메뉴 건너뛰기




Volumn 272, Issue 9, 2005, Pages 2088-2097

Protein families and RNA recognition

Author keywords

[No Author keywords available]

Indexed keywords

BACTERIAL PROTEIN; RIBONUCLEOPROTEIN; RNA BINDING PROTEIN; VIRUS PROTEIN; ZINC FINGER PROTEIN;

EID: 18444383371     PISSN: 1742464X     EISSN: None     Source Type: Journal    
DOI: 10.1111/j.1742-4658.2005.04650.x     Document Type: Short Survey
Times cited : (133)

References (87)
  • 1
    • 0027315727 scopus 로고
    • RNA recognition: A family matter?
    • Mattaj IW (1993) RNA recognition: a family matter? Cell 73, 837-840.
    • (1993) Cell , vol.73 , pp. 837-840
    • Mattaj, I.W.1
  • 2
    • 0025221731 scopus 로고
    • Structure of the RNA-binding domain of the U1 small nuclear ribonucleoprotein A
    • Nagai K, Oubridge C, Jessen TH, Li J & Evans PR (1990) Structure of the RNA-binding domain of the U1 small nuclear ribonucleoprotein A. Nature 348, 515-520.
    • (1990) Nature , vol.348 , pp. 515-520
    • Nagai, K.1    Oubridge, C.2    Jessen, T.H.3    Li, J.4    Evans, P.R.5
  • 3
    • 0026687213 scopus 로고
    • The structure of ribosomal protein S5 reveals sites of interaction with 16S rRNA
    • Ramakrishnan V & White SW (1992) The structure of ribosomal protein S5 reveals sites of interaction with 16S rRNA. Nature 358, 768-771.
    • (1992) Nature , vol.358 , pp. 768-771
    • Ramakrishnan, V.1    White, S.W.2
  • 5
    • 0029608909 scopus 로고
    • Ribosomal proteins and elongation factors
    • Liljas A & Garber M (1995) Ribosomal proteins and elongation factors. Curr Opin Struct Biol 5, 721-727.
    • (1995) Curr Opin Struct Biol , vol.5 , pp. 721-727
    • Liljas, A.1    Garber, M.2
  • 8
    • 0024095588 scopus 로고
    • Functional domains required for Tat-induced transcriptional activation of the HIV-1 long terminal repeat
    • Garcia JA, Harrich D, Pearson L, Mitsuyasu R & Gaynor RB (1988) Functional domains required for Tat-induced transcriptional activation of the HIV-1 long terminal repeat. EMBO J 7, 3143-3147.
    • (1988) EMBO J , vol.7 , pp. 3143-3147
    • Garcia, J.A.1    Harrich, D.2    Pearson, L.3    Mitsuyasu, R.4    Gaynor, R.B.5
  • 12
    • 0025895051 scopus 로고
    • Heterologous basic domain substitutions in the HIV-1 Tat protein reveal an arginine-rich motif required for trans-activation
    • Subramanian T, Govindarajan R & Chinnadurai G (1991) Heterologous basic domain substitutions in the HIV-1 Tat protein reveal an arginine-rich motif required for trans-activation. EMBO J 10, 2311-2318.
    • (1991) EMBO J , vol.10 , pp. 2311-2318
    • Subramanian, T.1    Govindarajan, R.2    Chinnadurai, G.3
  • 13
    • 0025882673 scopus 로고
    • Human immunodeficiency virus type 1 regulator of virion expression, Rev, forms nucleoprotein filaments after binding to a purine-rich 'bubble' located within the Rev-response region of viral mRNAs
    • Heaphy S, Finch JT, gait MJ, Karn J & Singh M (1991) Human immunodeficiency virus type 1 regulator of virion expression, Rev, forms nucleoprotein filaments after binding to a purine-rich 'bubble' located within the Rev-response region of viral mRNAs. Proc Natl Acad Sci USA 88, 7366-7370.
