메뉴 건너뛰기




Volumn 29, Issue 12, 2009, Pages 4949-4958

Simultaneous identification and quantification of proteins by differential 16O/18O labeling and UPLC-MS/MS applied to mouse cerebellar phosphoproteome following irradiation

Author keywords

Cerebellum; IMAC; Oxygen 18; Phosphoproteome; UPLC

Indexed keywords

OXYGEN; OXYGEN 18; PROTEIN KINASE; PROTEOME;

EID: 75149146699     PISSN: 02507005     EISSN: None     Source Type: Journal    
DOI: None     Document Type: Article
Times cited : (15)

References (89)
  • 1
    • 0030068923 scopus 로고    scopus 로고
    • Protease-catalyzed incorporation of O-18 into peptide fragments and its application for protein sequencing by electrospray and matrix-assisted laser desorption/ionization mass spectrometry
    • Schnolzer M, Jedrzejewski P and Lehmann WD: Protease-catalyzed incorporation of O-18 into peptide fragments and its application for protein sequencing by electrospray and matrix-assisted laser desorption/ionization mass spectrometry. Electrophoresis 17: 945-953, 1996.
    • (1996) Electrophoresis , vol.17 , pp. 945-953
    • Schnolzer, M.1    Jedrzejewski, P.2    Lehmann, W.D.3
  • 2
    • 0030668981 scopus 로고    scopus 로고
    • Accurate peptide sequencing by post-source decay matrix-assisted laser desorption/ionization time-of-flight mass spectrometry
    • Mo WJ, Takao T and Shimonishi Y: Accurate peptide sequencing by post-source decay matrix-assisted laser desorption/ionization time-of-flight mass spectrometry. Rapid Commun Mass Spectrom 11: 1829-1834, 1997.
    • (1997) Rapid Commun Mass Spectrom , vol.11 , pp. 1829-1834
    • Mo, W.J.1    Takao, T.2    Shimonishi, Y.3
  • 3
    • 0030960366 scopus 로고    scopus 로고
    • Rapid 'de novo' peptide sequencing by a combination of nanoelectrospray, isotopic labeling and a quadrupole/time-of-flight mass spectrometer
    • Shevchenko A, Chernushevich I, Ens W, Standing KG, Thomson B, Wilm M and Mann M: Rapid 'de novo' peptide sequencing by a combination of nanoelectrospray, isotopic labeling and a quadrupole/time-of-flight mass spectrometer. Rapid Commun Mass Spectrom 11: 1015-1024, 1997.
    • (1997) Rapid Commun Mass Spectrom , vol.11 , pp. 1015-1024
    • Shevchenko, A.1    Chernushevich, I.2    Ens, W.3    Standing, K.G.4    Thomson, B.5    Wilm, M.6    Mann, M.7
  • 5
    • 0033915395 scopus 로고    scopus 로고
    • Quantitation of peptides and proteins by matrix-assisted laser desorption/ionization mass spectrometry using O-18-labeled internal standards
    • Mirgorodskaya OA, Kozmin YP, Titov MI, Korner R, Sonksen CP and Roepstorff P: Quantitation of peptides and proteins by matrix-assisted laser desorption/ionization mass spectrometry using O-18-labeled internal standards. Rapid Commun Mass Spectrom 14: 1226-1232, 2000.
    • (2000) Rapid Commun Mass Spectrom , vol.14 , pp. 1226-1232
    • Mirgorodskaya, O.A.1    Kozmin, Y.P.2    Titov, M.I.3    Korner, R.4    Sonksen, C.P.5    Roepstorff, P.6
  • 6
    • 13244262721 scopus 로고    scopus 로고
    • O-18-labeling quantitative proteomics using an ion-trap mass spectrometer
    • Sakai J, Kojima S, Yanagi K and Kanaoka M: O-18-labeling quantitative proteomics using an ion-trap mass spectrometer. Proteomics 5: 16-23, 2005.
    • (2005) Proteomics , vol.5 , pp. 16-23
    • Sakai, J.1    Kojima, S.2    Yanagi, K.3    Kanaoka, M.4
  • 7
    • 32344443165 scopus 로고    scopus 로고
    • Combined chemical and enzymatic stable isotope labeling for quantitative profiling of detergent-insoluble membrane proteins isolated using Triton X-100 and Brij-96
    • Blonder J, Yu LR, Radeva G, Chan KC, Lucas DA, Waybright TJ, Issaq HJ, Sharom FJ and Veenstra TD: Combined chemical and enzymatic stable isotope labeling for quantitative profiling of detergent-insoluble membrane proteins isolated using Triton X-100 and Brij-96. J Proteome Res 5: 349-360, 2006.
