메뉴 건너뛰기




Volumn 9, Issue 2, 2010, Pages 777-788

Phosphoproteome analysis of rat L6 myotubes using reversed-phase C18 prefractionation and titanium dioxide enrichment

Author keywords

2D LC MS MS; Phosphoproteome; Rat L6 myotubes; RP c18 Prefractionation; Signaling pathway; TiO2

Indexed keywords

B RAF KINASE; BETA ACTIN; INSULIN; MAMMALIAN TARGET OF RAPAMYCIN; MICROTUBULE ASSOCIATED PROTEIN 2; MITOGEN ACTIVATED PROTEIN KINASE; MITOGEN ACTIVATED PROTEIN KINASE 14; PAXILLIN; PHOSPHOINOSITIDE DEPENDENT PROTEIN KINASE 1; PHOSPHOPEPTIDE; PHOSPHOPROTEIN; PROTEIN KINASE B; PROTEIN KINASE B BETA; PROTEOME; RAS PROTEIN; SERINE; SERINE DERIVATIVE; SOMATOMEDIN C; SOS PROTEIN; THREONINE; TITANIUM DIOXIDE;

EID: 76149092855     PISSN: 15353893     EISSN: None     Source Type: Journal    
DOI: 10.1021/pr900646k     Document Type: Article
Times cited : (32)

References (73)
  • 1
    • 0034383949 scopus 로고    scopus 로고
    • The regulation of protein function by multisite phosphorylation - a 25 year update
    • Cohen, P. The regulation of protein function by multisite phosphorylation - a 25 year update. Trends Biochem. Sci. 2000, 25 (12), 596-601.
    • (2000) Trends Biochem. Sci , vol.25 , Issue.12 , pp. 596-601
    • Cohen, P.1
  • 2
    • 0034614490 scopus 로고    scopus 로고
    • Signaling-2000 and beyond
    • Hunter, T. Signaling-2000 and beyond. Cell 2000, 100, 113-127.
    • (2000) Cell , vol.100 , pp. 113-127
    • Hunter, T.1
  • 3
    • 0034651752 scopus 로고    scopus 로고
    • Protein phosphorylation and protein phosphatases
    • Zolnierowicz, S.; Bollen, M. Protein phosphorylation and protein phosphatases. EMBO J. 2000, 19 (4), 483-488.
    • (2000) EMBO J , vol.19 , Issue.4 , pp. 483-488
    • Zolnierowicz, S.1    Bollen, M.2
  • 5
    • 62349122241 scopus 로고    scopus 로고
    • High accuracy mass spectrometry in largescale analysis of protein phosphorylation
    • Olsen, J. V.; Macek, B. High accuracy mass spectrometry in largescale analysis of protein phosphorylation. Methods Mol. Biol. 2009, 492, 131-142.
    • (2009) Methods Mol. Biol , vol.492 , pp. 131-142
    • Olsen, J.V.1    Macek, B.2
  • 6
    • 59049086847 scopus 로고    scopus 로고
    • Human embryonic stem cell phosphoproteome revealed by electron transfer dissociation tandem mass spectrometry
    • Swaney, D. L.; Wenger, C. D.; Thomson, J. A.; Coon, J. J. Human embryonic stem cell phosphoproteome revealed by electron transfer dissociation tandem mass spectrometry. Proc. Natl. Acad. Sci. U.S.A. 2009, 106 (4), 995-1000.
    • (2009) Proc. Natl. Acad. Sci. U.S.A , vol.106 , Issue.4 , pp. 995-1000
    • Swaney, D.L.1    Wenger, C.D.2    Thomson, J.A.3    Coon, J.J.4
  • 7
    • 33847778786 scopus 로고    scopus 로고
    • Chi, A.; Huttenhower, C.; Geer, L. Y.; Coon, J. J.; Syka, J. E.; Bai, D. L.; Shabanowitz, J.; Burke, D. J.; Troyanskaya, O. G.; Hunt, D. F. Analysis of phosphorylation sites on proteins from Saccharomyces cerevisiae by electron transfer dissociation (ETD) mass spectrometry. Proc. Natl. Acad. Sci. U.S.A. 2007, 104 (7)), 2193-2198.