    • (1991) Proc Natl Acad Sci USA , vol.88 , pp. 7366-7370
    • Heaphy, S.1    Finch, J.T.2    Gait, M.J.3    Karn, J.4    Singh, M.5
  • 14
    • 0027452957 scopus 로고
    • High affinity binding of TAR RNA by the human immunodeficiency type-1 Tat protein requires base-pairs in the RNA stem and amino acid residues flanking the basic region
    • Churcher MJ, Lament C, Hamy F, Dingwall C, Green SM, Lowe AD, Butler PJG, Gait MJ & Karn J (1993) High affinity binding of TAR RNA by the human immunodeficiency type-1 Tat protein requires base-pairs in the RNA stem and amino acid residues flanking the basic region. J Mol Biol 230, 90-110.
    • (1993) J Mol Biol , vol.230 , pp. 90-110
    • Churcher, M.J.1    Lament, C.2    Hamy, F.3    Dingwall, C.4    Green, S.M.5    Lowe, A.D.6    Butler, P.J.G.7    Gait, M.J.8    Karn, J.9
  • 15
    • 0032559232 scopus 로고    scopus 로고
    • Induced folding in RNA-protein recognition: More than a simple molecular handshake
    • Frankel AD & Smith CA (1998) Induced folding in RNA-protein recognition: more than a simple molecular handshake. Cell 92, 149-151.
    • (1998) Cell , vol.92 , pp. 149-151
    • Frankel, A.D.1    Smith, C.A.2
  • 16
    • 0028858599 scopus 로고
    • Solution structure of a bovine immunodeficiency virus Tat-TAR peptide-RNA complex
    • Puglisi JD, Chen L, Blanchard S & Frankel AD (1995) Solution structure of a bovine immunodeficiency virus Tat-TAR peptide-RNA complex. Science 270, 1200-1203.
    • (1995) Science , vol.270 , pp. 1200-1203
    • Puglisi, J.D.1    Chen, L.2    Blanchard, S.3    Frankel, A.D.4
  • 17
    • 0029613238 scopus 로고
    • Molecular recognition in the bovine immunodeficiency virus Tat peptide-TAR RNA complex
    • Ye X, Kumar RA & Patel DJ (1995) Molecular recognition in the bovine immunodeficiency virus Tat peptide-TAR RNA complex. Chem Biol 2, 827-840.
    • (1995) Chem Biol , vol.2 , pp. 827-840
    • Ye, X.1    Kumar, R.A.2    Patel, D.J.3
  • 19
    • 0032540286 scopus 로고    scopus 로고
    • NMR structure of the bacteriophage λ N-Peptide/ BoxB RNA complex: Recognition of a GNRA fold by an arginine-rich motif
    • Legault P, Li J, Mogridge J, Greenblatt J & Kay LE (1998) NMR structure of the bacteriophage λ N-Peptide/ BoxB RNA complex: recognition of a GNRA fold by an arginine-rich motif. Cell 93, 289-299.
    • (1998) Cell , vol.93 , pp. 289-299
    • Legault, P.1    Li, J.2    Mogridge, J.3    Greenblatt, J.4    Kay, L.E.5
  • 21
    • 3042776646 scopus 로고    scopus 로고
    • Structural mimicry of retroviral Tat proteins by constrained β-hairpin peptidomimetics - New ligands with high affinity and selectivity for viral TAR RNA regulatory elements
    • Athanassiou Z, Dias RLA, Moehle K, Dobson N, Varani G & Robinson JA (2004) Structural mimicry of retroviral Tat proteins by constrained β-hairpin peptidomimetics - new ligands with high affinity and selectivity for viral TAR RNA regulatory elements. J Am Chem Soc 126, 6906-6913.
    • (2004) J Am Chem Soc , vol.126 , pp. 6906-6913
    • Athanassiou, Z.1    Dias, R.L.A.2    Moehle, K.3    Dobson, N.4    Varani, G.5    Robinson, J.A.6
  • 23
    • 0025266929 scopus 로고
    • Functional substitution of the basic domain of the HIV-1 trans-activator, Tat, with the basic domain of the functionally heterologous Rev
    • Subramanian T, Kuppuswamy M, Venkatesh L, Srinivasan A & Chinnadurai G (1990) Functional substitution of the basic domain of the HIV-1 trans-activator, Tat, with the basic domain of the functionally heterologous Rev. Virology 176, 178-183.
