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Volumn 8, Issue 7, 2009, Pages 3451-3463

Orthogonal separation techniques for the characterization of the yeast nuclear proteome

Author keywords

Mass spectrometry; Nucleus; Peptide IEF; Phosphocellulose P11; Prefractionation; Protein complex; Saccharomyces cerevisiae; SCX

Indexed keywords

CELLULOSE PHOSPHATE; DNA BINDING PROTEIN; NUCLEAR PROTEIN; PROTEOME;

EID: 67650385681     PISSN: 15353893     EISSN: None     Source Type: Journal    
DOI: 10.1021/pr9000948     Document Type: Article
Times cited : (15)

References (78)
  • 2
    • 55549141877 scopus 로고    scopus 로고
    • Histone H2A.Z and DNA methylation are mutually antagonistic chromatin marks
    • Zilberman, D.; Coleman-Derr, D.; Ballinger, T.; Henikoff, S. Histone H2A.Z and DNA methylation are mutually antagonistic chromatin marks. Nature 2008, 456 (7218), 125-9.
    • (2008) Nature , vol.456 , Issue.7218 , pp. 125-129
    • Zilberman, D.1    Coleman-Derr, D.2    Ballinger, T.3    Henikoff, S.4
  • 3
    • 0034708133 scopus 로고    scopus 로고
    • Proteomics for the pore
    • Blobel, G.; Wozniak, R. W. Proteomics for the pore. Nature 2000, 403 (6772), 835-6.
    • (2000) Nature , vol.403 , Issue.6772 , pp. 835-836
    • Blobel, G.1    Wozniak, R.W.2
  • 6
    • 56049084903 scopus 로고    scopus 로고
    • Carrera, I.; Treisman, J. E. Message in a nucleus: signaling to the transcriptional machinery. Curr. Opin. Genet. Dev. 2008, 18 (5), 397-403.
    • Carrera, I.; Treisman, J. E. Message in a nucleus: signaling to the transcriptional machinery. Curr. Opin. Genet. Dev. 2008, 18 (5), 397-403.
  • 9
    • 0034806227 scopus 로고    scopus 로고
    • The nuclear pore complex
    • REVIEWS0007
    • Adam, S. A. The nuclear pore complex. GenomeBiology 2001, 2 (9), REVIEWS0007.
    • (2001) GenomeBiology , vol.2 , Issue.9
    • Adam, S.A.1
  • 10
    • 0031028382 scopus 로고    scopus 로고
    • Nuclear localization of cyclin B1 mediates its biological activity and is regulated by phosphorylation
    • Li, J.; Meyer, A. N.; Donoghue, D. J. Nuclear localization of cyclin B1 mediates its biological activity and is regulated by phosphorylation. Proc. Natl. Acad. Sci. U.S.A. 1997, 94 (2), 502-7.
    • (1997) Proc. Natl. Acad. Sci. U.S.A , vol.94 , Issue.2 , pp. 502-507
    • Li, J.1    Meyer, A.N.2    Donoghue, D.J.3
  • 11
    • 0032533225 scopus 로고    scopus 로고
    • Glycogen synthase kinase-3beta regulates cyclin D1 proteolysis and subcellular localization
    • Diehl, J. A.; Cheng, M.; Roussel, M. F.; Sherr, C. J. Glycogen synthase kinase-3beta regulates cyclin D1 proteolysis and subcellular localization. Genes Dev. 1998, 12 (22), 3499-511.
    • (1998) Genes Dev , vol.12 , Issue.22 , pp. 3499-3511
    • Diehl, J.A.1    Cheng, M.2    Roussel, M.F.3    Sherr, C.J.4
  • 12
    • 0030768948 scopus 로고    scopus 로고
    • Cdc25 mitotic inducer targeted by chk1 DNA damage checkpoint kinase
    • Furnari, B.; Rhind, N.; Russell, P. Cdc25 mitotic inducer targeted by chk1 DNA damage checkpoint kinase. Science 1997, 277 (5331), 1495-7.
    • (1997) Science , vol.277 , Issue.5331 , pp. 1495-1497
    • Furnari, B.1    Rhind, N.2    Russell, P.3
  • 14
    • 0034738489 scopus 로고    scopus 로고
    • Diverse nuclear transport pathways regulate cell proliferation and oncogenesis
    • Hood, J. K.; Silver, P. A. Diverse nuclear transport pathways regulate cell proliferation and oncogenesis. Biochim. Biophys. Acta 2000, 1471 (1), M31-41.
