메뉴 건너뛰기




Volumn 7, Issue 3, 2008, Pages 546-559

ISG20L2, a novel vertebrate nucleolar exoribonuclease involved in ribosome biogenesis

Author keywords

[No Author keywords available]

Indexed keywords

EXORIBONUCLEASE; NUCLEAR PROTEIN; PROTEIN ISG20L2; PROTEIN SUBUNIT; RIBOSOME RNA; RNA 12S; UNCLASSIFIED DRUG;

EID: 41549160174     PISSN: 15359476     EISSN: None     Source Type: Journal    
DOI: 10.1074/mcp.M700510-MCP200     Document Type: Article
Times cited : (40)

References (76)
  • 1
    • 0035365808 scopus 로고    scopus 로고
    • Functional architecture in the cell nucleus
    • Dundr, M., and Misteli, T. (2001) Functional architecture in the cell nucleus. Biochem. J. 366, 297-310
    • (2001) Biochem. J , vol.366 , pp. 297-310
    • Dundr, M.1    Misteli, T.2
  • 2
    • 0029055194 scopus 로고
    • The nucleolus: An organelle formed by the act of building a ribosome
    • Melese, T., and Xue, Z. (1995) The nucleolus: an organelle formed by the act of building a ribosome. Curr. Opin. Cell Biol. 7, 319-324
    • (1995) Curr. Opin. Cell Biol , vol.7 , pp. 319-324
    • Melese, T.1    Xue, Z.2
  • 3
    • 30544439063 scopus 로고    scopus 로고
    • Nuclear export and cytoplasmic processing of precursors to the 40S ribosomal subunits in mammalian cells
    • Rouquette, J., Choesmel, V., and Gleizes, P. E. (2005) Nuclear export and cytoplasmic processing of precursors to the 40S ribosomal subunits in mammalian cells. EMBO J. 24, 2862-2872
    • (2005) EMBO J , vol.24 , pp. 2862-2872
    • Rouquette, J.1    Choesmel, V.2    Gleizes, P.E.3
  • 4
    • 0034193778 scopus 로고    scopus 로고
    • The nucleolus: An old factory with unexpected capabilities
    • Olson, M. O., Dundr, M., and Szebeni, A. (2000) The nucleolus: an old factory with unexpected capabilities. Trends Cell Biol. 110, 189-196
    • (2000) Trends Cell Biol , vol.110 , pp. 189-196
    • Olson, M.O.1    Dundr, M.2    Szebeni, A.3
  • 5
    • 0027367147 scopus 로고
    • Nuclear FINase MRP is required for correct processing of pre-5.8S rRNA in Saccharomyces cerevisiae
    • Schmitt, M. E., and Clayton, D. A. (1993) Nuclear FINase MRP is required for correct processing of pre-5.8S rRNA in Saccharomyces cerevisiae. Mol. Cell. Biol. 13, 7935-7941
    • (1993) Mol. Cell. Biol , vol.13 , pp. 7935-7941
    • Schmitt, M.E.1    Clayton, D.A.2
  • 6
    • 0036719183 scopus 로고    scopus 로고
    • Ngl2p is a Ccr4p-like RNA nuclease essential for the final step in 3′-end processing of 5.8S rRNA in Saccharomyces cerevisiae
    • Faber, A. W., Van Dijk, M., Raue, H. A., and Vos, J. C. (2002) Ngl2p is a Ccr4p-like RNA nuclease essential for the final step in 3′-end processing of 5.8S rRNA in Saccharomyces cerevisiae. RNA 8, 1095-1101
    • (2002) RNA , vol.8 , pp. 1095-1101
    • Faber, A.W.1    Van Dijk, M.2    Raue, H.A.3    Vos, J.C.4
  • 7
    • 0028342849 scopus 로고
    • The 5′ end of yeast 5.8S rRNA is generated by exoucleases from an upstream cleavage site
    • Henry, Y., Wood, H., Morrissey, J. P., Petfalski, E., Kearsey, S., and Tollervey, D. (1994) The 5′ end of yeast 5.8S rRNA is generated by exoucleases from an upstream cleavage site. EMBO J. 13, 2452-2463
    • (1994) EMBO J , vol.13 , pp. 2452-2463
    • Henry, Y.1    Wood, H.2    Morrissey, J.P.3    Petfalski, E.4    Kearsey, S.5    Tollervey, D.6
  • 8
    • 0034653440 scopus 로고    scopus 로고
