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Volumn 1803, Issue 6, 2010, Pages 673-683

Driving ribosome assembly

Author keywords

Bowen Conradi syndrome; Cancer; Cartilage hair hypoplasia; Diamond Blackfan anemia; Dyskeratosis congenita; Nuclear export of ribosomes; Quality control of ribosomes; Ribosome assembly; Shwachman Diamond syndrome

Indexed keywords

ABC TRANSPORTER; ADENOSINE TRIPHOSPHATASE; PHOSPHOTRANSFERASE; PROTON TRANSPORTING ADENOSINE TRIPHOSPHATASE; RIBOSOME RNA; RNA 40S; RNA 60S; SMALL NUCLEOLAR RNA; SMALL SUBUNIT RIBOSOMAL RNA; UNCLASSIFIED DRUG;

EID: 77953027564     PISSN: 01674889     EISSN: None     Source Type: Journal    
DOI: 10.1016/j.bbamcr.2009.10.009     Document Type: Review
Times cited : (405)

References (165)
  • 2
    • 60149099539 scopus 로고    scopus 로고
    • Fidelity at the molecular level: lessons from protein synthesis
    • Zaher H.S., Green R. Fidelity at the molecular level: lessons from protein synthesis. Cell 2009, 136:746-762.
    • (2009) Cell , vol.136 , pp. 746-762
    • Zaher, H.S.1    Green, R.2
  • 3
    • 39749138785 scopus 로고    scopus 로고
    • A structural understanding of the dynamic ribosome machine
    • Steitz T.A. A structural understanding of the dynamic ribosome machine. Nat. Rev. Mol. Cell Biol. 2008, 9:242-253.
    • (2008) Nat. Rev. Mol. Cell Biol. , vol.9 , pp. 242-253
    • Steitz, T.A.1
  • 4
    • 0033229970 scopus 로고    scopus 로고
    • The economics of ribosome biosynthesis in yeast
    • Warner J.R. The economics of ribosome biosynthesis in yeast. Trends Biochem.Sci. 1999, 24:437-440.
    • (1999) Trends Biochem.Sci. , vol.24 , pp. 437-440
    • Warner, J.R.1
  • 7
    • 0038738334 scopus 로고    scopus 로고
    • Pre-ribosomes on the road from the nucleolus to the cytoplasm
    • Tschochner H., Hurt E. Pre-ribosomes on the road from the nucleolus to the cytoplasm. Trends Cell Biol. 2003, 13:255-263.
    • (2003) Trends Cell Biol. , vol.13 , pp. 255-263
    • Tschochner, H.1    Hurt, E.2
  • 8
    • 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.C. 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.C.5
  • 9
    • 0037536219 scopus 로고    scopus 로고
    • The path from nucleolar 90S to cytoplasmic 40S pre-ribosomes
    • Schäfer T., Strau D., Petfalski E., Tollervey D., Hurt E.C. The path from nucleolar 90S to cytoplasmic 40S pre-ribosomes. EMBO J. 2003, 22:1370-1380.
    • (2003) EMBO J. , vol.22 , pp. 1370-1380
    • Schäfer, T.1    Strau, D.2    Petfalski, E.3    Tollervey, D.4    Hurt, E.C.5
  • 10
    • 2142754126 scopus 로고    scopus 로고
    • Ribosome biogenesis: of knobs and RNA processing
    • Granneman S., Baserga S.J. Ribosome biogenesis: of knobs and RNA processing. Exp. Cell. Res. 2004, 296:43-50.
    • (2004) Exp. Cell. Res. , vol.296 , pp. 43-50
    • Granneman, S.1    Baserga, S.J.2
  • 11
    • 33750044901 scopus 로고    scopus 로고
    • Ribosome biogenesis and cell growth: mTOR coordinates transcription by all three classes of nuclear RNA polymerases
    • Mayer C., Grummt I. Ribosome biogenesis and cell growth: mTOR coordinates transcription by all three classes of nuclear RNA polymerases. Oncogene 2006, 25:6384-6391.
    • (2006) Oncogene , vol.25 , pp. 6384-6391
    • Mayer, C.1    Grummt, I.2
  • 12
  • 13
    • 5444237797 scopus 로고    scopus 로고
    • What better measure than ribosome synthesis?
    • Rudra D., Warner J.R. What better measure than ribosome synthesis?. Genes Dev. 2004, 18:2431-2436.
    • (2004) Genes Dev. , vol.18 , pp. 2431-2436
    • Rudra, D.1    Warner, J.R.2
  • 14
    • 33748948242 scopus 로고    scopus 로고
    • Regulation of ribosome biogenesis: where is TOR?
    • Martin D.E., Powers T., Hall M.N. Regulation of ribosome biogenesis: where is TOR?. Cell. Metab. 2006, 4:259-260.
    • (2006) Cell. Metab. , vol.4 , pp. 259-260
    • Martin, D.E.1    Powers, T.2    Hall, M.N.3
  • 15
    • 2942610793 scopus 로고    scopus 로고
    • RNA structure and function in C/D and H/ACA s(no)RNPs
    • Henras A.K., Dez C., Henry Y. RNA structure and function in C/D and H/ACA s(no)RNPs. Curr. Opin. Struct. Biol. 2004, 14:335-343.
    • (2004) Curr. Opin. Struct. Biol. , vol.14 , pp. 335-343
    • Henras, A.K.1    Dez, C.2    Henry, Y.3
  • 16
    • 0033367325 scopus 로고    scopus 로고
    • Ribosome synthesis in Saccharomyces cerevisiae
    • Venema J., Tollervey D. Ribosome synthesis in Saccharomyces cerevisiae. Annu. Rev. Genet. 1999, 33:261-311.
    • (1999) Annu. Rev. Genet. , vol.33 , pp. 261-311
    • Venema, J.1    Tollervey, D.2
  • 17
    • 10944222974 scopus 로고    scopus 로고
    • Pre-18S ribosomal RNA is structurally compacted into the SSU processome prior to being cleaved from nascent transcripts in Saccharomyces cerevisiae
    • Osheim Y.N., French S.L., Keck K.M., Champion E.A., Spasov K., Dragon F., Baserga S.J., Beyer A.L. Pre-18S ribosomal RNA is structurally compacted into the SSU processome prior to being cleaved from nascent transcripts in Saccharomyces cerevisiae. Mol. Cell 2004, 16:943-954.
    • (2004) Mol. Cell , vol.16 , pp. 943-954
    • Osheim, Y.N.1    French, S.L.2    Keck, K.M.3    Champion, E.A.4    Spasov, K.5    Dragon, F.6    Baserga, S.J.7    Beyer, A.L.8
  • 18
    • 34547163927 scopus 로고    scopus 로고
    • The 90S preribosome is a multimodular structure that is assembled through a hierarchical mechanism
    • Perez-Fernandez J., Roman A., De Las Rivas J., Bustelo X.R., Dosil M. The 90S preribosome is a multimodular structure that is assembled through a hierarchical mechanism. Mol. Cell. Biol. 2007, 27:5414-5429.
    • (2007) Mol. Cell. Biol. , vol.27 , pp. 5414-5429
    • Perez-Fernandez, J.1    Roman, A.2    De Las Rivas, J.3    Bustelo, X.R.4    Dosil, M.5
  • 22
    • 33745228890 scopus 로고    scopus 로고
    • Hrr25-dependent phosphorylation state regulates organization of the pre-40S subunit
    • Schäfer T., Maco B., Petfalski E., Tollervey D., Bottcher B., Aebi U., Hurt E. Hrr25-dependent phosphorylation state regulates organization of the pre-40S subunit. Nature 2006, 441:651-655.
    • (2006) Nature , vol.441 , pp. 651-655
    • Schäfer, T.1    Maco, B.2    Petfalski, E.3    Tollervey, D.4    Bottcher, B.5    Aebi, U.6    Hurt, E.7
  • 23
  • 24
    • 27944478055 scopus 로고    scopus 로고
    • The putative NTPase Fap7 mediates cytoplasmic 20S pre-rRNA processing through a direct interaction with Rps14
    • Granneman S., Nandineni M.R., Baserga S.J. The putative NTPase Fap7 mediates cytoplasmic 20S pre-rRNA processing through a direct interaction with Rps14. Mol. Cell. Biol. 2005, 25:10352-10364.
