메뉴 건너뛰기




Volumn 11, Issue 5, 2012, Pages 2697-2709

Single-step inline hydroxyapatite enrichment facilitates identification and quantitation of phosphopeptides from mass-limited proteomes with MudPIT

Author keywords

hydroxyapatite; mouse amygdale; MudPIT; phosphopeptide enrichment; phosphorylation cooperativity; whole cell lysate

Indexed keywords

HYDROXYAPATITE; PHOSPHOPEPTIDE; PROTEOME;

EID: 84860636838     PISSN: 15353893     EISSN: 15353907     Source Type: Journal    
DOI: 10.1021/pr300200x     Document Type: Article
Times cited : (50)

References (87)
  • 1
    • 36749010218 scopus 로고    scopus 로고
    • The age of crosstalk: Phosphorylation, ubiquitination, and beyond
    • Hunter, T. The age of crosstalk: phosphorylation, ubiquitination, and beyond Mol. Cell 2007, 28 (5) 730-8
    • (2007) Mol. Cell , vol.28 , Issue.5 , pp. 730-738
    • Hunter, T.1
  • 4
    • 0033611663 scopus 로고    scopus 로고
    • The Croonian Lecture 1998. Identification of a protein kinase cascade of major importance in insulin signal transduction
    • Cohen, P. The Croonian Lecture 1998. Identification of a protein kinase cascade of major importance in insulin signal transduction Philo.s Trans. R. Soc., B 1999, 354 (1382) 485-95
    • (1999) Philo.s Trans. R. Soc., B , vol.354 , Issue.1382 , pp. 485-495
    • Cohen, P.1
  • 6
    • 78651277460 scopus 로고    scopus 로고
    • PHOSIDA 2011: The posttranslational modification database
    • Gnad, F.; Gunawardena, J.; Mann, M. PHOSIDA 2011: the posttranslational modification database Nucleic Acids Res. 2011, 39 (Database issue) D253-60
    • (2011) Nucleic Acids Res. , vol.39 , Issue.DATABASE ISSUE , pp. 253-260
    • Gnad, F.1    Gunawardena, J.2    Mann, M.3
  • 7
    • 30744432140 scopus 로고    scopus 로고
    • Quantitative phosphoproteomic analysis of the tumor necrosis factor pathway
    • Cantin, G. T.; Venable, J. D.; Cociorva, D.; Yates, J. R., 3rd Quantitative phosphoproteomic analysis of the tumor necrosis factor pathway J. Proteome Res. 2006, 5 (1) 127-34
    • (2006) J. Proteome Res. , vol.5 , Issue.1 , pp. 127-134
    • Cantin, G.T.1    Venable, J.D.2    Cociorva, D.3    Yates III, J.R.4
  • 8
    • 58149385852 scopus 로고    scopus 로고
    • Quantitative analysis of brain nuclear phosphoproteins identifies developmentally regulated phosphorylation events
    • Liao, L.; McClatchy, D. B.; Park, S. K.; Xu, T.; Lu, B.; Yates, J. R., 3rd Quantitative analysis of brain nuclear phosphoproteins identifies developmentally regulated phosphorylation events J. Proteome Res. 2008, 7 (11) 4743-55
    • (2008) J. Proteome Res. , vol.7 , Issue.11 , pp. 4743-4755
    • Liao, L.1    McClatchy, D.B.2    Park, S.K.3    Xu, T.4    Lu, B.5    Yates III, J.R.6
  • 10
    • 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, P. J.; Foong, L. Y.; Ding, V. M.; Lemeer, S.; van Breukelen, B.; Philp, R.; Boekhorst, J.; Snel, B.; den Hertog, J.; Choo, A. B.; Heck, A. J. In-depth qualitative and quantitative profiling of tyrosine phosphorylation using a combination of phosphopeptide immunoaffinity purification and stable isotope dimethyl labeling Mol. Cell. Proteomics 2010, 9 (1) 84-99
    • (2010) Mol. Cell. Proteomics , vol.9 , Issue.1 , pp. 84-99
    • Boersema, P.J.1    Foong, L.Y.2    Ding, V.M.3    Lemeer, S.4    Van Breukelen, B.5    Philp, R.6    Boekhorst, J.7    Snel, B.8    Den Hertog, J.9    Choo, A.B.10    Heck, A.J.11
  • 11
    • 79251648840 scopus 로고    scopus 로고
    • Differential proteomic analysis of mammalian tissues using SILAM
    • McClatchy, D. B.; Liao, L.; Park, S. K.; Xu, T.; Lu, B.; Yates Iii, J. R. Differential proteomic analysis of mammalian tissues using SILAM PLoS One 2011, 6 (1) e16039
    • (2011) PLoS One , vol.6 , Issue.1 , pp. 16039
    • McClatchy, D.B.1    Liao, L.2    Park, S.K.3    Xu, T.4    Lu, B.5    Yates III, J.R.6
  • 15
    • 79957540957 scopus 로고    scopus 로고
    • Phosphoproteomics identifies oncogenic Ras signaling targets and their involvement in lung adenocarcinomas
    • Sudhir, P. R.; Hsu, C. L.; Wang, M. J.; Wang, Y. T.; Chen, Y. J.; Sung, T. Y.; Hsu, W. L.; Yang, U. C.; Chen, J. Y. Phosphoproteomics identifies oncogenic Ras signaling targets and their involvement in lung adenocarcinomas PLoS One 2011, 6 (5) e20199
