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Volumn 77, Issue , 2012, Pages 521-530

Novel nucleolar isolation method reveals rapid response of human nucleolar proteomes to serum stimulation

Author keywords

Nucleolar isolation; Quantitative proteomics; Stable isotope labelling by amino acids in cell culture

Indexed keywords

KI 67 ANTIGEN; NUCLEOLIN;

EID: 84870390339     PISSN: 18743919     EISSN: 18767737     Source Type: Journal    
DOI: 10.1016/j.jprot.2012.09.031     Document Type: Article
Times cited : (15)

References (42)
  • 1
    • 18644372079 scopus 로고    scopus 로고
    • 60S pre-ribosome formation viewed from assembly in the nucleolus until export to the cytoplasm
    • Nissan T.A., Bassler J., Petfalski E., Tollervey D., Hurt E. 60S pre-ribosome formation viewed from assembly in the nucleolus until export to the cytoplasm. EMBO J 2002, 21:5539-5547.
    • (2002) EMBO J , vol.21 , pp. 5539-5547
    • Nissan, T.A.1    Bassler, J.2    Petfalski, E.3    Tollervey, D.4    Hurt, E.5
  • 2
    • 35648956087 scopus 로고    scopus 로고
    • Analysis of the in vivo assembly pathway of eukaryotic 40S ribosomal proteins
    • Ferreira-Cerca S., Poll G., Kuhn H., Neueder A., Jakob S., Tschochner H., et al. Analysis of the in vivo assembly pathway of eukaryotic 40S ribosomal proteins. Mol Cell 2007, 28:446-457.
    • (2007) Mol Cell , vol.28 , pp. 446-457
    • Ferreira-Cerca, S.1    Poll, G.2    Kuhn, H.3    Neueder, A.4    Jakob, S.5    Tschochner, H.6
  • 4
    • 33748582906 scopus 로고    scopus 로고
    • Crystal structure of a 70S ribosome-tRNA complex reveals functional interactions and rearrangements
    • Korostelev A., Trakhanov S., Laurberg M., Noller H.F. Crystal structure of a 70S ribosome-tRNA complex reveals functional interactions and rearrangements. Cell 2006, 126:1065-1077.
    • (2006) Cell , vol.126 , pp. 1065-1077
    • Korostelev, A.1    Trakhanov, S.2    Laurberg, M.3    Noller, H.F.4
  • 6
    • 0037205270 scopus 로고    scopus 로고
    • At the center of eukaryotic life
    • Moss T., Stefanovsky V.Y. At the center of eukaryotic life. Cell 2002, 109:545-548.
    • (2002) Cell , vol.109 , pp. 545-548
    • Moss, T.1    Stefanovsky, V.Y.2
  • 7
    • 0034114866 scopus 로고    scopus 로고
    • Nucleolar size indicates the rapidity of cell proliferation in cancer tissues
    • Derenzini M., Trere D., Pession A., Govoni M., Sirri V., Chieco P. Nucleolar size indicates the rapidity of cell proliferation in cancer tissues. J Pathol 2000, 191:181-186.
    • (2000) J Pathol , vol.191 , pp. 181-186
    • Derenzini, M.1    Trere, D.2    Pession, A.3    Govoni, M.4    Sirri, V.5    Chieco, P.6
  • 8
    • 0034174683 scopus 로고    scopus 로고
    • Proliferation assessment in breast cancer: a double-staining technique for AgNOR quantification in MIB-1 positive cells especially adapted for image cytometry
    • Lorenzato M., Abboud P., Lechki C., Browarnyj F., O'Donohue M.F., Ploton D., et al. Proliferation assessment in breast cancer: a double-staining technique for AgNOR quantification in MIB-1 positive cells especially adapted for image cytometry. Micron 2000, 31:151-159.
    • (2000) Micron , vol.31 , pp. 151-159
    • Lorenzato, M.1    Abboud, P.2    Lechki, C.3    Browarnyj, F.4    O'Donohue, M.F.5    Ploton, D.6
  • 9
    • 0035995289 scopus 로고    scopus 로고
    • Conventional and nonconventional roles of the nucleolus
