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Volumn 277, Issue 16, 2010, Pages 3295-3307

Plant nuclear proteomics-inside the cell maestro

Author keywords

cell culture; cellular proteomics; plant nuclear bodies; plant nuclear proteome; proteome comparison

Indexed keywords

DNA; RNA; VEGETABLE PROTEIN;

EID: 77955233100     PISSN: 1742464X     EISSN: 17424658     Source Type: Journal    
DOI: 10.1111/j.1742-4658.2010.07748.x     Document Type: Review
Times cited : (20)

References (98)
  • 2
    • 66349131897 scopus 로고    scopus 로고
    • Self-organization in the genome
    • Misteli T (2009) Self-organization in the genome. Proc Natl Acad Sci USA 106, 6885 6886.
    • (2009) Proc Natl Acad Sci USA , vol.106 , pp. 6885-6886
    • Misteli, T.1
  • 3
    • 0037435030 scopus 로고    scopus 로고
    • Mass spectrometry-based proteomics
    • Aebersold R Mann M (2003) Mass spectrometry-based proteomics. Nature 422, 198 207.
    • (2003) Nature , vol.422 , pp. 198-207
    • Aebersold, R.1    Mann, M.2
  • 4
    • 36749100886 scopus 로고    scopus 로고
    • Toward a high-resolution view of nuclear dynamics
    • Trinkle-Mulcahy L Lamond AI (2007) Toward a high-resolution view of nuclear dynamics. Science 318, 1402 1407.
    • (2007) Science , vol.318 , pp. 1402-1407
    • Trinkle-Mulcahy, L.1    Lamond, A.I.2
  • 5
    • 0033773392 scopus 로고    scopus 로고
    • Proteomics meets cell biology: The establishment of subcellular proteomes
    • Jung E, Heller M, Sanchez JC Hochstrasser DF (2000) Proteomics meets cell biology: the establishment of subcellular proteomes. Electrophoresis 21, 3369 3377.
    • (2000) Electrophoresis , vol.21 , pp. 3369-3377
    • Jung, E.1    Heller, M.2    Sanchez, J.C.3    Hochstrasser, D.F.4
  • 6
    • 33646239605 scopus 로고    scopus 로고
    • Arabidopsis thaliana proteomics: From proteome to genome
    • Baginsky S Gruissem W (2006) Arabidopsis thaliana proteomics: from proteome to genome. J Exp Bot 57, 1485 1491.
    • (2006) J Exp Bot , vol.57 , pp. 1485-1491
    • Baginsky, S.1    Gruissem, W.2
  • 7
    • 0034649566 scopus 로고    scopus 로고
    • Analysis of the genome sequence of the flowering plant Arabidopsis thaliana
    • The Arabidopsis Genome Initiative
    • The Arabidopsis Genome Initiative (2000) Analysis of the genome sequence of the flowering plant Arabidopsis thaliana. Nature 408, 796 815.
    • (2000) Nature , vol.408 , pp. 796-815
  • 8
    • 63349097597 scopus 로고    scopus 로고
    • Plant proteomics update (2007-2008): Second-generation proteomic techniques, an appropriate experimental design, and data analysis to fulfill MIAPE standards, increase plant proteome coverage and expand biological knowledge
    • Jorrin-Novo JV, Maldonado AM, Echevarria-Zomeno S, Valledor L, Castillejo MA, Curto M, Valero J, Sghaier B, Donoso G Redondo I (2009) Plant proteomics update (2007-2008): second-generation proteomic techniques, an appropriate experimental design, and data analysis to fulfill MIAPE standards, increase plant proteome coverage and expand biological knowledge. J Proteomics 72, 285 314.
    • (2009) J Proteomics , vol.72 , pp. 285-314
    • Jorrin-Novo, J.V.1    Maldonado, A.M.2    Echevarria-Zomeno, S.3    Valledor, L.4    Castillejo, M.A.5    Curto, M.6    Valero, J.7    Sghaier, B.8    Donoso, G.9    Redondo, I.10
  • 9
    • 63349108911 scopus 로고    scopus 로고
    • Plant proteomics
    • Jorrin-Novo JV (2009) Plant proteomics. J Proteomics 72, 283 284.