    • (2006) J Proteome Res , vol.5 , pp. 349-360
    • Blonder, J.1    Yu, L.R.2    Radeva, G.3    Chan, K.C.4    Lucas, D.A.5    Waybright, T.J.6    Issaq, H.J.7    Sharom, F.J.8    Veenstra, T.D.9
  • 10
    • 4444271864 scopus 로고    scopus 로고
    • Global differential non-gel proteomics by quantitative and stable labeling of tryptic peptides with oxygen-18
    • Staes A, Demol H, Van Damme J, Martens L, Vandekerckhove J and Gevaert K: Global differential non-gel proteomics by quantitative and stable labeling of tryptic peptides with oxygen-18. J Proteome Res 3: 786-791, 2004.
    • (2004) J Proteome Res , vol.3 , pp. 786-791
    • Staes, A.1    Demol, H.2    Van Damme, J.3    Martens, L.4    Vandekerckhove, J.5    Gevaert, K.6
  • 11
    • 0035384687 scopus 로고    scopus 로고
    • Proteolytic 0-18 labeling for comparative proteomics: Model studies with two serotypes of adenovirus
    • Yao XD, Freas A, Ramirez J, Demirev PA and Fenselau C: Proteolytic 0-18 labeling for comparative proteomics: Model studies with two serotypes of adenovirus. Anal Chem 73: 2836-2842, 2001.
    • (2001) Anal Chem , vol.73 , pp. 2836-2842
    • Yao, X.D.1    Freas, A.2    Ramirez, J.3    Demirev, P.A.4    Fenselau, C.5
  • 12
    • 4444228797 scopus 로고    scopus 로고
    • Proteomic analysis of ductal carcinoma of the breast using laser capture microdissection, LC-MS, and 0-16/0-18 isotopic labeling
    • Zang L, Toy DP, Hancock WS, Sgroi DC and Karger BL: Proteomic analysis of ductal carcinoma of the breast using laser capture microdissection, LC-MS, and 0-16/0-18 isotopic labeling. J Proteome Res 3: 604-612, 2004.
    • (2004) J Proteome Res , vol.3 , pp. 604-612
    • Zang, L.1    Toy, D.P.2    Hancock, W.S.3    Sgroi, D.C.4    Karger, B.L.5
  • 13
    • 0037417791 scopus 로고    scopus 로고
    • Quantitation of changes in protein phosphorylation: A simple method based on stable isotope labeling and mass spectrometry
    • Bonenfant D, Schmelzle T, Jacinto E, Crespo JL, Mini T, Hall MN and Jenoe P: Quantitation of changes in protein phosphorylation: A simple method based on stable isotope labeling and mass spectrometry. Proc Natl Acad Sci USA 100: 880-885, 2003.
    • (2003) Proc Natl Acad Sci USA , vol.100 , pp. 880-885
    • Bonenfant, D.1    Schmelzle, T.2    Jacinto, E.3    Crespo, J.L.4    Mini, T.5    Hall, M.N.6    Jenoe, P.7
  • 14
    • 0026698693 scopus 로고
    • A method for determination of N-glycosylation sites in glycoproteins by collision-induced dissociation analysis in fast-atom- bombardment mass-spectrometry - identification of the positions of carbohydrate-linked asparagine in recombinant alpha-amylase by treatment with peptide-N-glycosidase-F in O-18-labeled water
    • Gonzalez J, Takao T, Hori H, Besada V, Rodriguez R, Padron G and Shimonishi Y: A method for determination of N-glycosylation sites in glycoproteins by collision-induced dissociation analysis in fast-atom- bombardment mass-spectrometry - identification of the positions of carbohydrate-linked asparagine in recombinant alpha-amylase by treatment with peptide-N-glycosidase-F in O-18-labeled water. Anal Biochem 205: 151-158, 1992.
    • (1992) Anal Biochem , vol.205 , pp. 151-158
    • Gonzalez, J.1    Takao, T.2    Hori, H.3    Besada, V.4    Rodriguez, R.5    Padron, G.6    Shimonishi, Y.7
  • 15
    • 0033106490 scopus 로고    scopus 로고
    • O-18-Labeling of N-glycosylation sites to improve the identification of gel-separated glycoproteins using peptide mass mapping and database searching
    • Kuster B and Mann M: O-18-Labeling of N-glycosylation sites to improve the identification of gel-separated glycoproteins using peptide mass mapping and database searching. Anal Chem 71: 1431-1440, 1999.
    • (1999) Anal Chem , vol.71 , pp. 1431-1440
    • Kuster, B.1    Mann, M.2
  • 16
    • 0036391333 scopus 로고    scopus 로고
    • Proteolytic 0-18 labeling for comparative proteomics: Evaluation of endoprotease Glu-C as the catalytic agent
    • Reynolds KJ, Yao XD and Fenselau C: Proteolytic 0-18 labeling for comparative proteomics: Evaluation of endoprotease Glu-C as the catalytic agent. J Proteome Res 1: 27-33, 2002.
    • (2002) J Proteome Res , vol.1 , pp. 27-33
    • Reynolds, K.J.1    Yao, X.D.2    Fenselau, C.3
  • 17
    • 0028172521 scopus 로고
    • Incorporation of 2 O-18 atoms into a peptide during isoaspartyl repair reveals repeated passage through a succinimide intermediate
    • Lindquist JA and McFadden PN: Incorporation of 2 O-18 atoms into a peptide during isoaspartyl repair reveals repeated passage through a succinimide intermediate. J Protein Chem 13: 553-560, 1994.
