메뉴 건너뛰기




Volumn 6, Issue 11, 2007, Pages 4489-4497

Applying a targeted label-free approach using LC-MS AMT tags to evaluate changes in protein phosphorylation following phosphatase inhibition

Author keywords

20 m ID monolithic column; AMT tag pipeline; Comparative phosphoproteomics; Immobilized metal ion affinity chromatography (IMAC); Label free quantitation; Mass spectrometry; Phosphoprotein phosphatase (PPP) family; Targeted MS MS

Indexed keywords

A KINASE ANCHORING PROTEIN 8; CALYCULIN A; CATENIN; CYCLIC AMP DEPENDENT PROTEIN KINASE ANCHORING PROTEIN; CYTOCHROME P450C17; PHOSPHOPROTEIN PHOSPHATASE; STATHMIN; UNCLASSIFIED DRUG;

EID: 36348975222     PISSN: 15353893     EISSN: None     Source Type: Journal    
DOI: 10.1021/pr070068e     Document Type: Article
Times cited : (21)

References (70)
  • 1
    • 27944448894 scopus 로고    scopus 로고
    • Involvement of PP2A in viral and cellular transformation
    • Arroyo, J. D.; Hahn, W. C. Involvement of PP2A in viral and cellular transformation. Oncogene 2005, 24 (52), 7746-7755.
    • (2005) Oncogene , vol.24 , Issue.52 , pp. 7746-7755
    • Arroyo, J.D.1    Hahn, W.C.2
  • 2
    • 0035787093 scopus 로고    scopus 로고
    • The role of protein phosphatase-1 in insulin action
    • Brady, M. J.; Saltiel, A. R. The role of protein phosphatase-1 in insulin action. Recent Prog. Horm. Res. 2001, 56, 157-173.
    • (2001) Recent Prog. Horm. Res , vol.56 , pp. 157-173
    • Brady, M.J.1    Saltiel, A.R.2
  • 3
    • 0032159462 scopus 로고    scopus 로고
    • Physiologic importance of protein phosphatase inhibitors
    • Oliver, C. J.; Shenolikar, S. Physiologic importance of protein phosphatase inhibitors. Front. Biosci. 1998, 3, D961-D972.
    • (1998) Front. Biosci , vol.3
    • Oliver, C.J.1    Shenolikar, S.2
  • 5
    • 23944453389 scopus 로고    scopus 로고
    • Global phosphoproteome of HT-29 human colon adenocarcinoma cells
    • Kim, J. E.; Tannenbaum, S. R.; White, F. M. Global phosphoproteome of HT-29 human colon adenocarcinoma cells. J. Proteome Res. 2005, 4 (4), 1339-1346.
    • (2005) J. Proteome Res , vol.4 , Issue.4 , pp. 1339-1346
    • Kim, J.E.1    Tannenbaum, S.R.2    White, F.M.3
  • 6
    • 30744439090 scopus 로고    scopus 로고
    • Phosphoproteomic analysis of rat liver by high capacity IMAC and LC-MS/MS
    • Moser, K.; White, F. M. Phosphoproteomic analysis of rat liver by high capacity IMAC and LC-MS/MS. J. Proteome Res. 2006, 5 (1), 98-104.
    • (2006) J. Proteome Res , vol.5 , Issue.1 , pp. 98-104
    • Moser, K.1    White, F.M.2
  • 12
    • 26844576371 scopus 로고    scopus 로고
    • Time-resolved mass spectrometry of tyrosine phosphorylation sites in the epidermal growth factor receptor signaling network reveals dynamic modules
    • Zhang, Y.; Wolf-Yadlin, A.; Ross, P. L.; Pappin, D. J.; Rush, J.; Lauffenburger, D. A.; White, F. M. Time-resolved mass spectrometry of tyrosine phosphorylation sites in the epidermal growth factor receptor signaling network reveals dynamic modules. Mol. Cell. Proteomics 2005, 4 (9), 1240-1250.
    • (2005) Mol. Cell. Proteomics , vol.4 , Issue.9 , pp. 1240-1250
    • Zhang, Y.1    Wolf-Yadlin, A.2    Ross, P.L.3    Pappin, D.J.4    Rush, J.5    Lauffenburger, D.A.6    White, F.M.7
  • 13
    • 33750456519 scopus 로고    scopus 로고
    • Global, in vivo, and site-specific phosphorylation dynamics in signaling networks
    • Olsen, J. V.; Blagoev, B.; Gnad, F.; Macek, B.; Kumar, C.; Mortensen, P.; Mann, M. Global, in vivo, and site-specific phosphorylation dynamics in signaling networks. Cell 2006, 127 (3), 635-648.