    • (2009) J Proteomics , vol.72 , pp. 283-284
    • Jorrin-Novo, J.V.1
  • 10
    • 1642569324 scopus 로고    scopus 로고
    • Proteomic studies in plants
    • Park OK (2004) Proteomic studies in plants. J Biochem Mol Biol 37, 133 138.
    • (2004) J Biochem Mol Biol , vol.37 , pp. 133-138
    • Park, O.K.1
  • 12
    • 0034485106 scopus 로고    scopus 로고
    • Proteomics: A link between genomics, genetics and physiology
    • Zivy M de Vienne D (2000) Proteomics: a link between genomics, genetics and physiology. Plant Mol Biol 44, 575 580.
    • (2000) Plant Mol Biol , vol.44 , pp. 575-580
    • Zivy, M.1    De Vienne, D.2
  • 13
    • 0034987772 scopus 로고    scopus 로고
    • Challenges and prospects of plant proteomics
    • van Wijk KJ (2001) Challenges and prospects of plant proteomics. Plant Physiol 126, 501 508.
    • (2001) Plant Physiol , vol.126 , pp. 501-508
    • Van Wijk, K.J.1
  • 14
    • 0035365808 scopus 로고    scopus 로고
    • Functional architecture in the cell nucleus
    • Dundr M Misteli T (2001) Functional architecture in the cell nucleus. Biochem J 356, 297 310.
    • (2001) Biochem J , vol.356 , pp. 297-310
    • Dundr, M.1    Misteli, T.2
  • 15
    • 0035889085 scopus 로고    scopus 로고
    • The concept of self-organization in cellular architecture
    • Misteli T (2001) The concept of self-organization in cellular architecture. J Cell Biol 155, 181 185.
    • (2001) J Cell Biol , vol.155 , pp. 181-185
    • Misteli, T.1
  • 16
    • 0035110880 scopus 로고    scopus 로고
    • Experimental observations of a nuclear matrix
    • Nickerson J (2001) Experimental observations of a nuclear matrix. J Cell Sci 114, 463 474.
    • (2001) J Cell Sci , vol.114 , pp. 463-474
    • Nickerson, J.1
  • 17
    • 0141529726 scopus 로고    scopus 로고
    • A proteomic study of the arabidopsis nuclear matrix
    • Calikowski TT, Meulia T Meier I (2003) A proteomic study of the arabidopsis nuclear matrix. J Cell Biochem 90, 361 378.
    • (2003) J Cell Biochem , vol.90 , pp. 361-378
    • Calikowski, T.T.1    Meulia, T.2    Meier, I.3
  • 19
    • 0032031347 scopus 로고    scopus 로고
    • Nuclear matrix attachment regions and plant gene expression
    • Holmes-Davis R (1998) Nuclear matrix attachment regions and plant gene expression. Trends Plant Sci 3, 91 97.
    • (1998) Trends Plant Sci , vol.3 , pp. 91-97
    • Holmes-Davis, R.1
  • 21
    • 0033779678 scopus 로고    scopus 로고
    • Diffusional protein transport within the nucleus: A message in the medium
    • Pederson T (2000) Diffusional protein transport within the nucleus: a message in the medium. Nat Cell Biol 2, E73 74.
    • (2000) Nat Cell Biol , vol.2 , pp. 73-74
    • Pederson, T.1
  • 22
    • 0033638658 scopus 로고    scopus 로고
    • Self-association of coilin reveals a common theme in nuclear body localization
    • Hebert MD Matera AG (2000) Self-association of coilin reveals a common theme in nuclear body localization. Mol Biol Cell 11, 4159 4171.
    • (2000) Mol Biol Cell , vol.11 , pp. 4159-4171
    • Hebert, M.D.1    Matera, A.G.2
  • 23
    • 0034618074 scopus 로고    scopus 로고
    • The dynamics of postmitotic reassembly of the nucleolus
    • Dundr M, Misteli T Olson MO (2000) The dynamics of postmitotic reassembly of the nucleolus. J Cell Biol 150, 433 446.