    • (1990) Virology , vol.176 , pp. 178-183
    • Subramanian, T.1    Kuppuswamy, M.2    Venkatesh, L.3    Srinivasan, A.4    Chinnadurai, G.5
  • 24
    • 0027509632 scopus 로고
    • Hydrogen bonding contacts in the major groove are required for human immunodeficiency virus type 1 Tat protein recognition of TAR RNA
    • Hamy F, Asseline V, Grasby J, Iwai S, Pritchard C, Slim G, Butler PJG, Karn J & Gait M (1993) Hydrogen bonding contacts in the major groove are required for human immunodeficiency virus type 1 Tat protein recognition of TAR RNA. J Mol Biol 230, 111-123.
    • (1993) J Mol Biol , vol.230 , pp. 111-123
    • Hamy, F.1    Asseline, V.2    Grasby, J.3    Iwai, S.4    Pritchard, C.5    Slim, G.6    Butler, P.J.G.7    Karn, J.8    Gait, M.9
  • 25
    • 0031614914 scopus 로고    scopus 로고
    • Independent ligand-induced folding of the RNA-binding domain and two functionally distinct antitermination regions in the phage λ N protein
    • Mogridge J, Legault P, Li J, Van Oene MD, Kay LE & Greenblatt J (1998) Independent Ligand-Induced Folding of the RNA-Binding Domain and Two Functionally Distinct Antitermination Regions in the Phage λ N Protein. Mol Cell 1, 265-275.
    • (1998) Mol Cell , vol.1 , pp. 265-275
    • Mogridge, J.1    Legault, P.2    Li, J.3    Van Oene, M.D.4    Kay, L.E.5    Greenblatt, J.6
  • 27
    • 0031860374 scopus 로고    scopus 로고
    • RNA recognition by RNP proteins during RNA processing and maturation
    • Varani G & Nagai K (1998) RNA recognition by RNP proteins during RNA processing and maturation. Ann Rev Biophys Biomol Struct 27, 407-445.
    • (1998) Ann Rev Biophys Biomol Struct , vol.27 , pp. 407-445
    • Varani, G.1    Nagai, K.2
  • 28
    • 0028004607 scopus 로고
    • Crystal structure at 1.92 Å resolution of the RNA-binding domain of the U1A spliceosomal protein complexed with an RNA hairpin
    • Oubridge C, Ito N, Evans PR, Teo C-H & Nagai K (1994) Crystal structure at 1.92 Å resolution of the RNA-binding domain of the U1A spliceosomal protein complexed with an RNA hairpin. Nature 372, 432-438.
    • (1994) Nature , vol.372 , pp. 432-438
    • Oubridge, C.1    Ito, N.2    Evans, P.R.3    Teo, C.-H.4    Nagai, K.5
  • 29
    • 0029920331 scopus 로고    scopus 로고
    • Specificity of ribonucleoprotein interaction determined by RNA folding during complex formation
    • Allain F-HT, Gubser CC, Howe PWA, Nagai K, Neuhaus D & Varani G (1996) Specificity of ribonucleoprotein interaction determined by RNA folding during complex formation. Nature 380, 646-650.
    • (1996) Nature , vol.380 , pp. 646-650
    • Allain, F.-H.T.1    Gubser, C.C.2    Howe, P.W.A.3    Nagai, K.4    Neuhaus, D.5    Varani, G.6
  • 30
    • 0034672094 scopus 로고    scopus 로고
    • Molecular basis of sequence-specific recognition of pre-ribosomal RNA by nucleolin
    • Allain FH-T, Bouvet P, Dieckmann T & Feigon J (2000) Molecular basis of sequence-specific recognition of pre-ribosomal RNA by nucleolin. EMBO J 19, 6870-6881.
    • (2000) EMBO J , vol.19 , pp. 6870-6881
    • Allain, F.H.-T.1    Bouvet, P.2    Dieckmann, T.3    Feigon, J.4
  • 31
    • 3042737403 scopus 로고    scopus 로고
    • U2AF homology motifs: Protein recognition in the RRM world
    • Kielkop CL, Lücke S & Green MR (2004) U2AF homology motifs: protein recognition in the RRM world. Genes Dev 18, 1513-1526.
    • (2004) Genes Dev , vol.18 , pp. 1513-1526
    • Kielkop, C.L.1    Lücke, S.2    Green, M.R.3
  • 32
    • 0038298868 scopus 로고    scopus 로고
    • Structural basis for the molecular recognition between human splicing factors U2AF 65 and SF1/mBBP
    • Selenko P, Gregorovic G, Sprangeers R, Stier G, Rhani Z, Kramer A & Sattler M (2003) Structural basis for the molecular recognition between human splicing factors U2AF 65 and SF1/mBBP. Mol Cell 11, 965-976.
