메뉴 건너뛰기




Volumn 70, Issue 11, 2013, Pages 1875-1895

RNA recognition by double-stranded RNA binding domains: A matter of shape and sequence

Author keywords

dsRBD; dsRBD extensions; dsRBM; dsRNA; Nuclear localization signal; Nuclear retention; Nucleic acids recognition; Protein RNA interactions; Protein RNA recognition; RNA editing; RNA interference; RNA minor groove; RNA processing; Sequence specificity; Structures

Indexed keywords

DOUBLE STRANDED DNA;

EID: 84878270899     PISSN: 1420682X     EISSN: 14209071     Source Type: Journal    
DOI: 10.1007/s00018-012-1119-x     Document Type: Review
Times cited : (203)

References (118)
  • 1
    • 0025876881 scopus 로고
    • Characterization of a human TAR RNA-binding protein that activates the HIV-1 LTR
    • 2011739 1:CAS:528:DyaK3MXlslKgs7w%3D 10.1126/science.2011739
    • A Gatignol A Buckler-White B Berkhout KT Jeang 1991 Characterization of a human TAR RNA-binding protein that activates the HIV-1 LTR Science 251 5001 1597 1600 2011739 1:CAS:528:DyaK3MXlslKgs7w%3D 10.1126/science.2011739
    • (1991) Science , vol.251 , Issue.5001 , pp. 1597-1600
    • Gatignol, A.1    Buckler-White, A.2    Berkhout, B.3    Jeang, K.T.4
  • 2
    • 0028639195 scopus 로고
    • Staufen protein associates with the 3′UTR of bicoid mRNA to form particles that move in a microtubule-dependent manner
    • 8001156 1:STN:280:DyaK2M%2FpsVaqtQ%3D%3D 10.1016/0092-8674(94)90013-2
    • D Ferrandon L Elphick C Nüsslein-Volhard D St Johnston 1994 Staufen protein associates with the 3′UTR of bicoid mRNA to form particles that move in a microtubule-dependent manner Cell 79 7 1221 1232 8001156 1:STN:280:DyaK2M%2FpsVaqtQ%3D%3D 10.1016/0092-8674(94)90013-2
    • (1994) Cell , vol.79 , Issue.7 , pp. 1221-1232
    • Ferrandon, D.1    Elphick, L.2    Nüsslein-Volhard, C.3    St Johnston, D.4
  • 3
    • 0027772363 scopus 로고
    • RNA editing of AMPA receptor subunit GluR-B: A base-paired intron-exon structure determines position and efficiency
    • 8269514 1:CAS:528:DyaK2cXntVOqsA%3D%3D 10.1016/0092-8674(93)90622-W
    • M Higuchi FN Single M Köhler B Sommer R Sprengel PH Seeburg 1993 RNA editing of AMPA receptor subunit GluR-B: a base-paired intron-exon structure determines position and efficiency Cell 75 7 1361 1370 8269514 1:CAS:528:DyaK2cXntVOqsA%3D%3D 10.1016/0092-8674(93)90622-W
    • (1993) Cell , vol.75 , Issue.7 , pp. 1361-1370
    • Higuchi, M.1    Single, F.N.2    Köhler, M.3    Sommer, B.4    Sprengel, R.5    Seeburg, P.H.6
  • 4
    • 0032932638 scopus 로고    scopus 로고
    • Function, mechanism and regulation of bacterial ribonucleases
    • 10371039 1:CAS:528:DyaK1MXjsVSju74%3D 10.1111/j.1574-6976.1999.tb00405.x
    • AW Nicholson 1999 Function, mechanism and regulation of bacterial ribonucleases FEMS Microbiol Rev 23 3 371 390 10371039 1:CAS:528: DyaK1MXjsVSju74%3D 10.1111/j.1574-6976.1999.tb00405.x
    • (1999) FEMS Microbiol Rev , vol.23 , Issue.3 , pp. 371-390
    • Nicholson, A.W.1
  • 5
    • 0035905766 scopus 로고    scopus 로고
    • Role for a bidentate ribonuclease in the initiation step of RNA interference
    • 11201747 1:CAS:528:DC%2BD3MXms12ksA%3D%3D 10.1038/35053110
    • E Bernstein AA Caudy SM Hammond GJ Hannon 2001 Role for a bidentate ribonuclease in the initiation step of RNA interference Nature 409 6818 363 366 11201747 1:CAS:528:DC%2BD3MXms12ksA%3D%3D 10.1038/35053110
    • (2001) Nature , vol.409 , Issue.6818 , pp. 363-366
    • Bernstein, E.1    Caudy, A.A.2    Hammond, S.M.3    Hannon, G.J.4
  • 6
    • 0035800521 scopus 로고    scopus 로고
    • A cellular function for the RNA-interference enzyme Dicer in the maturation of the let-7 small temporal RNA
    • 11452083 10.1126/science.1062961
    • G Hutvágner J McLachlan AE Pasquinelli E Bálint T Tuschl PD Zamore 2001 A cellular function for the RNA-interference enzyme Dicer in the maturation of the let-7 small temporal RNA Science 293 5531 834 838 11452083 10.1126/science.1062961
    • (2001) Science , vol.293 , Issue.5531 , pp. 834-838
    • Hutvágner, G.1    McLachlan, J.2    Pasquinelli, A.E.3    Bálint, E.4    Tuschl, T.5    Zamore, P.D.6
  • 7
    • 60149088848 scopus 로고    scopus 로고
    • Origins and mechanisms of miRNAs and siRNAs
    • 19239886 1:CAS:528:DC%2BD1MXkvFGksb0%3D 10.1016/j.cell.2009.01.035
    • RW Carthew EJ Sontheimer 2009 Origins and mechanisms of miRNAs and siRNAs Cell 136 4 642 655 19239886 1:CAS:528:DC%2BD1MXkvFGksb0%3D 10.1016/j.cell.2009. 01.035
    • (2009) Cell , vol.136 , Issue.4 , pp. 642-655
    • Carthew, R.W.1    Sontheimer, E.J.2
  • 8
    • 0034192148 scopus 로고    scopus 로고
    • Proteins binding to duplexed RNA: One motif, multiple functions
    • 10782096 1:CAS:528:DC%2BD3cXjtVeru7c%3D 10.1016/S0968-0004(00)01580-2
    • I Fierro-Monti MB Mathews 2000 Proteins binding to duplexed RNA: one motif, multiple functions Trends Biochem Sci 25 5 241 246 10782096 1:CAS:528:DC%2BD3cXjtVeru7c%3D 10.1016/S0968-0004(00)01580-2
    • (2000) Trends Biochem Sci , vol.25 , Issue.5 , pp. 241-246
    • Fierro-Monti, I.1    Mathews, M.B.2
  • 9
    • 0037711199 scopus 로고    scopus 로고
    • The dsRNA binding protein family: Critical roles, diverse cellular functions
    • 12773480 1:CAS:528:DC%2BD3sXktl2htLg%3D 10.1096/fj.02-0958rev
    • LR Saunders GN Barber 2003 The dsRNA binding protein family: critical roles, diverse cellular functions FASEB J 17 9 961 983 12773480 1:CAS:528:DC%2BD3sXktl2htLg%3D 10.1096/fj.02-0958rev
    • (2003) FASEB J , vol.17 , Issue.9 , pp. 961-983
    • Saunders, L.R.1    Barber, G.N.2
  • 10
    • 10044246238 scopus 로고    scopus 로고
    • The double-stranded-RNA-binding motif: Interference and much more
    • 15573138 1:CAS:528:DC%2BD2cXhtVarsbzK 10.1038/nrm1528
    • B Tian PC Bevilacqua A Diegelman-Parente MB Mathews 2004 The double-stranded-RNA-binding motif: interference and much more Nat Rev Mol Cell Biol 5 12 1013 1023 15573138 1:CAS:528:DC%2BD2cXhtVarsbzK 10.1038/nrm1528
    • (2004) Nat Rev Mol Cell Biol , vol.5 , Issue.12 , pp. 1013-1023
    • Tian, B.1    Bevilacqua, P.C.2    Diegelman-Parente, A.3    Mathews, M.B.4
  • 11
    • 18544377013 scopus 로고    scopus 로고