    • (2005) Mol. Cell. Biol. , vol.25 , pp. 10352-10364
    • Granneman, S.1    Nandineni, M.R.2    Baserga, S.J.3
  • 25
    • 0037373221 scopus 로고    scopus 로고
    • Late cytoplasmic maturation of the small ribosomal subunit requires RIO proteins in Saccharomyces cerevisiae
    • Vanrobays E., Gelugne J.P., Gleizes P.E., Caizergues-Ferrer M. Late cytoplasmic maturation of the small ribosomal subunit requires RIO proteins in Saccharomyces cerevisiae. Mol. Cell Biol. 2003, 23:2083-2095.
    • (2003) Mol. Cell Biol. , vol.23 , pp. 2083-2095
    • Vanrobays, E.1    Gelugne, J.P.2    Gleizes, P.E.3    Caizergues-Ferrer, M.4
  • 26
    • 0034844836 scopus 로고    scopus 로고
    • Bms1p, a novel GTP-binding protein, and the related Tsr1p are required for distinct steps of 40S ribosome biogenesis in yeast
    • Gelperin D., Horton L., Beckman J., Hensold J., Lemmon S.K. Bms1p, a novel GTP-binding protein, and the related Tsr1p are required for distinct steps of 40S ribosome biogenesis in yeast. RNA 2001, 7:1268-1283.
    • (2001) RNA , vol.7 , pp. 1268-1283
    • Gelperin, D.1    Horton, L.2    Beckman, J.3    Hensold, J.4    Lemmon, S.K.5
  • 27
    • 7044231044 scopus 로고    scopus 로고
    • PIN domain of Nob1p is required for D-site cleavage in 20S pre-rRNA
    • Fatica A., Tollervey D., Dlakic M. PIN domain of Nob1p is required for D-site cleavage in 20S pre-rRNA. RNA 2004, 10:1698-1701.
    • (2004) RNA , vol.10 , pp. 1698-1701
    • Fatica, A.1    Tollervey, D.2    Dlakic, M.3
  • 28
    • 70449656291 scopus 로고    scopus 로고
    • RNA helicase Prp43 and its co-factor Pfa1 promote 20S to 18S rRNA processing catalyzed by the endonuclease Nob1
    • Pertschy B., Schneider C., Gnädig M., Schäfer T., Tollervey D., Hurt E. RNA helicase Prp43 and its co-factor Pfa1 promote 20S to 18S rRNA processing catalyzed by the endonuclease Nob1. J. Biol. Chem 2009, 284:35079-35091. http://www.jbc.org/content/early/2009/09/29/jbc.M109.040774.long.
    • (2009) J. Biol. Chem , vol.284 , pp. 35079-35091
    • Pertschy, B.1    Schneider, C.2    Gnädig, M.3    Schäfer, T.4    Tollervey, D.5    Hurt, E.6
  • 29
    • 70149120737 scopus 로고    scopus 로고
    • Nob1 binds the single-stranded cleavage site D at the 3'-end of 18S rRNA with its PIN domain
    • Lamanna A.C., Karbstein K. Nob1 binds the single-stranded cleavage site D at the 3'-end of 18S rRNA with its PIN domain. Pric. Natl. Acad. Sci. U.S.A. 2009, 106:14259-14264.
    • (2009) Pric. Natl. Acad. Sci. U.S.A. , vol.106 , pp. 14259-14264
    • Lamanna, A.C.1    Karbstein, K.2
  • 30
    • 0036184160 scopus 로고    scopus 로고
    • Ssf1p prevents premature processing of an early pre-60S ribosomal particle
    • Fatica A., Cronshaw A.D., Tollervey D.M.D. Ssf1p prevents premature processing of an early pre-60S ribosomal particle. Mol. Cell 2002, 9:341-351.
    • (2002) Mol. Cell , vol.9 , pp. 341-351
    • Fatica, A.1    Cronshaw, A.D.2    Tollervey, D.M.D.3
  • 33
    • 0035890063 scopus 로고    scopus 로고
    • Nog2p, a putative GTPase associated with pre-60S subunits and required for late 60S maturation steps
    • Saveanu C., Bienvenu D., Namane A., Gleizes P.E., Gas N., Jacquier A., Fromont-Racine M. Nog2p, a putative GTPase associated with pre-60S subunits and required for late 60S maturation steps. EMBO J. 2001, 20:6475-6484.
    • (2001) EMBO J. , vol.20 , pp. 6475-6484
    • Saveanu, C.1    Bienvenu, D.2    Namane, A.3    Gleizes, P.E.4    Gas, N.5    Jacquier, A.6    Fromont-Racine, M.7
  • 35
    • 45349094341 scopus 로고    scopus 로고
    • The AAA ATPase Rix7 powers progression of ribosome biogenesis by stripping Nsa1 from pre-60S particles
    • Kressler D., Roser D., Pertschy B., Hurt E. The AAA ATPase Rix7 powers progression of ribosome biogenesis by stripping Nsa1 from pre-60S particles. J. Cell Biol. 2008, 181:935-944.
    • (2008) J. Cell Biol. , vol.181 , pp. 935-944
    • Kressler, D.1    Roser, D.2    Pertschy, B.3    Hurt, E.4
  • 36
    • 3042671460 scopus 로고    scopus 로고
    • Npa1p, a component of very early pre-60S ribosomal particles, associates with a subset of small nucleolar RNPs required for peptidyl transferase center modification
    • Dez C., Froment C., Noaillac-Depeyre J., Monsarrat B., Caizergues-Ferrer M., Henry Y. Npa1p, a component of very early pre-60S ribosomal particles, associates with a subset of small nucleolar RNPs required for peptidyl transferase center modification. Mol. Cell. Biol. 2004, 24:6324-6337.
    • (2004) Mol. Cell. Biol. , vol.24 , pp. 6324-6337
    • Dez, C.1    Froment, C.2    Noaillac-Depeyre, J.3    Monsarrat, B.4    Caizergues-Ferrer, M.5    Henry, Y.6
  • 38
    • 51349144693 scopus 로고    scopus 로고
    • Interactions among Ytm1, Erb1, and Nop7 required for assembly of the Nop7-subcomplex in yeast preribosomes
    • Tang L., Sahasranaman A., Jakovljevic J., Schleifman E., Woolford J.L. Interactions among Ytm1, Erb1, and Nop7 required for assembly of the Nop7-subcomplex in yeast preribosomes. Mol. Biol. Cell 2008, 19:2844-2856.
    • (2008) Mol. Biol. Cell , vol.19 , pp. 2844-2856
    • Tang, L.1    Sahasranaman, A.2    Jakovljevic, J.3    Schleifman, E.4    Woolford, J.L.5
  • 42
    • 3242694353 scopus 로고    scopus 로고
    • A pre-ribosome with a tadpole-like structure functions in ATP-dependent maturation of 60S subunits
    • Nissan T.A., Galani K., Maco B., Tollervey D., Aebi U., Hurt E. A pre-ribosome with a tadpole-like structure functions in ATP-dependent maturation of 60S subunits. Mol. Cell 2004, 15:295-301.
    • (2004) Mol. Cell , vol.15 , pp. 295-301
    • Nissan, T.A.1    Galani, K.2    Maco, B.3    Tollervey, D.4    Aebi, U.5    Hurt, E.6
  • 43
    • 34147113397 scopus 로고    scopus 로고
    • Nuclear export of ribosomal 60S subunits by the general mRNA export receptor Mex67-Mtr2
    • Yao W., Roser D., Köhler A., Bradatsch B., Bassler J., Hurt E. Nuclear export of ribosomal 60S subunits by the general mRNA export receptor Mex67-Mtr2. Mol. Cell 2007, 26:51-62.
    • (2007) Mol. Cell , vol.26 , pp. 51-62
    • Yao, W.1    Roser, D.2    Köhler, A.3    Bradatsch, B.4    Bassler, J.5    Hurt, E.6
  • 45
    • 70349901353 scopus 로고    scopus 로고
    • Ribosome stalk assembly requires the dual specificity phosphatase Yvh1 for the exchange of Mrt4 with P0
    • Lo K.-Y., Li Z., Wang F., Marcotte E., Johnson A.W. Ribosome stalk assembly requires the dual specificity phosphatase Yvh1 for the exchange of Mrt4 with P0. J. Cell Biol. 2009, 186.