    • (2000) Biochim. Biophys. Acta , vol.1471 , Issue.1
    • Hood, J.K.1    Silver, P.A.2
  • 16
    • 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, J. E.; Thoreen, C. C.; Licklider, L. J.; Gygi, S. P. Evaluation of multidimensional chromatography coupled with tandem mass spectrometry (LC/LC-MS/MS) for large-scale protein analysis: the yeast proteome. J. Proteome Res. 2003, 2 (1), 43-50.
    • (2003) J. Proteome Res , vol.2 , Issue.1 , pp. 43-50
    • Peng, J.1    Elias, J.E.2    Thoreen, C.C.3    Licklider, L.J.4    Gygi, S.P.5
  • 17
    • 55249096894 scopus 로고    scopus 로고
    • Comprehensive mass-spectrometry-based proteome quantification of haploid versus diploid yeast
    • de Godoy, L. M.; Olsen, J. V.; Cox, J.; Nielsen, M. L.; Hubner, N. C.; Frohlich, F.; Walther, T. C.; Mann, M. Comprehensive mass-spectrometry-based proteome quantification of haploid versus diploid yeast. Nature 2008, 455 (7217), 1251-4.
    • (2008) Nature , vol.455 , Issue.7217 , pp. 1251-1254
    • de Godoy, L.M.1    Olsen, J.V.2    Cox, J.3    Nielsen, M.L.4    Hubner, N.C.5    Frohlich, F.6    Walther, T.C.7    Mann, M.8
  • 18
    • 33644555054 scopus 로고    scopus 로고
    • Gavin, A. C.; Aloy, P.; Grandi, P.; Krause, R.; Boesche, M.; Marzioch, M.; Rau, C.; Jensen, L. J.; Bastuck, S.; Dumpelfeld, B.; Edelmann, A.; Heurtier, M. A.; Hoffman, V.; Hoefert, C.; Klein, K.; Hudak, M.; Michon, A. M.; Schelder, M.; Schirle, M.; Remor, M.; Rudi, T.; Hooper, S.; Bauer, A.; Bouwmeester, T.; Casari, G.; Drewes, G.; Neubauer, G.; Rick, J. M.; Kuster, B.; Bork, P.; Russell, R. B.; Superti-Furga, G. Proteome survey reveals modularity of the yeast cell machinery. Nature 2006, 440 (7084), 631-6.
    • Gavin, A. C.; Aloy, P.; Grandi, P.; Krause, R.; Boesche, M.; Marzioch, M.; Rau, C.; Jensen, L. J.; Bastuck, S.; Dumpelfeld, B.; Edelmann, A.; Heurtier, M. A.; Hoffman, V.; Hoefert, C.; Klein, K.; Hudak, M.; Michon, A. M.; Schelder, M.; Schirle, M.; Remor, M.; Rudi, T.; Hooper, S.; Bauer, A.; Bouwmeester, T.; Casari, G.; Drewes, G.; Neubauer, G.; Rick, J. M.; Kuster, B.; Bork, P.; Russell, R. B.; Superti-Furga, G. Proteome survey reveals modularity of the yeast cell machinery. Nature 2006, 440 (7084), 631-6.
  • 19
    • 0037306721 scopus 로고    scopus 로고
    • Protein complexes and proteome organization from yeast to man
    • Gavin, A. C.; Superti-Furga, G. Protein complexes and proteome organization from yeast to man. Curr. Opin. Chem. Biol. 2003, 7 (1), 21-7.
    • (2003) Curr. Opin. Chem. Biol , vol.7 , Issue.1 , pp. 21-27
    • Gavin, A.C.1    Superti-Furga, G.2
  • 20
    • 0037050004 scopus 로고    scopus 로고
    • Ho, Y.; Gruhler, A.; Heilbut, A.; Bader, G. D.; Moore, L.; Adams, S. L.; Millar, A.; Taylor, P.; Bennett, K.; Boutilier, K.; Yang, L.; Wolting, C.; Donaldson, I.; Schandorff, S.; Shewnarane, J.; Vo, M.; Taggart, J.; Goudreault, M.; Muskat, B.; Alfarano, C.; Dewar, D.; Lin, Z.; Michalickova, K.; Willems, A. R.; Sassi, H.; Nielsen, P. A.; Rasmussen, K. J.; Andersen, J. R.; Johansen, L. E.; Hansen, L. H.; Jespersen, H.; Podtelejnikov, A.; Nielsen, E.; Crawford, J.; Poulsen, V.; Sorensen, B. D.; Matthiesen, J.; Hendrickson, R. C.; Gleeson, F.; Pawson, T.; Moran, M. F.; Durocher, D.; Mann, M.; Hogue, C. W.; Figeys, D.; Tyers, M. Systematic identification of protein complexes in Saccharomyces cerevisiae by mass spectrometry. Nature 2002, 415 (6868), 180-3.