    • (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
  • 14
    • 23044510003 scopus 로고    scopus 로고
    • Preparation of 20-mu m-i.d. silica-based monolithic columns and their performance for proteomics analyses
    • Luo, Q. Z.; Shen, Y. F.; Hixson, K. K.; Zhao, R.; Yang, F.; Moore, R. J.; Mottaz, H. M.; Smith, R. D. Preparation of 20-mu m-i.d. silica-based monolithic columns and their performance for proteomics analyses. Anal. Chem. 2005, 77 (15), 5028-5035.
    • (2005) Anal. Chem , vol.77 , Issue.15 , pp. 5028-5035
    • Luo, Q.Z.1    Shen, Y.F.2    Hixson, K.K.3    Zhao, R.4    Yang, F.5    Moore, R.J.6    Mottaz, H.M.7    Smith, R.D.8
  • 15
    • 33646583172 scopus 로고    scopus 로고
    • More sensitive and quantitative proteomic measurements using very low flow rate porous silica monolithic LC columns with electrospray ionization-mass spectrometry
    • Luo, Q. Z.; Tang, K. Q.; Yang, F.; Elias, A.; Shen, Y. F.; Moore, R. J.; Zhao, R.; Hixson, K. K.; Rossie, S. S.; Smith, R. D. More sensitive and quantitative proteomic measurements using very low flow rate porous silica monolithic LC columns with electrospray ionization-mass spectrometry. J. Proteome Res. 2006, 5 (5), 1091-1097.
    • (2006) J. Proteome Res , vol.5 , Issue.5 , pp. 1091-1097
    • Luo, Q.Z.1    Tang, K.Q.2    Yang, F.3    Elias, A.4    Shen, Y.F.5    Moore, R.J.6    Zhao, R.7    Hixson, K.K.8    Rossie, S.S.9    Smith, R.D.10
  • 16
    • 33750743755 scopus 로고    scopus 로고
    • Robust algorithm for alignment of liquid chromatography-mass spectrometry analyses in an accurate mass and time tag data analysis pipeline
    • Jaitly, N.; Monroe, M. E.; Petyuk, V. A.; Clauss, T. R. W.; Adkins, J. N.; Smith, R. D. Robust algorithm for alignment of liquid chromatography-mass spectrometry analyses in an accurate mass and time tag data analysis pipeline. Anal. Chem. 2006, 78 (21), 7397-7409.
    • (2006) Anal. Chem , vol.78 , Issue.21 , pp. 7397-7409
    • Jaitly, N.1    Monroe, M.E.2    Petyuk, V.A.3    Clauss, T.R.W.4    Adkins, J.N.5    Smith, R.D.6
  • 18
    • 0036099050 scopus 로고    scopus 로고
    • Harkewicz, R.; Belov, M. E.; Anderson, D. A.; Pasa-Tolic, L.; Masselon, C. D.; Prior, D. C.; Udseth, H. R.; Smith, R. D. ESI-FTICR Mass Spectrometry Employing Data-Dependent External Ion Selection and Accumulation. J. Amer. Soc. Mass Spectrom. 2002, 13 144-154.
    • Harkewicz, R.; Belov, M. E.; Anderson, D. A.; Pasa-Tolic, L.; Masselon, C. D.; Prior, D. C.; Udseth, H. R.; Smith, R. D. ESI-FTICR Mass Spectrometry Employing Data-Dependent External Ion Selection and Accumulation. J. Amer. Soc. Mass Spectrom. 2002, 13 144-154.
  • 19
    • 33646264529 scopus 로고    scopus 로고
    • Advances in proteomics data analysis and display using an accurate mass and time tag approach
    • Zimmer, J. S. D.; Monroe, M. E.; Qian, W. J.; Smith, R. D. Advances in proteomics data analysis and display using an accurate mass and time tag approach. Mass Spectrom. Rev. 2006, 25 (3), 450-482.
    • (2006) Mass Spectrom. Rev , vol.25 , Issue.3 , pp. 450-482
    • Zimmer, J.S.D.1    Monroe, M.E.2    Qian, W.J.3    Smith, R.D.4
  • 20
    • 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, 1-8.
    • (2006) Nat. Biotechnol , pp. 1-8
    • Beausoleil, S.A.1    Villén, J.2    Gerber, S.A.3    Rush, J.4    Gygi, S.P.5
  • 22
    • 0024454195 scopus 로고
    • The tumour promoter okadaic acid inhibits reticulocyte-lysate protein synthesis by increasing the net phosphorylation of elongation factor 2
    • Redpath, N. T.; Proud, C. G. The tumour promoter okadaic acid inhibits reticulocyte-lysate protein synthesis by increasing the net phosphorylation of elongation factor 2. Biochem. J. 1989, 262 (1), 69-75.
    • (1989) Biochem. J , vol.262 , Issue.1 , pp. 69-75
    • Redpath, N.T.1    Proud, C.G.2
  • 23
    • 0025250558 scopus 로고
    • Activity of protein phosphatases against initiation factor-2 and elongation factor-2
    • Redpath, N. T.; Proud, C. G. Activity of protein phosphatases against initiation factor-2 and elongation factor-2. Biochem. J. 1990, 272 (1), 175-80.
