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Volumn , Issue , 2007, Pages 247-269

Proteomic analysis of the plant nucleolus

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EID: 77957758503     PISSN: None     EISSN: None     Source Type: Book    
DOI: 10.1007/978-3-540-72617-3_16     Document Type: Chapter
Times cited : (1)

References (77)
  • 1
    • 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
  • 2
    • 26844486610 scopus 로고    scopus 로고
    • Phosphoproteome analysis of HeLa cells using stable isotope labeling with amino acids in cell culture (SILAC)
    • Amanchy R, Kalume DE, Iwahori A, Zhong J, Pandey A (2005) Phosphoproteome analysis of HeLa cells using stable isotope labeling with amino acids in cell culture (SILAC). J Proteome Res 4:1661-1671.
    • (2005) J Proteome Res , vol.4 , pp. 1661-1671
    • Amanchy, R.1    Kalume, D.E.2    Iwahori, A.3    Zhong, J.4    Pandey, A.5
  • 5
    • 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
  • 6
    • 4444371652 scopus 로고    scopus 로고
    • Temporal analysis of phosphotyrosinedependent signaling networks by quantitative proteomics
    • Blagoev B, Ong SE, Kratchmarova I, Mann M (2004) Temporal analysis of phosphotyrosinedependent signaling networks by quantitative proteomics. Nat Biotechnol 22:1139-1145.
    • (2004) Nat Biotechnol , vol.22 , pp. 1139-1145
    • Blagoev, B.1    Ong, S.E.2    Kratchmarova, I.3    Mann, M.4
  • 7
    • 0042386232 scopus 로고    scopus 로고
    • Exploiting the complementary nature of LC/MALDI/MS/MS and LC/ESI/MS/MS for increased proteome coverage
    • Bodnar WM, Blackburn RK, Krise JM, Moseley MA (2003) Exploiting the complementary nature of LC/MALDI/MS/MS and LC/ESI/MS/MS for increased proteome coverage. J Am Soc Mass Spectrom 14:971-979.
    • (2003) J Am Soc Mass Spectrom , vol.14 , pp. 971-979
    • Bodnar, W.M.1    Blackburn, R.K.2    Krise, J.M.3    Moseley, M.A.4
  • 9
    • 7044272787 scopus 로고    scopus 로고
    • Potential for false positive identifications from large databases through tandem mass spectrometry
    • Cargile BJ, Bundy JL, Stephenson JL Jr (2004) Potential for false positive identifications from large databases through tandem mass spectrometry. J Proteome Res 3:1082-1085.
    • (2004) J Proteome Res , vol.3 , pp. 1082-1085
    • Cargile, B.J.1    Bundy, J.L.2    Stephenson, J.L.3
  • 10
    • 3042735127 scopus 로고    scopus 로고
    • The need for guidelines in publication of peptide and protein identification data: Working Group on Publication Guidelines for Peptide and Protein Identification Data
    • Carr S, Aebersold R, Baldwin M, Burlingame A, Clauser K, Nesvizhskii A (2004) The need for guidelines in publication of peptide and protein identification data: Working Group on Publication Guidelines for Peptide and Protein Identification Data. Mol Cell Proteomics 3:531-533.
    • (2004) Mol Cell Proteomics , vol.3 , pp. 531-533
    • Carr, S.1    Aebersold, R.2    Baldwin, M.3    Burlingame, A.4    Clauser, K.5    Nesvizhskii, A.6
  • 11
    • 0036490141 scopus 로고    scopus 로고
    • Mass spectrometrybased methods for phosphorylation site mapping of hyperphosphorylated proteins applied to Net1, a regulator of exit from mitosis in yeast
    • Chen SL, Huddleston MJ, Shou WY, Deshaies RJ, Annan RS, Carr SA (2002) Mass spectrometrybased methods for phosphorylation site mapping of hyperphosphorylated proteins applied to Net1, a regulator of exit from mitosis in yeast. Mol Cell Proteomics 1:186-196.
