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Volumn 406, Issue 12, 2014, Pages 2841-2852

Screening Dyrk1A inhibitors by MALDI-QqQ mass spectrometry: Systematic comparison to established radiometric, luminescence, and LC-UV-MS assays

Author keywords

Enzyme inhibitors; Kinase assay; Phosphopeptide assay .MALDI triple quadrupole

Indexed keywords

CONTRAST MEDIA; DIAGNOSIS; ENZYMES; LIQUID CHROMATOGRAPHY; LUMINESCENCE; MASS SPECTROMETRY; PEPTIDES; PHOSPHORYLATION; RADIOMETRY; SUGAR SUBSTITUTES;

EID: 84904381452     PISSN: 16182642     EISSN: 16182650     Source Type: Journal    
DOI: 10.1007/s00216-014-7703-1     Document Type: Article
Times cited : (4)

References (58)
  • 1
    • 0033026444 scopus 로고    scopus 로고
    • Strategies toward the design of novel and selective protein tyrosine kinase inhibitors
    • doi:10.1016/S0163-7258(98)00044-8
    • Traxler P, Furet P (1999) Strategies toward the design of novel and selective protein tyrosine kinase inhibitors. Pharmacol Ther 82:195-206. doi:10.1016/S0163-7258(98)00044-8
    • (1999) Pharmacol Ther , vol.82 , pp. 195-206
    • Traxler, P.1    Furet, P.2
  • 2
    • 70350747591 scopus 로고    scopus 로고
    • Targeting protein kinases in central nervous system disorders
    • doi:10.1038/nrd2999
    • Chico LK, Van Eldik LJ, Watterson DM (2009) Targeting protein kinases in central nervous system disorders. Nat Rev Drug Discov 8: 892-909. doi:10.1038/nrd2999
    • (2009) Nat Rev Drug Discov , vol.8 , pp. 892-909
    • Chico, L.K.1    Van Eldik, L.J.2    Watterson, D.M.3
  • 3
    • 72849127628 scopus 로고    scopus 로고
    • Kinase mutations in human disease: Interpreting genotype-phenotype relationships
    • doi:10.1038/nrg2707
    • Lahiry P, Torkamani A, Schork NJ, Hegele RA (2010) Kinase mutations in human disease: interpreting genotype-phenotype relationships. Nat Rev Genet 11:60-74. doi:10.1038/nrg2707
    • (2010) Nat Rev Genet , vol.11 , pp. 60-74
    • Lahiry, P.1    Torkamani, A.2    Schork, N.J.3    Hegele, R.A.4
  • 4
    • 0032475973 scopus 로고    scopus 로고
    • Sequence characteristics, subcellular localization, and substrate specificity of DYRK-related kinases, a novel family of dual specificity protein kinases
    • doi:10.1074/jbc.273.40.25893
    • Becker W, Weber Y, Wetzel K, Eirmbter K, Tejedor FJ, Joost HG (1998) Sequence characteristics, subcellular localization, and substrate specificity of DYRK-related kinases, a novel family of dual specificity protein kinases. J Biol Chem 273:25893-25902. doi:10.1074/jbc.273.40.25893
    • (1998) J Biol Chem , vol.273 , pp. 25893-25902
    • Becker, W.1    Weber, Y.2    Wetzel, K.3    Eirmbter, K.4    Tejedor, F.J.5    Joost, H.G.6
  • 6
    • 20444387985 scopus 로고    scopus 로고
    • Activationloop autophosphorylation is mediated by a novel transitional intermediate formofDYRKs
    • doi:10.1016/j.cell.2005.03.034
    • Lochhead PA, Sibbet G, Morrice N, Cleghon V (2005) Activationloop autophosphorylation is mediated by a novel transitional intermediate formofDYRKs. Cell 121:925-936. doi:10.1016/j.cell.2005.03.034
    • (2005) Cell , vol.121 , pp. 925-936
    • Lochhead, P.A.1    Sibbet, G.2    Morrice, N.3    Cleghon, V.4
  • 7
    • 0032603540 scopus 로고    scopus 로고
    • Structural and functional characteristics of Dyrk, a novel subfamily of protein kinases with dual specificity
    • doi:10.1016/S0079-6603(08)60503-6