    • (2009) J. Cell Biol. , pp. 186
    • Lo, K.-Y.1    Li, Z.2    Wang, F.3    Marcotte, E.4    Johnson, A.W.5
  • 46
    • 70349924070 scopus 로고    scopus 로고
    • Yvh1 is required for a late maturation step in the 60S biogenesis pathway
    • Kemmler S., Occhipinti L., Veisu M., Panse G.V. Yvh1 is required for a late maturation step in the 60S biogenesis pathway. J. Cell Biol. 2009, 186.
    • (2009) J. Cell Biol. , pp. 186
    • Kemmler, S.1    Occhipinti, L.2    Veisu, M.3    Panse, G.V.4
  • 48
    • 43249092177 scopus 로고    scopus 로고
    • The exonuclease ERI-1 has a conserved dual role in 5.8S rRNA processing and RNAi
    • Gabel H.W., Ruvkun G. The exonuclease ERI-1 has a conserved dual role in 5.8S rRNA processing and RNAi. Nat. Struct. Mol. Biol. 2008, 15:531-533.
    • (2008) Nat. Struct. Mol. Biol. , vol.15 , pp. 531-533
    • Gabel, H.W.1    Ruvkun, G.2
  • 50
    • 33646582609 scopus 로고    scopus 로고
    • Nuclear recycling of the pre-60S ribosomal subunit-associated factor Arx1 depends on Rei1 in Saccharomyces cerevisiae
    • Hung N.J., Johnson A.W. Nuclear recycling of the pre-60S ribosomal subunit-associated factor Arx1 depends on Rei1 in Saccharomyces cerevisiae. Mol. Cell. Biol. 2006, 26:3718-3727.
    • (2006) Mol. Cell. Biol. , vol.26 , pp. 3718-3727
    • Hung, N.J.1    Johnson, A.W.2
  • 52
    • 34548341809 scopus 로고    scopus 로고
    • The Hsp40 chaperone Jjj1 is required for the nucleo-cytoplasmic recycling of preribosomal factors in Saccharomyces cerevisiae
    • Demoinet E., Jacquier A., Lutfalla G., Fromont-Racine M. The Hsp40 chaperone Jjj1 is required for the nucleo-cytoplasmic recycling of preribosomal factors in Saccharomyces cerevisiae. RNA 2007, 13:1570-1581.
    • (2007) RNA , vol.13 , pp. 1570-1581
    • Demoinet, E.1    Jacquier, A.2    Lutfalla, G.3    Fromont-Racine, M.4
  • 53
    • 33846818906 scopus 로고    scopus 로고
    • The specialized cytosolic J-protein, Jjj1, functions in 60S ribosomal subunit biogenesis
    • Meyer A.E., Hung N.J., Yang P., Johnson A.W., Craig E.A. The specialized cytosolic J-protein, Jjj1, functions in 60S ribosomal subunit biogenesis. Proc. Natl. Acad. Sci. U. S. A. 2007, 104:1558-1563.
    • (2007) Proc. Natl. Acad. Sci. U. S. A. , vol.104 , pp. 1558-1563
    • Meyer, A.E.1    Hung, N.J.2    Yang, P.3    Johnson, A.W.4    Craig, E.A.5
  • 56
    • 0037013954 scopus 로고    scopus 로고
    • The permeability barrier of nuclear pore complexes appears to operate via hydrophobic exclusion
    • Ribbeck K., Görlich D. The permeability barrier of nuclear pore complexes appears to operate via hydrophobic exclusion. EMBO J. 2002, 21:2664-2671.
    • (2002) EMBO J. , vol.21 , pp. 2664-2671
    • Ribbeck, K.1    Görlich, D.2
  • 57
    • 0037844806 scopus 로고    scopus 로고
    • Coordinated nuclear export of 60S ribosomal subunits and NMD3 in vertebrates
    • Trotta C.R., Lund E., Kahan L., Johnson A.W., Dahlberg J.E. Coordinated nuclear export of 60S ribosomal subunits and NMD3 in vertebrates. EMBO J. 2003, 22:2841-2851.
    • (2003) EMBO J. , vol.22 , pp. 2841-2851
    • Trotta, C.R.1    Lund, E.2    Kahan, L.3    Johnson, A.W.4    Dahlberg, J.E.5
  • 58
    • 0033535052 scopus 로고    scopus 로고
    • A novel in vivo assay reveals inhibition of ribosomal nuclear export in Ran-cycle and nucleoporin mutants
    • Hurt E., Hannus S., Schmelzl B., Lau D., Tollervey D., Simos G. A novel in vivo assay reveals inhibition of ribosomal nuclear export in Ran-cycle and nucleoporin mutants. J. Cell Biol. 1999, 144:389-401.
    • (1999) J. Cell Biol. , vol.144 , pp. 389-401
    • Hurt, E.1    Hannus, S.2    Schmelzl, B.3    Lau, D.4    Tollervey, D.5    Simos, G.6
  • 59
    • 0037099045 scopus 로고    scopus 로고
    • Requirements for the nuclear export of the small ribosomal subunit
    • Moy T.I., Silver P.A. Requirements for the nuclear export of the small ribosomal subunit. J. Cell. Sci. 2002, 115:2985-2995.
    • (2002) J. Cell. Sci. , vol.115 , pp. 2985-2995
    • Moy, T.I.1    Silver, P.A.2
  • 60
    • 0033567356 scopus 로고    scopus 로고
    • Nuclear export of the small ribosomal subunit requires the Ran-GTPase cycle and certain nucleoporins
    • Moy T.I., Silver P.A. Nuclear export of the small ribosomal subunit requires the Ran-GTPase cycle and certain nucleoporins. Genes Dev. 1999, 13:2118-2133.
    • (1999) Genes Dev. , vol.13 , pp. 2118-2133
    • Moy, T.I.1    Silver, P.A.2
  • 61
    • 0037716643 scopus 로고    scopus 로고
    • Biogenesis and nuclear export of ribosomal subunits in higher eukaryotes depend on the CRM1 export pathway
    • Thomas F., Kutay U. Biogenesis and nuclear export of ribosomal subunits in higher eukaryotes depend on the CRM1 export pathway. J. Cell. Sci. 2003, 116:2409-2419.
    • (2003) J. Cell. Sci. , vol.116 , pp. 2409-2419
    • Thomas, F.1    Kutay, U.2
  • 62
    • 0042830859 scopus 로고    scopus 로고
    • Nucleocytoplasmic transport: taking an inventory
    • Fried H., Kutay U. Nucleocytoplasmic transport: taking an inventory. Cell. Mol. Life Sci. 2003, 60:1659-1688.
    • (2003) Cell. Mol. Life Sci. , vol.60 , pp. 1659-1688
    • Fried, H.1    Kutay, U.2
  • 64
    • 0035027807 scopus 로고    scopus 로고
    • Nuclear export of 60S ribosomal subunits depends on Xpo1p and requires a NES-containing factor Nmd3p that associates with the large subunit protein Rpl10p
    • Gadal O., Strau D., Kessl J., Trumpower B., Tollervey D., Hurt E. Nuclear export of 60S ribosomal subunits depends on Xpo1p and requires a NES-containing factor Nmd3p that associates with the large subunit protein Rpl10p. Mol. Cell. Biol. 2001, 21:3405-3415.
    • (2001) Mol. Cell. Biol. , vol.21 , pp. 3405-3415
    • Gadal, O.1    Strau, D.2    Kessl, J.3    Trumpower, B.4    Tollervey, D.5    Hurt, E.6
  • 65
    • 0034722372 scopus 로고    scopus 로고
    • Nmd3p is a Crm1p-dependent adapter protein for nuclear export of the large ribosomal subunit
    • Ho J.H.N., Kallstrom G., Johnson A.W. Nmd3p is a Crm1p-dependent adapter protein for nuclear export of the large ribosomal subunit. J. Cell Biol. 2000, 151:1057-1066.
    • (2000) J. Cell Biol. , vol.151 , pp. 1057-1066
    • Ho, J.H.N.1    Kallstrom, G.2    Johnson, A.W.3
  • 66
    • 33846009103 scopus 로고    scopus 로고
    • Mapping the functional domains of yeast NMD3, the nuclear export adapter for the 60 S ribosomal subunit
    • Hedges J., Chen Y.I., West M., Bussiere C., Johnson A.W. Mapping the functional domains of yeast NMD3, the nuclear export adapter for the 60 S ribosomal subunit. J. Biol. Chem. 2006, 281:36579-36587.
