메뉴 건너뛰기




Volumn 13, Issue 12, 2014, Pages 6176-6186

Off-line high-pH reversed-phase fractionation for in-depth phosphoproteomics

Author keywords

enrichment; fractionation; high pH reversed phase; Orbitrap; peptides; Phosphoproteomics; phosphorylation; titanium dioxide

Indexed keywords

PEPTIDE; PHOSPHOPEPTIDE; CATION EXCHANGE RESIN; PHOSPHOPROTEIN; PROTEOME; TITANIUM; TITANIUM DIOXIDE;

EID: 84915751028     PISSN: 15353893     EISSN: 15353907     Source Type: Journal    
DOI: 10.1021/pr500893m     Document Type: Article
Times cited : (246)

References (38)
  • 1
    • 84890644637 scopus 로고    scopus 로고
    • Status of large-scale analysis of post-translational modifications by mass spectrometry
    • Olsen, J. V.; Mann, M. Status of large-scale analysis of post-translational modifications by mass spectrometry Mol. Cell. Proteomics 2013, 12, 3444-3452
    • (2013) Mol. Cell. Proteomics , vol.12 , pp. 3444-3452
    • Olsen, J.V.1    Mann, M.2
  • 2
    • 77953896432 scopus 로고    scopus 로고
    • Cell signaling by receptor tyrosine kinases
    • Lemmon, M. A.; Schlessinger, J. Cell signaling by receptor tyrosine kinases Cell 2010, 141, 1117-1134
    • (2010) Cell , vol.141 , pp. 1117-1134
    • Lemmon, M.A.1    Schlessinger, J.2
  • 3
    • 84907205494 scopus 로고    scopus 로고
    • 4+-IMAC and label free quantitation enables in-depth monitoring of phosphorylation dynamics with high reproducibility and temporal resolution
    • 4+-IMAC and label free quantitation enables in-depth monitoring of phosphorylation dynamics with high reproducibility and temporal resolution Mol. Cell. Proteomics 2014, 13, 2426-2434
    • (2014) Mol. Cell. Proteomics , vol.13 , pp. 2426-2434
    • De Graaf, E.L.1    Giansanti, P.2    Altelaar, A.F.M.3    Heck, A.J.R.4
  • 5
    • 0035106351 scopus 로고    scopus 로고
    • Large-scale analysis of the yeast proteome by multidimensional protein identification technology
    • Washburn, M. P.; Wolters, D.; Yates, J. R. Large-scale analysis of the yeast proteome by multidimensional protein identification technology Nat. Biotechnol. 2001, 19, 242-247
    • (2001) Nat. Biotechnol. , vol.19 , pp. 242-247
    • Washburn, M.P.1    Wolters, D.2    Yates, J.R.3
  • 6
    • 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
  • 7
    • 79955550970 scopus 로고    scopus 로고
    • Zwitterionic hydrophilic interaction liquid chromatography (ZIC-HILIC and ZIC-cHILIC) provide high resolution separation and increase sensitivity in proteome analysis
    • Di Palma, S.; Boersema, P. J.; Heck, A. J. R.; Mohammed, S. Zwitterionic hydrophilic interaction liquid chromatography (ZIC-HILIC and ZIC-cHILIC) provide high resolution separation and increase sensitivity in proteome analysis Anal. Chem. 2011, 83, 3440-3447
    • (2011) Anal. Chem. , vol.83 , pp. 3440-3447
    • Di Palma, S.1    Boersema, P.J.2    Heck, A.J.R.3    Mohammed, S.4
  • 8
    • 77954368187 scopus 로고    scopus 로고
    • Novel application of electrostatic repulsion-hydrophilic interaction chromatography (ERLIC) in shotgun proteomics: Comprehensive profiling of rat kidney proteome
    • Hao, P.; Guo, T.; Li, X.; Adav, S. S.; Yang, J.; Wei, M.; Sze, S. K. Novel application of electrostatic repulsion-hydrophilic interaction chromatography (ERLIC) in shotgun proteomics: comprehensive profiling of rat kidney proteome J. Proteome Res. 2010, 9, 3520-3526
    • (2010) J. Proteome Res. , vol.9 , pp. 3520-3526
    • Hao, P.1    Guo, T.2    Li, X.3    Adav, S.S.4    Yang, J.5    Wei, M.6    Sze, S.K.7
  • 13
    • 33750456519 scopus 로고    scopus 로고
    • Global, in vivo, and site-specific phosphorylation dynamics in signaling networks
    • 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, 635-648
    • (2006) Cell , vol.127 , 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
  • 15
    • 43849091451 scopus 로고    scopus 로고
    • Hydrophilic interaction chromatography reduces the complexity of the phosphoproteome and improves global phosphopeptide isolation and detection
    • 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, 971-980
    • (2008) Mol. Cell. Proteomics , vol.7 , pp. 971-980
    • McNulty, D.E.1    Annan, R.S.2
  • 16
    • 26444539668 scopus 로고    scopus 로고
    • Orthogonality of separation in two-dimensional liquid chromatography
    • Gilar, M.; Olivova, P.; Daly, A. E.; Gebler, J. C. Orthogonality of separation in two-dimensional liquid chromatography Anal. Chem. 2005, 77, 6426-6434
    • (2005) Anal. Chem. , vol.77 , pp. 6426-6434
    • Gilar, M.1    Olivova, P.2    Daly, A.E.3    Gebler, J.C.4
  • 19
    • 84874619400 scopus 로고    scopus 로고
    • Refined preparation and use of anti-diglycine remnant (K-ε-GG) antibody enables routine quantification of 10,000s of ubiquitination sites in single proteomics experiments
