메뉴 건너뛰기




Volumn 8, Issue 3, 2000, Pages

RNA bulges as architectural and recognition motifs

Author keywords

[No Author keywords available]

Indexed keywords

COMPLEX FORMATION; CONFORMATIONAL TRANSITION; MOLECULAR INTERACTION; MOLECULAR RECOGNITION; MOLECULAR STABILITY; PRIORITY JOURNAL; PROTEIN BINDING; PROTEIN FOLDING; RNA ANALYSIS; RNA STRUCTURE; SHORT SURVEY;

EID: 0034653899     PISSN: 09692126     EISSN: None     Source Type: Journal    
DOI: 10.1016/S0969-2126(00)00110-6     Document Type: Review
Times cited : (132)

References (64)
  • 2
    • 0033544719 scopus 로고    scopus 로고
    • Stitching together RNA tertiary architectures
    • Hermann T., Patel D.J. Stitching together RNA tertiary architectures. J. Mol. Biol. 294:1999;829-849.
    • (1999) J. Mol. Biol. , vol.294 , pp. 829-849
    • Hermann, T.1    Patel, D.J.2
  • 4
    • 0032870204 scopus 로고    scopus 로고
    • Structural motifs in RNA
    • Moore P.B. Structural motifs in RNA. Annu. Rev. Biochem. 67:1999;287-300.
    • (1999) Annu. Rev. Biochem. , vol.67 , pp. 287-300
    • Moore, P.B.1
  • 5
    • 0027370486 scopus 로고
    • Major groove accessibility of RNA
    • Weeks K.M., Crothers D.M. Major groove accessibility of RNA. Science. 261:1993;1574-1577.
    • (1993) Science , vol.261 , pp. 1574-1577
    • Weeks, K.M.1    Crothers, D.M.2
  • 6
    • 0033529304 scopus 로고    scopus 로고
    • Structure of tau exon 10 splicing regulatory element RNA and destabilization by mutations of frontotemporal dementia and Parkinsonism linked to chromosome 17
    • Varani L., Varani G.et al. Structure of tau exon 10 splicing regulatory element RNA and destabilization by mutations of frontotemporal dementia and Parkinsonism linked to chromosome 17. Proc. Natl Acad. Sci. USA. 96:1999;8229-8234.
    • (1999) Proc. Natl Acad. Sci. USA , vol.96 , pp. 8229-8234
    • Varani, L.1    Varani, G.2
  • 7
    • 0029024877 scopus 로고
    • Proton NMR and structural features of a 24-nucleotide RNA hairpin
    • Borer P.N., Pelczer I.et al. Proton NMR and structural features of a 24-nucleotide RNA hairpin. Biochemistry. 34:1995;6488-6503.
    • (1995) Biochemistry , vol.34 , pp. 6488-6503
    • Borer, P.N.1    Pelczer, I.2
  • 8
    • 0030090986 scopus 로고    scopus 로고
    • Crystal structure of an A-form duplex with single-adenosine bulges and a conformational basis for site-specific RNA self-cleavage
    • Portmann S., Grimm S., Workman C., Usman N., Egli M. Crystal structure of an A-form duplex with single-adenosine bulges and a conformational basis for site-specific RNA self-cleavage. Chem. Biol. 3:1996;173-184.
    • (1996) Chem. Biol. , vol.3 , pp. 173-184
    • Portmann, S.1    Grimm, S.2    Workman, C.3    Usman, N.4    Egli, M.5
  • 9
    • 0030585428 scopus 로고    scopus 로고
    • Solution structure of the donor site of a trans-splicing RNA
    • Greenbaum N.L., Radhakrishnan I., Patel D.J., Hirsh D. Solution structure of the donor site of a trans-splicing RNA. Structure. 4:1996;725-733.
    • (1996) Structure , vol.4 , pp. 725-733
    • Greenbaum, N.L.1    Radhakrishnan, I.2    Patel, D.J.3    Hirsh, D.4
  • 10
    • 0028858599 scopus 로고
    • Solution structure of a bovine immunodeficiency virus Tat-TAR peptide-RNA complex
    • Puglisi J.D., Chen L., Blanchard S., Frankel A.D. Solution structure of a bovine immunodeficiency virus Tat-TAR peptide-RNA complex. Science. 270:1995;1200-1203.
