메뉴 건너뛰기




Volumn 4, Issue 5, 2011, Pages 575-

Phosphoproteomic profiling of the myocyte

Author keywords

Mass spectrometry; Myocardium; Pathway analysis; Phosphoproteins; Phosphoproteomics

Indexed keywords

PHOSPHOPROTEIN; PHOSPHOPROTEOME; UNCLASSIFIED DRUG;

EID: 82955189746     PISSN: 1942325X     EISSN: 19423268     Source Type: Journal    
DOI: 10.1161/CIRCGENETICS.110.957787     Document Type: Article
Times cited : (11)

References (50)
  • 2
    • 1042268061 scopus 로고    scopus 로고
    • Lessons from Old and New Kinases
    • DOI 10.1161/01.RES.0000117526.17737.40
    • Van Eyk JE. Lessons from old and new kinases. Circ Res. 2004;94: 135-137. (Pubitemid 38197443)
    • (2004) Circulation Research , vol.94 , Issue.2 , pp. 135-137
    • Van Eyk, J.E.1
  • 3
    • 64149113543 scopus 로고    scopus 로고
    • Ablation of ventricular myosin regulatory light chain phosphorylation in mice causes cardiac dysfunction in situ and affects neighboring myofilament protein phosphorylation
    • Scruggs SB, Hinken AC, Thawornkaiwong A, Robbins J, Walker LA, de Tombe PP, Geenen DL, Buttrick PM, Solaro RJ. Ablation of ventricular myosin regulatory light chain phosphorylation in mice causes cardiac dysfunction in situ and affects neighboring myofilament protein phosphorylation. J Biol Chem. 2009;284:5097-5106.
    • (2009) J Biol Chem. , vol.284 , pp. 5097-5106
    • Scruggs, S.B.1    Hinken, A.C.2    Thawornkaiwong, A.3    Robbins, J.4    Walker, L.A.5    De Tombe, P.P.6    Geenen, D.L.7    Buttrick, P.M.8    Solaro, R.J.9
  • 5
    • 70349973075 scopus 로고    scopus 로고
    • Quantitative mitochondrial phosphoproteomics ITRAQ using on an LTQ-Orbitrap with high energy collision dissociation
    • Boja ES, Phillips D, French SA, Harris RA, Balaban RS. Quantitative mitochondrial phosphoproteomics using iTRAQ on an LTQ-Orbitrap with high energy collision dissociation. J Proteome Res. 2009;8: 4665-4675.
    • (2009) J Proteome Res. , vol.8 , pp. 4665-4675
    • Boja, E.S.1    Phillips, D.2    French, S.A.3    Harris, R.A.4    Balaban, R.S.5
  • 6
    • 0034829027 scopus 로고    scopus 로고
    • Effects of chronic alcohol consumption on regulation of myocardial protein synthesis
    • Vary TC, Lynch CJ, Lang CH. Effects of chronic alcohol consumption on regulation of myocardial protein synthesis. Am J Physiol Heart Circ Physiol. 2001;281:H1242-H1251.
    • (2001) Am J Physiol Heart Circ Physiol. , vol.281
    • Vary, T.C.1    Lynch, C.J.2    Lang, C.H.3
  • 9
    • 72449196261 scopus 로고    scopus 로고
    • Global effects of kinase inhibitors on signaling networks revealed by quantitative phosphoproteomics
    • Pan C, Olsen JV, Daub H, Mann M. Global effects of kinase inhibitors on signaling networks revealed by quantitative phosphoproteomics. Mol Cell Proteomics. 2009;8:2796-2808.
    • (2009) Mol Cell Proteomics. , vol.8 , pp. 2796-2808
    • Pan, C.1    Olsen, J.V.2    Daub, H.3    Mann, M.4
  • 12
    • 33750456519 scopus 로고    scopus 로고
    • Global, In Vivo, and Site-Specific Phosphorylation Dynamics in Signaling Networks
    • DOI 10.1016/j.cell.2006.09.026, PII S0092867406012748
    • Olsen JV, 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. (Pubitemid 44647421)
    • (2006) Cell , vol.127 , Issue.3 , 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
  • 13
    • 24944519450 scopus 로고    scopus 로고
    • Highly selective enrichment of phosphorylated peptides from peptide mixtures using titanium dioxide microcolumns
    • DOI 10.1074/mcp.T500007-MCP200
    • Larsen MR, Thingholm TE, Jensen ON, Roepstorff P, Jorgensen TJD. Highly selective enrichment of phosphorylated peptides from peptide mixtures using titanium dioxide microcolumns. Mol Cell Proteomics. 2005;4:873-886. (Pubitemid 41309146)
