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Volumn 44, Issue 1, 2011, Pages 95-122

Structures of ribonucleoprotein particle modification enzymes

Author keywords

[No Author keywords available]

Indexed keywords

ENZYME; RIBONUCLEOPROTEIN; RNA;

EID: 79951676937     PISSN: 00335835     EISSN: 14698994     Source Type: Journal    
DOI: 10.1017/S0033583510000235     Document Type: Article
Times cited : (18)

References (152)
  • 1
  • 2
    • 67349200973 scopus 로고    scopus 로고
    • Crystal structure of an RluF-RNA complex: A base-pair rearrangement is the key to selectivity of RluF for U2604 of the ribosome
    • ALIAN, A., DEGIOVANNI, A., GRINER, S. L., FINER-MOORE, J. S. & STROUD, R. M. (2009). Crystal structure of an RluF-RNA complex: a base-pair rearrangement is the key to selectivity of RluF for U2604 of the ribosome. Journal of Molecular Biology 388, 785-800.
    • (2009) Journal of Molecular Biology , vol.388 , pp. 785-800
    • Alian, A.1    Degiovanni, A.2    Griner, S.L.3    Finer-Moore, J.S.4    Stroud, R.M.5
  • 3
    • 0036794074 scopus 로고    scopus 로고
    • The SBP2 and 15-5 kD/Snu13p proteins share the same RNA binding domain: Identification of SBP2 amino acids important to SECIS RNA binding
    • ALLMANG, C., CARBON, P. & KROL, A. (2002). The SBP2 and 15-5 kD/Snu13p proteins share the same RNA binding domain: identification of SBP2 amino acids important to SECIS RNA binding. RNA 8, 1308-1318.
    • (2002) RNA , vol.8 , pp. 1308-1318
    • Allmang, C.1    Carbon, P.2    Krol, A.3
  • 4
    • 0033214175 scopus 로고    scopus 로고
    • Functions of the exosome in rRNA, snoRNA and snRNA synthesis
    • DOI 10.1093/emboj/18.19.5399
    • ALLMANG, C, KUFEL, J., CHANFREAU, G., MITCHELL, P., PETFALSKI, E. & TOLLERVEY, D. (1999). Functions of the exosome in rRNA, snoRNA and snRNA synthesis. EMBO Journal 18, 5399-5410. (Pubitemid 29465589)
    • (1999) EMBO Journal , vol.18 , Issue.19 , pp. 5399-5410
    • Allmang, C.1    Kufel, J.2    Chanfreau, G.3    Mitchell, P.4    Petfalski, E.5    Tollervey, D.6
  • 5
    • 0036132209 scopus 로고    scopus 로고
    • SPOUT: A class of methyltransferases that includes spoU and trmD RNA methylase superfamilies, and novel superfamilies of predicted prokaryotic RNA methylases
    • ANANTHARAMAN, V., KOONIN, E. V. & ARAVIND, L. (2002). SPOUT: a class of methyltransferases that includes spoU and trmD RNA methylase superfamilies, and novel superfamilies of predicted prokaryotic RNA me-thylases. Journal ofMolecular Microbiology and Biotechnology 4, 71-75. (Pubitemid 33121215)
    • (2002) Journal of Molecular Microbiology and Biotechnology , vol.4 , Issue.1 , pp. 71-75
    • Anantharam, V.1    Koonin, E.V.2    Aravind, L.3
  • 6
    • 0842347403 scopus 로고    scopus 로고
    • U17/snR30 is a Ubiquitous snoRNA with Two Conserved Sequence Motifs Essential for 18S rRNA Production
    • DOI 10.1128/MCB.24.4.1769-1778.2004
    • ATZORN, V., FRAGAPANE, P. & KISS, T. (2004). U17/snR30 is a ubiquitous snoRNA with two conserved sequence motifs essential for 18S rRNA production. Molecular and Cellular Biology 24, 1769-1778. (Pubitemid 38167097)
    • (2004) Molecular and Cellular Biology , vol.24 , Issue.4 , pp. 1769-1778
    • Atzorn, V.1    Fragapane, P.2    Kiss, T.3
  • 7
    • 0032080005 scopus 로고    scopus 로고
    • Gar1p binds to the small nucleolar RNAs snR10 and snR30 in vitro through a nontypical RNA binding element
    • DOI 10.1074/jbc.273.18.10868
    • BAGNI, C. & LAPEYRE, B. (1998). Gar1p binds to the small nucleolar RNAs snR10 and snR30 in vitro through a nontypical RNA binding element. Journal of Biological Chemistry 273, 10868-10873. (Pubitemid 28204922)
    • (1998) Journal of Biological Chemistry , vol.273 , Issue.18 , pp. 10868-10873
    • Bagni, C.1    Lapeyre, B.2
  • 8
    • 18844397555 scopus 로고    scopus 로고
    • RNA-guided RNA modification: Functional organization of the archaeal H/ACA RNP
    • DOI 10.1101/gad.1309605
    • BAKER D. L., YOUSSEF O. A., CHASTKOFSKY M. I., DY D. A., TERNS R. M., TERNS M. P. (2005). RNA-guided RNA modification: functional organization of the archaeal H/ACA RNP. Genes and Development 19, 1238-1248. (Pubitemid 40696189)
    • (2005) Genes and Development , vol.19 , Issue.10 , pp. 1238-1248
    • Baker, D.L.1    Youssef, O.A.2    Chastkofsky, M.I.R.3    Dy, D.A.4    Terns, R.M.5    Terns, M.P.6
  • 9
    • 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
    • DOI 10.1016/S0092-8674(00)80156-7
    • BALAKIN, A. G., SMITH, L. & FOURNIER, M. J. (1996). The RNA world of the nucleolus: two major families of small RNAs defined by different box elements with related functions. Cell 86, 823-834. (Pubitemid 26303450)
    • (1996) Cell , vol.86 , Issue.5 , pp. 823-834
    • Balakin, A.G.1    Smith, L.2    Fournier, M.J.3
  • 10
    • 75649096366 scopus 로고    scopus 로고
    • Nucleotide modifications in three functionally important regions of the Saccharomyces cerevisiae ribosome affect translation accuracy
    • BAUDIN-BAILLIEU, A., FABRET, C., LIANG, X. H., PIEKNA-PRZYBYLSKA, D., FOURNIER, M.J. & ROUSSET, J.P. (2009). Nucleotide modifications in three functionally important regions of the Saccharomyces cerevisiae ribosome affect translation accuracy. Nucleic Acids Research 37, 7665-7677.
    • (2009) Nucleic Acids Research , vol.37 , pp. 7665-7677
    • Baudin-Baillieu, A.1    Fabret, C.2    Liang, X.H.3    Piekna-Przybylska, D.4    Fournier, M.J.5    Rousset, J.P.6
  • 12
    • 34250305146 scopus 로고    scopus 로고
    • Identification and analysis of functional elements in 1% of the human genome by the ENCODE pilot project
    • DOI 10.1038/nature05874, PII NATURE05874
    • BIRNEY, E., STAMATOYANNOPOULOS, J.A., DUTTA, A., GUIGO, R., GINGERAS, T. R., MARGULIES, E. H., WENG, Z., SNYDER, M., DERMITZAKIS, E. T., THURMAN, R. E., KUEHN, M. S., TAYLOR, C. M., NEPH, S., KOCH, C. M., ASTHANA, S., MALHOTRA, A., ADZHUBEI, I., GREENBAUM, J. A., ANDREWS, R. M., FLICEK, P., BOYLE, P. J., CAO, H., CARTER, N. P., CLELLAND, G. K., DAVIS, S., DAY, N., DHAMI, P., DILLON, S. C., DORSCHNER, M. O., FIEGLER, H., GIRESI, P. G., GOLDY, J., HAWRYLYCZ, M., HAYDOCK, A., HUMBERT, R., JAMES, K.D., JOHNSON, B.E., JOHNSON, E.M., FRUM, T.T., ROSENZWEIG, E.R., KARNANI, N., LEE, K., LEFEBVRE, G. C., NAVAS, P. A., NERI, F., PARKER, S. C., SABO, P. J., SANDSTROM, R., SHAFER, A., VETRIE, D., WEAVER, M., WILCOX, S., YU, M., COLLINS, F. S., DEKKER, J., LIEB, J. D., TULLIUS, T. D., CRAWFORD, G. E., SUNYAEV, S., NOBLE, W. S., DUNHAM, I., DENOEUD, F., REYMOND, A., KAPRANOV, P., ROZOWSKY, J., ZHENG, D., CASTELO, R., FRANKISH, A., HARROW, J., GHOSH, S., SANDELIN, A., HOFACKER, I. L., BAERTSCH, R., KEEFE, D., DIKE, S., CHENG, J., HIRSCH, H. A., SEKINGER, E.A., LAGARDE, J., ABRIL, J. F., SHAHAB, A., FLAMM, C., FRIED, C., HACKERMULLER, J., HERTEL, J., LINDEMEYER, M., MISSAL, K., TANZER, A., WASHIETL, S., KORBEL, J., EMANUELSSON, O., PEDERSEN, J. S., HOLROYD, N., TAYLOR, R., SWARBRECK, D., MATTHEWS, N., DICKSON, M.C., THOMAS, D.J., WEIRAUCH, M. T., GILBERT, J., DRENKOW, J., BELL, I., ZHAO, X., SRINIVASAN, K. G., SUNG, W. K., OOI, H. S., CHIU, K.P., FOISSAC, S., ALIOTO, T., BRENT, M., PACHTER, L., TRESS, M. L., VALENCIA, A., CHOO, S. W., CHOO, C.Y., UCLA, C., MANZANO, C., WYSS, C., CHEUNG, E., CLARK, T. G., BROWN, J. B., GANESH, M., PATEL, S., TAMMANA, H., CHRAST, J., HENRICHSEN, C. N., KAI, C., KAWAI, J., NAGALAKSHMI, U., WU, J., LIAN, Z., LIAN, J., NEWBURGER, P., ZHANG, X., BICKEL, P., MATTICK, J.S., CARNINCI, P., HAYASHIZAKI, Y., WEISSMAN, S., HUBBARD, T., MYERS, R. M., ROGERS, J., STADLER, P. F., LOWE, T. M., WEI, C. L., RUAN, Y., STRUHL, K., GERSTEIN, M., ANTONARAKIS, S. E., FU, Y., GREEN, E.D., KARAOZ, U., SIEPEL, A., TAYLOR, J., LIEFER, L.A., WETTERSTRAND, K.A., GOOD, P.J., FEINGOLD, E.A., GUYER, M.S., COOPER, G.M., ASIMENOS, G., DEWEY, C. N., HOU, M., NIKOLAEV, S., MONTOYA-BURGOS, J. I., LOYTYNOJA, A., WHELAN, S., PARDI, F., MASSINGHAM, T., HUANG, H., ZHANG, N. R., HOLMES, I., MULLIKIN, J. C., URETA-VIDAL, A., PATEN, B., SERINGHAUS, M., CHURCH, D., ROSENBLOOM, K., KENT, W. J., STONE, E. A., BATZOGLOU, S., GOLDMAN, N., HARDISON, R. C., HAUSSLER, D., MILLER, W., SIDOW, A., TRINKLEIN, N.D., ZHANG, Z.D., BARRERA, L., STUART, R., KING, D. C., AMEUR, A., ENROTH, S., BIEDA, M. C., KIM, J., BHINGE, A. A., JIANG, N., LIU, J., YAO, F., VEGA, V. B., LEE, C. W., NG, P., SHAHAB, A., YANG, A., MOQTADERI, Z., ZHU, Z., XU, X., SQUAZZO, S., OBERLEY, M. J., INMAN, D., SINGER, M. A., RICHMOND, T. A., MUNN, K.J., RADA-IGLESIAS, A., WALLERMAN, O., KOMOROWSKI, J., FOWLER, J.C., COUTTET, P., BRUCE, A. W., DOVEY, O. M., ELLIS, P. D., LANGFORD, C. F., NIX, D.A., EUSKIRCHEN, G., HARTMAN, S., URBAN, A. E., KRAUS, P., VAN CALCAR, S., HEINTZMAN, N., KIM, T. H., WANG, K., QU, C., HON, G., LUNA, R., GLASS, C. K., ROSENFELD, M. G., ALDRED, S. F., COOPER, S. J., HALEES, A., LIN, J. M., SHULHA, H. P., ZHANG, X., XU, M., HAIDAR, J. N., YU, Y., RUAN, Y., IYER, V. R., GREEN, R. D., WADELIUS, C., FARNHAM, P. J., REN, B., HARTE, R. A., HINRICHS, A. S., TRUMBOWER, H., CLAWSON, H., HILLMAN-JACKSON, J., ZWEIG, A.S., SMITH, K., THAKKAPALLAYIL, A., BARBER, G., KUHN, R.M., KAROLCHIK, D., ARMENGOL, L., BIRD, C. P., DE BAKKER, P. I., KERN, A. D., LOPEZ-BIGAS, N., MARTIN, J. D., STRANGER, B. E., WOODROFFE, A., DAVYDOV, E., DIMAS, A., EYRAS, E., HALLGRIMSDOTTIR, I.B., HUPPERT, J., ZODY, M. C., ABECASIS, G. R., ESTIVILL, X., BOUFFARD, G. G., GUAN, X., HANSEN, N. F., IDOL, J. R., MADURO, V. V., MASKERI, B., MCDOWELL, J. C., PARK, M., THOMAS, P. J., YOUNG, A. C., BLAKESLEY, R. W., MUZNY, D. M., SODERGREN, E., WHEELER, D. A., WORLEY, K. C., JIANG, H., WEINSTOCK, G.M., GIBBS, R.A., GRAVES, T., FULTON, R., MARDIS, E. R., WILSON, R. K., CLAMP, M., CUFF, J., GNERRE, S., JAFFE, D.B., CHANG, J.L., LINDBLAD-TOH, K., LANDER, E.S., KORIABINE, M., NEFEDOV, M., OSOEGAWA, K., YOSHINAGA, Y., ZHU, B. & DE JONG, P. J. (2007). Identification and analysis of functional elements in 1% of the human genome by the ENCODE pilot project. Nature 447, 799-816. (Pubitemid 46920138)
    • (2007) Nature , vol.447 , Issue.7146 , pp. 799-816
    • Birney, E.1    Stamatoyannopoulos, J.A.2    Dutta, A.3    Guigo, R.4    Gingeras, T.R.5    Margulies, E.H.6    Weng, Z.7    Snyder, M.8    Dermitzakis, E.T.9    Thurman, R.E.10    Kuehn, M.S.11    Taylor, C.M.12    Neph, S.13    Koch, C.M.14    Asthana, S.15    Malhotra, A.16    Adzhubei, I.17    Greenbaum, J.A.18    Andrews, R.M.19    Flicek, P.20    more..
  • 17
    • 0037099680 scopus 로고    scopus 로고
    • Site-specific cross-linking analyses reveal an asymmetric protein distribution for a box C/D snoRNP
    • DOI 10.1093/emboj/cdf376
    • CAHILL, N. M., FRIEND, K., SPECKMANN, W., LI, Z. H., TERNS, R. M., TERNS, M. P. & STEITZ, J. A. (2002). Site-specific cross-linking analyses reveal an asymmetric protein distribution for a box C/D snoRNP. EMBO Journal 21, 3816-3828. (Pubitemid 34787054)
    • (2002) EMBO Journal , vol.21 , Issue.14 , pp. 3816-3828
    • Cahill, N.M.1    Friend, K.2    Speckmann, W.3    Li, Z.-H.4    Terns, R.M.5    Terns, M.P.6    Steitz, J.A.7
  • 18
    • 0032126735 scopus 로고    scopus 로고
    • Processing of a dicistronic small nucleolar RNA precursor by the RNA endonuclease Rnt1
    • DOI 10.1093/emboj/17.13.3726
    • CHANFREAU, G., ROTONDO, G., LEGRAIN, P. & JACQUIER, A. (1998). Processing of a dicistronic small nucleolar RNA precursor by the RNA endonuclease Rnt1. EMBO Journal 17, 3726-3737. (Pubitemid 28327390)
    • (1998) EMBO Journal , vol.17 , Issue.13 , pp. 3726-3737
    • Chanfreau, G.1    Rotondo, G.2    Legrain, P.3    Jacquier, A.4
  • 19
    • 3142608984 scopus 로고    scopus 로고
    • Joint X-ray and NMR refinement of the yeast L30e-mRNA complex
    • DOI 10.1016/j.str.2004.04.023, PII S0969212604002047
    • CHAO, J. A. & WILLIAMSON, J. R. (2004). Joint X-ray and NMR refinement of the yeast L30e-mRNA complex. Structure 12, 1165-1176. (Pubitemid 38900759)
    • (2004) Structure , vol.12 , Issue.7 , pp. 1165-1176
    • Chao, J.A.1    Williamson, J.R.2
  • 20
    • 20144374350 scopus 로고    scopus 로고
    • Reconstitution of archaeal H/ACA small ribonucleoprotein complexes active in pseudouridylation
    • DOI 10.1093/nar/gki630
    • CHARPENTIER, B., MULLER, S. & BRANLANT, C. (2005). Reconstitution of archaeal H/ACA small ribonucleo-protein complexes active in pseudouridylation. Nucleic Acids Research 33, 3133-3144. (Pubitemid 41194457)
    • (2005) Nucleic Acids Research , vol.33 , Issue.10 , pp. 3133-3144
    • Charpentier, B.1    Muller, S.2    Branlant, C.3
  • 21
    • 0035883736 scopus 로고    scopus 로고
    • AdoMet-dependent methylation, DNA methyltransferases and base flipping
    • CHENG, X. & ROBERTS, R. J. (2001). AdoMet-dependent methylation, DNA methyltransferases and base flipping. Nucleic Acids Research 29, 3784-3795. (Pubitemid 32910519)
    • (2001) Nucleic Acids Research , vol.29 , Issue.18 , pp. 3784-3795
    • Cheng, X.1    Roberts, R.J.2
  • 22
    • 0035890644 scopus 로고    scopus 로고
    • Box C/D RNA guides for the ribose methylation of archaeal tRNAs. The tRNATrp intron guides the formation of two ribose-methylated nucleosides in the mature tRNATrp
    • CLOUET D'ORVAL, B., BORTOLIN, M.L., GASPIN, C. & BACHELLERIE, J. P. (2001). Box C/D RNA guides for the ribose methylation of archaeal tRNAs. The tRNATrp intron guides the formation of two ribose-methylated nucleosides in the mature tRNATrp. Nucleic Acids Research 29, 4518-4529. (Pubitemid 33095012)
    • (2001) Nucleic Acids Research , vol.29 , Issue.22 , pp. 4518-4529
    • D'Orval, B.C.1    Bortolin, M.-L.2    Gaspin, C.3    Bachellerie, J.-P.4
  • 23
    • 33745862398 scopus 로고    scopus 로고
    • The biogenesis and regulation of telomerase holoenzymes
    • DOI 10.1038/nrm1961, PII NRM1961
    • COLLINS, K. (2006). The biogenesis and regulation of telomerase holoenzymes. Nature Reviews Molecular Cell Biology 7, 484-494. (Pubitemid 44036454)
    • (2006) Nature Reviews Molecular Cell Biology , vol.7 , Issue.7 , pp. 484-494
    • Collins, K.1
  • 25
    • 27844495652 scopus 로고    scopus 로고
    • Small non-coding RNAs in Archaea
    • DOI 10.1016/j.mib.2005.10.013, PII S1369527405001694, Growth Development
    • DENNIS, P. P. & OMER, A. (2005). Small non-coding RNAs in archaea. Current Opinion in Microbiology 8, 685-694. (Pubitemid 41643037)
    • (2005) Current Opinion in Microbiology , vol.8 , Issue.6 , pp. 685-694
    • Dennis, P.P.1    Omer, A.2
  • 27
    • 65649140052 scopus 로고    scopus 로고
    • Structural mechanism of substrate RNA recruitment in H/ACA RNA-guided pseudouridine synthase
    • DUAN, J., LI, L., LU, J., WANG, W. & YE, K. (2009). Structural mechanism of substrate RNA recruitment in H/ACA RNA-guided pseudouridine synthase. Molecular Cell 34, 427-439.