    • (2000) J Cell Biol , vol.150 , pp. 433-446
    • Dundr, M.1    Misteli, T.2    Olson, M.O.3
  • 24
    • 0034083175 scopus 로고    scopus 로고
    • Cell biology of transcription and pre-mRNA splicing: Nuclear architecture meets nuclear function
    • Misteli T (2000) Cell biology of transcription and pre-mRNA splicing: nuclear architecture meets nuclear function. J Cell Sci 113 (Pt 11 1841 1849.
    • (2000) J Cell Sci , vol.113 , Issue.PART 11 , pp. 1841-1849
    • Misteli, T.1
  • 25
    • 0344668825 scopus 로고    scopus 로고
    • Analysis of the Arabidopsis nuclear proteome and its response to cold stress
    • Bae MS, Cho EJ, Choi EY Park OK (2003) Analysis of the Arabidopsis nuclear proteome and its response to cold stress. Plant J 36, 652 663.
    • (2003) Plant J , vol.36 , pp. 652-663
    • Bae, M.S.1    Cho, E.J.2    Choi, E.Y.3    Park, O.K.4
  • 26
    • 33748547288 scopus 로고    scopus 로고
    • Guilt by association: The nuclear envelope proteome and disease
    • Wilkie GS Schirmer EC (2006) Guilt by association: the nuclear envelope proteome and disease. Mol Cell Proteomics 5, 1865 1875.
    • (2006) Mol Cell Proteomics , vol.5 , pp. 1865-1875
    • Wilkie, G.S.1    Schirmer, E.C.2
  • 28
    • 0033835333 scopus 로고    scopus 로고
    • Sorting out the complexity of SR protein functions
    • Graveley BR (2000) Sorting out the complexity of SR protein functions. RNA 6, 1197 1211.
    • (2000) RNA , vol.6 , pp. 1197-1211
    • Graveley, B.R.1
  • 29
    • 0037182588 scopus 로고    scopus 로고
    • Ribosomal genes in focus: New transcripts label the dense fibrillar components and form clusters indicative of 'Christmas trees' in situ
    • Koberna K, Malinsky J, Pliss A, Masata M, Vecerova J, Fialova M, Bednar J Raska I (2002) Ribosomal genes in focus: new transcripts label the dense fibrillar components and form clusters indicative of 'Christmas trees' in situ. J Cell Biol 157, 743 748.
    • (2002) J Cell Biol , vol.157 , pp. 743-748
    • Koberna, K.1    Malinsky, J.2    Pliss, A.3    Masata, M.4    Vecerova, J.5    Fialova, M.6    Bednar, J.7    Raska, I.8
  • 30
    • 0034880712 scopus 로고    scopus 로고
    • Single ribosomal transcription units are linear, compacted Christmas trees in plant nucleoli
    • Gonzalez-Melendi P, Wells B, Beven AF Shaw PJ (2001) Single ribosomal transcription units are linear, compacted Christmas trees in plant nucleoli. Plant J 27, 223 233.
    • (2001) Plant J , vol.27 , pp. 223-233
    • Gonzalez-Melendi, P.1    Wells, B.2    Beven, A.F.3    Shaw, P.J.4
  • 32
    • 0028968051 scopus 로고
    • The organization of spliceosomal components in the nuclei of higher plants
    • Beven AF, Simpson GG, Brown JW Shaw PJ (1995) The organization of spliceosomal components in the nuclei of higher plants. J Cell Sci 108 (Pt 2 509 518.
    • (1995) J Cell Sci , vol.108 , Issue.PART 2 , pp. 509-518
    • Beven, A.F.1    Simpson, G.G.2    Brown, J.W.3    Shaw, P.J.4
  • 33
    • 0029941248 scopus 로고    scopus 로고
    • The organization of ribosomal RNA processing correlates with the distribution of nucleolar snRNAs
    • Beven AF, Lee R, Razaz M, Leader DJ, Brown JW Shaw PJ (1996) The organization of ribosomal RNA processing correlates with the distribution of nucleolar snRNAs. J Cell Sci 109 (Pt 6 1241 1251.