    • (2003) Mol Cell , vol.11 , pp. 965-976
    • Selenko, P.1    Gregorovic, G.2    Sprangeers, R.3    Stier, G.4    Rhani, Z.5    Kramer, A.6    Sattler, M.7
  • 34
    • 0027105279 scopus 로고
    • Two RNA-binding motifs in the double-stranded RNA-activated protein kinase, DAI
    • Green SR & Matthews MB (1992) Two RNA-binding motifs in the double-stranded RNA-activated protein kinase, DAI. Genes Dev 6, 2478-2490.
    • (1992) Genes Dev , vol.6 , pp. 2478-2490
    • Green, S.R.1    Matthews, M.B.2
  • 35
    • 0034192148 scopus 로고    scopus 로고
    • Proteins binding to duplexed RNA: One motif, multiple functions
    • Fierro-Monti I & Mathwes MB (2000) Proteins binding to duplexed RNA: one motif, multiple functions. Trends Biochem Sci 25, 241-246.
    • (2000) Trends Biochem Sci , vol.25 , pp. 241-246
    • Fierro-Monti, I.1    Mathwes, M.B.2
  • 36
    • 0029782652 scopus 로고    scopus 로고
    • Minor-groove recognition of the double-stranded RNA-binding domain from the RNA-activated protein kinase PKR
    • Bevilacqua PC & Cech TR (1996) Minor-groove recognition of the double-stranded RNA-binding domain from the RNA-activated protein kinase PKR. Biochemistry 35, 9983-9994.
    • (1996) Biochemistry , vol.35 , pp. 9983-9994
    • Bevilacqua, P.C.1    Cech, T.R.2
  • 37
    • 0032485912 scopus 로고    scopus 로고
    • Binding of the protein kinase PKR to RNAs with secondary structure defects: Role of the tandem A-G mismatch and noncontiguous helixes
    • Bevilacqua PC, George CX, Samuel CE & Cech TR (1998) Binding of the protein kinase PKR to RNAs with secondary structure defects: role of the tandem A-G mismatch and noncontiguous helixes. Biochemistry 37, 6303-6316.
    • (1998) Biochemistry , vol.37 , pp. 6303-6316
    • Bevilacqua, P.C.1    George, C.X.2    Samuel, C.E.3    Cech, T.R.4
  • 39
    • 0028639195 scopus 로고
    • Staufen protein associates with the 3′UTR of bicoid mRNA to form particles that move in a microtubule-dependent manner
    • Ferrandon D, Elphick L, Nüsslein-Volhard C & St Johnston D (1994) Staufen protein associates with the 3′UTR of bicoid mRNA to form particles that move in a microtubule-dependent manner. Cell 79, 1221-1232.
    • (1994) Cell , vol.79 , pp. 1221-1232
    • Ferrandon, D.1    Elphick, L.2    Nüsslein-Volhard, C.3    St. Johnston, D.4
  • 41
    • 0036276292 scopus 로고    scopus 로고
    • A physical interaction between Gar1p and Rnt1p is required for the nuclear import of H/ACA small nucleolar RNA-associated proteins
    • Tremblay A, Lamontagne B, Catala M, Yam Y, Larose S, Good L & Abou Elela S (2002) A physical interaction between Gar1p and Rnt1p is required for the nuclear import of H/ACA small nucleolar RNA-associated proteins. Mol Cell Biol 22, 4792-4802.
    • (2002) Mol Cell Biol , vol.22 , pp. 4792-4802
    • Tremblay, A.1    Lamontagne, B.2    Catala, M.3    Yam, Y.4    Larose, S.5    Good, L.6    Abou Elela, S.7
  • 42
    • 2442679207 scopus 로고    scopus 로고
    • Structural basis for overhang-specific small interfering RNA recognition by the PAZ domain
    • Ma JB, Ye K & Patel DJ (2004) Structural basis for overhang-specific small interfering RNA recognition by the PAZ domain. Nature 429, 318-322.