    • Ho, Y.; Gruhler, A.; Heilbut, A.; Bader, G. D.; Moore, L.; Adams, S. L.; Millar, A.; Taylor, P.; Bennett, K.; Boutilier, K.; Yang, L.; Wolting, C.; Donaldson, I.; Schandorff, S.; Shewnarane, J.; Vo, M.; Taggart, J.; Goudreault, M.; Muskat, B.; Alfarano, C.; Dewar, D.; Lin, Z.; Michalickova, K.; Willems, A. R.; Sassi, H.; Nielsen, P. A.; Rasmussen, K. J.; Andersen, J. R.; Johansen, L. E.; Hansen, L. H.; Jespersen, H.; Podtelejnikov, A.; Nielsen, E.; Crawford, J.; Poulsen, V.; Sorensen, B. D.; Matthiesen, J.; Hendrickson, R. C.; Gleeson, F.; Pawson, T.; Moran, M. F.; Durocher, D.; Mann, M.; Hogue, C. W.; Figeys, D.; Tyers, M. Systematic identification of protein complexes in Saccharomyces cerevisiae by mass spectrometry. Nature 2002, 415 (6868), 180-3.
  • 22
    • 33751074671 scopus 로고    scopus 로고
    • Characterisation of organellar proteomes: A guide to subcellular proteomic fractionation and analysis
    • Ho, E.; Hayen, A.; Wilkins, M. R. Characterisation of organellar proteomes: a guide to subcellular proteomic fractionation and analysis. Proteomics 2006, 6 (21), 5746-57.
    • (2006) Proteomics , vol.6 , Issue.21 , pp. 5746-5757
    • Ho, E.1    Hayen, A.2    Wilkins, M.R.3
  • 23
    • 51149109591 scopus 로고    scopus 로고
    • Gauthier, D. J.; Lazure, C. Complementary methods to assist subcellular fractionation in organellar proteomics. Expert Rev. Proteomics 2008, 5 (4), 603-17.
    • Gauthier, D. J.; Lazure, C. Complementary methods to assist subcellular fractionation in organellar proteomics. Expert Rev. Proteomics 2008, 5 (4), 603-17.
  • 25
    • 60649087511 scopus 로고    scopus 로고
    • A label free quantitative proteomic analysis of the Saccharomyces cerevisiae nucleus
    • Mosley, A. L.; Florens, L.; Wen, Z.; Washburn, M. P. A label free quantitative proteomic analysis of the Saccharomyces cerevisiae nucleus. J. Proteomics 2009, 72 (1), 110-20.
    • (2009) J. Proteomics , vol.72 , Issue.1 , pp. 110-120
    • Mosley, A.L.1    Florens, L.2    Wen, Z.3    Washburn, M.P.4
  • 26
    • 33745857712 scopus 로고    scopus 로고
    • In-gel isoelectric focusing of peptides as a tool for improved protein identification
    • Krijgsveld, J.; Gauci, S.; Dormeyer, W.; Heck, A. J. In-gel isoelectric focusing of peptides as a tool for improved protein identification. J. Proteome Res. 2006, 5 (7), 1721-30.
    • (2006) J. Proteome Res , vol.5 , Issue.7 , pp. 1721-1730
    • Krijgsveld, J.1    Gauci, S.2    Dormeyer, W.3    Heck, A.J.4
  • 27
    • 33745851905 scopus 로고    scopus 로고
    • Toward the complete yeast mitochondrial proteome: Multidimensional separation techniques for mitochondrial proteomics
    • Reinders, J.; Zahedi, R. P.; Pfanner, N.; Meisinger, C.; Sickmann, A. Toward the complete yeast mitochondrial proteome: multidimensional separation techniques for mitochondrial proteomics. J. Proteome Res. 2006, 5 (7), 1543-54.
    • (2006) J. Proteome Res , vol.5 , Issue.7 , pp. 1543-1554
    • Reinders, J.1    Zahedi, R.P.2    Pfanner, N.3    Meisinger, C.4    Sickmann, A.5
  • 28
    • 13244271374 scopus 로고    scopus 로고
    • A comparison of immobilized pH gradient isoelectric focusing and strong-cation-exchange chromatography as a first dimension in shotgun proteomics
    • Essader, A. S.; Cargile, B. J.; Bundy, J. L.; Stephenson, J. L., Jr. A comparison of immobilized pH gradient isoelectric focusing and strong-cation-exchange chromatography as a first dimension in shotgun proteomics. Proteomics 2005, 5 (1), 24-34.