    • Chi, A.; Huttenhower, C.; Geer, L. Y.; Coon, J. J.; Syka, J. E.; Bai, D. L.; Shabanowitz, J.; Burke, D. J.; Troyanskaya, O. G.; Hunt, D. F. Analysis of phosphorylation sites on proteins from Saccharomyces cerevisiae by electron transfer dissociation (ETD) mass spectrometry. Proc. Natl. Acad. Sci. U.S.A. 2007, 104 (7)), 2193-2198.
  • 8
    • 0034624002 scopus 로고    scopus 로고
    • Identification of a novel immunoreceptor tyrosine-based activation motif-containing molecule, STAM2, by mass spectrometry and its involvement in growth factor and cytokine receptor signaling pathways
    • Pandey, A.; Fernandez, M. M.; Steen, H.; Blagoev, B.; Nielsen, M. M.; Roche, S.; Mann, M.; Lodish, H. F. Identification of a novel immunoreceptor tyrosine-based activation motif-containing molecule, STAM2, by mass spectrometry and its involvement in growth factor and cytokine receptor signaling pathways. J. Biol. Chem. 2000, 275, 38633-38639.
    • (2000) J. Biol. Chem , vol.275 , pp. 38633-38639
    • Pandey, A.1    Fernandez, M.M.2    Steen, H.3    Blagoev, B.4    Nielsen, M.M.5    Roche, S.6    Mann, M.7    Lodish, H.F.8
  • 9
    • 36749061271 scopus 로고    scopus 로고
    • Quantitative phosphoproteome profiling of Wnt3a-mediated signaling network: Indicating the involvement of ribonucleoside-diphosphate reductase M2 subunit phosphorylation at residue serine 20 in canonical Wnt signal transduction
    • Tang, L. Y.; Deng, N.; Wang, L. S.; Dai, J.; Wang, Z. L.; Jiang, X. S.; Li, S. J.; Li, L.; Sheng, Q. H.; Wu, D. Q.; Li, L.; Zeng, R. Quantitative phosphoproteome profiling of Wnt3a-mediated signaling network: indicating the involvement of ribonucleoside-diphosphate reductase M2 subunit phosphorylation at residue serine 20 in canonical Wnt signal transduction. Mol. Cell. Proteomics 2007, 6 (11), 1952-1967.
    • (2007) Mol. Cell. Proteomics , vol.6 , Issue.11 , pp. 1952-1967
    • Tang, L.Y.1    Deng, N.2    Wang, L.S.3    Dai, J.4    Wang, Z.L.5    Jiang, X.S.6    Li, S.J.7    Li, L.8    Sheng, Q.H.9    Wu, D.Q.10    Li, L.11    Zeng, R.12
  • 11
    • 0033565503 scopus 로고    scopus 로고
    • Immobilized gallium(III) affinity chromatography of phosphopeptides
    • Posewitz, M. C.; Tempst, P. Immobilized gallium(III) affinity chromatography of phosphopeptides. Anal. Chem. 1999, 71, 2883-2892.
    • (1999) Anal. Chem , vol.71 , pp. 2883-2892
    • Posewitz, M.C.1    Tempst, P.2
  • 12
    • 11444263845 scopus 로고    scopus 로고
    • Largescale analysis of in vivo phosphorylated membrane proteins by immobilized metal ion affinity chromatography and mass spectrometry
    • Nuhse, T. S.; Stensballe, A.; Jensen, O. N.; Peck, S. C. Largescale analysis of in vivo phosphorylated membrane proteins by immobilized metal ion affinity chromatography and mass spectrometry. Mol. Cell. Proteomics 2003, 2, 1234-1243.
    • (2003) Mol. Cell. Proteomics , vol.2 , pp. 1234-1243
    • Nuhse, T.S.1    Stensballe, A.2    Jensen, O.N.3    Peck, S.C.4
  • 13
    • 3242688830 scopus 로고    scopus 로고
    • Selective isolation at the femtomole level of phosphopeptides from proteolytic digests using 2D-NanoLC-ESI-MS/MS and titanium oxide precolumns
    • Pinkse, M. W.; Uitto, P. M.; Hilhorst, M. J.; Ooms, B.; Heck, A. J. Selective isolation at the femtomole level of phosphopeptides from proteolytic digests using 2D-NanoLC-ESI-MS/MS and titanium oxide precolumns. Anal. Chem. 2004, 76 (14), 3935-3943.
    • (2004) Anal. Chem , vol.76 , Issue.14 , pp. 3935-3943
    • Pinkse, M.W.1    Uitto, P.M.2    Hilhorst, M.J.3    Ooms, B.4    Heck, A.J.5
  • 14
    • 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), 873-886.
