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Volumn 23, Issue 4, 2004, Pages 259-280

Identification of protein associations in organelles, using mass spectrometry-based proteomics

Author keywords

Bioinformatics; Organelle; Protein complexes; Protein protein interactions; Proteomics

Indexed keywords

BIOINFORMATICS; ORGANELLE; PROTEIN COMPLEX; PROTEIN-PROTEIN INTERACTION; PROTEOMICS;

EID: 3042687234     PISSN: 02777037     EISSN: None     Source Type: Journal    
DOI: 10.1002/mas.10077     Document Type: Review
Times cited : (40)

References (108)
  • 1
    • 0037072739 scopus 로고    scopus 로고
    • A functionally active human FIFO ATPase can be purified by immunocapture from heart tissue and fibroblast cell lines. Subunit structure and activity studies
    • Aggeler R, Coons J, Taylor SW, Ghosh SS, Garcia JJ, Capaldi RA, Marusich MF 2002. A functionally active human FIFO ATPase can be purified by immunocapture from heart tissue and fibroblast cell lines. Subunit structure and activity studies. J Biol Chem 277:33906-33912.
    • (2002) J Biol Chem , vol.277 , pp. 33906-33912
    • Aggeler, R.1    Coons, J.2    Taylor, S.W.3    Ghosh, S.S.4    Garcia, J.J.5    Capaldi, R.A.6    Marusich, M.F.7
  • 3
    • 0035800787 scopus 로고    scopus 로고
    • Proteomic analysis of nucleoporin interacting proteins
    • Alien NP, Huang L, Burlingame A, Rexach M. 2001. Proteomic analysis of nucleoporin interacting proteins. J Biol Chem 276:29268-29274.
    • (2001) J Biol Chem , vol.276 , pp. 29268-29274
    • Alien, N.P.1    Huang, L.2    Burlingame, A.3    Rexach, M.4
  • 6
    • 0037245913 scopus 로고    scopus 로고
    • BIND: The biomolecular interaction network database
    • Bader GD, Betel D, Hogue CW. 2003. BIND: The biomolecular interaction network database. Nucleic Acids Res 31:248-250.
    • (2003) Nucleic Acids Res , vol.31 , pp. 248-250
    • Bader, G.D.1    Betel, D.2    Hogue, C.W.3
  • 8
    • 0030861438 scopus 로고    scopus 로고
    • The SWISS-PROT protein sequence data bank and its supplement TrEMBL
    • Bairoch A, Apweiler R. 1997. The SWISS-PROT protein sequence data bank and its supplement TrEMBL. Nucleic Acids Res 25:31-36.
    • (1997) Nucleic Acids Res , vol.25 , pp. 31-36
    • Bairoch, A.1    Apweiler, R.2
  • 10
    • 0036187913 scopus 로고    scopus 로고
    • Extensive feature detection of N-terminal protein sorting signals
    • Bannai H, Tamada Y, Maruyama O, Nakai K, Miyano S. 2002. Extensive feature detection of N-terminal protein sorting signals. Bioinformatics 18:298-305.
    • (2002) Bioinformatics , vol.18 , pp. 298-305
    • Bannai, H.1    Tamada, Y.2    Maruyama, O.3    Nakai, K.4    Miyano, S.5
  • 12
    • 0037264524 scopus 로고    scopus 로고
    • The GRID: The general repository for interaction datasets
    • Breitkreutz BJ, Stark C, Tyers M. 2003. The GRID: The general repository for interaction datasets. Genome Biol 4:R23.
    • (2003) Genome Biol , vol.4
    • Breitkreutz, B.J.1    Stark, C.2    Tyers, M.3
  • 13
    • 0037431026 scopus 로고    scopus 로고
    • Identification of 14 new phosphoproteins involved in important plant mitochondrial processes
    • Bykova NV, Egsgaard H, Moller IM. 2003. Identification of 14 new phosphoproteins involved in important plant mitochondrial processes. FEES Lett 540:141-146.
    • (2003) FEES Lett , vol.540 , pp. 141-146
    • Bykova, N.V.1    Egsgaard, H.2    Moller, I.M.3
  • 14
    • 0037184987 scopus 로고    scopus 로고
    • Definition of the nuclear encoded protein composition of bovine heart mitochondrial complex I. Identification of two new subunits
    • Carroll J, Shannon RJ, Fearnley IM, Walker JE, Hirst J. 2002. Definition of the nuclear encoded protein composition of bovine heart mitochondrial complex I. Identification of two new subunits. J Biol Chem 277:50311 -50317.
    • (2002) J Biol Chem , vol.277 , pp. 50311-50317
    • Carroll, J.1    Shannon, R.J.2    Fearnley, I.M.3    Walker, J.E.4    Hirst, J.5
  • 16
    • 0036690387 scopus 로고    scopus 로고
    • Hyperphosphorylated C-terminal repeat domain-associating proteins in the nuclear proteome link transcription to DNA/chromatin modification and RNA processing
    • Carty SM, Greenleaf AL. 2002. Hyperphosphorylated C-terminal repeat domain-associating proteins in the nuclear proteome link transcription to DNA/chromatin modification and RNA processing. Mol Cell Proteomics 1:598-610.
    • (2002) Mol Cell Proteomics , vol.1 , pp. 598-610
    • Carty, S.M.1    Greenleaf, A.L.2
  • 17
    • 0035380711 scopus 로고    scopus 로고
    • The small subunit of the mammalian mitochondrial ribosome. Identification of the full complement of ribosomal proteins present
    • Cavdar Koc E, Burkhart W, Blackburn K, Moseley A, Spremulli LL. 2001. The small subunit of the mammalian mitochondrial ribosome. Identification of the full complement of ribosomal proteins present. J Biol Chem 276:19363-19374.