    • (2004) Nature , vol.429 , pp. 318-322
    • Ma, J.B.1    Ye, K.2    Patel, D.J.3
  • 43
    • 2542461104 scopus 로고    scopus 로고
    • Structural basis for 3′-end recognition of nucleic acids by the Drosophila Argonaute2 PAZ domain
    • Lingel A, Simon B, Izaurralde E & Sattler M (2004) Structural basis for 3′-end recognition of nucleic acids by the Drosophila Argonaute2 PAZ domain. Nat Struct Mol Biol 11, 576-577.
    • (2004) Nat Struct Mol Biol , vol.11 , pp. 576-577
    • Lingel, A.1    Simon, B.2    Izaurralde, E.3    Sattler, M.4
  • 44
    • 0345359925 scopus 로고    scopus 로고
    • The Argonaute2 PAZ domain adopts a novel nucleic acid binding fold
    • Lingel A, Simon B, Izaurralde E & Sattler M (2003) The Argonaute2 PAZ domain adopts a novel nucleic acid binding fold. Nature 426, 465-469.
    • (2003) Nature , vol.426 , pp. 465-469
    • Lingel, A.1    Simon, B.2    Izaurralde, E.3    Sattler, M.4
  • 45
    • 0642345790 scopus 로고    scopus 로고
    • Structure and conserved RNA binding of the PAZ domain
    • Van KS, Van S, Farooq A, Han A, Zeng L & Zhou M (2003) Structure and conserved RNA binding of the PAZ domain. Nature 426, 468-474.
    • (2003) Nature , vol.426 , pp. 468-474
    • Van, K.S.1    Van, S.2    Farooq, A.3    Han, A.4    Zeng, L.5    Zhou, M.6
  • 46
    • 4444302947 scopus 로고    scopus 로고
    • Crystal structure of Argonaute and its implications for RISC sheer activity
    • Song J-J, Smith SK, Hannon GJ & Joshua-Tor L (2004) Crystal structure of Argonaute and its implications for RISC sheer activity. Science 305, 1434-1437.
    • (2004) Science , vol.305 , pp. 1434-1437
    • Song, J.-J.1    Smith, S.K.2    Hannon, G.J.3    Joshua-Tor, L.4
  • 49
    • 0031024655 scopus 로고    scopus 로고
    • The RNA binding domain of ribosomal protein L11 is structurally similar to homeodomains
    • Xing Y, GuhaThakurta D & Draper DE (1997) The RNA binding domain of ribosomal protein L11 is structurally similar to homeodomains. Nat Struct Biol 4, 24-27.
    • (1997) Nat Struct Biol , vol.4 , pp. 24-27
    • Xing, Y.1    GuhaThakurta, D.2    Draper, D.E.3
  • 50
    • 0033553625 scopus 로고    scopus 로고
    • Crystal structure of a conserved ribosomal protein-RNA complex
    • Conn GL, Draper DE, Lattman EE & Gittis AG (1999) Crystal structure of a conserved ribosomal protein-RNA complex. Science 284, 1171-1174.
    • (1999) Science , vol.284 , pp. 1171-1174
    • Conn, G.L.1    Draper, D.E.2    Lattman, E.E.3    Gittis, A.G.4
  • 51
    • 0033553439 scopus 로고    scopus 로고
    • A detailed view of a ribosomal active site: The structure of the L11-RNA complex
    • Wimberly BT, Guymon R, McCutcheon JP, White SW & Ramakrishnan V (1999) A detailed view of a ribosomal active site: the structure of the L11-RNA complex. Cell 97, 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
  • 52
    • 0029099218 scopus 로고
    • Eleven down and nine to go
    • Cusack S (1995) Eleven down and nine to go. Nat Struct Biol 2, 824-831.
    • (1995) Nat Struct Biol , vol.2 , pp. 824-831
    • Cusack, S.1
  • 54
    • 0028225137 scopus 로고
    • A Novel RNA-binding motif in omnipresent suppressors of translational termination, ribosomal proteins and a ribosome modification enzyme
    • Koonin EV, Bork P & Sander C (1994) A Novel RNA-binding motif in omnipresent suppressors of translational termination, ribosomal proteins and a ribosome modification enzyme. Nucleic Acids Res 22, 2166-2167.