    • (1990) Biochem. J , vol.272 , Issue.1 , pp. 175-180
    • Redpath, N.T.1    Proud, C.G.2
  • 24
    • 0030769624 scopus 로고    scopus 로고
    • A Distinct roles of PP1 and PP2A-like phosphatases in control of microtubule dynamics during mitosis
    • Tournebize, R.; Andersen, S. S.; Verde, F.; Doree, M.; Karsenti, E.; Hyman, A. A Distinct roles of PP1 and PP2A-like phosphatases in control of microtubule dynamics during mitosis. EMBO J. 1997, 16 (18), 5537-5549.
    • (1997) EMBO J , vol.16 , Issue.18 , pp. 5537-5549
    • Tournebize, R.1    Andersen, S.S.2    Verde, F.3    Doree, M.4    Karsenti, E.5    Hyman, A.6
  • 25
    • 0037474198 scopus 로고    scopus 로고
    • Protein phosphatase 2A and phosphoprotein SET regulate androgen production by P450c17
    • Pandey, A. V.; Mellon, S. H.; Miller, W. L. Protein phosphatase 2A and phosphoprotein SET regulate androgen production by P450c17. J. Biol. Chem. 2003, 278 (5), 2837-2844.
    • (2003) J. Biol. Chem , vol.278 , Issue.5 , pp. 2837-2844
    • Pandey, A.V.1    Mellon, S.H.2    Miller, W.L.3
  • 26
    • 1642360566 scopus 로고    scopus 로고
    • Specific in vivo phosphorylation sites determine the assembly dynamics of vimentin intermediate filaments
    • Eriksson, J. E.; He, T.; Trejo-Skalli, A. V.; Harmala-Brasken, A. S.; Hellman, I.; Chou, Y. H.; Goldman, R. D. Specific in vivo phosphorylation sites determine the assembly dynamics of vimentin intermediate filaments. J. Cell Sci. 2004, 117 (Pt 6), 919-932.
    • (2004) J. Cell Sci , vol.117 , Issue.PART 6 , pp. 919-932
    • Eriksson, J.E.1    He, T.2    Trejo-Skalli, A.V.3    Harmala-Brasken, A.S.4    Hellman, I.5    Chou, Y.H.6    Goldman, R.D.7
  • 27
    • 0037144405 scopus 로고    scopus 로고
    • Naringin-sensitive phosphorylation of plectin, a cytoskeletal cross-linking protein, in isolated rat hepatocytes
    • Larsen, A. K.; Moller, M. T.; Blankson, H.; Samari, H. R.; Holden, L.; Seglen, P. O. Naringin-sensitive phosphorylation of plectin, a cytoskeletal cross-linking protein, in isolated rat hepatocytes. J. Biol. Chem. 2002, 277 (38), 34826-34835.
    • (2002) J. Biol. Chem , vol.277 , Issue.38 , pp. 34826-34835
    • Larsen, A.K.1    Moller, M.T.2    Blankson, H.3    Samari, H.R.4    Holden, L.5    Seglen, P.O.6
  • 28
    • 0027217660 scopus 로고
    • Phosphorylation of human hnRNP protein A1 abrogates in vitro strand annealing activity
    • Cobianchi, F.; Calvio, C.; Stoppini, M.; Buvoli, M.; Riva, S. Phosphorylation of human hnRNP protein A1 abrogates in vitro strand annealing activity. Nucleic Acids Res. 1993, 21 (4), 949-955.
    • (1993) Nucleic Acids Res , vol.21 , Issue.4 , pp. 949-955
    • Cobianchi, F.1    Calvio, C.2    Stoppini, M.3    Buvoli, M.4    Riva, S.5
  • 29
    • 0030724902 scopus 로고    scopus 로고
    • Modulation of AUUUA response element binding by heterogeneous nuclear ribonucleoprotein A1 in human T lymphocytes. The roles of cytoplasmic location, transcription, and phosphorylation
    • Hamilton, B. J.; Burns, C. M.; Nichols, R. C.; Rigby, W. F. Modulation of AUUUA response element binding by heterogeneous nuclear ribonucleoprotein A1 in human T lymphocytes. The roles of cytoplasmic location, transcription, and phosphorylation. J. Biol. Chem. 1997, 272 (45), 28732-28741.
    • (1997) J. Biol. Chem , vol.272 , Issue.45 , pp. 28732-28741
    • Hamilton, B.J.1    Burns, C.M.2    Nichols, R.C.3    Rigby, W.F.4
  • 31
    • 0034967855 scopus 로고    scopus 로고
    • Chromatin assembly during S phase: Contributions from histone deposition, DNA replication and the cell division cycle
    • Krude, T.; Keller, C. Chromatin assembly during S phase: contributions from histone deposition, DNA replication and the cell division cycle. Cell. Mol. Life Sci. 2001, 58, (5-6), 665-72.
