메뉴 건너뛰기




Volumn , Issue , 2009, Pages 450-460

Multicomponent Machines in RNA Modification: H/ACA Ribonucleoproteins

Author keywords

[No Author keywords available]

Indexed keywords


EID: 80955171919     PISSN: None     EISSN: None     Source Type: Book    
DOI: None     Document Type: Chapter
Times cited : (4)

References (123)
  • 1
    • 0037428520 scopus 로고    scopus 로고
    • Rna-guided nucleotide modification of ribosomal and other rnas
    • Decatur WA, Fournier MJ. RNA-guided nucleotide modification of ribosomal and other RNAs. J Biol Chem 2003; 278:695-698.
    • (2003) J Biol Chem , vol.278 , pp. 695-698
    • Decatur, W.A.1    Fournier, M.J.2
  • 3
    • 33847187076 scopus 로고    scopus 로고
    • Noncoding rnas: Lessons from the small nuclear and small nucleolar rnas
    • Matera AG, Terns RM, Terns MP. Noncoding RNAs: lessons from the small nuclear and small nucleolar RNAs. Nat Rev Mol Cell Biol 2007; 8:209-220.
    • (2007) Nat Rev Mol Cell Biol , vol.8 , pp. 209-220
    • Matera, A.G.1    Terns, R.M.2    Terns, M.P.3
  • 4
    • 19444374397 scopus 로고    scopus 로고
    • The many facets of h/aca ribonucleoproteins
    • Meier UT. The many facets of H/ACA ribonucleoproteins. Chromosoma 2005; 114:1-14.
    • (2005) Chromosoma , vol.114 , pp. 1-14
    • Meier, U.T.1
  • 5
    • 0036591884 scopus 로고    scopus 로고
    • Biogenesis of small nucleolar ribonucleoproteins
    • Filipowicz W, Pogacic V. Biogenesis of small nucleolar ribonucleoproteins. Curr Opin Cell Biol 2002; 14:319-327.
    • (2002) Curr Opin Cell Biol , vol.14 , pp. 319-327
    • Filipowicz, W.1    Pogacic, V.2
  • 6
    • 2942610793 scopus 로고    scopus 로고
    • Rna structure and function in c/d and h/aca s(No)rnps
    • Henras AK, 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
  • 7
    • 0037133942 scopus 로고    scopus 로고
    • Small nucleolar rnas: An abundant group of noncoding rnas with diverse cellular functions
    • Kiss T. Small nucleolar RNAs: an abundant group of noncoding RNAs with diverse cellular functions. Cell 2002; 109:145-148.
    • (2002) Cell , vol.109 , pp. 145-148
    • Kiss, T.1
  • 8
    • 0031758488 scopus 로고    scopus 로고
    • Birth of the snornps: The evolution of the modification-guide snornas
    • Lafontaine DL, Tollervey D. Birth of the snoRNPs: the evolution of the modification-guide snoRNAs. Trends Biochem Sci 1998; 23:383-388.
    • (1998) Trends Biochem Sci , vol.23 , pp. 383-388
    • Lafontaine, D.L.1    Tollervey, D.2
  • 9
    • 0030656387 scopus 로고    scopus 로고
    • Sno storm in the nucleolus: New roles for myriad small rnps
    • Smith CM, Steitz JA. Sno storm in the nucleolus: new roles for myriad small RNPs. Cell 1997; 89:669-672.
    • (1997) Cell , vol.89 , pp. 669-672
    • Smith, C.M.1    Steitz, J.A.2
  • 10
    • 0031003901 scopus 로고    scopus 로고
    • The family of box ac a small nucleolar rnas is defined by an evolutionarily conserved secondary structure and ubiquitous sequence elements essential for rna accumulation
    • Ganot P, Caizergues-Ferrer M, Kiss T. The family of box AC A small nucleolar RNAs is defined by an evolutionarily conserved secondary structure and ubiquitous sequence elements essential for RNA accumulation. Genes Dev 1997; 11:941-956.
    • (1997) Genes Dev , vol.11 , pp. 941-956
    • Ganot, P.1    Caizergues-Ferrer, M.2    Kiss, T.3
  • 11
    • 0030572699 scopus 로고    scopus 로고
    • The rna world of the nucleolus: Two major families of small rnas defined by different box elements with related functions
    • Balakin AG, Smith L, Fournier MJ. The RNA world of the nucleolus: two major families of small RNAs defined by different box elements with related functions. Cell 1996; 86:823-834.
    • (1996) Cell , vol.86 , pp. 823-834
    • Balakin, A.G.1    Smith, L.2    Fournier, M.J.3
  • 12
    • 0030711050 scopus 로고    scopus 로고
    • Site-specific pseudouridinc formation in preribosomal rna is guided by small nucleolar rnas
    • Ganot P, Bortolin ML, Kiss T. Site-specific pseudouridinc formation in preribosomal RNA is guided by small nucleolar RNAs. Cell 1997; 89:799-809.
    • (1997) Cell , vol.89 , pp. 799-809
    • Ganot, P.1    Bortolin, M.L.2    Kiss, T.3
  • 13
    • 0030771087 scopus 로고    scopus 로고
    • Small nucleolar rnas direct site-specific synthesis of pseudouridine in ribosomal rna
    • Ni J, Tien AL, Fournier MJ. Small nucleolar RNAs direct site-specific synthesis of pseudouridine in ribosomal RNA. Cell 1997; 89:565-573.
    • (1997) Cell , vol.89 , pp. 565-573
    • Ni, J.1    Tien, A.L.2    Fournier, M.J.3
  • 14
    • 0035355205 scopus 로고    scopus 로고
    • Rnomics: An experimental approach that identifies 201 candidates for novel, small, nonmessenger rnas in mouse
    • Huttenhofer A, Kiefmann M, Meier-Ewert S et al. RNomics: an experimental approach that identifies 201 candidates for novel, small, nonmessenger RNAs in mouse. EMBO J 2001; 20:2943-2953.
    • (2001) EMBO J , vol.20 , pp. 2943-2953
    • Huttenhofer, A.1    Kiefmann, M.2    Meier-Ewert, S.3
  • 15
    • 0035253857 scopus 로고    scopus 로고
    • A small nucleolar guide rna functions both in 2'-0-ribose methylation and pseudou-ridylation of the u5 spliceosomal rna
    • Jady BE, Kiss T. A small nucleolar guide RNA functions both in 2'-0-ribose methylation and pseudou-ridylation of the U5 spliceosomal RNA. EMBO J 2001; 20:541-551.
    • (2001) EMBO J , vol.20 , pp. 541-551
    • Jady, B.E.1    Kiss, T.2
  • 16
    • 0037013831 scopus 로고    scopus 로고
    • Cajal body-specific small nuclear rnas: A novel class of 2′-0-methylation and pseudouridylation guide rnas
    • Darzacq X, Jady BE, Verheggen C et al. Cajal body-specific small nuclear RNAs: a novel class of 2′-0-methylation and pseudouridylation guide RNAs. EMBO J 2002; 21:2746-2756.
    • (2002) EMBO J , vol.21 , pp. 2746-2756
    • Darzacq, X.1    Jady, B.E.2    Verheggen, C.3
  • 17
    • 28444456713 scopus 로고    scopus 로고
    • Cajal bodies: A long history of discovery
    • Cioce M, Lamond Al. Cajal bodies: a long history of discovery. Annu Rev Cell Dev Biol 2005; 21:105-131.
    • (2005) Annu Rev Cell Dev Biol , vol.21 , pp. 105-131
    • Cioce, M.1    Al, L.2
  • 18
    • 30444437477 scopus 로고    scopus 로고
    • Subnuclear organelles: New insights intoform and function
    • Handwergcr KE, Gall JG. Subnuclear organelles: new insights intoform and function. Trends Cell Biol 2006; 16:19-26.