    • Three conserved members of the RNase D family have unique and overlapping functions in the processing of 5S, 5.8S, U4, U5, RNase MRP and RNase P RNAs in yeast
    • van Hoof, A., Lennertz, P., and Parker, R. (2000) Three conserved members of the RNase D family have unique and overlapping functions in the processing of 5S, 5.8S, U4, U5, RNase MRP and RNase P RNAs in yeast. EMBO J. 19, 1357-1365
    • (2000) EMBO J , vol.19 , pp. 1357-1365
    • van Hoof, A.1    Lennertz, P.2    Parker, R.3
  • 9
    • 0029939247 scopus 로고    scopus 로고
    • The 3′ end of yeast 5.8S rRNA is generated by an exonuclease processing mechanism
    • Mitchell, P., Petfalski, E., and Tollervey, D. (1996) The 3′ end of yeast 5.8S rRNA is generated by an exonuclease processing mechanism. Genes Dev. 10, 502-513
    • (1996) Genes Dev , vol.10 , pp. 502-513
    • Mitchell, P.1    Petfalski, E.2    Tollervey, D.3
  • 10
    • 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
  • 12
    • 34249868208 scopus 로고    scopus 로고
    • Optimization of ribosome structure and function by rRNA base modification
    • Baxter-Roshek, J. L., Petrov, A. N., and Dinman, J. D. (2007) Optimization of ribosome structure and function by rRNA base modification. PLoS ONE 2, e174
    • (2007) PLoS ONE , vol.2
    • Baxter-Roshek, J.L.1    Petrov, A.N.2    Dinman, J.D.3
  • 15
    • 2342538485 scopus 로고    scopus 로고
    • Aberrant mRNA translation in cancer pathogenesis: An old concept revisited comes finally of age
    • Pandolfi, P. P. (2004) Aberrant mRNA translation in cancer pathogenesis: an old concept revisited comes finally of age. Oncogene 23, 3134-3137
    • (2004) Oncogene , vol.23 , pp. 3134-3137
    • Pandolfi, P.P.1
  • 17
    • 0033509092 scopus 로고    scopus 로고
    • Protein trans-acting factors involved in ribosome biogenesis in Saccharomyces cerevisiae
    • Kressler, D., Linder, P., and de La Cruz, J. (1999) Protein trans-acting factors involved in ribosome biogenesis in Saccharomyces cerevisiae. Mol, Cell. Biol. 19, 7897-7912
    • (1999) Mol, Cell. Biol , vol.19 , pp. 7897-7912
    • Kressler, D.1    Linder, P.2    de La Cruz, J.3
  • 18
    • 0033367325 scopus 로고    scopus 로고
    • Ribosome synthesis in Saccharomyces cerevislae
    • Venema, J., and Tollervey, D. (1999) Ribosome synthesis in Saccharomyces cerevislae. Annu. Rev. Genet 33, 261-311
    • (1999) Annu. Rev. Genet , vol.33 , pp. 261-311
    • Venema, J.1    Tollervey, D.2
  • 20
    • 0038738334 scopus 로고    scopus 로고
    • Pre-ribosomes on the road from the nucleolus to the cytoplasm
    • Tschochner, H., and Hurt, E. (2003) Pre-ribosomes on the road from the nucleolus to the cytoplasm. Trends Cell Biol. 13, 255-263
    • (2003) Trends Cell Biol , vol.13 , pp. 255-263
    • Tschochner, H.1    Hurt, E.2
  • 27
    • 3042666256 scopus 로고    scopus 로고
    • MUSCLE: Multiple sequence alignment with high accuracy and high throughput
    • Edgar, R. C. (2004) MUSCLE: multiple sequence alignment with high accuracy and high throughput. Nucleic Acids Res. 32, 1792-1797
    • (2004) Nucleic Acids Res , vol.32 , pp. 1792-1797
    • Edgar, R.C.1
  • 28
    • 0242578620 scopus 로고    scopus 로고
    • A simple, fast, and accurate algorithm to estimate large phylogenies by maximum likelihood
    • Guindon, S., and Gascuel, O. (2003) A simple, fast, and accurate algorithm to estimate large phylogenies by maximum likelihood. Syst. Biol. 52, 696-704