    • (2001) J Biol Chem , vol.276 , pp. 19363-19374
    • Cavdar Koc, E.1    Burkhart, W.2    Blackburn, K.3    Moseley, A.4    Spremulli, L.L.5
  • 19
    • 0029915525 scopus 로고    scopus 로고
    • Computational method to predict mitochondrially imported proteins and their targeting sequences
    • Claros MG, Vincens P. 1996. Computational method to predict mitochondrially imported proteins and their targeting sequences. Eur J Biochem 241:779-786.
    • (1996) Eur J Biochem , vol.241 , pp. 779-786
    • Claros, M.G.1    Vincens, P.2
  • 20
    • 0034331073 scopus 로고    scopus 로고
    • Finding nuclear localization signals
    • Cokol M, Nair R, Rost B. 2000. Finding nuclear localization signals. EMBO Rep 1:411-415.
    • (2000) EMBO Rep , vol.1 , pp. 411-415
    • Cokol, M.1    Nair, R.2    Rost, B.3
  • 23
    • 0038316341 scopus 로고    scopus 로고
    • ER-mediated phagocytosis: A new membrane for new functions
    • Desjardins M. 2003. ER-mediated phagocytosis: A new membrane for new functions. Nat Rev Immunol 3:280-291.
    • (2003) Nat Rev Immunol , vol.3 , pp. 280-291
    • Desjardins, M.1
  • 24
    • 0028328732 scopus 로고
    • Biogenesis of phagolysosomes proceeds through a sequential series of interactions with the endocytic apparatus
    • Desjardins M, Huber LA, Parton RG, Griffiths G. 1994. Biogenesis of phagolysosomes proceeds through a sequential series of interactions with the endocytic apparatus. J Cell Biol 124:677-688.
    • (1994) J Cell Biol , vol.124 , pp. 677-688
    • Desjardins, M.1    Huber, L.A.2    Parton, R.G.3    Griffiths, G.4
  • 25
    • 0037934549 scopus 로고    scopus 로고
    • Subcellular proteomics
    • Dreger M. 2003. Subcellular proteomics. Mass Spectrom Rev 22:27-56.
    • (2003) Mass Spectrom Rev , vol.22 , pp. 27-56
    • Dreger, M.1
  • 26
    • 0031888036 scopus 로고    scopus 로고
    • High throughput protein characterization by automated reverse-phase chromatography/electrospray tandem mass spectrometry
    • Ducret A, Van Oostveen I, Eng JK, Yates JR III, Aebersold R. 1998. High throughput protein characterization by automated reverse-phase chromatography/electrospray tandem mass spectrometry. Protein Sei 7:706-719.
    • (1998) Protein Sei , vol.7 , pp. 706-719
    • Ducret, A.1    Van Oostveen, I.2    Eng, J.K.3    Yates III, J.R.4    Aebersold, R.5
  • 27
    • 0037084502 scopus 로고    scopus 로고
    • Identification and characterization of a novel human plant pathogenesis-related protein that localizes to lipid-enriched microdomains in the Golgi complex
    • Eberle HB, Serrano RL, Fullekrug J, Schlosser A, Lehmann WD, Lottspeich F, Kaloyanova D, Wieland FT, Helms JB. 2002. Identification and characterization of a novel human plant pathogenesis-related protein that localizes to lipid-enriched microdomains in the Golgi complex. J Cell Sei 115:827-838.
    • (2002) J Cell Sei , vol.115 , pp. 827-838
    • Eberle, H.B.1    Serrano, R.L.2    Fullekrug, J.3    Schlosser, A.4    Lehmann, W.D.5    Lottspeich, F.6    Kaloyanova, D.7    Wieland, F.T.8    Helms, J.B.9
  • 28
    • 0037388895 scopus 로고    scopus 로고
    • Hepatic protein expression of lean mice and obese diabetic mice treated with peroxisome proliferator-activated receptor activators
    • Edvardsson U, Brockenhuus Von Lowenhielm H, Panfilov O, Nystrom AC, Nilsson F, Dahllof B. 2003. Hepatic protein expression of lean mice and obese diabetic mice treated with peroxisome proliferator-activated receptor activators. Proteomics 3:468-478.
    • (2003) Proteomics , vol.3 , pp. 468-478
    • Edvardsson, U.1    Brockenhuus Von Lowenhielm, H.2    Panfilov, O.3    Nystrom, A.C.4    Nilsson, F.5    Dahllof, B.6
  • 29
    • 0032935861 scopus 로고    scopus 로고
    • ChloroP, a neural network-based method for predicting chloroplast transit peptides and their cleavage sites
    • Emanuelsson O, Nielsen H, von Heijne G. 1999. ChloroP, a neural network-based method for predicting chloroplast transit peptides and their cleavage sites, Protein Sei 8:978-984.
    • (1999) Protein Sei , vol.8 , pp. 978-984
    • Emanuelsson, O.1    Nielsen, H.2    Von Heijne, G.3
  • 30
    • 0034697980 scopus 로고    scopus 로고
    • Predicting subcellular localization of proteins based on their N-terminal amino acid sequence
    • Emanuelsson O, Nielsen H, Brunak S, von Heijne G. 2000. Predicting subcellular localization of proteins based on their N-terminal amino acid sequence. J Mol Biol 300:1005-1016.
    • (2000) J Mol Biol , vol.300 , pp. 1005-1016
    • Emanuelsson, O.1    Nielsen, H.2    Brunak, S.3    Von Heijne, G.4
  • 31
    • 0035914435 scopus 로고    scopus 로고
    • GRIM-19, a cell death regulatory gene product, is a subunit of bovine mitochondrial NADH:ubiquinone oxidoreductase (complex I)
    • Fearnley IM, Carroll J, Shannon RJ, Runswick MJ, Walker JE, Hirst J. 2001. GRIM-19, a cell death regulatory gene product, is a subunit of bovine mitochondrial NADH:ubiquinone oxidoreductase (complex I). J Biol Chem 276: 38345-38348.