    • (2006) Trends Cell Biol , vol.16 , pp. 19-26
    • Handwergcr, K.E.1    Gall, J.G.2
  • 19
    • 0042967786 scopus 로고    scopus 로고
    • A common sequence motif determines the cajal body-specific localization of box h/aca scarnas
    • Richard P, Darzacq X, Bertrand E et al. A common sequence motif determines the Cajal body-specific localization of box H/ACA scaRNAs. EMBO J 2003; 22:4283-4293.
    • (2003) EMBO J , vol.22 , pp. 4283-4293
    • Richard, P.1    Darzacq, X.2    Bertrand, E.3
  • 20
    • 12344275917 scopus 로고    scopus 로고
    • Biogenesis of small nuclear rnps
    • Kiss T. Biogenesis of small nuclear RNPs. J Cell Sci 2004; 117:5949-5951.
    • (2004) J Cell Sci , vol.117 , pp. 5949-5951
    • Kiss, T.1
  • 21
    • 43249108205 scopus 로고    scopus 로고
    • Different mechanisms for pseudouridine formation in yeast 5s and 5.8s rrnas
    • Decatur WA, Schnare MN. Different mechanisms for pseudouridine formation in yeast 5S and 5.8S rRNAs. Mol Cell Biol 2008; 28:3089-3100.
    • (2008) Mol Cell Biol , vol.28 , pp. 3089-3100
    • Decatur, W.A.1    Schnare, M.N.2
  • 22
    • 0028117705 scopus 로고
    • Nap57, a mammalian nucleolar protein with a putative homolog in yeast and bacteria
    • Meier UT, Blobel G. NAP57, a mammalian nucleolar protein with a putative homolog in yeast and bacteria. J Cell Biol 1994; 127:1505-1514.
    • (1994) J Cell Biol , vol.127 , pp. 1505-1514
    • Meier, U.T.1    Blobel, G.2
  • 23
    • 0027182790 scopus 로고
    • An essential yeast protein, cbf5p, binds in vitro to centromeres and microtubules
    • Jiang W, Middleton K, Yoon H-J et al. An essential yeast protein, CBF5p, binds in vitro to centromeres and microtubules. Mol Cell Biol 1993; 13:4884-4893.
    • (1993) Mol Cell Biol , vol.13 , pp. 4884-4893
    • Jiang, W.1    Middleton, K.2    Yoon, H.-J.3
  • 24
    • 0029258983 scopus 로고
    • Purification, cloning and properties of the trna w55 synthase from escherichia coli
    • Nurse K, Wrzesinski J, Bakin A et al. Purification, cloning and properties of the tRNA W55 synthase from Escherichia coli. RNA 1995; 1:102-112.
    • (1995) RNA , vol.1 , pp. 102-112
    • Nurse, K.1    Wrzesinski, J.2    Bakin, A.3
  • 25
    • 0033435203 scopus 로고    scopus 로고
    • The mechanism of pseudouridinc synthase i as deduced from its interaction with 5-fluorouracil-trna
    • Gu X, Liu Y, Santi DV. The mechanism of pseudouridinc synthase I as deduced from its interaction with 5-fluorouracil-tRNA. Proc Natl Acad Sci USA 1999; 96:14270-14275.
    • (1999) Proc Natl Acad Sci USA , vol.96 , pp. 14270-14275
    • Gu, X.1    Liu, Y.2    Santi, D.V.3
  • 26
    • 0035966271 scopus 로고    scopus 로고
    • Cocrystal structure of a trna psi55 pseudouridinc synthase: Nucleotide flipping by an rna-modifying enzyme
    • Hoang C, Ferre-DAmare AR. Cocrystal structure of a tRNA Psi55 pseudouridinc synthase: nucleotide flipping by an RNA-modifying enzyme. Cell 2001; 107:929-939
    • (2001) Cell , vol.107 , pp. 929-939
    • Hoang, C.1    Ferre-DAmare, A.R.2
  • 27
    • 0032488657 scopus 로고    scopus 로고
    • A conserved aspartate of trna pscudouridine synthase is essential for activity and a probable nucleophilic catalyst
    • Huang L, Pookanjanatavip M, Gu X et al. A conserved aspartate of tRNA pscudouridine synthase is essential for activity and a probable nucleophilic catalyst. Biochemistry 1998; 37:344-351.
    • (1998) Biochemistry , vol.37 , pp. 344-351
    • Huang, L.1    Pookanjanatavip, M.2    Gu, X.3
  • 28
    • 5644289361 scopus 로고    scopus 로고
    • The pseudouridinc synthases: Revisiting a mechanism that seemed settled
    • Spcdalierc CJ, Ginter JM, Johnston MV et al. The pseudouridinc synthases: revisiting a mechanism that seemed settled. J Am Chem Soc 2004; 126:12758-12759.
    • (2004) J am Chem Soc , vol.126 , pp. 12758-12759
    • Spcdalierc, C.J.1    Ginter, J.M.2    Johnston, M.V.3
  • 29
    • 0029832294 scopus 로고    scopus 로고
    • Identification of new rna modifying enzymes by iterative genome search using known modifying enzymes as probes
    • Gustafsson C, Reid R, Greene PJ et al. Identification of new RNA modifying enzymes by iterative genome search using known modifying enzymes as probes. Nucleic Acids Res 1996; 24:3756-3762.
    • (1996) Nucleic Acids Res , vol.24 , pp. 3756-3762
    • Gustafsson, C.1    Reid, R.2    Greene, P.J.3
  • 30
    • 0033046425 scopus 로고    scopus 로고
    • Novel predicted rna-binding domains associated with the translation machinery
    • Aravind L, Koonin EV. Novel predicted RNA-binding domains associated with the translation machinery. J Mol Evol 1999; 48:291-302.
    • (1999) J Mol Evol , vol.48 , pp. 291-302
    • Aravind, L.1    Koonin, E.V.2
  • 31
    • 0029945504 scopus 로고    scopus 로고
    • Pseudouridine synthases: Four families of enzymes containing a putative uridine-binding motif also conserved in dutpases and dctp deaminases
    • Koonin EV. Pseudouridine synthases: four families of enzymes containing a putative uridine-binding motif also conserved in dUTPases and dCTP deaminases. Nucleic Acids Res 1996; 24:2411-2415.
    • (1996) Nucleic Acids Res , vol.24 , pp. 2411-2415
    • Koonin, E.V.1
  • 32
    • 34748912322 scopus 로고    scopus 로고
    • The pua domain—a structural and functional overview
    • Perez-Arcllano I, Gallcgo J, Cervera J. The PUA domain—a structural and functional overview. FEBS J 2007; 274:4972-4984.
    • (2007) FEBS J , vol.274 , pp. 4972-4984
    • Perez-Arcllano, I.1    Gallcgo, J.2    Cervera, J.3
  • 33
    • 0032754538 scopus 로고    scopus 로고
    • Dyskerin localizes to the nucleolus and its mislocalization is unlikely to play a role in the pathogenesis of dyskeratosis congenita
    • Heiss NS, Girod A, Salowsky R et al. Dyskerin localizes to the nucleolus and its mislocalization is unlikely to play a role in the pathogenesis of dyskeratosis congenita. Hum Mol Genet 1999; 8:2515-2524.