    • (1996) J Cell Sci , vol.109 , Issue.PART 6 , pp. 1241-1251
    • Beven, A.F.1    Lee, R.2    Razaz, M.3    Leader, D.J.4    Brown, J.W.5    Shaw, P.J.6
  • 34
    • 0034739848 scopus 로고    scopus 로고
    • Vivo analysis of Cajal body movement, separation, and joining in live human cells
    • Platani M, Goldberg I, Swedlow JR Lamond AI (2000) In vivo analysis of Cajal body movement, separation, and joining in live human cells. J Cell Biol 151, 1561 1574.
    • (2000) J Cell Biol , vol.151 , pp. 1561-1574
    • Platani, M.1    Goldberg, I.2    Swedlow, J.R.3    Lamond, A.I.4
  • 35
    • 0037078322 scopus 로고    scopus 로고
    • Cajal bodies and coilin - Moving towards function
    • Ogg SC Lamond AI (2002) Cajal bodies and coilin - moving towards function. J Cell Biol 159, 17 21.
    • (2002) J Cell Biol , vol.159 , pp. 17-21
    • Ogg, S.C.1    Lamond, A.I.2
  • 41
    • 26944472085 scopus 로고    scopus 로고
    • Update on proteomics in Arabidopsis. Where do we go from here?
    • Peck SC (2005) Update on proteomics in Arabidopsis. Where do we go from here?. Plant Physiol 138, 591 599.
    • (2005) Plant Physiol , vol.138 , pp. 591-599
    • Peck, S.C.1
  • 44
  • 45
    • 33646907417 scopus 로고    scopus 로고
    • AGRIS and AtRegNet. a platform to link cis-regulatory elements and transcription factors into regulatory networks
    • Palaniswamy SK, James S, Sun H, Lamb RS, Davuluri RV Grotewold E (2006) AGRIS and AtRegNet. a platform to link cis-regulatory elements and transcription factors into regulatory networks. Plant Physiol 140, 818 829.
    • (2006) Plant Physiol , vol.140 , pp. 818-829
    • Palaniswamy, S.K.1    James, S.2    Sun, H.3    Lamb, R.S.4    Davuluri, R.V.5    Grotewold, E.6
  • 52
    • 77952267071 scopus 로고    scopus 로고
    • WDBTF: An integrated database resource for studying wheat transcription factor families
    • Romeuf I, Tessier D, Dardevet M, Branlard G, Charmet G Ravel C (2010) wDBTF: an integrated database resource for studying wheat transcription factor families. BMC Genomics 11, 1 15.
    • (2010) BMC Genomics , vol.11 , pp. 1-15
    • Romeuf, I.1    Tessier, D.2    Dardevet, M.3    Branlard, G.4    Charmet, G.5    Ravel, C.6
  • 54
    • 34848899190 scopus 로고    scopus 로고
    • Shotgun proteomic analysis of Arabidopsis thaliana leaves
    • Lee J, Garrett WM Cooper B (2007) Shotgun proteomic analysis of Arabidopsis thaliana leaves. J Sep Sci 30, 2225 2230.
    • (2007) J Sep Sci , vol.30 , pp. 2225-2230
    • Lee, J.1    Garrett, W.M.2    Cooper, B.3
  • 55
    • 26444574929 scopus 로고    scopus 로고
    • Protein detection methods in proteomics research
    • Westermeier R Marouga R (2005) Protein detection methods in proteomics research. Biosci Rep 25, 19 32.
    • (2005) Biosci Rep , vol.25 , pp. 19-32
    • Westermeier, R.1    Marouga, R.2
  • 58
    • 70349513813 scopus 로고    scopus 로고
    • Dehydration-responsive nuclear proteome of rice (Oryza sativa L.) illustrates protein network, novel regulators of cellular adaptation, and evolutionary perspective
    • Choudhary MK, Basu D, Datta A, Chakraborty N Chakraborty S (2009) Dehydration-responsive nuclear proteome of rice (Oryza sativa L.) illustrates protein network, novel regulators of cellular adaptation, and evolutionary perspective. Mol Cell Proteomics 8, 1579 1598.