    • The RNA recognition motif, a plastic RNA-binding platform to regulate post-transcriptional gene expression
    • 15853797 1:CAS:528:DC%2BD2MXktlCqtr8%3D 10.1111/j.1742-4658.2005.04653.x
    • C Maris C Dominguez FH-T Allain 2005 The RNA recognition motif, a plastic RNA-binding platform to regulate post-transcriptional gene expression FEBS J 272 9 2118 2131 15853797 1:CAS:528:DC%2BD2MXktlCqtr8%3D 10.1111/j.1742-4658. 2005.04653.x
    • (2005) FEBS J , vol.272 , Issue.9 , pp. 2118-2131
    • Maris, C.1    Dominguez, C.2    Allain, F.-T.3
  • 12
    • 13844297911 scopus 로고    scopus 로고
    • Zinc finger proteins: Getting a grip on RNA
    • 15718139 1:CAS:528:DC%2BD2MXhsFShtLw%3D 10.1016/j.sbi.2005.01.006
    • RS Brown 2005 Zinc finger proteins: getting a grip on RNA Curr Opin Struct Biol 15 1 94 98 15718139 1:CAS:528:DC%2BD2MXhsFShtLw%3D 10.1016/j.sbi.2005.01.006
    • (2005) Curr Opin Struct Biol , vol.15 , Issue.1 , pp. 94-98
    • Brown, R.S.1
  • 13
    • 20444495969 scopus 로고    scopus 로고
    • Multiple modes of RNA recognition by zinc finger proteins
    • 15963892 1:CAS:528:DC%2BD2MXlt1Srsbw%3D 10.1016/j.sbi.2005.04.004
    • TM Hall 2005 Multiple modes of RNA recognition by zinc finger proteins Curr Opin Struct Biol 15 3 367 373 15963892 1:CAS:528:DC%2BD2MXlt1Srsbw%3D 10.1016/j.sbi.2005.04.004
    • (2005) Curr Opin Struct Biol , vol.15 , Issue.3 , pp. 367-373
    • Hall, T.M.1
  • 14
    • 0242581682 scopus 로고    scopus 로고
    • Crystal structure of a zinc-finger-RNA complex reveals two modes of molecular recognition
    • 14603324 1:CAS:528:DC%2BD3sXoslSjtbk%3D 10.1038/nature02088
    • D Lu MA Searles A Klug 2003 Crystal structure of a zinc-finger-RNA complex reveals two modes of molecular recognition Nature 426 6962 96 100 14603324 1:CAS:528:DC%2BD3sXoslSjtbk%3D 10.1038/nature02088
    • (2003) Nature , vol.426 , Issue.6962 , pp. 96-100
    • Lu, D.1    Searles, M.A.2    Klug, A.3
  • 15
    • 32244447225 scopus 로고    scopus 로고
    • Shape-specific recognition in the structure of the Vts1p SAM domain with RNA
    • 16429156 1:CAS:528:DC%2BD28XhtFajsL8%3D 10.1038/nsmb1038
    • FC Oberstrass A Lee R Stefl M Janis G Chanfreau FH Allain 2006 Shape-specific recognition in the structure of the Vts1p SAM domain with RNA Nat Struct Mol Biol 13 2 160 167 16429156 1:CAS:528:DC%2BD28XhtFajsL8%3D 10.1038/nsmb1038
    • (2006) Nat Struct Mol Biol , vol.13 , Issue.2 , pp. 160-167
    • Oberstrass, F.C.1    Lee, A.2    Stefl, R.3    Janis, M.4    Chanfreau, G.5    Allain, F.H.6
  • 16
    • 32244436130 scopus 로고    scopus 로고
    • Sequence-specific recognition of RNA hairpins by the SAM domain of Vts1p
    • 16429151 1:CAS:528:DC%2BD28XhtFajtrw%3D 10.1038/nsmb1053
    • T Aviv Z Lin G Ben-Ari CA Smibert F Sicheri 2006 Sequence-specific recognition of RNA hairpins by the SAM domain of Vts1p Nat Struct Mol Biol 13 2 168 176 16429151 1:CAS:528:DC%2BD28XhtFajtrw%3D 10.1038/nsmb1053
    • (2006) Nat Struct Mol Biol , vol.13 , Issue.2 , pp. 168-176
    • Aviv, T.1    Lin, Z.2    Ben-Ari, G.3    Smibert, C.A.4    Sicheri, F.5
  • 17
    • 81855205059 scopus 로고    scopus 로고
    • ADAR proteins: Double-stranded RNA and Z-DNA binding domains
    • 21728134 1:CAS:528:DC%2BC38XhsFCqs7fF 10.1007/82-2011-145
    • P Barraud FH-T Allain 2012 ADAR proteins: double-stranded RNA and Z-DNA binding domains Curr Top Microbiol Immunol 353 35 60 21728134 1:CAS:528:DC%2BC38XhsFCqs7fF 10.1007/82-2011-145
    • (2012) Curr Top Microbiol Immunol , vol.353 , pp. 35-60
    • Barraud, P.1    Allain, F.-T.2
  • 18
    • 0033546005 scopus 로고    scopus 로고
    • Crystal structure of the Zalpha domain of the human editing enzyme ADAR1 bound to left-handed Z-DNA
    • 10364558 1:CAS:528:DyaK1MXjvFSqtr4%3D 10.1126/science.284.5421.1841
    • T Schwartz MA Rould K Lowenhaupt A Herbert A Rich 1999 Crystal structure of the Zalpha domain of the human editing enzyme ADAR1 bound to left-handed Z-DNA Science 284 5421 1841 1845 10364558 1:CAS:528:DyaK1MXjvFSqtr4%3D 10.1126/science.284.5421.1841
    • (1999) Science , vol.284 , Issue.5421 , pp. 1841-1845
    • Schwartz, T.1    Rould, M.A.2    Lowenhaupt, K.3    Herbert, A.4    Rich, A.5
  • 19
    • 34047263964 scopus 로고    scopus 로고
    • A left-handed RNA double helix bound by the Z alpha domain of the RNA-editing enzyme ADAR1
    • 17437712 1:CAS:528:DC%2BD2sXkt1aju7k%3D 10.1016/j.str.2007.03.001
    • D Placido BA Brown 2nd K Lowenhaupt A Rich A Athanasiadis 2007 A left-handed RNA double helix bound by the Z alpha domain of the RNA-editing enzyme ADAR1 Structure 15 4 395 404 17437712 1:CAS:528:DC%2BD2sXkt1aju7k%3D 10.1016/j.str.2007.03.001
    • (2007) Structure , vol.15 , Issue.4 , pp. 395-404
    • Placido, D.1    Brown II, B.A.2    Lowenhaupt, K.3    Rich, A.4    Athanasiadis, A.5
  • 20
    • 34047142206 scopus 로고    scopus 로고
    • The testis-specific human protein RBMY recognizes RNA through a novel mode of interaction
    • 17318228 1:CAS:528:DC%2BD2sXjs1yqtLo%3D 10.1038/sj.embor.7400910
    • L Skrisovska CF Bourgeois R Stefl SN Grellscheid L Kister P Wenter DJ Elliott J Stevenin FH Allain 2007 The testis-specific human protein RBMY recognizes RNA through a novel mode of interaction EMBO Rep 8 4 372 379 17318228 1:CAS:528:DC%2BD2sXjs1yqtLo%3D 10.1038/sj.embor.7400910
    • (2007) EMBO Rep , vol.8 , Issue.4 , pp. 372-379
    • Skrisovska, L.1    Bourgeois, C.F.2    Stefl, R.3    Grellscheid, S.N.4    Kister, L.5    Wenter, P.6    Elliott, D.J.7    Stevenin, J.8    Allain, F.H.9
  • 21
    • 0028004607 scopus 로고
    • Crystal structure at 1.92 A resolution of the RNA-binding domain of the U1A spliceosomal protein complexed with an RNA hairpin
    • 7984237 1:CAS:528:DyaK2MXisVGqsbg%3D 10.1038/372432a0
    • C Oubridge N Ito PR Evans CH Teo K Nagai 1994 Crystal structure at 1.92 A resolution of the RNA-binding domain of the U1A spliceosomal protein complexed with an RNA hairpin Nature 372 6505 432 438 7984237 1:CAS:528:DyaK2MXisVGqsbg%3D 10.1038/372432a0
    • (1994) Nature , vol.372 , Issue.6505 , pp. 432-438
    • Oubridge, C.1    Ito, N.2    Evans, P.R.3    Teo, C.H.4    Nagai, K.5
  • 22
    • 0029920331 scopus 로고    scopus 로고