    • (2006) J. Biol. Chem. , vol.281 , pp. 36579-36587
    • Hedges, J.1    Chen, Y.I.2    West, M.3    Bussiere, C.4    Johnson, A.W.5
  • 67
    • 14844327974 scopus 로고    scopus 로고
    • Release of the export adapter, Nmd3p, from the 60S ribosomal subunit requires Rpl10p and the cytoplasmic GTPase Lsg1p
    • Hedges J., West M., Johnson A.W. Release of the export adapter, Nmd3p, from the 60S ribosomal subunit requires Rpl10p and the cytoplasmic GTPase Lsg1p. EMBO J. 2005, 24:567-579.
    • (2005) EMBO J. , vol.24 , pp. 567-579
    • Hedges, J.1    West, M.2    Johnson, A.W.3
  • 68
    • 17644379370 scopus 로고    scopus 로고
    • Defining the order in which Nmd3p and Rpl10p load onto nascent 60S ribosomal subunits
    • West M., Hedges J.B., Chen A., Johnson A.W. Defining the order in which Nmd3p and Rpl10p load onto nascent 60S ribosomal subunits. Mol. Cell. Biol. 2005, 25:3802-3813.
    • (2005) Mol. Cell. Biol. , vol.25 , pp. 3802-3813
    • West, M.1    Hedges, J.B.2    Chen, A.3    Johnson, A.W.4
  • 69
    • 0034698683 scopus 로고    scopus 로고
    • Binding of the Mex67p/Mtr2p heterodimer to FXFG, GLFG, and FG repeat nucleoporins is essential for nuclear mRNA export
    • Strässer K., Bassler J., Hurt E.C. Binding of the Mex67p/Mtr2p heterodimer to FXFG, GLFG, and FG repeat nucleoporins is essential for nuclear mRNA export. J. Cell Biol. 2000, 150:695-706.
    • (2000) J. Cell Biol. , vol.150 , pp. 695-706
    • Strässer, K.1    Bassler, J.2    Hurt, E.C.3
  • 72
    • 26944450063 scopus 로고    scopus 로고
    • Roles of eukaryotic ribosomal proteins in maturation and transport of pre-18S rRNA and ribosome function
    • Ferreira-Cerca S., Poll G., Gleizes P.E., Tschochner H., Milkereit P. Roles of eukaryotic ribosomal proteins in maturation and transport of pre-18S rRNA and ribosome function. Mol. Cell 2005, 20:263-275.
    • (2005) Mol. Cell , vol.20 , pp. 263-275
    • Ferreira-Cerca, S.1    Poll, G.2    Gleizes, P.E.3    Tschochner, H.4    Milkereit, P.5
  • 74
    • 52949107245 scopus 로고    scopus 로고
    • TOR regulates the subcellular distribution of DIM2, a KH domain protein required for cotranscriptional ribosome assembly and pre-40S ribosome export
    • Vanrobays E., Leplus A., Osheim Y.N., Beyer A.L., Wacheul L., Lafontaine D.L. TOR regulates the subcellular distribution of DIM2, a KH domain protein required for cotranscriptional ribosome assembly and pre-40S ribosome export. RNA 2008, 14:2061-2073.
    • (2008) RNA , vol.14 , pp. 2061-2073
    • Vanrobays, E.1    Leplus, A.2    Osheim, Y.N.3    Beyer, A.L.4    Wacheul, L.5    Lafontaine, D.L.6
  • 77
    • 33645727798 scopus 로고    scopus 로고
    • Surveillance of nuclear-restricted pre-ribosomes within a subnucleolar region of Saccharomyces cerevisiae
    • Dez C., Houseley J., Tollervey D. Surveillance of nuclear-restricted pre-ribosomes within a subnucleolar region of Saccharomyces cerevisiae. EMBO J. 2006, 25:1534-1546.
    • (2006) EMBO J. , vol.25 , pp. 1534-1546
    • Dez, C.1    Houseley, J.2    Tollervey, D.3
  • 78
    • 0942301279 scopus 로고    scopus 로고
    • A pre-ribosome-associated HEAT-repeat protein is required for export of both ribosomal subunits
    • Oeffinger M., Dlakic M., Tollervey D. A pre-ribosome-associated HEAT-repeat protein is required for export of both ribosomal subunits. Genes Dev. 2004, 18:196-209.
    • (2004) Genes Dev. , vol.18 , pp. 196-209
    • Oeffinger, M.1    Dlakic, M.2    Tollervey, D.3
  • 79
    • 0027182114 scopus 로고
    • Helicases: amino acid sequence comparisons and structure-function relationships
    • Gorbalenya A.E., Koonin E.V. Helicases: amino acid sequence comparisons and structure-function relationships. Curr. Opin. Struct. Biol. 1993, 3:419-429.
    • (1993) Curr. Opin. Struct. Biol. , vol.3 , pp. 419-429
    • Gorbalenya, A.E.1    Koonin, E.V.2
  • 80
    • 3042571314 scopus 로고    scopus 로고
    • Ribosomal subunit assembly
    • Landes Bioscience/Eurekah.com, Georgetown, Texas, M.O.J. Olson (Ed.)
    • de la Cruz J., Kressler D., Linder P. Ribosomal subunit assembly. The Nucleolus 2004, 258-285. Landes Bioscience/Eurekah.com, Georgetown, Texas. M.O.J. Olson (Ed.).
    • (2004) The Nucleolus , pp. 258-285
    • de la Cruz, J.1    Kressler, D.2    Linder, P.3
  • 81
    • 33344473656 scopus 로고    scopus 로고
    • The DEAD-box protein family of RNA helicases
    • Cordin O., Banroques J., Tanner N.K., Linder P. The DEAD-box protein family of RNA helicases. Gene 2006, 367:17-37.
    • (2006) Gene , vol.367 , pp. 17-37
    • Cordin, O.1    Banroques, J.2    Tanner, N.K.3    Linder, P.4
  • 82
    • 34547211817 scopus 로고    scopus 로고
    • The long unwinding road of RNA helicases
    • Bleichert F., Baserga S.J. The long unwinding road of RNA helicases. Mol. Cell 2007, 27:339-352.
    • (2007) Mol. Cell , vol.27 , pp. 339-352
    • Bleichert, F.1    Baserga, S.J.2
  • 83
    • 33749139723 scopus 로고    scopus 로고
    • Dead-box proteins: a family affair-active and passive players in RNP-remodeling
    • Linder P. Dead-box proteins: a family affair-active and passive players in RNP-remodeling. Nucleic Acids Res. 2006, 34:4168-4180.
    • (2006) Nucleic Acids Res. , vol.34 , pp. 4168-4180
    • Linder, P.1
  • 85
    • 33749130843 scopus 로고    scopus 로고
    • Remodeling of ribonucleoprotein complexes with DExH/D RNA helicases
    • Jankowsky E., Bowers H. Remodeling of ribonucleoprotein complexes with DExH/D RNA helicases. Nucleic Acids Res. 2006, 34:4181-4188.
    • (2006) Nucleic Acids Res. , vol.34 , pp. 4181-4188
    • Jankowsky, E.1    Bowers, H.2
  • 86
    • 1542344429 scopus 로고    scopus 로고
    • DEAD-box proteins: the driving forces behind RNA metabolism
    • Rocak S., Linder P. DEAD-box proteins: the driving forces behind RNA metabolism. Nat. Rev. Mol. Cell Biol. 2004, 5:232-241.
    • (2004) Nat. Rev. Mol. Cell Biol. , vol.5 , pp. 232-241
    • Rocak, S.1    Linder, P.2
  • 87
    • 0001607723 scopus 로고
    • Distantly related sequences in the alpha- and beta-subunits of ATP synthase, myosin, kinases and other ATP-requiring enzymes and a common nucleotide binding fold
    • Walker J.E., Saraste M., Runswick M.J., Gay N.J. Distantly related sequences in the alpha- and beta-subunits of ATP synthase, myosin, kinases and other ATP-requiring enzymes and a common nucleotide binding fold. EMBO J. 1982, 1:945-951.
    • (1982) EMBO J. , vol.1 , pp. 945-951
    • Walker, J.E.1    Saraste, M.2    Runswick, M.J.3    Gay, N.J.4
  • 88
    • 33646017369 scopus 로고    scopus 로고
    • Structural basis for RNA unwinding by the DEAD-box protein Drosophila vasa
    • Sengoku T., Nureki O., Nakamura A., Kobayashi S., Yokoyama S. Structural basis for RNA unwinding by the DEAD-box protein Drosophila vasa. Cell 2006, 125:287-300.