    • (2002) Mol Cell Proteomics , vol.1 , pp. 186-196
    • Chen, S.L.1    Huddleston, M.J.2    Shou, W.Y.3    Deshaies, R.J.4    Annan, R.S.5    Carr, S.A.6
  • 12
    • 0028966570 scopus 로고
    • A polymerase switch in the synthesis of ribosomal-RNA in Saccharomyces cerevisiae
    • Conrad-Webb H, Butow RA (1995) A polymerase switch in the synthesis of ribosomal-RNA in Saccharomyces cerevisiae. Mol Cell Biol 15:2420-2428.
    • (1995) Mol Cell Biol , vol.15 , pp. 2420-2428
    • Conrad-Webb, H.1    Butow, R.A.2
  • 14
    • 0028973842 scopus 로고
    • The origin and early diversification of angiosperms
    • Crane PR, Friis EM, Pedersen KR (1995) The origin and early diversification of angiosperms. Nature 374:27-33.
    • (1995) Nature , vol.374 , pp. 27-33
    • Crane, P.R.1    Friis, E.M.2    Pedersen, K.R.3
  • 15
    • 0034724178 scopus 로고    scopus 로고
    • Random GFP::cDNA fusions enable visualization of subcellular structures in cells of Arabidopsis at a high frequency
    • Cutler SR, Ehrhardt DW, Griffitts JS, Somerville CR (2000) Random GFP::cDNA fusions enable visualization of subcellular structures in cells of Arabidopsis at a high frequency. Proc Natl Acad Sci USA 97:3718-3723.
    • (2000) Proc Natl Acad Sci USA , vol.97 , pp. 3718-3723
    • Cutler, S.R.1    Ehrhardt, D.W.2    Griffitts, J.S.3    Somerville, C.R.4
  • 16
    • 3042660176 scopus 로고    scopus 로고
    • The use of isotope-coded affinity tags (ICAT) to study organelle proteomes in Arabidopsis thaliana
    • Dunkley TP, Dupree P, Watson RB, Lilley KS (2004a) The use of isotope-coded affinity tags (ICAT) to study organelle proteomes in Arabidopsis thaliana. Biochem Soc Trans 32:520-523.
    • (2004) Biochem Soc Trans , vol.32 , pp. 520-523
    • Dunkley, T.P.1    Dupree, P.2    Watson, R.B.3    Lilley, K.S.4
  • 20
    • 0038381715 scopus 로고    scopus 로고
    • High-throughput viral expression of cDNA-green fluorescent protein fusions reveals novel subcellular addresses and identifies unique proteins that interact with plasmodesmata
    • Escobar NM, Haupt S, Thow G, Boevink P, Chapman S, Oparka K (2003) High-throughput viral expression of cDNA-green fluorescent protein fusions reveals novel subcellular addresses and identifies unique proteins that interact with plasmodesmata. Plant Cell 15:1507-1523.
    • (2003) Plant Cell , vol.15 , pp. 1507-1523
    • Escobar, N.M.1    Haupt, S.2    Thow, G.3    Boevink, P.4    Chapman, S.5    Oparka, K.6
  • 22
    • 33646853354 scopus 로고    scopus 로고
    • Mapping a nucleolar targeting sequence of an RNA binding nucleolar protein, Nop25
    • Fujiwara T, Suzuki S, Kanno M, Sugiyama H, Takahashi H, Tanaka J (2006) Mapping a nucleolar targeting sequence of an RNA binding nucleolar protein, Nop25. Exp Cell Res 312:1703-1712.
    • (2006) Exp Cell Res , vol.312 , pp. 1703-1712
    • Fujiwara, T.1    Suzuki, S.2    Kanno, M.3    Sugiyama, H.4    Takahashi, H.5    Tanaka, J.6
  • 23
    • 28644448658 scopus 로고    scopus 로고
    • Stable isotope labeling of Arabidopsis thaliana cells and quantitative proteomics by mass spectrometry
    • Gruhler A, Schulze WX, Matthiesen R, Mann M, Jensen ON (2005) Stable isotope labeling of Arabidopsis thaliana cells and quantitative proteomics by mass spectrometry. Mol Cell Proteomics 4:1697-1709.
