메뉴 건너뛰기




Volumn 1355, Issue , 2016, Pages 105-121

Enrichment strategies in phosphoproteomics

(1)  Leitner, Alexander a  

a NONE

Author keywords

Fractionation; Mass spectrometry; Phosphopeptide enrichment; Sample preparation

Indexed keywords

METAL OXIDE; PHOSPHOPEPTIDE; PHOSPHOPROTEIN;

EID: 84947983002     PISSN: 10643745     EISSN: None     Source Type: Book Series    
DOI: 10.1007/978-1-4939-3049-4_7     Document Type: Chapter
Times cited : (44)

References (77)
  • 1
    • 84901599553 scopus 로고    scopus 로고
    • A draft map of the human proteome
    • Kim M-S, Pinto SM, Getnet D et al (2014) A draft map of the human proteome. Nature 509:575–581
    • (2014) Nature , vol.509 , pp. 575-581
    • Kim, M.-S.1    Pinto, S.M.2    Getnet, D.3
  • 2
    • 84901611036 scopus 로고    scopus 로고
    • Mass-spectrometry-based draft of the human proteome
    • Wilhelm M, Schlegl J, Hahne H et al (2014) Mass-spectrometry-based draft of the human proteome. Nature 509:582–587
    • (2014) Nature , vol.509 , pp. 582-587
    • Wilhelm, M.1    Schlegl, J.2    Hahne, H.3
  • 3
    • 84867041794 scopus 로고    scopus 로고
    • Advances in phosphopeptide enrichment techniques for phosphoproteomics
    • Beltran L, Cutillas PR (2012) Advances in phosphopeptide enrichment techniques for phosphoproteomics. Amino Acids 43:1009–1024
    • (2012) Amino Acids , vol.43 , pp. 1009-1024
    • Beltran, L.1    Cutillas, P.R.2
  • 4
    • 84867036962 scopus 로고    scopus 로고
    • Enrichment techniques employed in phosphoproteomics
    • Fila J, Honys D (2012) Enrichment techniques employed in phosphoproteomics. Amino Acids 43:1025–1047
    • (2012) Amino Acids , vol.43 , pp. 1025-1047
    • Fila, J.1    Honys, D.2
  • 5
    • 84874964821 scopus 로고    scopus 로고
    • Technologies and challenges in large-scale phosphoproteomics
    • Engholm-Keller K, Larsen MR (2013) Technologies and challenges in large-scale phosphoproteomics. Proteomics 13:910–931
    • (2013) Proteomics , vol.13 , pp. 910-931
    • Engholm-Keller, K.1    Larsen, M.R.2
  • 7
    • 84873990418 scopus 로고    scopus 로고
    • Integration of phosphoproteomic, chemical, and biological strategies for the functional analysis of targeted protein phosphorylation
    • Guo M, Huang BX (2013) Integration of phosphoproteomic, chemical, and biological strategies for the functional analysis of targeted protein phosphorylation. Proteomics 13: 424–437
    • (2013) Proteomics , vol.13 , pp. 424-437
    • Guo, M.1    Huang, B.X.2
  • 8
    • 84890641204 scopus 로고    scopus 로고
    • The coming of age of phosphoproteomics—from large data sets to inference of protein functions
    • Roux PP, Thibault P (2013) The coming of age of phosphoproteomics—from large data sets to inference of protein functions. Mol Cell Proteomics 12:3453–3464
    • (2013) Mol Cell Proteomics , vol.12 , pp. 3453-3464
    • Roux, P.P.1    Thibault, P.2
  • 9
    • 84890367496 scopus 로고    scopus 로고
    • Mass spectrometry- driven phosphoproteomics: Patterning the systems biology mosaic
    • Jünger MA, Aebersold R (2014) Mass spectrometry- driven phosphoproteomics: patterning the systems biology mosaic. Wiley Interdiscip Rev Dev Biol 3:83–112
    • (2014) Wiley Interdiscip Rev Dev Biol , vol.3 , pp. 83-112
    • Jünger, M.A.1    Aebersold, R.2
  • 10
    • 30144438909 scopus 로고    scopus 로고
    • Collisioninduced dissociation (CID) of peptides and proteins
    • Wells JM, McLuckey SA (2005) Collisioninduced dissociation (CID) of peptides and proteins. Methods Enzymol 402:148–185
    • (2005) Methods Enzymol , vol.402 , pp. 148-185
    • Wells, J.M.1    McLuckey, S.A.2
  • 11
    • 67649213067 scopus 로고    scopus 로고
    • Phosphopeptide fragmentation and analysis by mass spectrometry
    • Boersema PJ, Mohammed S, Heck AJR (2009) Phosphopeptide fragmentation and analysis by mass spectrometry. J Mass Spectrom 44: 861–878
    • (2009) J Mass Spectrom , vol.44 , pp. 861-878
    • Boersema, P.J.1    Mohammed, S.2    Heck, A.3
  • 12
    • 84860879590 scopus 로고    scopus 로고