    • (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
  • 15
    • 38049035341 scopus 로고    scopus 로고
    • Global profiling of phosphopeptides by titania affinity enrichment
    • Wu, J.; Shakey, Q.; Liu, W.; Schuller, A.; Follettie, M. T. Global profiling of phosphopeptides by titania affinity enrichment. J. Proteome Res. 2007, 6 (12), 4684-4689.
    • (2007) J. Proteome Res , vol.6 , Issue.12 , pp. 4684-4689
    • Wu, J.1    Shakey, Q.2    Liu, W.3    Schuller, A.4    Follettie, M.T.5
  • 16
    • 0035072715 scopus 로고    scopus 로고
    • A systematic approach to the analysis of protein phosphorylation
    • Zhou, H.; Watts, J. D.; Aebersold, R. A systematic approach to the analysis of protein phosphorylation. Nat. Biotechnol. 2001, 19 (4), 375-378.
    • (2001) Nat. Biotechnol , vol.19 , Issue.4 , pp. 375-378
    • Zhou, H.1    Watts, J.D.2    Aebersold, R.3
  • 17
    • 42649139982 scopus 로고    scopus 로고
    • SIMAC (sequential elution from IMAC), a phosphoproteomic strategy for the rapid separation of mono-phosphorylated from multiply phosphorylated peptides
    • Thingholm, T. E.; Jensen, O. N.; Robinson, P. J.; Larsen, M. R. SIMAC (sequential elution from IMAC), a phosphoproteomic strategy for the rapid separation of mono-phosphorylated from multiply phosphorylated peptides. Mol. Cell. Proteomics 2008, 7 (4), 661-671.
    • (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
  • 18
    • 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, 2032-2042.
    • (2007) Mol. Cell. Proteomics , vol.6 , pp. 2032-2042
    • Zhang, X.1    Ye, J.2    Jensen, O.N.3    Roepstorff, P.4
  • 20
    • 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
  • 21
    • 84984933087 scopus 로고    scopus 로고
    • The SCX/IMAC enrichment approach for global phosphorylation analysis by mass spectrometry
    • Villén, J.; Gygi, S. P. The SCX/IMAC enrichment approach for global phosphorylation analysis by mass spectrometry. Nat. Protoc. 2008, 3 (10), 1630-1638.
    • (2008) Nat. Protoc , vol.3 , Issue.10 , pp. 1630-1638
    • Villén, J.1    Gygi, S.P.2
  • 22
    • 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.; Jiang, X.; Feng, S.; Jiang, X.; Tian, R.; Wan, D.; Zou, H.; Gu, J. Large-scale phosphoproteome analysis of human liver tissue by enrichment and fractionation of phosphopeptides with strong anion exchange chromatography. Proteomics 2008, 8 (7), 1346-1361.
    • (2008) Proteomics , vol.8 , Issue.7 , pp. 1346-1361
    • Han, G.1    Ye, M.2    Zhou, H.3    Jiang, X.4    Feng, S.5    Jiang, X.6    Tian, R.7    Wan, D.8    Zou, H.9    Gu, J.10
  • 23
    • 33846610475 scopus 로고    scopus 로고
    • Protein phosphorylation and expression profiling by Yin-yang multidimensional liquid chromatography (Yin-yang MDLC) mass spectrometry
    • Dai, J.; Jin, W. H.; Sheng, Q. H.; Shieh, C. H.; Wu, J. R.; Zeng, R. Protein phosphorylation and expression profiling by Yin-yang multidimensional liquid chromatography (Yin-yang MDLC) mass spectrometry. J. Proteome Res. 2007, 6 (1), 250-262.
    • (2007) J. Proteome Res , vol.6 , Issue.1 , pp. 250-262
    • Dai, J.1    Jin, W.H.2    Sheng, Q.H.3    Shieh, C.H.4    Wu, J.R.5    Zeng, R.6
  • 24
    • 61349179532 scopus 로고    scopus 로고
    • Phosphorylation analysis of primary human T lymphocytes using sequential IMAC and titanium oxide enrichment
    • Carrascal, M.; Ovelleiro, D.; Casas, V.; Gay, M.; Abian, J. Phosphorylation analysis of primary human T lymphocytes using sequential IMAC and titanium oxide enrichment. J. Proteome Res. 2008, 7 (12), 5167-5176.