    • (1999) Hum Mol Genet , vol.8 , pp. 2515-2524
    • Heiss, N.S.1    Girod, A.2    Salowsky, R.3
  • 34
    • 0033368572 scopus 로고    scopus 로고
    • Analysis of epitope-tagged forms of the dyskeratosis congenital protein (Dyskerin): Identification of a nuclear localization signal
    • Youssoufian H, Gharibyan V, Qatanani M. Analysis of epitope-tagged forms of the dyskeratosis congenital protein (dyskerin): identification of a nuclear localization signal. Blood Cells Mol Ois 1999; 25:305-309.
    • (1999) Blood Cells Mol Ois , vol.25 , pp. 305-309
    • Youssoufian, H.1    Gharibyan, V.2    Qatanani, M.3
  • 35
    • 0032401740 scopus 로고    scopus 로고
    • Nhp2p and nopl0p are essential for the function of h/aca snornps
    • Henras A, Henry Y, Bousquet-Antonelli C et al. Nhp2p and Nopl0p are essential for the function of H/ACA snoRNPs. EMBO J 1998; 17:7078-7090.
    • (1998) EMBO J , vol.17 , pp. 7078-7090
    • Henras, A.1    Henry, Y.2    Bousquet-Antonelli, C.3
  • 36
    • 44949173192 scopus 로고    scopus 로고
    • Noplo is a conserved h/aca snornp molecular adaptor
    • Reichow SL, Varani G. NoplO is a conserved H/ACA snoRNP molecular adaptor. Biochemistry 2008; 47:6148-6156.
    • (2008) Biochemistry , vol.47 , pp. 6148-6156
    • Reichow, S.L.1    Varani, G.2
  • 37
    • 2442542173 scopus 로고    scopus 로고
    • Architecture and assembly of mammalian h/aca small nucleolar and tclomerase ribonucleoproteins
    • Wang C, Meier UT. Architecture and assembly of mammalian H/ACA small nucleolar and tclomerase ribonucleoproteins. EMBO J 2004; 23:1857-1867.
    • (2004) EMBO J , vol.23 , pp. 1857-1867
    • Wang, C.1    Meier, U.T.2
  • 38
    • 0023741397 scopus 로고
    • Amino-terminal sequence of a saccharomyces cerevisiae nuclear protein, nhp6, shows significant identity to bovine hmg1
    • Kolodrubetz D, Haggren W, Burgum A. Amino-terminal sequence of a Saccharomyces cerevisiae nuclear protein, NHP6, shows significant identity to bovine HMG1. FEBS Lett 1988; 238:175-179.
    • (1988) FEBS Lett , vol.238 , pp. 175-179
    • Kolodrubetz, D.1    Haggren, W.2    Burgum, A.3
  • 39
    • 0037071545 scopus 로고    scopus 로고
    • In vivo analysis of nhpx reveals a novel nucleolar localization pathway involving a transient accumulation in splicing speckles
    • Leung AK, Lamond AI. In vivo analysis of NHPX reveals a novel nucleolar localization pathway involving a transient accumulation in splicing speckles. J Cell Biol 2002; 157:615-629.
    • (2002) J Cell Biol , vol.157 , pp. 615-629
    • Leung, A.K.1    Lamond, A.I.2
  • 40
    • 0031788801 scopus 로고    scopus 로고
    • Cbf5p, a potential pscudouridine synthase and nhp2p, a putative rna- binding protein, arc present together with garlp in all box h/aca-motif snornps and constitute a common bipartite structure
    • Watkins NJ, Gottschalk A, Neubauer G et al. Cbf5p, a potential pscudouridine synthase and Nhp2p, a putative RNA- binding protein, arc present together with Garlp in all box H/ACA-motif snoRNPs and constitute a common bipartite structure. RNA 1998; 4:1549-1568.
    • (1998) RNA , vol.4 , pp. 1549-1568
    • Watkins, N.J.1    Gottschalk, A.2    Neubauer, G.3
  • 41
    • 0034721649 scopus 로고    scopus 로고
    • A common core rnp structure shared between the small nucleolar box c/d rnps and the sphccosomal u4 snrnp
    • Watkins NJ, Segault V, Charpentier B et al. A common core RNP structure shared between the small nucleolar box C/D RNPs and the sphccosomal U4 snRNP. Cell 2000; 103:457-466.
    • (2000) Cell , vol.103 , pp. 457-466
    • Watkins, N.J.1    Segault, V.2    Charpentier, B.3
  • 42
    • 0033229873 scopus 로고    scopus 로고
    • Functional interaction of a novel 15.5 kd [u4/u6.U5] tri-snrnp protein with the 5' stem-loop of u4 snrna
    • Nottrott S, Hartmuth K, Fabrizio P et al. Functional interaction of a novel 15.5 kD [U4/U6.U5] tri-snRNP protein with the 5' stem-loop of U4 snRNA. EMBO J 1999; 18:6119-6133.
    • (1999) EMBO J , vol.18 , pp. 6119-6133
    • Nottrott, S.1    Hartmuth, K.2    Fabrizio, P.3
  • 43
    • 0037324527 scopus 로고    scopus 로고
    • Binding of l7ae protein to the k-tum of archaeal snornas: A shared rna binding motif for c/d and h/aca box snornas in archaca
    • Rozhdestvensky TS, Tang TH, Tchirkova IV et al. Binding of L7Ae protein to the K-tum of archaeal snoRNAs: a shared RNA binding motif for C/D and H/ACA box snoRNAs in Archaca. Nucleic Acids Res 2003; 31:869-877.
    • (2003) Nucleic Acids Res , vol.31 , pp. 869-877
    • Rozhdestvensky, T.S.1    Tang, T.H.2    Tchirkova, I.V.3
  • 44
    • 0035394728 scopus 로고    scopus 로고
    • Accumulation of h/aca snornps depends on the integrity of the conserved central domain of the rna-binding protein nhp2p
    • Henras A, Dez C, Noaillac-Depeyrc J et al. Accumulation of H/ACA snoRNPs depends on the integrity of the conserved central domain of the RNA-binding protein Nhp2p. Nucleic Acids Res 2001; 29:2733-2746.
    • (2001) Nucleic Acids Res , vol.29 , pp. 2733-2746
    • Henras, A.1    Dez, C.2    Noaillac-Depeyrc, J.3
  • 45
    • 0034509631 scopus 로고    scopus 로고
    • Crystal structure of the spliceosomal 15.5 kd protein bound to a u4 snrna fragment
    • Vidovic I, Nottrott S, Hartmuth K et al. Crystal structure of the spliceosomal 15.5 kD protein bound to a U4 snRNA fragment. Mol Cell 2000; 6:1331-1342.
    • (2000) Mol Cell , vol.6 , pp. 1331-1342
    • Vidovic, I.1    Nottrott, S.2    Hartmuth, K.3
  • 46
    • 0026583945 scopus 로고
    • Gar1 is an essential small nucleolar rnp protein required for prerrna processing in yeast
    • Girard JP, Lehtonen H, Caizergues-Fcrrcr M et al. GAR1 is an essential small nucleolar RNP protein required for prerRNA processing in yeast. EMBO J 1992; 11:673-682.
    • (1992) EMBO J , vol.11 , pp. 673-682
    • Girard, J.P.1    Lehtonen, H.2    Caizergues-Fcrrcr, M.3
  • 47
    • 30744445688 scopus 로고    scopus 로고
    • Crystal structure of a cbb-noplo-garl complex and implications in rna-guided pscudouridylation and dyskeratosis congenita
    • Rashid R, Liang B, Baker DL et al. Crystal structure of a CbB-NoplO-Garl complex and implications in RNA-guided pscudouridylation and dyskeratosis congenita. Mol Cell 2006; 21:249-260.
