaction with disease-relevant human proteins by synthetic metal-chelate receptors
    • Riechers A., et al. Binding of phosphorylated peptides and inhibition of their interaction with disease-relevant human proteins by synthetic metal-chelate receptors. J. Mol. Recognit. 2010, 23:329-334.
    • (2010) J. Mol. Recognit. , vol.23 , pp. 329-334
    • Riechers, A.1
  • 65
    • 55049090531 scopus 로고    scopus 로고
    • Synthetic receptors for the differentiation of phosphorylated peptides with nanomolar affinities
    • Grauer A., et al. Synthetic receptors for the differentiation of phosphorylated peptides with nanomolar affinities. Chem. Eur. J. 2008, 14:8922-8927.
    • (2008) Chem. Eur. J. , vol.14 , pp. 8922-8927
    • Grauer, A.1
  • 66
    • 36849050225 scopus 로고    scopus 로고
    • Selectivity and recovery performance of phosphate-selective molecularly imprinted polymer
    • Kugimiya A., Takei H. Selectivity and recovery performance of phosphate-selective molecularly imprinted polymer. Anal. Chim. Acta 2008, 606:252-256.
    • (2008) Anal. Chim. Acta , vol.606 , pp. 252-256
    • Kugimiya, A.1    Takei, H.2
  • 67
    • 55049083485 scopus 로고    scopus 로고
    • A phosphotyrosine-imprinted polymer receptor for the recognition of Ttyrosine phosphorylated peptides
    • Emgenbroich M., et al. A phosphotyrosine-imprinted polymer receptor for the recognition of Ttyrosine phosphorylated peptides. Chem. Eur. J. 2008, 14:9516-9529.
    • (2008) Chem. Eur. J. , vol.14 , pp. 9516-9529
    • Emgenbroich, M.1
  • 68
    • 79952181729 scopus 로고    scopus 로고
    • Ultratrace enrichment of tyrosine phosphorylated peptides on an imprinted polymer
    • Helling S., et al. Ultratrace enrichment of tyrosine phosphorylated peptides on an imprinted polymer. Anal. Chem. 2011, 83:1862-1865.
    • (2011) Anal. Chem. , vol.83 , pp. 1862-1865
    • Helling, S.1
  • 69
    • 43849094501 scopus 로고    scopus 로고
    • A web-based tool for in silico biomarker discovery based on tissue-specific protein profiles in normal and cancer tissues
    • Björling E., et al. A web-based tool for in silico biomarker discovery based on tissue-specific protein profiles in normal and cancer tissues. Mol. Cell. Proteomics 2008, 7:825-844.
    • (2008) Mol. Cell. Proteomics , vol.7 , pp. 825-844
    • Björling, E.1
  • 70
    • 34548448107 scopus 로고    scopus 로고
    • Affinity reagent resources for human proteome detection: initiatives and perspectives
    • Stoevesandt O., Taussig M.J. Affinity reagent resources for human proteome detection: initiatives and perspectives. Proteomics 2007, 7:2738-2750.
    • (2007) Proteomics , vol.7 , pp. 2738-2750
    • Stoevesandt, O.1    Taussig, M.J.2
  • 71
    • 33845921119 scopus 로고    scopus 로고
    • ProteomeBinders: planning a European resource of affinity reagents for analysis of the human proteome
    • Taussig M.J., et al. ProteomeBinders: planning a European resource of affinity reagents for analysis of the human proteome. Nat. Methods 2007, 4:13-18.
    • (2007) Nat. Methods , vol.4 , pp. 13-18
    • Taussig, M.J.1
  • 72
    • 78649483808 scopus 로고    scopus 로고
    • Iminodiacetic acid-modifi{ligature}ed magnetic poly(2-hydroxyethyl methacrylate)-based microspheres for phosphopeptide enrichment
    • Novotna L., et al. Iminodiacetic acid-modifi{ligature}ed magnetic poly(2-hydroxyethyl methacrylate)-based microspheres for phosphopeptide enrichment. J. Chromatogr. A 2010, 1217:8032-8040.
    • (2010) J. Chromatogr. A , vol.1217 , pp. 8032-8040
    • Novotna, L.1
  • 73
    • 78049326007 scopus 로고    scopus 로고
    • Functional Fe3O4@ZnO magnetic nanoparticle-assisted enrichment and enzymatic digestion of phosphoproteins from saliva
    • Chen W.-Y., Chen Y.-C. Functional Fe3O4@ZnO magnetic nanoparticle-assisted enrichment and enzymatic digestion of phosphoproteins from saliva. Anal. Bioanal. Chem. 2010, 398:2049-2057.
    • (2010) Anal. Bioanal. Chem. , vol.398 , pp. 2049-2057
    • Chen, W.-Y.1    Chen, Y.-C.2
  • 74
    • 34248215724 scopus 로고    scopus 로고
    • Concerted experimental approach for sequential mapping of peptides and phosphopeptides using C18-functionalized magnetic nanoparticles
    • Hsiao H.-H., et al. Concerted experimental approach for sequential mapping of peptides and phosphopeptides using C18-functionalized magnetic nanoparticles. J. Proteome Res. 2007, 6:1313-1324.
    • (2007) J. Proteome Res. , vol.6 , pp. 1313-1324
    • Hsiao, H.-H.1
  • 75
    • 78349310118 scopus 로고    scopus 로고
    • Phosphoproteomics in cancer
    • Harsha H.C., Pandey A. Phosphoproteomics in cancer. Mol. Oncol. 2010, 4:482-495.
    • (2010) Mol. Oncol. , vol.4 , pp. 482-495
    • Harsha, H.C.1    Pandey, A.2
  • 76
    • 77950631558 scopus 로고    scopus 로고
    • Phosphopeptide analysis reveals two discrete clusters of phosphorylation in the N-terminus and the Roc domain of the Parkinson-disease associated protein kinase LRRK2
    • Gloeckner C.J., et al. Phosphopeptide analysis reveals two discrete clusters of phosphorylation in the N-terminus and the Roc domain of the Parkinson-disease associated protein kinase LRRK2. J. Proteome Res. 2010, 9:1738-1745.
    • (2010) J. Proteome Res. , vol.9 , pp. 1738-1745
    • Gloeckner, C.J.1
  • 77
    • 61849088424 scopus 로고    scopus 로고
    • Tau phosphorylation: the therapeutic challenge for neurodegenerative disease
    • Hanger D.P., et al. Tau phosphorylation: the therapeutic challenge for neurodegenerative disease. Trends Mol. Med. 2009, 15:112-119.
    • (2009) Trends Mol. Med. , vol.15 , pp. 112-119
    • Hanger, D.P.1
  • 78
    • 47549101249 scopus 로고    scopus 로고
    • Biomarker discovery in psychiatric disorders
    • Schwarz E., Bahn S. Biomarker discovery in psychiatric disorders. Electrophoresis 2008, 29:2884-2890.
    • (2008) Electrophoresis , vol.29 , pp. 2884-2890
    • Schwarz, E.1    Bahn, S.2
  • 79
    • 38349188638 scopus 로고    scopus 로고
    • Phosphoproteomics for the discovery of kinases as cancer biomarkers and drug targets
    • Yu L.-R., et al. Phosphoproteomics for the discovery of kinases as cancer biomarkers and drug targets. Proteomics Clin. Appl. 2007, 1:1042-1057.
    • (2007) Proteomics Clin. Appl. , vol.1 , pp. 1042-1057
    • Yu, L.-R.1


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