    • (2009) Molecular Cell , vol.34 , pp. 427-439
    • Duan, J.1    L, L.I.2    J, L.U.3    Wang, W.4    K, Y.E.5
  • 28
    • 0033534387 scopus 로고    scopus 로고
    • +-C base-pair and by pseudouridine
    • DOI 10.1006/jmbi.1998.2297
    • DURANT, P. C. & DAVIS, D. R. (1999). Stabilization of the anticodon stem-loop of tRNALys,3 by an A+-C base-pair and by pseudouridine. Journal of Molecular Biology 285, 115-131. (Pubitemid 29034031)
    • (1999) Journal of Molecular Biology , vol.285 , Issue.1 , pp. 115-131
    • Durant, P.C.1    Davis, D.R.2
  • 29
    • 33646552752 scopus 로고    scopus 로고
    • The vertebrate E1/U17 small nucleolar ribonucleoprotein particle
    • DOI 10.1002/jcb.20821
    • ELICEIRI, G. L. (2006). The vertebrate E1/U17 small nu-cleolar ribonucleoprotein particle. Journal of Cellular Biochemistry 98, 486-495. (Pubitemid 43727171)
    • (2006) Journal of Cellular Biochemistry , vol.98 , Issue.3 , pp. 486-495
    • Eliceiri, G.L.1
  • 30
    • 0036591881 scopus 로고    scopus 로고
    • Making ribosomes
    • DOI 10.1016/S0955-0674(02)00336-8
    • FATICA, A. & TOLLERVEY, D. (2002). Making ribosomes. Current Opinion in Cell Biology 14, 313-318. (Pubitemid 34626969)
    • (2002) Current Opinion in Cell Biology , vol.14 , Issue.3 , pp. 313-318
    • Fatica, A.1    Tollervey, D.2
  • 31
    • 0033987499 scopus 로고    scopus 로고
    • The structural basis for tRNA recognition and pseudouridine formation by pseudouridine synthase I
    • DOI 10.1038/71219
    • FOSTER, P. G., HUANG, L., SANTI, D. V. & STROUD, R. M. (2000). The structural basis for tRNA recognition and pseudouridine formation by pseudouridine synthase I. Nature Structural Biology 7, 23-27. (Pubitemid 30043243)
    • (2000) Nature Structural Biology , vol.7 , Issue.1 , pp. 23-27
    • Foster, P.G.1    Huang, L.2    Santi, D.V.3    Stroud, R.M.4
  • 32
    • 33748460634 scopus 로고    scopus 로고
    • Assembly of the Archaeal Box C/D sRNP Can Occur via Alternative Pathways and Requires Temperature-facilitated sRNA Remodeling
    • DOI 10.1016/j.jmb.2006.07.091, PII S0022283606009910
    • GAGNON, K. T., ZHANG, X., AGRIS, P. F. & MAXWELL, E. S. (2006). Assembly of the archaeal box C/D sRNP can occur via alternative pathways and requires temperature-facilitated sRNA remodeling. Journal of Molecular Biology 362, 1025-1042. (Pubitemid 44353524)
    • (2006) Journal of Molecular Biology , vol.362 , Issue.5 , pp. 1025-1042
    • Gagnon, K.T.1    Zhang, X.2    Agris, P.F.3    Maxwell, E.S.4
  • 33
    • 0030698635 scopus 로고    scopus 로고
    • Nucleolar KKE/D repeat proteins Nop56p and Nop58p interact with Nop1p and are required for ribosome biogenesis
    • GAUTIER, T., BERGES, T., TOLLERVEY, D. & HURT, E. (1997). Nucleolar KKE/D repeat proteins Nop56p and Nop58p interact with Nop1p and are required for ribosome biogenesis. Molecular Cell Biology 17, 7088-7098. (Pubitemid 27505938)
    • (1997) Molecular and Cellular Biology , vol.17 , Issue.12 , pp. 7088-7098
    • Gautier, T.1    Berges, T.2    Tollervey, D.3    Hurt, E.4
  • 36
    • 67349095697 scopus 로고    scopus 로고
    • The Box H/ACA snoRNP assembly factor Shq1p is a chaperone protein homologous to Hsp90 cochaperones that binds to the Cbf5p enzyme
    • GODIN, K. S., WALBOTT, H., LEULLIOT, N., VAN TILBEURGH, H. & VARANI, G. (2009). The Box H/ACA snoRNP assembly factor Shq1p is a chaperone protein homologous to Hsp90 cochaperones that binds to the Cbf5p enzyme. Journal of Molecular Biology 390, 231-244.
    • (2009) Journal of Molecular Biology , vol.390 , pp. 231-244
    • Godin, K.S.1    Walbott, H.2    Leulliot, N.3    Van Tilbeurgh, H.4    Varani, G.5
  • 37
    • 1642458421 scopus 로고    scopus 로고
    • The kink-turn motif in RNA is dimorphic, and metal ion-dependent
    • DOI 10.1261/rna.5176604
    • GOODY, T. A., MELCHER, S. E., NORMAN, D. G. & LILLEY, D. M. (2004). The kink-turn motif in RNA is dimor phic, and metal ion-dependent. RNA 10, 254-264. (Pubitemid 38129830)
    • (2004) RNA , vol.10 , Issue.2 , pp. 254-264
    • Goody, T.A.1    Melcher, S.E.2    Norman, D.G.3    Lilley, D.M.J.4
  • 39
    • 66449111635 scopus 로고    scopus 로고
    • SHQ1 is required prior to NAF1 for assembly of H/ACA small nucleolar and telomerase RNPs
    • GROZDANOV, P. N., ROY, S., KITTUR, N. & MEIER, U. T. (2009). SHQ1 is required prior to NAF1 for assembly of H/ACA small nucleolar and telomerase RNPs. RNA 15, 1188-1197.
    • (2009) RNA , vol.15 , pp. 1188-1197
    • Grozdanov, P.N.1    Roy, S.2    Kittur, N.3    Meier, U.T.4
  • 40
    • 0033435203 scopus 로고    scopus 로고
    • The mechanism of pseudouridine synthase I as deduced from its interaction with 5-fluorouracil-tRNA
    • DOI 10.1073/pnas.96.25.14270
    • GU, X., LIU, Y. & SANTI, D. V. (1999). The mechanism of pseudouridine synthase I as deduced from its interaction with 5-fluorouracil-tRNA. Proceedings of the National Academy of Sciences of the United States of America 96, 14270-14275. (Pubitemid 30000640)
    • (1999) Proceedings of the National Academy of Sciences of the United States of America , vol.96 , Issue.25 , pp. 14270-14275
    • Gu, X.1    Liu, Y.2    Santi, D.V.3
  • 41
    • 36248957607 scopus 로고    scopus 로고
    • Differential roles of archaeal box H/ACA proteins in guide RNA-dependent and independent pseudouridine formation
    • GURHA, P., JOARDAR, A., CHAURASIA, P. & GUPTA, R. (2007). Differential roles of archaeal box H/ACA proteins in guide RNA-dependent and independent pseu-douridine formation. RNA Biology 4, 101-109. (Pubitemid 350127834)
    • (2007) RNA Biology , vol.4 , Issue.2 , pp. 101-109
    • Gurha, P.1    Joardar, A.2    Chaurasia, P.3    Gupta, R.4
  • 42
    • 10944267609 scopus 로고    scopus 로고
    • A surfeit of factors: Why is ribosome assembly so much more complicated in eukaryotes than bacteria?
    • HAGE, A. E. & TOLLERVEY, D. (2004). A surfeit of factors: why is ribosome assembly so much more complicated in eukaryotes than bacteria? RNA Biology 1, 10-15.
    • (2004) RNA Biology , vol.1 , pp. 10-15
    • Hage, A.E.1    Tollervey, D.2
  • 43
    • 2342638215 scopus 로고    scopus 로고
    • Structure of protein L7Ae bound to a K-turn derived from an archaeal box H/ACA sRNA at 1.8 Å resolution
    • DOI 10.1016/j.str.2004.03.015, PII S0969212604000966
    • HAMMA, T. & FERRE-D'AMARE, A. R. (2004). Structure of protein L7Ae bound to a K-turn derived from an ar-chaeal box H/ACA sRNA at 1.8 A resolution. Structure (Cambridge) 12, 893-903. (Pubitemid 38595777)
    • (2004) Structure , vol.12 , Issue.5 , pp. 893-903
    • Hamma, T.1    Ferre-D'Amare, A.R.2
  • 44
    • 33750972578 scopus 로고    scopus 로고
    • Pseudouridine synthases
    • DOI 10.1016/j.chembiol.2006.09.009, PII S1074552106003425
    • HAMMA, T. & FERRE-D'AMARE, A. R. (2006). Pseudouridine synthases. Chemistry and Biology 13, 1125-1135. (Pubitemid 44750730)
    • (2006) Chemistry and Biology , vol.13 , Issue.11 , pp. 1125-1135
    • Hamma, T.1    Ferre-D'Amare, A.R.2
  • 45
    • 28544449371 scopus 로고    scopus 로고
    • The Cbf5-Nop10 complex is a molecular bracket that organizes box H/ACA RNPs
    • DOI 10.1038/nsmb1036
    • HAMMA, T., REICHOW, S. L., VARANI, G. & FERRE-D'AMARE, A. R. (2005). The Cbf5-Nop10 complex is a molecular bracket that organizes box H/ACA RNPs. Nature Structural and Molecular Biology 12, 1101-1107. (Pubitemid 41746781)
    • (2005) Nature Structural and Molecular Biology , vol.12 , Issue.12 , pp. 1101-1107
    • Hamma, T.1    Reichow, S.L.2    Varani, G.3    Ferre-D'Amare, A.R.4
  • 47
    • 0031799895 scopus 로고    scopus 로고
    • X-linked dyskeratosis congenita is caused by mutations in a highly conserved gene with putative nucleolar functions
    • DOI 10.1038/ng0598-32
    • HEISS, N.S., KNIGHT, S. W., VULLIAMY, T.J., KLAUCK, S. M., WIEMANN, S., MASON, P.J., POUSTKA, A. & DOKAL, I. (1998). X-linked dyskeratosis congenita is caused by mutations in a highly conserved gene with putative nucleolar functions. Nature Genetics 19, 32-38. (Pubitemid 28242019)
    • (1998) Nature Genetics , vol.19 , Issue.1 , pp. 32-38
    • Heiss, N.S.1    Knight, S.W.2    Vulliamy, T.J.3    Klauck, S.M.4    Wiemann, S.5    Mason, P.J.6    Poustka, A.7    Dokal, I.8
  • 49
    • 33748169778 scopus 로고    scopus 로고
    • A Spliceosomal Intron Binding Protein, IBP160, Links Position-Dependent Assembly of Intron-Encoded Box C/D snoRNP to Pre-mRNA Splicing
    • DOI 10.1016/j.molcel.2006.07.011, PII S1097276506004916
    • HIROSE, T., IDEUE, T., NAGAI, M., HAGIWARA, M., SHU, M. D. & STEITZ, J. A. (2006). A spliceosomal intron binding protein, IBP160, links position-dependent assembly of intron-encoded box C/D snoRNP to pre-mRNA splicing. Molecular Cell 23, 673-684. (Pubitemid 44308588)
    • (2006) Molecular Cell , vol.23 , Issue.5 , pp. 673-684
    • Hirose, T.1    Ideue, T.2    Nagai, M.3    Hagiwara, M.4    Shu, M.-D.5    Steitz, J.A.6
  • 50
    • 0043172414 scopus 로고    scopus 로고
    • Splicing-dependent and -independent modes of assembly for intron-encoded box C/D snoRNPs in mammalian cells
    • DOI 10.1016/S1097-2765(03)00267-3
    • HIROSE, T., SHU, M. D. & STEITZ, J. A. (2003). Splicing-dependent and -independent modes of assembly for intron-encoded box C/D snoRNPs in mammalian cells. Molecular Cell 12, 113-123. (Pubitemid 36945040)
    • (2003) Molecular Cell , vol.12 , Issue.1 , pp. 113-123
    • Hirose, T.1    Shu, M.-D.2    Steitz, J.A.3
  • 51