    • (2005) Proteomics , vol.5 , Issue.1 , pp. 24-34
    • Essader, A.S.1    Cargile, B.J.2    Bundy, J.L.3    Stephenson Jr., J.L.4
  • 29
    • 45549093903 scopus 로고    scopus 로고
    • Online automated in vivo zebrafish phosphoproteomics: From large-scale analysis down to a single embryo
    • Lemeer, S.; Pinkse, M. W.; Mohammed, S.; van Breukelen, B.; den Hertog, J.; Slijper, M.; Heck, A. J. Online automated in vivo zebrafish phosphoproteomics: from large-scale analysis down to a single embryo. J. Proteome Res. 2008, 7 (4), 1555-64.
    • (2008) J. Proteome Res , vol.7 , Issue.4 , pp. 1555-1564
    • Lemeer, S.1    Pinkse, M.W.2    Mohammed, S.3    van Breukelen, B.4    den Hertog, J.5    Slijper, M.6    Heck, A.J.7
  • 30
    • 33749054454 scopus 로고    scopus 로고
    • Isolation and mass spectrometry of specific DNA binding proteins
    • Yaneva, M.; Tempst, P. Isolation and mass spectrometry of specific DNA binding proteins. Methods Mol. Biol. 2006, 338, 291-303.
    • (2006) Methods Mol. Biol , vol.338 , pp. 291-303
    • Yaneva, M.1    Tempst, P.2
  • 31
    • 33644861546 scopus 로고    scopus 로고
    • Immobilized pH gradient isoelectric focusing as a first-dimension separation in shotgun proteomics
    • Cargile, B. J.; Sevinsky, J. R.; Essader, A. S.; Stephenson, J. L., Jr.; Bundy, J. L. Immobilized pH gradient isoelectric focusing as a first-dimension separation in shotgun proteomics. J. Biomol. Tech. 2005, 16 (3), 181-9.
    • (2005) J. Biomol. Tech , vol.16 , Issue.3 , pp. 181-189
    • Cargile, B.J.1    Sevinsky, J.R.2    Essader, A.S.3    Stephenson Jr., J.L.4    Bundy, J.L.5
  • 32
    • 0035106351 scopus 로고    scopus 로고
    • Large-scale analysis of the yeast proteome by multidimensional protein identification technology
    • Washburn, M. P.; Wolters, D.; Yates, J. R., III. Large-scale analysis of the yeast proteome by multidimensional protein identification technology. Nat. Biotechnol. 2001, 19 (3), 242-7.
    • (2001) Nat. Biotechnol , vol.19 , Issue.3 , pp. 242-247
    • Washburn, M.P.1    Wolters, D.2    Yates III, J.R.3
  • 33
    • 44449132255 scopus 로고    scopus 로고
    • Phosphoproteome analysis of fission yeast
    • Wilson-Grady, J. T.; Villen, J.; Gygi, S. P. Phosphoproteome analysis of fission yeast. J. Proteome Res. 2008, 7 (3), 1088-97.
    • (2008) J. Proteome Res , vol.7 , Issue.3 , pp. 1088-1097
    • Wilson-Grady, J.T.1    Villen, J.2    Gygi, S.P.3
  • 34
    • 0035582244 scopus 로고    scopus 로고
    • An automated multidimensional protein identification technology for shotgun proteomics
    • Wolters, D. A.; Washburn, M. P.; Yates, J. R., III. An automated multidimensional protein identification technology for shotgun proteomics. Anal. Chem. 2001, 73 (23), 5683-90.
    • (2001) Anal. Chem , vol.73 , Issue.23 , pp. 5683-5690
    • Wolters, D.A.1    Washburn, M.P.2    Yates III, J.R.3
  • 35
    • 34447265519 scopus 로고    scopus 로고
    • pI-based phosphopeptide enrichment combined with nanoESI-MS
    • Hung, C. W.; Kubler, D.; Lehmann, W. D. pI-based phosphopeptide enrichment combined with nanoESI-MS. Electrophoresis 2007, 28 (12), 2044-52.
    • (2007) Electrophoresis , vol.28 , Issue.12 , pp. 2044-2052
    • Hung, C.W.1    Kubler, D.2    Lehmann, W.D.3
  • 36
    • 29144480261 scopus 로고    scopus 로고
    • Added value for tandem mass spectrometry shotgun proteomics data validation through isoelectric focusing of peptides
    • Heller, M.; Ye, M.; Michel, P. E.; Morier, P.; Stalder, D.; Junger, M. A.; Aebersold, R.; Reymond, F.; Rossier, J. S. Added value for tandem mass spectrometry shotgun proteomics data validation through isoelectric focusing of peptides. J. Proteome Res. 2005, 4 (6), 2273-82.
