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Volumn , Issue SUPPL.49, 2010, Pages

Purification of ribosomes from human cell lines

Author keywords

Cell fractionation; Ribosome; Translation

Indexed keywords

NUCLEOLIN; RIBOSOME PROTEIN; RIBOSOME RNA; RIBOZYME;

EID: 79953187584     PISSN: 19342500     EISSN: 19342616     Source Type: Journal    
DOI: 10.1002/0471143030.cb0340s49     Document Type: Article
Times cited : (45)

References (48)
  • 1
    • 79953209433 scopus 로고
    • Role of the ribonucleoprotein particle in protein synthesis and the effects of growth hormone
    • Balis, M.E., Samarth, K.D., Hamilton, M.G., and Petermann, M.L. 1958. Role of the ribonucleoprotein particle in protein synthesis and the effects of growth hormone. J. Biol. Chem. 233:1152-1155.
    • (1958) J. Biol. Chem. , vol.233 , pp. 1152-1155
    • Balis, M.E.1    Samarth, K.D.2    Hamilton, M.G.3    Petermann, M.L.4
  • 2
    • 0034637111 scopus 로고    scopus 로고
    • The complete atomic structure of the large ribosomal subunit at 2.4 Å resolution
    • Ban, N., Nissen, P., Hansen, J.H., Moore, P.B., and Steitz, T.A. 2000. The complete atomic structure of the large ribosomal subunit at 2.4 Å resolution. Science 289:905-920.
    • (2000) Science , vol.289 , pp. 905-920
    • Ban, N.1    Nissen, P.2    Hansen, J.H.3    Moore, P.B.4    Steitz, T.A.5
  • 4
    • 75649107664 scopus 로고    scopus 로고
    • Uncoupling ribosome biogenesis regulation from RNA polymerase I activity during herpes simplex virus type 1 infection
    • Belin, S., Kindbeiter, K., Hacot, S., Albaret, M.A., Roca-Martinez, J.X., Therizols, G., Grosso, R., and Diaz, J.J. 2010. Uncoupling ribosome biogenesis regulation from RNA polymerase I activity during herpes simplex virus type 1 infection. RNA 16:131-140.
    • (2010) RNA , vol.16 , pp. 131-140
    • Belin, S.1    Kindbeiter, K.2    Hacot, S.3    Albaret, M.A.4    Roca-Martinez, J.X.5    Therizols, G.6    Grosso, R.7    Diaz, J.J.8
  • 5
    • 0034636956 scopus 로고    scopus 로고
    • Structural biology. The ribosome is a ribozyme
    • Cech, T.R. 2000. Structural biology. The ribosome is a ribozyme. Science 289:878-879.
    • (2000) Science , vol.289 , pp. 878-879
    • Cech, T.R.1
  • 6
    • 0030598855 scopus 로고    scopus 로고
    • The primary structure of rat ribosomal protein L10: Relationship to a Jun-binding protein and to a putative Wilms' tumor suppressor
    • Chan, Y.L., Diaz, J.J., Denoroy, L., Madjar, J.J., and Wool, I.G. 1996. The primary structure of rat ribosomal protein L10: Relationship to a Jun-binding protein and to a putative Wilms' tumor suppressor. Biochem. Biophys. Res. Commun. 225:952-956.
    • (1996) Biochem. Biophys. Res. Commun. , vol.225 , pp. 952-956
    • Chan, Y.L.1    Diaz, J.J.2    Denoroy, L.3    Madjar, J.J.4    Wool, I.G.5
  • 9
    • 0036629250 scopus 로고    scopus 로고
    • rRNA modifications and ribosome function
    • Decatur, W.A. and Fournier, M.J. 2002. rRNA modifications and ribosome function. Trends Biochem. Sci. 27:344-351.
    • (2002) Trends Biochem. Sci. , vol.27 , pp. 344-351
    • Decatur, W.A.1    Fournier, M.J.2
  • 10
    • 0024381517 scopus 로고
    • Increase in ribosomal protein S6 phosphorylation is due to verbB-transforming activity and not to verbA mitogenic activity in avian erythroblastosis virus-infected chicken embryo fibroblasts
    • Diaz, J.J., Gandrillon, O., Hentzen, D., Leguellic, D., Samarut, J., and Madjar, J.J. 1989. Increase in ribosomal protein S6 phosphorylation is due to verbB-transforming activity and not to verbA mitogenic activity in avian erythroblastosis virus-infected chicken embryo fibroblasts. Oncogene Res. 4:163-175.