    • 0035818553 scopus 로고    scopus 로고
    • Position within the host intron is critical for efficient processing of box C/D snoRNAs in mammalian cells
    • DOI 10.1073/pnas.231490998
    • HIROSE, T. & STEITZ, J. A. (2001). Position within the host intron is critical for efficient processing of box C/D snoRNAs in mammalian cells. Proceedings of the National Academy of Sciences of the United States of America 98, 12914-12919. (Pubitemid 33051294)
    • (2001) Proceedings of the National Academy of Sciences of the United States of America , vol.98 , Issue.23 , pp. 12914-12919
    • Hirose, T.1    Steitz, J.A.2
  • 52
    • 33751013845 scopus 로고    scopus 로고
    • Crystal structure of pseudouridine synthase RluA: Indirect sequence readout through protein-induced RNA structure
    • DOI 10.1016/j.molcel.2006.09.017
    • HOANG, C., CHEN, J., VIZTHUM, C.A., KANDEL, J. M., HAMILTON, C. S., MUELLER, E. G. & FERRE-D'AMARE, A. R. (2006). Crystal structure of pseudouridine syn-thase RluA: indirect sequence readout through protein-induced RNA structure. Molecular Cell 24, 535-545. (Pubitemid 350284223)
    • (2006) Molecular Cell , vol.24 , Issue.4 , pp. 535-545
    • Hoang, C.1    Chen, J.2    Vizthum, C.A.3    Kandel, J.M.4    Hamilton, C.S.5    Mueller, E.G.6    Ferre-D'Amare, A.R.7
  • 53
    • 0035966271 scopus 로고    scopus 로고
    • Cocrystal structure of a tRNA Ψ55 pseudouridine synthase: Nucleotide flipping by an RNA-modifying enzyme
    • DOI 10.1016/S0092-8674(01)00618-3
    • HOANG, C. & FERRE-D'AMARE, A. R. (2001). Cocrystal structure of a tRNA Psi55 pseudouridine synthase: nucleotide flipping by an RNA-modifying enzyme. Cell 107, 929-939. (Pubitemid 34084983)
    • (2001) Cell , vol.107 , Issue.7 , pp. 929-939
    • Hoang, C.1    Ferre-D'Amare, A.R.2
  • 54
    • 23644435149 scopus 로고    scopus 로고
    • Precursor complex structure of pseudouridine synthase TruB suggests coupling of active site perturbations to an RNA-sequestering peripheral protein domain
    • DOI 10.1110/ps.051493605
    • HOANG, C., HAMILTON, C. S., MUELLER, E. G. & FERRE-D'AMARE, A. R. (2005). Precursor complex structure of pseudouridine synthase TruB suggests coupling of active site perturbations to an RNA-sequestering peripheral protein domain. Protein Science 14, 2201-2206. (Pubitemid 41132385)
    • (2005) Protein Science , vol.14 , Issue.8 , pp. 2201-2206
    • Hoang, C.1    Hamilton, C.S.2    Mueller, E.G.3    Ferre-D'Amare, A.R.4
  • 55
    • 0032488657 scopus 로고    scopus 로고
    • A conserved aspartate of tRNA pseudouridine synthase is essential for activity and a probable nucleophilic catalyst
    • DOI 10.1021/bi971874+
    • HUANG, L., POOKANJANATAVIP, M., GU, X. & SANTI, D. V. (1998). A conserved aspartate of tRNA pseudouridine synthase is essential for activity and a probable nucleo-philic catalyst. Biochemistry 37, 344-351. (Pubitemid 28049138)
    • (1998) Biochemistry , vol.37 , Issue.1 , pp. 344-351
    • Huang, L.1    Pookanjanatavip, M.2    Gu, X.3    Santi, D.V.4
  • 56
    • 34247199024 scopus 로고    scopus 로고
    • How U38, 39, and 40 of Many tRNAs Become the Targets for Pseudouridylation by TruA
    • DOI 10.1016/j.molcel.2007.02.027, PII S1097276507001451
    • HUR, S. & STROUD, R. M. (2007). How U38, 39, and 40 of many tRNAs become the targets for pseudouridylation by TruA. Molecular Cell 26, 189-203. (Pubitemid 46617334)
    • (2007) Molecular Cell , vol.26 , Issue.2 , pp. 189-203
    • Hur, S.1    Stroud, R.M.2
  • 57
    • 17944388104 scopus 로고    scopus 로고
    • Human telomerase RNA and box H/ACA scaRNAs share a common Cajal body-specific localization signal
    • DOI 10.1083/jcb.200310138
    • JADY, B. E., BERTRAND, E. & KISS, T. (2004). Human telomerase RNA and box H/ACA scaRNAs share a common Cajal body-specific localization signal. Journal of Cell Biology 164, 647-652. (Pubitemid 38282948)
    • (2004) Journal of Cell Biology , vol.164 , Issue.5 , pp. 647-652
    • Jady, B.E.1    Bertrand, E.2    Kiss, T.3
  • 58
    • 34247278771 scopus 로고    scopus 로고
    • Solution Structure of an rRNA Substrate Bound to the Pseudouridylation Pocket of a Box H/ACA snoRNA
    • DOI 10.1016/j.molcel.2007.03.014, PII S1097276507001840
    • JIN, H., LORIA, J. P. & MOORE, P. B. (2007). Solution structure of an rRNA substrate bound to the pseudouridylation pocket of a Box H/ACA snoRNA. Molecular Cell 26, 205-215. (Pubitemid 46617337)
    • (2007) Molecular Cell , vol.26 , Issue.2 , pp. 205-215
    • Jin, H.1    Loria, J.P.2    Moore, P.B.3
  • 59
    • 55749101781 scopus 로고    scopus 로고
    • Box C/D RNA-guided 2k-O-methylations and the in-tron of tRNATrp are not essential for the viability of Haloferax volcanii
    • JOARDAR, A., GURHA, P., SKARIAH, G. & GUPTA, R. (2008). Box C/D RNA-guided 2k-O-methylations and the in-tron of tRNATrp are not essential for the viability of Haloferax volcanii. Journal of Bacteriol 190, 7308-7313.
    • (2008) Journal of Bacteriol , vol.190 , pp. 7308-7313
    • Joardar, A.1    Gurha, P.2    Skariah, G.3    Gupta, R.4
  • 60
    • 0025276512 scopus 로고
    • The U3 small nucleolar ribonucleoprotein functions in the first step of preribosomal RNA processing
    • KASS, S., TYC, K., STEITZ, J. A. & SOLLNER-WEBB, B. (1990). The U3 small nucleolar ribonucleoprotein functions in the first step of preribosomal RNA processing. Cell 60, 897-908.
    • (1990) Cell , vol.60 , pp. 897-908
    • Kass, S.1    Tyc, K.2    Steitz, J.A.3    Sollner-Webb, B.4
  • 61
    • 0026524798 scopus 로고
    • Conformational rigidity of specific pyrimidine residues in tRNA arises from posttranscriptional modifications that enhance steric interaction between the base and the 2k-hydroxyl group
    • KAWAI, G., YAMAMOTO, Y., KAMIMURA, T., MASEGI, T., SEKINE, M., HATA, T., IIMORI, T., WATANABE, T., MIYAZAWA, T. & YOKOYAMA, S. (1992). Conformational rigidity of specific pyrimidine residues in tRNA arises from posttranscriptional modifications that enhance steric interaction between the base and the 2k-hydroxyl group. Biochemistry 31, 1040-1046.
    • (1992) Biochemistry , vol.31 , pp. 1040-1046
    • Kawai, G.1    Yamamoto, Y.2    Kamimura, T.3    Masegi, T.4    Sekine, M.5    Hata, T.6    Iimori, T.7    Watanabe, T.8    Miyazawa, T.9    Yokoyama, S.10
  • 62
    • 0034769951 scopus 로고    scopus 로고
    • A well-connected and conserved nucleoplasmic helicase is required for production of box C/D and H/ACA snoRNAs and localization of snoRNP proteins
    • DOI 10.1128/MCB.21.22.7731-7746.2001
    • KING, T. H., DECATUR, W. A., BERTRAND, E., MAXWELL, E. S. & FOURNIER, M. J. (2001). A well-connected and conserved nucleoplasmic helicase is required for production of box C/D and H/ACA snoRNAs and localization of snoRNP proteins. Molecular and Cellular Biology 21, 7731-7746. (Pubitemid 32988783)
    • (2001) Molecular and Cellular Biology , vol.21 , Issue.22 , pp. 7731-7746
    • King, T.H.1    Decatur, W.A.2    Bertrand, E.3    Maxwell, E.S.4    Fournier, M.J.5
  • 63
    • 0030604698 scopus 로고    scopus 로고
    • Site-specific ribose methylation of preribosomal RNA: A novel function for small nucleolar RNAs
    • DOI 10.1016/S0092-8674(00)81308-2
    • KISS-LASZLO, Z., HENRY, Y., BACHELLERIE, J.P., CAIZERGUES-FERRER, M. & KISS, T. (1996). Site-specific ribose methylation of preribosomal RNA: a novel function for small nucleolar RNAs. Cell 85, 1077-1088. (Pubitemid 26231174)
    • (1996) Cell , vol.85 , Issue.7 , pp. 1077-1088
    • Kiss-Laszlo, Z.1    Henry, Y.2    Bachellerie, J.-P.3    Caizergues-Ferrer, M.4    Kiss, T.5
  • 64
    • 0037133942 scopus 로고    scopus 로고
    • Small nucleolar RNAs: An abundant group of noncoding RNAs with diverse cellular functions
    • DOI 10.1016/S0092-8674(02)00718-3
    • KISS, T. (2002). Small nucleolar RNAs: an abundant group of noncoding RNAs with diverse cellular functions. Cell 109, 145-148. (Pubitemid 34518252)
    • (2002) Cell , vol.109 , Issue.2 , pp. 145-148
    • Kiss, T.1
  • 65
    • 33748431061 scopus 로고    scopus 로고
    • SnoRNP biogenesis meets Pre-mRNA splicing
    • DOI 10.1016/j.molcel.2006.08.023, PII S1097276506006058
    • KISS, T. (2006). SnoRNP biogenesis meets Pre-mRNA splicing. Molecular Cell 23, 775-776. (Pubitemid 44344525)
    • (2006) Molecular Cell , vol.23 , Issue.6 , pp. 775-776
    • Kiss, T.1
  • 68
    • 0027171750 scopus 로고
    • Small nucleolar RNAs encoded by introns of the human cell cycle regulatory gene RCC1
    • KISS, T. & FILIPOWICZ, W. (1993). Small nucleolar RNAs encoded by introns of the human cell cycle regulatory gene RCC1. EMBO Journal 12, 2913-2920. (Pubitemid 23218341)
    • (1993) EMBO Journal , vol.12 , Issue.7 , pp. 2913-2920
    • Kiss, T.1    Filipowicz, W.2
  • 69
    • 33845265038 scopus 로고    scopus 로고
    • Dynamic association and localization of human H/ACA RNP proteins
    • DOI 10.1261/rna.249306
    • KITTUR, N., DARZACQ, X., ROY, S., SINGER, R. H. & MEIER, U. T. (2006). Dynamic association and localization of human H/ACA RNP proteins. RNA 12, 2057-2062. (Pubitemid 44865953)
    • (2006) RNA , vol.12 , Issue.12 , pp. 2057-2062
    • Kittur, N.1    Darzacq, X.2    Roy, S.3    Singer, R.H.4    Meier, U.T.5
  • 70
    • 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, E. V. (1996). Pseudouridine synthases: four families of enzymes containing a putative uridine-binding motif also conserved in dUTPases and dCTP deaminases. Nucleic Acids Research 24, 2411-2415.