    • (2006) Cell , vol.125 , pp. 287-300
    • Sengoku, T.1    Nureki, O.2    Nakamura, A.3    Kobayashi, S.4    Yokoyama, S.5
  • 89
    • 33750593917 scopus 로고    scopus 로고
    • The DEAD-box protein Ded1 unwinds RNA duplexes by a mode distinct from translocating helicases
    • Yang Q., Jankowsky E. The DEAD-box protein Ded1 unwinds RNA duplexes by a mode distinct from translocating helicases. Nat. Struct. Mol. Biol. 2006, 13:981-986.
    • (2006) Nat. Struct. Mol. Biol. , vol.13 , pp. 981-986
    • Yang, Q.1    Jankowsky, E.2
  • 90
    • 35348941874 scopus 로고    scopus 로고
    • DEAD-box proteins unwind duplexes by local strand separation
    • Yang Q., Del Campo M., Lambowitz A.M., Jankowsky E. DEAD-box proteins unwind duplexes by local strand separation. Mol. Cell 2007, 28:253-263.
    • (2007) Mol. Cell , vol.28 , pp. 253-263
    • Yang, Q.1    Del Campo, M.2    Lambowitz, A.M.3    Jankowsky, E.4
  • 91
    • 58149481225 scopus 로고    scopus 로고
    • ATP hydrolysis is required for DEAD-box protein recycling but not for duplex unwinding
    • Liu F., Putnam A., Jankowsky E. ATP hydrolysis is required for DEAD-box protein recycling but not for duplex unwinding. Proc. Natl. Acad. Sci. U. S. A. 2008, 105:20209-20214.
    • (2008) Proc. Natl. Acad. Sci. U. S. A. , vol.105 , pp. 20209-20214
    • Liu, F.1    Putnam, A.2    Jankowsky, E.3
  • 92
    • 67349117103 scopus 로고    scopus 로고
    • Unwinding by local strand separation is critical for the function of DEAD-box proteins as RNA chaperones
    • Del Campo M., Mohr S., Jiang Y., Jia H., Jankowsky E., Lambowitz A.M. Unwinding by local strand separation is critical for the function of DEAD-box proteins as RNA chaperones. J. Mol. Biol. 2009, 389:674-693.
    • (2009) J. Mol. Biol. , vol.389 , pp. 674-693
    • Del Campo, M.1    Mohr, S.2    Jiang, Y.3    Jia, H.4    Jankowsky, E.5    Lambowitz, A.M.6
  • 93
    • 33646032358 scopus 로고    scopus 로고
    • Bent out of shape: RNA unwinding by the DEAD-box helicase Vasa
    • Linder P., Lasko P. Bent out of shape: RNA unwinding by the DEAD-box helicase Vasa. Cell 2006, 125:219-221.
    • (2006) Cell , vol.125 , pp. 219-221
    • Linder, P.1    Lasko, P.2
  • 94
    • 0033133863 scopus 로고    scopus 로고
    • Unwiding RNA in Saccharomyces cerevisiae: DEAD-box proteins and related families
    • De la Cruz J., Kressler D., Linder P. Unwiding RNA in Saccharomyces cerevisiae: DEAD-box proteins and related families. Trends Biochem. Sci. 1999, 24:192-198.
    • (1999) Trends Biochem. Sci. , vol.24 , pp. 192-198
    • De la Cruz, J.1    Kressler, D.2    Linder, P.3
  • 95
    • 0038024236 scopus 로고    scopus 로고
    • The human DDX and DHX gene families of putative RNA helicases
    • Abdelhaleem M., Maltais L., Wain H. The human DDX and DHX gene families of putative RNA helicases. Genomics 2003, 81:618-622.
    • (2003) Genomics , vol.81 , pp. 618-622
    • Abdelhaleem, M.1    Maltais, L.2    Wain, H.3
  • 96
    • 33745406566 scopus 로고    scopus 로고
    • The nucleolar protein Esf2 interacts directly with the DExD/H box RNA helicase, Dbp8, to stimulate ATP hydrolysis
    • Granneman S., Lin C., Champion E.A., Nandineni M.R., Zorca C., Baserga S.J. The nucleolar protein Esf2 interacts directly with the DExD/H box RNA helicase, Dbp8, to stimulate ATP hydrolysis. Nucleic Acids Res. 2006, 34:3189-3199.
    • (2006) Nucleic Acids Res. , vol.34 , pp. 3189-3199
    • Granneman, S.1    Lin, C.2    Champion, E.A.3    Nandineni, M.R.4    Zorca, C.5    Baserga, S.J.6
  • 97
    • 38049069276 scopus 로고    scopus 로고
    • Degradation of hypomodified tRNA(iMet) in vivo involves RNA-dependent ATPase activity of the DExH helicase Mtr4p
    • Wang X., Jia H., Jankowsky E., Anderson J.T. Degradation of hypomodified tRNA(iMet) in vivo involves RNA-dependent ATPase activity of the DExH helicase Mtr4p. RNA 2008, 14:107-116.
    • (2008) RNA , vol.14 , pp. 107-116
    • Wang, X.1    Jia, H.2    Jankowsky, E.3    Anderson, J.T.4
  • 98
    • 32044462969 scopus 로고    scopus 로고
    • Comprehensive mutational analysis of yeast DEXD/H box RNA helicases required for small ribosomal subunit synthesis
    • Granneman S., Bernstein K.A., Bleichert F., Baserga S.J. Comprehensive mutational analysis of yeast DEXD/H box RNA helicases required for small ribosomal subunit synthesis. Mol. Cell. Biol. 2006, 26:1183-1194.
    • (2006) Mol. Cell. Biol. , vol.26 , pp. 1183-1194
    • Granneman, S.1    Bernstein, K.A.2    Bleichert, F.3    Baserga, S.J.4
  • 99
    • 14244260321 scopus 로고    scopus 로고
    • Characterization of the ATPase and unwinding activities of the yeast DEAD-box protein Has1p and the analysis of the roles of the conserved motifs
    • Rocak S., Emery B., Tanner N.K., Linder P. Characterization of the ATPase and unwinding activities of the yeast DEAD-box protein Has1p and the analysis of the roles of the conserved motifs. Nucleic Acids Res. 2005, 33:999-1009.
    • (2005) Nucleic Acids Res. , vol.33 , pp. 999-1009
    • Rocak, S.1    Emery, B.2    Tanner, N.K.3    Linder, P.4
  • 100
    • 32044449843 scopus 로고    scopus 로고
    • Comprehensive mutational analysis of yeast DEXD/H box RNA helicases involved in large ribosomal subunit biogenesis
    • Bernstein K.A., Granneman S., Lee A.V., Manickam S., Baserga S.J. Comprehensive mutational analysis of yeast DEXD/H box RNA helicases involved in large ribosomal subunit biogenesis. Mol. Cell. Biol. 2006, 26:1195-1208.
    • (2006) Mol. Cell. Biol. , vol.26 , pp. 1195-1208
    • Bernstein, K.A.1    Granneman, S.2    Lee, A.V.3    Manickam, S.4    Baserga, S.J.5
  • 101
    • 25844432236 scopus 로고    scopus 로고
    • The Putative RNA Helicase Dbp4p Is Required for Release of the U14 snoRNA from Preribosomes in Saccharomyces cerevisiae
    • Kos M., Tollervey D. The Putative RNA Helicase Dbp4p Is Required for Release of the U14 snoRNA from Preribosomes in Saccharomyces cerevisiae. Mol. Cell 2005, 20:53-64.
    • (2005) Mol. Cell , vol.20 , pp. 53-64
    • Kos, M.1    Tollervey, D.2
  • 102
    • 56749093106 scopus 로고    scopus 로고
    • Differential RNA-dependent ATPase activities of four rRNA processing yeast DEAD-box proteins
    • Garcia I., Uhlenbeck O.C. Differential RNA-dependent ATPase activities of four rRNA processing yeast DEAD-box proteins. Biochemistry 2008, 47:12562-12573.
    • (2008) Biochemistry , vol.47 , pp. 12562-12573
    • Garcia, I.1    Uhlenbeck, O.C.2
  • 103
    • 41949126822 scopus 로고    scopus 로고
    • Characterization of the essential activities of Saccharomyces cerevisiae Mtr4p, a 3'->5' helicase partner of the nuclear exosome
    • Bernstein J., Patterson D.N., Wilson G.M., Toth E.A. Characterization of the essential activities of Saccharomyces cerevisiae Mtr4p, a 3'->5' helicase partner of the nuclear exosome. J. Biol. Chem. 2008, 283:4930-4942.