    • (2001) Cell. Mol. Life Sci , vol.58 , Issue.5-6 , pp. 665-672
    • Krude, T.1    Keller, C.2
  • 32
    • 0034634581 scopus 로고    scopus 로고
    • Requirement of Cyclin/Cdk2 and protein phosphatase 1 activity for chromatin assembly factor 1-dependent chromatin assembly during DNA synthesis
    • Keller, C.; Krude, T. Requirement of Cyclin/Cdk2 and protein phosphatase 1 activity for chromatin assembly factor 1-dependent chromatin assembly during DNA synthesis. J. Biol. Chem. 2000, 275 (45), 35512-35521.
    • (2000) J. Biol. Chem , vol.275 , Issue.45 , pp. 35512-35521
    • Keller, C.1    Krude, T.2
  • 33
    • 2642521977 scopus 로고    scopus 로고
    • Identification of phosphoproteins and their phosphorylation sites in the WEHI-231 B lymphoma cell line
    • Shu, H.; Chen, S.; Bi, Q.; Mumby, M.; Brekken, D. L. Identification of phosphoproteins and their phosphorylation sites in the WEHI-231 B lymphoma cell line. Mol. Cell Proteomics 2004, 3, (3), 279-286.
    • (2004) Mol. Cell Proteomics , vol.3 , Issue.3 , pp. 279-286
    • Shu, H.1    Chen, S.2    Bi, Q.3    Mumby, M.4    Brekken, D.L.5
  • 34
    • 0037458030 scopus 로고    scopus 로고
    • Salomon, A. R.; Ficarro, S. B.; Brill, L. M.; Blinker, A.; Phung, Q. T.; Ericson, C.; Sauer, K.; Brock, A.; Horn, D. M.; Schultz, P. G.; Peters, E. C Profiling of tyrosine phosphorylation pathways in human cells using mass spectrometry. Proc. Natl. Acad. Sci. U.S.A. 2003, 100 (2), 443-448.
    • Salomon, A. R.; Ficarro, S. B.; Brill, L. M.; Blinker, A.; Phung, Q. T.; Ericson, C.; Sauer, K.; Brock, A.; Horn, D. M.; Schultz, P. G.; Peters, E. C Profiling of tyrosine phosphorylation pathways in human cells using mass spectrometry. Proc. Natl. Acad. Sci. U.S.A. 2003, 100 (2), 443-448.
  • 35
    • 2442658049 scopus 로고    scopus 로고
    • Robust phosphoproteomic profiling of tyrosine phosphorylation sites from human T cells using immobilized metal affinity chromatography and tandem mass spectrometry
    • Brill, L. M.; Salomon, A. R.; Ficarro, S. B.; Mukherji, M.; Stettler-Gill, M.; Peters, E. C. Robust phosphoproteomic profiling of tyrosine phosphorylation sites from human T cells using immobilized metal affinity chromatography and tandem mass spectrometry. Anal. Chem. 2004, 76 (10), 2763-2772.
    • (2004) Anal. Chem , vol.76 , Issue.10 , pp. 2763-2772
    • Brill, L.M.1    Salomon, A.R.2    Ficarro, S.B.3    Mukherji, M.4    Stettler-Gill, M.5    Peters, E.C.6
  • 36
    • 0032697492 scopus 로고    scopus 로고
    • Signaling pathways and structural domains required for phosphorylation of EMS1/cortactin
    • Campbell, D. H.; Sutherland, R. L.; Daly, R. J. Signaling pathways and structural domains required for phosphorylation of EMS1/cortactin. Cancer Res. 1999, 59 (20), 5376-5385.
    • (1999) Cancer Res , vol.59 , Issue.20 , pp. 5376-5385
    • Campbell, D.H.1    Sutherland, R.L.2    Daly, R.J.3
  • 38
    • 2642580994 scopus 로고    scopus 로고
    • Pulmonary endothelial cell barrier enhancement by sphingosine 1-phosphate: Roles for cortactin and myosin light chain kinase
    • Dudek, S. M.; Jacobson, J. R.; Chiang, E. T.; Birukov, K. C.; Wang, P.; Zhan, X.; Garcia, J. G. Pulmonary endothelial cell barrier enhancement by sphingosine 1-phosphate: roles for cortactin and myosin light chain kinase. J. Biol. Chem. 2004, 279 (23), 24692-24700.
    • (2004) J. Biol. Chem , vol.279 , Issue.23 , pp. 24692-24700
    • Dudek, S.M.1    Jacobson, J.R.2    Chiang, E.T.3    Birukov, K.C.4    Wang, P.5    Zhan, X.6    Garcia, J.G.7
  • 39
    • 0032476012 scopus 로고    scopus 로고
    • The role of tyrosine phosphorylation of cortactin in the locomotion of endothelial cells
    • Huang, C.; Liu, J.; Haudenschild, C. C.; Zhan, X. The role of tyrosine phosphorylation of cortactin in the locomotion of endothelial cells. J. Biol. Chem. 1998, 273 (40), 25770-25776.