    • Modification site localization scoring: Strategies and performance
    • Chalkley RJ, Clauser KR (2012) Modification site localization scoring: strategies and performance. Mol Cell Proteomics 11:3–14
    • (2012) Mol Cell Proteomics , vol.11 , pp. 3-14
    • Chalkley, R.J.1    Clauser, K.R.2
  • 13
    • 21144458164 scopus 로고    scopus 로고
    • Immunoaffinity profiling of tyrosine phosphorylation in cancer cells
    • Rush J, Moritz A, Lee KA et al (2005) Immunoaffinity profiling of tyrosine phosphorylation in cancer cells. Nat Biotechnol 23: 94–101
    • (2005) Nat Biotechnol , vol.23 , pp. 94-101
    • Rush, J.1    Moritz, A.2    Lee, K.A.3
  • 14
    • 76649110554 scopus 로고    scopus 로고
    • In-depth qualitative and quantitative profiling of tyrosine phosphorylation using a combination of phosphopeptide immunoaffinity purification and stable isotope dimethyl labeling
    • Boersema PJ, Foong LY, Ding VMY et al (2010) In-depth qualitative and quantitative profiling of tyrosine phosphorylation using a combination of phosphopeptide immunoaffinity purification and stable isotope dimethyl labeling. Mol Cell Proteomics 9:84–99
    • (2010) Mol Cell Proteomics , vol.9 , pp. 84-99
    • Boersema, P.J.1    Foong, L.Y.2    Ding, V.3
  • 15
    • 84879416831 scopus 로고    scopus 로고
    • A pan-specific antibody for direct detection of protein histidine phosphorylation
    • Kee J-M, Oslund RC, Perlman DH et al (2013) A pan-specific antibody for direct detection of protein histidine phosphorylation. Nat Chem Biol 9:416–421
    • (2013) Nat Chem Biol , vol.9 , pp. 416-421
    • Kee, J.-M.1    Oslund, R.C.2    Perlman, D.H.3
  • 16
    • 0016717761 scopus 로고
    • Metal chelate affinity chromatography, a new approach to protein fractionation
    • Porath J, Carlsson J, Olsson I et al (1975) Metal chelate affinity chromatography, a new approach to protein fractionation. Nature 258:598–599
    • (1975) Nature , vol.258 , pp. 598-599
    • Porath, J.1    Carlsson, J.2    Olsson, I.3
  • 17
    • 0022541790 scopus 로고
    • Isolation of phosphoproteins by immobilized metal (Fe3+) affinity chromatography
    • Andersson L, Porath J (1986) Isolation of phosphoproteins by immobilized metal (Fe3+) affinity chromatography. Anal Biochem 154:250–254
    • (1986) Anal Biochem , vol.154 , pp. 250-254
    • Andersson, L.1    Porath, J.2
  • 18
    • 55249104113 scopus 로고    scopus 로고
    • Specific phosphopeptide enrichment with immobilized titanium ion affinity chromatography adsorbent for phosphoproteome analysis
    • Zhou H, Ye M, Dong J et al (2008) Specific phosphopeptide enrichment with immobilized titanium ion affinity chromatography adsorbent for phosphoproteome analysis. J Proteome Res 7:3957–3967
    • (2008) J Proteome Res , vol.7 , pp. 3957-3967
    • Zhou, H.1    Ye, M.2    Dong, J.3
  • 19
    • 84875208164 scopus 로고    scopus 로고
    • Robust phosphoproteome enrichment using monodisperse microsphere-based immobilized titanium (IV) ion affinity chromatography
    • Zhou H, Ye M, Dong J et al (2013) Robust phosphoproteome enrichment using monodisperse microsphere-based immobilized titanium (IV) ion affinity chromatography. Nat Protoc 8:461–480
    • (2013) Nat Protoc , vol.8 , pp. 461-480
    • Zhou, H.1    Ye, M.2    Dong, J.3
  • 20
    • 77957978971 scopus 로고    scopus 로고
    • In-depth analyses of kinase-dependent tyrosine phosphoproteomes based on metal ionfunctionalized soluble nanopolymers
    • Iliuk AB, Martin VA, Alicie BM et al (2010) In-depth analyses of kinase-dependent tyrosine phosphoproteomes based on metal ionfunctionalized soluble nanopolymers. Mol Cell Proteomics 9:2162–2172
    • (2010) Mol Cell Proteomics , vol.9 , pp. 2162-2172
    • Iliuk, A.B.1    Martin, V.A.2    Alicie, B.M.3
  • 21
    • 84903747405 scopus 로고    scopus 로고
    • Global phosphoproteomics of activated b cells using complementary metal ion functionalized soluble nanopolymers
    • Jayasundera KB, Iliuk AB, Nguyen A et al (2014) Global phosphoproteomics of activated b cells using complementary metal ion functionalized soluble nanopolymers. Anal Chem 86:6363–6371