    • (2005) Molecular and Cellular 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.D.5
  • 14
    • 84984933087 scopus 로고    scopus 로고
    • The SCX/IMAC enrichment approach for global phosphorylation analysis by mass spectrometry
    • Villen J, Gygi SP. The SCX/IMAC enrichment approach for global phosphorylation analysis by mass spectrometry. Nat Protoc. 2008;3: 1630-1638.
    • (2008) Nat Protoc. , vol.3 , pp. 1630-1638
    • Villen, J.1    Gygi, S.P.2
  • 15
    • 29544444603 scopus 로고    scopus 로고
    • Efficient enrichment of intact phosphorylated proteins by modified immobilized metal-affinity chromatography
    • DOI 10.1002/pmic.200500002
    • Dubrovska A, Souchelnytskyi S. Efficient enrichment of intact phosphorylated proteins by modified immobilized metal-affinity chromatography. Proteomics. 2005;5:4678-4683. (Pubitemid 43016889)
    • (2005) Proteomics , vol.5 , Issue.18 , pp. 4678-4683
    • Dubrovska, A.1    Souchelnytskyi, S.2
  • 16
    • 63449087384 scopus 로고    scopus 로고
    • Optimization of immobilized gallium (III) ion affinity chromatography for selective binding and recovery of phosphopeptides from protein digests
    • Aryal UK, Olson DJ, Ross AR. Optimization of immobilized gallium (III) ion affinity chromatography for selective binding and recovery of phosphopeptides from protein digests. J Biomol Tech. 2008;19:296-310.
    • (2008) J Biomol Tech. , vol.19 , pp. 296-310
    • Aryal, U.K.1    Olson, D.J.2    Ross, A.R.3
  • 17
    • 42649139982 scopus 로고    scopus 로고
    • SIMAC (Sequential Elution from IMAC), a phosphoproteomics strategy for the rapid separation of monophosphorylated from multiply phosphorylated peptides
    • DOI 10.1074/mcp.M700362-MCP200
    • Thingholm TE, Jensen ON, Robinson PJ, Larsen MR. SIMAC (sequential elution from IMAC), a phosphoproteomics strategy for the rapid separation of monophosphorylated from multiply phosphorylated peptides. Mol Cell Proteomics. 2008;7:661-671. (Pubitemid 351597478)
    • (2008) Molecular and Cellular 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
    • 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;7:5167-5176.
    • (2008) J Proteome Res. , vol.7 , pp. 5167-5176
    • Carrascal, M.1    Ovelleiro, D.2    Casas, V.3    Gay, M.4    Abian, J.5
  • 19
    • 33645217942 scopus 로고    scopus 로고
    • Selective zirconium dioxide-based enrichment of phosphorylated peptides for mass spectrometric analysis
    • Kweon HK, Håkansson K. Selective zirconium dioxide-based enrichment of phosphorylated peptides for mass spectrometric analysis. Anal Chem. 2006;78:1743-1749.
    • (2006) Anal Chem. , vol.78 , pp. 1743-1749
    • Kweon, H.K.1    Håkansson, K.2
  • 20
  • 21
    • 70349321247 scopus 로고    scopus 로고
    • Receptor tyrosine kinase signaling: A view from quantitative proteomics
    • Dengjel J, Kratchmarova I, Blagoev B. Receptor tyrosine kinase signaling: a view from quantitative proteomics. Mol Biosyst. 2009;5: 1112-1121.
    • (2009) Mol Biosyst. , vol.5 , pp. 1112-1121
    • Dengjel, J.1    Kratchmarova, I.2    Blagoev, B.3
  • 24
    • 44149105911 scopus 로고    scopus 로고
    • PHOSIDA (phosphorylation site database): Management, structural and evolutionary investigation, and prediction of phosphosites
    • Gnad F, Ren S, Cox J, Olsen JV, Macek B, Oroshi M, Mann M. PHOSIDA (phosphorylation site database): management, structural and evolutionary investigation, and prediction of phosphosites. Genome Biol. 2007;8:R250.
    • (2007) Genome Biol. , vol.8
    • Gnad, F.1    Ren, S.2    Cox, J.3    Olsen, J.V.4    Macek, B.5    Oroshi, M.6    Mann, M.7
  • 25