    • (1994) Nucleic Acids Res , vol.22 , pp. 2166-2167
    • Koonin, E.V.1    Bork, P.2    Sander, C.3
  • 55
    • 0034509631 scopus 로고    scopus 로고
    • Crystal structure of the spliceosomal 15.5kD protein bound to a U4 snRNA fragment
    • Vidovic I, Nottrott S, Kartmuth K, Lührmann R & Ficner R (2000) Crystal structure of the spliceosomal 15.5kD protein bound to a U4 snRNA fragment. Mol Cell 6, 1331-1342.
    • (2000) Mol Cell , vol.6 , pp. 1331-1342
    • Vidovic, I.1    Nottrott, S.2    Kartmuth, K.3    Lührmann, R.4    Ficner, R.5
  • 56
    • 0035423087 scopus 로고    scopus 로고
    • The kink-turn: A new RNA secondary structure motif
    • Klein DJ, Schmeing TM, Moore PB & Steitz TA (2001) The kink-turn: a new RNA secondary structure motif. EMBO J 20, 4214-4221.
    • (2001) EMBO J , vol.20 , pp. 4214-4221
    • Klein, D.J.1    Schmeing, T.M.2    Moore, P.B.3    Steitz, T.A.4
  • 57
    • 0027280280 scopus 로고
    • TFIIIA: Nine fingers - Three hands?
    • Pieler T & Theunissen O (1993) TFIIIA: nine fingers - three hands? Trends Biochem Sci 18, 226-230.
    • (1993) Trends Biochem Sci , vol.18 , pp. 226-230
    • Pieler, T.1    Theunissen, O.2
  • 59
    • 0242581682 scopus 로고    scopus 로고
    • Crystal structure of a zinc-finger-RNA complex reveals two modes of molecular recognition
    • Lu D, Searles MA & Klug A (2003) Crystal structure of a zinc-finger-RNA complex reveals two modes of molecular recognition. Nature 426, 96-100.
    • (2003) Nature , vol.426 , pp. 96-100
    • Lu, D.1    Searles, M.A.2    Klug, A.3
  • 63
    • 0035917508 scopus 로고    scopus 로고
    • Structure of Pumilio reveals similarity between RNA and peptide binding motifs
    • Edwards TA, Pyle SE, Wharton RP & Aggarwal AK (2001) Structure of Pumilio reveals similarity between RNA and peptide binding motifs. Cell 105, 281-289.
    • (2001) Cell , vol.105 , pp. 281-289
    • Edwards, T.A.1    Pyle, S.E.2    Wharton, R.P.3    Aggarwal, A.K.4
  • 64
  • 65
    • 0035022798 scopus 로고    scopus 로고
    • Crystal structure of a Pumilio homology domain
    • Wang X, Zamore PD & Tanaka-Hall TM (2001) Crystal structure of a Pumilio homology domain. Mol Cell 7, 855-865.
    • (2001) Mol Cell , vol.7 , pp. 855-865
    • Wang, X.1    Zamore, P.D.2    Tanaka-Hall, T.M.3
  • 66
    • 0037162703 scopus 로고    scopus 로고
    • Modular recognition of RNA by a human Pumilio-homology domain
    • Wang X, McLachlan J, Zamore PD & Tanaka-Hall TM (2002) Modular recognition of RNA by a human Pumilio-homology domain. Cell 110, 501-512.
    • (2002) Cell , vol.110 , pp. 501-512
    • Wang, X.1    McLachlan, J.2    Zamore, P.D.3    Tanaka-Hall, T.M.4
  • 67
    • 0033524941 scopus 로고    scopus 로고
    • Crystal structures of two Sm protein complexes and their implications for the assembly of the spliceosomal snRNPs
    • Kambach C, Walke S, Young R, Avis JM, de la Fortelle E, Raker VA, Lührmann R, Li J & Nagai K (1999) Crystal structures of two Sm protein complexes and their implications for the assembly of the spliceosomal snRNPs. Cell 96, 375-387.
    • (1999) Cell , vol.96 , pp. 375-387
    • Kambach, C.1    Walke, S.2    Young, R.3    Avis, J.M.4    De La Fortelle, E.5    Raker, V.A.6    Lührmann, R.7    Li, J.8    Nagai, K.9
  • 68
    • 0036645689 scopus 로고    scopus 로고
    • Structures of the pleiotropic translational regulator Hfq and an Hfq-RNA complex: A bacterial Sm-like protein
    • Schumacher MA, Pearson RF, Moller T, Valentin-Hansen P & Brennan RG (2002) Structures of the pleiotropic translational regulator Hfq and an Hfq-RNA complex: a bacterial Sm-like protein. EMBO J 21, 3546-3556.