    • (2014) Anal Chem , vol.86 , pp. 6363-6371
    • Jayasundera, K.B.1    Iliuk, A.B.2    Nguyen, A.3
  • 22
    • 84891771545 scopus 로고    scopus 로고
    • Sequential phosphoproteomic enrichment through complementary metal-directed immobilized metal ion affinity chromatography
    • Tsai C-F, Hsu C-C, Hung J-N et al (2014) Sequential phosphoproteomic enrichment through complementary metal-directed immobilized metal ion affinity chromatography. Anal Chem 86:685–693
    • (2014) Anal Chem , vol.86 , pp. 685-693
    • Tsai, C.-F.1    Hsu, C.-C.2    Hung, J.-N.3
  • 23
    • 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 MWH, Uitto PM, Hilhorst MJ et al (2004) Selective isolation at the femtomole level of phosphopeptides from proteolytic digests using 2D-NanoLC-ESI-MS/MS and titanium oxide precolumns. Anal Chem 76:3935–3943
    • (2004) Anal Chem , vol.76 , pp. 3935-3943
    • Pinkse, M.1    Uitto, P.M.2    Hilhorst, M.J.3
  • 24
    • 24944519450 scopus 로고    scopus 로고
    • Highly selective enrichment of phosphorylated peptides from peptide mixtures using titanium dioxide microcolumns
    • Larsen MR, Thingholm TE, Jensen ON et al (2005) Highly selective enrichment of phosphorylated peptides from peptide mixtures using titanium dioxide microcolumns. Mol Cell Proteomics 4:873–886
    • (2005) Mol Cell Proteomics , vol.4 , pp. 873-886
    • Larsen, M.R.1    Thingholm, T.E.2    Jensen, O.N.3
  • 25
    • 77949293684 scopus 로고    scopus 로고
    • Phosphopeptide enrichment using metal oxide affinity chromatography
    • Leitner A (2010) Phosphopeptide enrichment using metal oxide affinity chromatography. Trends Anal Chem 29:177–185
    • (2010) Trends Anal Chem , vol.29 , pp. 177-185
    • Leitner, A.1
  • 26
    • 34347403192 scopus 로고    scopus 로고
    • Phosphopeptide enrichment by aliphatic hydroxy acid-modified metal oxide chromatography for nano-LC-MS/MS in proteomics applications
    • Sugiyama N, Masuda T, Shinoda K et al (2007) Phosphopeptide enrichment by aliphatic hydroxy acid-modified metal oxide chromatography for nano-LC-MS/MS in proteomics applications. Mol Cell Proteomics 6:1103–1109
    • (2007) Mol Cell Proteomics , vol.6 , pp. 1103-1109
    • Sugiyama, N.1    Masuda, T.2    Shinoda, K.3
  • 27
    • 84890038573 scopus 로고    scopus 로고
    • Optimization of enrichment conditions on TiO2 chromatography using glycerol as an additive reagent for effective phosphoproteomic analysis
    • Fukuda I, Hirabayashi-Ishioka Y, Sakikawa I et al (2013) Optimization of enrichment conditions on TiO2 chromatography using glycerol as an additive reagent for effective phosphoproteomic analysis. J Proteome Res 12:5587–5597
    • (2013) J Proteome Res , vol.12 , pp. 5587-5597
    • Fukuda, I.1    Hirabayashi-Ishioka, Y.2    Sakikawa, I.3
  • 28
    • 55949129082 scopus 로고    scopus 로고
    • Successive and selective release of phosphorylated peptides captured by hydroxy acidmodified metal oxide chromatography
    • Kyono Y, Sugiyama N, Imami K et al (2008) Successive and selective release of phosphorylated peptides captured by hydroxy acidmodified metal oxide chromatography. J Proteome Res 7:4585–4593
    • (2008) J Proteome Res , vol.7 , pp. 4585-4593
    • Kyono, Y.1    Sugiyama, N.2    Imami, K.3
  • 29
    • 42949170563 scopus 로고    scopus 로고
    • Automated phosphoproteome analysis for cultured cancer cells by two-dimensional NanoLC-MS using a calcined titania/C18 Biphasic column
    • Imami K, Sugiyama N, Kyono Y et al (2008) Automated phosphoproteome analysis for cultured cancer cells by two-dimensional NanoLC-MS using a calcined titania/C18 Biphasic column. Anal Sci 24:161–166
    • (2008) Anal Sci , vol.24 , pp. 161-166
    • Imami, K.1    Sugiyama, N.2    Kyono, Y.3
  • 30
    • 70449392251 scopus 로고    scopus 로고
    • Effect of peptide-to-TiO2 beads ratio on phosphopeptide enrichment selectivity
    • Li Q-R, Ning Z-B, Tang J-S et al (2009) Effect of peptide-to-TiO2 beads ratio on phosphopeptide enrichment selectivity. J Proteome Res 8:5375–5381
    • (2009) J Proteome Res , vol.8 , pp. 5375-5381