    • (1996) Nucleic Acids Research , vol.24 , pp. 2411-2415
    • Koonin, E.V.1
  • 73
    • 0033053360 scopus 로고    scopus 로고
    • Nop58p is a common component of the box C+D snoRNPs that is required for snoRNA stability
    • DOI 10.1017/S135583829998192X
    • LAFONTAINE, D. L. & TOLLERVEY, D. (1999). Nop58p is a common component of the box C+D snoRNPs that is required for snoRNA stability. RNA 5, 455-467. (Pubitemid 29125004)
    • (1999) RNA , vol.5 , Issue.3 , pp. 455-467
    • Lafontaine, D.L.J.1    Tollervey, D.2
  • 74
    • 0034126359 scopus 로고    scopus 로고
    • Synthesis and assembly of the box C+D small nucleolar RNPs
    • DOI 10.1128/MCB.20.8.2650-2659.2000
    • LAFONTAINE, D. L. & TOLLERVEY, D. (2000). Synthesis and assembly of the box C+D small nucleolar RNPs. Molecular and Cellular Biology 20, 2650-2659. (Pubitemid 30183483)
    • (2000) Molecular and Cellular Biology , vol.20 , Issue.8 , pp. 2650-2659
    • Lafontaine, D.L.J.1    Tollervey, D.2
  • 76
    • 34547559807 scopus 로고    scopus 로고
    • The Box H/ACA RNP Assembly Factor Naf1p Contains a Domain Homologous to Gar1p Mediating its Interaction with Cbf5p
    • DOI 10.1016/j.jmb.2007.06.031, PII S0022283607008224
    • LEULLIOT, N., GODIN, K.S., HOAREAU-AVEILLA, C., QUEVILLON-CHERUEL, S., VARANI, G., HENRY, Y. & VAN TILBEURGH, H. (2007). The Box H/ACA RNP assembly factor Naf1p contains a domain homologous to Gar1p mediating its interaction with Cbf5p. Journal of Molecular Biology 371, 1338-1353. (Pubitemid 47198265)
    • (2007) Journal of Molecular Biology , vol.371 , Issue.5 , pp. 1338-1353
    • Leulliot, N.1    Godin, K.S.2    Hoareau-Aveilla, C.3    Quevillon-Cheruel, S.4    Varani, G.5    Henry, Y.6    Van Tilbeurgh, H.7
  • 77
    • 33748947672 scopus 로고    scopus 로고
    • Crystal structure of an H/ACA box ribonucleoprotein particle
    • LI, L. & YE, K. (2006). Crystal structure of an H/ACA box ribonucleoprotein particle. Nature 443, 302-307.
    • (2006) Nature , vol.443 , pp. 302-307
    • L, L.I.1    K, Y.E.2
  • 78
    • 52949118507 scopus 로고    scopus 로고
    • Long-distance placement of substrate RNA by H/ACA proteins
    • LIANG, B., KAHEN, E. J., CALVIN, K., ZHOU, J., BLANCO, M. & LI, H. (2008). Long-distance placement of substrate RNA by H/ACA proteins. RNA 14, 2086-2094.
    • (2008) RNA , vol.14 , pp. 2086-2094
    • Liang, B.1    Kahen, E.J.2    Calvin, K.3    Zhou, J.4    Blanco, M.5    H, L.I.6
  • 79
    • 36849034965 scopus 로고    scopus 로고
    • Substrate RNA positioning in the archaeal H/ACA ribonucleoprotein complex
    • DOI 10.1038/nsmb1336, PII NSMB1336
    • LIANG, B., XUE, S., TERNS, R. M., TERNS, M. P. & LI, H. (2007a). Substrate RNA positioning in the archaeal H/ACA ribonucleoprotein complex. Nature Structural and Molecular Biology 14, 1189-1195. (Pubitemid 350223336)
    • (2007) Nature Structural and Molecular Biology , vol.14 , Issue.12 , pp. 1189-1195
    • Liang, B.1    Xue, S.2    Terns, R.M.3    Terns, M.P.4    Li, H.5
  • 81
    • 0028818298 scopus 로고
    • U14 base-pairs with 18S rRNA: A novel snoRNA interaction required for rRNA processing
    • LIANG, W. Q. & FOURNIER, M. J. (1995). U14 base-pairs with 18S rRNA: a novel snoRNA interaction required for rRNA processing. Genes and Development 9, 2433-2443.
    • (1995) Genes and Development , vol.9 , pp. 2433-2443
    • Liang, W.Q.1    Fournier, M.J.2
  • 82
    • 37349128219 scopus 로고    scopus 로고
    • rRNA modifications in an intersubunit bridge of the ribosome strongly affect both ribosome biogenesis and activity
    • DOI 10.1016/j.molcel.2007.10.012, PII S1097276507006946
    • LIANG, X. H., LIU, Q. & FOURNIER, M. J. (2007b). rRNA modifications in an intersubunit bridge of the ribosome strongly affect both ribosome biogenesis and activity. Molecular Cell 28, 965-977. (Pubitemid 350297021)
    • (2007) Molecular Cell , vol.28 , Issue.6 , pp. 965-977
    • Liang, X.-h.1    Liu, Q.2    Fournier, M.J.3
  • 83
    • 69049089806 scopus 로고    scopus 로고
    • Loss of rRNA modifications in the decoding center of the ribosome impairs translation and strongly delays pre-rRNA processing
    • LIANG, X. H., LIU, Q. & FOURNIER, M. J. (2009b). Loss of rRNA modifications in the decoding center of the ribosome impairs translation and strongly delays pre-rRNA processing. RNA 15, 1716-1728.
    • (2009) RNA , vol.15 , pp. 1716-1728
    • Liang, X.H.1    Liu, Q.2    Fournier, M.J.3
  • 84
    • 57349109265 scopus 로고    scopus 로고
    • Mis-targeted methylation in rRNA can severely impair ribosome synthesis and activity
    • LIU, B., LIANG, X. H., PIEKNA-PRZYBYLSKA, D., LIU, Q. & FOURNIER, M. J. (2008). Mis-targeted methylation in rRNA can severely impair ribosome synthesis and activity. RNA Biology 5, 249-254.
    • (2008) RNA Biology , vol.5 , pp. 249-254
    • Liu, B.1    Liang, X.H.2    Piekna-Przybylska, D.3    Liu, Q.4    Fournier, M.J.5
  • 85
    • 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
    • DOI 10.1093/nar/gkj482
    • MANIVAL, X., CHARRON, C., FOURMANN, J. B., GODARD, F., CHARPENTIER, B. & BRANLANT, C. (2006). 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 Research 34, 826-839. (Pubitemid 43380668)
    • (2006) Nucleic Acids Research , vol.34 , Issue.3 , pp. 826-839
    • Manival, X.1    Charron, C.2    Fourmann, J.-B.3    Godard, F.4    Charpentier, B.5    Branlant, C.6
  • 87
    • 19444383162 scopus 로고    scopus 로고
    • Dyskeratosis congenita: Telomerase, telomeres and anticipation
    • DOI 10.1016/j.gde.2005.04.004, PII S0959437X05000560
    • MARRONE, A., WALNE, A. & DOKAL, I. (2005). Dyskeratosis congenita: telomerase, telomeres and anticipation. Current Opinion in Genetics and Development 15, 249-257. (Pubitemid 40726047)
    • (2005) Current Opinion in Genetics and Development , vol.15 , Issue.3 SPEC. ISS. , pp. 249-257
    • Marrone, A.1    Walne, A.2    Dokal, I.3
  • 88
    • 0036917889 scopus 로고    scopus 로고
    • SAM (dependent) I AM: The S-adenosylmethionine-dependent methyltransferase fold
    • DOI 10.1016/S0959-440X(02)00391-3
    • MARTIN, J. L. & MCMILLAN, F. M. (2002). SAM (dependent) I AM: the S-adenosylmethionine-dependent methyl-transferase fold. Current Opinion in Structural Biology 12, 783-793. (Pubitemid 36009496)
    • (2002) Current Opinion in Structural Biology , vol.12 , Issue.6 , pp. 783-793
    • Martin, J.L.1    McMillan, F.M.2
  • 89
    • 33847187076 scopus 로고    scopus 로고
    • Non-coding RNAs: Lessons from the small nuclear and small nucleolar RNAs
    • MATERA, A. G., TERNS, R. M. & TERNS, M. P. (2007). Non-coding RNAs: lessons from the small nuclear and small nucleolar RNAs. Nature Reviews 8, 209-220.
    • (2007) Nature Reviews , vol.8 , pp. 209-220
    • Matera, A.G.1    Terns, R.M.2    Terns, M.P.3
  • 91
    • 35148886286 scopus 로고    scopus 로고
    • Crystal structure of human Pus10, a novel pseudouridine synthase
    • DOI 10.1016/j.jmb.2007.08.053, PII S0022283607011345
    • MCCLEVERTY, C.J., HORNSBY, M., SPRAGGON, G. & KREUSCH, A. (2007). Crystal structure of human Pus10, a novel pseudouridine synthase. Journal of Molecular Biology 373, 1243-1254. (Pubitemid 47539484)
    • (2007) Journal of Molecular Biology , vol.373 , Issue.5 , pp. 1243-1254
    • McCleverty, C.J.1    Hornsby, M.2    Spraggon, G.3    Kreusch, A.4
  • 92
    • 19444374397 scopus 로고    scopus 로고
    • The many facets of H/ACA ribonu-cleoproteins
    • MEIER, U. T. (2005). The many facets of H/ACA ribonu-cleoproteins. Chromosoma 114, 1-14.
    • (2005) Chromosoma , vol.114 , pp. 1-14
    • Meier, U.T.1
  • 93
    • 0032961170 scopus 로고    scopus 로고
    • A box H/ACA small nucleolar RNA-like domain at the human telomerase RNA 3' end
    • MITCHELL, J. R., CHENG, J. & COLLINS, K. (1999a). A box H/ACA small nucleolar RNA-like domain at the human telomerase RNA 3k end. Molecular and Cellular Biology 19, 567-576. (Pubitemid 29018458)
    • (1999) Molecular and Cellular Biology , vol.19 , Issue.1 , pp. 567-576
    • Mitchell, J.R.1    Cheng, J.2    Collins, K.3
  • 94
    • 0033518188 scopus 로고    scopus 로고
    • A tel-omerase component is defective in the human disease dyskeratosis congenita
    • MITCHELL, J. R., WOOD, E. & COLLINS, K. (1999b). A tel-omerase component is defective in the human disease dyskeratosis congenita. Nature 402, 551-555.