    • Olson M.O., Hingorani K., Szebeni A. Conventional and nonconventional roles of the nucleolus. Int Rev Cytol 2002, 219:199-266.
    • (2002) Int Rev Cytol , vol.219 , pp. 199-266
    • Olson, M.O.1    Hingorani, K.2    Szebeni, A.3
  • 10
    • 0032169650 scopus 로고    scopus 로고
    • The plurifunctional nucleolus
    • Pederson T. The plurifunctional nucleolus. Nucleic Acids Res 1998, 26:3871-3876.
    • (1998) Nucleic Acids Res , vol.26 , pp. 3871-3876
    • Pederson, T.1
  • 12
    • 57349182457 scopus 로고    scopus 로고
    • A putative function of the nucleolus in the assembly or maturation of specialized messenger ribonucleoprotein complexes
    • Jellbauer S., Jansen R.P. A putative function of the nucleolus in the assembly or maturation of specialized messenger ribonucleoprotein complexes. RNA Biol 2008, 5:225-229.
    • (2008) RNA Biol , vol.5 , pp. 225-229
    • Jellbauer, S.1    Jansen, R.P.2
  • 13
    • 0345133268 scopus 로고    scopus 로고
    • Modulation of RNA editing by functional nucleolar sequestration of ADAR2
    • Sansam C.L., Wells K.S., Emeson R.B. Modulation of RNA editing by functional nucleolar sequestration of ADAR2. Proc Natl Acad Sci U S A 2003, 100:14018-14023.
    • (2003) Proc Natl Acad Sci U S A , vol.100 , pp. 14018-14023
    • Sansam, C.L.1    Wells, K.S.2    Emeson, R.B.3
  • 14
    • 4644334616 scopus 로고    scopus 로고
    • Cell-specific nucleolar localization of TBP-related factor 2
    • Kieffer-Kwon P., Martianov I., Davidson I. Cell-specific nucleolar localization of TBP-related factor 2. Mol Biol Cell 2004, 15:4356-4368.
    • (2004) Mol Biol Cell , vol.15 , pp. 4356-4368
    • Kieffer-Kwon, P.1    Martianov, I.2    Davidson, I.3
  • 15
    • 4444230597 scopus 로고    scopus 로고
    • Nucleolar localization of the human telomeric repeat binding factor 2 (TRF2)
    • Zhang S., Hemmerich P., Grosse F. Nucleolar localization of the human telomeric repeat binding factor 2 (TRF2). J Cell Sci 2004, 117:3935-3945.
    • (2004) J Cell Sci , vol.117 , pp. 3935-3945
    • Zhang, S.1    Hemmerich, P.2    Grosse, F.3
  • 17
    • 4544330157 scopus 로고    scopus 로고
    • Quantitative kinetic analysis of nucleolar breakdown and reassembly during mitosis in live human cells
    • Leung A.K., Gerlich D., Miller G., Lyon C., Lam Y.W., Lleres D., et al. Quantitative kinetic analysis of nucleolar breakdown and reassembly during mitosis in live human cells. J Cell Biol 2004, 166:787-800.
    • (2004) J Cell Biol , vol.166 , pp. 787-800
    • Leung, A.K.1    Gerlich, D.2    Miller, G.3    Lyon, C.4    Lam, Y.W.5    Lleres, D.6
  • 20
    • 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, 17:749-760.
    • (2007) Curr Biol , vol.17 , pp. 749-760
    • Lam, Y.W.1    Lamond, A.I.2    Mann, M.3    Andersen, J.S.4
  • 23
    • 80051504639 scopus 로고    scopus 로고
    • Quantitative nucleolar proteomics reveals nuclear re-organization during stress-induced senescence in mouse fibroblast
    • Kar B., Liu B., Zhou Z., Lam Y.W. Quantitative nucleolar proteomics reveals nuclear re-organization during stress-induced senescence in mouse fibroblast. BMC Cell Biol 2011, 12:33.
    • (2011) BMC Cell Biol , vol.12 , pp. 33
    • Kar, B.1    Liu, B.2    Zhou, Z.3    Lam, Y.W.4
  • 24
    • 77649159264 scopus 로고    scopus 로고
    • A quantitative proteomics analysis of subcellular proteome localization and changes induced by DNA damage