    • Specificity of ribonucleoprotein interaction determined by RNA folding during complex formulation
    • 8602269 1:CAS:528:DyaK28XisVegurk%3D 10.1038/380646a0
    • FH Allain CC Gubser PW Howe K Nagai D Neuhaus G Varani 1996 Specificity of ribonucleoprotein interaction determined by RNA folding during complex formulation Nature 380 6575 646 650 8602269 1:CAS:528:DyaK28XisVegurk%3D 10.1038/380646a0
    • (1996) Nature , vol.380 , Issue.6575 , pp. 646-650
    • Allain, F.H.1    Gubser, C.C.2    Howe, P.W.3    Nagai, K.4    Neuhaus, D.5    Varani, G.6
  • 23
    • 0034672094 scopus 로고    scopus 로고
    • Molecular basis of sequence-specific recognition of pre-ribosomal RNA by nucleolin
    • 11118222 1:CAS:528:DC%2BD3MXns1amug%3D%3D 10.1093/emboj/19.24.6870
    • FH Allain P Bouvet T Dieckmann J Feigon 2000 Molecular basis of sequence-specific recognition of pre-ribosomal RNA by nucleolin EMBO J 19 24 6870 6881 11118222 1:CAS:528:DC%2BD3MXns1amug%3D%3D 10.1093/emboj/19.24.6870
    • (2000) EMBO J , vol.19 , Issue.24 , pp. 6870-6881
    • Allain, F.H.1    Bouvet, P.2    Dieckmann, T.3    Feigon, J.4
  • 24
    • 0003458038 scopus 로고
    • Springer New York 10.1007/978-1-4612-5190-3 Saenger W (1984) Principles of nucleic acid structure. Springer, New York
    • W Saenger 1984 Principles of nucleic acid structure Springer New York 10.1007/978-1-4612-5190-3 Saenger W (1984) Principles of nucleic acid structure. Springer, New York
    • (1984) Principles of Nucleic Acid Structure
    • Saenger, W.1
  • 25
    • 0000127073 scopus 로고
    • Sequence-specific recognition of double helical nucleic acids by proteins
    • 1062791 1:CAS:528:DyaE28XhsVKgsL8%3D 10.1073/pnas.73.3.804
    • NC Seeman JM Rosenberg A Rich 1976 Sequence-specific recognition of double helical nucleic acids by proteins Proc Natl Acad Sci USA 73 3 804 808 1062791 1:CAS:528:DyaE28XhsVKgsL8%3D 10.1073/pnas.73.3.804
    • (1976) Proc Natl Acad Sci USA , vol.73 , Issue.3 , pp. 804-808
    • Seeman, N.C.1    Rosenberg, J.M.2    Rich, A.3
  • 26
    • 0025280401 scopus 로고
    • Structural studies of protein-nucleic acid interaction: The sources of sequence-specific binding
    • 2204954 1:CAS:528:DyaK3cXlvVKltLo%3D 10.1017/S0033583500005552
    • TA Steitz 1990 Structural studies of protein-nucleic acid interaction: the sources of sequence-specific binding Q Rev Biophys 23 3 205 280 2204954 1:CAS:528:DyaK3cXlvVKltLo%3D 10.1017/S0033583500005552
    • (1990) Q Rev Biophys , vol.23 , Issue.3 , pp. 205-280
    • Steitz, T.A.1
  • 27
    • 18444380595 scopus 로고    scopus 로고
    • The double-stranded RNA-binding motif, a versatile macromolecular docking platform
    • 15853796 1:CAS:528:DC%2BD2MXkt1Wmtr0%3D 10.1111/j.1742-4658.2005.04652.x
    • K-Y Chang A Ramos 2005 The double-stranded RNA-binding motif, a versatile macromolecular docking platform FEBS J 272 9 2109 2117 15853796 1:CAS:528:DC%2BD2MXkt1Wmtr0%3D 10.1111/j.1742-4658.2005.04652.x
    • (2005) FEBS J , vol.272 , Issue.9 , pp. 2109-2117
    • Chang, K.-Y.1    Ramos, A.2
  • 28
    • 17844404891 scopus 로고    scopus 로고
    • RNA sequence- and shape-dependent recognition by proteins in the ribonucleoprotein particle
    • 15643449 1:CAS:528:DC%2BD2MXitVeqtQ%3D%3D 10.1038/sj.embor.7400325
    • R Stefl L Skrisovska FH-T Allain 2005 RNA sequence- and shape-dependent recognition by proteins in the ribonucleoprotein particle EMBO Rep 6 1 33 38 15643449 1:CAS:528:DC%2BD2MXitVeqtQ%3D%3D 10.1038/sj.embor.7400325
    • (2005) EMBO Rep , vol.6 , Issue.1 , pp. 33-38
    • Stefl, R.1    Skrisovska, L.2    Allain, F.-T.3
  • 29
    • 18444383371 scopus 로고    scopus 로고
    • Protein families and RNA recognition
    • 15853794 1:CAS:528:DC%2BD2MXkt1Wmtr8%3D 10.1111/j.1742-4658.2005.04650.x
    • Y Chen G Varani 2005 Protein families and RNA recognition FEBS J 272 9 2088 2097 15853794 1:CAS:528:DC%2BD2MXkt1Wmtr8%3D 10.1111/j.1742-4658.2005. 04650.x
    • (2005) FEBS J , vol.272 , Issue.9 , pp. 2088-2097
    • Chen, Y.1    Varani, G.2
  • 30
    • 77952293063 scopus 로고    scopus 로고
    • Functions and regulation of RNA editing by ADAR deaminases
    • 20192758 1:CAS:528:DC%2BC3cXpslShtr0%3D 10.1146/annurev-biochem-060208- 105251
    • K Nishikura 2010 Functions and regulation of RNA editing by ADAR deaminases Annu Rev Biochem 79 321 349 20192758 1:CAS:528:DC%2BC3cXpslShtr0%3D 10.1146/annurev-biochem-060208-105251
    • (2010) Annu Rev Biochem , vol.79 , pp. 321-349
    • Nishikura, K.1
  • 31
    • 0042838304 scopus 로고    scopus 로고
    • Recognition of double-stranded RNA by proteins and small molecules
    • 12925995 1:CAS:528:DC%2BD3sXntlKlu7c%3D 10.1002/bip.10413
    • CB Carlson OM Stephens PA Beal 2003 Recognition of double-stranded RNA by proteins and small molecules Biopolymers 70 1 86 102 12925995 1:CAS:528:DC%2BD3sXntlKlu7c%3D 10.1002/bip.10413
    • (2003) Biopolymers , vol.70 , Issue.1 , pp. 86-102
    • Carlson, C.B.1    Stephens, O.M.2    Beal, P.A.3
  • 32
    • 0036600739 scopus 로고    scopus 로고
    • RNA-protein interactions
    • 12127445 1:CAS:528:DC%2BD38Xlt1Siu7g%3D 10.1016/S0959-440X(02)00323-8
    • KB Hall 2002 RNA-protein interactions Curr Opin Struct Biol 12 3 283 288 12127445 1:CAS:528:DC%2BD38Xlt1Siu7g%3D 10.1016/S0959-440X(02)00323-8
    • (2002) Curr Opin Struct Biol , vol.12 , Issue.3 , pp. 283-288
    • Hall, K.B.1
  • 33
    • 0026480392 scopus 로고
    • A conserved double-stranded RNA-binding domain
    • 1438302 1:CAS:528:DyaK3sXkvV2ht70%3D 10.1073/pnas.89.22.10979
    • D St Johnston NH Brown JG Gall M Jantsch 1992 A conserved double-stranded RNA-binding domain Proc Natl Acad Sci USA 89 22 10979 10983 1438302 1:CAS:528:DyaK3sXkvV2ht70%3D 10.1073/pnas.89.22.10979
    • (1992) Proc Natl Acad Sci USA , vol.89 , Issue.22 , pp. 10979-10983
    • St Johnston, D.1    Brown, N.H.2    Gall, J.G.3    Jantsch, M.4
  • 34
    • 0026716255 scopus 로고
    • Mechanism of interferon action: Identification of a RNA binding domain within the N-terminal region of the human RNA-dependent P1/eIF-2 alpha protein kinase
    • 1373554 1:CAS:528:DyaK3sXkvFSjsbk%3D 10.1016/0042-6822(92)90733-6