    • (2008) J. Proteome Res , vol.7 , Issue.12 , pp. 5167-5176
    • Carrascal, M.1    Ovelleiro, D.2    Casas, V.3    Gay, M.4    Abian, J.5
  • 25
    • 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), 971-980.
    • (2008) Mol. Cell. Proteomics , vol.7 , Issue.5 , pp. 971-980
    • McNulty, D.E.1    Annan, R.S.2
  • 27
    • 44449132255 scopus 로고    scopus 로고
    • Phosphoproteome analysis of fission yeast
    • Wilson-Grady, J. T.; Villén, J.; Gygi, S. P. Phosphoproteome analysis of fission yeast. J. Proteome Res. 2008, 7 (3), 1088-1097.
    • (2008) J. Proteome Res , vol.7 , Issue.3 , pp. 1088-1097
    • Wilson-Grady, J.T.1    Villén, J.2    Gygi, S.P.3
  • 28
    • 35148898785 scopus 로고    scopus 로고
    • Signaling pathways initiated by beta-hydroxy-beta-methylbutyrate to attenuate the depression of protein synthesis in skeletal muscle in response to cachectic stimuli
    • Eley, H. L.; Russell, S. T.; Baxter, J. H.; Mukerji, P.; Tisdale, M. J. Signaling pathways initiated by beta-hydroxy-beta-methylbutyrate to attenuate the depression of protein synthesis in skeletal muscle in response to cachectic stimuli. Am. J. Physiol.: Endocrinol. Metab. 2007, 293 (4), 923-931.
    • (2007) Am. J. Physiol.: Endocrinol. Metab , vol.293 , Issue.4 , pp. 923-931
    • Eley, H.L.1    Russell, S.T.2    Baxter, J.H.3    Mukerji, P.4    Tisdale, M.J.5
  • 29
    • 34250834362 scopus 로고    scopus 로고
    • A diacylglycerol kinase inhibitor, R59022, stimulates glucose transport through a MKK3/6-p38 signaling pathway in skeletal muscle cells
    • Takahashi, N.; Nagamine, M.; Tanno, S.; Motomura, W.; Kohgo, Y.; Okumura, T. A diacylglycerol kinase inhibitor, R59022, stimulates glucose transport through a MKK3/6-p38 signaling pathway in skeletal muscle cells. Biochem. Biophys. Res. Commun. 2007, 360 (1), 244-250.
    • (2007) Biochem. Biophys. Res. Commun , vol.360 , Issue.1 , pp. 244-250
    • Takahashi, N.1    Nagamine, M.2    Tanno, S.3    Motomura, W.4    Kohgo, Y.5    Okumura, T.6
  • 30
    • 63049089189 scopus 로고    scopus 로고
    • Preliminary quantitative profile of differential protein expression between rat L6 myoblasts and myotubes by stable isotope labeling with amino acids in cell culture
    • Cui, Z.; Chen, X.; Lu, B.; Park, S.K,; Xu, T.; Xie, Z.; Xue, P.; Hou, J.; Hang, H.; Yates, J. R., III; Yang, F. Preliminary quantitative profile of differential protein expression between rat L6 myoblasts and myotubes by stable isotope labeling with amino acids in cell culture. Proteomics 2009, 9, 1274-1292.
    • (2009) Proteomics , vol.9 , pp. 1274-1292
    • Cui, Z.1    Chen, X.2    Lu, B.3    Park, S.K.4    Xu, T.5    Xie, Z.6    Xue, P.7    Hou, J.8    Hang, H.9    Yates III, J.R.10    Yang, F.11
  • 31
    • 10944252091 scopus 로고    scopus 로고
    • Comparative proteomes of the proliferating C(2)C(12) myoblasts and fully differentiated myotubes reveal the complexity of the skeletal muscle differentiation program
    • Tannu, N. S.; Rao, V. K.; Chaudhary, R. M.; Giorgianni, F.; Saeed, A. E.; Gao, Y.; Raghow, R. Comparative proteomes of the proliferating C(2)C(12) myoblasts and fully differentiated myotubes reveal the complexity of the skeletal muscle differentiation program. Mol. Cell. Proteomics 2004, 3, 1065-1082.
    • (2004) Mol. Cell. Proteomics , vol.3 , pp. 1065-1082
    • Tannu, N.S.1    Rao, V.K.2    Chaudhary, R.M.3    Giorgianni, F.4    Saeed, A.E.5    Gao, Y.6    Raghow, R.7
  • 32
    • 49249124901 scopus 로고    scopus 로고
    • Phospho-proteomic approach to identify new targets of leucine deprivation in muscle cells
    • Talvas, J.; Obled, A.; Sayd, T.; Chambon, C.; Mordier, S.; Fafournoux, P. Phospho-proteomic approach to identify new targets of leucine deprivation in muscle cells. Anal. Biochem. 2008, 381, 148-150.