    • Li, Q.-R.1    Ning, Z.-B.2    Tang, J.-S.3
  • 31
    • 84893208515 scopus 로고    scopus 로고
    • Quantitative phosphoproteomics reveals the role of protein arginine phosphorylation in the bacterial stress response
    • Schmidt A, Trentini DB, Spiess S et al (2014) Quantitative phosphoproteomics reveals the role of protein arginine phosphorylation in the bacterial stress response. Mol Cell Proteomics 13:537–550
    • (2014) Mol Cell Proteomics , vol.13 , pp. 537-550
    • Schmidt, A.1    Trentini, D.B.2    Spiess, S.3
  • 32
    • 4344574540 scopus 로고    scopus 로고
    • Large-scale characterization of HeLa cell nuclear phosphoproteins
    • Beausoleil SA, Jedrychowski M, Schwartz D et al (2004) Large-scale characterization of HeLa cell nuclear phosphoproteins. Proc Natl Acad Sci U S A 101:12130–12135
    • (2004) Proc Natl Acad Sci U S A , vol.101 , pp. 12130-12135
    • Beausoleil, S.A.1    Jedrychowski, M.2    Schwartz, D.3
  • 33
    • 33750456519 scopus 로고    scopus 로고
    • Global, in vivo, and site-specific phosphorylation dynamics in signaling networks
    • Olsen JV, Blagoev B, Gnad F et al (2006) Global, in vivo, and site-specific phosphorylation dynamics in signaling networks. Cell 127:635–648
    • (2006) Cell , vol.127 , pp. 635-648
    • Olsen, J.V.1    Blagoev, B.2    Gnad, F.3
  • 34
    • 40549130385 scopus 로고    scopus 로고
    • Large-scale phosphoproteome analysis of human liver tissue by enrichment and fractionation of phosphopeptides with strong anion exchange chromatography
    • Han G, Ye M, Zhou H et al (2008) Large-scale phosphoproteome analysis of human liver tissue by enrichment and fractionation of phosphopeptides with strong anion exchange chromatography. Proteomics 8:1346–1361
    • (2008) Proteomics , vol.8 , pp. 1346-1361
    • Han, G.1    Ye, M.2    Zhou, H.3
  • 35
    • 42449147408 scopus 로고    scopus 로고
    • Hydrophilic interaction liquid chromatography (HILIC) in proteomics
    • Boersema PJ, Mohammed S, Heck AJR (2008) Hydrophilic interaction liquid chromatography (HILIC) in proteomics. Anal Bioanal Chem 391:151–159
    • (2008) Anal Bioanal Chem , vol.391 , pp. 151-159
    • Boersema, P.J.1    Mohammed, S.2    Heck, A.3
  • 36
    • 43849091451 scopus 로고    scopus 로고
    • Hydrophilic interaction chromatography reduces the complexity of the phosphoproteome and improves global phosphopeptide isolation and detection
    • McNulty DE, Annan RS (2008) Hydrophilic interaction chromatography reduces the complexity of the phosphoproteome and improves global phosphopeptide isolation and detection. Mol Cell Proteomics 7:971–980
    • (2008) Mol Cell Proteomics , vol.7 , pp. 971-980
    • McNulty, D.E.1    Annan, R.S.2
  • 37
    • 41149110237 scopus 로고    scopus 로고
    • Electrostatic repulsion hydrophilic interaction chromatography for isocratic separation of charged solutes and selective isolation of phosphopeptides
    • Alpert AJ (2008) Electrostatic repulsion hydrophilic interaction chromatography for isocratic separation of charged solutes and selective isolation of phosphopeptides. Anal Chem 80:62–76
    • (2008) Anal Chem , vol.80 , pp. 62-76
    • Alpert, A.J.1
  • 38
    • 36749031608 scopus 로고    scopus 로고
    • Highly efficient phosphopeptide enrichment by calcium phosphate precipitation combined with subsequent IMAC enrichment
    • Zhang X, Ye J, Jensen ON et al (2007) Highly efficient phosphopeptide enrichment by calcium phosphate precipitation combined with subsequent IMAC enrichment. Mol Cell Proteomics 6:2032–2042
    • (2007) Mol Cell Proteomics , vol.6 , pp. 2032-2042
    • Zhang, X.1    Ye, J.2    Jensen, O.N.3
  • 39
    • 52049117223 scopus 로고    scopus 로고
    • Motif-specific sampling of phosphoproteomes
    • Ruse CI, McClatchy DB, Lu B et al (2008) Motif-specific sampling of phosphoproteomes. J Proteome Res 7:2140–2150
    • (2008) J Proteome Res , vol.7 , pp. 2140-2150
    • Ruse, C.I.1    McClatchy, D.B.2    Lu, B.3
  • 40
    • 84876705178 scopus 로고    scopus 로고