    • (1995) Science , vol.270 , pp. 1200-1203
    • Puglisi, J.D.1    Chen, L.2    Blanchard, S.3    Frankel, A.D.4
  • 11
    • 0029613238 scopus 로고
    • Molecular recognition in the bovine immunodeficiency virus Tat peptide-TAR RNA complex
    • Ye X., Kumar R.A., Patel D.J. Molecular recognition in the bovine immunodeficiency virus Tat peptide-TAR RNA complex. Chem. Biol. 2:1995;827-840.
    • (1995) Chem. Biol. , vol.2 , pp. 827-840
    • Ye, X.1    Kumar, R.A.2    Patel, D.J.3
  • 12
    • 0033571104 scopus 로고    scopus 로고
    • The crystal structure of the dimerization initiation site of genomic HIV-1 RNA reveals an extended duplex with two adenine-bulges
    • Ennifar E., Dumas P.et al. The crystal structure of the dimerization initiation site of genomic HIV-1 RNA reveals an extended duplex with two adenine-bulges. Structure. 7:1999;1439-1449.
    • (1999) Structure , vol.7 , pp. 1439-1449
    • Ennifar, E.1    Dumas, P.2
  • 13
    • 0026669321 scopus 로고
    • A small metalloribozyme with a two-step mechanism
    • Pan T., Uhlenbeck O.C. A small metalloribozyme with a two-step mechanism. Nature. 358:1992;560-563.
    • (1992) Nature , vol.358 , pp. 560-563
    • Pan, T.1    Uhlenbeck, O.C.2
  • 14
    • 0033010809 scopus 로고    scopus 로고
    • Crystal structure of a lead-dependent ribozyme revealing metal binding sites relevant to catalysis
    • Wedekind J.E., McKay D.B. Crystal structure of a lead-dependent ribozyme revealing metal binding sites relevant to catalysis. Nat. Struct. Biol. 6:1999;261-268.
    • (1999) Nat. Struct. Biol. , vol.6 , pp. 261-268
    • Wedekind, J.E.1    McKay, D.B.2
  • 15
    • 0032573424 scopus 로고    scopus 로고
    • NMR solution structure of the lead-dependent ribozyme: Evidence for dynamics in RNA catalysis
    • Hoogstraten C.G., Legault P., Pardi A. NMR solution structure of the lead-dependent ribozyme: evidence for dynamics in RNA catalysis. J. Mol. Biol. 284:1998;337-350.
    • (1998) J. Mol. Biol. , vol.284 , pp. 337-350
    • Hoogstraten, C.G.1    Legault, P.2    Pardi, A.3
  • 16
    • 0029820625 scopus 로고    scopus 로고
    • Crystal structure of a group I ribozyme domain: Principles of RNA packing
    • Cate J.H., Doudna J.A.et al. Crystal structure of a group I ribozyme domain. principles of RNA packing Science. 273:1996;1678-1685.
    • (1996) Science , vol.273 , pp. 1678-1685
    • Cate, J.H.1    Doudna, J.A.2
  • 17
    • 0030929889 scopus 로고    scopus 로고
    • A magnesium ion core at the heart of a ribozyme domain
    • Cate J.H., Hanna R.L., Doudna J.A. A magnesium ion core at the heart of a ribozyme domain. Nat. Struct. Biol. 4:1997;553-558.
    • (1997) Nat. Struct. Biol. , vol.4 , pp. 553-558
    • Cate, J.H.1    Hanna, R.L.2    Doudna, J.A.3
  • 18
    • 0027960331 scopus 로고
    • Crystal structure of an RNA bacteriophage coat protein-operator complex
    • Vålegard K., Murray J.B., Stockley P.G., Stonehouse N.J., Liljas L. Crystal structure of an RNA bacteriophage coat protein-operator complex. Nature. 371:1994;623-626.