    • (2001) J Biol Chem , vol.276 , pp. 38345-38348
    • Fearnley, I.M.1    Carroll, J.2    Shannon, R.J.3    Runswick, M.J.4    Walker, J.E.5    Hirst, J.6
  • 33
    • 0036211823 scopus 로고    scopus 로고
    • RADARS, a bioinformatics solution that automates proteome mass spectral analysis, optimises protein identification, and archives data in a relational database
    • Field HI, Fenyo D, Beavis RC. 2002. RADARS, a bioinformatics solution that automates proteome mass spectral analysis, optimises protein identification, and archives data in a relational database. Proteomics 2:36-47.
    • (2002) Proteomics , vol.2 , pp. 36-47
    • Field, H.I.1    Fenyo, D.2    Beavis, R.C.3
  • 34
    • 0037947831 scopus 로고    scopus 로고
    • Unbiased quantitative proteomics of lipid rafts reveals high specificity for signaling factors
    • Foster LJ, De Hoog CL, Mann M. 2003. Unbiased quantitative proteomics of lipid rafts reveals high specificity for signaling factors. Proc Natl Acad Sei USA 100:5813-5818.
    • (2003) Proc Natl Acad Sei USA , vol.100 , pp. 5813-5818
    • Foster, L.J.1    De Hoog, C.L.2    Mann, M.3
  • 35
    • 0037269174 scopus 로고    scopus 로고
    • The mitochondrial proteins of the neuroblastoma cell line IMR-32
    • Fountoulakis M, Schlaeger EJ. 2003, The mitochondrial proteins of the neuroblastoma cell line IMR-32. Electrophoresis 24:260-275.
    • (2003) Electrophoresis , vol.24 , pp. 260-275
    • Fountoulakis, M.1    Schlaeger, E.J.2
  • 36
    • 0041733229 scopus 로고    scopus 로고
    • Proteomic study of the Arabidopsis thaliana chloroplastic envelope membrane utilizing alternatives to traditional two-dimensional electrophoresis
    • Froehlich JE, Wilkerson CGW, Ray K, McAndrew RS, Osteryoung KW, Gage DA, Phinney BS. 2003. Proteomic study of the Arabidopsis thaliana chloroplastic envelope membrane utilizing alternatives to traditional two-dimensional electrophoresis. J Proteome Res 2:413-425.
    • (2003) J Proteome Res , vol.2 , pp. 413-425
    • Froehlich, J.E.1    Wilkerson, C.G.W.2    Ray, K.3    McAndrew, R.S.4    Osteryoung, K.W.5    Gage, D.A.6    Phinney, B.S.7
  • 37
    • 0038641860 scopus 로고    scopus 로고
    • A proteomic approach to the identification of heterogeneous nuclear ribonucleoproteins as a new family of poly(ADP-ribose)-binding proteins
    • Gagne JP, Hunter JM, Labrecque B, Chabot B, Poirier GG. 2003. A proteomic approach to the identification of heterogeneous nuclear ribonucleoproteins as a new family of poly(ADP-ribose)-binding proteins. Biochem J 371:331-340.
    • (2003) Biochem J , vol.371 , pp. 331-340
    • Gagne, J.P.1    Hunter, J.M.2    Labrecque, B.3    Chabot, B.4    Poirier, G.G.5
  • 39
    • 0036428536 scopus 로고    scopus 로고
    • Tag-mediated isolation of yeast mitochondrial ribosome and mass spectrometric identification of its new components
    • Gan X, Kitakawa M, Yoshino K, Oshiro N, Yonezawa K, Isono K. 2002. Tag-mediated isolation of yeast mitochondrial ribosome and mass spectrometric identification of its new components. Eur J Biochem 269:5203-5214.
    • (2002) Eur J Biochem , vol.269 , pp. 5203-5214
    • Gan, X.1    Kitakawa, M.2    Yoshino, K.3    Oshiro, N.4    Yonezawa, K.5    Isono, K.6
  • 43
  • 44
    • 0035044161 scopus 로고    scopus 로고
    • A novel subfractionation approach for mitochondrial proteins: A three-dimensional mitochondrial proteome map
    • Hanson BJ, Schulenberg B, Patton WF, Capaldi RA. 2001. A novel subfractionation approach for mitochondrial proteins: A three-dimensional mitochondrial proteome map. Electrophoresis 22:950-959.
    • (2001) Electrophoresis , vol.22 , pp. 950-959
    • Hanson, B.J.1    Schulenberg, B.2    Patton, W.F.3    Capaldi, R.A.4
  • 45
    • 0021719707 scopus 로고
    • Endocytosis and intracellular processing of transferrin and colloidal gold-transferrin in rat reticulocytes: Demonstration of a pathway for receptor shedding
    • Harding C, Heuser J, Stahl P. 1984. Endocytosis and intracellular processing of transferrin and colloidal gold-transferrin in rat reticulocytes: Demonstration of a pathway for receptor shedding. Eur J Cell Biol 35:256-263.
    • (1984) Eur J Cell Biol , vol.35 , pp. 256-263
    • Harding, C.1    Heuser, J.2    Stahl, P.3
  • 46
    • 0038433229 scopus 로고    scopus 로고
    • Mitochondrial complex I from Arabidopsis and rice: Orthologs of mammalian and fungal components coupled with plant-specific subunits
    • Heazlewood JL, Howell KA, Millar AH. 2003a. Mitochondrial complex I from Arabidopsis and rice: Orthologs of mammalian and fungal components coupled with plant-specific subunits. Biochim Biophys Acta 1604:159-169.