    • Becker W, Joost HG (1999) Structural and functional characteristics of Dyrk, a novel subfamily of protein kinases with dual specificity. Prog Nucleic Acid Res Mol Biol 62:1-17. doi:10.1016/S0079-6603(08)60503-6
    • (1999) Prog Nucleic Acid Res Mol Biol , vol.62 , pp. 1-17
    • Becker, W.1    Joost, H.G.2
  • 8
    • 0035340295 scopus 로고    scopus 로고
    • The kinase DYRK phosphorylates protein-synthesis initiation factor eIF2Bepsilon at Ser539 and the microtubule-Associated protein tau at Thr212: Potential role for DYRK as a glycogen synthase kinase 3-priming kinase
    • Woods YL, Cohen P, BeckerW, Jakes R, GoedertM,Wang X, Proud CG (2001) The kinase DYRK phosphorylates protein-synthesis initiation factor eIF2Bepsilon at Ser539 and the microtubule-Associated protein tau at Thr212: potential role for DYRK as a glycogen synthase kinase 3-priming kinase. Biochem J 355:609-615
    • (2001) Biochem J , vol.355 , pp. 609-615
    • Woods, Y.L.1    Cohen, P.2    Beckerw Jakes, R.3    Goedertmwang, X.4    Proud, C.G.5
  • 9
    • 33846430088 scopus 로고    scopus 로고
    • Trisomy-driven overexpression of DYRK1A kinase in the brain of subjects with Down syndrome
    • doi:10.1016/j.neulet.2006.11.026
    • DowjatWK, Adayev T, Kuchna I, Nowicki K, Palminiello S, Hwang Y-W, Wegiel J (2007) Trisomy-driven overexpression of DYRK1A kinase in the brain of subjects with Down syndrome. Neurosci Lett 413:77-81. doi:10.1016/j.neulet.2006. 11.026
    • (2007) Neurosci Lett , vol.413 , pp. 77-81
    • Dowjat, W.K.1    Adayev, T.2    Kuchna, I.3    Nowicki, K.4    Palminiello, S.5    Hwang, Y.-W.6    Wegiel, J.7
  • 10
    • 10144260033 scopus 로고    scopus 로고
    • A human homologue of Drosophila minibrain (MNB) is expressed in the neuronal regions affected in Down syndrome and maps to the critical region
    • doi:10.1093/hmg/5.9.1305
    • Guimerá J, Casas C, Pucharcòs C, Solans A, Doménech A, Planas AM, Ashley J, Lovett M, Estivill X, Pritchard MA (1996) A human homologue of Drosophila minibrain (MNB) is expressed in the neuronal regions affected in Down syndrome and maps to the critical region. Hum Mol Genet 5:1305-1310. doi:10.1093/hmg/5.9.1305
    • (1996) Hum Mol Genet , vol.5 , pp. 1305-1310
    • Guimerá, J.1    Casas, C.2    Pucharcòs, C.3    Solans, A.4    Doménech, A.5    Planas, A.M.6    Ashley, J.7    Lovett, M.8    Estivill, X.9    Pritchard, M.A.10
  • 11
    • 51349109221 scopus 로고    scopus 로고
    • Overexpression of Dyrk1A contributes to neurofibrillary degeneration in Down syndrome
    • doi:10.1096/fj.07-104539
    • Liu F, Liang Z, Wegiel J, Hwang Y-W, Iqbal K, Grundke-Iqbal I, Ramakrishna N, Gong C-X (2008) Overexpression of Dyrk1A contributes to neurofibrillary degeneration in Down syndrome. FASEB J 22:3224-3233. doi:10.1096/fj.07-104539
    • (2008) FASEB J , vol.22 , pp. 3224-3233
    • Liu, F.1    Liang, Z.2    Wegiel, J.3    Hwang, Y.-W.4    Iqbal, K.5    Grundke-Iqbal, I.6    Ramakrishna, N.7    Gong, C.-X.8
  • 12
    • 12344323961 scopus 로고    scopus 로고
    • Tau phosphorylation in neuronal cell function and dysfunction
    • doi:10.1242/jcs.01558
    • Johnson GVW, StoothoffWH (2004) Tau phosphorylation in neuronal cell function and dysfunction. J Cell Sci 117:5721-5729. doi:10.1242/jcs.01558
    • (2004) J Cell Sci , vol.117 , pp. 5721-5729
    • Johnson, G.V.W.1    Stoothoff, W.H.2
  • 13
    • 37049027122 scopus 로고    scopus 로고
    • Tau phosphorylation sites work in concert to promote neurotoxicity in vivo
    • doi:10.1091/mbc.E07-04-0327