    • (1994) Nature , vol.371 , pp. 623-626
    • Vålegard, K.1    Murray, J.B.2    Stockley, P.G.3    Stonehouse, N.J.4    Liljas, L.5
  • 19
    • 0031951789 scopus 로고    scopus 로고
    • Crystal structure of an RNA aptamer-protein complex at 2.8 Å resolution
    • Convery M.A., Stockley P.G.et al. Crystal structure of an RNA aptamer-protein complex at 2.8 Å resolution. Nat. Struct. Biol. 5:1998;133-139.
    • (1998) Nat. Struct. Biol. , vol.5 , pp. 133-139
    • Convery, M.A.1    Stockley, P.G.2
  • 20
    • 0030887815 scopus 로고    scopus 로고
    • Saccharide-RNA recognition in an aminoglycoside antibiotic-RNA aptamer complex
    • Jiang L., Suri A.K., Fiala R., Patel D.J. Saccharide-RNA recognition in an aminoglycoside antibiotic-RNA aptamer complex. Chem. Biol. 4:1997;35-50.
    • (1997) Chem. Biol. , vol.4 , pp. 35-50
    • Jiang, L.1    Suri, A.K.2    Fiala, R.3    Patel, D.J.4
  • 21
    • 0031688019 scopus 로고    scopus 로고
    • Solution structure of the tobramycin-RNA aptamer complex
    • Jiang L., Patel D.J. Solution structure of the tobramycin-RNA aptamer complex. Nat. Struct. Biol. 5:1998;769-774.
    • (1998) Nat. Struct. Biol. , vol.5 , pp. 769-774
    • Jiang, L.1    Patel, D.J.2
  • 22
    • 0033565449 scopus 로고    scopus 로고
    • Saccharide-RNA recognition in a complex formed between neomycin B and an RNA aptamer
    • Jiang L., Majumdar A., Hu W., Jaishree T.J., Xu W., Patel D.J. Saccharide-RNA recognition in a complex formed between neomycin B and an RNA aptamer. Structure. 7:1999;817-827.
    • (1999) Structure , vol.7 , pp. 817-827
    • Jiang, L.1    Majumdar, A.2    Hu, W.3    Jaishree, T.J.4    Xu, W.5    Patel, D.J.6
  • 23
    • 0033200399 scopus 로고    scopus 로고
    • RNA architecture dictates bound peptide conformations
    • Ye X., Patel D.J.et al. RNA architecture dictates bound peptide conformations. Chem. Biol. 6:1999;657-669.
    • (1999) Chem. Biol. , vol.6 , pp. 657-669
    • Ye, X.1    Patel, D.J.2
  • 24
    • 0033572743 scopus 로고    scopus 로고
    • Anchoring an extended HTLV-1 Rex peptide within an RNA major groove containing junctional base triples
    • Jiang F., Patel D.J.et al. Anchoring an extended HTLV-1 Rex peptide within an RNA major groove containing junctional base triples. Structure. 7:1999;1461-1472.
    • (1999) Structure , vol.7 , pp. 1461-1472
    • Jiang, F.1    Patel, D.J.2
  • 25
    • 0032532765 scopus 로고    scopus 로고
    • Exploration of metal ion binding sites in RNA folds by Brownian-dynamics simulations
    • Hermann T., Westhof E. Exploration of metal ion binding sites in RNA folds by Brownian-dynamics simulations. Structure. 6:1998;1303-1314.
    • (1998) Structure , vol.6 , pp. 1303-1314
    • Hermann, T.1    Westhof, E.2
  • 26
    • 0032701796 scopus 로고    scopus 로고
    • Tackling Tat
    • Karn J. Tackling Tat. J. Mol. Biol. 293:1999;235-254.
    • (1999) J. Mol. Biol. , vol.293 , pp. 235-254
    • Karn, J.1
  • 27
    • 0032543957 scopus 로고    scopus 로고
    • A 1.3 Å resolution crystal structure of the HIV-1 trans-activation response region RNA stem reveals a metal ion-dependent bulge conformation
    • Ippolito J.A., Steitz T.A. A 1.3 Å resolution crystal structure of the HIV-1 trans-activation response region RNA stem reveals a metal ion-dependent bulge conformation. Proc. Natl Acad. Sci. USA. 95:1998;9819-9824.