    • (2005) J. Proteome Res , vol.4 , Issue.6 , pp. 2273-2282
    • Heller, M.1    Ye, M.2    Michel, P.E.3    Morier, P.4    Stalder, D.5    Junger, M.A.6    Aebersold, R.7    Reymond, F.8    Rossier, J.S.9
  • 37
    • 33747881750 scopus 로고    scopus 로고
    • The general transcription machinery and general cofactors
    • Thomas, M. C.; Chiang, C. M. The general transcription machinery and general cofactors. Crit. Rev. Biochem. Mol. Biol. 2006, 41 (3), 105-78.
    • (2006) Crit. Rev. Biochem. Mol. Biol , vol.41 , Issue.3 , pp. 105-178
    • Thomas, M.C.1    Chiang, C.M.2
  • 38
    • 0025013883 scopus 로고
    • Components of the yeast spindle and spindle pole body
    • Rout, M. P.; Kilmartin, J. V. Components of the yeast spindle and spindle pole body. J. Cell Biol. 1990, 111 (5 Pt. 1), 1913-27.
    • (1990) J. Cell Biol , vol.111 , Issue.5 PART. 1 , pp. 1913-1927
    • Rout, M.P.1    Kilmartin, J.V.2
  • 40
    • 0037317228 scopus 로고    scopus 로고
    • Stop and go extraction tips for matrix-assisted laser desorption/ionization, nanoelectrospray, and LC/MS sample pretreatment in proteomics
    • Rappsilber, J.; Ishihama, Y.; Mann, M. Stop and go extraction tips for matrix-assisted laser desorption/ionization, nanoelectrospray, and LC/MS sample pretreatment in proteomics. Anal. Chem. 2003, 75 (3), 663-70.
    • (2003) Anal. Chem , vol.75 , Issue.3 , pp. 663-670
    • Rappsilber, J.1    Ishihama, Y.2    Mann, M.3
  • 41
    • 0037108887 scopus 로고    scopus 로고
    • Empirical statistical model to estimate the accuracy of peptide identifications made by MS/MS and database search
    • Keller, A.; Nesvizhskii, A. I.; Kolker, E.; Aebersold, R. Empirical statistical model to estimate the accuracy of peptide identifications made by MS/MS and database search. Anal. Chem. 2002, 74 (20), 5383-92.
    • (2002) Anal. Chem , vol.74 , Issue.20 , pp. 5383-5392
    • Keller, A.1    Nesvizhskii, A.I.2    Kolker, E.3    Aebersold, R.4
  • 42
    • 0042338362 scopus 로고    scopus 로고
    • A statistical model for identifying proteins by tandem mass spectrometry
    • Nesvizhskii, A. I.; Keller, A.; Kolker, E.; Aebersold, R. A statistical model for identifying proteins by tandem mass spectrometry. Anal. Chem. 2003, 75 (17), 4646-58.
    • (2003) Anal. Chem , vol.75 , Issue.17 , pp. 4646-4658
    • Nesvizhskii, A.I.1    Keller, A.2    Kolker, E.3    Aebersold, R.4
  • 43
    • 57649220813 scopus 로고    scopus 로고
    • A versatile peptide pI calculator for phosphorylated and N-terminal acetylated peptides experimentally tested using peptide isoelectric focusing
    • Gauci, S.; van Breukelen, B.; Lemeer, S. M.; Krijgsveld, J.; Heck, A. J. A versatile peptide pI calculator for phosphorylated and N-terminal acetylated peptides experimentally tested using peptide isoelectric focusing. Proteomics 2008.
    • (2008) Proteomics
    • Gauci, S.1    van Breukelen, B.2    Lemeer, S.M.3    Krijgsveld, J.4    Heck, A.J.5
  • 44
    • 1642485152 scopus 로고    scopus 로고
    • Immobilized pH gradients as a first dimension in shotgun proteomics and analysis of the accuracy of pI predictability of peptides
    • Cargile, B. J.; Talley, D. L.; Stephenson, J. L., Jr. Immobilized pH gradients as a first dimension in shotgun proteomics and analysis of the accuracy of pI predictability of peptides. Electrophoresis 2004, 25 (6), 936-45.
