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Volumn 457, Issue B, 2009, Pages 81-96

Chapter 5 Selective Enrichment in Phosphopeptides for the Identification of Phosphorylated Mitochondrial Proteins

Author keywords

[No Author keywords available]

Indexed keywords

MITOCHONDRIAL PROTEIN; PHOSPHATASE; PHOSPHATE; PHOSPHOPEPTIDE; PHOSPHOPROTEIN; PHOSPHOSERINE; PHOSPHOTHREONINE; PHOSPHOTYROSINE; PROTEIN KINASE; SERINE; THREONINE; TYROSINE;

EID: 65449139503     PISSN: 00766879     EISSN: None     Source Type: Book Series    
DOI: 10.1016/S0076-6879(09)05005-8     Document Type: Review
Times cited : (4)

References (41)
  • 3
    • 32544451945 scopus 로고    scopus 로고
    • MiGenes: A searchable interspecies database of mitochondrial proteins curated using gene ontology annotation
    • Basu S., Bremer E., Zhou C., and Bogenhagen D.F. MiGenes: A searchable interspecies database of mitochondrial proteins curated using gene ontology annotation. Bioinformatics 22 (2006) 485-492
    • (2006) Bioinformatics , vol.22 , pp. 485-492
    • Basu, S.1    Bremer, E.2    Zhou, C.3    Bogenhagen, D.F.4
  • 5
    • 0345863901 scopus 로고    scopus 로고
    • MitoProteome: Mitochondrial protein sequence database and annotation system
    • Cotter D., Guda P., Fahy E., and Subramaniam S. MitoProteome: Mitochondrial protein sequence database and annotation system. Nucleic Acids Res. 32 (2004) D463-D467
    • (2004) Nucleic Acids Res. , vol.32
    • Cotter, D.1    Guda, P.2    Fahy, E.3    Subramaniam, S.4
  • 6
    • 34547869591 scopus 로고    scopus 로고
    • Identification of phosphoproteins and determination of phosphorylation sites by zirconium dioxide enrichment and SELDI-MS/MS
    • Cuccurullo M., Schlosser G., Cacace G., Malorni L., and Pocsfalvi G. Identification of phosphoproteins and determination of phosphorylation sites by zirconium dioxide enrichment and SELDI-MS/MS. J. Mass Spectrom. 42 (2007) 1069-1078
    • (2007) J. Mass Spectrom. , vol.42 , pp. 1069-1078
    • Cuccurullo, M.1    Schlosser, G.2    Cacace, G.3    Malorni, L.4    Pocsfalvi, G.5
  • 7
    • 34247634168 scopus 로고    scopus 로고
    • Post-translational modifications of rat liver mitochondrial outer membrane proteins identified by mass spectrometry
    • Distler A.M., Kerner J., and Hoppel C.L. Post-translational modifications of rat liver mitochondrial outer membrane proteins identified by mass spectrometry. Biochim. Biophys. Acta (BBA) Proteins Proteomics 1774 (2007) 628-636
    • (2007) Biochim. Biophys. Acta (BBA) Proteins Proteomics , vol.1774 , pp. 628-636
    • Distler, A.M.1    Kerner, J.2    Hoppel, C.L.3
  • 9
    • 34848886063 scopus 로고    scopus 로고
    • Immobilized zirconium ion affinity chromatography for specific enrichment of phosphopeptides in phosphoproteome analysis
    • Feng S., Ye M., Zhou H., Jiang X., Jiang X., Zou H., and Gong B. Immobilized zirconium ion affinity chromatography for specific enrichment of phosphopeptides in phosphoproteome analysis. Mol. Cell Proteomics 6 (2007) 1656-1665
    • (2007) Mol. Cell Proteomics , vol.6 , pp. 1656-1665
    • Feng, S.1    Ye, M.2    Zhou, H.3    Jiang, X.4    Jiang, X.5    Zou, H.6    Gong, B.7
  • 10
    • 45249106836 scopus 로고    scopus 로고
    • Niobium(V) Oxide (Nb2O5): Application to phosphoproteomics
    • Ficarro S.B., Parikh J.R., Blank N.C., and Marto J.A. Niobium(V) Oxide (Nb2O5): Application to phosphoproteomics. Anal. Chem. 80 (2008) 4606-4613
    • (2008) Anal. Chem. , vol.80 , pp. 4606-4613
    • Ficarro, S.B.1    Parikh, J.R.2    Blank, N.C.3    Marto, J.A.4
  • 11
    • 33745937467 scopus 로고    scopus 로고