    • (2005) Mol Cell Proteomics , vol.4 , pp. 1697-1709
    • Gruhler, A.1    Schulze, W.X.2    Matthiesen, R.3    Mann, M.4    Jensen, O.N.5
  • 24
  • 26
    • 0037626984 scopus 로고    scopus 로고
    • Integrated plant proteomics - putting the green genomes to work
    • Heazlewood JL, Millar AH (2003) Integrated plant proteomics - putting the green genomes to work. Funct Plant Biol 30:471-482.
    • (2003) Funct Plant Biol , vol.30 , pp. 471-482
    • Heazlewood, J.L.1    Millar, A.H.2
  • 28
    • 0035983223 scopus 로고    scopus 로고
    • The nucleolus - A gateway to viral infection?
    • Hiscox JA (2002) The nucleolus - A gateway to viral infection? Arch Virol 147:1077-1089.
    • (2002) Arch Virol , vol.147 , pp. 1077-1089
    • Hiscox, J.A.1
  • 29
    • 33745608428 scopus 로고    scopus 로고
    • Systematic characterization of nuclear proteome during apoptosis: A quantitative proteomic study by differential extraction and stable isotope labeling
    • Hwang SI, Lundgren DH, Mayya V, Rezaul K, Cowan AE, Eng JK, Han DK (2006) Systematic characterization of nuclear proteome during apoptosis: A quantitative proteomic study by differential extraction and stable isotope labeling. Mol Cell Proteomics 5:1131-1145.
    • (2006) Mol Cell Proteomics , vol.5 , pp. 1131-1145
    • Hwang, S.I.1    Lundgren, D.H.2    Mayya, V.3    Rezaul, K.4    Cowan, A.E.5    Eng, J.K.6    Han, D.K.7
  • 30
    • 0037012884 scopus 로고    scopus 로고
    • Proteomics. Public-private group maps out initiatives
    • Kaiser J (2002) Proteomics. Public-private group maps out initiatives. Science 296:827.
    • (2002) Science , vol.296 , pp. 827
    • Kaiser, J.1
  • 31
    • 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
  • 34
    • 11144287643 scopus 로고    scopus 로고
    • High-throughput protein localization in Arabidopsis using Agrobacterium-mediated transient expression of GFP-ORF fusions
    • Koroleva OA, Tomlinson ML, Leader D, Shaw P, Doonan JH (2005) High-throughput protein localization in Arabidopsis using Agrobacterium-mediated transient expression of GFP-ORF fusions. Plant J 41:162-174.
    • (2005) Plant J , vol.41 , pp. 162-174
    • Koroleva, O.A.1    Tomlinson, M.L.2    Leader, D.3    Shaw, P.4    Doonan, J.H.5
  • 35
    • 0023003653 scopus 로고
    • Protein and cDNA sequence of a glycine-rich, dimethylarginine-containing region located near the corboxylterminal end of nucleolin (C23 and 100 kDa)
    • Lapeyre B, Amalric F, Ghaffari SH, Rao SVV, Dumbar TS, Olson MOJ (1986) Protein and cDNA sequence of a glycine-rich, dimethylarginine-containing region located near the corboxylterminal end of nucleolin (C23 and 100 kDa). J Biol Chem 261:9167-9173.
    • (1986) J Biol Chem , vol.261 , pp. 9167-9173
    • Lapeyre, B.1    Amalric, F.2    Ghaffari, S.H.3    Rao, S.V.V.4    Dumbar, T.S.5    Olson, M.O.J.6
  • 37
    • 1042284932 scopus 로고    scopus 로고
    • Protein profiling with cleavable isotope-coded affinity tag (cICAT) reagents: The yeast salinity stress response
    • Li J, Steen H, Gygi SP (2003) Protein profiling with cleavable isotope-coded affinity tag (cICAT) reagents: The yeast salinity stress response. Mol Cell Proteomics 2:1198-1204.