    • (2004) Electrophoresis , vol.25 , Issue.6 , pp. 936-945
    • Cargile, B.J.1    Talley, D.L.2    Stephenson Jr., J.L.3
  • 45
    • 0026802039 scopus 로고
    • Factors involved in specific transcription by mammalian RNA polymerase II. Identification and characterization of factor IIH
    • Flores, O.; Lu, H.; Reinberg, D. Factors involved in specific transcription by mammalian RNA polymerase II. Identification and characterization of factor IIH. J. Biol. Chem. 1992, 267 (4), 2786-93.
    • (1992) J. Biol. Chem , vol.267 , Issue.4 , pp. 2786-2793
    • Flores, O.1    Lu, H.2    Reinberg, D.3
  • 47
    • 0020119904 scopus 로고
    • Limited proteolysis of liver aldolase and fructose 1,6-bisphosphatase by lysosomal proteinases: Effect on complex formation
    • Pontremoli, S.; Melloni, E.; Michetti, M.; Salamino, F.; Sparatore, B.; Horecker, B. L. Limited proteolysis of liver aldolase and fructose 1,6-bisphosphatase by lysosomal proteinases: effect on complex formation. Proc. Natl. Acad. Sci. U.S.A. 1982, 79 (8), 2451-4.
    • (1982) Proc. Natl. Acad. Sci. U.S.A , vol.79 , Issue.8 , pp. 2451-2454
    • Pontremoli, S.1    Melloni, E.2    Michetti, M.3    Salamino, F.4    Sparatore, B.5    Horecker, B.L.6
  • 48
    • 0042235200 scopus 로고    scopus 로고
    • Partial reconstitution of human interstrand cross-link repair in vitro: Characterization of the roles of RPA and PCNA
    • Zhang, N.; Lu, X.; Legerski, R. J. Partial reconstitution of human interstrand cross-link repair in vitro: characterization of the roles of RPA and PCNA. Biochem. Biophys. Res. Commun. 2003, 309 (1), 71-8.
    • (2003) Biochem. Biophys. Res. Commun , vol.309 , Issue.1 , pp. 71-78
    • Zhang, N.1    Lu, X.2    Legerski, R.J.3
  • 49
    • 0018843370 scopus 로고
    • Replication of alfalfa mosaic virus RNA: Evidence for a soluble replicase in healthy and infected tobacco leaves
    • Chifflot, S.; Sommer, P.; Hartmann, D.; Stussi-Garaud, C.; Hirth, L. Replication of alfalfa mosaic virus RNA: evidence for a soluble replicase in healthy and infected tobacco leaves. Virology 1980, 100 (1), 91-100.
    • (1980) Virology , vol.100 , Issue.1 , pp. 91-100
    • Chifflot, S.1    Sommer, P.2    Hartmann, D.3    Stussi-Garaud, C.4    Hirth, L.5
  • 50
    • 0036269973 scopus 로고    scopus 로고
    • Proteomics of the eukaryotic transcription machinery: Identification of proteins associated with components of yeast TFIID by multidimensional mass spectrometry
    • Sanders, S. L.; Jennings, J.; Canutescu, A.; Link, A. J.; Weil, P. A. Proteomics of the eukaryotic transcription machinery: identification of proteins associated with components of yeast TFIID by multidimensional mass spectrometry. Mol. Cell. Biol. 2002, 22 (13), 4723-38.
    • (2002) Mol. Cell. Biol , vol.22 , Issue.13 , pp. 4723-4738
    • Sanders, S.L.1    Jennings, J.2    Canutescu, A.3    Link, A.J.4    Weil, P.A.5
  • 52
    • 40949091947 scopus 로고    scopus 로고
    • Proteomics of yeast mitochondria
    • Reinders, J.; Sickmann, A. Proteomics of yeast mitochondria. Methods Mol. Biol. 2007, 372, 543-57.
    • (2007) Methods Mol. Biol , vol.372 , pp. 543-557
    • Reinders, J.1    Sickmann, A.2
  • 53
  • 57
    • 33644874178 scopus 로고    scopus 로고
    • Leung, A. K.; Trinkle-Mulcahy, L.; Lam, Y. W.; Andersen, J. S.; Mann, M.; Lamond, A. I. NOPdb: Nucleolar Proteome Database. Nucleic Acids Res. 2006, 34 (Database issue), D218-20.
    • Leung, A. K.; Trinkle-Mulcahy, L.; Lam, Y. W.; Andersen, J. S.; Mann, M.; Lamond, A. I. NOPdb: Nucleolar Proteome Database. Nucleic Acids Res. 2006, 34 (Database issue), D218-20.
  • 59
    • 0036512117 scopus 로고    scopus 로고
    • Messenger-RNA-binding proteins and the messages they carry
    • Dreyfuss, G.; Kim, V. N.; Kataoka, N. Messenger-RNA-binding proteins and the messages they carry. Nat. Rev. Mol. Cell Biol. 2002, 3 (3), 195-205.