    • (2011) PLoS One , vol.6 , Issue.5 , pp. 20199
    • Sudhir, P.R.1    Hsu, C.L.2    Wang, M.J.3    Wang, Y.T.4    Chen, Y.J.5    Sung, T.Y.6    Hsu, W.L.7    Yang, U.C.8    Chen, J.Y.9
  • 16
    • 79961014854 scopus 로고    scopus 로고
    • Large-scale phosphosite quantification in tissues by a spike-in SILAC method
    • Monetti, M.; Nagaraj, N.; Sharma, K.; Mann, M. Large-scale phosphosite quantification in tissues by a spike-in SILAC method Nat. Methods 2011, 8 (8) 655-8
    • (2011) Nat. Methods , vol.8 , Issue.8 , pp. 655-658
    • Monetti, M.1    Nagaraj, N.2    Sharma, K.3    Mann, M.4
  • 17
    • 79961013401 scopus 로고    scopus 로고
    • Correct interpretation of comprehensive phosphorylation dynamics requires normalization by protein expression changes
    • 10.1074/mcp.M111.009654
    • Wu, R.; Dephoure, N.; Haas, W.; Huttlin, E. L.; Zhai, B.; Sowa, M. E.; Gygi, S. P. Correct interpretation of comprehensive phosphorylation dynamics requires normalization by protein expression changes Mol. Cell. Proteomics 2011, 10.1074/mcp.M111.009654
    • (2011) Mol. Cell. Proteomics
    • Wu, R.1    Dephoure, N.2    Haas, W.3    Huttlin, E.L.4    Zhai, B.5    Sowa, M.E.6    Gygi, S.P.7
  • 18
    • 79960979428 scopus 로고    scopus 로고
    • A large-scale method to measure absolute protein phosphorylation stoichiometries
    • Wu, R.; Haas, W.; Dephoure, N.; Huttlin, E. L.; Zhai, B.; Sowa, M. E.; Gygi, S. P. A large-scale method to measure absolute protein phosphorylation stoichiometries Nat. Methods 2011, 8 (8) 677-83
    • (2011) Nat. Methods , vol.8 , Issue.8 , pp. 677-683
    • Wu, R.1    Haas, W.2    Dephoure, N.3    Huttlin, E.L.4    Zhai, B.5    Sowa, M.E.6    Gygi, S.P.7
  • 19
    • 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 (5) 971-80
    • (2008) Mol. Cell. Proteomics , vol.7 , Issue.5 , pp. 971-980
    • McNulty, D.E.1    Annan, R.S.2
  • 20
    • 84984933087 scopus 로고    scopus 로고
    • The SCX/IMAC enrichment approach for global phosphorylation analysis by mass spectrometry
    • Villen, J.; Gygi, S. P. The SCX/IMAC enrichment approach for global phosphorylation analysis by mass spectrometry Nat. Protoc. 2008, 3 (10) 1630-8
    • (2008) Nat. Protoc. , vol.3 , Issue.10 , pp. 1630-1638
    • Villen, J.1    Gygi, S.P.2
  • 21
    • 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., 3rd Large-scale analysis of the yeast proteome by multidimensional protein identification technology Nat. Biotechnol. 2001, 19 (3) 242-7
    • (2001) Nat. Biotechnol. , vol.19 , Issue.3 , pp. 242-247
    • Washburn, M.P.1    Wolters, D.2    Yates III, J.R.3
  • 22
    • 0035582244 scopus 로고    scopus 로고
    • An automated multidimensional protein identification technology for shotgun proteomics
    • Wolters, D. A.; Washburn, M. P.; Yates, J. R., III An automated multidimensional protein identification technology for shotgun proteomics Anal. Chem. 2001, 73 (23) 5683-5690
    • (2001) Anal. Chem. , vol.73 , Issue.23 , pp. 5683-5690
    • Wolters, D.A.1    Washburn, M.P.2    Yates III, J.R.3
  • 23
    • 80054711609 scopus 로고    scopus 로고
    • Microscale phosphoproteome analysis of 10,000 cells from human cancer cell lines
    • Masuda, T.; Sugiyama, N.; Tomita, M.; Ishihama, Y. Microscale phosphoproteome analysis of 10,000 cells from human cancer cell lines Anal. Chem. 2011, 83 (20) 7698-703
    • (2011) Anal. Chem. , vol.83 , Issue.20 , pp. 7698-7703
    • Masuda, T.1    Sugiyama, N.2    Tomita, M.3    Ishihama, Y.4
  • 24
    • 34347216365 scopus 로고    scopus 로고
    • Optimizing TiO2-based phosphopeptide enrichment for automated multidimensional liquid chromatography coupled to tandem mass spectrometry
    • Cantin, G. T.; Shock, T. R.; Park, S. K.; Madhani, H. D.; Yates, J. R., 3rd Optimizing TiO2-based phosphopeptide enrichment for automated multidimensional liquid chromatography coupled to tandem mass spectrometry Anal. Chem. 2007, 79 (12) 4666-73
    • (2007) Anal. Chem. , vol.79 , Issue.12 , pp. 4666-4673