    • (2003) Mol Cell Proteomics , vol.2 , pp. 1198-1204
    • Li, J.1    Steen, H.2    Gygi, S.P.3
  • 38
    • 33745669487 scopus 로고    scopus 로고
    • Systematic analysis of Arabidopsis organelles and a protein localization database for facilitating fluorescent tagging of full-length Arabidopsis proteins
    • Li SJ, Ehrhardt DW, Rhee SY (2006) Systematic analysis of Arabidopsis organelles and a protein localization database for facilitating fluorescent tagging of full-length Arabidopsis proteins. Plant Physiol 141:527-539.
    • (2006) Plant Physiol , vol.141 , pp. 527-539
    • Li, S.J.1    Ehrhardt, D.W.2    Rhee, S.Y.3
  • 39
    • 33646227179 scopus 로고    scopus 로고
    • Methods of quantitative proteomics and their application to plant organelle characterization
    • Lilley KS, Dupree P (2006) Methods of quantitative proteomics and their application to plant organelle characterization. J Exp Bot 57:1493-1499.
    • (2006) J Exp Bot , vol.57 , pp. 1493-1499
    • Lilley, K.S.1    Dupree, P.2
  • 40
    • 33344469184 scopus 로고    scopus 로고
    • Nucleolar adaptation in human cancer
    • Maggi LB, Weber JD (2005) Nucleolar adaptation in human cancer. Cancer Invest 23:599-608.
    • (2005) Cancer Invest , vol.23 , pp. 599-608
    • Maggi, L.B.1    Weber, J.D.2
  • 42
    • 25444473870 scopus 로고    scopus 로고
    • Cellular stress and nucleolar function
    • Mayer C, Grummt I (2005) Cellular stress and nucleolar function. Cell Cycle 4:1036-1038.
    • (2005) Cell Cycle , vol.4 , pp. 1036-1038
    • Mayer, C.1    Grummt, I.2
  • 43
    • 0029055194 scopus 로고
    • The nucleolus - An organelle formed by the act of building a ribosome
    • Melese T, Xue Z (1995) The nucleolus - An organelle formed by the act of building a ribosome. Curr Opin Cell Biol 7:319-324.
    • (1995) Curr Opin Cell Biol , vol.7 , pp. 319-324
    • Melese, T.1    Xue, Z.2
  • 44
    • 0037169534 scopus 로고    scopus 로고
    • Nucleolar delocalization of human topoisomerase I in response to topotecan correlates with sumoylation of the protein
    • Mo YY, Yu YN, Shen ZY, Beck WT (2002) Nucleolar delocalization of human topoisomerase I in response to topotecan correlates with sumoylation of the protein. J Biol Chem 277:2958-2964.
    • (2002) J Biol Chem , vol.277 , pp. 2958-2964
    • Mo, Y.Y.1    Yu, Y.N.2    Shen, Z.Y.3    Beck, W.T.4
  • 45
    • 0027156138 scopus 로고
    • Peptides with sequences similar to glycine, arginine-rich motifs in proteins interacting with RNA are efficiently recognized by methyltransferase(s) modifying arginine in numerous proteins
    • Najbauer J, Johnson BA, Young AL, Aswad DW (1993) Peptides with sequences similar to glycine, arginine-rich motifs in proteins interacting with RNA are efficiently recognized by methyltransferase(s) modifying arginine in numerous proteins. J Biol Chem 268:10501-10509.
    • (1993) J Biol Chem , vol.268 , pp. 10501-10509
    • Najbauer, J.1    Johnson, B.A.2    Young, A.L.3    Aswad, D.W.4
  • 46
    • 33644853802 scopus 로고    scopus 로고
    • Histone modifications: Signalling receptors and potential elements of a heritable genetic code
    • Nightingale KP, O'Neill LP, Turner BM (2006) Histone modifications: Signalling receptors and potential elements of a heritable genetic code. Curr Opin Genet Dev 16:125-136.