    • Boisvert F.M., Lam Y.W., Lamont D., Lamond A.I. A quantitative proteomics analysis of subcellular proteome localization and changes induced by DNA damage. Mol Cell Proteomics 2010, 9:457-470.
    • (2010) Mol Cell Proteomics , vol.9 , pp. 457-470
    • Boisvert, F.M.1    Lam, Y.W.2    Lamont, D.3    Lamond, A.I.4
  • 26
    • 36749100886 scopus 로고    scopus 로고
    • Toward a high-resolution view of nuclear dynamics
    • Trinkle-Mulcahy L., Lamond A.I. Toward a high-resolution view of nuclear dynamics. Science 2007, 318:1402-1407.
    • (2007) Science , vol.318 , pp. 1402-1407
    • Trinkle-Mulcahy, L.1    Lamond, A.I.2
  • 27
    • 83055176400 scopus 로고    scopus 로고
    • Regulation of intrahepatic biliary duct morphogenesis by Claudin 15-like b
    • Cheung I.D., Bagnat M., Ma T.P., Datta A., Evason K., Moore J.C., et al. Regulation of intrahepatic biliary duct morphogenesis by Claudin 15-like b. Dev Biol 2012, 361:68-78.
    • (2012) Dev Biol , vol.361 , pp. 68-78
    • Cheung, I.D.1    Bagnat, M.2    Ma, T.P.3    Datta, A.4    Evason, K.5    Moore, J.C.6
  • 28
    • 77957977633 scopus 로고    scopus 로고
    • Biochemical characterization of the cell-biomaterial interface by quantitative proteomics
    • Tong W.Y., Liang Y.M., Tam V., Yip H.K., Kao Y.T., Cheung K.M., et al. Biochemical characterization of the cell-biomaterial interface by quantitative proteomics. Mol Cell Proteomics 2010, 9:2089-2098.
    • (2010) Mol Cell Proteomics , vol.9 , pp. 2089-2098
    • Tong, W.Y.1    Liang, Y.M.2    Tam, V.3    Yip, H.K.4    Kao, Y.T.5    Cheung, K.M.6
  • 30
    • 3242715867 scopus 로고    scopus 로고
    • Essential role of ribosomal protein L11 in mediating growth inhibition-induced p53 activation
    • Bhat K.P., Itahana K., Jin A., Zhang Y. Essential role of ribosomal protein L11 in mediating growth inhibition-induced p53 activation. EMBO J 2004, 23:2402-2412.
    • (2004) EMBO J , vol.23 , pp. 2402-2412
    • Bhat, K.P.1    Itahana, K.2    Jin, A.3    Zhang, Y.4
  • 31
    • 0022343076 scopus 로고
    • Alterations in immunolocalization of the phosphoprotein B23 in HeLa cells during serum starvation
    • Chan P.K., Aldrich M., Busch H. Alterations in immunolocalization of the phosphoprotein B23 in HeLa cells during serum starvation. Exp Cell Res 1985, 161:101-110.
    • (1985) Exp Cell Res , vol.161 , pp. 101-110
    • Chan, P.K.1    Aldrich, M.2    Busch, H.3
  • 33
    • 0035895621 scopus 로고    scopus 로고
    • Growth factor-dependent signaling and cell cycle progression
    • Jones S.M., Kazlauskas A. Growth factor-dependent signaling and cell cycle progression. FEBS Lett 2001, 490:110-116.
    • (2001) FEBS Lett , vol.490 , pp. 110-116
    • Jones, S.M.1    Kazlauskas, A.2
  • 34
    • 44649133144 scopus 로고    scopus 로고
    • Effect of serum starvation and chemical inhibitors on cell cycle synchronization of canine dermal fibroblasts
    • Khammanit R., Chantakru S., Kitiyanant Y., Saikhun J. Effect of serum starvation and chemical inhibitors on cell cycle synchronization of canine dermal fibroblasts. Theriogenology 2008, 70:27-34.
    • (2008) Theriogenology , vol.70 , pp. 27-34
    • Khammanit, R.1    Chantakru, S.2    Kitiyanant, Y.3    Saikhun, J.4
  • 36
    • 0036154096 scopus 로고    scopus 로고
    • Specific interaction of Smn, the spinal muscular atrophy determining gene product, with hnRNP-R and gry-rbp/hnRNP-Q: a role for Smn in RNA processing in motor axons?