    • 65349106511 scopus 로고    scopus 로고
    • Hydrophilic interaction chromatography for fractionation and enrichment of the phosphoproteome
    • McNulty DE, Annan RS. Hydrophilic interaction chromatography for fractionation and enrichment of the phosphoproteome. Methods Mol Biol. 2009;527:93-105.
    • (2009) Methods Mol Biol. , vol.527 , pp. 93-105
    • McNulty, D.E.1    Annan, R.S.2
  • 26
    • 42449147408 scopus 로고    scopus 로고
    • Hydrophilic interaction liquid chromatography (HILIC) in proteomics
    • Boersema PJ, Mohammed S, Heck AJ. Hydrophilic interaction liquid chromatography (HILIC) in proteomics. Anal Bioanal Chem. 2008;391: 151-159.
    • (2008) Anal Bioanal Chem. , vol.391 , pp. 151-159
    • Boersema, P.J.1    Mohammed, S.2    Heck, A.J.3
  • 27
    • 67651173106 scopus 로고    scopus 로고
    • Proteomics by mass spectrometry: Approaches, advances, and applications
    • Yates JR, Ruse CI, Nakorchevsky A. Proteomics by mass spectrometry: approaches, advances, and applications. Annu Rev Biomed Eng. 2009;11: 49-79.
    • (2009) Annu Rev Biomed Eng. , vol.11 , pp. 49-79
    • Yates, J.R.1    Ruse, C.I.2    Nakorchevsky, A.3
  • 28
    • 67649213067 scopus 로고    scopus 로고
    • Phosphopeptide fragmentation and analysis by mass spectrometry
    • Boersema PJ, Mohammed S, Heck AJ. Phosphopeptide fragmentation and analysis by mass spectrometry. J Mass Spectrom. 2009;44:861-878.
    • (2009) J Mass Spectrom. , vol.44 , pp. 861-878
    • Boersema, P.J.1    Mohammed, S.2    Heck, A.J.3
  • 29
    • 36749068401 scopus 로고    scopus 로고
    • Performance characteristics of electron transfer dissociation mass spectrometry
    • DOI 10.1074/mcp.M700073-MCP200
    • Good DM, Wirtala M, McAlister GC, Coon JJ. Performance characteristics of electron transfer dissociation mass spectrometry. Mol Cell Proteomics. 2007;6:1942-1951. (Pubitemid 350213868)
    • (2007) Molecular and Cellular Proteomics , vol.6 , Issue.11 , pp. 1942-1951
    • Good, D.M.1    Wirtala, M.2    McAlister, G.C.3    Coon, J.J.4
  • 30
    • 33846269339 scopus 로고    scopus 로고
    • Supplemental activation method for high-efficiency electron-transfer dissociation of doubly protonated peptide precursors
    • DOI 10.1021/ac061457f
    • Swaney DL, McAlister GC, Wirtala M, Schwartz JC, Syka JE, Coon JJ. Supplemental activation method for high-efficiency electron-transfer dissociation of doubly protonated peptide precursors. Anal Chem. 2007;79: 477-485. (Pubitemid 46110632)
    • (2007) Analytical Chemistry , vol.79 , Issue.2 , pp. 477-485
    • Swaney, D.L.1    McAlister, G.C.2    Wirtala, M.3    Schwartz, J.C.4    Syka, J.E.P.5    Coon, J.J.6
  • 31
    • 59149090911 scopus 로고    scopus 로고
    • Strong cation exchange-based fractionation of Lys-N-generated peptides facilitates the targeted analysis of post-translational modifications
    • Taouatas N, Altelaar AF, Drugan MM, Helbig AO, Mohammed S, Heck AJ. Strong cation exchange-based fractionation of Lys-N-generated peptides facilitates the targeted analysis of post-translational modifications. Mol Cell Proteomics. 2009;8:190-200.
    • (2009) Mol Cell Proteomics. , vol.8 , pp. 190-200
    • Taouatas, N.1    Altelaar, A.F.2    Drugan, M.M.3    Helbig, A.O.4    Mohammed, S.5    Heck, A.J.6
  • 32
    • 0033434080 scopus 로고    scopus 로고
    • Probability-based protein identification by searching sequence databases using mass spectrometry data
    • Perkins DN, Pappin DJ, Creasy DM, Cottrell JS. Probability-based protein identification by searching sequence databases using mass spectrometry data. Electrophoresis. 1999;20:3551-3567. (Pubitemid 30007252)
    • (1999) Electrophoresis , vol.20 , Issue.18 , pp. 3551-3567