    • SJ McCormack DC Thomis CE Samuel 1992 Mechanism of interferon action: identification of a RNA binding domain within the N-terminal region of the human RNA-dependent P1/eIF-2 alpha protein kinase Virology 188 1 47 56 1373554 1:CAS:528:DyaK3sXkvFSjsbk%3D 10.1016/0042-6822(92)90733-6
    • (1992) Virology , vol.188 , Issue.1 , pp. 47-56
    • McCormack, S.J.1    Thomis, D.C.2    Samuel, C.E.3
  • 35
    • 0026653870 scopus 로고
    • Identification of double-stranded RNA-binding domains in the interferon-induced double-stranded RNA-activated p68 kinase
    • 1351683 1:CAS:528:DyaK3sXisFSnur4%3D 10.1073/pnas.89.12.5447
    • GS Feng K Chong A Kumar BR Williams 1992 Identification of double-stranded RNA-binding domains in the interferon-induced double-stranded RNA-activated p68 kinase Proc Natl Acad Sci USA 89 12 5447 5451 1351683 1:CAS:528:DyaK3sXisFSnur4%3D 10.1073/pnas.89.12.5447
    • (1992) Proc Natl Acad Sci USA , vol.89 , Issue.12 , pp. 5447-5451
    • Feng, G.S.1    Chong, K.2    Kumar, A.3    Williams, B.R.4
  • 36
    • 0027105279 scopus 로고
    • Two RNA-binding motifs in the double-stranded RNA-activated protein kinase, DAI
    • 1364113 1:CAS:528:DyaK3sXns1Sluw%3D%3D 10.1101/gad.6.12b.2478
    • SR Green MB Mathews 1992 Two RNA-binding motifs in the double-stranded RNA-activated protein kinase, DAI Genes Dev 6 12B 2478 2490 1364113 1:CAS:528:DyaK3sXns1Sluw%3D%3D 10.1101/gad.6.12b.2478
    • (1992) Genes Dev , vol.6 , Issue.12 B , pp. 2478-2490
    • Green, S.R.1    Mathews, M.B.2
  • 37
    • 0029959285 scopus 로고    scopus 로고
    • Comparative mutational analysis of the double-stranded RNA binding domains of Xenopus laevis RNA-binding protein A
    • 8910425 1:CAS:528:DyaK28XmvVWlur8%3D 10.1074/jbc.271.45.28112
    • BC Krovat MF Jantsch 1996 Comparative mutational analysis of the double-stranded RNA binding domains of Xenopus laevis RNA-binding protein A J Biol Chem 271 45 28112 28119 8910425 1:CAS:528:DyaK28XmvVWlur8%3D 10.1074/jbc.271.45.28112
    • (1996) J Biol Chem , vol.271 , Issue.45 , pp. 28112-28119
    • Krovat, B.C.1    Jantsch, M.F.2
  • 38
    • 0029058994 scopus 로고
    • Structure of the dsRNA binding domain of E. coli RNase III
    • 7628457 1:CAS:528:DyaK2MXnt1amtLY%3D
    • A Kharrat MJ Macias TJ Gibson M Nilges A Pastore 1995 Structure of the dsRNA binding domain of E. coli RNase III EMBO J 14 14 3572 3584 7628457 1:CAS:528:DyaK2MXnt1amtLY%3D
    • (1995) EMBO J , vol.14 , Issue.14 , pp. 3572-3584
    • Kharrat, A.1    MacIas, M.J.2    Gibson, T.J.3    Nilges, M.4    Pastore, A.5
  • 39
    • 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
    • 7628456 1:CAS:528:DyaK2MXnt1amtLk%3D
    • M Bycroft S Grünert AG Murzin M Proctor D St Johnston 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 14 3563 3571 7628456 1:CAS:528:DyaK2MXnt1amtLk%3D
    • (1995) EMBO J , vol.14 , Issue.14 , pp. 3563-3571
    • Bycroft, M.1    Grünert, S.2    Murzin, A.G.3    Proctor, M.4    St Johnston, D.5
  • 41
    • 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
    • 15150409 1:CAS:528:DC%2BD2cXkvFOms7c%3D 10.1073/pnas.0402627101
    • H Wu A Henras G Chanfreau J Feigon 2004 Structural basis for recognition of the AGNN tetraloop RNA fold by the double-stranded RNA-binding domain of Rnt1p RNase III Proc Natl Acad Sci USA 101 22 8307 8312 15150409 1:CAS:528:DC%2BD2cXkvFOms7c%3D 10.1073/pnas.0402627101
    • (2004) Proc Natl Acad Sci USA , vol.101 , Issue.22 , pp. 8307-8312
    • Wu, H.1    Henras, A.2    Chanfreau, G.3    Feigon, J.4
  • 42
    • 79960173334 scopus 로고    scopus 로고
    • Structure of a yeast RNase III dsRBD complex with a noncanonical RNA substrate provides new insights into binding specificity of dsRBDs
    • 21742266 1:CAS:528:DC%2BC3MXoslWhsbs%3D 10.1016/j.str.2011.03.022
    • Z Wang E Hartman K Roy G Chanfreau J Feigon 2011 Structure of a yeast RNase III dsRBD complex with a noncanonical RNA substrate provides new insights into binding specificity of dsRBDs Structure 19 7 999 1010 21742266 1:CAS:528:DC%2BC3MXoslWhsbs%3D 10.1016/j.str.2011.03.022
    • (2011) Structure , vol.19 , Issue.7 , pp. 999-1010
    • Wang, Z.1    Hartman, E.2    Roy, K.3    Chanfreau, G.4    Feigon, J.5
  • 43
    • 1542581581 scopus 로고    scopus 로고
    • Noncatalytic assembly of ribonuclease III with double-stranded RNA
    • 15016361 1:CAS:528:DC%2BD2cXitFKlu7k%3D 10.1016/j.str.2004.02.004
    • J Blaszczyk J Gan JE Tropea DL Court DS Waugh X Ji 2004 Noncatalytic assembly of ribonuclease III with double-stranded RNA Structure 12 3 457 466 15016361 1:CAS:528:DC%2BD2cXitFKlu7k%3D 10.1016/j.str.2004.02.004
    • (2004) Structure , vol.12 , Issue.3 , pp. 457-466
    • Blaszczyk, J.1    Gan, J.2    Tropea, J.E.3    Court, D.L.4    Waugh, D.S.5    Ji, X.6
  • 44
    • 26444436343 scopus 로고    scopus 로고
    • Intermediate states of ribonuclease III in complex with double-stranded RNA
    • 16216575 1:CAS:528:DC%2BD2MXhtFWhtrzP 10.1016/j.str.2005.06.014
    • J Gan JE Tropea BP Austin DL Court DS Waugh X Ji 2005 Intermediate states of ribonuclease III in complex with double-stranded RNA Structure 13 10 1435 1442 16216575 1:CAS:528:DC%2BD2MXhtFWhtrzP 10.1016/j.str.2005.06.014
    • (2005) Structure , vol.13 , Issue.10 , pp. 1435-1442
    • Gan, J.1    Tropea, J.E.2    Austin, B.P.3    Court, D.L.4    Waugh, D.S.5    Ji, X.6
  • 45
    • 31044448524 scopus 로고    scopus 로고
    • Structural insight into the mechanism of double-stranded RNA processing by ribonuclease III
    • 16439209 1:CAS:528:DC%2BD28Xht1Kktbw%3D 10.1016/j.cell.2005.11.034
    • J Gan JE Tropea BP Austin DL Court DS Waugh X Ji 2006 Structural insight into the mechanism of double-stranded RNA processing by ribonuclease III Cell 124 2 355 366 16439209 1:CAS:528:DC%2BD28Xht1Kktbw%3D 10.1016/j.cell.2005.11.034
    • (2006) Cell , vol.124 , Issue.2 , pp. 355-366
    • Gan, J.1    Tropea, J.E.2    Austin, B.P.3    Court, D.L.4    Waugh, D.S.5    Ji, X.6
  • 46
    • 36849013062 scopus 로고    scopus 로고
    • A stepwise model for double-stranded RNA processing by ribonuclease III
    • 18047582 1:CAS:528:DC%2BD1cXitVGjtrs%3D 10.1111/j.1365-2958.2007.06032.x