    • (2009) Mol Cell Proteomics , vol.8 , pp. 1579-1598
    • Choudhary, M.K.1    Basu, D.2    Datta, A.3    Chakraborty, N.4    Chakraborty, S.5
  • 59
    • 0034026047 scopus 로고    scopus 로고
    • Proteomics of the chloroplast: Systematic identification and targeting analysis of lumenal and peripheral thylakoid proteins
    • Peltier JB, Friso G, Kalume DE, Roepstorff P, Nilsson F, Adamska I van Wijk KJ (2000) Proteomics of the chloroplast: systematic identification and targeting analysis of lumenal and peripheral thylakoid proteins. Plant Cell 12, 319 341.
    • (2000) Plant Cell , vol.12 , pp. 319-341
    • Peltier, J.B.1    Friso, G.2    Kalume, D.E.3    Roepstorff, P.4    Nilsson, F.5    Adamska, I.6    Van Wijk, K.J.7
  • 60
    • 0024438708 scopus 로고
    • Electrospray ionization for mass spectrometry of large biomolecules
    • Fenn JB, Mann M, Meng CK, Wong SF Whitehouse CM (1989) Electrospray ionization for mass spectrometry of large biomolecules. Science 246, 64 71.
    • (1989) Science , vol.246 , pp. 64-71
    • Fenn, J.B.1    Mann, M.2    Meng, C.K.3    Wong, S.F.4    Whitehouse, C.M.5
  • 61
    • 0024289037 scopus 로고
    • Laser desorption ionization of proteins with molecular masses exceeding 10,000 daltons
    • Karas M Hillenkamp F (1988) Laser desorption ionization of proteins with molecular masses exceeding 10,000 daltons. Anal Chem 60, 2299 2301.
    • (1988) Anal Chem , vol.60 , pp. 2299-2301
    • Karas, M.1    Hillenkamp, F.2
  • 62
    • 0034789979 scopus 로고    scopus 로고
    • Quantitative profiling of differentiation-induced microsomal proteins using isotope-coded affinity tags and mass spectrometry
    • Han DK, Eng J, Zhou H Aebersold R (2001) Quantitative profiling of differentiation-induced microsomal proteins using isotope-coded affinity tags and mass spectrometry. Nat Biotechnol 19, 946 951.
    • (2001) Nat Biotechnol , vol.19 , pp. 946-951
    • Han, D.K.1    Eng, J.2    Zhou, H.3    Aebersold, R.4
  • 63
    • 50449103703 scopus 로고    scopus 로고
    • Purification and proteomic characterization of plastids from Brassica napus developing embryos
    • Jain R, Katavic V, Agrawal GK, Guzov VM Thelen JJ (2008) Purification and proteomic characterization of plastids from Brassica napus developing embryos. Proteomics 8, 3397 3405.
    • (2008) Proteomics , vol.8 , pp. 3397-3405
    • Jain, R.1    Katavic, V.2    Agrawal, G.K.3    Guzov, V.M.4    Thelen, J.J.5
  • 64
    • 18844427007 scopus 로고    scopus 로고
    • Proteome analysis of Arabidopsis thaliana by two-dimensional gel electrophoresis and matrix-assisted laser desorption/ionisation-time of flight mass spectrometry
    • Giavalisco P, Nordhoff E, Kreitler T, Kloppel KD, Lehrach H, Klose J Gobom J (2005) Proteome analysis of Arabidopsis thaliana by two-dimensional gel electrophoresis and matrix-assisted laser desorption/ionisation-time of flight mass spectrometry. Proteomics 5, 1902 1913.
    • (2005) Proteomics , vol.5 , pp. 1902-1913
    • Giavalisco, P.1    Nordhoff, E.2    Kreitler, T.3    Kloppel, K.D.4    Lehrach, H.5    Klose, J.6    Gobom, J.7
  • 66
    • 2942530586 scopus 로고    scopus 로고
    • Chloroplast proteomics: Potentials and challenges
    • Baginsky S Gruissem W (2004) Chloroplast proteomics: potentials and challenges. J Exp Bot 55, 1213 1220.