    • (2003) Biochim Biophys Acta , vol.1604 , pp. 159-169
    • Heazlewood, J.L.1    Howell, K.A.2    Millar, A.H.3
  • 47
    • 0037430978 scopus 로고    scopus 로고
    • The products of the mitochondrial orf25 and orfB genes are FO components in the plant FIFO ATP synthase
    • Heazlewood JL, Whelan J, Millar AH. 2003c. The products of the mitochondrial orf25 and orfB genes are FO components in the plant FIFO ATP synthase. FEES Lett 540:201-215.
    • (2003) FEES Lett , vol.540 , pp. 201-215
    • Heazlewood, J.L.1    Whelan, J.2    Millar, A.H.3
  • 49
    • 0037468460 scopus 로고    scopus 로고
    • Proteomic identification of divalent metal cation binding proteins in plant mitochondria
    • Herald VL, Heazlewood JL, Day DA, Millar AH. 2003. Proteomic identification of divalent metal cation binding proteins in plant mitochondria. FEES Lett 537:96-100.
    • (2003) FEES Lett , vol.537 , pp. 96-100
    • Herald, V.L.1    Heazlewood, J.L.2    Day, D.A.3    Millar, A.H.4
  • 50
    • 0020071663 scopus 로고
    • Hepatic Golgi fractions resolved into membrane and content subfractions
    • Howell KE, Palade GE. 1982. Hepatic Golgi fractions resolved into membrane and content subfractions. J Cell Biol 92: 822-832.
    • (1982) J Cell Biol , vol.92 , pp. 822-832
    • Howell, K.E.1    Palade, G.E.2
  • 51
    • 0038364020 scopus 로고    scopus 로고
    • Organelle proteomics: Implications for subcellular fractionation in proteomics
    • Huber LA, Pfaller K, Victor I. 2003. Organelle proteomics: Implications for subcellular fractionation in proteomics. Circ Res 92:962-968.
    • (2003) Circ Res , vol.92 , pp. 962-968
    • Huber, L.A.1    Pfaller, K.2    Victor, I.3
  • 52
    • 0038325540 scopus 로고    scopus 로고
    • A modular on-line three-dimensional liquid chromatography-tandem mass spectrometry approach to characterization of organelle proteomes
    • Johnson KL, Loegering DA, Gleich GJ, Naylor S. 2003. A modular on-line three-dimensional liquid chromatography-tandem mass spectrometry approach to characterization of organelle proteomes, Biomed Chromatogr 17:106-112.
    • (2003) Biomed Chromatogr , vol.17 , pp. 106-112
    • Johnson, K.L.1    Loegering, D.A.2    Gleich, G.J.3    Naylor, S.4
  • 53
    • 0036668520 scopus 로고    scopus 로고
    • Proteomic analysis of human lysosomes: Application to monocytic and breast cancer cells
    • Journet A, Chapel A, Kieffer S, Roux F, Garin J. 2002. Proteomic analysis of human lysosomes: Application to monocytic and breast cancer cells. Proteomics 2:1026-1040.
    • (2002) Proteomics , vol.2 , pp. 1026-1040
    • Journet, A.1    Chapel, A.2    Kieffer, S.3    Roux, F.4    Garin, J.5
  • 54
    • 0037402769 scopus 로고    scopus 로고
    • Microanalysis of N-linked oligosaccharides in a glycoprotein by capillary liquid chromatography/mass spectrometry and liquid chromatography/tandem mass spectrometry
    • Kawasaki N, Itoh S, Ohta M, Hayakawa T. 2003. Microanalysis of N-linked oligosaccharides in a glycoprotein by capillary liquid chromatography/mass spectrometry and liquid chromatography/tandem mass spectrometry. Anal Biochem 316:15-22.
    • (2003) Anal Biochem , vol.316 , pp. 15-22
    • Kawasaki, N.1    Itoh, S.2    Ohta, M.3    Hayakawa, T.4
  • 55
    • 0035941287 scopus 로고    scopus 로고
    • The large subunit of the mammalian mitochondrial ribosome. Analysis of the complement of ribosomal proteins present
    • Koc EC, Burkhart W, Blackburn K, Moyer MB, Schlatzer DM, Moseley A, Spremulli LL. 2001. The large subunit of the mammalian mitochondrial ribosome. Analysis of the complement of ribosomal proteins present. J Biol Chem 276: 43958-43969.
    • (2001) J Biol Chem , vol.276 , pp. 43958-43969
    • Koc, E.C.1    Burkhart, W.2    Blackburn, K.3    Moyer, M.B.4    Schlatzer, D.M.5    Moseley, A.6    Spremulli, L.L.7
  • 56
    • 0036800808 scopus 로고    scopus 로고
    • The predicted candidates of Arabidopsis plastid inner envelope membrane proteins and their expression profiles
    • Koo AJ, Ohlrogge JB. 2002. The predicted candidates of Arabidopsis plastid inner envelope membrane proteins and their expression profiles. Plant Physiol 130:823-836.
    • (2002) Plant Physiol , vol.130 , pp. 823-836
    • Koo, A.J.1    Ohlrogge, J.B.2
  • 57
    • 0035910270 scopus 로고    scopus 로고
    • Predicting transmembrane protein topology with a hidden Markov model: Application to complete genomes
    • Krogh A, Larsson B, von Heijne G, Sonnhammer EL. 2001. Predicting transmembrane protein topology with a hidden Markov model: Application to complete genomes. J Mol Biol 305:567-580.
    • (2001) J Mol Biol , vol.305 , pp. 567-580
    • Krogh, A.1    Larsson, B.2    Von Heijne, G.3    Sonnhammer, E.L.4
  • 60
    • 0035072551 scopus 로고    scopus 로고
    • Clustering of highly homologous sequences to reduce the size of large protein databases
    • Li W, Jaroszewski L, Godzik A. 2001. Clustering of highly homologous sequences to reduce the size of large protein databases. Bioinformatics 17:282-283.