    • (1989) Oncogene Res , vol.4 , pp. 163-175
    • Diaz, J.J.1    Gandrillon, O.2    Hentzen, D.3    Leguellic, D.4    Samarut, J.5    Madjar, J.J.6
  • 11
    • 0027481858 scopus 로고
    • The herpes simplex virus type 1 US11 gene product is a phosphorylated protein found to be non-specifically associated with both ribosomal subunits
    • Diaz, J.J., Simonin, D., Masse, T., Deviller, P., Kindbeiter, K., Denoroy, L., and Madjar, J.J. 1993. The herpes simplex virus type 1 US11 gene product is a phosphorylated protein found to be non-specifically associated with both ribosomal subunits. J. Gen. Virol. 74:397-406.
    • (1993) J. Gen. Virol. , vol.74 , pp. 397-406
    • Diaz, J.J.1    Simonin, D.2    Masse, T.3    Deviller, P.4    Kindbeiter, K.5    Denoroy, L.6    Madjar, J.J.7
  • 12
    • 13344276604 scopus 로고    scopus 로고
    • Post-transcriptional transactivation of human retroviral envelope glycoprotein expression by herpes simplex virus Us11 protein
    • Diaz, J.J., Dodon, M.D., Schaerer-Ulthurralt, N., Simonin, D., Kindbeiter, K., Gazzolo, L., and Madjar, J.J. 1996. Post-transcriptional transactivation of human retroviral envelope glycoprotein expression by herpes simplex virus Us11 protein. Nature 379:273-277.
    • (1996) Nature , vol.379 , pp. 273-277
    • Diaz, J.J.1    Dodon, M.D.2    Schaerer-Ulthurralt, N.3    Simonin, D.4    Kindbeiter, K.5    Gazzolo, L.6    Madjar, J.J.7
  • 15
    • 39849092319 scopus 로고    scopus 로고
    • One-dimensional SDS gel electrophoresis of proteins
    • Gallagher, S.R. 2006. One-dimensional SDS gel electrophoresis of proteins. Curr. Protoc. Mol. Biol. 75:10.2A.1-10.2A.37.
    • (2006) Curr. Protoc. Mol. Biol. , vol.75
    • Gallagher, S.R.1
  • 16
    • 0037563355 scopus 로고    scopus 로고
    • Very alkaline immobilized pH gradients for two-dimensional electrophoresis of ribosomal and nuclear proteins
    • Görg, A., Obermaier, C., Boguth, G., Csordas, A., Diaz, J.J., and Madjar, J.J. 1997. Very alkaline immobilized pH gradients for two-dimensional electrophoresis of ribosomal and nuclear proteins. Electrophoresis 18:328-337.
    • (1997) Electrophoresis , vol.18 , pp. 328-337
    • Görg, A.1    Obermaier, C.2    Boguth, G.3    Csordas, A.4    Diaz, J.J.5    Madjar, J.J.6
  • 17
    • 0035321969 scopus 로고    scopus 로고
    • Identification of ribosome-associated viral and cellular basic proteins during the course of infection with herpes simplex virus type 1
    • Greco, A., Bienvenut, W., Sanchez, J.C., Kindbeiter, K., Hochstrasser, D., Madjar, J.J., and Diaz, J.J. 2001. Identification of ribosome-associated viral and cellular basic proteins during the course of infection with herpes simplex virus type 1. Proteomics 1:545-549.
    • (2001) Proteomics , vol.1 , pp. 545-549
    • Greco, A.1    Bienvenut, W.2    Sanchez, J.C.3    Kindbeiter, K.4    Hochstrasser, D.5    Madjar, J.J.6    Diaz, J.J.7
  • 18
    • 34248543639 scopus 로고    scopus 로고
    • Cells depleted for RPS19, a protein associated with Diamond Blackfan Anemia, show defects in 18S ribosomal RNA synthesis and small ribosomal subunit production
    • Idol, R.A., Robledo. S., Du, H.Y., Crimmins, D.L., Wilson, D.B., Ladenson, J.H., Besler, M., and Mason, P.J. 2007. Cells depleted for RPS19, a protein associated with Diamond Blackfan Anemia, show defects in 18S ribosomal RNA synthesis and small ribosomal subunit production. Blood Cells Mol. Dis. 39:35-43.