    • (2003) Syst. Biol , vol.52 , pp. 696-704
    • Guindon, S.1    Gascuel, O.2
  • 29
    • 23144433822 scopus 로고    scopus 로고
    • PHYML Online - a web server for fast maximum likelihood-based phylogenetic inference
    • Guindon, S., Lethiec, F., Duroux, P., and Gascuel, O. (2005) PHYML Online - a web server for fast maximum likelihood-based phylogenetic inference. Nucleic Acids Res. 33, W557-W559
    • (2005) Nucleic Acids Res , vol.33
    • Guindon, S.1    Lethiec, F.2    Duroux, P.3    Gascuel, O.4
  • 30
    • 0026691182 scopus 로고
    • The rapid generation of mutation data matrices from protein sequences
    • Jones, D. T., Taylor, W. R., and Thomton, J. M. (1992) The rapid generation of mutation data matrices from protein sequences. Comput. Appl. Biosci. 8, 275-282
    • (1992) Comput. Appl. Biosci , vol.8 , pp. 275-282
    • Jones, D.T.1    Taylor, W.R.2    Thomton, J.M.3
  • 34
    • 0035283033 scopus 로고    scopus 로고
    • Exoribonuclease superfamilies: Structural analysis and phylogenetic distribution
    • Zuo, Y., and Deutscher, M. P. (2001) Exoribonuclease superfamilies: structural analysis and phylogenetic distribution. Nucleic Acids Res. 29, 1017-1026
    • (2001) Nucleic Acids Res , vol.29 , pp. 1017-1026
    • Zuo, Y.1    Deutscher, M.P.2
  • 35
    • 0036800015 scopus 로고    scopus 로고
    • Deletions in the S1 domain of Rrp5p cause processing at a novel site in ITS1 of yeast pre-rRNA that depends on Rex4p
    • Eppens, N. A., Faber, A. W., Rondaij, M., Jahangir, R. S., van Hemert, S., Vos, J. C., Venema, J., and Raue, H. A. (2002) Deletions in the S1 domain of Rrp5p cause processing at a novel site in ITS1 of yeast pre-rRNA that depends on Rex4p. Nucleic Acids Res. 30, 4222-4231
    • (2002) Nucleic Acids Res , vol.30 , pp. 4222-4231
    • Eppens, N.A.1    Faber, A.W.2    Rondaij, M.3    Jahangir, R.S.4    van Hemert, S.5    Vos, J.C.6    Venema, J.7    Raue, H.A.8
  • 36
    • 9344261419 scopus 로고    scopus 로고
    • The RNA catabolic enzymes Rex4p, Rnt1p, and Dbr1p show genetic interaction with trans-acting factors involved in processing of ITS1 in Saccharomyces cerevisiae pre-rRNA
    • Faber, A. W., Vos, J. C., Vos, H. R., Ghazal, G., Elela, S. A., and Raue, H. A. (2004) The RNA catabolic enzymes Rex4p, Rnt1p, and Dbr1p show genetic interaction with trans-acting factors involved in processing of ITS1 in Saccharomyces cerevisiae pre-rRNA. RNA 10, 1946-1956
    • (2004) RNA , vol.10 , pp. 1946-1956
    • Faber, A.W.1    Vos, J.C.2    Vos, H.R.3    Ghazal, G.4    Elela, S.A.5    Raue, H.A.6
  • 37
    • 0030799493 scopus 로고    scopus 로고
    • Molecular cloning of a new interferon-induced PML nuclear body-associated protein
    • Gongora, C., David, G., Pintard, L., Tissot, C., Hua, T. D., Dejean, A., and Mechti, N. (1997) Molecular cloning of a new interferon-induced PML nuclear body-associated protein. J. Biol. Chem. 272, 19457-19463
    • (1997) J. Biol. Chem , vol.272 , pp. 19457-19463
    • Gongora, C.1    David, G.2    Pintard, L.3    Tissot, C.4    Hua, T.D.5    Dejean, A.6    Mechti, N.7
  • 38
    • 0038521287 scopus 로고    scopus 로고
    • ISG20, a new interferon-induced RNase specific for single-stranded RNA, defines an alternative antiviral pathway against RNA genomic viruses