    • (2006) Mol Cell , vol.21 , pp. 249-260
    • Rashid, R.1    Liang, B.2    Baker, D.L.3
  • 48
    • 33748947672 scopus 로고    scopus 로고
    • Crystal structure of an h/aca box ribonucleoprotein particle
    • Li L, Ye K. Crystal structure of an H/ACA box ribonucleoprotein particle. Nature 2006; 443:302-307.
    • (2006) Nature , vol.443 , pp. 302-307
    • Li, L.1    Ye, K.2
  • 49
    • 18844397555 scopus 로고    scopus 로고
    • Rna-guided rna modification: Functional organization of the archaeal h/aca rnp
    • Baker DL, Youssef OA, Chastkofsky MI et al. RNA-guided RNA modification: functional organization of the archaeal H/ACA RNP. Genes Dev 2005; 19:1238-1248.
    • (2005) Genes Dev , vol.19 , pp. 1238-1248
    • Baker, D.L.1    Youssef, O.A.2    Chastkofsky, M.I.3
  • 50
    • 20144374350 scopus 로고    scopus 로고
    • Reconstitution of archaeal h/aca small ribonucleoprotein complexes active in pscudouridylation
    • Charpentier B, Muller S, Branlant C. Reconstitution of archaeal H/ACA small ribonucleoprotein complexes active in pscudouridylation. Nucleic Acids Res 2005; 33:3133-3144.
    • (2005) Nucleic Acids Res , vol.33 , pp. 3133-3144
    • Charpentier, B.1    Muller, S.2    Branlant, C.3
  • 51
    • 0029055768 scopus 로고
    • Isolation and characterization of the small nucleolar ribonudeo-protcin particle snr30 from saccharomyces cerevisiae
    • Liibben B, Fabrizio P, Kastner B et al. Isolation and characterization of the small nucleolar ribonudeo-protcin particle snR30 from Saccharomyces cerevisiae. J Biol Chem 1995; 270:11549-11554.
    • (1995) J Biol Chem , vol.270 , pp. 11549-11554
    • Liibben, B.1    Fabrizio, P.2    Kastner, B.3
  • 52
    • 0037148271 scopus 로고    scopus 로고
    • Tclomerase in the human organism
    • Collins K, Mitchell JR. Tclomerase in the human organism. Oncogene 2002; 21:564-579.
    • (2002) Oncogene , vol.21 , pp. 564-579
    • Collins, K.1    Mitchell, J.R.2
  • 53
    • 33646552752 scopus 로고    scopus 로고
    • The vertebrate e1/u17 small nucleolar ribonucleoprotein particle
    • Elicciri GL. The vertebrate E1/U17 small nucleolar ribonucleoprotein particle. J Cell Biochem 2006; 98:486-495.
    • (2006) J Cell Biochem , vol.98 , pp. 486-495
    • Elicciri, G.L.1
  • 54
    • 0027447757 scopus 로고
    • Yeast snr30 is a small nucleolar rna required for 18s rrna synthesis
    • Morrissey JP, Tollcrvey D. Yeast snR30 is a small nucleolar RNA required for 18S rRNA synthesis. Mol Cell Biol 1993; 13:2469-2477.
    • (1993) Mol Cell Biol , vol.13 , pp. 2469-2477
    • Morrissey, J.P.1    Tollcrvey, D.2
  • 55
    • 0842347403 scopus 로고    scopus 로고
    • U17/snr30 is a ubiquitous snorna with two conserved sequence motifs essential for 18s rrna production
    • Atzom V, Fragapane P, Kiss T. U17/snR30 is a ubiquitous snoRNA with two conserved sequence motifs essential for 18S rRNA production. Mol Cell Biol 2004; 24:1769-1778.
    • (2004) Mol Cell Biol , vol.24 , pp. 1769-1778
    • Atzom, V.1    Fragapane, P.2    Kiss, T.3
  • 56
    • 0041670894 scopus 로고    scopus 로고
    • Structural and sequence evolution of u17 small nucleolar rna (Snorna) and its phylogenetic congruence in chclonians
    • Cervelli M, Oliverio M, Bellini A et al. Structural and sequence evolution of U17 small nucleolar RNA (snoRNA) and its phylogenetic congruence in chclonians. J Mol Evol 2003; 57:73-84.
    • (2003) J Mol Evol , vol.57 , pp. 73-84
    • Cervelli, M.1    Oliverio, M.2    Bellini, A.3
  • 57
    • 33749588453 scopus 로고    scopus 로고
    • The helicasc haslp is required for snorna release from prerrna
    • Liang XH, Fournier MJ. The helicasc Haslp is required for snoRNA release from prerRNA. Mol Cell Biol 2006; 26:7437-7450.
    • (2006) Mol Cell Biol , vol.26 , pp. 7437-7450
    • Liang, X.H.1    Fournier, M.J.2
  • 58
    • 14744270698 scopus 로고    scopus 로고
    • Uv-crosslinking of el small nucleolar rna to proteins in frog oocytes
    • Smith JL, Walton AH, Eliceiri GL. UV-crosslinking of El small nucleolar RNA to proteins in frog oocytes. J Cell Physiol 2005; 203:202-208.
    • (2005) J Cell Physiol , vol.203 , pp. 202-208
    • Smith, J.L.1    Walton, A.H.2    Eliceiri, G.L.3
  • 59
    • 0032961170 scopus 로고    scopus 로고
    • A box h/aca small nucleolar rna-like domain at the human telomerasc rna 3' end
    • Mitchell JR, Cheng J, Collins K. A box H/ACA small nucleolar RNA-like domain at the human telomerasc RNA 3' end. Mol Cell Biol 1999; 19:567-576.
    • (1999) Mol Cell Biol , vol.19 , pp. 567-576
    • Mitchell, J.R.1    Cheng, J.2    Collins, K.3
  • 60
    • 0035253526 scopus 로고    scopus 로고
    • Stable expression in yeast of the mature form of human telomcrase rna depends on its association with the box h/aca small nucleolar rnp proteins cbf5p, nhp2p and nop10p
    • Dez C, Henras A, Faucon B et al. Stable expression in yeast of the mature form of human telomcrase RNA depends on its association with the box H/ACA small nucleolar RNP proteins Cbf5p, Nhp2p and Nop10p. Nucleic Acids Res 2001; 29:598-603.
    • (2001) Nucleic Acids Res , vol.29 , pp. 598-603
    • Dez, C.1    Henras, A.2    Faucon, B.3
  • 61
    • 34748845108 scopus 로고    scopus 로고
    • Structural and functional characterization of human telomerasc rna processing and cajal body localization signals
    • Theimer CA, Jady BE, Chim N et al. Structural and functional characterization of human telomerasc RNA processing and cajal body localization signals. Mol Cell 2007; 27:869-881.
    • (2007) Mol Cell , vol.27 , pp. 869-881
    • Theimer, C.A.1    Jady, B.E.2    Chim, N.3
  • 62
    • 55549090746 scopus 로고    scopus 로고
    • Telomerasc reverse transcriptase is required for the localization of telomerase rna to cajal bodies and telomeres in human cancer cells
    • Tomlinson RL, Abreu EB, Ziegler T et al. Telomerasc reverse transcriptase is required for the localization of telomerase RNA to Cajal bodies and telomeres in human cancer cells. Mol Biol Cell 2008; 19:3793-3800.
    • (2008) Mol Biol Cell , vol.19 , pp. 3793-3800
    • Tomlinson, R.L.1    Abreu, E.B.2    Ziegler, T.3
  • 63
    • 17944388104 scopus 로고    scopus 로고
    • Human telomerase rna and box h/aca scarnas share a common cajal body-specific localization signal
    • Jady BE, Bertrand E, Kiss T. Human telomerase RNA and box H/ACA scaRNAs share a common Cajal body-specific localization signal. J Cell Biol 2004; 164:647-652.