    • Highly selective recovery of phosphopeptides using trypsin-assisted digestion of precipitated lanthanide-phosphoprotein complexes
    • Güzel Y, Rainer M, Mirza MR et al (2013) Highly selective recovery of phosphopeptides using trypsin-assisted digestion of precipitated lanthanide-phosphoprotein complexes. Analyst 138:2897–2905
    • (2013) Analyst , vol.138 , pp. 2897-2905
    • Güzel, Y.1    Rainer, M.2    Mirza, M.R.3
  • 41
    • 65349147669 scopus 로고    scopus 로고
    • Chemical tagging strategies for mass spectrometry-based phospho-proteomics
    • Leitner A, Lindner W (2009) Chemical tagging strategies for mass spectrometry-based phospho-proteomics. Methods Mol Biol 527:229–243
    • (2009) Methods Mol Biol , vol.527 , pp. 229-243
    • Leitner, A.1    Lindner, W.2
  • 42
    • 0035072715 scopus 로고    scopus 로고
    • A systematic approach to the analysis of protein phosphorylation
    • Zhou H, Watts JD, Aebersold R (2001) A systematic approach to the analysis of protein phosphorylation. Nat Biotechnol 19:375–378
    • (2001) Nat Biotechnol , vol.19 , pp. 375-378
    • Zhou, H.1    Watts, J.D.2    Aebersold, R.3
  • 43
    • 23144441172 scopus 로고    scopus 로고
    • Quantitative phosphoproteome analysis using a dendrimer conjugation chemistry and tandem mass spectrometry
    • Tao WA, Wollscheid B, O’Brien R et al (2005) Quantitative phosphoproteome analysis using a dendrimer conjugation chemistry and tandem mass spectrometry. Nat Methods 2:591–598
    • (2005) Nat Methods , vol.2 , pp. 591-598
    • Tao, W.A.1    Wollscheid, B.2    O’Brien, R.3
  • 44
    • 84865773882 scopus 로고    scopus 로고
    • Phosphopeptide characterization by mass spectrometry using reversed-phase supports for solid-phase β-elimination/michael addition
    • Nika H, Lee J, Willis IM et al (2012) Phosphopeptide characterization by mass spectrometry using reversed-phase supports for solid-phase β-elimination/michael addition. J Biomol Tech 23:51–68
    • (2012) J Biomol Tech , vol.23 , pp. 51-68
    • Nika, H.1    Lee, J.2    Willis, I.M.3
  • 45
    • 84883614316 scopus 로고    scopus 로고
    • Optimization of the β-elimination/michael addition chemistry on reversed-phase supports for mass spectrometry analysis of O-linked protein modifications
    • Nika H, Nieves E, Hawke DH et al (2013) Optimization of the β-elimination/michael addition chemistry on reversed-phase supports for mass spectrometry analysis of O-linked protein modifications. J Biomol Tech 24:132–153
    • (2013) J Biomol Tech , vol.24 , pp. 132-153
    • Nika, H.1    Nieves, E.2    Hawke, D.H.3
  • 46
    • 84860636838 scopus 로고    scopus 로고
    • Single-step inline hydroxyapatite enrichment facilitates identification and quantitation of phosphopeptides from mass-limited proteomes with MudPIT
    • Fonslow BR, Niessen SM, Singh M et al (2012) Single-step inline hydroxyapatite enrichment facilitates identification and quantitation of phosphopeptides from mass-limited proteomes with MudPIT. J Proteome Res 11:2697–2709
    • (2012) J Proteome Res , vol.11 , pp. 2697-2709
    • Fonslow, B.R.1    Niessen, S.M.2    Singh, M.3
  • 47
    • 84892736472 scopus 로고    scopus 로고
    • Singlecrystalline hyperbranched nanostructure of iron hydroxyl phosphate Fe5 (PO4)4 (OH)3 x 2 H2 O for highly selective capture of phosphopeptides
    • 2 O for highly selective capture of phosphopeptides. Sci Rep 4:3753
    • (2014) Sci Rep , vol.4 , pp. 3753
    • Chen, Q.1    Wei, C.2    Zhang, Y.3
  • 48
    • 84862924598 scopus 로고    scopus 로고
    • Zirconium arsenate-modified magnetic nanoparticles: Preparation, characterization and application to the enrichment of phosphopeptides
    • Li X-S, Xu L-D, Zhu G-T et al (2012) Zirconium arsenate-modified magnetic nanoparticles: preparation, characterization and application to the enrichment of phosphopeptides. Analyst 137:959–967
    • (2012) Analyst , vol.137 , pp. 959-967
    • Li, X.-S.1    Xu, L.-D.2    Zhu, G.-T.3
  • 49
    • 84873291025 scopus 로고    scopus 로고
    • SnO2 - ZnSn(OH)6 : A novel binary affinity probe for global phosphopeptide detection