    • (1994) J Protein Chem , vol.13 , pp. 553-560
    • Lindquist, J.A.1    McFadden, P.N.2
  • 18
    • 0029840382 scopus 로고    scopus 로고
    • Characterization of a beta-Asp33 isoform of recombinant hirudin sequence variant 1 by low-energy collision-induced dissociation
    • Schindler P, Muller D, Marki W, Grossenbacher H and Richter WJ: Characterization of a beta-Asp33 isoform of recombinant hirudin sequence variant 1 by low-energy collision-induced dissociation. J Mass Spectrom 31: 967-974, 1996.
    • (1996) J Mass Spectrom , vol.31 , pp. 967-974
    • Schindler, P.1    Muller, D.2    Marki, W.3    Grossenbacher, H.4    Richter, W.J.5
  • 19
    • 34247108057 scopus 로고    scopus 로고
    • 0-18 labeling method for identification and quantification of succinimide in proteins
    • Xiao G, Bondarenko PV, Jacob J, Chu GC and Chelius D: 0-18 labeling method for identification and quantification of succinimide in proteins. Anal Chem 79: 2714-2721, 2007.
    • (2007) Anal Chem , vol.79 , pp. 2714-2721
    • Xiao, G.1    Bondarenko, P.V.2    Jacob, J.3    Chu, G.C.4    Chelius, D.5
  • 20
    • 43549104450 scopus 로고    scopus 로고
    • Use of 0-18 labels to monitor deamidation during protein and peptide sample processing
    • Li XJ, Cournoyer JJ, Lin C and O'Cormora PB: Use of 0-18 labels to monitor deamidation during protein and peptide sample processing. J Am Soc Mass Spectrom 19: 855-864, 2008.
    • (2008) J Am Soc Mass Spectrom , vol.19 , pp. 855-864
    • Li, X.J.1    Cournoyer, J.J.2    Lin, C.3    O'Cormora, P.B.4
  • 21
    • 33846105280 scopus 로고    scopus 로고
    • Proteolytic O-18-labeling strategies for quantitative proteomics
    • Miyagi M and Rao KCS: Proteolytic O-18-labeling strategies for quantitative proteomics. Mass Spectrom Rev 26: 121-136, 2007.
    • (2007) Mass Spectrom Rev , vol.26 , pp. 121-136
    • Miyagi, M.1    Rao, K.C.S.2
  • 24
    • 34447570967 scopus 로고    scopus 로고
    • A review of quantitative methods for proteomic studies
    • Fenselau C: A review of quantitative methods for proteomic studies. J Chrom B Anal Tech Biomed Life Sci 855: 14-20, 2007.
    • (2007) J Chrom B Anal Tech Biomed Life Sci , vol.855 , pp. 14-20
    • Fenselau, C.1
  • 25
    • 20444508181 scopus 로고    scopus 로고
    • Mass spectrometry-based quantitative proteomics
    • Heck AJR and Krijgsveld J: Mass spectrometry-based quantitative proteomics. Exp Rev Proteomics 1: 317-326, 2004.
    • (2004) Exp Rev Proteomics , vol.1 , pp. 317-326
    • Heck, A.J.R.1    Krijgsveld, J.2
  • 26
    • 33845329203 scopus 로고    scopus 로고
    • Functional and quantitative proteomics using SILAC
    • Mann M: Functional and quantitative proteomics using SILAC. Nat Rev Mol Cell Biol 7: 952-958, 2006.
    • (2006) Nat Rev Mol Cell Biol , vol.7 , pp. 952-958
    • Mann, M.1
  • 27
    • 33845899942 scopus 로고    scopus 로고
    • Proteomic applications of protein quantification by isotope-dilution mass spectrometry
    • Mayya V and Han DK: Proteomic applications of protein quantification by isotope-dilution mass spectrometry. Exp Rev Proteomics 3: 597-610, 2006.
    • (2006) Exp Rev Proteomics , vol.3 , pp. 597-610
    • Mayya, V.1    Han, D.K.2
  • 28
    • 51649130184 scopus 로고    scopus 로고
    • O-18 Labeling over a coffee break: A rapid strategy for quantitative proteomics
    • Mirza SP, Greene AS and Olivier M: O-18 Labeling over a coffee break: A rapid strategy for quantitative proteomics. J Proteome Res 7: 3042-3048, 2008.
    • (2008) J Proteome Res , vol.7 , pp. 3042-3048
    • Mirza, S.P.1    Greene, A.S.2    Olivier, M.3
  • 29
    • 44149116180 scopus 로고    scopus 로고
    • Ultrasonic energy as a new tool for fast isotopic O-18 labeling of proteins for mass spectrometry-based techniques: Preliminary results
    • Carreira RJ, Rial-Otero R, Lopez-Ferrer D, Lodeiro C and Capelo JL: Ultrasonic energy as a new tool for fast isotopic O-18 labeling of proteins for mass spectrometry-based techniques: Preliminary results. Talanta 76: 400-406, 2008.