    • (2002) Nat. Rev. Mol. Cell Biol , vol.3 , Issue.3 , pp. 195-205
    • Dreyfuss, G.1    Kim, V.N.2    Kataoka, N.3
  • 60
    • 34249096783 scopus 로고    scopus 로고
    • Intranucleolar sites of ribosome biogenesis defined by the localization of early binding ribosomal proteins
    • Kruger, T.; Zentgraf, H.; Scheer, U. Intranucleolar sites of ribosome biogenesis defined by the localization of early binding ribosomal proteins. J. Cell Biol. 2007, 177 (4), 573-8.
    • (2007) J. Cell Biol , vol.177 , Issue.4 , pp. 573-578
    • Kruger, T.1    Zentgraf, H.2    Scheer, U.3
  • 61
    • 34247391127 scopus 로고    scopus 로고
    • Analysis of nucleolar protein dynamics reveals the nuclear degradation of ribosomal proteins
    • Lam, Y. W.; Lamond, A. I.; Mann, M.; Andersen, J. S. Analysis of nucleolar protein dynamics reveals the nuclear degradation of ribosomal proteins. Curr. Biol. 2007, 17 (9), 749-60.
    • (2007) Curr. Biol , vol.17 , Issue.9 , pp. 749-760
    • Lam, Y.W.1    Lamond, A.I.2    Mann, M.3    Andersen, J.S.4
  • 62
    • 34249982906 scopus 로고    scopus 로고
    • Nuclear export and cytoplasmic maturation of ribosomal subunits
    • Zemp, I.; Kutay, U. Nuclear export and cytoplasmic maturation of ribosomal subunits. FEBS Lett. 2007, 581 (15), 2783-93.
    • (2007) FEBS Lett , vol.581 , Issue.15 , pp. 2783-2793
    • Zemp, I.1    Kutay, U.2
  • 63
    • 85052429959 scopus 로고    scopus 로고
    • The nuclear ubiquitin-proteasome system: Visualization of proteasomes, protein aggregates, and proteolysis in the cell nucleus
    • von Mikecz, A.; Chen, M.; Rockel, T.; Scharf, A. The nuclear ubiquitin-proteasome system: visualization of proteasomes, protein aggregates, and proteolysis in the cell nucleus. Methods Mol. Biol. 2008, 463, 191-202.
    • (2008) Methods Mol. Biol , vol.463 , pp. 191-202
    • von Mikecz, A.1    Chen, M.2    Rockel, T.3    Scharf, A.4
  • 64
    • 29244480602 scopus 로고    scopus 로고
    • Proteasomes degrade proteins in focal subdomains of the human cell nucleus
    • Rockel, T. D.; Stuhlmann, D.; von Mikecz, A. Proteasomes degrade proteins in focal subdomains of the human cell nucleus. J. Cell Sci. 2005, 118 (Pt. 22), 5231-42.
    • (2005) J. Cell Sci , vol.118 , Issue.PART. 22 , pp. 5231-5242
    • Rockel, T.D.1    Stuhlmann, D.2    von Mikecz, A.3
  • 65
    • 0028080463 scopus 로고
    • TRiC-P5, a novel TCP1-related protein, is localized in the cytoplasm and in the nuclear matrix
    • Joly, E. C.; Tremblay, E.; Tanguay, R. M.; Wu, Y.; Bibor-Hardy, V. TRiC-P5, a novel TCP1-related protein, is localized in the cytoplasm and in the nuclear matrix. J. Cell Sci. 1994, 107 (Pt. 10), 2851-9.
    • (1994) J. Cell Sci , vol.107 , Issue.PART. 10 , pp. 2851-2859
    • Joly, E.C.1    Tremblay, E.2    Tanguay, R.M.3    Wu, Y.4    Bibor-Hardy, V.5
  • 67
    • 0035997387 scopus 로고    scopus 로고
    • Nuclear actin and actin-related proteins in chromatin remodeling
    • Olave, I. A.; Reck-Peterson, S. L.; Crabtree, G. R. Nuclear actin and actin-related proteins in chromatin remodeling. Annu. Rev. Biochem. 2002, 71, 755-81.
    • (2002) Annu. Rev. Biochem , vol.71 , pp. 755-781
    • Olave, I.A.1    Reck-Peterson, S.L.2    Crabtree, G.R.3
  • 71
    • 33750435187 scopus 로고    scopus 로고
    • Regulatory functions of nuclear hexokinase1 complex in glucose signaling
    • Cho, Y. H.; Yoo, S. D.; Sheen, J. Regulatory functions of nuclear hexokinase1 complex in glucose signaling. Cell 2006, 127 (3), 579-89.