    • Espert, L., Degols, G., Gongora, C., Blondel, D., Williams, B. R., Silverman, R. H., and Mechti, N. (2003) ISG20, a new interferon-induced RNase specific for single-stranded RNA, defines an alternative antiviral pathway against RNA genomic viruses. J. Biol. Chem. 278, 16151-16158
    • (2003) J. Biol. Chem , vol.278 , pp. 16151-16158
    • Espert, L.1    Degols, G.2    Gongora, C.3    Blondel, D.4    Williams, B.R.5    Silverman, R.H.6    Mechti, N.7
  • 39
    • 0034602152 scopus 로고    scopus 로고
    • Identification and characterization of a novel factor that regulates quinone reductase gene transcriptional activity
    • Montano, M. M., Wittmann, B. M., and Bianco, N. R. (2000) Identification and characterization of a novel factor that regulates quinone reductase gene transcriptional activity. J. Biol. Chem. 275, 34306-34313
    • (2000) J. Biol. Chem , vol.275 , pp. 34306-34313
    • Montano, M.M.1    Wittmann, B.M.2    Bianco, N.R.3
  • 40
    • 33746458898 scopus 로고    scopus 로고
    • The exonuclease ISG20 mainly localizes in the nucleolus and the Cajal (Coiled) bodies and is associated with nuclear SMN protein-containing complexes
    • Espert, L., Eldin, P., Gongora, C., Bayard, B., Harper, F., Chelbi-Alix, M. K., Bertrand, E., Degols, G., and Mechti, N. (2006) The exonuclease ISG20 mainly localizes in the nucleolus and the Cajal (Coiled) bodies and is associated with nuclear SMN protein-containing complexes. J. Cell. Biochem. 98, 1320-1333
    • (2006) J. Cell. Biochem , vol.98 , pp. 1320-1333
    • Espert, L.1    Eldin, P.2    Gongora, C.3    Bayard, B.4    Harper, F.5    Chelbi-Alix, M.K.6    Bertrand, E.7    Degols, G.8    Mechti, N.9
  • 41
    • 0035793376 scopus 로고    scopus 로고
    • Protein dynamics: Implications for nuclear architecture and gene expression
    • Misteli, T. (2001) Protein dynamics: implications for nuclear architecture and gene expression. Science 291, 843-847
    • (2001) Science , vol.291 , pp. 843-847
    • Misteli, T.1
  • 42
    • 0027466092 scopus 로고
    • Alternative pre-rRNA processing pathways in human cells and their alteration by cycloheximide inhibition of protein synthesis
    • Hadjiolova, K. V., Nicoloso, M., Mazan, S., Hadjiolov, A. A., and Bachellerie, J. P. (1993) Alternative pre-rRNA processing pathways in human cells and their alteration by cycloheximide inhibition of protein synthesis. Eur. J. Biochem. 212, 211-215
    • (1993) Eur. J. Biochem , vol.212 , pp. 211-215
    • Hadjiolova, K.V.1    Nicoloso, M.2    Mazan, S.3    Hadjiolov, A.A.4    Bachellerie, J.P.5
  • 43
    • 0027184481 scopus 로고
    • A general two-metal-ion mechanism for catalytic RNA
    • Steitz, T. A., and Steitz, J. A. (1993) A general two-metal-ion mechanism for catalytic RNA. Proc. Natl. Acad. Sci. U. S. A. 90, 6498-6502
    • (1993) Proc. Natl. Acad. Sci. U. S. A , vol.90 , pp. 6498-6502
    • Steitz, T.A.1    Steitz, J.A.2
  • 44
    • 0022366980 scopus 로고
    • RNase T is responsible for the and-turnover of tRNA in Escherichia coil
    • Deutscher, M. P., Marlor, C. W., and Zaniewski, R. (1985) RNase T is responsible for the and-turnover of tRNA in Escherichia coil. Proc. Natl. Acad. Sci. U. S. A. 82, 6427-6430
    • (1985) Proc. Natl. Acad. Sci. U. S. A , vol.82 , pp. 6427-6430
    • Deutscher, M.P.1    Marlor, C.W.2    Zaniewski, R.3
  • 45
    • 0030576503 scopus 로고    scopus 로고
    • Maturation pathways for E. coli tRNA precursors: A random multienzyme process in vivo