    • (2007) Blood Cells Mol. Dis. , vol.39 , pp. 35-43
    • Idol, R.A.1    Robledo, S.2    Du, H.Y.3    Crimmins, D.L.4    Wilson, D.B.5    Ladenson, J.H.6    Besler, M.7    Mason, P.J.8
  • 19
    • 35548973466 scopus 로고    scopus 로고
    • Functional specificity among ribosomal proteins regulates gene expression
    • Komili, S., Farny, N.G., Roth, F.P., and Silver, P.A. 2007. Functional specificity among ribosomal proteins regulates gene expression. Cell 131:557-571.
    • (2007) Cell , vol.131 , pp. 557-571
    • Komili, S.1    Farny, N.G.2    Roth, F.P.3    Silver, P.A.4
  • 20
    • 0011719748 scopus 로고
    • Preparation of ribosomes and ribosomal proteins from cultured cells
    • (J.E. Celis, ed.), Academic Press, New York
    • Madjar, J.J. 1994. Preparation of ribosomes and ribosomal proteins from cultured cells. In Cell Biology: A Laboratory Handbook (J.E. Celis, ed.) pp. 657-661. Academic Press, New York.
    • (1994) Cell Biology: A Laboratory Handbook , pp. 657-661
    • Madjar, J.J.1
  • 21
    • 0019347738 scopus 로고
    • Bombyx mori L. ribosomal proteins: Resolution, nomenclature, molecular weights and in vivo phosphorylation
    • Madjar, J.J. and Fournier, A. 1981. Bombyx mori L. ribosomal proteins: Resolution, nomenclature, molecular weights and in vivo phosphorylation. Mol. Gen. Gene. 182:273-278.
    • (1981) Mol. Gen. Gene. , vol.182 , pp. 273-278
    • Madjar, J.J.1    Fournier, A.2
  • 22
    • 0017499788 scopus 로고
    • Comparison of the protein content of free and membrane-bound rat liver polysomes and of the derived subunits
    • Madjar, J.J., Arpin, M., Marion, M.J., and Reboud, J.P. 1977. Comparison of the protein content of free and membrane-bound rat liver polysomes and of the derived subunits. Mol. Biol. Rep. 3:289-296.
    • (1977) Mol. Biol. Rep. , vol.3 , pp. 289-296
    • Madjar, J.J.1    Arpin, M.2    Marion, M.J.3    Reboud, J.P.4
  • 23
    • 0018292212 scopus 로고
    • Spot position of rat liver ribosomal proteins by four different two-dimensional electrophoreses in polyacrylamide gel
    • Madjar, J.J., Arpin, M., Buisson, M., and Reboud, P. 1979. Spot position of rat liver ribosomal proteins by four different two-dimensional electrophoreses in polyacrylamide gel. Mol. Gen. Genet. 171:121-134.
    • (1979) Mol. Gen. Genet. , vol.171 , pp. 121-134
    • Madjar, J.J.1    Arpin, M.2    Buisson, M.3    Reboud, P.4
  • 24
    • 0023660020 scopus 로고
    • Single crystals of large ribosomal particles from Halobacterium marismortui diffract to 6 Å
    • Makowski, I., Frolow, F., Saper, M.A., Shoham, M., Whitmann, H.G., and Yonath, A. 1987. Single crystals of large ribosomal particles from Halobacterium marismortui diffract to 6 Å. J. Mol. Biol. 193:819-822.
    • (1987) J. Mol. Biol. , vol.193 , pp. 819-822
    • Makowski, I.1    Frolow, F.2    Saper, M.A.3    Shoham, M.4    Whitmann, H.G.5    Yonath, A.6
  • 25
    • 0025202576 scopus 로고
    • Herpes simplex virus type-1-induced stimulation of ribosomal protein S6 phosphoxrylation is inhibited in neomycin-treated human epidermoid carcinoma 2 cells and in rastransformed cells
    • Massé, T., Garcin, D., Jacquemont, B., and Madjar, J.J. 1990a. Herpes simplex virus type-1-induced stimulation of ribosomal protein S6 phosphorylation is inhibited in neomycin-treated human epidermoid carcinoma 2 cells and in rastransformed cells. Eur. J. Biochem. 194:287-291.