    • (2008) Talanta , vol.76 , pp. 400-406
    • Carreira, R.J.1    Rial-Otero, R.2    Lopez-Ferrer, D.3    Lodeiro, C.4    Capelo, J.L.5
  • 30
    • 27644463394 scopus 로고    scopus 로고
    • Peptidyl-Lys metalloendopeptidase-catalyzed O-18 labeling for comparative proteomics-Application to cytokine/lipolysaccharide-treated human retinal pigment epithelium cell line
    • Rao KCS, Palamalai V, Dunlevy JR and Miyagi M: Peptidyl-Lys metalloendopeptidase-catalyzed O-18 labeling for comparative proteomics-Application to cytokine/lipolysaccharide-treated human retinal pigment epithelium cell line. Mol Cell Proteomics 4: 1550-1557, 2005.
    • (2005) Mol Cell Proteomics , vol.4 , pp. 1550-1557
    • Rao, K.C.S.1    Palamalai, V.2    Dunlevy, J.R.3    Miyagi, M.4
  • 31
    • 33745844853 scopus 로고    scopus 로고
    • pH dependency of the carboxyl oxygen exchange reaction catalyzed by lysyl endopeptidase and trypsin
    • Hajkova D, Rao KCS and Miyagi M: pH dependency of the carboxyl oxygen exchange reaction catalyzed by lysyl endopeptidase and trypsin. J Proteome Res 5: 1667-1673, 2006.
    • (2006) J Proteome Res , vol.5 , pp. 1667-1673
    • Hajkova, D.1    Rao, K.C.S.2    Miyagi, M.3
  • 33
    • 33750616893 scopus 로고    scopus 로고
    • Trypsin is the primary mechanism by which the O-18 isotopic label is lost in quantitative proteomic studies
    • Angel PM and Orlando R: Trypsin is the primary mechanism by which the O-18 isotopic label is lost in quantitative proteomic studies. Anal Biochem 359: 26-34, 2006.
    • (2006) Anal Biochem , vol.359 , pp. 26-34
    • Angel, P.M.1    Orlando, R.2
  • 34
    • 33845309673 scopus 로고    scopus 로고
    • Considerations for proteolytic labeling-optimization of O-18 incorporation and prohibition of back-exchange
    • Storms HF, van der Heijden R, Tjaden UR and van der Greef J: Considerations for proteolytic labeling-optimization of O-18 incorporation and prohibition of back-exchange. Rapid Commun Mass Spectrom 20: 3491-3497, 2006.
    • (2006) Rapid Commun Mass Spectrom , vol.20 , pp. 3491-3497
    • Storms, H.F.1    van der Heijden, R.2    Tjaden, U.R.3    van der Greef, J.4
  • 35
    • 33847651332 scopus 로고    scopus 로고
    • Minimizing back exchange in O-18/O-16 quantitative proteomics experiments by incorporation of immobilized trypsin into the initial digestion step
    • Sevinsky JR, Brown KJ, Cargile BJ, Bundy JL and Stephenson JL: Minimizing back exchange in O-18/O-16 quantitative proteomics experiments by incorporation of immobilized trypsin into the initial digestion step. Anal Chem 79: 2158-2162, 2007.
    • (2007) Anal Chem , vol.79 , pp. 2158-2162
    • Sevinsky, J.R.1    Brown, K.J.2    Cargile, B.J.3    Bundy, J.L.4    Stephenson, J.L.5
  • 36
    • 1642462855 scopus 로고    scopus 로고
    • A method for calculating O-16/O-18 peptide ion ratios for the relative quantification of proteomes
    • Johnson KL and Muddiman DC: A method for calculating O-16/O-18 peptide ion ratios for the relative quantification of proteomes. J Am Soc Mass Spectrom 15: 437-445, 2004.
    • (2004) J Am Soc Mass Spectrom , vol.15 , pp. 437-445
    • Johnson, K.L.1    Muddiman, D.C.2
  • 37
    • 19444367322 scopus 로고    scopus 로고
    • Simultaneous quantification and identification using O-18 labeling with an ion trap mass spectrometer and the analysis software application "ZoomQuant
    • Hicks WA, Halligan BD, Slyper RY, Twigger SN, Greene AS and Olivier M: Simultaneous quantification and identification using O-18 labeling with an ion trap mass spectrometer and the analysis software application "ZoomQuant". J Am Soc Mass Spectrom 16: 916-925, 2005.
    • (2005) J Am Soc Mass Spectrom , vol.16 , pp. 916-925
    • Hicks, W.A.1    Halligan, B.D.2    Slyper, R.Y.3    Twigger, S.N.4    Greene, A.S.5    Olivier, M.6
  • 39
    • 33644669753 scopus 로고    scopus 로고
    • Automated comparative proteomics based on multiplex tandem mass spectrometry and stable isotope labeling
    • Zhang GA and Neubert TA: Automated comparative proteomics based on multiplex tandem mass spectrometry and stable isotope labeling. Mol Cell Proteomics 5: 401-411, 2006.