    • J Gan G Shaw JE Tropea DS Waugh DL Court X Ji 2008 A stepwise model for double-stranded RNA processing by ribonuclease III Mol Microbiol 67 1 143 154 18047582 1:CAS:528:DC%2BD1cXitVGjtrs%3D 10.1111/j.1365-2958.2007.06032.x
    • (2008) Mol Microbiol , vol.67 , Issue.1 , pp. 143-154
    • Gan, J.1    Shaw, G.2    Tropea, J.E.3    Waugh, D.S.4    Court, D.L.5    Ji, X.6
  • 47
    • 40649086065 scopus 로고    scopus 로고
    • Structural and biochemical insights into the dicing mechanism of mouse Dicer: A conserved lysine is critical for dsRNA cleavage
    • 18268334 1:CAS:528:DC%2BD1cXis1KhtLw%3D 10.1073/pnas.0711506105
    • Z Du JK Lee R Tjhen RM Stroud TL James 2008 Structural and biochemical insights into the dicing mechanism of mouse Dicer: a conserved lysine is critical for dsRNA cleavage Proc Natl Acad Sci USA 105 7 2391 2396 18268334 1:CAS:528:DC%2BD1cXis1KhtLw%3D 10.1073/pnas.0711506105
    • (2008) Proc Natl Acad Sci USA , vol.105 , Issue.7 , pp. 2391-2396
    • Du, Z.1    Lee, J.K.2    Tjhen, R.3    Stroud, R.M.4    James, T.L.5
  • 48
    • 80054907588 scopus 로고    scopus 로고
    • An extended dsRBD with a novel zinc-binding motif mediates nuclear retention of fission yeast Dicer
    • 21847092 1:CAS:528:DC%2BC3MXhtVWrtL3N 10.1038/emboj.2011.300
    • P Barraud S Emmerth Y Shimada H-R Hotz FH-T Allain M Bühler 2011 An extended dsRBD with a novel zinc-binding motif mediates nuclear retention of fission yeast Dicer EMBO J 30 20 4223 4235 21847092 1:CAS:528:DC%2BC3MXhtVWrtL3N 10.1038/emboj.2011.300
    • (2011) EMBO J , vol.30 , Issue.20 , pp. 4223-4235
    • Barraud, P.1    Emmerth, S.2    Shimada, Y.3    Hotz, H.-R.4    Allain, F.-T.5    Bühler, M.6
  • 49
    • 79960186717 scopus 로고    scopus 로고
    • The inside-out mechanism of Dicers from budding yeasts
    • 21784247 1:CAS:528:DC%2BC3MXptleksbc%3D 10.1016/j.cell.2011.06.021
    • DE Weinberg K Nakanishi DJ Patel DP Bartel 2011 The inside-out mechanism of Dicers from budding yeasts Cell 146 2 262 276 21784247 1:CAS:528: DC%2BC3MXptleksbc%3D 10.1016/j.cell.2011.06.021
    • (2011) Cell , vol.146 , Issue.2 , pp. 262-276
    • Weinberg, D.E.1    Nakanishi, K.2    Patel, D.J.3    Bartel, D.P.4
  • 50
    • 78650324516 scopus 로고    scopus 로고
    • Solution structure of the Drosha double-stranded RNA-binding domain
    • 20226070 10.1186/1758-907X-1-2 1:CAS:528:DC%2BC3cXksFensLc%3D
    • GA Mueller MT Miller EF Derose M Ghosh RE London TMT Hall 2010 Solution structure of the Drosha double-stranded RNA-binding domain Silence 1 1 2 20226070 10.1186/1758-907X-1-2 1:CAS:528:DC%2BC3cXksFensLc%3D
    • (2010) Silence , vol.1 , Issue.1 , pp. 2
    • Mueller, G.A.1    Miller, M.T.2    Derose, E.F.3    Ghosh, M.4    London, R.E.5    Hall, T.M.T.6
  • 51
    • 32044468729 scopus 로고    scopus 로고
    • Structure and specific RNA binding of ADAR2 double-stranded RNA binding motifs
    • 16472753 1:CAS:528:DC%2BD28XhtlKltrY%3D 10.1016/j.str.2005.11.013
    • R Stefl M Xu L Skrisovska RB Emeson FH-T Allain 2006 Structure and specific RNA binding of ADAR2 double-stranded RNA binding motifs Structure 14 2 345 355 16472753 1:CAS:528:DC%2BD28XhtlKltrY%3D 10.1016/j.str.2005.11.013
    • (2006) Structure , vol.14 , Issue.2 , pp. 345-355
    • Stefl, R.1    Xu, M.2    Skrisovska, L.3    Emeson, R.B.4    Allain, F.-T.5
  • 52
    • 77957822421 scopus 로고    scopus 로고
    • The solution structure of the ADAR2 dsRBM-RNA complex reveals a sequence-specific readout of the minor groove
    • 20946981 1:CAS:528:DC%2BC3cXht12qurnP 10.1016/j.cell.2010.09.026
    • R Stefl FC Oberstrass JL Hood M Jourdan M Zimmermann L Skrisovska C Maris L Peng C Hofr RB Emeson, et al. 2010 The solution structure of the ADAR2 dsRBM-RNA complex reveals a sequence-specific readout of the minor groove Cell 143 2 225 237 20946981 1:CAS:528:DC%2BC3cXht12qurnP 10.1016/j.cell.2010.09.026
    • (2010) Cell , vol.143 , Issue.2 , pp. 225-237
    • Stefl, R.1    Oberstrass, F.C.2    Hood, J.L.3    Jourdan, M.4    Zimmermann, M.5    Skrisovska, L.6    Maris, C.7    Peng, L.8    Hofr, C.9    Emeson, R.B.10
  • 53
    • 84861599510 scopus 로고    scopus 로고
    • Solution structure of the N-terminal dsRBD of Drosophila ADAR and interaction studies with RNA
    • 22210494 1:CAS:528:DC%2BC38XnslKqsbk%3D 10.1016/j.biochi.2011.12.017
    • P Barraud BS Heale MA O'Connell FH Allain 2012 Solution structure of the N-terminal dsRBD of Drosophila ADAR and interaction studies with RNA Biochimie 94 7 1499 1509 22210494 1:CAS:528:DC%2BC38XnslKqsbk%3D 10.1016/j.biochi.2011.12. 017
    • (2012) Biochimie , vol.94 , Issue.7 , pp. 1499-1509
    • Barraud, P.1    Heale, B.S.2    O'Connell, M.A.3    Allain, F.H.4
  • 54
    • 0342723737 scopus 로고    scopus 로고
    • RNA recognition by a Staufen double-stranded RNA-binding domain
    • 10698941 1:CAS:528:DC%2BD3cXitVyrsrc%3D 10.1093/emboj/19.5.997
    • A Ramos S Grünert J Adams DR Micklem MR Proctor S Freund M Bycroft D St Johnston G Varani 2000 RNA recognition by a Staufen double-stranded RNA-binding domain EMBO J 19 5 997 1009 10698941 1:CAS:528:DC%2BD3cXitVyrsrc%3D 10.1093/emboj/19.5.997
    • (2000) EMBO J , vol.19 , Issue.5 , pp. 997-1009
    • Ramos, A.1    Grünert, S.2    Adams, J.3    Micklem, D.R.4    Proctor, M.R.5    Freund, S.6    Bycroft, M.7    St Johnston, D.8    Varani, G.9
  • 55
    • 0032535613 scopus 로고    scopus 로고
    • Molecular basis of double-stranded RNA-protein interactions: Structure of a dsRNA-binding domain complexed with dsRNA
    • 9857205 1:CAS:528:DyaK1MXksVGgug%3D%3D 10.1093/emboj/17.24.7505
    • JM Ryter SC Schultz 1998 Molecular basis of double-stranded RNA-protein interactions: structure of a dsRNA-binding domain complexed with dsRNA EMBO J 17 24 7505 7513 9857205 1:CAS:528:DyaK1MXksVGgug%3D%3D 10.1093/emboj/17.24.7505
    • (1998) EMBO J , vol.17 , Issue.24 , pp. 7505-7513
    • Ryter, J.M.1    Schultz, S.C.2
  • 56
    • 77952633582 scopus 로고    scopus 로고
    • Structure of Arabidopsis HYPONASTIC LEAVES1 and its molecular implications for miRNA processing
    • 20462493 1:CAS:528:DC%2BC3cXlvVGnu70%3D 10.1016/j.str.2010.02.006
    • SW Yang H-Y Chen J Yang S Machida N-H Chua YA Yuan 2010 Structure of Arabidopsis HYPONASTIC LEAVES1 and its molecular implications for miRNA processing Structure 18 5 594 605 20462493 1:CAS:528:DC%2BC3cXlvVGnu70%3D 10.1016/j.str.2010.02.006