    • (1998) Proc. Natl Acad. Sci. USA , vol.95 , pp. 9819-9824
    • Ippolito, J.A.1    Steitz, T.A.2
  • 28
    • 0029032837 scopus 로고
    • The bend in RNA created by the trans-activation response element bulge of human immunodeficiency virus is straightened by arginine and by Tat-derived peptide
    • Zacharias M., Hagerman P.J. The bend in RNA created by the trans-activation response element bulge of human immunodeficiency virus is straightened by arginine and by Tat-derived peptide. Proc. Natl Acad. Sci. USA. 92:1995;6052-6056.
    • (1995) Proc. Natl Acad. Sci. USA , vol.92 , pp. 6052-6056
    • Zacharias, M.1    Hagerman, P.J.2
  • 29
    • 0029852357 scopus 로고    scopus 로고
    • Structure of HIV-1 TAR RNA in the absence of ligands reveals a novel conformation of the trinucleotide bulge
    • Aboul-ela F., Karn J., Varani G. Structure of HIV-1 TAR RNA in the absence of ligands reveals a novel conformation of the trinucleotide bulge. Nucleic Acids Res. 24:1996;3974-3981.
    • (1996) Nucleic Acids Res. , vol.24 , pp. 3974-3981
    • Aboul-Ela, F.1    Karn, J.2    Varani, G.3
  • 31
    • 0028864394 scopus 로고
    • The structure of the human immunodeficiency virus type-1 TAR RNA reveals principles of RNA recognition by Tat protein
    • Aboul-ela F., Karn J., Varani G. The structure of the human immunodeficiency virus type-1 TAR RNA reveals principles of RNA recognition by Tat protein. J. Mol. Biol. 253:1995;313-332.
    • (1995) J. Mol. Biol. , vol.253 , pp. 313-332
    • Aboul-Ela, F.1    Karn, J.2    Varani, G.3
  • 32
    • 0030935060 scopus 로고    scopus 로고
    • Dissection of the proposed base triple in human immunodeficieny virus TAR RNA indicates the importance of Hoogsten interaction
    • Tao J., Chen L., Frankel A.D. Dissection of the proposed base triple in human immunodeficieny virus TAR RNA indicates the importance of Hoogsten interaction. Biochemistry. 36:1997;3491-3495.
    • (1997) Biochemistry , vol.36 , pp. 3491-3495
    • Tao, J.1    Chen, L.2    Frankel, A.D.3
  • 33
    • 0029784592 scopus 로고    scopus 로고
    • α Helix-RNA major groove recognition in an HIV-1 Rev peptide-RRE RNA complex
    • Battiste J.L., Williamson J.R.et al. α Helix-RNA major groove recognition in an HIV-1 Rev peptide-RRE RNA complex. Science. 273:1996;1547-1551.
    • (1996) Science , vol.273 , pp. 1547-1551
    • Battiste, J.L.1    Williamson, J.R.2
  • 34
    • 0030475417 scopus 로고    scopus 로고
    • Deep penetration of an α-helix into a widened RNA major groove in the HIV-1 Rev peptide-RNA aptamer complex
    • Ye X., Gorin A., Ellington A.D., Patel D.J. Deep penetration of an α-helix into a widened RNA major groove in the HIV-1 Rev peptide-RNA aptamer complex. Nat. Struct. Biol. 3:1996;1026-1033.
    • (1996) Nat. Struct. Biol. , vol.3 , pp. 1026-1033
    • Ye, X.1    Gorin, A.2    Ellington, A.D.3    Patel, D.J.4
  • 35
    • 0032513007 scopus 로고    scopus 로고
    • Aminoglycoside binding to the hammerhead ribozyme: A general model for the interaction of cationic antibiotics with RNA
    • Hermann T., Westhof E. Aminoglycoside binding to the hammerhead ribozyme: a general model for the interaction of cationic antibiotics with RNA. J. Mol. Biol. 276:1998;903-912.
    • (1998) J. Mol. Biol. , vol.276 , pp. 903-912
    • Hermann, T.1    Westhof, E.2
  • 36
    • 0033535566 scopus 로고    scopus 로고
    • Docking of cationic antibiotics to negatively charged pockets in RNA folds
    • Hermann T., Westhof E. Docking of cationic antibiotics to negatively charged pockets in RNA folds. J. Med. Chem. 42:1999;1250-1261.