    • (2006) Mol Cell Proteomics , vol.5 , pp. 401-411
    • Zhang, G.A.1    Neubert, T.A.2
  • 40
    • 60849090764 scopus 로고    scopus 로고
    • Citrate boosts the performance of phosphopeptide analysis by UPLC-ESI-MS/MS
    • Winter D, Seidler J, Ziv Y, Shiloh Y and Lehmann WD: Citrate boosts the performance of phosphopeptide analysis by UPLC-ESI-MS/MS. J Proteome Res 8: 418-424, 2009.
    • (2009) J Proteome Res , vol.8 , pp. 418-424
    • Winter, D.1    Seidler, J.2    Ziv, Y.3    Shiloh, Y.4    Lehmann, W.D.5
  • 43
    • 41649084998 scopus 로고    scopus 로고
    • Evaluation of HSP70 expression and DNA damage in cells of a human trophoblast cell line exposed to 1.8 GHz amplitude-modulated radiofrequency fields
    • Valbonesi P, Franzellitti S, Piano A, Contin A, Biondi C and Fabbri E: Evaluation of HSP70 expression and DNA damage in cells of a human trophoblast cell line exposed to 1.8 GHz amplitude-modulated radiofrequency fields. Radiation Res 169: 270-279, 2008.
    • (2008) Radiation Res , vol.169 , pp. 270-279
    • Valbonesi, P.1    Franzellitti, S.2    Piano, A.3    Contin, A.4    Biondi, C.5    Fabbri, E.6
  • 45
    • 44349165873 scopus 로고    scopus 로고
    • Spatial and temporal coordination of mitosis by Ran GTPase
    • Clarke PR and Zhang CM: Spatial and temporal coordination of mitosis by Ran GTPase. Nat Rev Mol Cell Biol 9: 464-477, 2008.
    • (2008) Nat Rev Mol Cell Biol , vol.9 , pp. 464-477
    • Clarke, P.R.1    Zhang, C.M.2
  • 46
    • 44949085340 scopus 로고    scopus 로고
    • The role of the DNA damage response in neuronal development, organization and maintenance
    • Barzilai A, Biton S and Shiloh Y: The role of the DNA damage response in neuronal development, organization and maintenance. DNA Repair 7: 1010-1027, 2008.
    • (2008) DNA Repair , vol.7 , pp. 1010-1027
    • Barzilai, A.1    Biton, S.2    Shiloh, Y.3
  • 48
    • 0033451741 scopus 로고    scopus 로고
    • Protein consensus sequence motifs
    • Aitken A: Protein consensus sequence motifs. Mol Biotech 12: 241-253, 1999.
    • (1999) Mol Biotech , vol.12 , pp. 241-253
    • Aitken, A.1
  • 49
    • 70449574788 scopus 로고    scopus 로고
    • Analysis of autophosphorylation sites in the recombinant catalytic subunit alpha of cAMP-dependent kinase by nanoUPLC-ESI-MS/MS
    • Seidler J, Adal M, Kubier D, Bossemeyer D and Lehmann WD: Analysis of autophosphorylation sites in the recombinant catalytic subunit alpha of cAMP-dependent kinase by nanoUPLC-ESI-MS/MS. Anal Bioanal Chem 395: 1713-1720, 2009.
    • (2009) Anal Bioanal Chem , vol.395 , pp. 1713-1720
    • Seidler, J.1    Adal, M.2    Kubier, D.3    Bossemeyer, D.4    Lehmann, W.D.5
  • 50
    • 0348010576 scopus 로고    scopus 로고
    • Cyclin-dependent kinase 5 in neurofilament function and regulation
    • Kesavapany S, Li BS and Pant HC: Cyclin-dependent kinase 5 in neurofilament function and regulation. Neurosignals 12: 252-264, 2003.
    • (2003) Neurosignals , vol.12 , pp. 252-264
    • Kesavapany, S.1    Li, B.S.2    Pant, H.C.3
  • 51
    • 42949127699 scopus 로고    scopus 로고
    • MAP kinase: It's been longer than fifteen minutes
    • Sturgill TW: MAP kinase: It's been longer than fifteen minutes. Biochem Biophys Res Commun 371: 1-4, 2008.
    • (2008) Biochem Biophys Res Commun , vol.371 , pp. 1-4
    • Sturgill, T.W.1
  • 52
    • 0033105821 scopus 로고    scopus 로고
    • Identity between TRAP and SMCC complexes indicates novel pathways for the function of nuclear receptors and diverse mammalian activators
    • Ito M, Yuan CX, Malik S, Gu W, Fondell JD, Yamamura S, Fu ZY, Zhang XL, Qin J and Roeder RG: Identity between TRAP and SMCC complexes indicates novel pathways for the function of nuclear receptors and diverse mammalian activators. Mol Cell 3: 361-370, 1999.