    • (2004) J Cell Biol , vol.164 , pp. 647-652
    • Jady, B.E.1    Bertrand, E.2    Kiss, T.3
  • 64
    • 0346099349 scopus 로고    scopus 로고
    • Telomerase rna accumulates in cajal bodies in human cancer cells
    • Zhu Y, Tomlinson RL, Lukowiak AA et al. Telomerase RNA accumulates in Cajal bodies in human cancer cells. Mol Biol Cell 2004; 15:81-90.
    • (2004) Mol Biol Cell , vol.15 , pp. 81-90
    • Zhu, Y.1    Tomlinson, R.L.2    Lukowiak, A.A.3
  • 65
    • 34748876539 scopus 로고    scopus 로고
    • Human telomerasc rna accumulation in cajal bodies facilitates telomerase recruitment to telomeres and telomere elongation
    • Cristofari G, Adolf E, Reichenbach P et al. Human telomerasc RNA accumulation in Cajal bodies facilitates telomerase recruitment to telomeres and telomere elongation. Mol Cell 2007; 27:882-889.
    • (2007) Mol Cell , vol.27 , pp. 882-889
    • Cristofari, G.1    Adolf, E.2    Reichenbach, P.3
  • 66
    • 77949607182 scopus 로고    scopus 로고
    • Fisher: A program for the detection of h/aca snornas using mfe secondary structure prediction and comparative genomics—assessment and update
    • Frcyhult E, Edvardsson S, Tamas I et al. Fisher: a program for the detection of H/ACA snoRNAs using MFE secondary structure prediction and comparative genomics—assessment and update. BMC Res Notes 2008; 1:49.
    • (2008) BMC Res Notes , vol.1 , pp. 49
    • Frcyhult, E.1    Edvardsson, S.2    Tamas, I.3
  • 67
    • 2942718696 scopus 로고    scopus 로고
    • Human box h/aca pseudouridylation guide rna machinery
    • Kiss AM, Jady BE, Bertrand E et al. Human box H/ACA pseudouridylation guide RNA machinery. Mol Cell Biol 2004; 24:5797-5807.
    • (2004) Mol Cell Biol , vol.24 , pp. 5797-5807
    • Kiss, A.M.1    Jady, B.E.2    Bertrand, E.3
  • 68
    • 33846932045 scopus 로고    scopus 로고
    • Genome-wide analyses of retrogenes derived from the human box h/aca snornas
    • Luo Y, Li S. Genome-wide analyses of retrogenes derived from the human box H/ACA snoRNAs. Nucleic Acids Res 2007; 35:559-571.
    • (2007) Nucleic Acids Res , vol.35 , pp. 559-571
    • Luo, Y.1    Li, S.2
  • 69
    • 29844435528 scopus 로고    scopus 로고
    • A computational screen for mammalian pseudouridylation guide h/aca rnas
    • Schattner P, Barberan-Soler S, Lowe TM. A computational screen for mammalian pseudouridylation guide H/ACA RNAs. RNA 2006; 12:15-25.
    • (2006) RNA , vol.12 , pp. 15-25
    • Schattner, P.1    Barberan-Soler, S.2    Lowe, T.M.3
  • 70
    • 33751009398 scopus 로고    scopus 로고
    • Snoseeker: An advanced computational package for screening of guide and orphan snorna genes in the human genome
    • Yang JH, Zhang XC, Huang ZP et al. SnoSeeker: an advanced computational package for screening of guide and orphan snoRNA genes in the human genome. Nucleic Acids Res 2006; 34:5112-5123.
    • (2006) Nucleic Acids Res , vol.34 , pp. 5112-5123
    • Yang, J.H.1    Zhang, X.C.2    Huang, Z.P.3
  • 71
    • 0034687740 scopus 로고    scopus 로고
    • Identification of brain-specific and imprinted small nucleolar rna genes exhibiting an unusual genomic organization
    • Cavaille J, Buiting K, Kiefmann M et al. Identification of brain-specific and imprinted small nucleolar RNA genes exhibiting an unusual genomic organization. Proc Nad Acad Sci USA 2000; 97:14311-14316.
    • (2000) Proc Nad Acad Sci USA , vol.97 , pp. 14311-14316
    • Cavaille, J.1    Buiting, K.2    Kiefmann, M.3
  • 72
    • 0344668837 scopus 로고    scopus 로고
    • Identification of 13 novel human modification guide rnas
    • Vitali P, Royo H, Seitz H et al. Identification of 13 novel human modification guide RNAs. Nucleic Acids Res 2003; 31:6543-6551.
    • (2003) Nucleic Acids Res , vol.31 , pp. 6543-6551
    • Vitali, P.1    Royo, H.2    Seitz, H.3
  • 73
    • 0343183144 scopus 로고    scopus 로고
    • In vitro assembly of human h/aca small nucleolar rnps reveals unique features of u17 and telomerase rnas
    • Dragon F, Pogacic V, Filipowicz W. In vitro assembly of human H/ACA small nucleolar RNPs reveals unique features of U17 and telomerase RNAs. Mol Cell Biol 2000; 20:3037-3048.
    • (2000) Mol Cell Biol , vol.20 , pp. 3037-3048
    • Dragon, F.1    Pogacic, V.2    Filipowicz, W.3
  • 74
    • 7044285916 scopus 로고    scopus 로고
    • Cbf5p, the putative pscudouridine synthase of h/aca-typc snornps, can form a complex with garlp and noplop in absence of nhp2p and box h/aca snornas
    • Henras AK, Capeyrou R, Henry Y et al. Cbf5p, the putative pscudouridine synthase of H/ACA-typc snoRNPs, can form a complex with Garlp and NoplOp in absence of Nhp2p and box H/ACA snoRNAs. RNA 2004; 10:1704-1712.
    • (2004) RNA , vol.10 , pp. 1704-1712
    • Henras, A.K.1    Capeyrou, R.2    Henry, Y.3
  • 75
    • 36849034965 scopus 로고    scopus 로고
    • Substrate rna positioning in the archacal h/aca ribonuclcoprotein complex
    • Liang B, Xue S, Terns RM et al. Substrate RNA positioning in the archacal H/ACA ribonuclcoprotein complex. Nat Struct Mol Biol 2007; 14:1189-1195.
    • (2007) Nat Struct Mol Biol , vol.14 , pp. 1189-1195
    • Liang, B.1    Xue, S.2    Terns, R.M.3
  • 76
    • 28544449371 scopus 로고    scopus 로고
    • The cbb-noplo complex is a molecular bracket that organizes box h/aca rnps
    • Hamma T, Reichow SL, Varani G et al. The CbB-NoplO complex is a molecular bracket that organizes box H/ACA RNPs. Nat Struct Mol Biol 2005; 12:1101-1107.
    • (2005) Nat Struct Mol Biol , vol.12 , pp. 1101-1107
    • Hamma, T.1    Reichow, S.L.2    Varani, G.3
  • 77
    • 33644867181 scopus 로고    scopus 로고
    • Crystal structure determination and site-directed mutagenesis of the pyrococcus abyssi acbf5-anop10 complex reveal crucial roles of the c-terminal domains of both proteins in h/aca srnp activity
    • Manival X, Charron C, Fourmann JB et al. Crystal structure determination and site-directed mutagenesis of the Pyrococcus abyssi aCBF5-aNOP10 complex reveal crucial roles of the C-terminal domains of both proteins in H/ACA sRNP activity. Nucleic Acids Res 2006; 34:826-839.