    • Udeshi, N. D.; Svinkina, T.; Mertins, P.; Kuhn, E.; Mani, D. R.; Qiao, J. W.; Carr, S. A. Refined preparation and use of anti-diglycine remnant (K-ε-GG) antibody enables routine quantification of 10,000s of ubiquitination sites in single proteomics experiments Mol. Cell. Proteomics 2012, 12, 825-831
    • (2012) Mol. Cell. Proteomics , vol.12 , pp. 825-831
    • Udeshi, N.D.1    Svinkina, T.2    Mertins, P.3    Kuhn, E.4    Mani, D.R.5    Qiao, J.W.6    Carr, S.A.7
  • 21
    • 24944519450 scopus 로고    scopus 로고
    • Highly selective enrichment of phosphorylated peptides from peptide mixtures using titanium dioxide microcolumns
    • Larsen, M. R.; Thingholm, T. E.; Jensen, O. N.; Roepstorff, P.; Jørgensen, T. J. D. Highly selective enrichment of phosphorylated peptides from peptide mixtures using titanium dioxide microcolumns Mol. Cell. Proteomics 2005, 4, 873-886
    • (2005) Mol. Cell. Proteomics , vol.4 , pp. 873-886
    • Larsen, M.R.1    Thingholm, T.E.2    Jensen, O.N.3    Roepstorff, P.4    Jørgensen, T.J.D.5
  • 22
    • 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. H.; Uitto, P. M.; Hilhorst, M. J.; Ooms, B.; Heck, A. J. R. 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, 3935-3943
    • (2004) Anal. Chem. , vol.76 , pp. 3935-3943
    • Pinkse, M.W.H.1    Uitto, P.M.2    Hilhorst, M.J.3    Ooms, B.4    Heck, A.J.R.5
  • 23
    • 34548183872 scopus 로고    scopus 로고
    • Protocol for micro-purification, enrichment, pre-fractionation and storage of peptides for proteomics using StageTips
    • Rappsilber, J.; Mann, M.; Ishihama, Y. Protocol for micro-purification, enrichment, pre-fractionation and storage of peptides for proteomics using StageTips Nat. Protoc. 2007, 2, 1896-1906
    • (2007) Nat. Protoc. , vol.2 , pp. 1896-1906
    • Rappsilber, J.1    Mann, M.2    Ishihama, Y.3
  • 24
  • 25
    • 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, 1367-1372
    • (2008) Nat. Biotechnol. , vol.26 , pp. 1367-1372
    • Cox, J.1    Mann, M.2
  • 27
    • 58549112996 scopus 로고    scopus 로고
    • Bioinformatics enrichment tools: Paths toward the comprehensive functional analysis of large gene lists
    • Huang, D. W.; Sherman, B. T.; Lempicki, R. A. Bioinformatics enrichment tools: paths toward the comprehensive functional analysis of large gene lists Nucleic Acids Res. 2009, 37, 1-13
    • (2009) Nucleic Acids Res. , vol.37 , pp. 1-13
    • Huang, D.W.1    Sherman, B.T.2    Lempicki, R.A.3
  • 28
    • 61449172037 scopus 로고    scopus 로고
    • Systematic and integrative analysis of large gene lists using DAVID bioinformatics resources
    • Huang, D. W.; Sherman, B. T.; Lempicki, R. A. Systematic and integrative analysis of large gene lists using DAVID bioinformatics resources Nat. Protoc. 2009, 4, 44-57
    • (2009) Nat. Protoc. , vol.4 , pp. 44-57
    • Huang, D.W.1    Sherman, B.T.2    Lempicki, R.A.3
  • 30
    • 84861800006 scopus 로고    scopus 로고
    • Optimized fast and sensitive acquisition methods for shotgun proteomics on a quadrupole Orbitrap mass spectrometer
    • Kelstrup, C. D.; Young, C.; Lavallee, R.; Nielsen, M. L.; Olsen, J. V. Optimized fast and sensitive acquisition methods for shotgun proteomics on a quadrupole Orbitrap mass spectrometer J. Proteome Res. 2012, 11, 3487-3497
    • (2012) J. Proteome Res. , vol.11 , pp. 3487-3497
    • Kelstrup, C.D.1    Young, C.2    Lavallee, R.3    Nielsen, M.L.4    Olsen, J.V.5
  • 32
    • 84899833857 scopus 로고    scopus 로고
    • Enhanced sensitivity and multiplexing with 2D LC/MRM-MS and labeled standards for deeper and more comprehensive protein quantitation
    • Percy, A. J.; Simon, R.; Chambers, A. G.; Borchers, C. H. Enhanced sensitivity and multiplexing with 2D LC/MRM-MS and labeled standards for deeper and more comprehensive protein quantitation J. Proteomics 2014, 106, 113-124
    • (2014) J. Proteomics , vol.106 , pp. 113-124
    • Percy, A.J.1    Simon, R.2    Chambers, A.G.3    Borchers, C.H.4
  • 35
    • 18844383462 scopus 로고    scopus 로고
    • A phosphoserine-lysine salt bridge within an α-helical peptide, the strongest α-helix side-chain interaction measured to date
    • Errington, N.; Doig, A. J. A phosphoserine-lysine salt bridge within an α-helical peptide, the strongest α-helix side-chain interaction measured to date Biochemistry 2005, 44, 7553-7558
    • (2005) Biochemistry , vol.44 , pp. 7553-7558
    • Errington, N.1    Doig, A.J.2
  • 37
    • 63749113783 scopus 로고    scopus 로고
    • Tyrosine phosphorylation: Thirty years and counting
    • Hunter, T. Tyrosine phosphorylation: thirty years and counting Curr. Opin. Cell Biol. 2009, 21, 140-146
    • (2009) Curr. Opin. Cell Biol. , vol.21 , pp. 140-146
    • Hunter, T.1
  • 38
    • 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, 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


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.