    • (1999) J. Med. Chem. , vol.42 , pp. 1250-1261
    • Hermann, T.1    Westhof, E.2
  • 37
    • 0031568305 scopus 로고    scopus 로고
    • Role REVersal: Understanding how RRE RNA binds its peptide ligand
    • Grate D., Wilson C. Role REVersal. understanding how RRE RNA binds its peptide ligand Structure. 5:1997;7-11.
    • (1997) Structure , vol.5 , pp. 7-11
    • Grate, D.1    Wilson, C.2
  • 38
    • 0032062750 scopus 로고    scopus 로고
    • RNA recognition and regulation of HIV-1 gene expression by viral factor Tat
    • Naryshkin N.A., Gait M.J., Ivanovskaya M.G. RNA recognition and regulation of HIV-1 gene expression by viral factor Tat. Biochemistry (Moscow). 63:1998;489-503.
    • (1998) Biochemistry (Moscow) , vol.63 , pp. 489-503
    • Naryshkin, N.A.1    Gait, M.J.2    Ivanovskaya, M.G.3
  • 39
    • 0032864043 scopus 로고    scopus 로고
    • Adaptive recognition in RNA complexes with peptides and protein modules
    • Patel D.J. Adaptive recognition in RNA complexes with peptides and protein modules. Curr. Opin. Struct. Biol. 9:1999;74-87.
    • (1999) Curr. Opin. Struct. Biol. , vol.9 , pp. 74-87
    • Patel, D.J.1
  • 40
    • 0032419420 scopus 로고    scopus 로고
    • Saccharide-RNA recognition
    • Hermann T., Westhof E. Saccharide-RNA recognition. Biopolymers. 48:1998;155-165.
    • (1998) Biopolymers , vol.48 , pp. 155-165
    • Hermann, T.1    Westhof, E.2
  • 41
    • 0028823853 scopus 로고
    • Inhibition of an HIV-1 Tat-derived peptide binding to TAR RNA by aminoglycoside antibiotics
    • Mei H.-Y., Czarnik A.W.et al. Inhibition of an HIV-1 Tat-derived peptide binding to TAR RNA by aminoglycoside antibiotics. Bioorg. Med. Chem. Lett. 5:1995;2755-2760.
    • (1995) Bioorg. Med. Chem. Lett. , vol.5 , pp. 2755-2760
    • Mei, H.-Y.1    Czarnik, A.W.2
  • 42
    • 0027370433 scopus 로고
    • Small molecules that selectively block RNA binding of HIV-1 Rev protein inhibit Rev function and viral production
    • Zapp M.L., Stern S., Green M.R. Small molecules that selectively block RNA binding of HIV-1 Rev protein inhibit Rev function and viral production. Cell. 74:1993;969-978.
    • (1993) Cell , vol.74 , pp. 969-978
    • Zapp, M.L.1    Stern, S.2    Green, M.R.3
  • 43
    • 0031894779 scopus 로고    scopus 로고
    • Modeling RNA-ligand interactions: The Rev-binding element RNA-aminoglycoside complex
    • Leclerc F., Cedergren R. Modeling RNA-ligand interactions: the Rev-binding element RNA-aminoglycoside complex. J. Med. Chem. 41:1998;175-182.
    • (1998) J. Med. Chem. , vol.41 , pp. 175-182
    • Leclerc, F.1    Cedergren, R.2
  • 44
    • 0029961381 scopus 로고    scopus 로고
    • Inhibition of HIV-1 Rev-RRE interaction by diphenylfuran derivatives
    • Ratmeyer L., Wilson W.D.et al. Inhibition of HIV-1 Rev-RRE interaction by diphenylfuran derivatives. Biochemistry. 35:1996;13689-13696.
    • (1996) Biochemistry , vol.35 , pp. 13689-13696
    • Ratmeyer, L.1    Wilson, W.D.2
  • 45
    • 0030976612 scopus 로고    scopus 로고
    • An inhibitor of the Tat/TAR RNA interaction that effectively suppresses HIV-1 replication
    • Hamy F., Klimkait T.et al. An inhibitor of the Tat/TAR RNA interaction that effectively suppresses HIV-1 replication. Proc. Natl Acad. Sci. USA. 94:1997;3548-3553.