    • (2001) Bioinformatics , vol.17 , pp. 282-283
    • Li, W.1    Jaroszewski, L.2    Godzik, A.3
  • 61
    • 0037388897 scopus 로고    scopus 로고
    • Monocyte lipid rafts contain proteins implicated in vesicular trafficking and phagosome formation
    • Li N, Mak A, Richards DP, Naber C, Keller BO, Li L, Shaw AR. 2003. Monocyte lipid rafts contain proteins implicated in vesicular trafficking and phagosome formation. Proteomics 3:536-548.
    • (2003) Proteomics , vol.3 , pp. 536-548
    • Li, N.1    Mak, A.2    Richards, D.P.3    Naber, C.4    Keller, B.O.5    Li, L.6    Shaw, A.R.7
  • 62
    • 0043198426 scopus 로고    scopus 로고
    • Proteomic tools for quantitation by mass spectrometry
    • Lill J. 2003. Proteomic tools for quantitation by mass spectrometry. Mass Spectrom Rev 22:182-194.
    • (2003) Mass Spectrom Rev , vol.22 , pp. 182-194
    • Lill, J.1
  • 65
    • 0037321898 scopus 로고    scopus 로고
    • Genomic and proteomic analysis of mitochondrial carrier proteins in Arabidopsis
    • Millar AH, Heazlewood JL. 2003. Genomic and proteomic analysis of mitochondrial carrier proteins in Arabidopsis. Plant Physiol 131:443-453.
    • (2003) Plant Physiol , vol.131 , pp. 443-453
    • Millar, A.H.1    Heazlewood, J.L.2
  • 66
    • 0141510019 scopus 로고    scopus 로고
    • Oxidative damage to mitochondrial complex I due to peroxynitrite: Identification of reactive tyrosines by mass spectrometry
    • Murray J, Taylor SW, Zhang B, Ghosh SS, Capaldi RA. 2003a. Oxidative damage to mitochondrial complex I due to peroxynitrite: Identification of reactive tyrosines by mass spectrometry. J Biol Chem 278:37223-37230.
    • (2003) J Biol Chem , vol.278 , pp. 37223-37230
    • Murray, J.1    Taylor, S.W.2    Zhang, B.3    Ghosh, S.S.4    Capaldi, R.A.5
  • 68
    • 0032972509 scopus 로고    scopus 로고
    • PSORT: A program for detecting sorting signals in proteins and predicting their subcellular localization
    • Nakai K, Horton P. 1999. PSORT: A program for detecting sorting signals in proteins and predicting their subcellular localization. Trends Biochem Sci 24:34-36.
    • (1999) Trends Biochem Sci , vol.24 , pp. 34-36
    • Nakai, K.1    Horton, P.2
  • 69
    • 0027105007 scopus 로고
    • A knowledge base for predicting protein localization sites in eukaryotic cells
    • Nakai K, Kanehisa M. 1992. A knowledge base for predicting protein localization sites in eukaryotic cells. Genomics 14:897-911.
    • (1992) Genomics , vol.14 , pp. 897-911
    • Nakai, K.1    Kanehisa, M.2
  • 70
    • 0033617448 scopus 로고    scopus 로고
    • In vivo mitochondrial import. A comparison of leader sequence charge and structural relationships with the in vitro model resulting in evidence for co-translational import
    • Ni L, Heard TS, Weiner H. 1999. In vivo mitochondrial import. A comparison of leader sequence charge and structural relationships with the in vitro model resulting in evidence for co-translational import. J Biol Chem 274:12685-12691.
    • (1999) J Biol Chem , vol.274 , pp. 12685-12691
    • Ni, L.1    Heard, T.S.2    Weiner, H.3
  • 71
    • 0030614959 scopus 로고    scopus 로고
    • Identification of prokaryotic and eukaryotic signal peptides and prediction of their cleavage sites
    • Nielsen H, Engelbrecht J, Brunak S, von Heijne G. 1997. Identification of prokaryotic and eukaryotic signal peptides and prediction of their cleavage sites. Protein Eng 10:1-6.
    • (1997) Protein Eng , vol.10 , pp. 1-6
    • Nielsen, H.1    Engelbrecht, J.2    Brunak, S.3    Von Heijne, G.4
  • 72
    • 0037621728 scopus 로고    scopus 로고
    • Progress in establishing common standards for exchanging proteomics data: The second meeting of the HUPO proteomics standards initiative
    • Orchard S, Kersey P, Zhu W, Montecchi-Palazzi L, Hermjakob H, Apweiler R. 2003. Progress in establishing common standards for exchanging proteomics data: The second meeting of the HUPO Proteomics Standards Initiative. Comp Funct Genomics 4:203-206.
    • (2003) Comp Funct Genomics , vol.4 , pp. 203-206
    • Orchard, S.1    Kersey, P.2    Zhu, W.3    Montecchi-Palazzi, L.4    Hermjakob, H.5    Apweiler, R.6
  • 73
    • 0038488182 scopus 로고    scopus 로고
    • Mass spectrometric analysis of the editosome and other multiprotein complexes in Trypanosoma brucei
    • Panigrahi AK, Alien TE, Stuart K, Haynes PA, Gygi SP. 2003. Mass spectrometric analysis of the editosome and other multiprotein complexes in Trypanosoma brucei. J Am Soc Mass Spectrom 14:728-735.