    • (1999) Nature , vol.402 , pp. 551-555
    • Mitchell, J.R.1    Wood, E.2    Collins, K.3
  • 95
    • 3242656131 scopus 로고    scopus 로고
    • Mouse dyskerin mutations affect accumulation of telomerase RNA and small nucleolar RNA, telomerase activity, and ribosomal RNA processing
    • DOI 10.1073/pnas.0402560101
    • MOCHIZUKI, Y., HE, J., KULKARNI, S., BESSLER, M. & MASON, P. J. (2004). Mouse dyskerin mutations affect accumulation of telomerase RNA and small nucleolar RNA, telomerase activity, and ribosomal RNA processing. Proceedings of the National Academy of Sciences of the United States of America 101, 10756-10761. (Pubitemid 38955815)
    • (2004) Proceedings of the National Academy of Sciences of the United States of America , vol.101 , Issue.29 , pp. 10756-10761
    • Mochizuki, Y.1    He, J.2    Kulkarni, S.3    Bessler, M.4    Mason, P.J.5
  • 96
    • 2342475659 scopus 로고    scopus 로고
    • Molecular basis of box C/D RNA-protein interactions: Cocrystal structure of archaeal L7Ae and a box C/D RNA
    • DOI 10.1016/j.str.2004.02.033, PII S0969212604001169
    • MOORE, T., ZHANG, Y., FENLEY, M. O. & LI, H. (2004). Molecular basis of box C/D RNA-protein interactions; cocrystal structure of archaeal L7Ae and a box C/D RNA. Structure (Cambridge) 12, 807-818. (Pubitemid 38595769)
    • (2004) Structure , vol.12 , Issue.5 , pp. 807-818
    • Moore, T.1    Zhang, Y.2    Fenley, M.O.3    Li, H.4
  • 97
    • 0038708223 scopus 로고    scopus 로고
    • Crystal structure of the avilamycin resistance-conferring methyltransferase AviRa from Streptomyces viridochromogenes
    • DOI 10.1016/S0022-2836(03)00407-8
    • MOSBACHER, T.G., BECHTHOLD, A. & SCHULZ, G.E. (2003). Crystal structure of the avilamycin resistance-conferring methyltransferase AviRa from Streptomyces viridochromogenes. Journal of Molecular Biology 329, 147-157. (Pubitemid 36555172)
    • (2003) Journal of Molecular Biology , vol.329 , Issue.1 , pp. 147-157
    • Mosbacher, T.G.1    Bechthold, A.2    Schulz, G.E.3
  • 98
    • 34548707914 scopus 로고    scopus 로고
    • Identification of determinants in the protein partners aCBF5 and aNOP10 necessary for the tRNA: Ψ55-synthase and RNA-guided RNA:Ψ-synthase activities
    • DOI 10.1093/nar/gkm606
    • MULLER, S., FOURMANN, J. B., LOEGLER, C., CHARPENTIER, B. & BRANLANT, C. (2007). Identification of determinants in the protein partners aCBF5 and aNOP10 necessary for the tRNA:{Psi}55-synthase and RNA-guided RNA:{Psi}-synthase activities. Nucleic Acids Research 35, 5610-5624. (Pubitemid 47423931)
    • (2007) Nucleic Acids Research , vol.35 , Issue.16 , pp. 5610-5624
    • Muller, S.1    Fourmann, J.-B.2    Loegler, C.3    Charpentier, B.4    Branlant, C.5
  • 100
    • 0034081813 scopus 로고    scopus 로고
    • Box C/D snoRNA-associated proteins: Two pairs of evolutionarily ancient proteins and possible links to replication and transcription
    • DOI 10.1017/S1355838200992446
    • NEWMAN, D. R., KUHN, J. F., SHANAB, G. M. & MAXWELL, E. S. (2000). Box C/D snoRNA-associated proteins: two pairs of evolutionarily ancient proteins and possible links to replication and transcription. RNA 6, 861-879. (Pubitemid 30396027)
    • (2000) RNA , vol.6 , Issue.6 , pp. 861-879
    • Newman, D.R.1    Kuhn, J.F.2    Shanab, G.M.3    Maxwell, E.S.4
  • 101
    • 0242469008 scopus 로고    scopus 로고
    • Fibrillarin Is Essential for Early Development and Required for Accumulation of an Intron-Encoded Small Nucleolar RNA in the Mouse
    • DOI 10.1128/MCB.23.23.8519-8527.2003
    • NEWTON, K., PETFALSKI, E., TOLLERVEY, D. & CACERES, J. F. (2003). Fibrillarin is essential for early development and required for accumulation of an intron-encoded small nucleolar RNA in the mouse. Molecular and Cellular Biology 23, 8519-8527. (Pubitemid 37433359)
    • (2003) Molecular and Cellular Biology , vol.23 , Issue.23 , pp. 8519-8527
    • Newton, K.1    Petfalski, E.2    Tollervey, D.3    Caceres, J.F.4
  • 103
    • 0034697257 scopus 로고    scopus 로고
    • Homologs of small nucleolar RNAs in Archaea
    • DOI 10.1126/science.288.5465.517
    • OMER, A. D., LOWE, T. M., RUSSELL, A. G., EBHARDT, H., EDDY, S. R. & DENNIS, P. P. (2000). Homologs of small nucleolar RNAs in archaea. Science 288, 517-522. (Pubitemid 30236034)
    • (2000) Science , vol.288 , Issue.5465 , pp. 517-522
    • Omer, A.D.1    Lowe, T.M.2    Russell, A.C.3    Ebhardt, H.4    Eddy, S.R.5    Dennis, P.P.6
  • 106
    • 20544468675 scopus 로고    scopus 로고
    • Structural comparison of yeast snoRNP and spliceosomal protein Snu13p with its homologs
    • DOI 10.1016/j.bbrc.2005.05.141, PII S0006291X05010776
    • ORUGANTI, S., ZHANG, Y. & LI, H. (2005). Structural comparison of yeast snoRNP and spliceosomal protein Snu13p with its homologs. Biochemical and Biophysical Research Communications 333, 550-554. (Pubitemid 40848326)
    • (2005) Biochemical and Biophysical Research Communications , vol.333 , Issue.2 , pp. 550-554
    • Oruganti, S.V.1    Zhang, Y.2    Li, H.3
  • 107
    • 34547586356 scopus 로고    scopus 로고
    • Alternative conformations of the archaeal Nop56/58-fibrillarin complex imply flexibility in box C/D RNPs
    • DOI 10.1016/j.jmb.2007.06.029, PII S0022283607008273
    • ORUGANTI, S., ZHANG, Y., LI, H., ROBINSON, H., TERNS, M. P., TERNS, R.M., YANG, W. & LI, H. (2007). Alternative conformations of the archaeal Nop56/58-fibrillarin complex imply flexibility in box C/D RNPs. Journal of Molecular Biology 371, 1141-1150. (Pubitemid 47198266)
    • (2007) Journal of Molecular Biology , vol.371 , Issue.5 , pp. 1141-1150
    • Oruganti, S.1    Zhang, Y.2    Li, H.3    Robinson, H.4    Terns, M.P.5    Terns, R.M.6    Yang, W.7    Li, H.8
  • 108
    • 0242331664 scopus 로고    scopus 로고
    • Structure of tRNA pseudouridine synthase TruB and its RNA complex: RNA recognition through a combination of rigid docking and induced fit
    • DOI 10.1073/pnas.2135585100
    • PAN, H., AGARWALLA, S., MOUSTAKAS, D. T., FINER-MOORE, J. & STROUD, R. M. (2003). Structure of tRNA pseu-douridine synthase TruB and its RNA complex: RNA recognition through a combination of rigid docking and induced fit. Proceedings of the National Academy Sciences of the United States of America 100, 12648-12653. (Pubitemid 37339953)
    • (2003) Proceedings of the National Academy of Sciences of the United States of America , vol.100 , Issue.22 , pp. 12648-12653
    • Pan, H.1    Agarwalla, S.2    Moustakas, D.T.3    Finer-Moore, J.4    Stroud, R.M.5
  • 109
    • 0027213118 scopus 로고
    • Disruption of U8 nucleolar snRNA inhibits 5.8S and 28S rRNA processing in the Xenopus oocyte
    • DOI 10.1016/0092-8674(93)90651-6
    • PECULIS, B. A. & STEITZ, J. A. (1993). Disruption of U8 nucleolar snRNA inhibits 5.8S and 28S rRNA processing in the Xenopus oocyte. Cell 73, 1233-1245. (Pubitemid 23180496)
    • (1993) Cell , vol.73 , Issue.6 , pp. 1233-1245
    • Peculis, B.A.1    Steitz, J.A.2
  • 110
    • 34748912322 scopus 로고    scopus 로고
    • The PUA domain - A structural and functional overview
    • DOI 10.1111/j.1742-4658.2007.06031.x
    • PEREZ-ARELLANO, I., GALLEGO, J. & CERVERA, J. (2007). The PUA domain - a structural and functional overview. FEBS Journal 274, 4972-4984. (Pubitemid 47481183)
    • (2007) FEBS Journal , vol.274 , Issue.19 , pp. 4972-4984
    • Perez-Arellano, I.1    Gallego, J.2    Cervera, J.3
  • 111
    • 34547163927 scopus 로고    scopus 로고
    • The 90S preribosome is a multimodular structure that is assembled through a hierarchical mechanism
    • DOI 10.1128/MCB.00380-07
    • PEREZ-FERNANDEZ, J., ROMAN, A., DE LAS RIVAS, J., BUSTELO, X. R. & DOSIL, M. (2007). The 90S preribo-some is a multimodular structure that is assembled through a hierarchical mechanism. Molecular and Cellular Biology 27, 5414-5429. (Pubitemid 47124395)
    • (2007) Molecular and Cellular Biology , vol.27 , Issue.15 , pp. 5414-5429
    • Perez-Fernandez, J.1    Roman, A.2    De Las Rivas, J.3    Bustelo, X.R.4    Dosil, M.5
  • 112
    • 28244473650 scopus 로고    scopus 로고
    • Dissecting the roles of a strictly conserved tyrosine in substrate recognition and catalysis by pseudouridine 55 synthase
    • DOI 10.1021/bi050961w
    • PHANNACHET, K., ELIAS, Y. & HUANG, R. H. (2005). Dissecting the roles of a strictly conserved tyrosine in substrate recognition and catalysis by pseudouridine 55 synthase. Biochemistry 44, 15488-15494. (Pubitemid 41706132)
    • (2005) Biochemistry , vol.44 , Issue.47 , pp. 15488-15494
    • Phannachet, K.1    Elias, Y.2    Huang, R.H.3
  • 115
    • 0141869105 scopus 로고    scopus 로고
    • Functional requirement for symmetric assembly of archaeal box C/D small ribonucleoprotein particles
    • DOI 10.1016/j.jmb.2003.08.012
    • RASHID, R., AITTALEB, M., CHEN, Q., SPIEGEL, K., DEMELER, B. & LI, H. (2003). Functional requirement for symmetric assembly of archaeal box C/D small ribonu-cleoprotein particles. Journal of Molecular Biology 333, 295-306. (Pubitemid 37188573)
    • (2003) Journal of Molecular Biology , vol.333 , Issue.2 , pp. 295-306
    • Rashid, R.1    Aittaleb, M.2    Chen, Q.3    Spiegel, K.4    Demeler, B.5    Li, H.6
  • 116
    • 30744445688 scopus 로고    scopus 로고
    • Crystal structure of a Cbf5-Nop10-Gar1 complex and implications in RNA-guided pseudouridylation and dyskeratosis congenita
    • DOI 10.1016/j.molcel.2005.11.017, PII S1097276505018046
    • RASHID, R., LIANG, B., BAKER, D. L., YOUSSEF, O. A., HE, Y., PHIPPS, K., TERNS, R.M., TERNS, M. P. & LI, H. (2006). Crystal structure of a Cbf5-Nop10-Gar1 complex and implications in RNA-guided pseudouridylation and dyskeratosis congenita. Molecular Cell 21, 249-260. (Pubitemid 43099940)
    • (2006) Molecular Cell , vol.21 , Issue.2 , pp. 249-260
    • Rashid, R.1    Liang, B.2    Baker, D.L.3    Youssef, O.A.4    He, Y.5    Phipps, K.6    Terns, R.M.7    Terns, M.P.8    Li, H.9
  • 117
    • 0019792769 scopus 로고
    • Characterization and subcellular localization of 7-8 S RNAs of Novikoff hepatoma
    • REDDY, R., LI, W. Y., HENNING, D., CHOI, Y. C., NOHGA, K. & BUSCH, H. (1981). Characterization and subcellular localization of 7-8 S RNAs of Novikoff hepatoma. Journal of Biological Chemistry 256, 8452-8457. (Pubitemid 12254794)
    • (1981) Journal of Biological Chemistry , vol.256 , Issue.16 , pp. 8452-8457
    • Reddy, R.1    Li, W.Y.2    Henning, D.3
  • 118
    • 33645296102 scopus 로고    scopus 로고
    • Cotranscriptional recognition of human intronic box H/ACA snoRNAs occurs in a splicing-independent manner
    • RICHARD, P., KISS, A. M., DARZACQ, X. & KISS, T. (2006). Cotranscriptional recognition of human intronic box H/ACA snoRNAs occurs in a splicing-independent manner. Molecular and Cellular Biology 26, 2540-2549.