    • (2006) Nucleic Acids Res , vol.34 , pp. 826-839
    • Manival, X.1    Charron, C.2    Fourmann, J.B.3
  • 78
    • 0035945611 scopus 로고    scopus 로고
    • Arrangement of rna and proteins in the spliceosomal u1 small nuclear ribonucleoprotein particle
    • Stark H, Dube P, Luhrmann R et al. Arrangement of RNA and proteins in the spliceosomal U1 small nuclear ribonucleoprotein particle. Nature 2001; 409:539-542.
    • (2001) Nature , vol.409 , pp. 539-542
    • Stark, H.1    Dube, P.2    Luhrmann, R.3
  • 79
    • 39149123489 scopus 로고    scopus 로고
    • Unveiling substrate rna binding to h/aca rnps: One side fits all
    • Li H. Unveiling substrate RNA binding to H/ACA RNPs: one side fits all. Curr Opin Struct Biol 2008; 18:78-85.
    • (2008) Curr Opin Struct Biol , vol.18 , pp. 78-85
    • Li, H.1
  • 80
    • 33745148277 scopus 로고    scopus 로고
    • How a single protein complex accommodates many different h/aca rnas
    • Meier UT. How a single protein complex accommodates many different H/ACA RNAs. Trends Biochem Sci 2006; 31:311-315.
    • (2006) Trends Biochem Sci , vol.31 , pp. 311-315
    • Meier, U.T.1
  • 81
    • 34249859415 scopus 로고    scopus 로고
    • H/aca small nucleolar rna pseudouridylation pockets bind substrate rna toform three-way junctions that position the target u for modification
    • Wu H, Feigon J. H/ACA small nucleolar RNA pseudouridylation pockets bind substrate RNA toform three-way junctions that position the target U for modification. Proc Nad Acad Sci USA 2007; 104:6655-6660.
    • (2007) Proc Nad Acad Sci USA , vol.104 , pp. 6655-6660
    • Wu, H.1    Feigon, J.2
  • 82
    • 34247278771 scopus 로고    scopus 로고
    • Solution structure of an rrna substrate bound to the pseudouridylation pocket of a box h/aca snorna
    • Jin H, Loria JP, Moore PB. Solution structure of an rRNA substrate bound to the pseudouridylation pocket of a box H/ACA snoRNA. Mol Cell 2007; 26:205-215
    • (2007) Mol Cell , vol.26 , pp. 205-215
    • Jin, H.1    Loria, J.P.2    Moore, P.B.3
  • 83
    • 0032520182 scopus 로고    scopus 로고
    • The box h+aca snornas carry cbf5p, the putative rrna pseudouridine synthase
    • Lafontaine DLJ, Bousquet-Antonelli C, Henry Y et al. The box H+ACA snoRNAs carry Cbf5p, the putative rRNA pseudouridine synthase. Genes Dev 1998; 12:527-537.
    • (1998) Genes Dev , vol.12 , pp. 527-537
    • Lafontaine, D.1    Bousquet-Antonelli, C.2    Henry, Y.3
  • 84
    • 0030837031 scopus 로고    scopus 로고
    • A small nucleolar rnp protein is required for pseudouridylation of eukaryotic ribosomal rnas
    • Bousquet-Antonelli C, Henry Y, G6lugne J-P et al. A small nucleolar RNP protein is required for pseudouridylation of eukaryotic ribosomal RNAs. EMBO J 1997; 16:4770-4776.
    • (1997) EMBO J , vol.16 , pp. 4770-4776
    • Bousquet-Antonelli, C.1    Henry, Y.2    G6lugne, J.-P.3
  • 85
    • 33845265038 scopus 로고    scopus 로고
    • Dynamic association and localization of human h/aca rnp proteins
    • Kittur N, Darzacq X, Roy S et al. Dynamic association and localization of human H/ACA RNP proteins. RNA 2006; 12:2057-2062.
    • (2006) RNA , vol.12 , pp. 2057-2062
    • Kittur, N.1    Darzacq, X.2    Roy, S.3
  • 86
    • 0036786962 scopus 로고    scopus 로고
    • Naflp, an essential nucleoplasmic factor specifically required for accumulation of box h/aca small nucleolar rnps
    • Dez C, Noaillac-Depcyre J, Caizcrgucs-Ferrer M et al. Naflp, an essential nucleoplasmic factor specifically required for accumulation of box H/ACA small nucleolar RNPs. Mol Cell Biol 2002; 22:7053-7065.
    • (2002) Mol Cell Biol , vol.22 , pp. 7053-7065
    • Dez, C.1    Noaillac-Depcyre, J.2    Caizcrgucs-Ferrer, M.3
  • 87
    • 0036916733 scopus 로고    scopus 로고
    • Naflp is a box h/aca snornp assembly factor
    • Fatica A, Dlakic M, Tollervey D. Naflp is a box H/ACA snoRNP assembly factor. RNA 2002; 8:1502-1514.
    • (2002) RNA , vol.8 , pp. 1502-1514
    • Fatica, A.1    Dlakic, M.2    Tollervey, D.3
  • 88
    • 0037159511 scopus 로고    scopus 로고
    • The shqlp.Naflp complex is required for box h/aca small nucleolar ribonucleoprotein particle biogenesis
    • Yang PK, Rotondo G, Porras T et al. The Shqlp.Naflp complex is required for box H/ACA small nucleolar ribonucleoprotein particle biogenesis. J Biol Chem 2002; 277:45235-45242.
    • (2002) J Biol Chem , vol.277 , pp. 45235-45242
    • Yang, P.K.1    Rotondo, G.2    Porras, T.3
  • 89
    • 20744440616 scopus 로고    scopus 로고
    • The cotranscriptional assembly of snornps controls the biosynthesis of h/aca snornas in saccharomyces cerevisiae
    • Ballarino M, Morlando M, Paganof et al. The cotranscriptional assembly of snoRNPs controls the biosynthesis of H/ACA snoRNAs in Saccharomyces cerevisiae. Mol Cell Biol 2005; 25:5396-5403.
    • (2005) Mol Cell Biol , vol.25 , pp. 5396-5403
    • Ballarino, M.1    Morlando, M.2    Pagano, F.3
  • 90
    • 33646076438 scopus 로고    scopus 로고
    • Stepwise rnp assembly at the site of h/aca rna transcription in human cells
    • Darzacq X, Kittur N, Roy S et al. Stepwise RNP assembly at the site of H/ACA RNA transcription in human cells. J Cell Biol 2006; 173:207-218.
    • (2006) J Cell Biol , vol.173 , pp. 207-218
    • Darzacq, X.1    Kittur, N.2    Roy, S.3
  • 91
    • 33646200076 scopus 로고    scopus 로고
    • Hnafl is required for accumulation of human box h/aca snornps. Scarnps and telomerase
    • Hoareau-Aveilla C, Bonoli M, Caizergues-Ferrer M et al. hNafl is required for accumulation of human box H/ACA snoRNPs. scaRNPs and telomerase. RNA 2006; 12:832-840.
    • (2006) RNA , vol.12 , pp. 832-840
    • Hoareau-Aveilla, C.1    Bonoli, M.2    Caizergues-Ferrer, M.3
  • 92
    • 16244366466 scopus 로고    scopus 로고
    • Cotranscriptional recruitment of the pseudouridylsynthetase cbf5p and of the rna binding protein naflp during h/aca snornp assembly
    • Yang PK. Hoareau C. Froment C et al. Cotranscriptional recruitment of the pseudouridylsynthetase Cbf5p and of the RNA binding protein Naflp during H/ACA snoRNP assembly. Mol Cell Biol 2005; 25:3295-3304.