    • Steinhilb ML, Dias-Santagata D, Fulga TA, Felch DL, Feany MB (2007) Tau phosphorylation sites work in concert to promote neurotoxicity in vivo.Mol Biol Cell 18:5060-5068. doi:10.1091/mbc.E07-04-0327
    • (2007) Mol Biol Cell , vol.18 , pp. 5060-5068
    • Steinhilb, M.L.1    Dias-Santagata, D.2    Fulga, T.A.3    Felch, D.L.4    Feany, M.B.5
  • 15
    • 78651061790 scopus 로고    scopus 로고
    • The role of DYRK1A in neurodegenerative diseases
    • doi:10.1111/j.1742-4658.2010.07955.x
    • Wegiel J, Gong C-X, Hwang Y-W (2011) The role of DYRK1A in neurodegenerative diseases. FEBS J 278:236-245. doi:10.1111/j.1742-4658.2010. 07955.x
    • (2011) FEBS J , vol.278 , pp. 236-245
    • Wegiel, J.1    Gong, C.-X.2    Hwang, Y.-W.3
  • 16
    • 20444432725 scopus 로고    scopus 로고
    • High-throughput screening for kinase inhibitors
    • doi:10.1002/cbic.200400211
    • Von Ahsen O, Bömer U (2005) High-throughput screening for kinase inhibitors. Chembiochem 6:481-490. doi:10.1002/cbic.200400211
    • (2005) Chembiochem , vol.6 , pp. 481-490
    • Von Ahsen, O.1    Bömer, U.2
  • 18
    • 78449276240 scopus 로고    scopus 로고
    • Multiplex enzyme assays and inhibitor screening by mass spectrometry
    • doi:10.1177/1087057110363824
    • Rathore R, Pribil P, Corr JJ, Seibel WL, Evdokimov A, Greis KD (2010) Multiplex enzyme assays and inhibitor screening by mass spectrometry. J Biomol Screen 15:1001-1007. doi:10.1177/1087057110363824
    • (2010) J Biomol Screen , vol.15 , pp. 1001-1007
    • Rathore, R.1    Pribil, P.2    Corr, J.J.3    Seibel, W.L.4    Evdokimov, A.5    Greis, K.D.6
  • 19
    • 68049144962 scopus 로고    scopus 로고
    • Academic HTS: Diverse portraits
    • doi:10.1016/j.ddtec.2009.01.001
    • Nelson SL (2008) Academic HTS: diverse portraits. Drug Discov Today Technol 5:e29-e33. doi:10.1016/j.ddtec.2009.01.001
    • (2008) Drug Discov Today Technol , vol.5
    • Nelson, S.L.1
  • 20
    • 34248545259 scopus 로고    scopus 로고
    • Mass spectrometry for enzyme assays and inhibitor screening: An emerging application in pharmaceutical research
    • doi:10.1002/mas.20127
    • Greis KD (2007) Mass spectrometry for enzyme assays and inhibitor screening: an emerging application in pharmaceutical research. Mass Spectrom Rev 26:324-339. doi:10.1002/mas.20127
    • (2007) Mass Spectrom Rev , vol.26 , pp. 324-339
    • Greis, K.D.1
  • 22
    • 32444451730 scopus 로고    scopus 로고
    • Applications of mass spectrometry in early stages of target based drug discovery
    • doi:10.1016/j.jpba.2005.08.038
    • Deng G, Sanyal G (2006) Applications of mass spectrometry in early stages of target based drug discovery. J Pharm Biomed Anal 40:528-538. doi:10.1016/j.jpba.2005.08.038
    • (2006) J Pharm Biomed Anal , vol.40 , pp. 528-538
    • Deng, G.1    Sanyal, G.2
  • 23
    • 56949102231 scopus 로고    scopus 로고
    • Monitoring enzyme reaction and screening of inhibitors of acetylcholinesterase by quantitative matrix-Assisted laser desorption/ ionization Fourier transform mass spectrometry
    • doi:10.1016/j.jasms.2008.07.025
    • Xu Z, Yao S, Wei Y, Zhou J, Zhang L, Wang C, Guo Y (2008) Monitoring enzyme reaction and screening of inhibitors of acetylcholinesterase by quantitative matrix-Assisted laser desorption/ ionization Fourier transform mass spectrometry. J Am Soc Mass Spectrom 19:1849-1855. doi:10.1016/j.jasms.2008.07. 025
    • (2008) J Am Soc Mass Spectrom , vol.19 , pp. 1849-1855