    • Perkins, D.N.1    Pappin, D.J.C.2    Creasy, D.M.3    Cottrell, J.S.4
  • 33
    • 0036828724 scopus 로고    scopus 로고
    • Probability based validation of protein identifications using a modified SEQUEST algorithm
    • DOI 10.1021/ac025826t
    • MacCoss MJ, Wu CC, Yates JR III. Probability-based validation of protein identifications using a modified SEQUEST algorithm. Anal Chem. 2002;74:5593-5599. (Pubitemid 35253125)
    • (2002) Analytical Chemistry , vol.74 , Issue.21 , pp. 5593-5599
    • MacCoss, M.J.1    Wu, C.C.2    Yates III, J.R.3
  • 34
    • 77951809436 scopus 로고    scopus 로고
    • Data processing algorithms for analysis of high resolution MSMS spectra of peptides with complex patterns of posttranslational modifications
    • Guan S, Burlingame AL. Data processing algorithms for analysis of high resolution MSMS spectra of peptides with complex patterns of posttranslational modifications. Mol Cell Proteomics. 2009;9:804-810.
    • (2009) Mol Cell Proteomics. , vol.9 , pp. 804-810
    • Guan, S.1    Burlingame, A.L.2
  • 35
    • 33847630405 scopus 로고    scopus 로고
    • Target-decoy search strategy for increased confidence in large-scale protein identifications by mass spectrometry
    • DOI 10.1038/nmeth1019, PII NMETH1019
    • Elias JE, Gygi SP. Target-decoy search strategy for increased confidence in large-scale protein identifications by mass spectrometry. Nat Methods. 2007;4:207-214. (Pubitemid 46358868)
    • (2007) Nature Methods , vol.4 , Issue.3 , pp. 207-214
    • Elias, J.E.1    Gygi, S.P.2
  • 36
    • 33749853607 scopus 로고    scopus 로고
    • A probability-based approach for high-throughput protein phosphorylation analysis and site localization
    • DOI 10.1038/nbt1240, PII NBT1240
    • Beausoleil SA, Villén J, Gerber SA, Rush J, Gygi SP. A probability-based approach for high-throughput protein phosphorylation analysis and site localization. Nat Biotechnol. 2006;24:1285-1292. (Pubitemid 44564776)
    • (2006) Nature Biotechnology , 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
  • 37
    • 57449099865 scopus 로고    scopus 로고
    • MaxQuant enables high peptide identification rates, individualized p.p.b.-range mass accuracies and proteome-wide protein quantification
    • Cox J, Mann M. MaxQuant enables high peptide identification rates, individualized p.p.b.-range mass accuracies and proteome-wide protein quantification. Nat Biotechnol. 2008;26:1367-1372.
    • (2008) Nat Biotechnol. , vol.26 , pp. 1367-1372
    • Cox, J.1    Mann, M.2
  • 38
    • 3042818018 scopus 로고    scopus 로고
    • The international protein index: An integrated database for proteomics experiments
    • DOI 10.1002/pmic.200300721
    • Kersey PJ, Duarte J, Williams A, Karavidopoulou Y, Birney E, Apweiler R. The International Protein Index: an integrated database for proteomics experiments. Proteomics. 2004;4:1985-1988. (Pubitemid 38880363)
    • (2004) Proteomics , vol.4 , Issue.7 , pp. 1985-1988
    • Kersey, P.J.1    Duarte, J.2    Williams, A.3    Karavidopoulou, Y.4    Birney, E.5    Apweiler, R.6
  • 39
    • 64749108158 scopus 로고    scopus 로고
    • Multiplex peptide stable isotope dimethyl labeling for quantitative proteomics
    • Boersema PJ, Raijmakers R, Lemeer S, Mohammed S, Heck AJ. Multiplex peptide stable isotope dimethyl labeling for quantitative proteomics. Nat Protoc. 2009;4:484-494.
    • (2009) Nat Protoc. , vol.4 , pp. 484-494
    • Boersema, P.J.1    Raijmakers, R.2    Lemeer, S.3    Mohammed, S.4    Heck, A.J.5
  • 41
    • 44449162195 scopus 로고    scopus 로고
    • Absolute SILAC for accurate quantitation of proteins in complex mixtures down to the attomole level