    • (2002) EMBO J , vol.21 , pp. 3546-3556
    • Schumacher, M.A.1    Pearson, R.F.2    Moller, T.3    Valentin-Hansen, P.4    Brennan, R.G.5
  • 69
    • 3142564584 scopus 로고    scopus 로고
    • The small RNA chaperone Hfq and multiple small RNAs control quorum sensing in Vibrio harveyi and Vibrio cholerae
    • Lenz DH, Mok KC, Lilley BN, Kulkarni RV, Wingreen NS & Bassler BL (2004) The small RNA chaperone Hfq and multiple small RNAs control quorum sensing in Vibrio harveyi and Vibrio cholerae. Cell 118, 69-82.
    • (2004) Cell , vol.118 , pp. 69-82
    • Lenz, D.H.1    Mok, K.C.2    Lilley, B.N.3    Kulkarni, R.V.4    Wingreen, N.S.5    Bassler, B.L.6
  • 70
    • 0037428440 scopus 로고    scopus 로고
    • Crystal structures of the Pyrococcus abyssi Sm core and its complex with RNA
    • Thore S, Matyer C, Sauter C, Weeks S & Suck D (2003) Crystal structures of the Pyrococcus abyssi Sm core and its complex with RNA. J Biol Chem 278, 1239-1247.
    • (2003) J Biol Chem , vol.278 , pp. 1239-1247
    • Thore, S.1    Matyer, C.2    Sauter, C.3    Weeks, S.4    Suck, D.5
  • 71
    • 0034673638 scopus 로고    scopus 로고
    • An RNA-directed nuclease mediates post-transcriptional gene silencing in Drosophila cells
    • Hammond SM, Bernstein E, Beach D & Hannon GJ (2000) An RNA-directed nuclease mediates post-transcriptional gene silencing in Drosophila cells. Nature 404, 293-296.
    • (2000) Nature , vol.404 , pp. 293-296
    • Hammond, S.M.1    Bernstein, E.2    Beach, D.3    Hannon, G.J.4
  • 72
    • 1442360415 scopus 로고    scopus 로고
    • RNase III enzymes and the initiation of gene silencing
    • Carmell MA & Hannon GJ (2004) RNase III enzymes and the initiation of gene silencing. Nat Struct Mol Biol 11, 214-218.
    • (2004) Nat Struct Mol Biol , vol.11 , pp. 214-218
    • Carmell, M.A.1    Hannon, G.J.2
  • 73
    • 0035966271 scopus 로고    scopus 로고
    • Cocrystal structure of a tRNA Y55 pseudouridine synthase: Nucleotide flipping by an RNA-modifying enzyme
    • Hoang C & Ferré-D'Amaré AR (2001) Cocrystal structure of a tRNA Y55 pseudouridine synthase: nucleotide flipping by an RNA-modifying enzyme. Cell 107, 929-939.
    • (2001) Cell , vol.107 , pp. 929-939
    • Hoang, C.1    Ferré-D'Amaré, A.R.2
  • 75
    • 0028873824 scopus 로고
    • Dissecting RNA-protein interactions: RNA-RNA Recognition by Rop
    • Predki PF, Nayak LM, Gottlieb MBC & Regan L (1995) Dissecting RNA-protein interactions: RNA-RNA Recognition by Rop. Cell 80, 41-50.
    • (1995) Cell , vol.80 , pp. 41-50
    • Predki, P.F.1    Nayak, L.M.2    Gottlieb, M.B.C.3    Regan, L.4
  • 76
    • 0033578927 scopus 로고    scopus 로고
    • Recognition of Polyadenylate RNA by the poly(A)-binding protein
    • Deo RC, Bonanno JB, Sonenberg N & Burley SK (1999) Recognition of Polyadenylate RNA by the poly(A)-binding protein. Cell 98, 835-845.