    • (1999) Mol Cell , vol.3 , pp. 361-370
    • Ito, M.1    Yuan, C.X.2    Malik, S.3    Gu, W.4    Fondell, J.D.5    Yamamura, S.6    Fu, Z.Y.7    Zhang, X.L.8    Qin, J.9    Roeder, R.G.10
  • 54
    • 0028803974 scopus 로고
    • The myristoylated alanine-rich C-kinase substrate (Marcks) is sequentially phosphorylated by conventional, novel and atypical isotypes of protein-kinase-C
    • Herget T, Oehrlein SA, Pappin DJC, Rozengurt E and Parker PJ: The myristoylated alanine-rich C-kinase substrate (Marcks) is sequentially phosphorylated by conventional, novel and atypical isotypes of protein-kinase-C. Eur Journal Biochem 233: 448-457, 1995.
    • (1995) Eur Journal Biochem , vol.233 , pp. 448-457
    • Herget, T.1    Oehrlein, S.A.2    Pappin, D.J.C.3    Rozengurt, E.4    Parker, P.J.5
  • 56
    • 0032167733 scopus 로고    scopus 로고
    • The R3H motif: A domain that binds single-stranded nucleic acids
    • Grishin NV: The R3H motif: A domain that binds single-stranded nucleic acids. Trends Biochem Sci 23: 329-330, 1998.
    • (1998) Trends Biochem Sci , vol.23 , pp. 329-330
    • Grishin, N.V.1
  • 57
    • 0028465425 scopus 로고
    • Beta-thymosins as actin-binding peptides
    • Safer D and Nachmias VT: Beta-thymosins as actin-binding peptides. Bioessays 16: 473-479, 1994.
    • (1994) Bioessays , vol.16 , pp. 473-479
    • Safer, D.1    Nachmias, V.T.2
  • 59
    • 33750120717 scopus 로고    scopus 로고
    • The MAPI family of microtubule-associated proteins
    • Halpain S and Dehmelt L: The MAPI family of microtubule-associated proteins. Genome Biol 7: 224-, 2006.
    • (2006) Genome Biol , vol.7 , pp. 224
    • Halpain, S.1    Dehmelt, L.2
  • 60
    • 33847164931 scopus 로고    scopus 로고
    • Two hydrophobic segments of the RTN1 family determine the ER localization and retention
    • Iwahashi J, Hamada N and Watanabe H: Two hydrophobic segments of the RTN1 family determine the ER localization and retention. Biochem Biophys Res Commun 355: 508-512, 2007.
    • (2007) Biochem Biophys Res Commun , vol.355 , pp. 508-512
    • Iwahashi, J.1    Hamada, N.2    Watanabe, H.3
  • 62
    • 0032523819 scopus 로고    scopus 로고
    • The Ulip family phosphoproteins-Common and specific properties
    • Byk T, Ozon S and Sobel A: The Ulip family phosphoproteins-Common and specific properties. Eur J Biochem 254: 14-24, 1998.
    • (1998) Eur J Biochem , vol.254 , pp. 14-24
    • Byk, T.1    Ozon, S.2    Sobel, A.3
  • 63
    • 0037166943 scopus 로고    scopus 로고
    • MAP2 and tau bind longitudinally along the outer ridges of microtubule protofilaments
    • Al-Bassam J, Ozer RS, Safer D, Halpain S and Milligan RA: MAP2 and tau bind longitudinally along the outer ridges of microtubule protofilaments. J Cell Biol 157: 1187-1196, 2002.
    • (2002) J Cell Biol , vol.157 , pp. 1187-1196
    • Al-Bassam, J.1    Ozer, R.S.2    Safer, D.3    Halpain, S.4    Milligan, R.A.5
  • 65
    • 0026686927 scopus 로고
    • Macmarcks, a novel member of the marcks family of protein-kinase-C substrates
    • Li JX and Aderem A: Macmarcks, a novel member of the marcks family of protein-kinase-C substrates. Cell 70: 791-801, 1992.
    • (1992) Cell , vol.70 , pp. 791-801
    • Li, J.X.1    Aderem, A.2
  • 68
    • 33750456519 scopus 로고    scopus 로고
    • Global, in vivo, and site-specific phosphorylation dynamics in signaling networks
    • Olsen JV, Blagoev B, Gnad F, Macek B, Kumar C, Mortensen P and Mann M: Global, in vivo, and site-specific phosphorylation dynamics in signaling networks. Cell 127: 635-648, 2006.
    • (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
  • 69
    • 0033602360 scopus 로고    scopus 로고
    • Graham SM, Oldham SM, Martin CB, Drugan JK, Zohn IE, Campbell S and Der CJ: TC21 and Ras share indistinguishable transforming and differentiating activities. Oncogene 18: 2107-2116, 1999.