    • 6 : a novel binary affinity probe for global phosphopeptide detection. Chem Commun 49:1762–1764
    • (2013) Chem Commun , vol.49 , pp. 1762-1764
    • Li, L.-P.1    Zheng, T.2    Xu, L.-N.3
  • 50
    • 84883351796 scopus 로고    scopus 로고
    • REPO4 (RE = La, Nd, Eu) affinity nanorods modified on a MALDI plate for rapid capture of target peptides from complex biosamples
    • 4 (RE = La, Nd, Eu) affinity nanorods modified on a MALDI plate for rapid capture of target peptides from complex biosamples. Chem Commun 49:8492–8494
    • (2013) Chem Commun , vol.49 , pp. 8492-8494
    • Cheng, G.1    Li, S.-M.2    Wang, Y.3
  • 51
    • 84880101965 scopus 로고    scopus 로고
    • Yolk-shell magnetic microspheres with mesoporous yttrium phosphate shells for selective capture and identification of phosphopeptides
    • Cheng G, Liu Y-L, Wang Z-G et al (2013) Yolk-shell magnetic microspheres with mesoporous yttrium phosphate shells for selective capture and identification of phosphopeptides. J Mater Chem B 1:3661–3669
    • (2013) J Mater Chem B , vol.1 , pp. 3661-3669
    • Cheng, G.1    Liu, Y.-L.2    Wang, Z.-G.3
  • 52
    • 84898832730 scopus 로고    scopus 로고
    • Enrichment and desalting of tryptic protein digests and the protein depletion using boron nitride
    • Fischnaller M, Köck R, Bakry R et al (2014) Enrichment and desalting of tryptic protein digests and the protein depletion using boron nitride. Anal Chim Acta 823:40–50
    • (2014) Anal Chim Acta , vol.823 , pp. 40-50
    • Fischnaller, M.1    Köck, R.2    Bakry, R.3
  • 53
    • 84896540445 scopus 로고    scopus 로고
    • Boron nitride as desalting material in combination with phosphopeptide enrichment in shotgun proteomics
    • Furuhashi T, Nukarinen E, Ota S et al (2014) Boron nitride as desalting material in combination with phosphopeptide enrichment in shotgun proteomics. Anal Biochem 452:16–18
    • (2014) Anal Biochem , vol.452 , pp. 16-18
    • Furuhashi, T.1    Nukarinen, E.2    Ota, S.3
  • 54
    • 84869815389 scopus 로고    scopus 로고
    • Complementary workfl ow for global phosphoproteome analysis
    • Li Q-R, Ning Z-B, Yang X-L (2012) Complementary workfl ow for global phosphoproteome analysis. Electrophoresis 33:3291–3298
    • (2012) Electrophoresis , vol.33 , pp. 3291-3298
    • Li, Q.-R.1    Ning, Z.-B.2    Yang, X.-L.3
  • 55
    • 42649139982 scopus 로고    scopus 로고
    • SIMAC (Sequential elution from IMAC), a phosphoproteomics strategy for the rapid separation of monophosphorylated from multiply phosphorylated peptides
    • Thingholm TE, Jensen ON, Robinson PJ et al (2008) SIMAC (sequential elution from IMAC), a phosphoproteomics strategy for the rapid separation of monophosphorylated from multiply phosphorylated peptides. Mol Cell Proteomics 7:661–671
    • (2008) Mol Cell Proteomics , vol.7 , pp. 661-671
    • Thingholm, T.E.1    Jensen, O.N.2    Robinson, P.J.3
  • 56
    • 84866093349 scopus 로고    scopus 로고
    • TiSH—a robust and sensitive global phosphoproteomics strategy employing a combination of TiO2 , SIMAC, and HILIC
    • 2 , SIMAC, and HILIC. J Proteomics 75:5749–5761
    • (2012) J Proteomics , vol.75 , pp. 5749-5761
    • Engholm-Keller, K.1    Birck, P.2    Storling, J.3
  • 57
    • 84879637572 scopus 로고    scopus 로고
    • Integrated proteomic analysis of posttranslational modifications by serial enrichment
    • Mertins P, Qiao JW, Patel J et al (2013) Integrated proteomic analysis of posttranslational modifications by serial enrichment. Nat Methods 10:634–637
    • (2013) Nat Methods , vol.10 , pp. 634-637
    • Mertins, P.1    Qiao, J.W.2    Patel, J.3
  • 58
    • 84879613791 scopus 로고    scopus 로고
    • Global analysis of phosphorylation and ubiquitylation cross-talk in protein degradation
    • Swaney DL, Beltrao P, Starita L et al (2013) Global analysis of phosphorylation and ubiquitylation cross-talk in protein degradation. Nat Methods 10:676–682
    • (2013) Nat Methods , vol.10 , pp. 676-682
    • Swaney, D.L.1    Beltrao, P.2    Starita, L.3
  • 59
    • 84905264803 scopus 로고    scopus 로고