    • (1999) Cell , vol.98 , pp. 835-845
    • Deo, R.C.1    Bonanno, J.B.2    Sonenberg, N.3    Burley, S.K.4
  • 77
    • 0035153840 scopus 로고    scopus 로고
    • Structural basis for recognition of AU-rich element RNA by Hu proteins
    • Wang X & Tanaka-Hall TM (2001) Structural basis for recognition of AU-rich element RNA by Hu proteins. Nat Struct Biol 8, 141-146.
    • (2001) Nat Struct Biol , vol.8 , pp. 141-146
    • Wang, X.1    Tanaka-Hall, T.M.2
  • 78
    • 0034603208 scopus 로고    scopus 로고
    • Sequence-specific RNA binding by a nova KH domain: Implications for para-neoplastic disease and the fragile X syndrome
    • Lewis HA, Musunuru K, Jensen KB, Edo C, Chen H, Darnell RB & Burley SK (2000) Sequence-specific RNA binding by a nova KH domain: implications for para-neoplastic disease and the fragile X syndrome. Cell 100, 323-332.
    • (2000) Cell , vol.100 , pp. 323-332
    • Lewis, H.A.1    Musunuru, K.2    Jensen, K.B.3    Edo, C.4    Chen, H.5    Darnell, R.B.6    Burley, S.K.7
  • 80
    • 3042704491 scopus 로고    scopus 로고
    • Structural basis for recognition of the AGNN tetraloop RNA fold by the double-stranded RNA-binding domain of Rnt1p RNase III
    • Wu H, Henras A, Chanfreau G & Feigon J (2004) Structural basis for recognition of the AGNN tetraloop RNA fold by the double-stranded RNA-binding domain of Rnt1p RNase III. Proc Natl Acact Sci USA 101, 8307-8312.
    • (2004) Proc Natl Acact Sci USA , vol.101 , pp. 8307-8312
    • Wu, H.1    Henras, A.2    Chanfreau, G.3    Feigon, J.4
  • 81
    • 0035662491 scopus 로고    scopus 로고
    • Crystallographic and modeling studies of RNase III suggest a mechanism for double-stranded RNA cleavage
    • Blaszczyk J, Tropea JE, Bubunenko M, Routzahn KM, Waugh DS, Court DL & Ji X (2001) Crystallographic and modeling studies of RNase III suggest a mechanism for double-stranded RNA cleavage. Structure 9, 1225-1236.
    • (2001) Structure , vol.9 , pp. 1225-1236
    • Blaszczyk, J.1    Tropea, J.E.2    Bubunenko, M.3    Routzahn, K.M.4    Waugh, D.S.5    Court, D.L.6    Ji, X.7
  • 83
    • 0029041105 scopus 로고
    • NMR solution structure of a dsRNA binding domain from Drosophila Staufen protein reveals homology to the N-terminal domain of ribosomal protein S5
    • Bycroft M, Grünert S, Murzin AG, Proctor M & St Johnston D (1995) NMR solution structure of a dsRNA binding domain from Drosophila Staufen protein reveals homology to the N-terminal domain of ribosomal protein S5. EMBO J 14, 3563-3571.
    • (1995) EMBO J , vol.14 , pp. 3563-3571
    • Bycroft, M.1    Grünert, S.2    Murzin, A.G.3    Proctor, M.4    St. Johnston, D.5
  • 85
    • 0031471204 scopus 로고    scopus 로고
    • The solution structure of the S1 RNA binding domain: A member of an ancient nucleic acid binding fold
    • Bycroft M, Hubbard TJP, Proctor M, Freund SMV & Murzin AG (1997) The solution structure of the S1 RNA binding domain: a member of an ancient nucleic acid binding fold. Cell 88, 235-242.
    • (1997) Cell , vol.88 , pp. 235-242
    • Bycroft, M.1    Hubbard, T.J.P.2    Proctor, M.3    Freund, S.M.V.4    Murzin, A.G.5
  • 87
    • 0028828745 scopus 로고
    • Crystal structure of the MATα1/MATα2 homeodomain heterodimer bound to DNA
    • Li T, Stark MR, Johnson AD & Wolberger C (1995) Crystal structure of the MATα1/MATα2 homeodomain heterodimer bound to DNA. Science 270, 262-269.
    • (1995) Science , vol.270 , pp. 262-269
    • Li, T.1    Stark, M.R.2    Johnson, A.D.3    Wolberger, C.4


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.