    • Xu, Z.1    Yao, S.2    Wei, Y.3    Zhou, J.4    Zhang, L.5    Wang, C.6    Guo, Y.7
  • 24
    • 84856656490 scopus 로고    scopus 로고
    • Assisted inhibition effect of acetylcholinesterase with n-octylphosphonic acid and application in high sensitive detection of organophosphorous pesticides by matrix-Assisted laser desorption/ionization Fourier transform mass spectrometry
    • doi:10.1016/j.aca.2011.08.035
    • Cai T, Zhang L,Wang H, Zhang J, Guo Y (2011) Assisted inhibition effect of acetylcholinesterase with n-octylphosphonic acid and application in high sensitive detection of organophosphorous pesticides by matrix-Assisted laser desorption/ionization Fourier transform mass spectrometry. Anal Chim Acta 706:291-296. doi:10.1016/j.aca.2011.08.035
    • (2011) Anal Chim Acta , vol.706 , pp. 291-296
    • Cai, T.1    Zhang, L.2    Wang, H.3    Zhang, J.4    Guo, Y.5
  • 25
    • 84855522034 scopus 로고    scopus 로고
    • Characterization of β-lactamase enzyme activity in bacterial lysates using MALDI-mass spectrometry
    • doi:10.1021/pr200858r
    • Hooff GP, van Kampen JJA, Meesters RJW, van Belkum A, Goessens WHF, Luider TM (2012) Characterization of β-lactamase enzyme activity in bacterial lysates using MALDI-mass spectrometry. J Proteome Res 11:79-84. doi:10.1021/pr200858r
    • (2012) J Proteome Res , vol.11 , pp. 79-84
    • Hooff, G.P.1    Van Kampen Jja2    Rjw, M.3    Van Belkum, A.4    Whf, G.5    Luider, T.M.6
  • 26
    • 77749299081 scopus 로고    scopus 로고
    • Determination of beta-lactamase residues in milk using matrixassisted laser desorption/ionization Fourier transform mass spectrometry
    • doi:10.1021/ac9019945
    • Xu Z, Wang H-Y, Huang S-X, Wei Y-L, Yao S-J, Guo Y-L (2010) Determination of beta-lactamase residues in milk using matrixassisted laser desorption/ionization Fourier transform mass spectrometry. Anal Chem 82:2113-2118. doi:10.1021/ac9019945
    • (2010) Anal Chem , vol.82 , pp. 2113-2118
    • Xu, Z.1    Wang, H.-Y.2    Huang, S.-X.3    Wei, Y.-L.4    Yao, S.-J.5    Guo, Y.-L.6
  • 29
    • 60749084976 scopus 로고    scopus 로고
    • MALDI-TOF mass-spectrometrybased versatile method for the characterization of protein kinases
    • doi:10.1002/chem.200801650
    • Kondo N, Nishimura S (2009) MALDI-TOF mass-spectrometrybased versatile method for the characterization of protein kinases. Chemistry 15:1413-1421. doi:10.1002/chem.200801650
    • (2009) Chemistry , vol.15 , pp. 1413-1421
    • Kondo, N.1    Nishimura, S.2
  • 30
    • 1442323792 scopus 로고    scopus 로고
    • Quantitative matrix-Assisted laser desorption/ionization mass spectrometry for the determination of enzyme activities
    • doi:10.1016/j.ab.2003.11.013
    • Bungert D, Heinzle E, Tholey A (2004) Quantitative matrix-Assisted laser desorption/ionization mass spectrometry for the determination of enzyme activities. Anal Biochem 326:167-175. doi:10.1016/j.ab.2003.11.013
    • (2004) Anal Biochem , vol.326 , pp. 167-175
    • Bungert, D.1    Heinzle, E.2    Tholey, A.3
  • 31
    • 70449365418 scopus 로고    scopus 로고
    • Extending matrix-Assisted laser desorption/ionization triple quadrupole mass spectrometry enzyme screening assays to targets with small molecule substrates
    • doi:10.1002/rcm.4248
    • Rathore R, Corr JJ, Lebre DT, Seibel WL, Greis KD (2009) Extending matrix-Assisted laser desorption/ionization triple quadrupole mass spectrometry enzyme screening assays to targets with small molecule substrates. Rapid Commun Mass Spectrom 23: 3293-3300. doi:10.1002/rcm.4248