    • (2008) Anal. Biochem , vol.381 , pp. 148-150
    • Talvas, J.1    Obled, A.2    Sayd, T.3    Chambon, C.4    Mordier, S.5    Fafournoux, P.6
  • 35
    • 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., III. 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 III, J.R.3
  • 36
    • 38049035341 scopus 로고    scopus 로고
    • Global profiling of phosphopeptides by titania affinity enrichment
    • Wu, J.; Shakey, Q.; Liu, W.; Schuller, A.; Follettie, M. T. Global profiling of phosphopeptides by titania affinity enrichment. J. Proteome Res. 2007, 6 (12), 4684-4689.
    • (2007) J. Proteome Res , vol.6 , Issue.12 , pp. 4684-4689
    • Wu, J.1    Shakey, Q.2    Liu, W.3    Schuller, A.4    Follettie, M.T.5
  • 37
    • 84934435370 scopus 로고    scopus 로고
    • Analysis of organelles by on-line two-dimensional liquid chromatography-tandem mass spectrometry
    • Romijn, E. P.; Yates, J. R., III. Analysis of organelles by on-line two-dimensional liquid chromatography-tandem mass spectrometry. Methods Mol. Biol. 2008, 432, 1-16.
    • (2008) Methods Mol. Biol , vol.432 , pp. 1-16
    • Romijn, E.P.1    Yates III, J.R.2
  • 38
    • 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.; Yates, J. R., III. 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, 976-989.
    • (1994) J. Am. Soc. Mass Spectrom , vol.5 , pp. 976-989
    • Eng, J.K.1    McCormack, A.2    Yates III, J.R.3
  • 39
    • 33847630405 scopus 로고    scopus 로고
    • Target-decoy search strategy for increased confidence in large-scale protein identifications by mass spectrometry
    • Elias, J. E.; Gygi, S. P. Target-decoy search strategy for increased confidence in large-scale protein identifications by mass spectrometry. Nat. Methods 2007, 4 (3), 207-214.
    • (2007) Nat. Methods , vol.4 , Issue.3 , pp. 207-214
    • Elias, J.E.1    Gygi, S.P.2
  • 40
    • 34948851348 scopus 로고    scopus 로고
    • An automated platform for analysis of phosphoproteomic datasets: Application to kidney collecting duct phosphoproteins
    • Hoffert, J. D.; Wang, G.; Pisitkun, T.; Shen, R. F.; Knepper, M. A. An automated platform for analysis of phosphoproteomic datasets: application to kidney collecting duct phosphoproteins. J. Proteome Res. 2007, 7 (9), 3501-3508.
    • (2007) J. Proteome Res , vol.7 , Issue.9 , pp. 3501-3508
    • Hoffert, J.D.1    Wang, G.2    Pisitkun, T.3    Shen, R.F.4    Knepper, M.A.5
  • 41
    • 0037108887 scopus 로고    scopus 로고
    • Empirical statistical model to estimate the accuracy of peptide identifications made by MS/MS and database search
    • Keller, A.; Nesvizhskii, A. I.; Kolker, E.; Aebersold, R. Empirical statistical model to estimate the accuracy of peptide identifications made by MS/MS and database search. Anal. Chem. 2002, 74 (20), 5383-5392.
    • (2002) Anal. Chem , vol.74 , Issue.20 , pp. 5383-5392
    • Keller, A.1    Nesvizhskii, A.I.2    Kolker, E.3    Aebersold, R.4
  • 42
    • 52749096518 scopus 로고    scopus 로고
    • Xu, H.; Yang, L.; Freitas, M. A. A robust linear regression based algorithm for automated evaluation of peptide identifications from shotgun proteomics by use of reversed-phase liquid chromatography retention time. BMC Bioinf. 2008, 9, 347.
    • Xu, H.; Yang, L.; Freitas, M. A. A robust linear regression based algorithm for automated evaluation of peptide identifications from shotgun proteomics by use of reversed-phase liquid chromatography retention time. BMC Bioinf. 2008, 9, 347.