    • (1998) J. Biol. Chem , vol.273 , Issue.40 , pp. 25770-25776
    • Huang, C.1    Liu, J.2    Haudenschild, C.C.3    Zhan, X.4
  • 40
    • 0025988705 scopus 로고
    • Regulatory phosphorylation of the p34cdc2 protein kinase in vertebrates
    • Norbury, C.; Blow, J.; Nurse, P. Regulatory phosphorylation of the p34cdc2 protein kinase in vertebrates. EMBOJ. 1991, 10 (11), 3321-3329.
    • (1991) EMBOJ , vol.10 , Issue.11 , pp. 3321-3329
    • Norbury, C.1    Blow, J.2    Nurse, P.3
  • 41
    • 0027007963 scopus 로고
    • Role of phosphorylation in p34cdc2 activation: Idenltification of an activating kinase
    • Solomon, M. J.; Lee, T.; Kirschner, M. W. Role of phosphorylation in p34cdc2 activation: idenltification of an activating kinase. Mol. Biol. Cell 1992, 3 (1), 13-27.
    • (1992) Mol. Biol. Cell , vol.3 , Issue.1 , pp. 13-27
    • Solomon, M.J.1    Lee, T.2    Kirschner, M.W.3
  • 42
    • 0026027660 scopus 로고
    • Differential phosphorylation of vertebrate p34cdc2 kinase at the G1/S and G2/M transitions of the cell cycle: Identification of major phosphorylation sites
    • Krek, W.; Nigg, E. A. Differential phosphorylation of vertebrate p34cdc2 kinase at the G1/S and G2/M transitions of the cell cycle: identification of major phosphorylation sites. EMBO J. 1991, 10 (2), 305-316.
    • (1991) EMBO J , vol.10 , Issue.2 , pp. 305-316
    • Krek, W.1    Nigg, E.A.2
  • 43
    • 23844516065 scopus 로고    scopus 로고
    • The Mnks are novel components in the control of TNF alpha biosynthesis and phosphorylate and regulate hnRNP A1
    • Buxade, M.; Parra, J. L.; Rousseau, S.; Shpiro, N.; Marquez, R.; Morrice, N.; Bain, J.; Espel, E.; Proud, C. G. The Mnks are novel components in the control of TNF alpha biosynthesis and phosphorylate and regulate hnRNP A1. Immunity 2005, 23 (2), 177-189.
    • (2005) Immunity , vol.23 , Issue.2 , pp. 177-189
    • Buxade, M.1    Parra, J.L.2    Rousseau, S.3    Shpiro, N.4    Marquez, R.5    Morrice, N.6    Bain, J.7    Espel, E.8    Proud, C.G.9
  • 44
    • 33747072663 scopus 로고    scopus 로고
    • Kwiek, N. C.; Thacker, D. F.; Datto, M. B.; Megosh, H. B.; Haystead, T. A. PITK, a PP1 targeting subunit that modulates the phosphorylation of the transcriptional regulator hnRNP K. Cell. Signal. 2006, 18 (10), 1769-1778.
    • Kwiek, N. C.; Thacker, D. F.; Datto, M. B.; Megosh, H. B.; Haystead, T. A. PITK, a PP1 targeting subunit that modulates the phosphorylation of the transcriptional regulator hnRNP K. Cell. Signal. 2006, 18 (10), 1769-1778.
  • 46
    • 0035800862 scopus 로고    scopus 로고
    • Zipper-interacting protein kinase induces Ca-(2+)-free smooth muscle contraction via myosin light chain phosphorylation
    • Niiro, N.; Ikebe, M. Zipper-interacting protein kinase induces Ca-(2+)-free smooth muscle contraction via myosin light chain phosphorylation. J. Biol. Chem. 2001, 276 (31), 29567-29574.
    • (2001) J. Biol. Chem , vol.276 , Issue.31 , pp. 29567-29574
    • Niiro, N.1    Ikebe, M.2
  • 47
    • 0037169533 scopus 로고    scopus 로고
    • Phosphorylation of the myosin-binding subunit of myosin phosphatase by Raf-1 and inhibition of phosphatase activity
    • Broustas, C. G.; Grammatikakis, N.; Eto, M.; Dent, P.; Brautigan, D. L.; Kasid, U. Phosphorylation of the myosin-binding subunit of myosin phosphatase by Raf-1 and inhibition of phosphatase activity. J. Biol. Chem. 2002, 277 (4), 3053-3059.