    • (2009) Rapid Commun Mass Spectrom , vol.23 , pp. 3293-3300
    • Rathore, R.1    Corr, J.J.2    Lebre, D.T.3    Seibel, W.L.4    Greis, K.D.5
  • 32
    • 0032127247 scopus 로고    scopus 로고
    • Nonradioactive phosphopeptide assay by matrix-Assisted laser desorption ionization time-offlight mass spectrometry: Application to calcium/ calmodulindependent protein kinase II
    • doi:10.1006/abio.1998.2691
    • Matsumoto H, Kahn ES, Komori N (1998) Nonradioactive phosphopeptide assay by matrix-Assisted laser desorption ionization time-offlight mass spectrometry: application to calcium/calmodulindependent protein kinase II. Anal Biochem 260:188-194. doi:10.1006/abio.1998.2691
    • (1998) Anal Biochem , vol.260 , pp. 188-194
    • Matsumoto, H.1    Kahn, E.S.2    Komori, N.3
  • 33
    • 0028166698 scopus 로고
    • Monitoring protein kinase and phosphatase reactions with matrix-Assisted laser desorption/ionization mass spectrometry and capillary zone electrophoresis: Comparison of the detection efficiency of peptide- phosphopeptide mixtures
    • doi:10.1002/bms.1200230810
    • Craig AG, Hoeger CA, Miller CL, Goedken T, Rivier JE, Fischer WH (1994) Monitoring protein kinase and phosphatase reactions with matrix-Assisted laser desorption/ionization mass spectrometry and capillary zone electrophoresis: comparison of the detection efficiency of peptide-phosphopeptide mixtures. BiolMass Spectrom 23: 519-528. doi:10.1002/bms.1200230810
    • (1994) BiolMass Spectrom , vol.23 , pp. 519-528
    • Craig, A.G.1    Hoeger, C.A.2    Miller, C.L.3    Goedken, T.4    Rivier, J.E.5    Fischer, W.H.6
  • 34
    • 0035337809 scopus 로고    scopus 로고
    • Assay of protein tyrosine phosphatases by using matrix-Assisted laser desorption ionization time-of-flight mass spectrometry
    • doi:10.1006/abio.2001.5071
    • Chen J, Qi Y, Zhao R, Zhou GW, Zhao ZJ (2001) Assay of protein tyrosine phosphatases by using matrix-Assisted laser desorption ionization time-of-flight mass spectrometry. Anal Biochem 292:51-58. doi:10.1006/abio.2001.5071
    • (2001) Anal Biochem , vol.292 , pp. 51-58
    • Chen, J.1    Qi, Y.2    Zhao, R.3    Zhou, G.W.4    Zhao, Z.J.5
  • 35
    • 31644439146 scopus 로고    scopus 로고
    • Phosphorylation analysis by mass spectrometry: Myths, facts, and the consequences for qualitative and quantitative measurements
    • doi:10.1074/mcp.M500135-MCP200
    • Steen H, Jebanathirajah JA, Rush J,Morrice N, KirschnerMW(2006) Phosphorylation analysis by mass spectrometry: myths, facts, and the consequences for qualitative and quantitative measurements. Mol Cell Proteomics 5:172-181. doi:10.1074/mcp.M500135-MCP200
    • (2006) Mol Cell Proteomics , vol.5 , pp. 172-181
    • Steen, H.1    Jebanathirajah, J.A.2    Rush, J.3    Morrice, N.4    Kirschner, M.W.5
  • 36
    • 84859718536 scopus 로고    scopus 로고
    • Correlation between phosphorylation ratios bymatrix-Assisted laser desorption/ionization time-of-flight mass spectrometry analysis and radioactivities by radioactive assay
    • doi:10.1016/j.ab.2011.08.035
    • Tsuchiya A, Asai D, Kang J-H, Mori T, Niidome T, Katayama Y (2012) Correlation between phosphorylation ratios bymatrix-Assisted laser desorption/ionization time-of-flight mass spectrometry analysis and radioactivities by radioactive assay. Anal Biochem 421:773-775. doi:10.1016/j.ab.2011.08.035