    • Graham SM, Oldham SM, Martin CB, Drugan JK, Zohn IE, Campbell S and Der CJ: TC21 and Ras share indistinguishable transforming and differentiating activities. Oncogene 18: 2107-2116, 1999.
  • 70
    • 46849106085 scopus 로고    scopus 로고
    • Relations between the mitogen-activated protein kinase and the cAMP-dependent protein kinase pathways: Comradeship and hostility
    • Gerits N, Kostenko S, Shiryaev A, Johannessen M and Moens U: Relations between the mitogen-activated protein kinase and the cAMP-dependent protein kinase pathways: Comradeship and hostility. Cell Signalling 20: 1592-1607, 2008.
    • (2008) Cell Signalling , vol.20 , pp. 1592-1607
    • Gerits, N.1    Kostenko, S.2    Shiryaev, A.3    Johannessen, M.4    Moens, U.5
  • 71
    • 33846600408 scopus 로고    scopus 로고
    • Regulation of cyclin-dependent kinase 5 and p53 by ERK1/2 pathway in the DNA damage-induced neuronal death
    • Lee JH and Kim KT: Regulation of cyclin-dependent kinase 5 and p53 by ERK1/2 pathway in the DNA damage-induced neuronal death. J Cell Physiol 210: 784-797, 2007.
    • (2007) J Cell Physiol , vol.210 , pp. 784-797
    • Lee, J.H.1    Kim, K.T.2
  • 72
    • 45349096573 scopus 로고    scopus 로고
    • Thymosin beta 4 is overexpressed in human pancreatic cancer cells and stimulates proinflammatory cytokine secretion and JNK activation
    • Zhang YQ, Feurino LW, Zhai QH, Wang H, Fisher WE, Chen CY, Yao QZ and Li M: Thymosin beta 4 is overexpressed in human pancreatic cancer cells and stimulates proinflammatory cytokine secretion and JNK activation. Cancer Biol Therapy 7: 419-423, 2008.
    • (2008) Cancer Biol Therapy , vol.7 , pp. 419-423
    • Zhang, Y.Q.1    Feurino, L.W.2    Zhai, Q.H.3    Wang, H.4    Fisher, W.E.5    Chen, C.Y.6    Yao, Q.Z.7    Li, M.8
  • 73
    • 1642420308 scopus 로고    scopus 로고
    • Interleukin-6 induces Alzheimer-type phosphorylation of tau protein by deregulating the cdk5/p35 pathway
    • Quintanilla RA, Orellana DI, Gonzalez-Billault C and Maccioni RB: Interleukin-6 induces Alzheimer-type phosphorylation of tau protein by deregulating the cdk5/p35 pathway. Exper Cell Res 295: 245-257, 2004.
    • (2004) Exper Cell Res , vol.295 , pp. 245-257
    • Quintanilla, R.A.1    Orellana, D.I.2    Gonzalez-Billault, C.3    Maccioni, R.B.4
  • 74
    • 34447130222 scopus 로고    scopus 로고
    • Phosphorylation of Huntingtin by cyclin-dependent kinase 5 is induced by DNA damage and regulates wild-type and mutant Huntingtin toxicity in neurons
    • Anne SL, Saudou F and Humbert S: Phosphorylation of Huntingtin by cyclin-dependent kinase 5 is induced by DNA damage and regulates wild-type and mutant Huntingtin toxicity in neurons. J Neurosci 27: 7318-7328, 2007.
    • (2007) J Neurosci , vol.27 , pp. 7318-7328
    • Anne, S.L.1    Saudou, F.2    Humbert, S.3
  • 75
    • 34447498931 scopus 로고    scopus 로고
    • Stabilization and activation of p53 induced by Cdk5 contributes to neuronal cell death
    • Lee JH, Kim HS, Lee SJ and Kim KT: Stabilization and activation of p53 induced by Cdk5 contributes to neuronal cell death. J Cell Sci 120: 2259-2271, 2007.
    • (2007) J Cell Sci , vol.120 , pp. 2259-2271
    • Lee, J.H.1    Kim, H.S.2    Lee, S.J.3    Kim, K.T.4
  • 76
    • 0036169172 scopus 로고    scopus 로고
    • Cdk5 behind the wheel: A role in trafficking and transport?
    • Smith DS and Tsai LH: Cdk5 behind the wheel: a role in trafficking and transport? Trends Cell Biol 12: 28-36, 2002.
    • (2002) Trends Cell Biol , vol.12 , pp. 28-36
    • Smith, D.S.1    Tsai, L.H.2
  • 77
    • 1642602693 scopus 로고    scopus 로고
    • The DNA damage checkpoint and PKA pathways converge on APC substrates and Cdc20 to regulate mitotic progression
    • Searle JS, Schollaert KL, Wilkins BJ and Sanchez Y: The DNA damage checkpoint and PKA pathways converge on APC substrates and Cdc20 to regulate mitotic progression. Nature Cell Biol 6: 138-145, 2004.