  • 44
    • 33749853607 scopus 로고    scopus 로고
    • A probability-based approach for high-throughput protein phosphorylation analysis and site localization
    • Beausoleil, S. A.; Villén, 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), 1285-1292.
    • (2006) Nat. Biotechnol , vol.24 , Issue.10 , pp. 1285-1292
    • Beausoleil, S.A.1    Villén, J.2    Gerber, S.A.3    Rush, J.4    Gygi, S.P.5
  • 45
    • 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), 1391-1398.
    • (2005) Nat. Biotechnol , vol.23 , Issue.11 , pp. 1391-1398
    • Schwartz, D.1    Gygi, S.P.2
  • 46
    • 44449132255 scopus 로고    scopus 로고
    • Phosphoproteome analysis of fission yeast
    • Wilson-Grady, J. T.; Villén, J.; Gygi, S. P. Phosphoproteome analysis of fission yeast. J. Proteome Res. 2008, 7 (13), 1088-1097.
    • (2008) J. Proteome Res , vol.7 , Issue.13 , pp. 1088-1097
    • Wilson-Grady, J.T.1    Villén, J.2    Gygi, S.P.3
  • 48
    • 38549109487 scopus 로고    scopus 로고
    • Linding, R.; Jensen, L. J.; Pasculescu, A.; Olhovsky, M.; Colwill, K.; Bork, P.; Yaffe, M. B.; Pawson, T. NetworKIN: a resource for exploring cellular phosphorylation networks. Nucleic Acids Res. 2008, (Database issue), D695-699.
    • Linding, R.; Jensen, L. J.; Pasculescu, A.; Olhovsky, M.; Colwill, K.; Bork, P.; Yaffe, M. B.; Pawson, T. NetworKIN: a resource for exploring cellular phosphorylation networks. Nucleic Acids Res. 2008, (Database issue), D695-699.
  • 50
    • 85142149057 scopus 로고    scopus 로고
    • Maere, S.; Heymans, K.; Kuiper, M. BiNGO: a Cytoscape plugin to assess overrepresentation of Gene Ontology categories in biological networks. Bioinformatics 2005, 21, 3448-3449.
    • Maere, S.; Heymans, K.; Kuiper, M. BiNGO: a Cytoscape plugin to assess overrepresentation of Gene Ontology categories in biological networks. Bioinformatics 2005, 21, 3448-3449.
  • 51
    • 0000109995 scopus 로고
    • Transforming gene product of Rous sarcoma virus phosphorylates tyrosine
    • Hunter, T.; Sefton, B. M. Transforming gene product of Rous sarcoma virus phosphorylates tyrosine. Proc. Natl. Acad. Sci. U.S.A. 1980, 77, 1311-1315.
    • (1980) Proc. Natl. Acad. Sci. U.S.A , vol.77 , pp. 1311-1315
    • Hunter, T.1    Sefton, B.M.2
  • 52
    • 5744223586 scopus 로고    scopus 로고
    • An improved model for prediction of retention times of tryptic peptides in ion pair reversed-phase HPLC
    • Krokhin, O. V.; Craig, R.; Spicer, V.; Ens, W.; Standing, K. G.; Beavis, R. C.; Wilkins, J. A. An improved model for prediction of retention times of tryptic peptides in ion pair reversed-phase HPLC. Mol. Cell. Proteomics 2004, 3 (9), 908-919.
    • (2004) Mol. Cell. Proteomics , vol.3 , Issue.9 , pp. 908-919
    • Krokhin, O.V.1    Craig, R.2    Spicer, V.3    Ens, W.4    Standing, K.G.5    Beavis, R.C.6    Wilkins, J.A.7
  • 54
    • 0026040191 scopus 로고
    • Consensus sequences as substrate specificity determinants for protein kinases and protein phosphatases
    • Kennelly, P. J.; Krebs, E. G. Consensus sequences as substrate specificity determinants for protein kinases and protein phosphatases. J. Biol. Chem. 1991, 266, 15555-15558.
    • (1991) J. Biol. Chem , vol.266 , pp. 15555-15558
    • Kennelly, P.J.1    Krebs, E.G.2
  • 56
    • 0027437376 scopus 로고
    • Pleiotropic insulin signals are engaged by multisite phosphorylation of IRS-1
    • Sun, X. J.; Crimmins, D. L.; Myers, M. G., Jr.; Miralpeix, M.; White, M. F. Pleiotropic insulin signals are engaged by multisite phosphorylation of IRS-1. Mol. Cell. Biol. 1993, 13, 7418-7428.