    • (2005) Mol Cell Biol , vol.25 , pp. 3295-3304
    • Yang, P.K.1    Hoareau, C.2    Froment, C.3
  • 93
    • 34547559807 scopus 로고    scopus 로고
    • The box h/aca rnp assembly factor naflp contains a domain homologous to garlp mediating its interaction with cbfjp
    • Leulliot N, Godin KS, Hoareau-Aveilla C et al. The box H/ACA RNP assembly factor Naflp contains a domain homologous to Garlp mediating its interaction with Cbfjp. J Mol Biol 2007; 371:1338-1353.
    • (2007) J Mol Biol , vol.371 , pp. 1338-1353
    • Leulliot, N.1    Godin, K.S.2    Hoareau-Aveilla, C.3
  • 94
    • 0028117705 scopus 로고
    • Nap57, a mammalian nucleolar protein with a putative homolog in yeast and bacteria
    • Meier UT, Blobel G. NAP57, a mammalian nucleolar protein with a putative homolog in yeast and bacteria. J Cell Biol (correction appeared in 140: 447) 1994; 127:1505-1514.
    • (1994) J Cell Biol (Correction Appeared in 140: 447) , vol.127 , pp. 1505-1514
    • Meier, U.T.1    Blobel, G.2
  • 95
    • 0035914360 scopus 로고    scopus 로고
    • Direct interaction of the spinal muscular atrophy disease protein smn with the small nucleolar rna-associated protein fibrillarin
    • Jones KW, Gorzynski K, Hales CM et al. Direct interaction of the spinal muscular atrophy disease protein SMN with the small nucleolar RNA-associated protein fibrillarin. J Biol Chem 2001; 276:38645-38651.
    • (2001) J Biol Chem , vol.276 , pp. 38645-38651
    • Jones, K.W.1    Gorzynski, K.2    Hales, C.M.3
  • 96
    • 0035943003 scopus 로고    scopus 로고
    • The survival of motor neurons (Smn) protein interacts with the snornp proteins fibrillarin and gar1
    • Pellizzoni L, Baccon J, Charroux B et al. The survival of motor neurons (SMN) protein interacts with the snoRNP proteins fibrillarin and GAR1. Curr Biol 2001; 11:1079-1088.
    • (2001) Curr Biol , vol.11 , pp. 1079-1088
    • Pellizzoni, L.1    Baccon, J.2    Charroux, B.3
  • 97
    • 0037073714 scopus 로고    scopus 로고
    • Determinants of the interaction of the spinal muscular atrophy disease protein smn with the dimethylarginine-modified box h/aca small nucleolar ribonucleoprotein gar1
    • Whitehead SE, Jones KW, Zhang X et al. Determinants of the interaction of the spinal muscular atrophy disease protein SMN with the diMethylarginine-modified box H/ACA small nucleolar ribonucleoprotein GAR1. J Biol Chem 2002; 277:48087-48093.
    • (2002) J Biol Chem , vol.277 , pp. 48087-48093
    • Whitehead, S.E.1    Jones, K.W.2    Zhang, X.3
  • 98
    • 39049164474 scopus 로고    scopus 로고
    • The hsp90 chaperone controls the biogenesis of l7ae rnps through conserved machinery
    • Boulon S. Marmier-Gourrier N. Pradet-Balade B et al. The Hsp90 chaperone controls the biogenesis of L7Ae RNPs through conserved machinery. J Cell Biol 2008; 180:579-595.
    • (2008) J Cell Biol , vol.180 , pp. 579-595
    • Boulon, S.1    Marmier-Gourrier, N.2    Pradet-Balade, B.3
  • 99
    • 0036889385 scopus 로고    scopus 로고
    • Conserved stem ii of the box c/d motif is essential for nucleolar localization and is required, along with the 15.5k protein, for the hierarchical assembly of the box c/d snornp
    • Watkins NJ, Dickmanns A, Luhrmann R. Conserved stem II of the box C/D motif is essential for nucleolar localization and is required, along with the 15.5K protein, for the hierarchical assembly of the box C/D snoRNP. Mol Cell Biol 2002; 22:8342-8352.
    • (2002) Mol Cell Biol , vol.22 , pp. 8342-8352
    • Watkins, N.J.1    Dickmanns, A.2    Luhrmann, R.3
  • 100
    • 0034769951 scopus 로고    scopus 로고
    • A well-connected and conserved nucleoplasmic helicasc is required for production of box c/d and h/aca snornas and localization of snornp proteins
    • King TH, Decatur WA, Bertrand E et al. A well-connected and conserved nucleoplasmic helicasc is required for production of box C/D and H/ACA snoRNAs and localization of snoRNP proteins. Mol Cell Biol 2001; 21:7731-7746.
    • (2001) Mol Cell Biol , vol.21 , pp. 7731-7746
    • King, T.H.1    Decatur, W.A.2    Bertrand, E.3
  • 101
    • 40749135820 scopus 로고    scopus 로고
    • Identification of atpases pontin and reptin as telomerase components essential for holoenzyme assembly
    • Venteicher AS, Mcng Z, Mason PJ et al. Identification of ATPases pontin and reptin as telomerase components essential for holoenzyme assembly. Cell 2008; 132:945-957.
    • (2008) Cell , vol.132 , pp. 945-957
    • Venteicher, A.S.1    McMCNGg, Z.2    Mason, P.J.3
  • 102
    • 39049143941 scopus 로고    scopus 로고
    • Molecular chaperone hsp90 stabilizes pihl/nopl7 to maintain r2tp complex activity that regulates snorna accumulation
    • Zhao R, Kakihara Y, Gribun A et al. Molecular chaperone Hsp90 stabilizes Pihl/Nopl7 to maintain R2TP complex activity that regulates snoRNA accumulation. J Cell Biol 2008; 180:563-578.
    • (2008) J Cell Biol , vol.180 , pp. 563-578
    • Zhao, R.1    Kakihara, Y.2    Gribun, A.3
  • 103
    • 0026729432 scopus 로고
    • Stem cell origin of the hematopoietic defect in dyskeratosis congenita
    • Marsh JC, Will AJ, Hows JM et al. “Stem cell” origin of the hematopoietic defect in dyskeratosis congenita. Blood 1992; 79:3138-3144.
    • (1992) Blood , vol.79 , pp. 3138-3144
    • Marsh, J.C.1    Will, A.J.2    Hows, J.M.3
  • 105
    • 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
  • 106
    • 0031799895 scopus 로고    scopus 로고
    • X-linked dyskeratosis congenita is caused by mutations in a highly conserved gene with putative nucleolar functions
    • Heiss NS, Knight SW, Vulliamy TJ et al. X-linked dyskeratosis congenita is caused by mutations in a highly conserved gene with putative nucleolar functions. Nat Genet 1998; 19:32-38.
    • (1998) Nat Genet , vol.19 , pp. 32-38
    • Heiss, N.S.1    Knight, S.W.2    Vulliamy, T.J.3
  • 107
    • 0033518188 scopus 로고    scopus 로고
    • A telomerase component is defective in the human disease dyskeratosis congenita
    • Mitchell JR, Wood E, Collins K. A telomerase component is defective in the human disease dyskeratosis congenita. Nature 1999; 402:551-555
    • (1999) Nature , vol.402 , pp. 551-555
    • Mitchell, J.R.1    Wood, E.2    Collins, K.3
  • 108
    • 40749085700 scopus 로고    scopus 로고
    • Tinf2, a component of the shelterin telomere protection complex, is mutated in dyskeratosis congenita
    • Savage SA, Giri N, Baerlocher GM et al. TINF2, a component of the shelterin telomere protection complex, is mutated in dyskeratosis congenita. Am J Hum Genet 2008; 82:501-509.