    • (2012) Anal Biochem , vol.421 , pp. 773-775
    • Tsuchiya, A.1    Asai, D.2    Kang, J.-H.3    Mori, T.4    Niidome, T.5    Katayama, Y.6
  • 38
    • 58149397935 scopus 로고    scopus 로고
    • Development of an inhibitor screening platform via mass spectrometry
    • doi:10.1177/1087057108326143
    • Rathore R, Corr JJ, Scott G, Vollmerhaus P, Greis KD (2008) Development of an inhibitor screening platform via mass spectrometry. J Biomol Screen 13:1007-1013. doi:10.1177/1087057108326143
    • (2008) J Biomol Screen , vol.13 , pp. 1007-1013
    • Rathore, R.1    Corr, J.J.2    Scott, G.3    Vollmerhaus, P.4    Greis, K.D.5
  • 40
    • 25644449539 scopus 로고    scopus 로고
    • Formation of phosphopeptide-metal ion complexes in liquid chromatography/electrospray mass spectrometry and their influence on phosphopeptide detection
    • doi:10.1002/rcm.2105
    • Liu S, Zhang C, Campbell JL, Zhang H, Yeung KK-C, Han VKM, Lajoie GA (2005) Formation of phosphopeptide-metal ion complexes in liquid chromatography/electrospray mass spectrometry and their influence on phosphopeptide detection. Rapid Commun Mass Spectrom 19:2747-2756. doi:10.1002/rcm.2105
    • (2005) Rapid Commun Mass Spectrom , vol.19 , pp. 2747-2756
    • Liu, S.1    Zhang, C.2    Campbell, J.L.3    Zhang, H.4    Kk-C, Y.5    Vkm, H.6    Lajoie, G.A.7
  • 41
    • 66249133391 scopus 로고    scopus 로고
    • The relative influence of phosphorylation andmethylation on responsiveness of peptides to MALDI and ESI mass spectrometry
    • doi:10.1002/jms.1581
    • Gropengiesser J, Varadarajan BT, Stephanowitz H, Krause E (2009) The relative influence of phosphorylation andmethylation on responsiveness of peptides to MALDI and ESI mass spectrometry. J Mass Spectrom 44:821-831. doi:10.1002/jms.1581
    • (2009) J Mass Spectrom , vol.44 , pp. 821-831
    • Gropengiesser, J.1    Varadarajan, B.T.2    Stephanowitz, H.3    Krause, E.4
  • 42
    • 84899847151 scopus 로고    scopus 로고
    • Design and synthesis of a library of lead-like 2,4-bisheterocyclic substituted thiophenes as selective Dyrk/Clk inhibitors
    • doi:10.1371/journal.pone.0087851
    • Schmitt C, Kail D, Mariano M, Empting M, Weber N, Paul T, Hartmann RW, Engel M (2014) Design and synthesis of a library of lead-like 2,4-bisheterocyclic substituted thiophenes as selective Dyrk/Clk inhibitors. PLoS One. doi:10.1371/journal.pone.0087851
    • (2014) PLoS One
    • Schmitt, C.1    Kail, D.2    Mariano, M.3    Empting, M.4    Weber, N.5    Paul, T.6    Hartmann, R.W.7    Engel, M.8
  • 43
    • 22744433154 scopus 로고    scopus 로고
    • Some fundamental and technical aspects of the quantitative analysis of pharmaceutical drugs by matrixassisted laser desorption/ionization mass spectrometry
    • doi:10.1002/rcm.2006
    • Sleno L, Volmer DA (2005) Some fundamental and technical aspects of the quantitative analysis of pharmaceutical drugs by matrixassisted laser desorption/ionization mass spectrometry. Rapid Commun Mass Spectrom 19:1928-1936. doi:10.1002/rcm.2006
    • (2005) Rapid Commun Mass Spectrom , vol.19 , pp. 1928-1936
    • Sleno, L.1    Volmer, D.A.2
  • 44
    • 33646745745 scopus 로고    scopus 로고
    • Assessing the properties of internal standards for quantitative matrix-Assisted laser desorption/ionization mass spectrometry of small molecules
    • doi:10.1002/rcm.2498