    • Hanke S, Besir H, Oesterhelt D, Mann M. Absolute SILAC for accurate quantitation of proteins in complex mixtures down to the attomole level. J Proteome Res. 2008;7:1118-1130.
    • (2008) J Proteome Res. , vol.7 , pp. 1118-1130
    • Hanke, S.1    Besir, H.2    Oesterhelt, D.3    Mann, M.4
  • 42
    • 70449412362 scopus 로고    scopus 로고
    • ITRAQ underestimation in simple and complex mixtures "the good, the bad and the ugly
    • Ow SY, Salim M, Noirel J, Evans C, Rehman I, Wright PC. ITRAQ underestimation in simple and complex mixtures: "the good, the bad and the ugly." J Proteome Res. 2009;8:5347-5355.
    • (2009) J Proteome Res. , vol.8 , pp. 5347-5355
    • Ow, S.Y.1    Salim, M.2    Noirel, J.3    Evans, C.4    Rehman, I.5    Wright, P.C.6
  • 43
    • 77953595441 scopus 로고    scopus 로고
    • Undesirable charge-enhancement of isobaric tagged phosphopeptides leads to reduced identification efficiency
    • Thingholm TE, Palmisano G, Kjeldsen F, Larsen MR. Undesirable charge-enhancement of isobaric tagged phosphopeptides leads to reduced identification efficiency. J Proteome Res. 2010;9:4045-4052.
    • (2010) J Proteome Res. , vol.9 , pp. 4045-4052
    • Thingholm, T.E.1    Palmisano, G.2    Kjeldsen, F.3    Larsen, M.R.4
  • 45
    • 2942564430 scopus 로고    scopus 로고
    • Prediction of post-translational glycosylation and phosphorylation of proteins from the amino acid sequence
    • DOI 10.1002/pmic.200300771
    • Blom N, Sicheritz-Ponten T, Gupta R, Gammeltoft S, Brunak S. Prediction of post-translational glycosylation and phosphorylation of proteins from the amino acid sequence. Proteomics. 2004;4: 1633-1649. (Pubitemid 38738322)
    • (2004) Proteomics , vol.4 , Issue.6 , pp. 1633-1649
    • Blom, N.1    Sicheritz-Ponten, T.2    Gupta, R.3    Gammeltoft, S.4    Brunak, So.5
  • 46
    • 27944499451 scopus 로고    scopus 로고
    • An iterative statistical approach to the identification of protein phosphorylation motifs from large-scale data sets
    • DOI 10.1038/nbt1146, PII N1146
    • Schwartz D, Gygi SP. An iterative statistical approach to the identification of protein phosphorylation motifs from large-scale data sets. Nat Biotechnol. 2005;23:1391-1398. (Pubitemid 41679391)
    • (2005) Nature Biotechnology , vol.23 , Issue.11 , pp. 1391-1398
    • Schwartz, D.1    Gygi, S.P.2
  • 48
    • 33744523162 scopus 로고    scopus 로고
    • Ischemia-specific phosphorylation and myofilament translocation of heat shock protein 27 precedes alpha B-crystallin and occurs independently of reactive oxygen species in rabbit myocardium
    • DOI 10.1016/j.yjmcc.2006.02.007, PII S0022282806000654
    • White MY, Hambly BD, Jeremy RW, Cordwell SJ. Ischemia-specific phosphorylation and myofilament translocation of heat shock protein 27 precedes alpha B-crystallin and occurs independently of reactive oxygen species in rabbit myocardium. J Mol Cell Cardiol. 2006;40:761-774. (Pubitemid 43817036)
    • (2006) Journal of Molecular and Cellular Cardiology , vol.40 , Issue.6 , pp. 761-774
    • White, M.Y.1    Hambly, B.D.2    Jeremy, R.W.3    Cordwell, S.J.4
  • 50
    • 2942598149 scopus 로고    scopus 로고
    • PhosphoSite: A bioinformatics resource dedicated to physiological protein phosphorylation
    • DOI 10.1002/pmic.200300772
    • Hornbeck PV, Chabra I, Kornhauser JM, Skrzypek E, Zhang B. PhosphoSite: a bioinformatics resource dedicated to physiological protein phosphorylation. Proteomics. 2004;4:1551-1561. (Pubitemid 38738314)
    • (2004) Proteomics , vol.4 , Issue.6 , pp. 1551-1561
    • Hornbeck, P.V.1    Chabra, I.2    Kornhauser, J.M.3    Skrzypek, E.4    Zhang, B.5


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.