    • (1993) Mol. Cell. Biol , vol.13 , pp. 7418-7428
    • Sun, X.J.1    Crimmins, D.L.2    Myers Jr., M.G.3    Miralpeix, M.4    White, M.F.5
  • 57
    • 55849150923 scopus 로고    scopus 로고
    • Proteomics and phosphoproteomics for the mapping of cellular signalling networks
    • Preisinger, C.; von Kriegsheim, A; Matallanas, D.; Kolch, W. Proteomics and phosphoproteomics for the mapping of cellular signalling networks. Proteomics 2008, 8 (21), 4402-4415.
    • (2008) Proteomics , vol.8 , Issue.21 , pp. 4402-4415
    • Preisinger, C.1    von Kriegsheim, A.2    Matallanas, D.3    Kolch, W.4
  • 58
    • 0033982936 scopus 로고    scopus 로고
    • KEGG: Kyoto encyclopedia of genes and genomes
    • Kanehisa, M.; Goto, S. KEGG: kyoto encyclopedia of genes and genomes. Nucleic Acids Res. 2000, 28, 27-30.
    • (2000) Nucleic Acids Res , vol.28 , pp. 27-30
    • Kanehisa, M.1    Goto, S.2
  • 60
    • 33745183356 scopus 로고    scopus 로고
    • The p38 MAPK signaling pathway: A major regulator of skeletal muscle development
    • Keren, A.; Tamir, Y.; Bengal, E. The p38 MAPK signaling pathway: a major regulator of skeletal muscle development. Mol. Cell. Endocrinol. 2006, 252 (1-2), 224-230.
    • (2006) Mol. Cell. Endocrinol , vol.252 , Issue.1-2 , pp. 224-230
    • Keren, A.1    Tamir, Y.2    Bengal, E.3
  • 61
    • 0024364301 scopus 로고
    • Insulin-like growth factors (IGF) in muscle development. Expression of IGF-I, the IGF-I receptor, and an IGF binding protein during myoblast differentiation
    • Tollefsen, S. E.; Lajara, R.; McCusker, R. H.; Clemmons, D. R.; Rotwein, P. Insulin-like growth factors (IGF) in muscle development. Expression of IGF-I, the IGF-I receptor, and an IGF binding protein during myoblast differentiation. J. Biol. Chem. 1989, 264 (23), 13810-13807.
    • (1989) J. Biol. Chem , vol.264 , Issue.23 , pp. 13810-13807
    • Tollefsen, S.E.1    Lajara, R.2    McCusker, R.H.3    Clemmons, D.R.4    Rotwein, P.5
  • 62
    • 0013968228 scopus 로고
    • Myogenesis: Fusion, myosin synthesis, and the mitotic cycle
    • Okazaki, K.; Holtzer, H. Myogenesis: fusion, myosin synthesis, and the mitotic cycle. Proc. Natl. Acad. Sci. U.S.A. 1966, 56 (5), 1484-1490.
    • (1966) Proc. Natl. Acad. Sci. U.S.A , vol.56 , Issue.5 , pp. 1484-1490
    • Okazaki, K.1    Holtzer, H.2
  • 63
    • 4444229881 scopus 로고    scopus 로고
    • The adaptor protein Grb14 regulates the localization of 3-phosphoinositide dependent kinase-1 (PDK-1)
    • King, C. C.; Newton, A. C. The adaptor protein Grb14 regulates the localization of 3-phosphoinositide dependent kinase-1 (PDK-1). J. Biol. Chem. 2004, 279 (36), 37518-37527.
    • (2004) J. Biol. Chem , vol.279 , Issue.36 , pp. 37518-37527
    • King, C.C.1    Newton, A.C.2
  • 64
    • 0033560707 scopus 로고    scopus 로고
    • Activation of serum- and glucocorticoi- dregulated protein kinase by agonists that activate phosphatidylinositide 3-kinase is mediated by 3-phosphoinositide-dependent protein kinase-1 (PDK1) and PDK2
    • Kobayashi, T.; Cohen, P. Activation of serum- and glucocorticoi- dregulated protein kinase by agonists that activate phosphatidylinositide 3-kinase is mediated by 3-phosphoinositide-dependent protein kinase-1 (PDK1) and PDK2. Biochem. J. 1999, 339 (2), 319-328.