    • Convergence of ubiquitylation and phosphorylation signaling in rapamycin-treated yeast cells
    • Iesmantavicius V, Weinert BT, Choudhary C (2014) Convergence of ubiquitylation and phosphorylation signaling in rapamycin-treated yeast cells. Mol Cell Proteomics 13:1979–1992
    • (2014) Mol Cell Proteomics , vol.13 , pp. 1979-1992
    • Iesmantavicius, V.1    Weinert, B.T.2    Choudhary, C.3
  • 60
    • 84902031172 scopus 로고    scopus 로고
    • Evolution and functional cross-talk of protein post-translational modifications
    • Beltrao P, Bork P, Krogan NJ et al (2013) Evolution and functional cross-talk of protein post-translational modifications. Mol Syst Biol 9:714
    • (2013) Mol Syst Biol , vol.9 , pp. 714
    • Beltrao, P.1    Bork, P.2    Krogan, N.J.3
  • 61
    • 0036198435 scopus 로고    scopus 로고
    • Phosphoproteome analysis by mass spectrometry and its application to Saccharomyces cerevisiae
    • Ficarro SB, McCleland ML, Stukenberg PT et al (2002) Phosphoproteome analysis by mass spectrometry and its application to Saccharomyces cerevisiae. Nat Biotechnol 20:301–305
    • (2002) Nat Biotechnol , vol.20 , pp. 301-305
    • Ficarro, S.B.1    McCleland, M.L.2    Stukenberg, P.T.3
  • 62
    • 84878633937 scopus 로고    scopus 로고
    • Orbitrap mass spectrometry
    • Zubarev RA, Makarov A (2013) Orbitrap mass spectrometry. Anal Chem 85:5288–5296
    • (2013) Anal Chem , vol.85 , pp. 5288-5296
    • Zubarev, R.A.1    Makarov, A.2
  • 63
    • 80052803732 scopus 로고    scopus 로고
    • Improving depth in phosphoproteomics by using a strong cation exchangeweak anion exchange-reversed phase multidimensional separation approach
    • Hennrich ML, Groenewold V, Kops GJ, Heck AJ et al (2011) Improving depth in phosphoproteomics by using a strong cation exchangeweak anion exchange-reversed phase multidimensional separation approach. Anal Chem 83:7137–7143
    • (2011) Anal Chem , vol.83 , pp. 7137-7143
    • Hennrich, M.L.1    Groenewold, V.2    Kops, G.J.3    Heck, A.J.4
  • 64
    • 84858809599 scopus 로고    scopus 로고
    • Ultra acidic strong cation exchange enabling the efficient enrichment of basic phosphopeptides
    • Hennrich ML, van den Toorn HWP, Groenewold V et al (2012) Ultra acidic strong cation exchange enabling the efficient enrichment of basic phosphopeptides. Anal Chem 84:1804–1808
    • (2012) Anal Chem , vol.84 , pp. 1804-1808
    • Hennrich, M.L.1    Van Den Toorn, H.2    Groenewold, V.3
  • 65
    • 78650466243 scopus 로고    scopus 로고
    • A tissue-specific atlas of mouse protein phosphorylation and expression
    • Huttlin EL, Jedrychowski MP, Elias JE et al (2010) A tissue-specific atlas of mouse protein phosphorylation and expression. Cell 143: 1174–1189
    • (2010) Cell , vol.143 , pp. 1174-1189
    • Huttlin, E.L.1    Jedrychowski, M.P.2    Elias, J.E.3
  • 66
    • 84863323068 scopus 로고    scopus 로고
    • Quantitative maps of protein phosphorlyation sites across 14 different rat organs and tissues
    • Lundby A, Secher A, Lage K et al (2012) Quantitative maps of protein phosphorlyation sites across 14 different rat organs and tissues. Nat Commun 3:876
    • (2012) Nat Commun , vol.3 , pp. 876
    • Lundby, A.1    Secher, A.2    Lage, K.3
  • 67
    • 84874907692 scopus 로고    scopus 로고
    • Quantitative global phosphoproteomics of human umbilical vein endothelial cells after activation of the Rap signaling pathway
    • Meijer LAT, Zhou H, Chan OYA et al (2013) Quantitative global phosphoproteomics of human umbilical vein endothelial cells after activation of the Rap signaling pathway. Mol Bio Syst 9:732–749
    • (2013) Mol Bio Syst , vol.9 , pp. 732-749
    • Meijer, L.1    Zhou, H.2    Chan, O.3
  • 68
    • 79961014854 scopus 로고    scopus 로고
    • Large-scale phosphosite quantification in tissues by a spike-in SILAC method
    • Monetti M, Nagaraj N, Sharma K et al (2011) Large-scale phosphosite quantification in tissues by a spike-in SILAC method. Nat Methods 8:655–658
    • (2011) Nat Methods , vol.8 , pp. 655-658
    • Monetti, M.1    Nagaraj, N.2    Sharma, K.3
  • 69