    • Cantin, G.T.1    Shock, T.R.2    Park, S.K.3    Madhani, H.D.4    Yates III, J.R.5
  • 25
    • 47749097929 scopus 로고    scopus 로고
    • Phosphorylation by casein kinase 1 regulates tonicity-induced osmotic response element-binding protein/tonicity enhancer-binding protein nucleocytoplasmic trafficking
    • Xu, S.; Wong, C. C.; Tong, E. H.; Chung, S. S.; Yates, J. R., 3rd; Yin, Y.; Ko, B. C. Phosphorylation by casein kinase 1 regulates tonicity-induced osmotic response element-binding protein/tonicity enhancer-binding protein nucleocytoplasmic trafficking J. Biol. Chem. 2008, 283 (25) 17624-34
    • (2008) J. Biol. Chem. , vol.283 , Issue.25 , pp. 17624-17634
    • Xu, S.1    Wong, C.C.2    Tong, E.H.3    Chung, S.S.4    Yates III, J.R.5    Yin, Y.6    Ko, B.C.7
  • 26
    • 67649683032 scopus 로고    scopus 로고
    • Budding yeast centrosome duplication requires stabilization of Spc29 via Mps1-mediated phosphorylation
    • Holinger, E. P.; Old, W. M.; Giddings, T. H., Jr.; Wong, C.; Yates, J. R., 3rd; Winey, M. Budding yeast centrosome duplication requires stabilization of Spc29 via Mps1-mediated phosphorylation J. Biol. Chem. 2009, 284 (19) 12949-55
    • (2009) J. Biol. Chem. , vol.284 , Issue.19 , pp. 12949-12955
    • Holinger, E.P.1    Old, W.M.2    Giddings Jr., T.H.3    Wong, C.4    Yates III, J.R.5    Winey, M.6
  • 27
    • 0001565428 scopus 로고
    • Crystal structure of hydroxyapatite
    • Kay, M. I.; Young, R. A.; Posner, A. S. Crystal structure of hydroxyapatite Nature 1964, 204, 1050-2
    • (1964) Nature , vol.204 , pp. 1050-1052
    • Kay, M.I.1    Young, R.A.2    Posner, A.S.3
  • 28
    • 0029146115 scopus 로고
    • Osteopontin and related phosphorylated sialoproteins: Effects on mineralization
    • Boskey, A. L. Osteopontin and related phosphorylated sialoproteins: effects on mineralization Ann. N.Y. Acad. Sci. 1995, 760, 249-56
    • (1995) Ann. N.Y. Acad. Sci. , vol.760 , pp. 249-256
    • Boskey, A.L.1
  • 29
    • 71549141982 scopus 로고    scopus 로고
    • Protein chromatography on hydroxyapatite columns
    • Cummings, L. J.; Snyder, M. A.; Brisack, K. Protein chromatography on hydroxyapatite columns Methods Enzymol. 2009, 463, 387-404
    • (2009) Methods Enzymol. , vol.463 , pp. 387-404
    • Cummings, L.J.1    Snyder, M.A.2    Brisack, K.3
  • 30
    • 34047253349 scopus 로고    scopus 로고
    • Current methods for phosphoprotein isolation and enrichment
    • Schmidt, S. R.; Schweikart, F.; Andersson, M. E. Current methods for phosphoprotein isolation and enrichment J. Chromatogr., B 2007, 849 (1-2) 154-62
    • (2007) J. Chromatogr., B , vol.849 , Issue.1-2 , pp. 154-162
    • Schmidt, S.R.1    Schweikart, F.2    Andersson, M.E.3
  • 33
    • 76649129012 scopus 로고    scopus 로고
    • Hydroxyapatite affinity chromatography for the highly selective enrichment of mono- and multi-phosphorylated peptides in phosphoproteome analysis
    • Mamone, G.; Picariello, G.; Ferranti, P.; Addeo, F. Hydroxyapatite affinity chromatography for the highly selective enrichment of mono- and multi-phosphorylated peptides in phosphoproteome analysis Proteomics 2010, 10 (3) 380-93
    • (2010) Proteomics , vol.10 , Issue.3 , pp. 380-393
    • Mamone, G.1    Picariello, G.2    Ferranti, P.3    Addeo, F.4
  • 34
    • 77957320034 scopus 로고    scopus 로고
    • Control of selectivity via nanochemistry: Monolithic capillary column containing hydroxyapatite nanoparticles for separation of proteins and enrichment of phosphopeptides
    • Krenkova, J.; Lacher, N. A.; Svec, F. Control of selectivity via nanochemistry: monolithic capillary column containing hydroxyapatite nanoparticles for separation of proteins and enrichment of phosphopeptides Anal. Chem. 2010, 82 (19) 8335-41
    • (2010) Anal. Chem. , vol.82 , Issue.19 , pp. 8335-8341
    • Krenkova, J.1    Lacher, N.A.2    Svec, F.3
  • 35
    • 34249335982 scopus 로고    scopus 로고
    • 15N metabolic labeling of mammalian tissue with slow protein turnover
    • McClatchy, D. B.; Dong, M. Q.; Wu, C. C.; Venable, J. D.; Yates, J. R., 3rd 15N metabolic labeling of mammalian tissue with slow protein turnover J. Proteome Res. 2007, 6 (5) 2005-10