    • (2006) Curr Opin Genet Dev , vol.16 , pp. 125-136
    • Nightingale, K.P.1    O'Neill, L.P.2    Turner, B.M.3
  • 47
    • 4544370533 scopus 로고    scopus 로고
    • Improved peptide identification in proteomics by two consecutive stages of mass spectrometric fragmentation
    • Olsen JV, Mann M (2004) Improved peptide identification in proteomics by two consecutive stages of mass spectrometric fragmentation. Proc Natl Acad Sci USA 101:13417-13422.
    • (2004) Proc Natl Acad Sci USA , vol.101 , pp. 13417-13422
    • Olsen, J.V.1    Mann, M.2
  • 48
    • 18744364184 scopus 로고    scopus 로고
    • The moving parts of the nucleolus
    • Olson MOJ, Dundr M (2005) The moving parts of the nucleolus. Histochem Cell Biol 123:203-216.
    • (2005) Histochem Cell Biol , vol.123 , pp. 203-216
    • Olson, M.O.J.1    Dundr, M.2
  • 50
    • 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
  • 51
    • 33748574525 scopus 로고    scopus 로고
    • Formation and nuclear export of preribosomes are functionally linker to the small-ubiquitin-related modifier pathway
    • Panse VG, Kressler D, Pauli A, Petfalski E, Gnadig M, Tollervey D, Hurt E (2006) Formation and nuclear export of preribosomes are functionally linker to the small-ubiquitin-related modifier pathway. Traffic 7:1311-1321.
    • (2006) Traffic , vol.7 , pp. 1311-1321
    • Panse, V.G.1    Kressler, D.2    Pauli, A.3    Petfalski, E.4    Gnadig, M.5    Tollervey, D.6    Hurt, E.7
  • 53
    • 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
  • 54
    • 0034611785 scopus 로고    scopus 로고
    • High mobility of proteins in the mammalian cell nucleus
    • Phair RD, Misteli T (2000) High mobility of proteins in the mammalian cell nucleus. Nature 404:604-609.
    • (2000) Nature , vol.404 , pp. 604-609
    • Phair, R.D.1    Misteli, T.2
  • 55
    • 33745690105 scopus 로고    scopus 로고
    • The Arabidopsis chromatin-modifying nuclear siRNA pathway involves a nucleolar RNA processing center
    • Pontes O, Li CF, Nunes PC, Haag J, Ream T, Vitins A, Jacobsen SE, Pikaard CS (2006) The Arabidopsis chromatin-modifying nuclear siRNA pathway involves a nucleolar RNA processing center. Cell 126:79-92.
    • (2006) Cell , vol.126 , pp. 79-92
    • Pontes, O.1    Li, C.F.2    Nunes, P.C.3    Haag, J.4    Ream, T.5    Vitins, A.6    Jacobsen, S.E.7    Pikaard, C.S.8
  • 56
    • 33746277552 scopus 로고    scopus 로고
    • Structure and function of the nucleolus in the spotlight
    • Raska I, Shaw PJ, Cmarko D (2006) Structure and function of the nucleolus in the spotlight. Curr Opin Cell Biol 18:325-334.
    • (2006) Curr Opin Cell Biol , vol.18 , pp. 325-334
    • Raska, I.1    Shaw, P.J.2    Cmarko, D.3
  • 57
    • 0037155853 scopus 로고    scopus 로고
    • Genes encoding calmodulin-binding proteins in the Arabidopsis genome
    • Reddy VS, Ali GS, Reddy AS (2002) Genes encoding calmodulin-binding proteins in the Arabidopsis genome. J Biol Chem 277:9840-9852.