    • (2004) Nature Cell Biol , vol.6 , pp. 138-145
    • Searle, J.S.1    Schollaert, K.L.2    Wilkins, B.J.3    Sanchez, Y.4
  • 78
    • 33750510335 scopus 로고    scopus 로고
    • PKA modulates GSK-3 beta- and cdk5-catalyzed phosphorylation of tau in site- and kinase-specific manners
    • Liu F, Liang ZH, Shi JH, Yin DM, El-Akkad E, Grundke-Iqbal I, Iqbal K and Gong CX: PKA modulates GSK-3 beta- and cdk5-catalyzed phosphorylation of tau in site- and kinase-specific manners. FEBS LET 580: 6269-6274, 2006.
    • (2006) FEBS LET , vol.580 , pp. 6269-6274
    • Liu, F.1    Liang, Z.H.2    Shi, J.H.3    Yin, D.M.4    El-Akkad, E.5    Grundke-Iqbal, I.6    Iqbal, K.7    Gong, C.X.8
  • 79
    • 1642493719 scopus 로고    scopus 로고
    • Doublecortin microtubule affinity is regulated by a balance of kinase and phosphatase activity at the leading edge of migrating neurons
    • Schaar BT, Kinoshita K and McConnell SK: Doublecortin microtubule affinity is regulated by a balance of kinase and phosphatase activity at the leading edge of migrating neurons. Neuron 41: 203-213, 2004.
    • (2004) Neuron , vol.41 , pp. 203-213
    • Schaar, B.T.1    Kinoshita, K.2    McConnell, S.K.3
  • 80
    • 1642452714 scopus 로고    scopus 로고
    • Cdk5 phosphorylation of Doublecortin Ser297 regulates its effect on neuronal migration
    • Tanaka T, Semeo FF, Tseng H-C, Kulkarni AB, Tsai L-H and Gleeson JG: Cdk5 phosphorylation of Doublecortin Ser297 regulates its effect on neuronal migration. Neuron 41: 215-227, 2004.
    • (2004) Neuron , vol.41 , pp. 215-227
    • Tanaka, T.1    Semeo, F.F.2    Tseng, H.-C.3    Kulkarni, A.B.4    Tsai, L.-H.5    Gleeson, J.G.6
  • 82
    • 49749110451 scopus 로고    scopus 로고
    • Protein kinase CK2 as a draggable target
    • Sarno S and Pinna LA: Protein kinase CK2 as a draggable target. Mol Biosys 4: 889-894, 2008.
    • (2008) Mol Biosys , vol.4 , pp. 889-894
    • Sarno, S.1    Pinna, L.A.2
  • 85
    • 49649089537 scopus 로고    scopus 로고
    • MDCl regulates intra-S-phase checkpoint by targeting NBS1 to DNA double-strand breaks
    • Wu LM, Luo KT, Lou ZK and Chen JJ: MDCl regulates intra-S-phase checkpoint by targeting NBS1 to DNA double-strand breaks. Proc Natl Acad Sci USA 105: 11200-11205, 2008.
    • (2008) Proc Natl Acad Sci USA , vol.105 , pp. 11200-11205
    • Wu, L.M.1    Luo, K.T.2    Lou, Z.K.3    Chen, J.J.4
  • 86
    • 53349118235 scopus 로고    scopus 로고
    • Cellular commitment to reentry into the cell cycle after stalled DNA is determined by site-specific phosphorylation of Chk1 and PTEN
    • Martin SA and Ouchi T: Cellular commitment to reentry into the cell cycle after stalled DNA is determined by site-specific phosphorylation of Chk1 and PTEN. Mol Cancer Therapeutics 7: 2509-2516, 2008.
    • (2008) Mol Cancer Therapeutics , vol.7 , pp. 2509-2516
    • Martin, S.A.1    Ouchi, T.2
  • 87
    • 33644970939 scopus 로고    scopus 로고
    • Protein kinase B/Akt is a novel cysteine string protein kinase that regulates exocytosis release kinetics and quantal size
    • Evans GJ, Barclay JW, Prescott GR, Jo SR, Burgoyne RD, Birnbaum MJ and Morgan A: Protein kinase B/Akt is a novel cysteine string protein kinase that regulates exocytosis release kinetics and quantal size. J Biol Chem 281: 1564-1572, 2006.
    • (2006) J Biol Chem , vol.281 , pp. 1564-1572
    • Evans, G.J.1    Barclay, J.W.2    Prescott, G.R.3    Jo, S.R.4    Burgoyne, R.D.5    Birnbaum, M.J.6    Morgan, A.7
  • 89
    • 45549104364 scopus 로고    scopus 로고
    • P53 stabilization in response to DNA damage requires Akt/PKB and DNA-PK
    • Boehme KA, Kulikov R and Blattner C: P53 stabilization in response to DNA damage requires Akt/PKB and DNA-PK. Proc Natl Acad Sci USA 105: 7785-7790, 2008.
    • (2008) Proc Natl Acad Sci USA , vol.105 , pp. 7785-7790
    • Boehme, K.A.1    Kulikov, R.2    Blattner, C.3


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.