    • (1997) Proc. Natl Acad. Sci. USA , vol.94 , pp. 3548-3553
    • Hamy, F.1    Klimkait, T.2
  • 46
    • 0030856838 scopus 로고    scopus 로고
    • Binding of Hoechst 33258 to the TAR RNA of HIV-1. Recognition of a pyrimidine bulge-dependent structure
    • Dassonneville L., Hamy F., Colson P., Houssier C., Bailly C. Binding of Hoechst 33258 to the TAR RNA of HIV-1. Recognition of a pyrimidine bulge-dependent structure. Nucleic Acids Res. 25:1997;4487-4492.
    • (1997) Nucleic Acids Res. , vol.25 , pp. 4487-4492
    • Dassonneville, L.1    Hamy, F.2    Colson, P.3    Houssier, C.4    Bailly, C.5
  • 47
    • 0032491152 scopus 로고    scopus 로고
    • Inhibitors of protein-RNA complexation that target the RNA: Specific recognition of human immunodeficieny virus type 1 TAR RNA by small organic molecules
    • Mei H.-Y., Czarnik A.W.et al. Inhibitors of protein-RNA complexation that target the RNA. specific recognition of human immunodeficieny virus type 1 TAR RNA by small organic molecules Biochemistry. 37:1998;14204-14212.
    • (1998) Biochemistry , vol.37 , pp. 14204-14212
    • Mei, H.-Y.1    Czarnik, A.W.2
  • 48
    • 0033013426 scopus 로고    scopus 로고
    • Inhibition of HIV-1 Tat-TAR interaction by diphenylfuran derivatives: Effects of the terminal basic side chains
    • Gelus N., Bailly C., Hamy F., Klimkait T., Wilson W.D., Boykin D.W. Inhibition of HIV-1 Tat-TAR interaction by diphenylfuran derivatives: effects of the terminal basic side chains. Bioorg. Med. Chem. 7:1999;1089-1096.
    • (1999) Bioorg. Med. Chem. , vol.7 , pp. 1089-1096
    • Gelus, N.1    Bailly, C.2    Hamy, F.3    Klimkait, T.4    Wilson, W.D.5    Boykin, D.W.6
  • 49
    • 0029043670 scopus 로고
    • Bulge-specific cleavage in transactivation response region RNA and its DNA analogue by neocarzinostatin chromophore
    • Kappen L.S., Goldberg I.H. Bulge-specific cleavage in transactivation response region RNA and its DNA analogue by neocarzinostatin chromophore. Biochemistry. 34:1995;5997-6002.
    • (1995) Biochemistry , vol.34 , pp. 5997-6002
    • Kappen, L.S.1    Goldberg, I.H.2
  • 50
    • 0030914320 scopus 로고    scopus 로고
    • Effect of ribonucleotide substitution on nucleic acid bulge recognition by neocarzinostatin
    • Kappen L.S., Goldberg I.H. Effect of ribonucleotide substitution on nucleic acid bulge recognition by neocarzinostatin. Bioorg. Med. Chem. 5:1997;1221-1227.
    • (1997) Bioorg. Med. Chem. , vol.5 , pp. 1221-1227
    • Kappen, L.S.1    Goldberg, I.H.2
  • 51
    • 0033485558 scopus 로고    scopus 로고
    • Non-Watson-Crick base pairs in RNA-protein recognition
    • Hermann T., Westhof E. Non-Watson-Crick base pairs in RNA-protein recognition. Chem. Biol. 1999;R335-R343.
    • (1999) Chem. Biol.
    • Hermann, T.1    Westhof, E.2
  • 52
    • 0026045893 scopus 로고
    • HIV-1 Rev regulation involves recognition of non-Watson-Crick base pairs in viral RNA
    • Bartel D.P., Zapp M.L., Green M.R., Szostak J.W. HIV-1 Rev regulation involves recognition of non-Watson-Crick base pairs in viral RNA. Cell. 67:1991;529-536.