    • (1990) Eur. J. Biochem. , vol.194 , pp. 287-291
    • Massé, T.1    Garcin, D.2    Jacquemont, B.3    Madjar, J.J.4
  • 26
    • 0025189709 scopus 로고
    • Ribosome and protein synthesis modifications after infection of human epidermoid carcinoma cells with herpes simplex virus type 1
    • Massé, T., Garcin, D., Jacquemont, B., and Nadjar, J.J. 1990b. Ribosome and protein synthesis modifications after infection of human epidermoid carcinoma cells with herpes simplex virus type 1. Mol. Gen. Genet. 220:377-388.
    • (1990) Mol. Gen. Genet. , vol.220 , pp. 377-388
    • Massé, T.1    Garcin, D.2    Jacquemont, B.3    Nadjar, J.J.4
  • 27
    • 0037062958 scopus 로고    scopus 로고
    • The involvement of RNA in ribosome function
    • Moore, P.B. and Steitz, T.A. 2002. The involvement of RNA in ribosome function. Nature 418:229-235.
    • (2002) Nature , vol.418 , pp. 229-235
    • Moore, P.B.1    Steitz, T.A.2
  • 28
    • 77951431225 scopus 로고    scopus 로고
    • Ribosomopathies: Human disorders of ribosome dysfunction
    • Narla, A. and Ebert, B.L. 2010. Ribosomopathies: Human disorders of ribosome dysfunction. Blood 115:3196-3205.
    • (2010) Blood , vol.115 , pp. 3196-3205
    • Narla, A.1    Ebert, B.L.2
  • 29
    • 0034637161 scopus 로고    scopus 로고
    • The structural basis of ribosome activity in peptide bond synthesis
    • Nissen, P., Hansen, J., Ban, N., Moore, P.B., and Steitz, T.A. 2000. The structural basis of ribosome activity in peptide bond synthesis. Science 289:920-930.
    • (2000) Science , vol.289 , pp. 920-930
    • Nissen, P.1    Hansen, J.2    Ban, N.3    Moore, P.B.4    Steitz, T.A.5
  • 30
    • 0002443434 scopus 로고
    • A small particulate component of the cytoplasm
    • Palade, G.E. 1955. A small particulate component of the cytoplasm. J. Biophys. Biochem. Cytol. 1:59-68.
    • (1955) J. Biophys. Biochem. Cytol. , vol.1 , pp. 59-68
    • Palade, G.E.1
  • 31
    • 5444237797 scopus 로고    scopus 로고
    • What better measure than ribosome synthesis?
    • Rudra, D. and Warner, J.R.. 2004. What better measure than ribosome synthesis? Genes Dev. 18: 2431-2436.
    • (2004) Genes Dev. , vol.18 , pp. 2431-2436
    • Rudra, D.1    Warner, J.R.2
  • 32
    • 0037363075 scopus 로고    scopus 로고
    • Does the ribosome translate cancer?
    • Ruggero, D. and Pandolfi, P.P. 2003. Does the ribosome translate cancer? Nat. Rev. Cancer 3:179-192.
    • (2003) Nat. Rev. Cancer , vol.3 , pp. 179-192
    • Ruggero, D.1    Pandolfi, P.P.2
  • 35
    • 49849100681 scopus 로고    scopus 로고
    • Spectrophotometric and colorimetric determination of protein concentration
    • Simonin, M.H. and Smith, J.A. 2008. Spectrophotometric and colorimetric determination of protein concentration. Curr. Protoc. Mol. Biol. 76:10.1A.1-10.1A.9.
    • (2008) Curr. Protoc. Mol. Biol. , vol.76
    • Simonin, M.H.1    Smith, J.A.2
  • 36
    • 0029157725 scopus 로고
    • Phosphorylation of herpes simplex virus type 1 Us11 protein is independent of viral genome expression
    • Simonin, D., Diaz, J.J., Kindbeiter, K., Pernas, P., and Madjar, J.J. 1995a. Phosphorylation of herpes simplex virus type 1 Us11 protein is independent of viral genome expression. Electrophoresis 16:1317-1322.
    • (1995) Electrophoresis , vol.16 , pp. 1317-1322
    • Simonin, D.1    Diaz, J.J.2    Kindbeiter, K.3    Pernas, P.4    Madjar, J.J.5
  • 37
    • 0029044217 scopus 로고
    • Phosphorylation of ribosomal protein L30 after herpes simplex virus type 1 infection
    • Simonin, D., Diaz, J.J., Kindbeiter, K., Denory, L., and Madjar, J.J. 1995b. Phosphorylation of ribosomal protein L30 after herpes simplex virus type 1 infection. Electrophoresis 16:854-859.