    • (2007) J. Proteome Res. , vol.6 , Issue.5 , pp. 2005-2010
    • McClatchy, D.B.1    Dong, M.Q.2    Wu, C.C.3    Venable, J.D.4    Yates III, J.R.5
  • 36
    • 4444346217 scopus 로고    scopus 로고
    • Metabolic labeling of mammalian organisms with stable isotopes for quantitative proteomic analysis
    • Wu, C. C.; MacCoss, M. J.; Howell, K. E.; Matthews, D. E.; Yates, J. R., 3rd Metabolic labeling of mammalian organisms with stable isotopes for quantitative proteomic analysis Anal. Chem. 2004, 76 (17) 4951-9
    • (2004) Anal. Chem. , vol.76 , Issue.17 , pp. 4951-4959
    • Wu, C.C.1    MacCoss, M.J.2    Howell, K.E.3    Matthews, D.E.4    Yates III, J.R.5
  • 37
    • 28544433959 scopus 로고    scopus 로고
    • Measurement of the isotope enrichment of stable isotope-labeled proteins using high-resolution mass spectra of peptides
    • MacCoss, M. J.; Wu, C. C.; Matthews, D. E.; Yates, J. R., 3rd Measurement of the isotope enrichment of stable isotope-labeled proteins using high-resolution mass spectra of peptides Anal. Chem. 2005, 77 (23) 7646-53
    • (2005) Anal. Chem. , vol.77 , Issue.23 , pp. 7646-7653
    • MacCoss, M.J.1    Wu, C.C.2    Matthews, D.E.3    Yates III, J.R.4
  • 40
    • 43349089502 scopus 로고    scopus 로고
    • Validation of tandem mass spectrometry database search results using DTASelect
    • Wiley: New York, Chapter 13, Unit 13 4
    • Cociorva, D.; Tabb, D. L.; Yates, J. R., Validation of tandem mass spectrometry database search results using DTASelect. In Current Protocols in Bioinformatics; Wiley: New York, 2007; Chapter 13, Unit 13 4.
    • (2007) Current Protocols in Bioinformatics
    • Cociorva, D.1    Tabb, D.L.2    Yates, J.R.3
  • 41
    • 0036393898 scopus 로고    scopus 로고
    • DTASelect and Contrast: Tools for assembling and comparing protein identifications from shotgun proteomics
    • Tabb, D. L.; McDonald, W. H.; Yates, J. R., 3rd DTASelect and Contrast: tools for assembling and comparing protein identifications from shotgun proteomics J. Proteome Res. 2002, 1 (1) 21-6
    • (2002) J. Proteome Res. , vol.1 , Issue.1 , pp. 21-26
    • Tabb, D.L.1    McDonald, W.H.2    Yates III, J.R.3
  • 42
    • 33749853607 scopus 로고    scopus 로고
    • A probability-based approach for high-throughput protein phosphorylation analysis and site localization
    • Beausoleil, S. A.; Villen, J.; Gerber, S. A.; Rush, J.; Gygi, S. P. A probability-based approach for high-throughput protein phosphorylation analysis and site localization Nat. Biotechnol. 2006, 24 (10) 1285-92
    • (2006) Nat. Biotechnol. , vol.24 , Issue.10 , pp. 1285-1292
    • Beausoleil, S.A.1    Villen, J.2    Gerber, S.A.3    Rush, J.4    Gygi, S.P.5
  • 43
    • 33847194634 scopus 로고    scopus 로고
    • Automatic validation of phosphopeptide identifications from tandem mass spectra
    • Lu, B.; Ruse, C.; Xu, T.; Park, S. K.; Yates, J., 3rd Automatic validation of phosphopeptide identifications from tandem mass spectra Anal. Chem. 2007, 79 (4) 1301-10
    • (2007) Anal. Chem. , vol.79 , Issue.4 , pp. 1301-1310
    • Lu, B.1    Ruse, C.2    Xu, T.3    Park, S.K.4    Yates III, J.5
  • 44
    • 41549117597 scopus 로고    scopus 로고
    • A quantitative analysis software tool for mass spectrometry-based proteomics
    • Park, S. K.; Venable, J. D.; Xu, T.; Yates, J. R., 3rd A quantitative analysis software tool for mass spectrometry-based proteomics Nat. Methods 2008, 5 (4) 319-22
    • (2008) Nat. Methods , vol.5 , Issue.4 , pp. 319-322
    • Park, S.K.1    Venable, J.D.2    Xu, T.3    Yates III, J.R.4
  • 45
    • 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.; Yates, J. R., 3rd Combining protein-based IMAC, peptide-based IMAC, and MudPIT for efficient phosphoproteomic analysis J. Proteome Res. 2008, 7 (3) 1346-51
    • (2008) J. Proteome Res. , vol.7 , Issue.3 , 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
  • 46
    • 77954375657 scopus 로고    scopus 로고
    • Optimized IMAC-IMAC protocol for phosphopeptide recovery from complex biological samples
    • Ye, J.; Zhang, X.; Young, C.; Zhao, X.; Hao, Q.; Cheng, L.; Jensen, O. N. Optimized IMAC-IMAC protocol for phosphopeptide recovery from complex biological samples J. Proteome Res. 2010, 9 (7) 3561-73