    • Li, Z., and Deutscher, M. P. (1996) Maturation pathways for E. coli tRNA precursors: a random multienzyme process in vivo. Cell 86, 503-512
    • (1996) Cell , vol.86 , pp. 503-512
    • Li, Z.1    Deutscher, M.P.2
  • 46
    • 0029151159 scopus 로고
    • The tRNA processing enzyme RNase T is essential for maturation of 5S RNA
    • Li, Z., and Deutscher, M. P. (1995) The tRNA processing enzyme RNase T is essential for maturation of 5S RNA. Proc. Natl. Acad. Sci. U. S. A. 92, 6883-6886
    • (1995) Proc. Natl. Acad. Sci. U. S. A , vol.92 , pp. 6883-6886
    • Li, Z.1    Deutscher, M.P.2
  • 47
    • 0032951885 scopus 로고    scopus 로고
    • Maturation of 23S ribosomal RNA requires the exoribonuclease RNase T
    • Li, Z., Pandit, S., and Deutscher, M. P. (1999) Maturation of 23S ribosomal RNA requires the exoribonuclease RNase T. RNA 5, 139-146
    • (1999) RNA , vol.5 , pp. 139-146
    • Li, Z.1    Pandit, S.2    Deutscher, M.P.3
  • 48
    • 0032539857 scopus 로고    scopus 로고
    • 3′ exoribonucleolytic trimming is a common feature of the maturation of small, stable RNAs in Escherichia coli
    • Li, Z., Pandit, S., and Deutscher, M. P. (1998) 3′ exoribonucleolytic trimming is a common feature of the maturation of small, stable RNAs in Escherichia coli. Proc. Natl. Acad. Sci. U. S. A. 95, 2856-2861
    • (1998) Proc. Natl. Acad. Sci. U. S. A , vol.95 , pp. 2856-2861
    • Li, Z.1    Pandit, S.2    Deutscher, M.P.3
  • 49
    • 0016817098 scopus 로고
    • A novel oligoribonuclease of Escherichia coil. I. Isolation and properties
    • Niyogi, S. K., and Datta, A. K. (1975) A novel oligoribonuclease of Escherichia coil. I. Isolation and properties. J. Biol. Chem. 250, 7307-7312
    • (1975) J. Biol. Chem , vol.250 , pp. 7307-7312
    • Niyogi, S.K.1    Datta, A.K.2
  • 50
    • 0033551137 scopus 로고    scopus 로고
    • Oligoribonuclease is an essential component of the mRNA decay pathway
    • Ghosh, S., and Deutscher, M. P. (1999) Oligoribonuclease is an essential component of the mRNA decay pathway. Proc. Natl. Acad. Sci. U. S. A. 96, 4372-4377
    • (1999) Proc. Natl. Acad. Sci. U. S. A , vol.96 , pp. 4372-4377
    • Ghosh, S.1    Deutscher, M.P.2
  • 51
    • 0026630153 scopus 로고
    • Properties of a HeLa cell 3′ exonuclease specific for degrading poly(A) tails of mammalian mRNA
    • Astrom, J., Astrom, A., and Virtanen, A. (1992) Properties of a HeLa cell 3′ exonuclease specific for degrading poly(A) tails of mammalian mRNA. J. Biol. Chem. 267, 18154-18159
    • (1992) J. Biol. Chem , vol.267 , pp. 18154-18159
    • Astrom, J.1    Astrom, A.2    Virtanen, A.3
  • 52
    • 0030070804 scopus 로고    scopus 로고
    • The yeast Pan2 protein is required for poly(A)-binding protein-stimulated poly(A)-nuclease activity
    • Boeck, R., Tarun, S., Jr., Rieger, M., Deardorff, J.A., Muller-Auer, S., and Sachs, A. B. (1996) The yeast Pan2 protein is required for poly(A)-binding protein-stimulated poly(A)-nuclease activity. J. Biol. Chem. 271, 432-438
    • (1996) J. Biol. Chem , vol.271 , pp. 432-438
    • Boeck, R.1    Tarun Jr., S.2    Rieger, M.3    Deardorff, J.A.4    Muller-Auer, S.5    Sachs, A.B.6
  • 53
    • 0034604553 scopus 로고    scopus 로고
    • A 54-kDa fragment of the poly(A)-specific ribonuclease is an oligomeric, processive, and cap-interacting poly(A)-specific 3′ exonuclease