    • (2002) J Biol Chem , vol.277 , pp. 9840-9852
    • Reddy, V.S.1    Ali, G.S.2    Reddy, A.S.3
  • 58
    • 33745026452 scopus 로고    scopus 로고
    • Delineation and modelling of a nucleolar retention signal in the coronavirus nucleocapsid protein
    • Reed ML, Dove BK, Jackson RM, Collins R, Brooks G, Hiscox JA (2006) Delineation and modelling of a nucleolar retention signal in the coronavirus nucleocapsid protein. Traffic 7:833-848.
    • (2006) Traffic , vol.7 , pp. 833-848
    • Reed, M.L.1    Dove, B.K.2    Jackson, R.M.3    Collins, R.4    Brooks, G.5    Hiscox, J.A.6
  • 59
    • 0032828715 scopus 로고    scopus 로고
    • A generic protein purification method for protein complex characterization and proteome exploration
    • Rigaut G, Shevchenko A, Rutz B, Wilm M, Mann M, Seraphin B (1999) A generic protein purification method for protein complex characterization and proteome exploration. Nat Biotechnol 17:1030-1032.
    • (1999) Nat Biotechnol , vol.17 , pp. 1030-1032
    • Rigaut, G.1    Shevchenko, A.2    Rutz, B.3    Wilm, M.4    Mann, M.5    Seraphin, B.6
  • 60
    • 1842430185 scopus 로고    scopus 로고
    • Improved tandem affinity purification tag and methods for isolation of protein heterocomplexes from plants
    • Rohila JS, Chen M, Cerny R, Fromm ME (2004) Improved tandem affinity purification tag and methods for isolation of protein heterocomplexes from plants. Plant J 38:172-181.
    • (2004) Plant J , vol.38 , pp. 172-181
    • Rohila, J.S.1    Chen, M.2    Cerny, R.3    Fromm, M.E.4
  • 62
    • 0344011603 scopus 로고    scopus 로고
    • Disruption of the nucleolus mediates stabilization of p53 in response to DNA damage and other stresses
    • Rubbi CP, Milner J (2003) Disruption of the nucleolus mediates stabilization of p53 in response to DNA damage and other stresses. EMBO J 22:6068-6077.
    • (2003) EMBO J , vol.22 , pp. 6068-6077
    • Rubbi, C.P.1    Milner, J.2
  • 63
    • 14844310253 scopus 로고    scopus 로고
    • An alternative tandem affinity purification strategy applied to Arabidopsis protein complex isolation
    • Rubio V, Shen Y, Saijo Y, Liu Y, Gusmaroli G, Dinesh-Kumar SP, Deng XW (2005) An alternative tandem affinity purification strategy applied to Arabidopsis protein complex isolation. Plant J 41:767-778.
    • (2005) Plant J , vol.41 , pp. 767-778
    • Rubio, V.1    Shen, Y.2    Saijo, Y.3    Liu, Y.4    Gusmaroli, G.5    Dinesh-Kumar, S.P.6    Deng, X.W.7
  • 66
    • 0034280113 scopus 로고    scopus 로고
    • Systematic subcellular localization of novel proteins identified by large-scale cDNA sequencing
    • Simpson JC, Wellenreuther R, Poustka A, Pepperkok R, Wiemann S (2000) Systematic subcellular localization of novel proteins identified by large-scale cDNA sequencing. EMBO Rep 1:287-292.
    • (2000) EMBO Rep , vol.1 , pp. 287-292
    • Simpson, J.C.1    Wellenreuther, R.2    Poustka, A.3    Pepperkok, R.4    Wiemann, S.5
  • 67
    • 17844396708 scopus 로고    scopus 로고
    • Identification of a novel nucleolar localization signal and degradation signal in Survivin-deltaEx3: A potential link between nucleolus and degradation
    • Song ZY, Wu M (2005) Identification of a novel nucleolar localization signal and degradation signal in Survivin-deltaEx3: A potential link between nucleolus and degradation. Oncogene 24:2723-2734.