    • (2010) Structure , vol.18 , Issue.5 , pp. 594-605
    • Yang, S.W.1    Chen, H.-Y.2    Yang, J.3    Machida, S.4    Chua, N.-H.5    Yuan, Y.A.6
  • 57
    • 78650763143 scopus 로고    scopus 로고
    • Structures of the first and second double-stranded RNA-binding domains of human TAR RNA-binding protein
    • 21080422 1:CAS:528:DC%2BC3MXktVKjsbo%3D 10.1002/pro.543
    • S Yamashita T Nagata M Kawazoe C Takemoto T Kigawa P Guntert N Kobayashi T Terada M Shirouzu M Wakiyama, et al. 2011 Structures of the first and second double-stranded RNA-binding domains of human TAR RNA-binding protein Protein Sci 20 1 118 130 21080422 1:CAS:528:DC%2BC3MXktVKjsbo%3D 10.1002/pro.543
    • (2011) Protein Sci , vol.20 , Issue.1 , pp. 118-130
    • Yamashita, S.1    Nagata, T.2    Kawazoe, M.3    Takemoto, C.4    Kigawa, T.5    Guntert, P.6    Kobayashi, N.7    Terada, T.8    Shirouzu, M.9    Wakiyama, M.10
  • 58
    • 77957082650 scopus 로고    scopus 로고
    • Structure and RNA interactions of the plant MicroRNA processing- associated protein HYL1
    • 20735118 1:CAS:528:DC%2BC3cXhtV2jtrvM 10.1021/bi100672x
    • RM Rasia J Mateos NG Bologna P Burdisso L Imbert JF Palatnik J Boisbouvier 2010 Structure and RNA interactions of the plant MicroRNA processing-associated protein HYL1 Biochemistry 49 38 8237 8239 20735118 1:CAS:528:DC%2BC3cXhtV2jtrvM 10.1021/bi100672x
    • (2010) Biochemistry , vol.49 , Issue.38 , pp. 8237-8239
    • Rasia, R.M.1    Mateos, J.2    Bologna, N.G.3    Burdisso, P.4    Imbert, L.5    Palatnik, J.F.6    Boisbouvier, J.7
  • 59
    • 70349939426 scopus 로고    scopus 로고
    • Structural insights into mechanisms of the small RNA methyltransferase HEN1
    • 19812675 1:CAS:528:DC%2BD1MXht1CisLvP 10.1038/nature08433
    • Y Huang L Ji Q Huang DG Vassylyev X Chen J-B Ma 2009 Structural insights into mechanisms of the small RNA methyltransferase HEN1 Nature 461 7265 823 827 19812675 1:CAS:528:DC%2BD1MXht1CisLvP 10.1038/nature08433
    • (2009) Nature , vol.461 , Issue.7265 , pp. 823-827
    • Huang, Y.1    Ji, L.2    Huang, Q.3    Vassylyev, D.G.4    Chen, X.5    Ma, J.-B.6
  • 60
    • 34548480185 scopus 로고    scopus 로고
    • Crystal structure of human DGCR8 core
    • 17704815 1:CAS:528:DC%2BD2sXpvFKksrg%3D 10.1038/nsmb1294
    • SY Sohn WJ Bae JJ Kim K-H Yeom VN Kim Y Cho 2007 Crystal structure of human DGCR8 core Nat Struct Mol Biol 14 9 847 853 17704815 1:CAS:528: DC%2BD2sXpvFKksrg%3D 10.1038/nsmb1294
    • (2007) Nat Struct Mol Biol , vol.14 , Issue.9 , pp. 847-853
    • Sohn, S.Y.1    Bae, W.J.2    Kim, J.J.3    Yeom, K.-H.4    Kim, V.N.5    Cho, Y.6
  • 61
    • 0032530310 scopus 로고    scopus 로고
    • Structure of the double-stranded RNA-binding domain of the protein kinase PKR reveals the molecular basis of its dsRNA-mediated activation
    • 9736623 1:CAS:528:DyaK1cXmsFOgsLw%3D 10.1093/emboj/17.18.5458
    • S Nanduri BW Carpick Y Yang BR Williams J Qin 1998 Structure of the double-stranded RNA-binding domain of the protein kinase PKR reveals the molecular basis of its dsRNA-mediated activation EMBO J 17 18 5458 5465 9736623 1:CAS:528:DyaK1cXmsFOgsLw%3D 10.1093/emboj/17.18.5458
    • (1998) EMBO J , vol.17 , Issue.18 , pp. 5458-5465
    • Nanduri, S.1    Carpick, B.W.2    Yang, Y.3    Williams, B.R.4    Qin, J.5
  • 62
    • 84860614277 scopus 로고    scopus 로고
    • Solution structures of the double-stranded RNA-binding domains from RNA helicase A
    • 22454253 1:CAS:528:DC%2BC38XksV2hsLs%3D 10.1002/prot.24059
    • T Nagata K Tsuda N Kobayashi M Shirouzu T Kigawa P Guntert S Yokoyama Y Muto 2012 Solution structures of the double-stranded RNA-binding domains from RNA helicase A Proteins 80 6 1699 1706 22454253 1:CAS:528:DC%2BC38XksV2hsLs%3D 10.1002/prot.24059
    • (2012) Proteins , vol.80 , Issue.6 , pp. 1699-1706
    • Nagata, T.1    Tsuda, K.2    Kobayashi, N.3    Shirouzu, M.4    Kigawa, T.5    Guntert, P.6    Yokoyama, S.7    Muto, Y.8
  • 63
    • 0028961190 scopus 로고
    • Two functionally distinct RNA-binding motifs in the regulatory domain of the protein kinase DAI
    • 7799944 1:CAS:528:DyaK2MXislamt7c%3D
    • SR Green L Manche MB Mathews 1995 Two functionally distinct RNA-binding motifs in the regulatory domain of the protein kinase DAI Mol Cell Biol 15 1 358 364 7799944 1:CAS:528:DyaK2MXislamt7c%3D
    • (1995) Mol Cell Biol , vol.15 , Issue.1 , pp. 358-364
    • Green, S.R.1    Manche, L.2    Mathews, M.B.3
  • 64
    • 0028796512 scopus 로고
    • Mutational analysis of the double-stranded RNA (dsRNA) binding domain of the dsRNA-activated protein kinase, PKR
    • 7852324 1:CAS:528:DyaK2MXjs1Kmt7g%3D 10.1074/jbc.270.6.2601
    • NA McMillan BW Carpick B Hollis WM Toone M Zamanian-Daryoush BR Williams 1995 Mutational analysis of the double-stranded RNA (dsRNA) binding domain of the dsRNA-activated protein kinase, PKR J Biol Chem 270 6 2601 2606 7852324 1:CAS:528:DyaK2MXjs1Kmt7g%3D 10.1074/jbc.270.6.2601
    • (1995) J Biol Chem , vol.270 , Issue.6 , pp. 2601-2606
    • McMillan, N.A.1    Carpick, B.W.2    Hollis, B.3    Toone, W.M.4    Zamanian-Daryoush, M.5    Williams, B.R.6
  • 65
    • 0029841348 scopus 로고    scopus 로고
    • Specific mutations near the amino terminus of double-stranded RNA-dependent protein kinase (PKR) differentially affect its double-stranded RNA binding and dimerization properties
    • 8810342 1:CAS:528:DyaK28Xmt1eltb8%3D 10.1074/jbc.271.41.25657
    • RC Patel P Stanton GC Sen 1996 Specific mutations near the amino terminus of double-stranded RNA-dependent protein kinase (PKR) differentially affect its double-stranded RNA binding and dimerization properties J Biol Chem 271 41 25657 25663 8810342 1:CAS:528:DyaK28Xmt1eltb8%3D 10.1074/jbc.271.41.25657
    • (1996) J Biol Chem , vol.271 , Issue.41 , pp. 25657-25663
    • Patel, R.C.1    Stanton, P.2    Sen, G.C.3
  • 66
    • 74049138689 scopus 로고    scopus 로고
    • Nuclear retention of fission yeast dicer is a prerequisite for RNAi-mediated heterochromatin assembly
    • 20152181 1:CAS:528:DC%2BC3cXkvVWhs7Y%3D 10.1016/j.devcel.2009.11.011