    • (2004) J Exp Bot , vol.55 , pp. 1213-1220
    • Baginsky, S.1    Gruissem, W.2
  • 68
    • 0036346730 scopus 로고    scopus 로고
    • Proteomic analysis of leaf peroxisomal proteins in greening cotyledons of Arabidopsis thaliana
    • Fukao Y, Hayashi M Nishimura M (2002) Proteomic analysis of leaf peroxisomal proteins in greening cotyledons of Arabidopsis thaliana. Plant Cell Physiol 43, 689 696.
    • (2002) Plant Cell Physiol , vol.43 , pp. 689-696
    • Fukao, Y.1    Hayashi, M.2    Nishimura, M.3
  • 69
    • 66149173521 scopus 로고    scopus 로고
    • Proteome of plant peroxisomes: New perspectives on the role of these organelles in cell biology
    • Palma JM, Corpas FJ del Rio LA (2009) Proteome of plant peroxisomes: new perspectives on the role of these organelles in cell biology. Proteomics 9, 2301 2312.
    • (2009) Proteomics , vol.9 , pp. 2301-2312
    • Palma, J.M.1    Corpas, F.J.2    Del Rio, L.A.3
  • 73
    • 15744385479 scopus 로고    scopus 로고
    • The vegetative vacuole proteome of Arabidopsis thaliana reveals predicted and unexpected proteins
    • Carter C, Pan S, Zouhar J, Avila EL, Girke T Raikhel NV (2004) The vegetative vacuole proteome of Arabidopsis thaliana reveals predicted and unexpected proteins. Plant Cell 16, 3285 3303.
    • (2004) Plant Cell , vol.16 , pp. 3285-3303
    • Carter, C.1    Pan, S.2    Zouhar, J.3    Avila, E.L.4    Girke, T.5    Raikhel, N.V.6
  • 76
    • 20444466570 scopus 로고    scopus 로고
    • Proteomic characterization of evolutionarily conserved and variable proteins of Arabidopsis cytosolic ribosomes
    • Chang IF, Szick-Miranda K, Pan S Bailey-Serres J (2005) Proteomic characterization of evolutionarily conserved and variable proteins of Arabidopsis cytosolic ribosomes. Plant Physiol 137, 848 862.
    • (2005) Plant Physiol , vol.137 , pp. 848-862
    • Chang, I.F.1    Szick-Miranda, K.2    Pan, S.3    Bailey-Serres, J.4
  • 82
    • 3242752095 scopus 로고    scopus 로고
    • Rice proteomics: Recent developments and analysis of nuclear proteins
    • Khan MM Komatsu S (2004) Rice proteomics: recent developments and analysis of nuclear proteins. Phytochemistry 65, 1671 1681.
    • (2004) Phytochemistry , vol.65 , pp. 1671-1681
    • Khan, M.M.1    Komatsu, S.2
  • 83
    • 38049067580 scopus 로고    scopus 로고
    • Proteome and phosphoproteome analysis of chromatin associated proteins in rice (Oryza sativa)
    • Tan F, Li G, Chitteti BR Peng Z (2007) Proteome and phosphoproteome analysis of chromatin associated proteins in rice (Oryza sativa). Proteomics 7, 4511 4527.
    • (2007) Proteomics , vol.7 , pp. 4511-4527
    • Tan, F.1    Li, G.2    Chitteti, B.R.3    Peng, Z.4
  • 84
    • 33750740399 scopus 로고    scopus 로고
    • The nucleosome: A little variation goes a long way
    • Bernstein E Hake SB (2006) The nucleosome: a little variation goes a long way. Biochem Cell Biol 84, 505 517.
    • (2006) Biochem Cell Biol , vol.84 , pp. 505-517
    • Bernstein, E.1    Hake, S.B.2
  • 86
    • 68549123673 scopus 로고    scopus 로고
    • Application of rice nuclear proteome analysis to the identification of evolutionarily conserved and glucose-responsive nuclear proteins
    • Aki T Yanagisawa S (2009) Application of rice nuclear proteome analysis to the identification of evolutionarily conserved and glucose-responsive nuclear proteins. J Proteome Res 8, 3912 3924.