    • (2005) Oncogene , vol.24 , pp. 2723-2734
    • Song, Z.Y.1    Wu, M.2
  • 68
    • 2542494838 scopus 로고    scopus 로고
    • Insights into the evolution of the nucleolus by an analysis of its protein domain repertoire
    • Staub E, Fiziev P, Rosenthal A, Hinzmann B (2004) Insights into the evolution of the nucleolus by an analysis of its protein domain repertoire. Bioessays 26:567-581.
    • (2004) Bioessays , vol.26 , pp. 567-581
    • Staub, E.1    Fiziev, P.2    Rosenthal, A.3    Hinzmann, B.4
  • 71
    • 0343376097 scopus 로고    scopus 로고
    • Difference gel electrophoresis: A single gel method for detecting changes in protein extracts
    • Unlu M, Morgan ME, Minden JS (1997) Difference gel electrophoresis: A single gel method for detecting changes in protein extracts. Electrophoresis 18:2071-2077.
    • (1997) Electrophoresis , vol.18 , pp. 2071-2077
    • Unlu, M.1    Morgan, M.E.2    Minden, J.S.3
  • 73
    • 13444263731 scopus 로고    scopus 로고
    • Organelle DB: A cross-species database of protein localization and function
    • Wiwatwattana N, Kumar A (2005) Organelle DB: A cross-species database of protein localization and function. Nucleic Acids Res 33:D598-D604.
    • (2005) Nucleic Acids Res , vol.33 , pp. D598-D604
    • Wiwatwattana, N.1    Kumar, A.2
  • 74
    • 33644845960 scopus 로고    scopus 로고
    • Comparative study of three proteomic quantitative methods, DIGE, cICAT, and iTRAQ, using 2D gel- or LC-MALDI TOF/TOF
    • Wu WW, Wang G, Baek SJ, Shen RF (2006) Comparative study of three proteomic quantitative methods, DIGE, cICAT, and iTRAQ, using 2D gel- or LC-MALDI TOF/TOF. J Proteome Res 5:651-658.
    • (2006) J Proteome Res , vol.5 , pp. 651-658
    • Wu, W.W.1    Wang, G.2    Baek, S.J.3    Shen, R.F.4
  • 75
    • 0038813707 scopus 로고    scopus 로고
    • In vivo analysis of nucleolar proteins modified by the yeast arginine methyltransferase Hmt1/Rmt1p
    • Xu C, Henry PA, Setya A, Henry MF (2003) In vivo analysis of nucleolar proteins modified by the yeast arginine methyltransferase Hmt1/Rmt1p. RNA 9:746-759.
    • (2003) RNA , vol.9 , pp. 746-759
    • Xu, C.1    Henry, P.A.2    Setya, A.3    Henry, M.F.4
  • 76
    • 21244504900 scopus 로고    scopus 로고
    • Genetic inactivation of the transcription factor TIF-I! leads to nucleolar disruption, cell cycle arrest, and p53-mediated apoptosis
    • Yuan XJ, Zhou YG, Casanova E, Chai MQ, Kiss E, Grone HJ, Schutz G, Grummt I (2005) Genetic inactivation of the transcription factor TIF-I! leads to nucleolar disruption, cell cycle arrest, and p53-mediated apoptosis. Mol Cell 19:77-87.
    • (2005) Mol Cell , vol.19 , pp. 77-87
    • Yuan, X.J.1    Zhou, Y.G.2    Casanova, E.3    Chai, M.Q.4    Kiss, E.5    Grone, H.J.6    Schutz, G.7    Grummt, I.8
  • 77
    • 33646269941 scopus 로고    scopus 로고
    • A perspective on the use of iTRAQ reagent technology for protein complex and profiling studies
    • Zieske LR (2006) A perspective on the use of iTRAQ reagent technology for protein complex and profiling studies. J Exp Bot 57:1501-1508.
    • (2006) J Exp Bot , vol.57 , pp. 1501-1508
    • Zieske, L.R.1


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.