    • S Emmerth H Schober D Gaidatzis T Roloff K Jacobeit M Bühler 2010 Nuclear retention of fission yeast dicer is a prerequisite for RNAi-mediated heterochromatin assembly Dev Cell 18 1 102 113 20152181 1:CAS:528: DC%2BC3cXkvVWhs7Y%3D 10.1016/j.devcel.2009.11.011
    • (2010) Dev Cell , vol.18 , Issue.1 , pp. 102-113
    • Emmerth, S.1    Schober, H.2    Gaidatzis, D.3    Roloff, T.4    Jacobeit, K.5    Bühler, M.6
  • 67
    • 84859350087 scopus 로고    scopus 로고
    • RNAi keeps Atf1-bound stress response genes in check at nuclear pores
    • 22431512 1:CAS:528:DC%2BC38XntVyqtLk%3D 10.1101/gad.186866.112
    • KJ Woolcock R Stunnenberg D Gaidatzis HR Hotz S Emmerth P Barraud M Buhler 2012 RNAi keeps Atf1-bound stress response genes in check at nuclear pores Genes Dev 26 7 683 692 22431512 1:CAS:528:DC%2BC38XntVyqtLk%3D 10.1101/gad.186866.112
    • (2012) Genes Dev , vol.26 , Issue.7 , pp. 683-692
    • Woolcock, K.J.1    Stunnenberg, R.2    Gaidatzis, D.3    Hotz, H.R.4    Emmerth, S.5    Barraud, P.6    Buhler, M.7
  • 68
    • 0037033792 scopus 로고    scopus 로고
    • Exportin-5, a novel karyopherin, mediates nuclear export of double-stranded RNA binding proteins
    • 11777942 1:CAS:528:DC%2BD38XjslOhtA%3D%3D 10.1083/jcb.200110082
    • AM Brownawell IG Macara 2002 Exportin-5, a novel karyopherin, mediates nuclear export of double-stranded RNA binding proteins J Cell Biol 156 1 53 64 11777942 1:CAS:528:DC%2BD38XjslOhtA%3D%3D 10.1083/jcb.200110082
    • (2002) J Cell Biol , vol.156 , Issue.1 , pp. 53-64
    • Brownawell, A.M.1    MacAra, I.G.2
  • 69
    • 0036856310 scopus 로고    scopus 로고
    • Nucleocytoplasmic distribution of human RNA-editing enzyme ADAR1 is modulated by double-stranded RNA-binding domains, a leucine-rich export signal, and a putative dimerization domain
    • 12429827 1:CAS:528:DC%2BD38XpsVait7c%3D 10.1091/mbc.E02-03-0161
    • A Strehblow M Hallegger MF Jantsch 2002 Nucleocytoplasmic distribution of human RNA-editing enzyme ADAR1 is modulated by double-stranded RNA-binding domains, a leucine-rich export signal, and a putative dimerization domain Mol Biol Cell 13 11 3822 3835 12429827 1:CAS:528:DC%2BD38XpsVait7c%3D 10.1091/mbc.E02-03-0161
    • (2002) Mol Biol Cell , vol.13 , Issue.11 , pp. 3822-3835
    • Strehblow, A.1    Hallegger, M.2    Jantsch, M.F.3
  • 70
    • 0347093422 scopus 로고    scopus 로고
    • Minihelix-containing RNAs mediate exportin-5-dependent nuclear export of the double-stranded RNA-binding protein ILF3
    • 14570900 1:CAS:528:DC%2BD2cXhtV2gsQ%3D%3D 10.1074/jbc.M306808200
    • C Gwizdek B Ossareh-Nazari AM Brownawell S Evers IG Macara C Dargemont 2004 Minihelix-containing RNAs mediate exportin-5-dependent nuclear export of the double-stranded RNA-binding protein ILF3 J Biol Chem 279 2 884 891 14570900 1:CAS:528:DC%2BD2cXhtV2gsQ%3D%3D 10.1074/jbc.M306808200
    • (2004) J Biol Chem , vol.279 , Issue.2 , pp. 884-891
    • Gwizdek, C.1    Ossareh-Nazari, B.2    Brownawell, A.M.3    Evers, S.4    MacAra, I.G.5    Dargemont, C.6
  • 71
    • 3843145108 scopus 로고    scopus 로고
    • The brain-specific double-stranded RNA-binding protein Staufen2: Nucleolar accumulation and isoform-specific exportin-5-dependent export
    • 15166236 1:CAS:528:DC%2BD2cXlslOrsL0%3D 10.1074/jbc.C400226200
    • P Macchi AM Brownawell B Grunewald L DesGroseillers IG Macara MA Kiebler 2004 The brain-specific double-stranded RNA-binding protein Staufen2: nucleolar accumulation and isoform-specific exportin-5-dependent export J Biol Chem 279 30 31440 31444 15166236 1:CAS:528:DC%2BD2cXlslOrsL0%3D 10.1074/jbc.C400226200
    • (2004) J Biol Chem , vol.279 , Issue.30 , pp. 31440-31444
    • MacChi, P.1    Brownawell, A.M.2    Grunewald, B.3    Desgroseillers, L.4    MacAra, I.G.5    Kiebler, M.A.6
  • 72
    • 62849103689 scopus 로고    scopus 로고
    • RNA-regulated interaction of transportin-1 and exportin-5 with the double-stranded RNA-binding domain regulates nucleocytoplasmic shuttling of ADAR1
    • 19124606 1:CAS:528:DC%2BD1MXjt1WlsL8%3D 10.1128/MCB.01519-08
    • J Fritz A Strehblow A Taschner S Schopoff P Pasierbek MF Jantsch 2009 RNA-regulated interaction of transportin-1 and exportin-5 with the double-stranded RNA-binding domain regulates nucleocytoplasmic shuttling of ADAR1 Mol Cell Biol 29 6 1487 1497 19124606 1:CAS:528:DC%2BD1MXjt1WlsL8%3D 10.1128/MCB.01519-08
    • (2009) Mol Cell Biol , vol.29 , Issue.6 , pp. 1487-1497
    • Fritz, J.1    Strehblow, A.2    Taschner, A.3    Schopoff, S.4    Pasierbek, P.5    Jantsch, M.F.6
  • 73
    • 0032480017 scopus 로고    scopus 로고
    • PACT, a protein activator of the interferon-induced protein kinase
    • 1:CAS:528:DyaK1cXlsFOltb8%3D 10.1093/emboj/17.15.4379
    • RC Patel GC Sen 1998 PACT, a protein activator of the interferon-induced protein kinase PKR. EMBO J 17 15 4379 4390 1:CAS:528:DyaK1cXlsFOltb8%3D 10.1093/emboj/17.15.4379
    • (1998) PKR. EMBO J , vol.17 , Issue.15 , pp. 4379-4390
    • Patel, R.C.1    Sen, G.C.2
  • 74
    • 0032526140 scopus 로고    scopus 로고
    • Miranda mediates asymmetric protein and RNA localization in the developing nervous system
    • 9637686 1:CAS:528:DyaK1cXktl2hsLc%3D 10.1101/gad.12.12.1847
    • AJ Schuldt JH Adams CM Davidson DR Micklem J Haseloff D St Johnston AH Brand 1998 Miranda mediates asymmetric protein and RNA localization in the developing nervous system Genes Dev 12 12 1847 1857 9637686 1:CAS:528: DyaK1cXktl2hsLc%3D 10.1101/gad.12.12.1847
    • (1998) Genes Dev , vol.12 , Issue.12 , pp. 1847-1857
    • Schuldt, A.J.1    Adams, J.H.2    Davidson, C.M.3    Micklem, D.R.4    Haseloff, J.5    St Johnston, D.6    Brand, A.H.7
  • 75
    • 0034653570 scopus 로고    scopus 로고
    • Distinct roles of two conserved Staufen domains in oskar mRNA localization and translation
    • 10716936 1:CAS:528:DC%2BD3cXit1Gmsb0%3D 10.1093/emboj/19.6.1366
    • DR Micklem J Adams S Grunert D St Johnston 2000 Distinct roles of two conserved Staufen domains in oskar mRNA localization and translation EMBO J 19 6 1366 1377 10716936 1:CAS:528:DC%2BD3cXit1Gmsb0%3D 10.1093/emboj/19.6.1366
    • (2000) EMBO J , vol.19 , Issue.6 , pp. 1366-1377
    • Micklem, D.R.1    Adams, J.2    Grunert, S.3    St Johnston, D.4