    • (1991) Cell , vol.67 , pp. 529-536
    • Bartel, D.P.1    Zapp, M.L.2    Green, M.R.3    Szostak, J.W.4
  • 54
  • 55
    • 0032062099 scopus 로고    scopus 로고
    • Solution structure of a substrate for the archaeal pre-tRNA splicing endonucleases: The bulge-helix-bulge motif
    • Diener J.L., Moore P.B. Solution structure of a substrate for the archaeal pre-tRNA splicing endonucleases: the bulge-helix-bulge motif. Mol. Cell. 1:1998;883-894.
    • (1998) Mol. Cell. , vol.1 , pp. 883-894
    • Diener, J.L.1    Moore, P.B.2
  • 56
    • 0033553625 scopus 로고    scopus 로고
    • Crystal structure of a conserved ribosomal protein-RNA complex
    • Conn G.L., Draper D.E., Lattmann E.E., Gittis A.G. Crystal structure of a conserved ribosomal protein-RNA complex. Science. 284:1999;1171-1174.
    • (1999) Science , vol.284 , pp. 1171-1174
    • Conn, G.L.1    Draper, D.E.2    Lattmann, E.E.3    Gittis, A.G.4
  • 57
    • 0033553439 scopus 로고    scopus 로고
    • A detailed view of a ribosomal active site: The structure of the L11-RNA complex
    • Wimberly B.T., Guymon R., McCutcheon J.P., White S.W., Ramakrishnan V. A detailed view of a ribosomal active site. the structure of the L11-RNA complex Cell. 97:1999;491-502.
    • (1999) Cell , vol.97 , pp. 491-502
    • Wimberly, B.T.1    Guymon, R.2    McCutcheon, J.P.3    White, S.W.4    Ramakrishnan, V.5
  • 58
    • 0025133312 scopus 로고
    • Recognition of exon-intron boundaries by the Halobacterium volcanii tRNA intron endonuclease
    • Thompson L., Daniels C. Recognition of exon-intron boundaries by the Halobacterium volcanii tRNA intron endonuclease. J. Biol. Chem. 265:1990;18104-18111.
    • (1990) J. Biol. Chem. , vol.265 , pp. 18104-18111
    • Thompson, L.1    Daniels, C.2
  • 59
    • 0028007314 scopus 로고
    • Structural characteristics of the stable RNA introns of archaeal hyperthermophiles and their splicing junctions
    • Lykke-Andersen J., Garrett R. Structural characteristics of the stable RNA introns of archaeal hyperthermophiles and their splicing junctions. J. Mol. Biol. 243:1994;846-855.
    • (1994) J. Mol. Biol. , vol.243 , pp. 846-855
    • Lykke-Andersen, J.1    Garrett, R.2
  • 60
    • 0030730242 scopus 로고    scopus 로고
    • Properties of the H. volcanii tRNA intron endonuclease reveal a relationship between the archeal and eukaryal tRNA intron processing systems
    • Kleman-Leyer K., Armbruster D., Daniels C. Properties of the H. volcanii tRNA intron endonuclease reveal a relationship between the archeal and eukaryal tRNA intron processing systems. Cell. 89:1997;839-847.
    • (1997) Cell , vol.89 , pp. 839-847
    • Kleman-Leyer, K.1    Armbruster, D.2    Daniels, C.3
  • 61
    • 0032502894 scopus 로고    scopus 로고
    • Crystal structure and evolution of a transfer RNA splicing enzyme
    • Li H., Trotta C.R., Abelson J. Crystal structure and evolution of a transfer RNA splicing enzyme. Science. 280:1998;279-284.
    • (1998) Science , vol.280 , pp. 279-284
    • Li, H.1    Trotta, C.R.2    Abelson, J.3
  • 63
    • 0033607003 scopus 로고    scopus 로고
    • Placement of protein and RNA structures into a 5 Å-resolution map of the 50S ribosomal subunit
    • Ban N., Nissen P., Hansen J., Capel M., Moore P.B., Steitz T.A. Placement of protein and RNA structures into a 5 Å-resolution map of the 50S ribosomal subunit. Nature. 400:1999;841-847.
    • (1999) Nature , vol.400 , pp. 841-847
    • Ban, N.1    Nissen, P.2    Hansen, J.3    Capel, M.4    Moore, P.B.5    Steitz, T.A.6


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.