    • 78649849874 scopus 로고    scopus 로고
    • Feasibility of large-scale phosphoproteomics with higher energy collisional dissociation fragmentation
    • Nagaraj N, D’Souza RCJ, Cox J et al (2010) Feasibility of large-scale phosphoproteomics with higher energy collisional dissociation fragmentation. J Proteome Res 9:6786–6794
    • (2010) J Proteome Res , vol.9 , pp. 6786-6794
    • Nagaraj, N.1    D’Souza, R.2    Cox, J.3
  • 70
    • 77951644400 scopus 로고    scopus 로고
    • Quantitative phosphoproteomics reveals widespread full phosphorylation site occupancy during mitosis
    • Olsen JV, Vermeulen M, Santamaria A et al (2010) Quantitative phosphoproteomics reveals widespread full phosphorylation site occupancy during mitosis. Sci Signal 3: ra3
    • (2010) Sci Signal , vol.3
    • Olsen, J.V.1    Vermeulen, M.2    Santamaria, A.3
  • 71
    • 80053374337 scopus 로고    scopus 로고
    • Proteomic and phosphoproteomic comparison of human ES and iPS cells
    • Phanstiel DH, Brumbaugh J, Wenger CD et al (2011) Proteomic and phosphoproteomic comparison of human ES and iPS cells. Nat Methods 8:821–827
    • (2011) Nat Methods , vol.8 , pp. 821-827
    • Phanstiel, D.H.1    Brumbaugh, J.2    Wenger, C.D.3
  • 72
    • 79952752375 scopus 로고    scopus 로고
    • System-wide temporal characterization of the proteome and phosphoproteome of human embryonic stem cell differentiation
    • Rigbolt KTG, Prokhorova TA, Akimov V et al (2011) System-wide temporal characterization of the proteome and phosphoproteome of human embryonic stem cell differentiation. Sci Signal 4: rs3
    • (2011) Sci Signal , vol.4
    • Rigbolt, K.1    Prokhorova, T.A.2    Akimov, V.3
  • 73
    • 84901677321 scopus 로고    scopus 로고
    • Quantitative phosphoproteomic analysis reveals system-wide signaling pathways downstream of SDF-1/ CXCR4 in breast cancer stem cells
    • Yi T, Zhai B, Yu Y et al (2014) Quantitative phosphoproteomic analysis reveals system-wide signaling pathways downstream of SDF-1/ CXCR4 in breast cancer stem cells. Proc Natl Acad Sci U S A 111:E2182–E2190
    • (2014) Proc Natl Acad Sci U S A , vol.111
    • Yi, T.1    Zhai, B.2    Yu, Y.3
  • 74
    • 84883780981 scopus 로고    scopus 로고
    • Combination of Multistep IMAC Enrichment with High-pH Reverse Phase Separation for In-Depth Phosphoproteomic Profiling
    • Yue X-S, Hummon AB (2013) Combination of Multistep IMAC Enrichment with High-pH Reverse Phase Separation for In-Depth Phosphoproteomic Profiling. J Proteome Res 12:4176–4186
    • (2013) J Proteome Res , vol.12 , pp. 4176-4186
    • Yue, X.-S.1    Hummon, A.B.2
  • 75
    • 84864616672 scopus 로고    scopus 로고
    • Combinatorial Use of Electrostatic Repulsion-Hydrophilic Interaction Chromatography (ERLIC) and Strong Cation Exchange (SCX) Chromatography for In-Depth Phosphoproteome Analysis
    • Zarei M, Sprenger A, Gretzmeier C et al. (2012) Combinatorial Use of Electrostatic Repulsion-Hydrophilic Interaction Chromatography (ERLIC) and Strong Cation Exchange (SCX) Chromatography for In-Depth Phosphoproteome Analysis. J Proteome Res 12: 4269–4276
    • (2012) J Proteome Res , vol.12 , pp. 4269-4276
    • Zarei, M.1    Sprenger, A.2    Gretzmeier, C.3
  • 76
    • 84874093507 scopus 로고    scopus 로고
    • Toward a Comprehensive Characterization of a Human Cancer Cell Phosphoproteome
    • Zhou H, Di Palma S, Preisinger C et al. (2013) Toward a Comprehensive Characterization of a Human Cancer Cell Phosphoproteome. J Proteome Res 13:260–271
    • (2013) J Proteome Res , vol.13 , pp. 260-271
    • Zhou, H.1    Di Palma, S.2    Preisinger, C.3
  • 77
    • 84914100244 scopus 로고    scopus 로고
    • In Situ Sample Processing Approach (ISPA) for comprehensive quantitative phosphoproteome analysis
    • Huang J, Qin H, Dong J et al (2014) In Situ Sample Processing Approach (iSPA) for comprehensive quantitative phosphoproteome analysis. J Proteome Res 13:3896–3904
    • (2014) J Proteome Res , vol.13 , pp. 3896-3904
    • Huang, J.1    Qin, H.2    Dong, J.3


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.