    • (2010) J. Proteome Res. , vol.9 , Issue.7 , pp. 3561-3573
    • Ye, J.1    Zhang, X.2    Young, C.3    Zhao, X.4    Hao, Q.5    Cheng, L.6    Jensen, O.N.7
  • 47
    • 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.; Jorgensen, T. J. Highly selective enrichment of phosphorylated peptides from peptide mixtures using titanium dioxide microcolumns Mol. Cell. Proteomics 2005, 4 (7) 873-86
    • (2005) Mol. Cell. Proteomics , vol.4 , Issue.7 , pp. 873-886
    • Larsen, M.R.1    Thingholm, T.E.2    Jensen, O.N.3    Roepstorff, P.4    Jorgensen, T.J.5
  • 48
    • 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.; Nakamura, A.; Tomita, M.; Ishihama, Y. Phosphopeptide enrichment by aliphatic hydroxy acid-modified metal oxide chromatography for nano-LC-MS/MS in proteomics applications Mol. Cell. Proteomics 2007, 6 (6) 1103-9
    • (2007) Mol. Cell. Proteomics , vol.6 , Issue.6 , pp. 1103-1109
    • Sugiyama, N.1    Masuda, T.2    Shinoda, K.3    Nakamura, A.4    Tomita, M.5    Ishihama, Y.6
  • 49
    • 0028218041 scopus 로고
    • A selective precipitation purification procedure for multiple phosphoseryl-containing peptides and methods for their identification
    • Reynolds, E. C.; Riley, P. F.; Adamson, N. J. A selective precipitation purification procedure for multiple phosphoseryl-containing peptides and methods for their identification Anal. Biochem. 1994, 217 (2) 277-84
    • (1994) Anal. Biochem. , vol.217 , Issue.2 , pp. 277-284
    • Reynolds, E.C.1    Riley, P.F.2    Adamson, N.J.3
  • 50
    • 51649095905 scopus 로고    scopus 로고
    • Phosphoproteomic analysis of human brain by calcium phosphate precipitation and mass spectrometry
    • Xia, Q.; Cheng, D.; Duong, D. M.; Gearing, M.; Lah, J. J.; Levey, A. I.; Peng, J. Phosphoproteomic analysis of human brain by calcium phosphate precipitation and mass spectrometry J. Proteome Res. 2008, 7 (7) 2845-51
    • (2008) J. Proteome Res. , vol.7 , Issue.7 , pp. 2845-2851
    • Xia, Q.1    Cheng, D.2    Duong, D.M.3    Gearing, M.4    Lah, J.J.5    Levey, A.I.6    Peng, J.7
  • 51
    • 36749031608 scopus 로고    scopus 로고
    • Highly efficient phosphopeptide enrichment by calcium phosphate precipitation combined with subsequent IMAC enrichment
    • Zhang, X.; Ye, J.; Jensen, O. N.; Roepstorff, P. Highly efficient phosphopeptide enrichment by calcium phosphate precipitation combined with subsequent IMAC enrichment Mol. Cell. Proteomics 2007, 6 (11) 2032-42
    • (2007) Mol. Cell. Proteomics , vol.6 , Issue.11 , pp. 2032-2042
    • Zhang, X.1    Ye, J.2    Jensen, O.N.3    Roepstorff, P.4
  • 54
    • 0000857494 scopus 로고
    • An approach to correlate tandem mass-spectral data of peptides with amino-acid-sequences in a protein database
    • Eng, J. K.; Mccormack, A. L.; Yates, J. R. An approach to correlate tandem mass-spectral data of peptides with amino-acid-sequences in a protein database J. Am. Soc. Mass Spectrom. 1994, 5 (11) 976-89
    • (1994) J. Am. Soc. Mass Spectrom. , vol.5 , Issue.11 , pp. 976-989
    • Eng, J.K.1    McCormack, A.L.2    Yates, J.R.3
  • 55
    • 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.; Coon, J. J. A neutral loss activation method for improved phosphopeptide sequence analysis by quadrupole ion trap mass spectrometry Anal. Chem. 2004, 76 (13) 3590-8
    • (2004) Anal. Chem. , vol.76 , Issue.13 , pp. 3590-3598
    • Schroeder, M.J.1    Shabanowitz, J.2    Schwartz, J.C.3    Hunt, D.F.4    Coon, J.J.5
  • 58
    • 33746263848 scopus 로고    scopus 로고
    • Automated ultra-high-pressure multidimensional protein identification technology (UHP-MudPIT) for improved peptide identification of proteomic samples
    • Motoyama, A.; Venable, J. D.; Ruse, C. I.; Yates, J. R., 3rd Automated ultra-high-pressure multidimensional protein identification technology (UHP-MudPIT) for improved peptide identification of proteomic samples Anal. Chem. 2006, 78 (14) 5109-18
    • (2006) Anal. Chem. , vol.78 , Issue.14 , pp. 5109-5118
    • Motoyama, A.1    Venable, J.D.2    Ruse, C.I.3    Yates III, J.R.4
  • 60