    • Rossoll W., Kroning A.K., Ohndorf U.M., Steegborn C., Jablonka S., Sendtner M. Specific interaction of Smn, the spinal muscular atrophy determining gene product, with hnRNP-R and gry-rbp/hnRNP-Q: a role for Smn in RNA processing in motor axons?. Hum Mol Genet 2002, 11:93-105.
    • (2002) Hum Mol Genet , vol.11 , pp. 93-105
    • Rossoll, W.1    Kroning, A.K.2    Ohndorf, U.M.3    Steegborn, C.4    Jablonka, S.5    Sendtner, M.6
  • 37
    • 77955272369 scopus 로고    scopus 로고
    • Regulation of post-translational protein arginine methylation during HeLa cell cycle
    • Kim C., Lim Y., Yoo B.C., Won N.H., Kim S., Kim G. Regulation of post-translational protein arginine methylation during HeLa cell cycle. Biochim Biophys Acta 2010, 1800:977-985.
    • (2010) Biochim Biophys Acta , vol.1800 , pp. 977-985
    • Kim, C.1    Lim, Y.2    Yoo, B.C.3    Won, N.H.4    Kim, S.5    Kim, G.6
  • 38
    • 79959283747 scopus 로고    scopus 로고
    • The nucleolar GTP-binding proteins Gnl2 and nucleostemin are required for retinal neurogenesis in developing zebrafish
    • Paridaen J.T., Janson E., Utami K.H., Pereboom T.C., Essers P.B., van Rooijen C., et al. The nucleolar GTP-binding proteins Gnl2 and nucleostemin are required for retinal neurogenesis in developing zebrafish. Dev Biol 2011, 355:286-301.
    • (2011) Dev Biol , vol.355 , pp. 286-301
    • Paridaen, J.T.1    Janson, E.2    Utami, K.H.3    Pereboom, T.C.4    Essers, P.B.5    van Rooijen, C.6
  • 39
    • 65549111786 scopus 로고    scopus 로고
    • DNA-dependent protein kinase (DNA-PK)-dependent cisplatin-induced loss of nucleolar facilitator of chromatin transcription (FACT) and regulation of cisplatin sensitivity by DNA-PK and FACT
    • Dejmek J., Iglehart J.D., Lazaro J.B. DNA-dependent protein kinase (DNA-PK)-dependent cisplatin-induced loss of nucleolar facilitator of chromatin transcription (FACT) and regulation of cisplatin sensitivity by DNA-PK and FACT. Mol Cancer Res 2009, 7:581-591.
    • (2009) Mol Cancer Res , vol.7 , pp. 581-591
    • Dejmek, J.1    Iglehart, J.D.2    Lazaro, J.B.3
  • 40
    • 31944443932 scopus 로고    scopus 로고
    • Ki-67 protein is associated with ribosomal RNA transcription in quiescent and proliferating cells
    • Bullwinkel J., Baron-Luhr B., Ludemann A., Wohlenberg C., Gerdes J., Scholzen T. Ki-67 protein is associated with ribosomal RNA transcription in quiescent and proliferating cells. J Cell Physiol 2006, 206:624-635.
    • (2006) J Cell Physiol , vol.206 , pp. 624-635
    • Bullwinkel, J.1    Baron-Luhr, B.2    Ludemann, A.3    Wohlenberg, C.4    Gerdes, J.5    Scholzen, T.6
  • 41
    • 0037196872 scopus 로고    scopus 로고
    • The utility of Ki-67 and BrdU as proliferative markers of adult neurogenesis
    • Kee N., Sivalingam S., Boonstra R., Wojtowicz J.M. The utility of Ki-67 and BrdU as proliferative markers of adult neurogenesis. J Neurosci Methods 2002, 115:97-105.
    • (2002) J Neurosci Methods , vol.115 , pp. 97-105
    • Kee, N.1    Sivalingam, S.2    Boonstra, R.3    Wojtowicz, J.M.4
  • 42
    • 27244443082 scopus 로고    scopus 로고
    • Proliferation marker Ki-67 in early breast cancer
    • Urruticoechea A., Smith I.E., Dowsett M. Proliferation marker Ki-67 in early breast cancer. J Clin Oncol 2005, 23:7212-7220.
    • (2005) J Clin Oncol , vol.23 , pp. 7212-7220
    • Urruticoechea, A.1    Smith, I.E.2    Dowsett, M.3


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.