    • (2003) J Am Soc Mass Spectrom , vol.14 , pp. 728-735
    • Panigrahi, A.K.1    Alien, T.E.2    Stuart, K.3    Haynes, P.A.4    Gygi, S.P.5
  • 74
  • 75
    • 0037277179 scopus 로고    scopus 로고
    • Evaluation of multidimensional chromatography coupled with tandem mass spectrometry (LC/LC-MS/MS) for large-scale protein analysis: The yeast proteome
    • Peng J, Elias JE, Thoreen CC, Licklider LJ, Gygi SP. 2003. Evaluation of multidimensional chromatography coupled with tandem mass spectrometry (LC/LC-MS/MS) for large-scale protein analysis: The yeast proteome. J Proteome Res 2:43-50.
    • (2003) J Proteome Res , vol.2 , pp. 43-50
    • Peng, J.1    Elias, J.E.2    Thoreen, C.C.3    Licklider, L.J.4    Gygi, S.P.5
  • 76
    • 0026486517 scopus 로고
    • Alterations in the protein composition of maturing phagosomes
    • Pitt A, Mayorga LS, Stahl PD, Schwartz AL. 1992. Alterations in the protein composition of maturing phagosomes. J Clin Invest 90:1978-1983.
    • (1992) J Clin Invest , vol.90 , pp. 1978-1983
    • Pitt, A.1    Mayorga, L.S.2    Stahl, P.D.3    Schwartz, A.L.4
  • 77
    • 0033967692 scopus 로고    scopus 로고
    • Introducing refseq and locuslink: Curated human genome resources at the NCBI
    • Pruitt KD, Katz KS, Sicotte H, Maglott DR. 2000. Introducing RefSeq and LocusLink: Curated human genome resources at the NCBI. Trends Genet 16:44-47.
    • (2000) Trends Genet , vol.16 , pp. 44-47
    • Pruitt, K.D.1    Katz, K.S.2    Sicotte, H.3    Maglott, D.R.4
  • 79
    • 0037005550 scopus 로고    scopus 로고
    • Lysosome-related organelles: A view from immunity and pigmentation
    • Raposo G, Fevrier B, Stoorvogel W, Marks MS. 2002. Lysosome-related organelles: A view from immunity and pigmentation. Cell Struct Funct 27:443-456.
    • (2002) Cell Struct Funct , vol.27 , pp. 443-456
    • Raposo, G.1    Fevrier, B.2    Stoorvogel, W.3    Marks, M.S.4
  • 80
    • 0038015611 scopus 로고    scopus 로고
    • Evolutionary diversification of mitochondrial proteomes: Implications for human disease
    • Richly E, Chinnery PF, Leister D. 2003. Evolutionary diversification of mitochondrial proteomes: Implications for human disease. Trends Genet 19:356-362.
    • (2003) Trends Genet , vol.19 , pp. 356-362
    • Richly, E.1    Chinnery, P.F.2    Leister, D.3
  • 81
    • 0038808989 scopus 로고    scopus 로고
    • A unique mechanism for protein processing and degradation in Arabidopsis thaliana
    • Rojo E, Zouhar J, Carter C, Kovaleva V, Raikhel NV. 2003. A unique mechanism for protein processing and degradation in Arabidopsis thaliana. Proc Natl Acad Sci USA 100:7389-7394.
    • (2003) Proc Natl Acad Sci USA , vol.100 , pp. 7389-7394
    • Rojo, E.1    Zouhar, J.2    Carter, C.3    Kovaleva, V.4    Raikhel, N.V.5
  • 82
    • 0000233053 scopus 로고    scopus 로고
    • Two-dimensional electrophoresis and mass spectrometric identification of mitochondrial proteins from an SH-SY5Y neuroblastoma cell line
    • Scheffler NK, Miller SW, Carroll AK, Anderson C, Davis RE, Ghosh SS, Gibson BW. 2001. Two-dimensional electrophoresis and mass spectrometric identification of mitochondrial proteins from an SH-SY5Y neuroblastoma cell line. Mitochondrion 1:161-179.
    • (2001) Mitochondrion , vol.1 , pp. 161-179
    • Scheffler, N.K.1    Miller, S.W.2    Carroll, A.K.3    Anderson, C.4    Davis, R.E.5    Ghosh, S.S.6    Gibson, B.W.7
  • 84
    • 0038034950 scopus 로고    scopus 로고
    • Analysis of steady-state protein phosphorylation in mitochondria using a novel fluorescent phosphosensor dye
    • Schulenberg B, Aggeler R, Beechem JM, Capaldi RA, Patton WF. 2003. Analysis of steady-state protein phosphorylation in mitochondria using a novel fluorescent phosphosensor dye. J Biol Chem 278:27251-27255.
    • (2003) J Biol Chem , vol.278 , pp. 27251-27255
    • Schulenberg, B.1    Aggeler, R.2    Beechem, J.M.3    Capaldi, R.A.4    Patton, W.F.5
  • 85
    • 0035980117 scopus 로고    scopus 로고
    • Proteomic analysis of the mammalian mitochondrial ribosome - Identification of protein components in the 28 S small subunit
    • Suzuki T, Terasaki M, Takemoto-Hori C, Hanada T, Ueda T, Wada A, Watanabe K. 2001 a. Proteomic analysis of the mammalian mitochondrial ribosome - Identification of protein components in the 28 S small subunit. J Biol Chem 276:33181-33195.
    • (2001) J Biol Chem , vol.276 , pp. 33181-33195
    • Suzuki, T.1    Terasaki, M.2    Takemoto-Hori, C.3    Hanada, T.4    Ueda, T.5    Wada, A.6    Watanabe, K.7
  • 86
    • 0035877697 scopus 로고    scopus 로고
    • Structural compensation for the deficit of rRNA with proteins in the mammalian mitochondrial ribosome. Systematic analysis of protein components of the large ribosomal subunit from mammalian mitochondria
    • Suzuki T, Terasaki M, Takemoto-Hori C, Hanada T, Ueda T, Wada A, Watanabe K. 200 Ib. Structural compensation for the deficit of rRNA with proteins in the mammalian mitochondrial ribosome. Systematic analysis of protein components of the large ribosomal subunit from mammalian mitochondria. J Biol Chem 276:21724-21736.