    • Differential mitochondrial protein expression profiling in neurodegenerative diseases
    • Frank G. Differential mitochondrial protein expression profiling in neurodegenerative diseases. Electrophoresis 27 (2006) 2814-2818
    • (2006) Electrophoresis , vol.27 , pp. 2814-2818
    • Frank, G.1
  • 12
    • 34249055571 scopus 로고    scopus 로고
    • Soluble nanopolymer-based phosphoproteomics for studying protein phosphatase
    • Guo M., Galan J., and Tao W.A. Soluble nanopolymer-based phosphoproteomics for studying protein phosphatase. Methods 42 (2007) 289-297
    • (2007) Methods , vol.42 , pp. 289-297
    • Guo, M.1    Galan, J.2    Tao, W.A.3
  • 13
    • 13444266365 scopus 로고    scopus 로고
    • AMPDB: The arabidopsis mitochondrial protein database
    • Heazlewood J.L., and Millar A.H. AMPDB: The arabidopsis mitochondrial protein database. Nucleic Acids Res. 33 (2005) D605-D610
    • (2005) Nucleic Acids Res. , vol.33
    • Heazlewood, J.L.1    Millar, A.H.2
  • 15
    • 0037199628 scopus 로고    scopus 로고
    • Mixed-mode reversed-phase and ion-exchange separations of cationic analytes on polybutadiene-coated zirconia
    • Hu Y., A Yang X., and A Carr P.W. Mixed-mode reversed-phase and ion-exchange separations of cationic analytes on polybutadiene-coated zirconia. J. Chromatogr. A 968 (2002) 17-29
    • (2002) J. Chromatogr. A , vol.968 , pp. 17-29
    • Hu, Y.1    A Yang, X.2    A Carr, P.W.3
  • 17
    • 42949170563 scopus 로고    scopus 로고
    • Automated phosphoproteome analysis for cultured cancer cells by two-dimensional NanoLC-MS using a calcined titania/C18 biphasic column
    • Imami K., Sugiyama N., Kyono Y., Tomita M., and Ishihama Y. Automated phosphoproteome analysis for cultured cancer cells by two-dimensional NanoLC-MS using a calcined titania/C18 biphasic column. Anal. Sci. 24 (2008) 161-166
    • (2008) Anal. Sci. , vol.24 , pp. 161-166
    • Imami, K.1    Sugiyama, N.2    Kyono, Y.3    Tomita, M.4    Ishihama, Y.5
  • 19
    • 33645217942 scopus 로고    scopus 로고
    • Selective zirconium dioxide-based enrichment of phosphorylated peptides for mass spectrometric analysis
    • Kweon H.K., and Hakansson K. Selective zirconium dioxide-based enrichment of phosphorylated peptides for mass spectrometric analysis. Anal. Chem. 78 (2006) 1743-1749
    • (2006) Anal. Chem. , vol.78 , pp. 1743-1749
    • Kweon, H.K.1    Hakansson, K.2
  • 21
    • 34247383227 scopus 로고    scopus 로고
    • Mitochondrial phosphoproteome revealed by an improved IMAC method and MS/MS/MS
    • Lee J., Xu Y., Chen Y., Sprung R., Kim S.C., Xie S., and Zhao Y. Mitochondrial phosphoproteome revealed by an improved IMAC method and MS/MS/MS. Mol. Cell. Proteomics 6 (2007) 669-676
    • (2007) Mol. Cell. Proteomics , vol.6 , pp. 669-676
    • Lee, J.1    Xu, Y.2    Chen, Y.3    Sprung, R.4    Kim, S.C.5    Xie, S.6    Zhao, Y.7
  • 22
    • 49849086333 scopus 로고    scopus 로고
    • Novel Fe3O4@TiO2 core-shell microspheres for selective enrichment of phosphopeptides in phosphoproteome analysis
    • Li Y., Xu X., Qi D., Deng C., Yang P., and Zhang X. Novel Fe3O4@TiO2 core-shell microspheres for selective enrichment of phosphopeptides in phosphoproteome analysis. J. Proteome Res. 7 (2008) 2526-2538
    • (2008) J. Proteome Res. , vol.7 , pp. 2526-2538
    • Li, Y.1    Xu, X.2    Qi, D.3    Deng, C.4    Yang, P.5    Zhang, X.6
  • 23
    • 52649175447 scopus 로고    scopus 로고
    • Comparative studies of early liver dysfunction in senescence-accelerated mouse using mitochondrial proteomics approaches