    • Martinez, J., Ren, Y. G., Thuresson, A. C., Hellman, U., Astrom, J., and Virtanen, A. (2000) A 54-kDa fragment of the poly(A)-specific ribonuclease is an oligomeric, processive, and cap-interacting poly(A)-specific 3′ exonuclease. J. Biol. Chem. 275, 24222-24230
    • (2000) J. Biol. Chem , vol.275 , pp. 24222-24230
    • Martinez, J.1    Ren, Y.G.2    Thuresson, A.C.3    Hellman, U.4    Astrom, J.5    Virtanen, A.6
  • 54
    • 0037147256 scopus 로고    scopus 로고
    • Zuo, Y., and Deutscher, M. P. (2002) Mechanism of action of RNase T. I. Identification of residues required for catalysis, substrate binding, and dimerization. J. Biol. Chem. 277, 50155-50159
    • Zuo, Y., and Deutscher, M. P. (2002) Mechanism of action of RNase T. I. Identification of residues required for catalysis, substrate binding, and dimerization. J. Biol. Chem. 277, 50155-50159
  • 55
    • 0347093310 scopus 로고    scopus 로고
    • Identification of a human cytoplasmic poly(A) nuclease complex stimulated by poly(A)-binding protein
    • Uchida, N., Hoshino, S., and Katada, T. (2004) Identification of a human cytoplasmic poly(A) nuclease complex stimulated by poly(A)-binding protein. J. Biol. Chem. 279, 1383-1391
    • (2004) J. Biol. Chem , vol.279 , pp. 1383-1391
    • Uchida, N.1    Hoshino, S.2    Katada, T.3
  • 56
    • 0021169997 scopus 로고
    • Ribonuclease T: New exoribonuclease possibly involved in end-turnover of tRNA
    • Deutscher, M. P., Marlor, C. W., and Zaniewski, R. (1984) Ribonuclease T: new exoribonuclease possibly involved in end-turnover of tRNA. Proc. Natl. Acad. Sci. U. S. A. 81, 4290-4293
    • (1984) Proc. Natl. Acad. Sci. U. S. A , vol.81 , pp. 4290-4293
    • Deutscher, M.P.1    Marlor, C.W.2    Zaniewski, R.3
  • 57
    • 0035912937 scopus 로고    scopus 로고
    • The human interferon- and estrogen-regulated ISG20/HEM45 gene product degrades single-stranded RNA and DNA in vitro
    • Nguyen, L. H., Espert, L., Mechti, N., and Wilson, D. M., 3rd (2001) The human interferon- and estrogen-regulated ISG20/HEM45 gene product degrades single-stranded RNA and DNA in vitro. Biochemistry 40, 7174-7179
    • (2001) Biochemistry , vol.40 , pp. 7174-7179
    • Nguyen, L.H.1    Espert, L.2    Mechti, N.3    Wilson 3rd, D.M.4
  • 58
    • 0035525579 scopus 로고    scopus 로고
    • Isolation and proteomic characterization of the major proteins of the nucleolin-binding ribonucleoprotein complexes
    • Yanagida, M., Shimamoto, A., Nishikawa, K., Furuichi, Y., Isobe, T., and Takahashi, N. (2001) Isolation and proteomic characterization of the major proteins of the nucleolin-binding ribonucleoprotein complexes. Proteomics 1, 1390-1404
    • (2001) Proteomics , vol.1 , pp. 1390-1404
    • Yanagida, M.1    Shimamoto, A.2    Nishikawa, K.3    Furuichi, Y.4    Isobe, T.5    Takahashi, N.6
  • 59
    • 0141668954 scopus 로고    scopus 로고
    • Proteomic analysis of human Nop56p-associated pre-ribosomal ribonucleoprotein complexes. Possible link between Nop56p and the nucleolar protein treacle responsible for Treacher Collins syndrome
    • Hayano, T., Yanagida, M., Yarnauchi, Y., Shinkawa, T., Isobe, T., and Takahashi, N. (2003) Proteomic analysis of human Nop56p-associated pre-ribosomal ribonucleoprotein complexes. Possible link between Nop56p and the nucleolar protein treacle responsible for Treacher Collins syndrome. J. Biol. Chem. 278, 34309-34319