    • (2001) J Biol Chem , vol.276 , pp. 21724-21736
    • Suzuki, T.1    Terasaki, M.2    Takemoto-Hori, C.3    Hanada, T.4    Ueda, T.5    Wada, A.6    Watanabe, K.7
  • 88
    • 0030822623 scopus 로고    scopus 로고
    • Characterization of the Golgi complex cleared of proteins in transit and examination of calcium uptake activities
    • Taylor RS, Jones SM, Dahl RH, Nordeen MH, Howell KE. 1997. Characterization of the Golgi complex cleared of proteins in transit and examination of calcium uptake activities. Mol Biol Cell 8:1911-1931.
    • (1997) Mol Biol Cell , vol.8 , pp. 1911-1931
    • Taylor, R.S.1    Jones, S.M.2    Dahl, R.H.3    Nordeen, M.H.4    Howell, K.E.5
  • 89
    • 0033769457 scopus 로고    scopus 로고
    • Proteomics of rat liver Golgi complex: Minor proteins are identified through sequential fractionation
    • Taylor RS, Wu CC, Hays LG, Eng JK, Yates JR III, Howell KE. 2000. Proteomics of rat liver Golgi complex: Minor proteins are identified through sequential fractionation. Electrophoresis 21:3441-3459.
    • (2000) Electrophoresis , vol.21 , pp. 3441-3459
    • Taylor, R.S.1    Wu, C.C.2    Hays, L.G.3    Eng, J.K.4    Yates III, J.R.5    Howell, K.E.6
  • 90
    • 0036766965 scopus 로고    scopus 로고
    • An alternative strategy to determine the mitochondrial proteome using sucrose gradient fractionation and ID PAGE on highly purified human heart mitochondria
    • Taylor SW, Warnock DE, Glenn GM, Zhang B, Fahy E, Gaucher SP, Capaldi RA, Gibson BW, Ghosh SS. 2002. An alternative strategy to determine the mitochondrial proteome using sucrose gradient fractionation and ID PAGE on highly purified human heart mitochondria. J Proteome Res 1:451 -458.
    • (2002) J Proteome Res , vol.1 , pp. 451-458
    • Taylor, S.W.1    Warnock, D.E.2    Glenn, G.M.3    Zhang, B.4    Fahy, E.5    Gaucher, S.P.6    Capaldi, R.A.7    Gibson, B.W.8    Ghosh, S.S.9
  • 91
    • 0038820056 scopus 로고    scopus 로고
    • Oxidative post-translational modification of tryptophan residues in cardiac mitochondrial proteins
    • Taylor SW, Fahy E, Murray J, Capaldi RA, Ghosh SS. 2003b. Oxidative post-translational modification of tryptophan residues in cardiac mitochondrial proteins. J Biol Chem 278:19587-19590.
    • (2003) J Biol Chem , vol.278 , pp. 19587-19590
    • Taylor, S.W.1    Fahy, E.2    Murray, J.3    Capaldi, R.A.4    Ghosh, S.S.5
  • 93
    • 0034649566 scopus 로고    scopus 로고
    • Analysis of the genome sequence of the flowering plant Arabidopsis thaliana
    • The Arabidopsis Initiative. 2000. Analysis of the genome sequence of the flowering plant Arabidopsis thaliana. Nature 408:796-815.
    • (2000) Nature , vol.408 , pp. 796-815
  • 94
    • 0036676445 scopus 로고    scopus 로고
    • Exosomes: Composition, biogenesis, and function
    • Thery C, Zitvogel L, Amigorena S. 2002. Exosomes: Composition, biogenesis, and function. Nat Rev Immunol 2:569-579.
    • (2002) Nat Rev Immunol , vol.2 , pp. 569-579
    • Thery, C.1    Zitvogel, L.2    Amigorena, S.3
  • 95
    • 0345034770 scopus 로고    scopus 로고
    • Peroxisome subpopulations of the rat liver. Isolation by immune free flow electrophoresis
    • Volkl A, Mohr H, Fahimi HD. 1999. Peroxisome subpopulations of the rat liver. Isolation by immune free flow electrophoresis. J Histochem Cytochem 47:1111 -1118.
    • (1999) J Histochem Cytochem , vol.47 , pp. 1111-1118
    • Volkl, A.1    Mohr, H.2    Fahimi, H.D.3
  • 96
    • 0037388506 scopus 로고    scopus 로고
    • Protein expression changes in the Sprague-Dawley rat liver proteome following administration of peroxisome proliferator activated receptor alpha and gamma ligands
    • White IR, Man WJ, Bryant D, Bugelski P, Camilleri P, Cutler P, Hayes W, Holbrook JD, Kramer K, Lord PG, Wood J. 2003. Protein expression changes in the Sprague-Dawley rat liver proteome following administration of peroxisome proliferator activated receptor alpha and gamma ligands. Proteomics 3:505-512.
    • (2003) Proteomics , vol.3 , pp. 505-512
    • White, I.R.1    Man, W.J.2    Bryant, D.3    Bugelski, P.4    Camilleri, P.5    Cutler, P.6    Hayes, W.7    Holbrook, J.D.8    Kramer, K.9    Lord, P.G.10    Wood, J.11
  • 97
    • 0012252011 scopus 로고    scopus 로고
    • Full subunit coverage liquid chromatography electrospray ionization mass spectrometry (LCMS+) of an oligomeric membrane protein: Cytochrome b(6)f complex from spinach and the cyanobacterium mastigocladus laminosus
    • Whitelegge JP, Zhang H, Aguilera R, Taylor RM, Cramer WA. 2002. Full subunit coverage liquid chromatography electrospray ionization mass spectrometry (LCMS+) of an oligomeric membrane protein: Cytochrome b(6)f complex from Spinach and the Cyanobacterium mastigocladus laminosus. Mol Cell Proteomics 1:816-827.