    • (2009) J Proteome Res , vol.8 , pp. 3912-3924
    • Aki, T.1    Yanagisawa, S.2
  • 88
    • 39049153858 scopus 로고    scopus 로고
    • Proteomics approach to identify dehydration responsive nuclear proteins from chickpea (Cicer arietinum L.)
    • Pandey A, Chakraborty S, Datta A Chakraborty N (2008) Proteomics approach to identify dehydration responsive nuclear proteins from chickpea (Cicer arietinum L.). Mol Cell Proteomics 7, 88 107.
    • (2008) Mol Cell Proteomics , vol.7 , pp. 88-107
    • Pandey, A.1    Chakraborty, S.2    Datta, A.3    Chakraborty, N.4
  • 90
    • 77149148724 scopus 로고    scopus 로고
    • Magnetic particles as powerful purification tool for high sensitive mass spectrometric screening procedures
    • Peter JF Otto AM (2010) Magnetic particles as powerful purification tool for high sensitive mass spectrometric screening procedures. Proteomics 10, 628 633.
    • (2010) Proteomics , vol.10 , pp. 628-633
    • Peter, J.F.1    Otto, A.M.2
  • 91
    • 74249106136 scopus 로고    scopus 로고
    • What does the future hold for Top Down mass spectrometry?
    • Garcia BA (2010) What does the future hold for Top Down mass spectrometry? J Am Soc Mass Spectrom 21, 193 202.
    • (2010) J Am Soc Mass Spectrom , vol.21 , pp. 193-202
    • Garcia, B.A.1
  • 92
    • 77952876849 scopus 로고    scopus 로고
    • Quantitative top-down proteomics of SILAC labelled human embryonic stem cells
    • Collier TS, Sarkar P, Rao B Muddiman DC (2010) Quantitative top-down proteomics of SILAC labelled human embryonic stem cells. J Am Soc Mass Spec 21, 879 889.
    • (2010) J Am Soc Mass Spec , vol.21 , pp. 879-889
    • Collier, T.S.1    Sarkar, P.2    Rao, B.3    Muddiman, D.C.4
  • 93
    • 47249157351 scopus 로고    scopus 로고
    • Combinatorial modification of human histone H4 quantitated by two-dimensional liquid chromatography coupled with top down mass spectrometry
    • Pesavento JJ, Bullock CR, LeDuc RD, Mizzen CA Kelleher NL (2008) Combinatorial modification of human histone H4 quantitated by two-dimensional liquid chromatography coupled with top down mass spectrometry. J Biol Chem 283, 14927 14937.
    • (2008) J Biol Chem , vol.283 , pp. 14927-14937
    • Pesavento, J.J.1    Bullock, C.R.2    Leduc, R.D.3    Mizzen, C.A.4    Kelleher, N.L.5
  • 94
    • 0036583926 scopus 로고    scopus 로고
    • Stable isotope labeling by amino acids in cell culture, SILAC, as a simple and accurate approach to expression proteomics
    • Ong SE, Blagoev B, Kratchmarova I, Kristensen DB, Steen H, Pandey A Mann M (2002) Stable isotope labeling by amino acids in cell culture, SILAC, as a simple and accurate approach to expression proteomics. Mol Cell Proteomics 1, 376 386.
    • (2002) Mol Cell Proteomics , vol.1 , pp. 376-386
    • Ong, S.E.1    Blagoev, B.2    Kratchmarova, I.3    Kristensen, D.B.4    Steen, H.5    Pandey, A.6    Mann, M.7
  • 98
    • 75149162532 scopus 로고    scopus 로고
    • Active learning for human protein-protein interaction prediction
    • Mohamed TP, Carbonell JG Ganapathiraju MK (2010) Active learning for human protein-protein interaction prediction. BMC Bioinformatics 11 (Suppl 1 1 9.
    • (2010) BMC Bioinformatics , vol.11 , Issue.SUPPL. 1 , pp. 1-9
    • Mohamed, T.P.1    Carbonell, J.G.2    Ganapathiraju, M.K.3


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.