    • (1999) Biochem. J , vol.339 , Issue.2 , pp. 319-328
    • Kobayashi, T.1    Cohen, P.2
  • 65
    • 0033199841 scopus 로고    scopus 로고
    • Phosphorylation of Ser-241 is essential for the activity of 3-phosphoinositide-dependent protein kinase-1: Identification of five sites of phosphorylation in vivo
    • Casamayor, A.; Morrice, N. A.; Alessi, D. R. Phosphorylation of Ser-241 is essential for the activity of 3-phosphoinositide-dependent protein kinase-1: identification of five sites of phosphorylation in vivo. Biochem. J. 1999, 342 (2), 287-292.
    • (1999) Biochem. J , vol.342 , Issue.2 , pp. 287-292
    • Casamayor, A.1    Morrice, N.A.2    Alessi, D.R.3
  • 66
    • 0037053364 scopus 로고    scopus 로고
    • Substitution of the autophosphorylation site Thr516 with a negatively charged residue confers constitutive activity to mouse 3-phosphoinositide- dependent protein kinase-1 in cells
    • Wick, M. J.; Wick, K. R.; Chen, H.; He, H.; Dong, L. Q.; Quon, M. J.; Liu, F. Substitution of the autophosphorylation site Thr516 with a negatively charged residue confers constitutive activity to mouse 3-phosphoinositide- dependent protein kinase-1 in cells. J. Biol. Chem. 2002, 277 (19), 16632-16638.
    • (2002) J. Biol. Chem , vol.277 , Issue.19 , pp. 16632-16638
    • Wick, M.J.1    Wick, K.R.2    Chen, H.3    He, H.4    Dong, L.Q.5    Quon, M.J.6    Liu, F.7
  • 67
    • 4444317558 scopus 로고    scopus 로고
    • Altered insulin signaling in retinal tissue in diabetic states
    • Kondo, T.; Kahn, C. R. Altered insulin signaling in retinal tissue in diabetic states. J. Biol. Chem. 2004, 279 (36), 37997-38006.
    • (2004) J. Biol. Chem , vol.279 , Issue.36 , pp. 37997-38006
    • Kondo, T.1    Kahn, C.R.2
  • 69
    • 0038458812 scopus 로고    scopus 로고
    • Subcellular redistribution of focal adhesion kinase and its related nonkinase in hypertrophic myocardium
    • Yi, X. P.; Wang, X.; Gerdes, A. M.; Li, F. Subcellular redistribution of focal adhesion kinase and its related nonkinase in hypertrophic myocardium. Hypertension 2003, 41 (6), 1317-1323.
    • (2003) Hypertension , vol.41 , Issue.6 , pp. 1317-1323
    • Yi, X.P.1    Wang, X.2    Gerdes, A.M.3    Li, F.4
  • 70
    • 0037160066 scopus 로고    scopus 로고
    • Casein kinase 1 regulates connexin-43 gap junction assembly
    • Cooper, C. D.; Lampe, P. D. Casein kinase 1 regulates connexin-43 gap junction assembly. J. Biol. Chem. 2002, 277 (47), 44962-44968.
    • (2002) J. Biol. Chem , vol.277 , Issue.47 , pp. 44962-44968
    • Cooper, C.D.1    Lampe, P.D.2
  • 71
    • 0842302372 scopus 로고    scopus 로고
    • Phosphorylation of serine 262 in the gap junction protein connexin-43 regulates DNA synthesis in cellcell contact forming cardiomyocytes
    • Doble, B. W.; Dang, X.; Ping, P.; Fandrich, R. R.; Nickel, B. E.; Jin, Y.; Cattini, P. A.; Kardami, E. Phosphorylation of serine 262 in the gap junction protein connexin-43 regulates DNA synthesis in cellcell contact forming cardiomyocytes. J. Cell Sci. 2004, 117 (Pt 3), 507-514.
    • (2004) J. Cell Sci , vol.117 , Issue.PART 3 , pp. 507-514
    • Doble, B.W.1    Dang, X.2    Ping, P.3    Fandrich, R.R.4    Nickel, B.E.5    Jin, Y.6    Cattini, P.A.7    Kardami, E.8
  • 72
    • 33644524918 scopus 로고    scopus 로고
    • Mass spectrometry-based proteomics turns quantitative
    • Ong, S. E.; Mann, M. Mass spectrometry-based proteomics turns quantitative. Nat. Chem. Biol. 2005, 5, 252-262.
    • (2005) Nat. Chem. Biol , vol.5 , pp. 252-262
    • Ong, S.E.1    Mann, M.2


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.