    • (2006) Cell , vol.127 , Issue.3 , pp. 579-589
    • Cho, Y.H.1    Yoo, S.D.2    Sheen, J.3
  • 72
    • 40449137922 scopus 로고    scopus 로고
    • Inhibition of glucokinase translocation by AMP-activated protein kinase is associated with phosphorylation of both GKRP and 6-phosphofructo-2-kinase/fructose-2,6-bisphosphatase
    • Mukhtar, M. H.; Payne, V. A.; Arden, C.; Harbottle, A.; Khan, S.; Lange, A. J.; Agius, L. Inhibition of glucokinase translocation by AMP-activated protein kinase is associated with phosphorylation of both GKRP and 6-phosphofructo-2-kinase/fructose-2,6-bisphosphatase. Am. J. Physiol.: Regul., Integr. Comp. Physiol. 2008, 294 (3), R766-74.
    • (2008) Am. J. Physiol.: Regul., Integr. Comp. Physiol , vol.294 , Issue.3
    • Mukhtar, M.H.1    Payne, V.A.2    Arden, C.3    Harbottle, A.4    Khan, S.5    Lange, A.J.6    Agius, L.7
  • 73
    • 33748298941 scopus 로고    scopus 로고
    • Nutrient regulates Tor1 nuclear localization and association with rDNA promoter
    • Li, H.; Tsang, C. K.; Watkins, M.; Bertram, P. G.; Zheng, X. F. Nutrient regulates Tor1 nuclear localization and association with rDNA promoter. Nature 2006, 442 (7106), 1058-61.
    • (2006) Nature , vol.442 , Issue.7106 , pp. 1058-1061
    • Li, H.1    Tsang, C.K.2    Watkins, M.3    Bertram, P.G.4    Zheng, X.F.5
  • 74
    • 33846566203 scopus 로고    scopus 로고
    • TOR-in(g) the nucleus
    • Tsang, C. K.; Zheng, X. F. TOR-in(g) the nucleus. Cell Cycle 2007, 6 (1), 25-9.
    • (2007) Cell Cycle , vol.6 , Issue.1 , pp. 25-29
    • Tsang, C.K.1    Zheng, X.F.2
  • 75
    • 0029818391 scopus 로고    scopus 로고
    • Prenylated isoforms of yeast casein kinase, I. including the novel Yck3p, suppress the gcs1 blockage of cell proliferation from stationary phase
    • Wang, X.; Hoekstra, M. F.; DeMaggio, A. J.; Dhillon, N.; Vancura, A.; Kuret, J.; Johnston, G. C.; Singer, R. A.; Prenylated isoforms of yeast casein kinase, I. including the novel Yck3p, suppress the gcs1 blockage of cell proliferation from stationary phase. Mol. Cell. Biol. 1996, 16 (10), 5375-85.
    • (1996) Mol. Cell. Biol , vol.16 , Issue.10 , pp. 5375-5385
    • Wang, X.1    Hoekstra, M.F.2    DeMaggio, A.J.3    Dhillon, N.4    Vancura, A.5    Kuret, J.6    Johnston, G.C.7    Singer, R.A.8
  • 76
    • 14544272335 scopus 로고    scopus 로고
    • Regulation of nuclear transport: Central role in development and transformation
    • Poon, I. K.; Jans, D. A. Regulation of nuclear transport: central role in development and transformation. Traffic 2005, 6 (3), 173-86.
    • (2005) Traffic , vol.6 , Issue.3 , pp. 173-186
    • Poon, I.K.1    Jans, D.A.2
  • 77
    • 0033598989 scopus 로고    scopus 로고
    • Transport of proteins and RNAs in and out of the nucleus
    • Nakielny, S.; Dreyfuss, G. Transport of proteins and RNAs in and out of the nucleus. Cell 1999, 99 (7), 677-90.
    • (1999) Cell , vol.99 , Issue.7 , pp. 677-690
    • Nakielny, S.1    Dreyfuss, G.2
  • 78
    • 0042830859 scopus 로고    scopus 로고
    • Nucleocytoplasmic transport: Taking an inventory
    • Fried, H.; Kutay, U. Nucleocytoplasmic transport: taking an inventory. Cell. Mol. Life Sci. 2003, 60 (8), 1659-88.
    • (2003) Cell. Mol. Life Sci , vol.60 , Issue.8 , pp. 1659-1688
    • Fried, H.1    Kutay, U.2


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