    • Sleno L, Volmer DA (2006) Assessing the properties of internal standards for quantitative matrix-Assisted laser desorption/ionization mass spectrometry of small molecules. Rapid Commun Mass Spectrom 20:1517-1524. doi:10.1002/rcm.2498
    • (2006) Rapid Commun Mass Spectrom , vol.20 , pp. 1517-1524
    • Sleno, L.1    Volmer, D.A.2
  • 45
    • 14744272825 scopus 로고    scopus 로고
    • Toxin screening in phytoplankton: Detection and quantitation using MALDI triple quadrupole mass spectrometry
    • doi:10.1021/ac0486600
    • Sleno L, Volmer DA (2005) Toxin screening in phytoplankton: detection and quantitation using MALDI triple quadrupole mass spectrometry. Anal Chem 77:1509-1517. doi:10.1021/ac0486600
    • (2005) Anal Chem , vol.77 , pp. 1509-1517
    • Sleno, L.1    Volmer, D.A.2
  • 46
    • 33749498659 scopus 로고    scopus 로고
    • Nonretentive solid-phase extraction of phosphorylated peptides from complex peptide mixtures for detection bymatrix-Assisted laser desorption/ionizationmass spectrometry
    • doi:10.1021/ac060485v
    • Kapkova P, Lattova E, Perreault H (2006) Nonretentive solid-phase extraction of phosphorylated peptides from complex peptide mixtures for detection bymatrix-Assisted laser desorption/ionizationmass spectrometry. Anal Chem 78:7027-7033. doi:10.1021/ac060485v
    • (2006) Anal Chem , vol.78 , pp. 7027-7033
    • Kapkova, P.1    Lattova, E.2    Perreault, H.3
  • 47
    • 67650908493 scopus 로고    scopus 로고
    • A binary matrix for improved detection of phosphopeptides in matrix-Assisted laser desorption/ ionization mass spectrometry
    • doi:10.1002/rcm.4139
    • Zhou L-H, Kang G-Y, Kim KP (2009) A binary matrix for improved detection of phosphopeptides in matrix-Assisted laser desorption/ ionization mass spectrometry. Rapid Commun Mass Spectrom 23: 2264-72. doi:10.1002/rcm.4139
    • (2009) Rapid Commun Mass Spectrom , vol.23 , pp. 2264-2272
    • Zhou, L.-H.1    Kang, G.-Y.2    Kim, K.P.3
  • 48
    • 79952116772 scopus 로고    scopus 로고
    • A robust procedure for comparing multiple means under heteroscedasticity in unbalanced designs
    • doi:10.1371/journal.pone. 0009788
    • Herberich E, Sikorski J, Hothorn T (2010) A robust procedure for comparing multiple means under heteroscedasticity in unbalanced designs. PLoS One 5:e9788. doi:10.1371/journal.pone. 0009788
    • (2010) PLoS One , vol.5
    • Herberich, E.1    Sikorski, J.2    Hothorn, T.3
  • 50
    • 70349947061 scopus 로고    scopus 로고
    • Harmine specifically inhibits protein kinase DYRK1A and interferes with neurite formation
    • doi:10.1111/j.1742-4658.2009.07346.x
    • Göckler N, Jofre G, Papadopoulos C, Soppa U, Tejedor FJ, Becker W, Gockler N (2009) Harmine specifically inhibits protein kinase DYRK1A and interferes with neurite formation. FEBS J 276:6324-6337. doi:10.1111/j.1742- 4658.2009.07346.x
    • (2009) FEBS J , vol.276 , pp. 6324-6337
    • Göckler, N.1    Jofre, G.2    Papadopoulos, C.3    Soppa, U.4    Tejedor, F.J.5    Becker, W.6    Gockler, N.7
  • 51
    • 66149169971 scopus 로고    scopus 로고
    • Phosphorylated serine and threonine residues promote sitespecific fragmentation of singly charged, arginine-containing peptide ions
    • doi:10.1002/ rcm.4019
    • Gehrig PM, Roschitzki B, Rutishauser D, Reiland S, Schlapbach R (2009) Phosphorylated serine and threonine residues promote sitespecific fragmentation of singly charged, arginine-containing peptide ions. Rapid Commun Mass Spectrom 23:1435-1445. doi:10.1002/ rcm.4019
    • (2009) Rapid Commun Mass Spectrom , vol.23 , pp. 1435-1445