    • 33847616949 scopus 로고    scopus 로고
    • Reproducible isolation of distinct, overlapping segments of the phosphoproteome
    • Bodenmiller, B.; Mueller, L. N.; Mueller, M.; Domon, B.; Aebersold, R. Reproducible isolation of distinct, overlapping segments of the phosphoproteome Nat. Methods 2007, 4 (3) 231-7
    • (2007) Nat. Methods , vol.4 , Issue.3 , pp. 231-237
    • Bodenmiller, B.1    Mueller, L.N.2    Mueller, M.3    Domon, B.4    Aebersold, R.5
  • 61
    • 79956146702 scopus 로고    scopus 로고
    • Classification of protein binding in hydroxyapatite chromatography: Synergistic interactions on the molecular scale
    • Hou, Y.; Morrison, C. J.; Cramer, S. M. Classification of protein binding in hydroxyapatite chromatography: synergistic interactions on the molecular scale Anal. Chem. 2011, 83 (10) 3709-16
    • (2011) Anal. Chem. , vol.83 , Issue.10 , pp. 3709-3716
    • Hou, Y.1    Morrison, C.J.2    Cramer, S.M.3
  • 62
    • 0025731508 scopus 로고
    • Role of acidic residues as substrate determinants for casein kinase i
    • Flotow, H.; Roach, P. J. Role of acidic residues as substrate determinants for casein kinase I J. Biol. Chem. 1991, 266 (6) 3724-7
    • (1991) J. Biol. Chem. , vol.266 , Issue.6 , pp. 3724-3727
    • Flotow, H.1    Roach, P.J.2
  • 63
    • 0037334895 scopus 로고    scopus 로고
    • One-thousand-and-one substrates of protein kinase CK2?
    • Meggio, F.; Pinna, L. A. One-thousand-and-one substrates of protein kinase CK2? FASEB J. 2003, 17 (3) 349-68
    • (2003) FASEB J. , vol.17 , Issue.3 , pp. 349-368
    • Meggio, F.1    Pinna, L.A.2
  • 64
    • 67349211782 scopus 로고    scopus 로고
    • Extraordinary pleiotropy of protein kinase CK2 revealed by weblogo phosphoproteome analysis
    • Salvi, M.; Sarno, S.; Cesaro, L.; Nakamura, H.; Pinna, L. A. Extraordinary pleiotropy of protein kinase CK2 revealed by weblogo phosphoproteome analysis Biochim. Biophys. Acta 2009, 1793 (5) 847-59
    • (2009) Biochim. Biophys. Acta , vol.1793 , Issue.5 , pp. 847-859
    • Salvi, M.1    Sarno, S.2    Cesaro, L.3    Nakamura, H.4    Pinna, L.A.5
  • 65
    • 84872864632 scopus 로고    scopus 로고
    • Protein kinase CK2 in health and disease: Protein kinase CK2: An ugly duckling in the kinome pond
    • Pinna, L. A.; Allende, J. E. Protein kinase CK2 in health and disease: Protein kinase CK2: an ugly duckling in the kinome pond Cell. Mol. Life Sci. 2009, 66 (11-12) 1795-9
    • (2009) Cell. Mol. Life Sci. , vol.66 , Issue.11-12 , pp. 1795-1799
    • Pinna, L.A.1    Allende, J.E.2
  • 66
    • 70349320107 scopus 로고    scopus 로고
    • Protein kinase CK2 in health and disease: CK2: A key player in cancer biology
    • Trembley, J. H.; Wang, G.; Unger, G.; Slaton, J.; Ahmed, K. Protein kinase CK2 in health and disease: CK2: a key player in cancer biology Cell. Mol. Life Sci. 2009, 66 (11-12) 1858-67
    • (2009) Cell. Mol. Life Sci. , vol.66 , Issue.11-12 , pp. 1858-1867
    • Trembley, J.H.1    Wang, G.2    Unger, G.3    Slaton, J.4    Ahmed, K.5
  • 67
    • 49749110451 scopus 로고    scopus 로고
    • Protein kinase CK2 as a druggable target
    • Sarno, S.; Pinna, L. A. Protein kinase CK2 as a druggable target Mol. Biosyst. 2008, 4 (9) 889-94
    • (2008) Mol. Biosyst. , vol.4 , Issue.9 , pp. 889-894
    • Sarno, S.1    Pinna, L.A.2
  • 68
    • 70349326247 scopus 로고    scopus 로고
    • Protein kinase CK2 in health and disease: CK2 and its role in Wnt and NF-kappaB signaling: Linking development and cancer
    • Dominguez, I.; Sonenshein, G. E.; Seldin, D. C. Protein kinase CK2 in health and disease: CK2 and its role in Wnt and NF-kappaB signaling: linking development and cancer Cell. Mol. Life Sci. 2009, 66 (11-12) 1850-7
    • (2009) Cell. Mol. Life Sci. , vol.66 , Issue.11-12 , pp. 1850-1857
    • Dominguez, I.1    Sonenshein, G.E.2    Seldin, D.C.3
  • 69
    • 70349326246 scopus 로고    scopus 로고
    • Protein kinase CK2 in health and disease: CK2: The kinase controlling the Hsp90 chaperone machinery
    • Miyata, Y. Protein kinase CK2 in health and disease: CK2: the kinase controlling the Hsp90 chaperone machinery Cell. Mol. Life Sci. 2009, 66 (11-12) 1840-9