    • (2002) J. Biol. Chem , vol.277 , Issue.4 , pp. 3053-3059
    • Broustas, C.G.1    Grammatikakis, N.2    Eto, M.3    Dent, P.4    Brautigan, D.L.5    Kasid, U.6
  • 48
    • 0037155132 scopus 로고    scopus 로고
    • Active Rho kinase (ROK-alpha) associates with insulin receptor substrate-1 and inhibits insulin signaling in vascular smooth muscle cells
    • Begum, N.; Sandu, O. A.; Ito, M.; Lohmann, S. M.; Smolenski, A. Active Rho kinase (ROK-alpha) associates with insulin receptor substrate-1 and inhibits insulin signaling in vascular smooth muscle cells. J. Biol. Chem. 2002, 277 (8), 6214-6222.
    • (2002) J. Biol. Chem , vol.277 , Issue.8 , pp. 6214-6222
    • Begum, N.1    Sandu, O.A.2    Ito, M.3    Lohmann, S.M.4    Smolenski, A.5
  • 49
    • 0141794500 scopus 로고    scopus 로고
    • 2+-dependent activation of Rho and Rho kinase in membrane depolarization-induced and receptor stimulation-induced vascular smooth muscle contraction
    • 2+-dependent activation of Rho and Rho kinase in membrane depolarization-induced and receptor stimulation-induced vascular smooth muscle contraction. Circ. Res. 2003, 93 (6), 548-556.
    • (2003) Circ. Res , vol.93 , Issue.6 , pp. 548-556
    • Sakurada, S.1    Takuwa, N.2    Sugimoto, N.3    Wang, Y.4    Seto, M.5    Sasaki, Y.6    Takuwa, Y.7
  • 50
    • 0347989369 scopus 로고    scopus 로고
    • Role of Rho GTPases in thrombin-induced lung vascular endothelial cells barrier dysfunction
    • Birukova, A. A.; Smurova, K.; Birukov, K. G.; Kaibuchi, K.; Garcia, J. G.; Verin, A. D. Role of Rho GTPases in thrombin-induced lung vascular endothelial cells barrier dysfunction. Microvasc. Res. 2004, 67 (1), 64-77.
    • (2004) Microvasc. Res , vol.67 , Issue.1 , pp. 64-77
    • Birukova, A.A.1    Smurova, K.2    Birukov, K.G.3    Kaibuchi, K.4    Garcia, J.G.5    Verin, A.D.6
  • 51
    • 2942718916 scopus 로고    scopus 로고
    • Protein kinase A attenuates endothelial cell barrier dysfunction induced by microtubule disassembly
    • Birukova, A. A.; Liu, F.; Garcia, J. G.; Verin, A. D. Protein kinase A attenuates endothelial cell barrier dysfunction induced by microtubule disassembly. Am. J. Physiol. Lung Cell Mol. Physiol. 2004, 287 (1), L86-L93.
    • (2004) Am. J. Physiol. Lung Cell Mol. Physiol , vol.287 , Issue.1
    • Birukova, A.A.1    Liu, F.2    Garcia, J.G.3    Verin, A.D.4
  • 53
    • 9644307938 scopus 로고    scopus 로고
    • Inhibition by Rho-kinase and protein kinase C of myosin phosphatase is involved in thrombin-induced shape change of megakaryocyte leukemia cell line UT-7/TPO
    • Yazaki, A.; Tamaru, S.; Sasaki, Y.; Komatsu, N.; Wada, H.; Shiku, H.; Nishikawa, M. Inhibition by Rho-kinase and protein kinase C of myosin phosphatase is involved in thrombin-induced shape change of megakaryocyte leukemia cell line UT-7/TPO. Cell. Signal. 2005, 17 (3), 321-330.
    • (2005) Cell. Signal , vol.17 , Issue.3 , pp. 321-330
    • Yazaki, A.1    Tamaru, S.2    Sasaki, Y.3    Komatsu, N.4    Wada, H.5    Shiku, H.6    Nishikawa, M.7
  • 54
    • 21244464353 scopus 로고    scopus 로고
    • Alphal-adrenoceptor-mediated phosphorylation of MYPT-1 and CPI-17 in the uterine artery: Role of ERK/PKC
    • Xiao, D.; Longo, L. D.; Zhang, L. Alphal-adrenoceptor-mediated phosphorylation of MYPT-1 and CPI-17 in the uterine artery: role of ERK/PKC. Am. J. Physiol. Heart Circ. Physiol. 2005, 288 (6), H2828-H2835.
    • (2005) Am. J. Physiol. Heart Circ. Physiol , vol.288 , Issue.6
    • Xiao, D.1    Longo, L.D.2    Zhang, L.3
  • 55
    • 19344371353 scopus 로고    scopus 로고
    • Activation of Rho-associated kinase during augmented contraction of the basilar artery to serotonin after subarachnoid hemorrhage
    • Watanabe, Y.; Faraci, F. M.; Heistad, D. D. Activation of Rho-associated kinase during augmented contraction of the basilar artery to serotonin after subarachnoid hemorrhage. Am. J. Physiol. Heart Circ. Physiol. 2005, 288 (6), H2653-H2658.