    • (2008) J. Biol. Chem. , vol.283 , pp. 4930-4942
    • Bernstein, J.1    Patterson, D.N.2    Wilson, G.M.3    Toth, E.A.4
  • 104
    • 57049142069 scopus 로고    scopus 로고
    • Quantitative analysis of snoRNA association with pre-ribosomes and release of snR30 by Rok1 helicase
    • Bohnsack M.T., Kos M., Tollervey D. Quantitative analysis of snoRNA association with pre-ribosomes and release of snR30 by Rok1 helicase. EMBO Rep. 2008, 9:1230-1236.
    • (2008) EMBO Rep. , vol.9 , pp. 1230-1236
    • Bohnsack, M.T.1    Kos, M.2    Tollervey, D.3
  • 105
    • 33749588453 scopus 로고    scopus 로고
    • The helicase Has1p is required for snoRNA release from pre-rRNA
    • Liang X.H., Fournier M.J. The helicase Has1p is required for snoRNA release from pre-rRNA. Mol. Cell. Biol. 2006, 26:7437-7450.
    • (2006) Mol. Cell. Biol. , vol.26 , pp. 7437-7450
    • Liang, X.H.1    Fournier, M.J.2
  • 106
    • 0032481316 scopus 로고    scopus 로고
    • Dob1p (Mtr4p) is a putative ATP-dependent RNA helicase required for the 3' end formation of 5.8S rRNA in Saccharomyces cerevisiae
    • De la Cruz J., Kressler D., Tollervey D., Linder P. Dob1p (Mtr4p) is a putative ATP-dependent RNA helicase required for the 3' end formation of 5.8S rRNA in Saccharomyces cerevisiae. EMBO J. 1998, 17:1128-1140.
    • (1998) EMBO J. , vol.17 , pp. 1128-1140
    • De la Cruz, J.1    Kressler, D.2    Tollervey, D.3    Linder, P.4
  • 108
    • 60149090021 scopus 로고    scopus 로고
    • The many pathways of RNA degradation
    • Houseley J., Tollervey D. The many pathways of RNA degradation. Cell 2009, 136:763-776.
    • (2009) Cell , vol.136 , pp. 763-776
    • Houseley, J.1    Tollervey, D.2
  • 109
    • 60749134015 scopus 로고    scopus 로고
    • Assembly of ribosomes and spliceosomes: complex ribonucleoprotein machines
    • Staley J.P., Woolford J.L. Assembly of ribosomes and spliceosomes: complex ribonucleoprotein machines. Curr. Opin. Cell Biol. 2009, 21:109-118.
    • (2009) Curr. Opin. Cell Biol. , vol.21 , pp. 109-118
    • Staley, J.P.1    Woolford, J.L.2
  • 112
    • 0041468805 scopus 로고    scopus 로고
    • Phosphorylation of mammalian eukaryotic translation initiation factor 6 and its Saccharomyces cerevisiae homologue Tif6p: evidence that phosphorylation of Tif6p regulates its nucleocytoplasmic distribution and is required for yeast cell growth
    • Basu U., Si K., Deng H., Maitra U. Phosphorylation of mammalian eukaryotic translation initiation factor 6 and its Saccharomyces cerevisiae homologue Tif6p: evidence that phosphorylation of Tif6p regulates its nucleocytoplasmic distribution and is required for yeast cell growth. Mol. Cell. Biol. 2003, 23:6187-6199.
    • (2003) Mol. Cell. Biol. , vol.23 , pp. 6187-6199
    • Basu, U.1    Si, K.2    Deng, H.3    Maitra, U.4
  • 113
    • 44349179816 scopus 로고    scopus 로고
    • The Saccharomyces cerevisiae 60 S ribosome biogenesis factor Tif6p is regulated by Hrr25p-mediated phosphorylation
    • Ray P., Basu U., Ray A., Majumdar R., Deng H., Maitra U. The Saccharomyces cerevisiae 60 S ribosome biogenesis factor Tif6p is regulated by Hrr25p-mediated phosphorylation. J. Biol. Chem. 2008, 283:9681-9691.
    • (2008) J. Biol. Chem. , vol.283 , pp. 9681-9691
    • Ray, P.1    Basu, U.2    Ray, A.3    Majumdar, R.4    Deng, H.5    Maitra, U.6
  • 114
    • 0036231380 scopus 로고    scopus 로고
    • Yeast Rio1p is the founding member of a novel subfamily of protein serine kinases involved in the control of cell cycle progression
    • Angermayr M., Roidl A., Bandlow W. Yeast Rio1p is the founding member of a novel subfamily of protein serine kinases involved in the control of cell cycle progression. Mol. Microbiol. 2002, 44:309-324.
    • (2002) Mol. Microbiol. , vol.44 , pp. 309-324
    • Angermayr, M.1    Roidl, A.2    Bandlow, W.3
  • 115
    • 0037928101 scopus 로고    scopus 로고
    • Rio2p, an evolutionarily conserved, low abundant protein kinase essential for processing of 20 S Pre-rRNA in Saccharomyces cerevisiae
    • Geerlings T.H., Faber A.W., Bister M.D., Vos J.C., Raue H.A. Rio2p, an evolutionarily conserved, low abundant protein kinase essential for processing of 20 S Pre-rRNA in Saccharomyces cerevisiae. J. Biol. Chem. 2003, 278:22537-22545.
    • (2003) J. Biol. Chem. , vol.278 , pp. 22537-22545
    • Geerlings, T.H.1    Faber, A.W.2    Bister, M.D.3    Vos, J.C.4    Raue, H.A.5
  • 117
    • 27844479168 scopus 로고    scopus 로고
    • A family portrait of the RIO kinases
    • LaRonde-LeBlanc N., Wlodawer A. A family portrait of the RIO kinases. J. Biol. Chem. 2005, 280:37297-37300.
    • (2005) J. Biol. Chem. , vol.280 , pp. 37297-37300
    • LaRonde-LeBlanc, N.1    Wlodawer, A.2
  • 118
    • 29144535787 scopus 로고    scopus 로고
    • The RIO kinases: an atypical protein kinase family required for ribosome biogenesis and cell cycle progression
    • LaRonde-LeBlanc N., Wlodawer A. The RIO kinases: an atypical protein kinase family required for ribosome biogenesis and cell cycle progression. Biochim. Biophys. Acta 2005, 1754:14-24.
    • (2005) Biochim. Biophys. Acta , vol.1754 , pp. 14-24
    • LaRonde-LeBlanc, N.1    Wlodawer, A.2
  • 119
    • 0142011067 scopus 로고    scopus 로고
    • Evolution and classification of P-loop kinases and related proteins
    • Leipe D.D., Koonin E.V., Aravind L. Evolution and classification of P-loop kinases and related proteins. J. Mol. Biol. 2003, 333:781-815.
    • (2003) J. Mol. Biol. , vol.333 , pp. 781-815
    • Leipe, D.D.1    Koonin, E.V.2    Aravind, L.3
  • 120
    • 33745041480 scopus 로고    scopus 로고
    • Evolutionary relationships and structural mechanisms of AAA+ proteins
    • Erzberger J.P., Berger J.M. Evolutionary relationships and structural mechanisms of AAA+ proteins. Annu. Rev. Biophys. Biomol. Struct. 2006, 35:93-114.
    • (2006) Annu. Rev. Biophys. Biomol. Struct. , vol.35 , pp. 93-114
    • Erzberger, J.P.1    Berger, J.M.2
  • 121
    • 0034632063 scopus 로고    scopus 로고
    • AAA proteins: lords of the ring
    • Vale R.D. AAA proteins: lords of the ring. J. Cell Biol. 2000, 150:13-19.
    • (2000) J. Cell Biol. , vol.150 , pp. 13-19
    • Vale, R.D.1
  • 123
    • 0037178795 scopus 로고    scopus 로고
    • Structural and enzymatic properties of the AAA protein Drg1p from Saccharomyces cerevisiae. Decoupling of intracellular function from ATPase activity and hexamerization
    • Zakalskiy A., Hogenauer G., Ishikawa T., Wehrschutz-Sigl E., Wendler F., Teis D., Zisser G., Steven A.C., Bergler H. Structural and enzymatic properties of the AAA protein Drg1p from Saccharomyces cerevisiae. Decoupling of intracellular function from ATPase activity and hexamerization. J. Biol. Chem. 2002, 277:26788-26795.