    • (2009) Cell. Mol. Life Sci. , vol.66 , Issue.11-12 , pp. 1840-1849
    • Miyata, Y.1
  • 70
    • 70349186117 scopus 로고    scopus 로고
    • Protein kinase CK2 in health and disease: From birth to death: The role of protein kinase CK2 in the regulation of cell proliferation and survival
    • St-Denis, N. A.; Litchfield, D. W. Protein kinase CK2 in health and disease: From birth to death: the role of protein kinase CK2 in the regulation of cell proliferation and survival Cell. Mol. Life Sci. 2009, 66 (11-12) 1817-29
    • (2009) Cell. Mol. Life Sci. , vol.66 , Issue.11-12 , pp. 1817-1829
    • St-Denis, N.A.1    Litchfield, D.W.2
  • 71
    • 77649117952 scopus 로고    scopus 로고
    • Cooperativity within proximal phosphorylation sites is revealed from large-scale proteomics data
    • Schweiger, R.; Linial, M. Cooperativity within proximal phosphorylation sites is revealed from large-scale proteomics data Biol. Direct 2010, 5, 6
    • (2010) Biol. Direct , vol.5 , pp. 6
    • Schweiger, R.1    Linial, M.2
  • 72
    • 77951634725 scopus 로고    scopus 로고
    • Systems-wide proteomic characterization of combinatorial post-translational modification patterns
    • Young, N. L.; Plazas-Mayorca, M. D.; Garcia, B. A. Systems-wide proteomic characterization of combinatorial post-translational modification patterns Expert Rev. Proteomics 2010, 7 (1) 79-92
    • (2010) Expert Rev. Proteomics , vol.7 , Issue.1 , pp. 79-92
    • Young, N.L.1    Plazas-Mayorca, M.D.2    Garcia, B.A.3
  • 73
    • 37249082641 scopus 로고    scopus 로고
    • Protein kinase A and casein kinases mediate sequential phosphorylation events in the circadian negative feedback loop
    • Huang, G.; Chen, S.; Li, S.; Cha, J.; Long, C.; Li, L.; He, Q.; Liu, Y. Protein kinase A and casein kinases mediate sequential phosphorylation events in the circadian negative feedback loop Genes Dev. 2007, 21 (24) 3283-95
    • (2007) Genes Dev. , vol.21 , Issue.24 , pp. 3283-3295
    • Huang, G.1    Chen, S.2    Li, S.3    Cha, J.4    Long, C.5    Li, L.6    He, Q.7    Liu, Y.8
  • 75
    • 80052967467 scopus 로고    scopus 로고
    • CREB-mediated alterations in the amygdala transcriptome: Coordinated regulation of immune response genes following cocaine
    • Ecke, L. E.; Cleck, J. N.; White, P.; Schug, J.; Mifflin, L.; Blendy, J. A. CREB-mediated alterations in the amygdala transcriptome: coordinated regulation of immune response genes following cocaine Int. J. Neuropsychopharmacol. 2011, 14 (8) 1111-26
    • (2011) Int. J. Neuropsychopharmacol. , vol.14 , Issue.8 , pp. 1111-1126
    • Ecke, L.E.1    Cleck, J.N.2    White, P.3    Schug, J.4    Mifflin, L.5    Blendy, J.A.6
  • 76
    • 79955498437 scopus 로고    scopus 로고
    • A human-mouse conserved sex bias in amygdala gene expression related to circadian clock and energy metabolism
    • Lin, L. C.; Lewis, D. A.; Sibille, E. A human-mouse conserved sex bias in amygdala gene expression related to circadian clock and energy metabolism Mol. Brain 2011, 4, 18
    • (2011) Mol. Brain , vol.4 , pp. 18
    • Lin, L.C.1    Lewis, D.A.2    Sibille, E.3
  • 77
    • 0034845275 scopus 로고    scopus 로고
    • Identification of genes expressed in the amygdala during the formation of fear memory
    • Stork, O.; Stork, S.; Pape, H. C.; Obata, K. Identification of genes expressed in the amygdala during the formation of fear memory Learn. Mem. 2001, 8 (4) 209-19
    • (2001) Learn. Mem. , vol.8 , Issue.4 , pp. 209-219
    • Stork, O.1    Stork, S.2    Pape, H.C.3    Obata, K.4
  • 78
    • 64949179797 scopus 로고    scopus 로고
    • Corticolimbic transcriptome changes are state-dependent and region-specific in a rodent model of depression and of antidepressant reversal
    • Surget, A.; Wang, Y.; Leman, S.; Ibarguen-Vargas, Y.; Edgar, N.; Griebel, G.; Belzung, C.; Sibille, E. Corticolimbic transcriptome changes are state-dependent and region-specific in a rodent model of depression and of antidepressant reversal Neuropsychopharmacology 2009, 34 (6) 1363-80
    • (2009) Neuropsychopharmacology , vol.34 , Issue.6 , pp. 1363-1380