    • (2005) Am. J. Physiol. Heart Circ. Physiol , vol.288 , Issue.6
    • Watanabe, Y.1    Faraci, F.M.2    Heistad, D.D.3
  • 56
    • 20444469676 scopus 로고    scopus 로고
    • The Pro33 isoform of integrin beta3 enhances outside-in signaling in human platelets by regulating the activation of serine/threonine phosphatases
    • Vijayan, K. V.; Liu, Y.; Sun, W.; Ito, M.; Bray, P. F. The Pro33 isoform of integrin beta3 enhances outside-in signaling in human platelets by regulating the activation of serine/threonine phosphatases. J. Biol. Chem. 2005, 280 (23), 21756-21762.
    • (2005) J. Biol. Chem , vol.280 , Issue.23 , pp. 21756-21762
    • Vijayan, K.V.1    Liu, Y.2    Sun, W.3    Ito, M.4    Bray, P.F.5
  • 57
    • 22144463225 scopus 로고    scopus 로고
    • Okadaic acid induces phosphorylation and translocation of myosin phosphatase target subunit 1 influencing myosin phosphorylation, stress fiber assembly and cell migration in HepG2 cells
    • Lontay, B.; Kiss, A.; Gergely, P.; Hartshorne, D. J.; Erdodi, F. Okadaic acid induces phosphorylation and translocation of myosin phosphatase target subunit 1 influencing myosin phosphorylation, stress fiber assembly and cell migration in HepG2 cells. Cell. Signal. 2005, 17 (10), 1265-1275.
    • (2005) Cell. Signal , vol.17 , Issue.10 , pp. 1265-1275
    • Lontay, B.1    Kiss, A.2    Gergely, P.3    Hartshorne, D.J.4    Erdodi, F.5
  • 59
    • 0032479215 scopus 로고    scopus 로고
    • Activation of protein phosphatase 2A by cAMP-dependent protein kinase-catalyzed phosphorylation of the 74-kDa B″ (delta) regulatory subunit in vitro and identification of the phosphorylation sites
    • Usui, H.; Inoue, R.; Tanabe, O.; Nishito, Y.; Shimizu, M.; Hayashi, H.; Kagamiyama, H.; Takeda, M. Activation of protein phosphatase 2A by cAMP-dependent protein kinase-catalyzed phosphorylation of the 74-kDa B″ (delta) regulatory subunit in vitro and identification of the phosphorylation sites. FEBS Lett. 1998, 430 (3), 312-316.
    • (1998) FEBS Lett , vol.430 , Issue.3 , pp. 312-316
    • Usui, H.1    Inoue, R.2    Tanabe, O.3    Nishito, Y.4    Shimizu, M.5    Hayashi, H.6    Kagamiyama, H.7    Takeda, M.8
  • 60
    • 0029062935 scopus 로고
    • Mutagenesis studies of the phosphorylation sites of recombinant human pyruvate dehydrogenase. Site-specific regulation
    • Korotchkina, L. G.; Patel, M. S. Mutagenesis studies of the phosphorylation sites of recombinant human pyruvate dehydrogenase. Site-specific regulation. J. Biol. Chem. 1995, 270 (24), 14297-14304.
    • (1995) J. Biol. Chem , vol.270 , Issue.24 , pp. 14297-14304
    • Korotchkina, L.G.1    Patel, M.S.2
  • 61
    • 0035813150 scopus 로고    scopus 로고
    • Site specificity of four pyruvate dehydrogenase kinase isoenzymes toward the three phosphorylation sites of human pyruvate dehydrogenase
    • Korotchkina, L. G.; Patel, M. S. Site specificity of four pyruvate dehydrogenase kinase isoenzymes toward the three phosphorylation sites of human pyruvate dehydrogenase. J. Biol. Chem. 2001, 276 (40), 37223-37229.
    • (2001) J. Biol. Chem , vol.276 , Issue.40 , pp. 37223-37229
    • Korotchkina, L.G.1    Patel, M.S.2
  • 62
    • 33646899689 scopus 로고    scopus 로고
    • Characterization of testis-specific isoenzyme of human pyruvate dehydrogenase
    • Korotchkina, L. G.; Sidhu, S.; Patel, M. S. Characterization of testis-specific isoenzyme of human pyruvate dehydrogenase. J. Biol. Chem. 2006, 281 (14), 9688-9696.
    • (2006) J. Biol. Chem , vol.281 , Issue.14 , pp. 9688-9696
    • Korotchkina, L.G.1    Sidhu, S.2    Patel, M.S.3
  • 64
    • 24644480042 scopus 로고    scopus 로고
    • Vimentin rearrangement during African swine fever virus infection involves retrograde transport along microtubules and phosphorylation of vimentin by calcium calmodulin kinase II
    • Stefanovic, S.; Windsor, M.; Nagata, K. I.; Inagaki, M.; Wileman, T. Vimentin rearrangement during African swine fever virus infection involves retrograde transport along microtubules and phosphorylation of vimentin by calcium calmodulin kinase II. J. Virol. 2005, 79 (18), 11766-11775.