    • (2006) Molecular and Cellular Biology , vol.26 , pp. 2540-2549
    • Richard, P.1    Kiss, A.M.2    Darzacq, X.3    Kiss, T.4
  • 119
    • 0037324527 scopus 로고    scopus 로고
    • Binding of L7Ae protein to the K-turn of archaeal snoRNAs: A shared RNA binding motif for C/D and H/ACA box snoRNAs in Archaea
    • DOI 10.1093/nar/gkg175
    • ROZHDESTVENSKY, T. S., TANG, T. H., TCHIRKOVA, I. V., BROSIUS, J., BACHELLERIE, J.P. & HUTTENHOFER, A. (2003). Binding of L7Ae protein to the K-turn of archaeal snoRNAs: a shared RNA binding motif for C/D and H/ACA box snoRNAs in archaea. Nucleic Acids Research 31, 869-877. (Pubitemid 36240424)
    • (2003) Nucleic Acids Research , vol.31 , Issue.3 , pp. 869-877
    • Rozhdestvensky, T.S.1    Tang, T.H.2    Tchirkova, I.V.3    Brosius, J.4    Bachellerie, J.-P.5    Huttenhofer, A.6
  • 120
    • 0141670243 scopus 로고    scopus 로고
    • Mechanistic studies of RNA modifying enzymes. RNA pseudouridine synthase and m5cytosine methyl transferase
    • SANTI, D. V. (2000). Mechanistic studies of RNA modifying enzymes. RNA pseudouridine synthase and m5cytosine methyl transferase. Nucleic Acids Symposium Series 44, 147-148.
    • (2000) Nucleic Acids Symposium Series , vol.44 , pp. 147-148
    • Santi, D.V.1
  • 121
    • 29844435528 scopus 로고    scopus 로고
    • A computational screen for mammalian pseudouridylation guide H/ACA RNAs
    • DOI 10.1261/rna.2210406
    • SCHATTNER, P., BARBERAN-SOLER, S. & LOWE, T. M. (2006). A computational screen for mammalian pseudouridyla-tion guide H/ACA RNAs. Rna 12, 15-25. (Pubitemid 43037449)
    • (2006) RNA , vol.12 , Issue.1 , pp. 15-25
    • Schattner, P.1    Barberan-Soler, S.2    Lowe, T.M.3
  • 122
    • 0038374971 scopus 로고    scopus 로고
    • Many paths to methyltransfer: A chronicle of convergence
    • DOI 10.1016/S0968-0004(03)00090-2
    • SCHUBERT, H. L., BLUMENTHAL, R. M. & CHENG, X. (2003). Many paths to methyltransfer: a chronicle of convergence. Trends in Biochemical Sciences 28, 329-335. (Pubitemid 36776296)
    • (2003) Trends in Biochemical Sciences , vol.28 , Issue.6 , pp. 329-335
    • Schubert, H.L.1    Blumenthal, R.M.2    Cheng, X.3
  • 123
    • 59449098081 scopus 로고    scopus 로고
    • Structure and functional studies of the CS domain of the essential H/ACA ribonucleoparticle assembly protein SHQ1
    • SINGH, M., GONZALES, F. A., CASCIO, D., HECKMANN, N., CHANFREAU, G. & FEIGON, J. (2009). Structure and functional studies of the CS domain of the essential H/ACA ribonucleoparticle assembly protein SHQ1. Journal of Biological Chemistry 284, 1906-1916.
    • (2009) Journal of Biological Chemistry , vol.284 , pp. 1906-1916
    • Singh, M.1    Gonzales, F.A.2    Cascio, D.3    Heckmann, N.4    Chanfreau, G.5    Feigon, J.6
  • 124
    • 45749152098 scopus 로고    scopus 로고
    • Dynamic guide-target interactions contribute to sequential 2′-O-methylation by a unique archaeal dual guide box C/D sRNP
    • DOI 10.1261/rna.1003308
    • SINGH, S. K., GURHA, P. & GUPTA, R. (2008). Dynamic guide-target interactions contribute to sequential 2'-O-methylation by a unique archaeal dual guide box C/D sRNP. RNA 14, 1411-1423. (Pubitemid 351872197)
    • (2008) RNA , vol.14 , Issue.7 , pp. 1411-1423
    • Singh, S.K.1    Gurha, P.2    Gupta, R.3
  • 126
    • 22244460838 scopus 로고    scopus 로고
    • The crystal structure of the Methanocaldococcus jannaschii multifunctional L7Ae RNA-binding protein reveals an induced-fit interaction with the box C/D RNAs
    • DOI 10.1021/bi050568q
    • SURYADI, J., TRAN, E. J., MAXWELL, E. S. & BROWN, II, B. A. (2005). The Crystal Structure of the Methanocaldococcus jannaschii multifunctional L7Ae RNA-binding protein reveals an induced-fit interaction with the Box C/D RNAs(,). Biochemistry 44, 9657-9672. (Pubitemid 40994360)
    • (2005) Biochemistry , vol.44 , Issue.28 , pp. 9657-9672
    • Suryadi, J.1    Tran, E.J.2    Maxwell, E.S.3    Brown II, B.A.4
  • 128
    • 0030963268 scopus 로고    scopus 로고
    • Function and synthesis of small nucleolar RNAs
    • DOI 10.1016/S0955-0674(97)80005-1
    • TOLLERVEY, D. & KISS, T. (1997). Function and synthesis of small nucleolar RNAs. Current Opinion in Cell Biology 9, 337-342. (Pubitemid 27263174)
    • (1997) Current Opinion in Cell Biology , vol.9 , Issue.3 , pp. 337-342
    • Tollervey, D.1    Kiss, T.2
  • 129
    • 13944251291 scopus 로고    scopus 로고
    • Conserved spacing between the box C/D and C′/D′ RNPs of the archaeal box C/D sRNP complex is required for efficient 2′-O-methylation of target RNAs
    • DOI 10.1261/rna.7223405
    • TRAN, E., ZHANG, X., LACKEY, L. & MAXWELL, E. S. (2005). Conserved spacing between the box C/D and 'C'/'D' RNPs of the archaeal box C/D sRNP complex is required for efficient 2'-O-methylation of target RNAs. RNA 11, 285-293. (Pubitemid 40270821)
    • (2005) RNA , vol.11 , Issue.3 , pp. 285-293
    • Tran, E.1    Zhang, X.2    Lackey, L.3    Maxwell, E.S.4
  • 130
    • 0043026864 scopus 로고    scopus 로고
    • Efficient RNA 2′-O-methylation requires juxtaposed and symmetrically assembled archaeal box C/D and C′/D′ RNPs
    • DOI 10.1093/emboj/cdg368
    • TRAN, E. J., ZHANG, X. & MAXWELL, E. S. (2003). Efficient RNA 2'-O-methylation requires juxtaposed and symmetrically assembled archaeal box C/D and 'C'/" RNPs. EMBO Journal 22, 3930-3940. (Pubitemid 36975719)
    • (2003) EMBO Journal , vol.22 , Issue.15 , pp. 3930-3940
    • Tran, E.J.1    Zhang, X.2    Maxwell, E.S.3
  • 131
    • 0024394168 scopus 로고
    • U3, U8 and U13 comprise a new class of mammalian snRNPs localized in the cell nucleolus
    • TYC, K. & STEITZ, J. A. (1989). U3, U8 and U13 comprise a new class of mammalian snRNPs localized in the cell nucleolus. EMBO Journal8, 3113-3119. (Pubitemid 19275012)
    • (1989) EMBO Journal , vol.8 , Issue.10 , pp. 3113-3119
    • Tyc, K.1    Steitz, J.A.2
  • 132
    • 63649111958 scopus 로고    scopus 로고
    • A conserved WD40 protein binds the Cajal body localization signal of scaRNP particles
    • TYCOWSKI, K. T., SHU, M. D., KUKOYI, A. & STEITZ, J. A. (2009). A conserved WD40 protein binds the Cajal body localization signal of scaRNP particles. Molecular Cell34, 47-57.