    • (2002) J. Biol. Chem. , vol.277 , pp. 26788-26795
    • Zakalskiy, A.1    Hogenauer, G.2    Ishikawa, T.3    Wehrschutz-Sigl, E.4    Wendler, F.5    Teis, D.6    Zisser, G.7    Steven, A.C.8    Bergler, H.9
  • 126
    • 33845939821 scopus 로고    scopus 로고
    • Cdc48 (p97): a "molecular gearbox" in the ubiquitin pathway?
    • Jentsch S., Rumpf S. Cdc48 (p97): a "molecular gearbox" in the ubiquitin pathway?. Trends Biochem. Sci. 2007, 32:6-11.
    • (2007) Trends Biochem. Sci. , vol.32 , pp. 6-11
    • Jentsch, S.1    Rumpf, S.2
  • 127
    • 33748574525 scopus 로고    scopus 로고
    • Formation and nuclear export of preribosomes are functionally linked to the small-ubiquitin-related modifier pathway
    • Panse V.G., Kressler D., Pauli A., Petfalski E., Gnadig M., Tollervey D., Hurt E. Formation and nuclear export of preribosomes are functionally linked to the small-ubiquitin-related modifier pathway. Traffic 2006, 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
  • 128
    • 11244304243 scopus 로고    scopus 로고
    • Rea1, a Dynein-related nuclear AAA-ATPase, is involved in late rRNA processing and nuclear export of 60 S subunits
    • Galani K., Nissan T.A., Petfalski E., Tollervey D., Hurt E. Rea1, a Dynein-related nuclear AAA-ATPase, is involved in late rRNA processing and nuclear export of 60 S subunits. J. Biol. Chem. 2004, 279:55411-55418.
    • (2004) J. Biol. Chem. , vol.279 , pp. 55411-55418
    • Galani, K.1    Nissan, T.A.2    Petfalski, E.3    Tollervey, D.4    Hurt, E.5
  • 129
    • 0005073263 scopus 로고    scopus 로고
    • Expression and genomic analysis of midasin, a novel and highly conserved AAA protein distantly related to dynein
    • Garbarino J.E., Gibbons I.R. Expression and genomic analysis of midasin, a novel and highly conserved AAA protein distantly related to dynein. BMC Genomics 2002, 3:18-28.
    • (2002) BMC Genomics , vol.3 , pp. 18-28
    • Garbarino, J.E.1    Gibbons, I.R.2
  • 130
    • 14744301484 scopus 로고    scopus 로고
    • Functional link between ribosome formation and biogenesis of iron-sulfur proteins
    • Yarunin A., Panse V.G., Petfalski E., Dez C., Tollervey D., Hurt E.C. Functional link between ribosome formation and biogenesis of iron-sulfur proteins. EMBO J. 2005, 24:580-588.
    • (2005) EMBO J. , vol.24 , pp. 580-588
    • Yarunin, A.1    Panse, V.G.2    Petfalski, E.3    Dez, C.4    Tollervey, D.5    Hurt, E.C.6
  • 131
    • 27644434348 scopus 로고    scopus 로고
    • The novel ATP-binding cassette protein ARB1 is a shuttling factor that stimulates 40S and 60S ribosome biogenesis
    • Dong J., Lai R., Jennings J.L., Link A.J., Hinnebusch A.G. The novel ATP-binding cassette protein ARB1 is a shuttling factor that stimulates 40S and 60S ribosome biogenesis. Mol. Cell. Biol. 2005, 25:9859-9873.
    • (2005) Mol. Cell. Biol. , vol.25 , pp. 9859-9873
    • Dong, J.1    Lai, R.2    Jennings, J.L.3    Link, A.J.4    Hinnebusch, A.G.5
  • 132
    • 4744350877 scopus 로고    scopus 로고
    • The essential ATP-binding cassette protein RLI1 functions in translation by promoting preinitiation complex assembly
    • Dong J., Lai R., Nielsen K., Fekete C.A., Qiu H., Hinnebusch A.G. The essential ATP-binding cassette protein RLI1 functions in translation by promoting preinitiation complex assembly. J. Biol. Chem. 2004, 279:42157-42168.
    • (2004) J. Biol. Chem. , vol.279 , pp. 42157-42168
    • Dong, J.1    Lai, R.2    Nielsen, K.3    Fekete, C.A.4    Qiu, H.5    Hinnebusch, A.G.6
  • 134
    • 0036295212 scopus 로고    scopus 로고
    • Classification and evolution of P-loop GTPases and related ATPases
    • Leipe D.D., Wolf Y.I., Koonin E.V., Aravind L. Classification and evolution of P-loop GTPases and related ATPases. J. Mol. Biol. 2002, 317:41-72.
    • (2002) J. Mol. Biol. , vol.317 , pp. 41-72
    • Leipe, D.D.1    Wolf, Y.I.2    Koonin, E.V.3    Aravind, L.4
  • 135
    • 27944487604 scopus 로고    scopus 로고
    • An essential GTPase promotes assembly of preribosomal RNA processing complexes
    • Karbstein K., Jonas S., Doudna J.A. An essential GTPase promotes assembly of preribosomal RNA processing complexes. Mol. Cell 2005, 20:633-643.
    • (2005) Mol. Cell , vol.20 , pp. 633-643
    • Karbstein, K.1    Jonas, S.2    Doudna, J.A.3
  • 136
    • 0034846319 scopus 로고    scopus 로고
    • Bms1p, a G-domain-containing protein, associates with Rcl1p and is required for 18S rRNA biogenesis in yeast
    • Wegierski T., Billy E., Nasr F., Filipowicz W. Bms1p, a G-domain-containing protein, associates with Rcl1p and is required for 18S rRNA biogenesis in yeast. RNA 2001, 7:1254-1267.
    • (2001) RNA , vol.7 , pp. 1254-1267
    • Wegierski, T.1    Billy, E.2    Nasr, F.3    Filipowicz, W.4
  • 137
    • 30744437648 scopus 로고    scopus 로고
    • GTP-dependent formation of a ribonucleoprotein subcomplex required for ribosome biogenesis
    • Karbstein K., Doudna J.A. GTP-dependent formation of a ribonucleoprotein subcomplex required for ribosome biogenesis. J. Mol. Biol. 2006, 356:432-443.
    • (2006) J. Mol. Biol. , vol.356 , pp. 432-443
    • Karbstein, K.1    Doudna, J.A.2
  • 138
    • 66449137253 scopus 로고    scopus 로고
    • Sdo1p, the yeast orthologue of Shwachman-Bodian-Diamond syndrome protein, binds RNA and interacts with nuclear rRNA-processing factors
    • Luz J.S., Georg R.C., Gomes C.H., Machado-Santelli G.M., Oliveira C.C. Sdo1p, the yeast orthologue of Shwachman-Bodian-Diamond syndrome protein, binds RNA and interacts with nuclear rRNA-processing factors. Yeast 2009, 26:287-298.
    • (2009) Yeast , vol.26 , pp. 287-298
    • Luz, J.S.1    Georg, R.C.2    Gomes, C.H.3    Machado-Santelli, G.M.4    Oliveira, C.C.5
  • 139
    • 0021160131 scopus 로고
    • Ribosomal subunit antiassociation activity in rabbit reticulocyte lysates. Evidence for a low molecular weight ribosomal subunit antiassociation protein factor (Mr=25,000)
    • Raychaudhuri P., Stringer E.A., Valenzuela D.M., Maitra U. Ribosomal subunit antiassociation activity in rabbit reticulocyte lysates. Evidence for a low molecular weight ribosomal subunit antiassociation protein factor (Mr=25,000). J. Biol. Chem. 1984, 259:11930-11935.
    • (1984) J. Biol. Chem. , vol.259 , pp. 11930-11935
    • Raychaudhuri, P.1    Stringer, E.A.2    Valenzuela, D.M.3    Maitra, U.4
  • 141
    • 34548606694 scopus 로고    scopus 로고
    • Role of GTPases in ribosome assembly
    • Karbstein K. Role of GTPases in ribosome assembly. Biopolymers 2007, 87:1-11.
    • (2007) Biopolymers , vol.87 , pp. 1-11
    • Karbstein, K.1
  • 142
    • 51549105967 scopus 로고    scopus 로고
    • Crystal structure of YlqF, a circularly permuted GTPase: implications for its GTPase activation in 50 S ribosomal subunit assembly
    • Kim do J., Jang J.Y., Yoon H.J., Suh S.W. Crystal structure of YlqF, a circularly permuted GTPase: implications for its GTPase activation in 50 S ribosomal subunit assembly. Proteins 2008, 72:1363-1370.