    • (2005) J. Virol , vol.79 , Issue.18 , pp. 11766-11775
    • Stefanovic, S.1    Windsor, M.2    Nagata, K.I.3    Inagaki, M.4    Wileman, T.5
  • 65
    • 21744440559 scopus 로고    scopus 로고
    • Silencing of p21-activated kinase attenuates vimentin phosphorylation on Ser-56 and reorientation of the vimentin network during stimulation of smooth muscle cells by 5-hydroxytryptamine
    • Tang, D. D.; Bai, Y.; Gunst, S. J. Silencing of p21-activated kinase attenuates vimentin phosphorylation on Ser-56 and reorientation of the vimentin network during stimulation of smooth muscle cells by 5-hydroxytryptamine. Biochem. J. 2005, 388 (Pt 3), 773-783.
    • (2005) Biochem. J , vol.388 , Issue.PART 3 , pp. 773-783
    • Tang, D.D.1    Bai, Y.2    Gunst, S.J.3
  • 66
    • 20444433540 scopus 로고    scopus 로고
    • The intermediate filament protein vimentin is a new target for epigallocatechin gallate
    • Ermakova, S.; Choi, B. Y.; Choi, H. S.; Kang, B. S.; Bode, A. M.; Dong, Z. The intermediate filament protein vimentin is a new target for epigallocatechin gallate. J. Biol. Chem. 2005, 280 (17), 16882-16890.
    • (2005) J. Biol. Chem , vol.280 , Issue.17 , pp. 16882-16890
    • Ermakova, S.1    Choi, B.Y.2    Choi, H.S.3    Kang, B.S.4    Bode, A.M.5    Dong, Z.6
  • 67
    • 0028151022 scopus 로고
    • Visualization and function of vimentin phosphorylation by cdc2 kinase during mitosis
    • Tsujimura, K.; Ogawara, M.; Takeuchi, Y.; Imajoh-Ohmi, S.; Ha, M. H.; Inagaki, M. Visualization and function of vimentin phosphorylation by cdc2 kinase during mitosis. J. Biol. Chem. 1994, 269 (49), 31097-31106.
    • (1994) J. Biol. Chem , vol.269 , Issue.49 , pp. 31097-31106
    • Tsujimura, K.1    Ogawara, M.2    Takeuchi, Y.3    Imajoh-Ohmi, S.4    Ha, M.H.5    Inagaki, M.6
  • 68
    • 33645800984 scopus 로고    scopus 로고
    • Regulation of mitotic function of Chk1 through phosphorylation at novel sites by cyclin-dependent kinase 1 (Cdk1)
    • Shiromizu, T.; Goto, H.; Tomono, Y.; Bartek, J.; Totsukawa, G.; Inoko, A.; Nakanishi, M.; Matsumura, F.; Inagaki, M. Regulation of mitotic function of Chk1 through phosphorylation at novel sites by cyclin-dependent kinase 1 (Cdk1). Genes Cells 2006, 11 (5), 477-485.
    • (2006) Genes Cells , vol.11 , Issue.5 , pp. 477-485
    • Shiromizu, T.1    Goto, H.2    Tomono, Y.3    Bartek, J.4    Totsukawa, G.5    Inoko, A.6    Nakanishi, M.7    Matsumura, F.8    Inagaki, M.9
  • 69
    • 0030976196 scopus 로고    scopus 로고
    • Glutamate-dependent phosphorylation of elongation factor-2 and inhibition of protein synthesis in neurons
    • Marin, P.; Nastiuk, K. L.; Daniel, N.; Girault, J. A.; Czernik, A. J.; Glowinski, J.; Nairn, A. C.; Premont, J. Glutamate-dependent phosphorylation of elongation factor-2 and inhibition of protein synthesis in neurons. J. Neurosci. 1997, 17(10) 3445-3454.
    • (1997) J. Neurosci , vol.17 , Issue.10 , pp. 3445-3454
    • Marin, P.1    Nastiuk, K.L.2    Daniel, N.3    Girault, J.A.4    Czernik, A.J.5    Glowinski, J.6    Nairn, A.C.7    Premont, J.8
  • 70
    • 33751089801 scopus 로고    scopus 로고
    • Fast track to a phosphoprotein sketch - MALDI-TOF characterization of TLC-based tryptic phosphopeptide maps at femtomolar detection sensitivity
    • Kochin, V.; Imanishi, S. Y.; Eriksson, I. E. Fast track to a phosphoprotein sketch - MALDI-TOF characterization of TLC-based tryptic phosphopeptide maps at femtomolar detection sensitivity. Proteomics 2006, 6, (21), 5676-5682.
    • (2006) Proteomics , vol.6 , Issue.21 , pp. 5676-5682
    • Kochin, V.1    Imanishi, S.Y.2    Eriksson, I.E.3


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.