    • (2003) J. Biol. Chem , vol.278 , pp. 34309-34319
    • Hayano, T.1    Yanagida, M.2    Yarnauchi, Y.3    Shinkawa, T.4    Isobe, T.5    Takahashi, N.6
  • 60
    • 0345826181 scopus 로고    scopus 로고
    • Human fibrillarin forms a sub-complex with splicing factor 2-associated p32, protein arginine methyltransferases, and tubulins α3 and β1 that is independent of its association with preribosomal ribonucleoprotein complexes
    • Yanagida, M., Hayano, T., Yamauchi, Y., Shinkawa, T., Natsume, T., Isobe, T., and Takahashi, N. (2004) Human fibrillarin forms a sub-complex with splicing factor 2-associated p32, protein arginine methyltransferases, and tubulins α3 and β1 that is independent of its association with preribosomal ribonucleoprotein complexes. J. Biol. Chem. 279, 1607-1614
    • (2004) J. Biol. Chem , vol.279 , pp. 1607-1614
    • Yanagida, M.1    Hayano, T.2    Yamauchi, Y.3    Shinkawa, T.4    Natsume, T.5    Isobe, T.6    Takahashi, N.7
  • 61
  • 62
    • 0034637578 scopus 로고    scopus 로고
    • Mapping the functional domains of nucleolar protein B23
    • Hingorani, K., Szebeni, A., and Olson, M. O. (2000) Mapping the functional domains of nucleolar protein B23. J. Biol. Chem. 275, 24451-24457
    • (2000) J. Biol. Chem , vol.275 , pp. 24451-24457
    • Hingorani, K.1    Szebeni, A.2    Olson, M.O.3
  • 63
    • 0347993098 scopus 로고    scopus 로고
    • Silencing of RNA helicase II/Gua inhibits mammalian ribosomal RNA production
    • Henning, D., So, R. B., Jin, R., Lau, L. F., and Valdez, B. C. (2003) Silencing of RNA helicase II/Gua inhibits mammalian ribosomal RNA production. J. Biol. Chem. 278, 52307-52314
    • (2003) J. Biol. Chem , vol.278 , pp. 52307-52314
    • Henning, D.1    So, R.B.2    Jin, R.3    Lau, L.F.4    Valdez, B.C.5
  • 64
    • 0023958908 scopus 로고
    • Involvement of DNA topoisomerase I in transcription of human ribosomal RNA genes
    • Zhang, H., Wang, J. C., and Liu, L. F. (1988) Involvement of DNA topoisomerase I in transcription of human ribosomal RNA genes. Proc. Natl. Acad. Sci. U. S. A. 85, 1060-1064
    • (1988) Proc. Natl. Acad. Sci. U. S. A , vol.85 , pp. 1060-1064
    • Zhang, H.1    Wang, J.C.2    Liu, L.F.3
  • 65
    • 1942501618 scopus 로고    scopus 로고
    • Role of the yeast Rrp1 protein in the dynamics of pre-ribosome maturation
    • Horsey, E. W., Jakovljevic, J., Miles, T. D., Hampichamchai, P., and Woolford, J. L., Jr. (2004) Role of the yeast Rrp1 protein in the dynamics of pre-ribosome maturation. RNA 10, 813-827
    • (2004) RNA , vol.10 , pp. 813-827
    • Horsey, E.W.1    Jakovljevic, J.2    Miles, T.D.3    Hampichamchai, P.4    Woolford Jr., J.L.5
  • 66
    • 0026470789 scopus 로고
    • A putative ATP-dependent RNA helicase involved in Saccharomyces cerevisiae ribosome assembly
    • Ripmaster, T. L., Vaughn, G. P., and Woofford, J. L., Jr. (1992) A putative ATP-dependent RNA helicase involved in Saccharomyces cerevisiae ribosome assembly. Proc. Natl. Acad. Sci. U. S. A. 89, 11131-11135
    • (1992) Proc. Natl. Acad. Sci. U. S. A , vol.89 , pp. 11131-11135
    • Ripmaster, T.L.1    Vaughn, G.P.2    Woofford Jr., J.L.3
  • 67
    • 0036512117 scopus 로고    scopus 로고
    • Messenger-RNA-binding proteins and the messages they carry
    • Dreyfuss, G., Kim, V. N., and Kataoka, N. (2002) Messenger-RNA-binding proteins and the messages they carry. Nat. Rev. Mol. Cell Biol. 3, 195-205