    • Gehrig, P.M.1    Roschitzki, B.2    Rutishauser, D.3    Reiland, S.4    Schlapbach, R.5
  • 52
    • 80052798356 scopus 로고    scopus 로고
    • Modelling of the gas-phase phosphate group loss and rearrangement in phosphorylated peptides
    • doi:10.1002/jms.1974
    • Rožman M (2011) Modelling of the gas-phase phosphate group loss and rearrangement in phosphorylated peptides. J Mass Spectrom 46: 949-955. doi:10.1002/jms.1974
    • (2011) J Mass Spectrom , vol.46 , pp. 949-955
    • Rožman, M.1
  • 53
    • 67649213067 scopus 로고    scopus 로고
    • Phosphopeptide fragmentation and analysis by mass spectrometry
    • doi:10.1002/jms.1599
    • Boersema PJ, Mohammed S, Heck AJR (2009) Phosphopeptide fragmentation and analysis by mass spectrometry. J Mass Spectrom 44:861-878. doi:10.1002/jms.1599
    • (2009) J Mass Spectrom , vol.44 , pp. 861-878
    • Boersema, P.J.1    Mohammed, S.2    Ajr, H.3
  • 54
    • 77149177961 scopus 로고    scopus 로고
    • A CE-based assay for human protein kinase CK2 activity measurement and inhibitor screening
    • doi:10.1002/elps.200900514
    • Gratz A, Götz C, Jose J (2010) A CE-based assay for human protein kinase CK2 activity measurement and inhibitor screening. Electrophoresis 31:634-640. doi:10.1002/elps.200900514
    • (2010) Electrophoresis , vol.31 , pp. 634-640
    • Gratz, A.1    Götz, C.2    Jose, J.3
  • 55
    • 0033003760 scopus 로고    scopus 로고
    • A simple statistical parameter for use in evaluation and validation of high throughput screening assays
    • doi:10.1177/108705719900400206
    • Zhang J-H (1999) A simple statistical parameter for use in evaluation and validation of high throughput screening assays. J Biomol Screen 4:67-73. doi:10.1177/108705719900400206
    • (1999) J Biomol Screen , vol.4 , pp. 67-73
    • Zhang, J.-H.1
  • 56
    • 76449108493 scopus 로고    scopus 로고
    • Comparison of bioluminescent kinase assays using substrate depletion and product formation
    • doi:10.1089/adt.2009.0230
    • Tanega C, Shen M, Mott BT, Thomas CJ, MacArthur R, Inglese J, Auld DS (2009) Comparison of bioluminescent kinase assays using substrate depletion and product formation. Assay Drug Dev Technol 7:606-614. doi:10.1089/adt.2009.0230
    • (2009) Assay Drug Dev Technol , vol.7 , pp. 606-614
    • Tanega, C.1    Shen, M.2    Mott, B.T.3    Thomas, C.J.4    Macarthur, R.5    Inglese, J.6    Auld, D.S.7
  • 57
    • 34548755067 scopus 로고    scopus 로고
    • Assay of protein kinases using radiolabeled ATP: A protocol
    • doi:10.1038/nprot.2006.149
    • Hastie CJ,McLauchlan HJ, Cohen P (2006) Assay of protein kinases using radiolabeled ATP: a protocol. Nat Protoc 1:968-971. doi:10.1038/nprot.2006.149
    • (2006) Nat Protoc , vol.1 , pp. 968-971
    • Hastie, C.J.1    McLauchlan, H.J.2    Cohen, P.3
  • 58
    • 33750287595 scopus 로고    scopus 로고
    • Monitoring enzyme reaction and screening enzyme inhibitor based on MALDI-TOF-MS platform with a matrix of oxidized carbon nanotubes
    • doi:10.1016/j.jasms.2006.07.005
    • Hu L, Jiang G, Xu S, Pan C, Zou H (2006) Monitoring enzyme reaction and screening enzyme inhibitor based on MALDI-TOF-MS platform with a matrix of oxidized carbon nanotubes. J Am SocMass Spectrom 17:1616-1619. doi:10.1016/j.jasms.2006.07.005
    • (2006) J Am SocMass Spectrom , vol.17 , pp. 1616-1619
    • Hu, L.1    Jiang, G.2    Xu, S.3    Pan, C.4    Zou, H.5


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