    • (2002) Mol Cell Proteomics , vol.1 , pp. 816-827
    • Whitelegge, J.P.1    Zhang, H.2    Aguilera, R.3    Taylor, R.M.4    Cramer, W.A.5
  • 98
    • 0036629335 scopus 로고    scopus 로고
    • Vesicle tethering complexes in membrane traffic
    • Whyte JR, Munro S. 2002. Vesicle tethering complexes in membrane traffic. J Cell Sci 115:2627-2637.
    • (2002) J Cell Sci , vol.115 , pp. 2627-2637
    • Whyte, J.R.1    Munro, S.2
  • 99
    • 0038561131 scopus 로고    scopus 로고
    • A method for the comprehensive proteomic analysis of membrane proteins
    • Wu CC, MacCoss MJ, Howell KE, Yates JR. 2003. A method for the comprehensive proteomic analysis of membrane proteins. Nat Biotechnol 21:532-538.
    • (2003) Nat Biotechnol , vol.21 , pp. 532-538
    • Wu, C.C.1    MacCoss, M.J.2    Howell, K.E.3    Yates, J.R.4
  • 101
    • 0036088133 scopus 로고    scopus 로고
    • DIP, the database of interacting proteins: A research tool for studying cellular networks of protein interactions
    • Xenarios I, Salwinski L, Duan XJ, Higney P, Kim SM, Eisenberg D. 2002. DIP, the database of interacting proteins: A research tool for studying cellular networks of protein interactions. Nucleic Acids Res 30:303-305.
    • (2002) Nucleic Acids Res , vol.30 , pp. 303-305
    • Xenarios, I.1    Salwinski, L.2    Duan, X.J.3    Higney, P.4    Kim, S.M.5    Eisenberg, D.6
  • 102
    • 0037238202 scopus 로고    scopus 로고
    • Proteomic identification of all plastid-specific ribosomal proteins in higher plant chloroplast 30s ribosomal subunit
    • Yamaguchi K, Subramanian AR. 2003. Proteomic identification of all plastid-specific ribosomal proteins in higher plant chloroplast 30S ribosomal subunit. Eur J Biochem 270:190-205.
    • (2003) Eur J Biochem , vol.270 , pp. 190-205
    • Yamaguchi, K.1    Subramanian, A.R.2
  • 103
    • 0036845834 scopus 로고    scopus 로고
    • Proteomic characterization of the small subunit of Chlamydomonas reinhardtii chloroplast ribosome: Identification of a novel S1 domaincontaining protein and unusually large orthologs of bacterial S2, S3, and S5
    • Yamaguchi K, Prieto S, Beligni MV, Haynes PA, McDonald WH, Yates JR III, Mayfield SP. 2002. Proteomic characterization of the small subunit of Chlamydomonas reinhardtii chloroplast ribosome: Identification of a novel S1 domaincontaining protein and unusually large orthologs of bacterial S2, S3, and S5. Plant Cell 14:2957-2974.
    • (2002) Plant Cell , vol.14 , pp. 2957-2974
    • Yamaguchi, K.1    Prieto, S.2    Beligni, M.V.3    Haynes, P.A.4    McDonald, W.H.5    Yates III, J.R.6    Mayfield, S.P.7
  • 104
    • 0141817918 scopus 로고    scopus 로고
    • Proteomic characterization of the Chlamydomonas reinhardtii chloroplast ribosome: Identification of proteins unique to the 70s ribosome
    • Yamaguchi K, Beligni MV, Prieto S, Haynes PA, McDonald WH, Yates JR III, Mayfield SP. 2003. Proteomic characterization of the Chlamydomonas reinhardtii chloroplast ribosome: Identification of proteins unique to the 70S ribosome. J Biol Chem 278:33774-33785.
    • (2003) J Biol Chem , vol.278 , pp. 33774-33785
    • Yamaguchi, K.1    Beligni, M.V.2    Prieto, S.3    Haynes, P.A.4    McDonald, W.H.5    Yates III, J.R.6    Mayfield, S.P.7
  • 107
    • 0036929475 scopus 로고    scopus 로고
    • Proteomics of light-harvesting proteins in different plant species. Analysis and comparison by liquid chromatography-electrospray ionization mass spectrometry
    • Zolla L, Rinalducci S, Timperio AM, Huber CG. 2002. Proteomics of light-harvesting proteins in different plant species. Analysis and comparison by liquid chromatography-electrospray ionization mass spectrometry. Photosystem I. Plant Physiol 130:1938-1950.
    • (2002) Photosystem I. Plant Physiol , vol.130 , pp. 1938-1950
    • Zolla, L.1    Rinalducci, S.2    Timperio, A.M.3    Huber, C.G.4
  • 108
    • 0037249679 scopus 로고    scopus 로고
    • Proteomics of light-harvesting proteins in different plant species. Analysis and comparison by liquid chromatography-electrospray ionization mass spectrometry
    • Zolla L, Timperio AM, Walcher W, Huber CG. 2003. Proteomics of light-harvesting proteins in different plant species. Analysis and comparison by liquid chromatography-electrospray ionization mass spectrometry. Photosystem II. Plant Physiol 131:198-214.
    • (2003) Photosystem II. Plant Physiol , vol.131 , pp. 198-214
    • Zolla, L.1    Timperio, A.M.2    Walcher, W.3    Huber, C.G.4


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