    • (1995) Electrophoresis , vol.16 , pp. 854-859
    • Simonin, D.1    Diaz, J.J.2    Kindbeiter, K.3    Denory, L.4    Madjar, J.J.5
  • 38
    • 0031036634 scopus 로고    scopus 로고
    • Persistence of ribosomal protein synthesis after infection of HeLa cells by herpes simplex virus type 1
    • Simonin, D., Diaz, J.J., Masse, T., and Madjar, J.J. 1997. Persistence of ribosomal protein synthesis after infection of HeLa cells by herpes simplex virus type 1. J. Gen. Virol. 78:435-443.
    • (1997) J. Gen. Virol. , vol.78 , pp. 435-443
    • Simonin, D.1    Diaz, J.J.2    Masse, T.3    Madjar, J.J.4
  • 39
    • 0035798380 scopus 로고    scopus 로고
    • Structure of the 80S ribosome from Saccharomyces cerevisiae-tRNA-ribosome and subunit-subunit interactions
    • Spahn, C.M., Beckmann, R., Eswar, N., Penczek, P.A., Sali, A., Blobel, G., and Frank, J. 2001. Structure of the 80S ribosome from Saccharomyces cerevisiae-tRNA-ribosome and subunit-subunit interactions. Cell 107:373-386.
    • (2001) Cell , vol.107 , pp. 373-386
    • Spahn, C.M.1    Beckmann, R.2    Eswar, N.3    Penczek, P.A.4    Sali, A.5    Blobel, G.6    Frank, J.7
  • 40
    • 0000815931 scopus 로고
    • Ribonucleo-protein particles from Escherichia coli
    • Tissieres, A. and Watson, J.D. 1958. Ribonucleo-protein particles from Escherichia coli. Nature 182:778-780.
    • (1958) Nature , vol.182 , pp. 778-780
    • Tissieres, A.1    Watson, J.D.2
  • 42
    • 0033229970 scopus 로고    scopus 로고
    • The economics of ribosome biosynthesis in yeast
    • Warner, J.R. 1999 The economics of ribosome biosynthesis in yeast. Trends Biochem. Sci. 24:437-440.
    • (1999) Trends Biochem. Sci. , vol.24 , pp. 437-440
    • Warner, J.R.1
  • 43
  • 45
    • 0001320597 scopus 로고    scopus 로고
    • Mammalian ribosomes: The structure and the evolution of the proteins
    • (J.W.B. Hershey and M.B. Mathews, eds.), Cold Spring Harbor Laboratory Press, Cold Spring Harbor, New York
    • Wool, I.G., Chan, Y.-L., and Glück, A. 1996. Mammalian ribosomes: the structure and the evolution of the proteins. In Translational Control (J.W.B. Hershey and M.B. Mathews, eds.) pp. 685-732. Cold Spring Harbor Laboratory Press, Cold Spring Harbor, New York.
    • (1996) In Translational Control , pp. 685-732
    • Wool, I.G.1    Chan, Y.-L.2    Glück, A.3
  • 46
    • 0021770782 scopus 로고
    • Some x-ray diffraction patterns from single crystals of the large ribosomal subunit from Bacillus stearothermophilus
    • Yonath, A., Bartunik, H.D., Bartels, K.S., and Witmann, H.G. 1984. Some x-ray diffraction patterns from single crystals of the large ribosomal subunit from Bacillus stearothermophilus. J. Mol. Biol. 177:201-206.
    • (1984) J. Mol. Biol. , vol.177 , pp. 201-206
    • Yonath, A.1    Bartunik, H.D.2    Bartels, K.S.3    Witmann, H.G.4
  • 47
    • 33646543044 scopus 로고    scopus 로고
    • Impaired control of IRES-mediated translation in X-linked dyskeratosis congenita
    • Yoon, A., Peng, G., Brandenburger, Y., Zoillo, O., Xu, W., Rego, E., and Ruggero, D. 2006. Impaired control of IRES-mediated translation in X-linked dyskeratosis congenita. Science 312:902-906.
    • (2006) Science , vol.312 , pp. 902-906
    • Yoon, A.1    Peng, G.2    Brandenburger, Y.3    Zoillo, O.4    Xu, W.5    Rego, E.6    Ruggero, D.7


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