    • (2002) Nat. Rev. Mol. Cell Biol , vol.3 , pp. 195-205
    • Dreyfuss, G.1    Kim, V.N.2    Kataoka, N.3
  • 68
    • 0032478506 scopus 로고    scopus 로고
    • Human Tra2 proteins are sequence-specific activators of pre-mRNA splicing
    • Tacke, R., Tohyama, M., Ogawa, S., and Manley, J. L. (1998) Human Tra2 proteins are sequence-specific activators of pre-mRNA splicing. Cell 93, 139-148
    • (1998) Cell , vol.93 , pp. 139-148
    • Tacke, R.1    Tohyama, M.2    Ogawa, S.3    Manley, J.L.4
  • 69
    • 4344573414 scopus 로고    scopus 로고
    • The exosome, a molecular machine for controlled RNA degradation in both nucleus and cytoplasm
    • Raijmakers, R., Schilders, G., and Pruijn, G. J. (2004) The exosome, a molecular machine for controlled RNA degradation in both nucleus and cytoplasm. Eur. J. Cell Biol. 83, 175-183
    • (2004) Eur. J. Cell Biol , vol.83 , pp. 175-183
    • Raijmakers, R.1    Schilders, G.2    Pruijn, G.J.3
  • 70
    • 33845407784 scopus 로고    scopus 로고
    • Reconstitution, activities, and structure of the eukaryotic RNA exosome
    • Liu, Q., Greimann, J. C., and Lima, C. D. (2006) Reconstitution, activities, and structure of the eukaryotic RNA exosome. Cell 127, 1223-1237
    • (2006) Cell , vol.127 , pp. 1223-1237
    • Liu, Q.1    Greimann, J.C.2    Lima, C.D.3
  • 71
    • 33846068920 scopus 로고    scopus 로고
    • A single subunit, Dis3, is essentially responsible for yeast exosome core activity
    • Dziembowski, A., Lorentzen, E., Conti, E., and Seraphin, B. (2007) A single subunit, Dis3, is essentially responsible for yeast exosome core activity. Nat. Struct. Mol. Biol. 14, 15-22
    • (2007) Nat. Struct. Mol. Biol , vol.14 , pp. 15-22
    • Dziembowski, A.1    Lorentzen, E.2    Conti, E.3    Seraphin, B.4
  • 72
    • 29244475356 scopus 로고    scopus 로고
    • MPP6 is an exosome-associated RNA-binding protein involved in 5.8S rRNA maturation
    • Schilders, G., Raijmakers, R., Raats, J. M., and Pruijn, G. J. (2005) MPP6 is an exosome-associated RNA-binding protein involved in 5.8S rRNA maturation. Nucleic Acids Res. 33, 6795-6804
    • (2005) Nucleic Acids Res , vol.33 , pp. 6795-6804
    • Schilders, G.1    Raijmakers, R.2    Raats, J.M.3    Pruijn, G.J.4
  • 75
    • 0031697184 scopus 로고    scopus 로고
    • Spb4p, an essential putative RNA helicase, is required for a late step in the assembly of 60S ribosomal subunits in Saccharomyces cerevisiae
    • de la Cruz, J., Kressler, D., Rojo, M., Tollervey, D., and Linder, P. (1998) Spb4p, an essential putative RNA helicase, is required for a late step in the assembly of 60S ribosomal subunits in Saccharomyces cerevisiae. RNA 4, 1268-1281
    • (1998) RNA , vol.4 , pp. 1268-1281
    • de la Cruz, J.1    Kressler, D.2    Rojo, M.3    Tollervey, D.4    Linder, P.5
  • 76
    • 41549145540 scopus 로고    scopus 로고
    • Bezin, L. G. B, and Morales, A. C, October 28, 2004 Method of calibration of reverse transcription using a synthetic messenger RNA (SmRNA) as an internal control. World Intellectual Property Organisation Patent WO/2004/092414
    • Bezin, L. G. B., and Morales, A. C. (October 28, 2004) Method of calibration of reverse transcription using a synthetic messenger RNA (SmRNA) as an internal control. World Intellectual Property Organisation Patent WO/2004/092414


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.