    • (2008) Proteins , vol.72 , pp. 1363-1370
    • Kim do, J.1    Jang, J.Y.2    Yoon, H.J.3    Suh, S.W.4
  • 143
    • 34548473560 scopus 로고    scopus 로고
    • Isolation and characterization of a dominant negative mutant of Bacillus subtilis GTP-binding protein, YlqF, essential for biogenesis and maintenance of the 50 S ribosomal subunit
    • Matsuo Y., Oshima T., Loh P.C., Morimoto T., Ogasawara N. Isolation and characterization of a dominant negative mutant of Bacillus subtilis GTP-binding protein, YlqF, essential for biogenesis and maintenance of the 50 S ribosomal subunit. J. Biol. Chem. 2007, 282:25270-25277.
    • (2007) J. Biol. Chem. , vol.282 , pp. 25270-25277
    • Matsuo, Y.1    Oshima, T.2    Loh, P.C.3    Morimoto, T.4    Ogasawara, N.5
  • 144
    • 33646371247 scopus 로고    scopus 로고
    • The GTP-binding protein YlqF participates in the late step of 50 S ribosomal subunit assembly in Bacillus subtilis
    • Matsuo Y., Morimoto T., Kuwano M., Loh P.C., Oshima T., Ogasawara N. The GTP-binding protein YlqF participates in the late step of 50 S ribosomal subunit assembly in Bacillus subtilis. J. Biol. Chem. 2006, 281:8110-8117.
    • (2006) J. Biol. Chem. , vol.281 , pp. 8110-8117
    • Matsuo, Y.1    Morimoto, T.2    Kuwano, M.3    Loh, P.C.4    Oshima, T.5    Ogasawara, N.6
  • 145
    • 33645050402 scopus 로고    scopus 로고
    • The essential GTPase RbgA (YlqF) is required for 50S ribosome assembly in Bacillus subtilis
    • Uicker W.C., Schaefer L., Britton R.A. The essential GTPase RbgA (YlqF) is required for 50S ribosome assembly in Bacillus subtilis. Mol. Microbiol. 2006, 59:528-540.
    • (2006) Mol. Microbiol. , vol.59 , pp. 528-540
    • Uicker, W.C.1    Schaefer, L.2    Britton, R.A.3
  • 146
    • 33747729420 scopus 로고    scopus 로고
    • The NUG1 GTPase reveals and N-terminal RNA-binding domain that is essential for association with 60 S pre-ribosomal particles
    • Bassler J., Kallas M., Hurt E. The NUG1 GTPase reveals and N-terminal RNA-binding domain that is essential for association with 60 S pre-ribosomal particles. J. Biol. Chem. 2006, 281:24737-24744.
    • (2006) J. Biol. Chem. , vol.281 , pp. 24737-24744
    • Bassler, J.1    Kallas, M.2    Hurt, E.3
  • 147
    • 65649104440 scopus 로고    scopus 로고
    • A convergence of rRNA and mRNA quality control pathways revealed by mechanistic analysis of nonfunctional rRNA decay
    • Cole S.E., LaRiviere F.J., Merrikh C.N., Moore M.J. A convergence of rRNA and mRNA quality control pathways revealed by mechanistic analysis of nonfunctional rRNA decay. Mol. Cell 2009, 34:440-450.
    • (2009) Mol. Cell , vol.34 , pp. 440-450
    • Cole, S.E.1    LaRiviere, F.J.2    Merrikh, C.N.3    Moore, M.J.4
  • 148
    • 65249168677 scopus 로고    scopus 로고
    • A role for ubiquitin in the clearance of nonfunctional rRNAs
    • Fujii K., Kitabatake M., Sakata T., Miyata A., Ohno M. A role for ubiquitin in the clearance of nonfunctional rRNAs. Genes Dev. 2009, 23:963-974.
    • (2009) Genes Dev. , vol.23 , pp. 963-974
    • Fujii, K.1    Kitabatake, M.2    Sakata, T.3    Miyata, A.4    Ohno, M.5
  • 149
    • 34447119616 scopus 로고    scopus 로고
    • The exosome and RNA quality control in the nucleus
    • Vanacova S., Stefl R. The exosome and RNA quality control in the nucleus. EMBO Rep. 2007, 8:651-657.
    • (2007) EMBO Rep. , vol.8 , pp. 651-657
    • Vanacova, S.1    Stefl, R.2
  • 150
    • 42049099544 scopus 로고    scopus 로고
    • Ribosomal dysfunction and inherited marrow failure
    • Ganapathi K.A., Shimamura A. Ribosomal dysfunction and inherited marrow failure. Br. J. Haematol. 2008, 141:376-387.
    • (2008) Br. J. Haematol. , vol.141 , pp. 376-387
    • Ganapathi, K.A.1    Shimamura, A.2
  • 153
    • 50649096622 scopus 로고    scopus 로고
    • The role of human ribosomal proteins in the maturation of rRNA and ribosome production
    • Robledo S., Idol R.A., Crimmins D.L., Ladenson J.H., Mason P.J., Bessler M. The role of human ribosomal proteins in the maturation of rRNA and ribosome production. RNA 2008, 14:1918-1929.
    • (2008) RNA , vol.14 , pp. 1918-1929
    • Robledo, S.1    Idol, R.A.2    Crimmins, D.L.3    Ladenson, J.H.4    Mason, P.J.5    Bessler, M.6
  • 156
    • 60749111467 scopus 로고    scopus 로고
    • Dyskerin, telomerase and the DNA damage response
    • Gu B., Bessler M., Mason P.J. Dyskerin, telomerase and the DNA damage response. Cell Cycle 2009, 8:6-10.
    • (2009) Cell Cycle , vol.8 , pp. 6-10
    • Gu, B.1    Bessler, M.2    Mason, P.J.3
  • 157
    • 38349144367 scopus 로고    scopus 로고
    • Dyskeratosis congenita: a genetic disorder of many faces
    • Kirwan M., Dokal I. Dyskeratosis congenita: a genetic disorder of many faces. Clin. Genet. 2008, 73:103-112.
    • (2008) Clin. Genet. , vol.73 , pp. 103-112
    • Kirwan, M.1    Dokal, I.2
  • 158
    • 56749105459 scopus 로고    scopus 로고
    • Cartilage-hair hypoplasia: molecular basis and heterogeneity of the immunological phenotype
    • Notarangelo L.D., Roifman C.M., Giliani S. Cartilage-hair hypoplasia: molecular basis and heterogeneity of the immunological phenotype. Curr. Opin. Allergy Clin. Immunol. 2008, 8:534-539.
    • (2008) Curr. Opin. Allergy Clin. Immunol. , vol.8 , pp. 534-539
    • Notarangelo, L.D.1    Roifman, C.M.2    Giliani, S.3
  • 159
    • 33947314376 scopus 로고    scopus 로고
    • RNase MRP RNA and human genetic diseases
    • Martin A.N., Li Y. RNase MRP RNA and human genetic diseases. Cell Res. 2007, 17:219-226.
    • (2007) Cell Res. , vol.17 , pp. 219-226
    • Martin, A.N.1    Li, Y.2
  • 162
    • 54849406775 scopus 로고    scopus 로고
    • Crosstalk between c-Myc and ribosome in ribosomal biogenesis and cancer
    • Dai M.S., Lu H. Crosstalk between c-Myc and ribosome in ribosomal biogenesis and cancer. J. Cell Biochem. 2008, 105:670-677.
    • (2008) J. Cell Biochem. , vol.105 , pp. 670-677
    • Dai, M.S.1    Lu, H.2
  • 165
    • 67649854477 scopus 로고    scopus 로고
    • Identification of protein binding sites on U3 snoRNA and pre-rRNA by UV cross-linking and high-throughput analysis of cDNAs
    • Granneman S., Kudla G., Petfalski E., Tollervey D. Identification of protein binding sites on U3 snoRNA and pre-rRNA by UV cross-linking and high-throughput analysis of cDNAs. Proc. Natl. Acad. Sci. U. S. A. 2009, 106:9613-9618.
    • (2009) Proc. Natl. Acad. Sci. U. S. A. , vol.106 , pp. 9613-9618
    • Granneman, S.1    Kudla, G.2    Petfalski, E.3    Tollervey, D.4


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