    • (2009) Molecular Cell , vol.34 , pp. 47-57
    • Tycowski, K.T.1    Shu, M.D.2    Kukoyi, A.3    Steitz, J.A.4
  • 134
    • 40749135820 scopus 로고    scopus 로고
    • Identification of ATPases pontin and reptin as telomerase components essential for holoenzyme assembly
    • DOI 10.1016/j.cell.2008.01.019, PII S0092867408001190
    • VENTEICHER, A. S., MENG, Z., MASON, P. J., VEENSTRA, T. D. & ARTANDI, S. E. (2008). Identification of ATPases pontin and reptin as telomerase components essential for holoenzyme assembly. Cell 132, 945-957. (Pubitemid 351381739)
    • (2008) Cell , vol.132 , Issue.6 , pp. 945-957
    • Venteicher, A.S.1    Meng, Z.2    Mason, P.J.3    Veenstra, T.D.4    Artandi, S.E.5
  • 135
    • 0034509631 scopus 로고    scopus 로고
    • Crystal structure of the spliceosomal 15.5kD protein bound to a U4 snRNA
    • DOI 10.1016/S1097-2765(00)00131-3
    • VIDOVIC, I., NOTTROTT, S., HARTMUTH, K., LUHRMANN, R. & FICNER, R. (2000). Crystal structure of the spliceoso-mal 15-5 kD protein bound to a U4 snRNA fragment. Molecular Cell 6, 1331-1342. (Pubitemid 32045926)
    • (2000) Molecular Cell , vol.6 , Issue.6 , pp. 1331-1342
    • Vidovic, I.1    Nottrott, S.2    Hartmuth, K.3    Luhrmann, R.4    Ficner, R.5
  • 137
    • 38849204872 scopus 로고    scopus 로고
    • Dyskeratosis Congenita: A historical perspective
    • DOI 10.1016/j.mad.2007.10.006, PII S0047637407001674
    • WALNE, A. J. & DOKAL, I. (2008). Dyskeratosis congenita: a historical perspective. Mechanisms of Ageing and Development 129, 48-59. (Pubitemid 351199862)
    • (2008) Mechanisms of Ageing and Development , vol.129 , Issue.1-2 , pp. 48-59
    • Walne, A.J.1    Dokal, I.2
  • 138
    • 2442542173 scopus 로고    scopus 로고
    • Architecture and assembly of mammalian H/ACA small nucleolar and telomerase ribonucleoproteins
    • DOI 10.1038/sj.emboj.7600181
    • WANG, C. & MEIER, U. T. (2004). Architecture and assembly of mammalian H/ACA small nucleolar and tel-omerase ribonucleoproteins. EMBO Journal 23, 1857-1867. (Pubitemid 38649648)
    • (2004) EMBO Journal , vol.23 , Issue.8 , pp. 1857-1867
    • Wang, C.1    Meier, U.T.2
  • 139
    • 0031788801 scopus 로고    scopus 로고
    • Cbf5p, a potential pseudouridine synthase, and Nhp2p, a putative RNA- binding protein, are present together with Gar1p in all H BOX/ACA-motif snoRNPs and constitute a common bipartite structure
    • DOI 10.1017/S1355838298980761
    • WATKINS, N. J., GOTTSCHALK, A., NEUBAUER, G., KASTNER, B., FABRIZIO, P., MANN, M. & LUHRMANN, R. (1998). Cbf5p, a potential pseudouridine synthase, and Nhp2p, a putative RNA-binding protein, are present together with Gar1p in all H BOX/ACA-motif snoRNPs and constitute a common bipartite structure. RNA 4, 1549-1568. (Pubitemid 28555217)
    • (1998) RNA , vol.4 , Issue.12 , pp. 1549-1568
    • Watkins, N.J.1    Gottschalk, A.2    Neubauer, G.3    Kastner, B.4    Fabrizio, P.5    Mann, M.6    Luhrmann, R.7
  • 141
    • 0033153297 scopus 로고    scopus 로고
    • Guided tours: From precursor snoRNA to functional snoRNP
    • DOI 10.1016/S0955-0674(99)80053-2
    • WEINSTEIN, L. B. & STEITZ, J. A. (1999). Guided tours: from precursor snoRNA to functional snoRNP. Current Opinion in Cell Biology 11, 378-384. (Pubitemid 29273810)
    • (1999) Current Opinion in Cell Biology , vol.11 , Issue.3 , pp. 378-384
    • Weinstein, L.B.1    Steitz, J.A.2
  • 142
    • 34249859415 scopus 로고    scopus 로고
    • H/ACA small nucleolar RNA pseudouridylation pockets bind substrate RNA to form three-way junctions that position the target U for modification
    • DOI 10.1073/pnas.0701534104
    • WU, H. & FEIGON, J. (2007). H/ACA small nucleolar RNA pseudouridylation pockets bind substrate RNA to form three-way junctions that position the target U for modification. Proceedings of the National Academy of Sciences of the United States of America 104, 6655-6660. (Pubitemid 47175556)
    • (2007) Proceedings of the National Academy of Sciences of the United States of America , vol.104 , Issue.16 , pp. 6655-6660
    • Wu, H.1    Feigon, J.2
  • 143
    • 0032569025 scopus 로고    scopus 로고
    • Nop5p is a small nucleolar ribonucleoprotein component required for pre- 18 S rRNA processing in yeast
    • DOI 10.1074/jbc.273.26.16453
    • WU, P., BROCKENBROUGH, J. S., METCALFE, A. C., CHEN, S. & ARIS, J. P. (1998). Nop5p is a small nucleolar ribo-nucleoprotein component required for pre-18S rRNA processing in yeast. Journal of Biological Chemistry 273, 16453-16463. (Pubitemid 28311428)
    • (1998) Journal of Biological Chemistry , vol.273 , Issue.26 , pp. 16453-16463
    • Wu, P.1    Brockenbrough, J.S.2    Metcalfe, A.C.3    Chen, S.4    Aris, J.P.5
  • 144
    • 77956912854 scopus 로고    scopus 로고
    • Structural basis for substrate placement by an archaeal box C/D ribonucleoprotein particle
    • XUE, S., WANG, R., YANG, F., TERNS, R. M., TERNS, M. P., ZHANG, X., MAXWELL, E. S. & LI, H. (2010). Structural basis for substrate placement by an archaeal box C/D ribonucleoprotein particle. Molecular Cell 39, 939-949.
    • (2010) Molecular Cell , vol.39 , pp. 939-949
    • Xue, S.1    Wang, R.2    Yang, F.3    Terns, R.M.4    Terns, M.P.5    Zhang, X.6    Maxwell, E.S.7    H, L.I.8
  • 145
    • 14844327762 scopus 로고    scopus 로고
    • Ψ35 in the branch site recognition region of U2 small nuclear RNA is important for pre-mRNA splicing in Saccharomyces cerevisiae
    • DOI 10.1074/jbc.M413288200
    • YANG, C., MCPHEETERS, D. S. & YU, Y. T. (2005a). Psi35 in the branch site recognition region of U2 small nuclear RNA is important for pre-mRNA splicing in Saccharomyces cerevisiae. Journal of Biological Chemistry 280, 6655-6662. (Pubitemid 40341218)
    • (2005) Journal of Biological Chemistry , vol.280 , Issue.8 , pp. 6655-6662
    • Yang, C.1    McPheeters, D.S.2    Yu, Y.-T.3
  • 146
    • 16244366466 scopus 로고    scopus 로고
    • Cotranscriptional recruitment of the pseudouridylsynthetase Cbf5p and of the RNA binding protein Naf1p during H/ACA snoRNP assembly
    • DOI 10.1128/MCB.25.8.3295-3304.2005
    • YANG, P. K., HOAREAU, C., FROMENT, C., MONSARRAT, B., HENRY, Y. & CHANFREAU, G. (2005b). Cotranscriptional recruitment of the pseudouridylsynthetase Cbf5p and of the RNA binding protein Naf1p during H/ACA snoRNP assembly. Molecular and Cellular Biology 25, 3295-3304. (Pubitemid 40464329)
    • (2005) Molecular and Cellular Biology , vol.25 , Issue.8 , pp. 3295-3304
    • Pok, K.Y.1    Hoareau, C.2    Froment, C.3    Monsarrat, B.4    Henry, Y.5    Chanfreau, G.6
  • 147
    • 0037159511 scopus 로고    scopus 로고
    • The Shq1p·Naf1p complex is required for box H/ACA small nucleolar ribonucleoprotein particle biogenesis
    • DOI 10.1074/jbc.M207669200
    • YANG, P.K., ROTONDO, G., PORRAS, T., LEGRAIN, P. & CHANFREAU, G. (2002). The Shq1p.Naf1p complex is required for box H/ACA small nucleolar ribonucleo-protein particle biogenesis. Journal of Biological Chemistry 277, 45235-45242. (Pubitemid 36159128)
    • (2002) Journal of Biological Chemistry , vol.277 , Issue.47 , pp. 45235-45242
    • Yang, P.K.1    Rotondo, G.2    Porras, T.3    Legrain, P.4    Chanfreau, G.5
  • 149
    • 0032189145 scopus 로고    scopus 로고
    • Modifications of U2 snRNA are required for snRNP assembly and pre-mRNA splicing
    • DOI 10.1093/emboj/17.19.5783
    • YU, Y. T., SHU, M. D. & STEITZ, J. A. (1998). Modifications of U2 snRNA are required for snRNP assembly and pre-mRNA splicing. EMBO Journal 17, 5783-5795. (Pubitemid 28445989)
    • (1998) EMBO Journal , vol.17 , Issue.19 , pp. 5783-5795
    • Yu, Y.-T.1    Shu, M.-D.2    Steitz, J.A.3
  • 150
    • 1642447085 scopus 로고    scopus 로고
    • Pseudouridines in and near the branch site recognition region of U2 snRNA are required for snRNP biogenesis and pre-mRNA splicing in Xenopus oocytes
    • DOI 10.1261/rna.5159504
    • ZHAO, X. & YU, Y. T. (2004). Pseudouridines in and near the branch site recognition region of U2 snRNA are required for snRNP biogenesis and pre-mRNA splicing in Xenopus oocytes. RNA 10, 681-690. (Pubitemid 38405946)
    • (2004) RNA , vol.10 , Issue.4 , pp. 681-690
    • Zhao, X.1    Yu, Y.-T.2
  • 151
    • 77954832927 scopus 로고    scopus 로고
    • Functional and structural impact of target uridine substitutions on H/ACA ribonucleoprotein particle pseudouridine synthase
    • ZHOU, J., LIANG, B. & LI, H. (2010a). Functional and structural impact of target uridine substitutions on H/ACA ribonucleoprotein particle pseudouridine synthase. Biochemistry 49, 6276-6281.
    • (2010) Biochemistry , vol.49 , pp. 6276-6281
    • Zhou, J.1    Liang, B.2    H, L.I.3
  • 152
    • 77955559262 scopus 로고    scopus 로고
    • Glycosidic bond conformation preference plays a pivotal role in catalysis of RNA pseudouridylation: A combined simulation and structural study
    • ZHOU, J., CHAO, L. V., LIANG, B., CHEN, M., YANG, W. & LI, H. (2010b). Glycosidic bond conformation preference plays a pivotal role in catalysis of RNA pseudouridylation: a combined simulation and structural study. Journal of Molecular Biology 401, 690-695.
    • (2010) Journal of Molecular Biology , vol.401 , pp. 690-695
    • Zhou, J.1    Chao, L.V.2    Liang, B.3    Chen, M.4    Yang, W.5    H, L.I.6


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