    • Liu Y., He J., Ji S., Wang Q., Pu H., Jiang T., Meng L., Yang X., and Ji J. Comparative studies of early liver dysfunction in senescence-accelerated mouse using mitochondrial proteomics approaches. Mol. Cell. Proteomics 7 (2008) 1737-1747
    • (2008) Mol. Cell. Proteomics , vol.7 , pp. 1737-1747
    • Liu, Y.1    He, J.2    Ji, S.3    Wang, Q.4    Pu, H.5    Jiang, T.6    Meng, L.7    Yang, X.8    Ji, J.9
  • 24
    • 46149095496 scopus 로고    scopus 로고
    • The mitochondrial proteome: From inventory to function
    • Meisinger C., Sickmann A., and Pfanner N. The mitochondrial proteome: From inventory to function. Cell 134 (2008) 22-24
    • (2008) Cell , vol.134 , pp. 22-24
    • Meisinger, C.1    Sickmann, A.2    Pfanner, N.3
  • 25
    • 46749084662 scopus 로고    scopus 로고
    • Mitochondria: A mirror into cellular dysfunction in heart disease
    • Melanie Y.W. Mitochondria: A mirror into cellular dysfunction in heart disease. Proteomics: Clin. Appl. 2 (2008) 845-861
    • (2008) Proteomics: Clin. Appl. , vol.2 , pp. 845-861
    • Melanie, Y.W.1
  • 26
    • 38649090322 scopus 로고    scopus 로고
    • Identification of phosphorylation sites in mammalian mitochondrial ribosomal protein DAP3
    • Miller J.L., Koc H., and Koc E.C. Identification of phosphorylation sites in mammalian mitochondrial ribosomal protein DAP3. Protein Sci. 17 (2008) 251-260
    • (2008) Protein Sci. , vol.17 , pp. 251-260
    • Miller, J.L.1    Koc, H.2    Koc, E.C.3
  • 28
    • 30944449043 scopus 로고    scopus 로고
    • Mitochondrial modulation: Reversible phosphorylation takes center stage?
    • Pagliarini D.J., and Dixon J.E. Mitochondrial modulation: Reversible phosphorylation takes center stage?. Trends Biochem. Sci. 31 (2006) 26-34
    • (2006) Trends Biochem. Sci. , vol.31 , pp. 26-34
    • Pagliarini, D.J.1    Dixon, J.E.2
  • 29
    • 55849147636 scopus 로고    scopus 로고
    • Quantitative phosphoproteome analysis of a mouse liver cell line reveals specificity of phosphatase inhibitors
    • Pan C., Gnad F., Olsen J.V., and Mann M. Quantitative phosphoproteome analysis of a mouse liver cell line reveals specificity of phosphatase inhibitors. Proteomics 8 (2008) 4534-4546
    • (2008) Proteomics , vol.8 , pp. 4534-4546
    • Pan, C.1    Gnad, F.2    Olsen, J.V.3    Mann, M.4
  • 30
    • 39749186759 scopus 로고    scopus 로고
    • Highly robust, automated, and sensitive online TiO2-based phosphoproteomics applied to study endogenous phosphorylation in Drosophila melanogaster
    • Pinkse M.W.H., Mohammed S., Gouw J.W., van Breukelen B., Vos H.R., and Heck A.J.R. Highly robust, automated, and sensitive online TiO2-based phosphoproteomics applied to study endogenous phosphorylation in Drosophila melanogaster. J. Proteome Res. 7 (2008) 687-697
    • (2008) J. Proteome Res. , vol.7 , pp. 687-697
    • Pinkse, M.W.H.1    Mohammed, S.2    Gouw, J.W.3    van Breukelen, B.4    Vos, H.R.5    Heck, A.J.R.6
  • 31
    • 33847634448 scopus 로고    scopus 로고
    • Phosphorylation of B14.5a subunit from bovine heart complex I identified by titanium dioxide selective enrichment and shotgun proteomics
    • Pocsfalvi G., Cuccurullo M., Schlosser G., Scacco S., Papa S., and Malorni A. Phosphorylation of B14.5a subunit from bovine heart complex I identified by titanium dioxide selective enrichment and shotgun proteomics. Mol. Cell. Proteomics 6 (2007) 231-238
    • (2007) Mol. Cell. Proteomics , vol.6 , pp. 231-238
    • Pocsfalvi, G.1    Cuccurullo, M.2    Schlosser, G.3    Scacco, S.4    Papa, S.5    Malorni, A.6
  • 34
    • 33745889628 scopus 로고    scopus 로고
    • Reversible lysine acetylation controls the activity of the mitochondrial enzyme acetyl-CoA synthetase 2