    • Surget, A.1    Wang, Y.2    Leman, S.3    Ibarguen-Vargas, Y.4    Edgar, N.5    Griebel, G.6    Belzung, C.7    Sibille, E.8
  • 79
    • 79954427252 scopus 로고    scopus 로고
    • Changes in brain protein expression are linked to magnesium restriction-induced depression-like behavior
    • Whittle, N.; Li, L.; Chen, W. Q.; Yang, J. W.; Sartori, S. B.; Lubec, G.; Singewald, N. Changes in brain protein expression are linked to magnesium restriction-induced depression-like behavior Amino Acids 2011, 40 (4) 1231-48
    • (2011) Amino Acids , vol.40 , Issue.4 , pp. 1231-1248
    • Whittle, N.1    Li, L.2    Chen, W.Q.3    Yang, J.W.4    Sartori, S.B.5    Lubec, G.6    Singewald, N.7
  • 80
    • 51749119227 scopus 로고    scopus 로고
    • Variation in mouse basolateral amygdala volume is associated with differences in stress reactivity and fear learning
    • Yang, R. J.; Mozhui, K.; Karlsson, R. M.; Cameron, H. A.; Williams, R. W.; Holmes, A. Variation in mouse basolateral amygdala volume is associated with differences in stress reactivity and fear learning Neuropsychopharmacology 2008, 33 (11) 2595-604
    • (2008) Neuropsychopharmacology , vol.33 , Issue.11 , pp. 2595-2604
    • Yang, R.J.1    Mozhui, K.2    Karlsson, R.M.3    Cameron, H.A.4    Williams, R.W.5    Holmes, A.6
  • 81
    • 55949129082 scopus 로고    scopus 로고
    • Successive and selective release of phosphorylated peptides captured by hydroxy acid-modified metal oxide chromatography
    • Kyono, Y.; Sugiyama, N.; Imami, K.; Tomita, M.; Ishihama, Y. Successive and selective release of phosphorylated peptides captured by hydroxy acid-modified metal oxide chromatography J. Proteome Res. 2008, 7 (10) 4585-93
    • (2008) J. Proteome Res. , vol.7 , Issue.10 , pp. 4585-4593
    • Kyono, Y.1    Sugiyama, N.2    Imami, K.3    Tomita, M.4    Ishihama, Y.5
  • 82
    • 42649139982 scopus 로고    scopus 로고
    • SIMAC (sequential elution from IMAC), a phosphoproteomics strategy for the rapid separation of monophosphorylated from multiply phosphorylated peptides
    • Thingholm, T. E.; Jensen, O. N.; Robinson, P. J.; Larsen, M. R. SIMAC (sequential elution from IMAC), a phosphoproteomics strategy for the rapid separation of monophosphorylated from multiply phosphorylated peptides Mol. Cell. Proteomics 2008, 7 (4) 661-71
    • (2008) Mol. Cell. Proteomics , vol.7 , Issue.4 , pp. 661-671
    • Thingholm, T.E.1    Jensen, O.N.2    Robinson, P.J.3    Larsen, M.R.4
  • 83
    • 54949129419 scopus 로고    scopus 로고
    • ProteoWizard: Open source software for rapid proteomics tools development
    • Kessner, D.; Chambers, M.; Burke, R.; Agus, D.; Mallick, P. ProteoWizard: open source software for rapid proteomics tools development Bioinformatics 2008, 24 (21) 2534-6
    • (2008) Bioinformatics , vol.24 , Issue.21 , pp. 2534-2536
    • Kessner, D.1    Chambers, M.2    Burke, R.3    Agus, D.4    Mallick, P.5
  • 85
    • 0004098488 scopus 로고    scopus 로고
    • 5 th ed. W.H. Freeman: New York, pp xix, 899, 42, 34, 126
    • Harris, D. C. Quantitative Chemical Analysis, 5 th ed.; W.H. Freeman: New York, 1999; pp xix, 899, 42, 34, 126.
    • (1999) Quantitative Chemical Analysis
    • Harris, D.C.1
  • 86
    • 27944499451 scopus 로고    scopus 로고
    • An iterative statistical approach to the identification of protein phosphorylation motifs from large-scale data sets
    • Schwartz, D.; Gygi, S. P. An iterative statistical approach to the identification of protein phosphorylation motifs from large-scale data sets Nat. Biotechnol. 2005, 23 (11) 1391-8
    • (2005) Nat. Biotechnol. , vol.23 , Issue.11 , pp. 1391-1398
    • Schwartz, D.1    Gygi, S.P.2
  • 87
    • 77954565509 scopus 로고    scopus 로고
    • Brain phosphoproteome obtained by a FASP-based method reveals plasma membrane protein topology
    • Wisniewski, J. R.; Nagaraj, N.; Zougman, A.; Gnad, F.; Man, M. Brain phosphoproteome obtained by a FASP-based method reveals plasma membrane protein topology J. Proteome Res. 2010, 9 (6) 3280-9
    • (2010) J. Proteome Res. , vol.9 , Issue.6 , pp. 3280-3289
    • Wisniewski, J.R.1    Nagaraj, N.2    Zougman, A.3    Gnad, F.4    Man, M.5


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.