    • (2008) Am J Hum Genet , vol.82 , pp. 501-509
    • Savage, S.A.1    Giri, N.2    Baerlocher, G.M.3
  • 109
    • 45849131292 scopus 로고    scopus 로고
    • Mutations in the telomerase component nhp2 cause the premature ageing syndrome dyskeratosis congenita
    • Vulliamy T, Beswick R, Kirwan M et al. Mutations in the telomerase component NHP2 cause the premature ageing syndrome dyskeratosis congenita. Proc Natl Acad Sci USA 2008; 105:8073-8078.
    • (2008) Proc Natl Acad Sci USA , vol.105 , pp. 8073-8078
    • Vulliamy, T.1    Beswick, R.2    Kirwan, M.3
  • 110
    • 34447307404 scopus 로고    scopus 로고
    • Genetic heterogeneity in autosomal recessive dyskeratosis congenita with one subtype due to mutations in the telomerasc-associatcd protein nop 10
    • Walne AJ, Vulliamy T, Marrone A et al. Genetic heterogeneity in autosomal recessive dyskeratosis congenita with one subtype due to mutations in the telomerasc-associatcd protein NOP 10. Hum Mol Genet 2007; 16:1619-1629.
    • (2007) Hum Mol Genet , vol.16 , pp. 1619-1629
    • Walne, A.J.1    Vulliamy, T.2    Marrone, A.3
  • 111
    • 55749094159 scopus 로고    scopus 로고
    • Tinf2 mutations result in very short telomeres: Analysis of a large cohort of patients with dyskeratosis congenita and related bone marrow failure syndromes
    • Walne AJ, Vulliamy TJ, Beswick R et al. TINF2 mutations result in very short telomeres: Analysis of a large cohort of patients with dyskeratosis congenita and related bone marrow failure syndromes. Blood 2008; 112(9):3594-600.
    • (2008) Blood , vol.112 , Issue.9 , pp. 3594-3600
    • Walne, A.J.1    Vulliamy, T.J.2    Beswick, R.3
  • 112
    • 27644574342 scopus 로고    scopus 로고
    • Haploinsufficiency of telomerase reverse transcriptase leads to anticipation in autosomal dominant dyskeratosis congenita
    • Armanios M, Chen JL, Chang YP et al. Haploinsufficiency of telomerase reverse transcriptase leads to anticipation in autosomal dominant dyskeratosis congenita. Proc Natl Acad Sci USA 2005; 102:15960-15964.
    • (2005) Proc Natl Acad Sci USA , vol.102 , pp. 15960-15964
    • Armanios, M.1    Chen, J.L.2    Chang, Y.P.3
  • 113
    • 0035960043 scopus 로고    scopus 로고
    • The rna component of telomerase is mutated in autosomal dominant dyskeratosis congenita
    • Vulliamy T, Marrone A, Goldman F et al. The RNA component of telomerase is mutated in autosomal dominant dyskeratosis congenita. Nature 2001; 413:432-435.
    • (2001) Nature , vol.413 , pp. 432-435
    • Vulliamy, T.1    Marrone, A.2    Goldman, F.3
  • 114
    • 28044471165 scopus 로고    scopus 로고
    • The effect of terc haploinsufficiency on the inheritance of telomere length
    • Goldman F, Bouarich R, Kulkami S et al. The effect of TERC haploinsufficiency on the inheritance of telomere length. Proc Natl Acad Sci USA 2005; 102:17119-17124.
    • (2005) Proc Natl Acad Sci USA , vol.102 , pp. 17119-17124
    • Goldman, F.1    Bouarich, R.2    Kulkami, S.3
  • 115
    • 48249112529 scopus 로고    scopus 로고
    • A pathogenic dyskerin mutation impairs proliferation and activates a dna damage response independent of telomere length in mice
    • Gu BW, Bessler M, Mason PJ. A pathogenic dyskerin mutation impairs proliferation and activates a DNA damage response independent of telomere length in mice. Proc Natl Acad Sci USA 2008; 105:10173-10178.
    • (2008) Proc Natl Acad Sci USA , vol.105 , pp. 10173-10178
    • Gu, B.W.1    Bessler, M.2    Mason, P.J.3
  • 116
    • 3242656131 scopus 로고    scopus 로고
    • Mouse dyskerin mutations affect accumulation of telomerase rna and small nucleolar rna, telomerase activity and ribosomal rna processing
    • Mochizuki Y, He J, Kulkami S et al. Mouse dyskerin mutations affect accumulation of telomerase RNA and small nucleolar RNA, telomerase activity and ribosomal RNA processing. Proc Natl Acad Sci USA 2004; 101:10756-10761.
    • (2004) Proc Natl Acad Sci USA , vol.101 , pp. 10756-10761
    • Mochizuki, Y.1    He, J.2    Kulkami, S.3
  • 117
    • 0037428129 scopus 로고    scopus 로고
    • Dyskeratosis congenita and cancer in mice deficient in ribosomal rna modification
    • Ruggero D, Grisendi S, Piazza F et al. Dyskeratosis congenita and cancer in mice deficient in ribosomal RNA modification. Science 2003; 299:259-262.
    • (2003) Science , vol.299 , pp. 259-262
    • Ruggero, D.1    Grisendi, S.2    Piazza, F.3
  • 118
    • 33646543044 scopus 로고    scopus 로고
    • Impaired control of ires-mcdiated translation in x-linked dyskeratosis congenita
    • Yoon A, Peng G, Brandcnburger Y et al. Impaired control of IRES-mcdiated translation in X-linked dyskeratosis congenita. Science 2006; 312:902-906.
    • (2006) Science , vol.312 , pp. 902-906
    • Yoon, A.1    Peng, G.2    Brandcnburger, Y.3
  • 119
    • 18044399024 scopus 로고    scopus 로고
    • Dyskeratosis congenita: Molecular insights into telomerase function, ageing and cancer
    • Marrone A, Dokal I. Dyskeratosis congenita: molecular insights into telomerase function, ageing and cancer. Expert Rev Mol Med 2004; 6:1-23.
    • (2004) Expert Rev Mol Med , vol.6 , pp. 1-23
    • Marrone, A.1    Dokal, I.2
  • 120
    • 0037292453 scopus 로고    scopus 로고
    • Ribosome structure and activity are altered in cells lacking snornps that form pseudouridines in the peptidyl transferase center
    • King TH, Liu B, McCully RR et al. Ribosome structure and activity are altered in cells lacking snoRNPs that form pseudouridines in the peptidyl transferase center. Mol Cell 2003; 11:425-435.
    • (2003) Mol Cell , vol.11 , pp. 425-435
    • King, T.H.1    Liu, B.2    McCully, R.R.3
  • 121
    • 37349128219 scopus 로고    scopus 로고
    • Fournier mj. Rrna modifications in an intersubunit bridge of the ribosome strongly affect both ribosome biogenesis and activity
    • Liang XH, Liu Q, Fournier MJ. rRNA modifications in an intersubunit bridge of the ribosome strongly affect both ribosome biogenesis and activity. Mol Cell 2007; 28:965-977.
    • (2007) Mol Cell , vol.28 , pp. 965-977
    • Liang, X.H.1    Liu, Q.2
  • 122
    • 0032718276 scopus 로고    scopus 로고
    • Point mutations in yeast cbf5 can abolish in vivo pseudou-ridylation of rrna
    • Zebarjadian Y, King T, Fournier MJ et al. Point mutations in yeast CBF5 can abolish in vivo pseudou-ridylation of rRNA. Mol Cell Biol 1999; 19:7461-7472.
    • (1999) Mol Cell Biol , vol.19 , pp. 7461-7472
    • Zebarjadian, Y.1    King, T.2    Fournier, M.J.3


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.