    • Schwer B., Bunkenborg J., Verdin R.O., Andersen J.S., and Verdin E. Reversible lysine acetylation controls the activity of the mitochondrial enzyme acetyl-CoA synthetase 2. Proc. Nat. Acad. Sci. USA 103 (2006) 10224-10229
    • (2006) Proc. Nat. Acad. Sci. USA , vol.103 , pp. 10224-10229
    • Schwer, B.1    Bunkenborg, J.2    Verdin, R.O.3    Andersen, J.S.4    Verdin, E.5
  • 35
    • 46649090918 scopus 로고    scopus 로고
    • Protein tyrosine nitration-Functional alteration or just a biomarker?
    • Souza J.M., Peluffo G., and Radi R. Protein tyrosine nitration-Functional alteration or just a biomarker?. Free Rad. Biol. Med. 45 (2008) 357-366
    • (2008) Free Rad. Biol. Med. , vol.45 , pp. 357-366
    • Souza, J.M.1    Peluffo, G.2    Radi, R.3
  • 36
    • 50949127353 scopus 로고    scopus 로고
    • Tin dioxide microspheres as a promising material for phosphopeptide enrichment prior to liquid chromatography-(tandem) mass spectrometry analysis
    • Sturm M., Leitner A., Jan-Henrik S., Mika, and Lindner L.W. Tin dioxide microspheres as a promising material for phosphopeptide enrichment prior to liquid chromatography-(tandem) mass spectrometry analysis. Adv. Funct. Mater. 18 (2008) 2381-2389
    • (2008) Adv. Funct. Mater. , vol.18 , pp. 2381-2389
    • Sturm, M.1    Leitner, A.2    Jan-Henrik, S.3    Mika4    Lindner, L.W.5
  • 37
    • 0033883489 scopus 로고    scopus 로고
    • Ubiquitinated sperm mitochondria, selective proteolysis, and the regulation of mitochondrial inheritance in mammalian embryos
    • Sutovsky P., Moreno R.D., Ramalho-Santos J., Dominko T., Simerly C., and Schatten G. Ubiquitinated sperm mitochondria, selective proteolysis, and the regulation of mitochondrial inheritance in mammalian embryos. Biol. Reprod. 63 (2000) 582-590
    • (2000) Biol. Reprod. , vol.63 , pp. 582-590
    • Sutovsky, P.1    Moreno, R.D.2    Ramalho-Santos, J.3    Dominko, T.4    Simerly, C.5    Schatten, G.6
  • 38
    • 0037468612 scopus 로고    scopus 로고
    • C-terminal 15 kDa fragment of cytoskeletal actin is posttranslationally N-myristoylated upon caspase-mediated cleavage and targeted to mitochondria
    • Toshihiko U., Nagisa S., Kengo N., and Rumi I. C-terminal 15 kDa fragment of cytoskeletal actin is posttranslationally N-myristoylated upon caspase-mediated cleavage and targeted to mitochondria. FEBS Lett. 539 (2003) 37-44
    • (2003) FEBS Lett. , vol.539 , pp. 37-44
    • Toshihiko, U.1    Nagisa, S.2    Kengo, N.3    Rumi, I.4
  • 39
    • 40849120423 scopus 로고    scopus 로고
    • Identification of new tyrosine phosphorylated proteins in rat brain mitochondria
    • Urs L., Albert S., Luca C., Anna Maria B., Antonio T., and Mauro S. Identification of new tyrosine phosphorylated proteins in rat brain mitochondria. FEBS Lett. 582 (2008) 1104-1110
    • (2008) FEBS Lett. , vol.582 , pp. 1104-1110
    • Urs, L.1    Albert, S.2    Luca, C.3    Anna Maria, B.4    Antonio, T.5    Mauro, S.6
  • 41
    • 55249104113 scopus 로고    scopus 로고
    • Specific phosphopeptide enrichment with immobilized titanium ion affinity chromatography adsorbent for phosphoproteome analysis
    • Zhou H., Ye M., Dong J., Han G., Jiang X., Wu R., and Zou H. Specific phosphopeptide enrichment with immobilized titanium ion affinity chromatography adsorbent for phosphoproteome analysis. J. Proteome Res. 7 (2008) 3957-3967
    • (2008) J. Proteome Res. , vol.7 , pp. 3957-3967
    • Zhou, H.1    Ye, M.2    Dong, J.3    Han, G.4    Jiang, X.5    Wu, R.6    Zou, H.7


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