  • 76
    • 0035816675 scopus 로고    scopus 로고
    • Binding of double-stranded RNA to protein kinase PKR is required for dimerization and promotes critical autophosphorylation events in the activation loop
    • 11337501 1:CAS:528:DC%2BD3MXlt1agtLk%3D 10.1074/jbc.M102108200
    • F Zhang PR Romano T Nagamura-Inoue B Tian TE Dever MB Mathews K Ozato AG Hinnebusch 2001 Binding of double-stranded RNA to protein kinase PKR is required for dimerization and promotes critical autophosphorylation events in the activation loop J Biol Chem 276 27 24946 24958 11337501 1:CAS:528: DC%2BD3MXlt1agtLk%3D 10.1074/jbc.M102108200
    • (2001) J Biol Chem , vol.276 , Issue.27 , pp. 24946-24958
    • Zhang, F.1    Romano, P.R.2    Nagamura-Inoue, T.3    Tian, B.4    Dever, T.E.5    Mathews, M.B.6    Ozato, K.7    Hinnebusch, A.G.8
  • 77
    • 0036276292 scopus 로고    scopus 로고
    • A physical interaction between Gar1p and Rnt1pi is required for the nuclear import of H/ACA small nucleolar RNA-associated proteins
    • 12052886 1:CAS:528:DC%2BD38Xks1yrtrk%3D 10.1128/MCB.22.13.4792-4802.2002
    • A Tremblay B Lamontagne M Catala Y Yam S Larose L Good SA Elela 2002 A physical interaction between Gar1p and Rnt1pi is required for the nuclear import of H/ACA small nucleolar RNA-associated proteins Mol Cell Biol 22 13 4792 4802 12052886 1:CAS:528:DC%2BD38Xks1yrtrk%3D 10.1128/MCB.22.13.4792-4802.2002
    • (2002) Mol Cell Biol , vol.22 , Issue.13 , pp. 4792-4802
    • Tremblay, A.1    Lamontagne, B.2    Catala, M.3    Yam, Y.4    Larose, S.5    Good, L.6    Elela, S.A.7
  • 78
    • 0142247418 scopus 로고    scopus 로고
    • The carboxy-terminal, M3 motifs of PACT and TRBP have opposite effects on PKR activity
    • 14585331 1:CAS:528:DC%2BD3sXosVKksro%3D 10.1016/S0042-6822(03)00589-0
    • V Gupta X Huang RC Patel 2003 The carboxy-terminal, M3 motifs of PACT and TRBP have opposite effects on PKR activity Virology 315 2 283 291 14585331 1:CAS:528:DC%2BD3sXosVKksro%3D 10.1016/S0042-6822(03)00589-0
    • (2003) Virology , vol.315 , Issue.2 , pp. 283-291
    • Gupta, V.1    Huang, X.2    Patel, R.C.3
  • 79
    • 4444248655 scopus 로고    scopus 로고
    • Oligomerization activity of a double-stranded RNA-binding domain
    • 15358534 1:CAS:528:DC%2BD2cXnsFGmu7g%3D 10.1016/j.febslet.2004.07.080
    • EG Hitti NB Sallacz VK Schoft MF Jantsch 2004 Oligomerization activity of a double-stranded RNA-binding domain FEBS Lett 574 1-3 25 30 15358534 1:CAS:528:DC%2BD2cXnsFGmu7g%3D 10.1016/j.febslet.2004.07.080
    • (2004) FEBS Lett , vol.574 , Issue.1-3 , pp. 25-30
    • Hitti, E.G.1    Sallacz, N.B.2    Schoft, V.K.3    Jantsch, M.F.4
  • 80
    • 27144550559 scopus 로고    scopus 로고
    • TRBP, a regulator of cellular PKR and HIV-1 virus expression, interacts with Dicer and functions in RNA silencing
    • 16142218 1:CAS:528:DC%2BD2MXhtV2gsbrJ 10.1038/sj.embor.7400509
    • AD Haase L Jaskiewicz H Zhang S Laine R Sack A Gatignol W Filipowicz 2005 TRBP, a regulator of cellular PKR and HIV-1 virus expression, interacts with Dicer and functions in RNA silencing EMBO Rep 6 10 961 967 16142218 1:CAS:528:DC%2BD2MXhtV2gsbrJ 10.1038/sj.embor.7400509
    • (2005) EMBO Rep , vol.6 , Issue.10 , pp. 961-967
    • Haase, A.D.1    Jaskiewicz, L.2    Zhang, H.3    Laine, S.4    Sack, R.5    Gatignol, A.6    Filipowicz, W.7
  • 81
    • 23644433363 scopus 로고    scopus 로고
    • TRBP recruits the Dicer complex to Ago2 for microRNA processing and gene silencing
    • 15973356 1:CAS:528:DC%2BD2MXmvFenur0%3D 10.1038/nature03868
    • TP Chendrimada RI Gregory E Kumaraswamy J Norman N Cooch K Nishikura R Shiekhattar 2005 TRBP recruits the Dicer complex to Ago2 for microRNA processing and gene silencing Nature 436 7051 740 744 15973356 1:CAS:528: DC%2BD2MXmvFenur0%3D 10.1038/nature03868
    • (2005) Nature , vol.436 , Issue.7051 , pp. 740-744
    • Chendrimada, T.P.1    Gregory, R.I.2    Kumaraswamy, E.3    Norman, J.4    Cooch, N.5    Nishikura, K.6    Shiekhattar, R.7
  • 82
    • 0020493719 scopus 로고
    • The anatomy of A-, B-, and Z-DNA
    • 7071593 1:CAS:528:DyaL38XhvFGhs7k%3D 10.1126/science.7071593
    • RE Dickerson HR Drew BN Conner RM Wing AV Fratini ML Kopka 1982 The anatomy of A-, B-, and Z-DNA Science 216 4545 475 485 7071593 1:CAS:528:DyaL38XhvFGhs7k%3D 10.1126/science.7071593
    • (1982) Science , vol.216 , Issue.4545 , pp. 475-485
    • Dickerson, R.E.1    Drew, H.R.2    Conner, B.N.3    Wing, R.M.4    Fratini, A.V.5    Kopka, M.L.6
  • 83
    • 77950673634 scopus 로고    scopus 로고
    • Recognition of siRNA asymmetry by TAR RNA binding protein
    • 20184375 1:CAS:528:DC%2BC3cXjt1ygtb0%3D 10.1021/bi902189s
    • JA Gredell MJ Dittmer M Wu C Chan SP Walton 2010 Recognition of siRNA asymmetry by TAR RNA binding protein Biochemistry 49 14 3148 3155 20184375 1:CAS:528:DC%2BC3cXjt1ygtb0%3D 10.1021/bi902189s
    • (2010) Biochemistry , vol.49 , Issue.14 , pp. 3148-3155
    • Gredell, J.A.1    Dittmer, M.J.2    Wu, M.3    Chan, C.4    Walton, S.P.5
  • 84
    • 31044434491 scopus 로고    scopus 로고
    • The interaction between DCL1 and HYL1 is important for efficient and precise processing of pri-miRNA in plant microRNA biogenesis
    • 16428603 1:CAS:528:DC%2BD28XhtlSjsrs%3D 10.1261/rna.2146906
    • Y Kurihara Y Takashi Y Watanabe 2006 The interaction between DCL1 and HYL1 is important for efficient and precise processing of pri-miRNA in plant microRNA biogenesis RNA 12 2 206 212 16428603 1:CAS:528:DC%2BD28XhtlSjsrs%3D 10.1261/rna.2146906
    • (2006) RNA , vol.12 , Issue.2 , pp. 206-212
    • Kurihara, Y.1    Takashi, Y.2    Watanabe, Y.3
  • 85
    • 0029782652 scopus 로고    scopus 로고
    • Minor-groove recognition of double-stranded RNA by the double-stranded RNA-binding domain from the RNA-activated protein kinase PKR
    • 8756460 1:CAS:528:DyaK28Xkt1ylu7o%3D 10.1021/bi9607259
    • PC Bevilacqua TR Cech 1996 Minor-groove recognition of double-stranded RNA by the double-stranded RNA-binding domain from the RNA-activated protein kinase PKR Biochemistry 35 31 9983 9994 8756460 1:CAS:528:DyaK28Xkt1ylu7o%3D 10.1021/bi9607259
    • (1996) Biochemistry , vol.35 , Issue.31 , pp. 9983-9994
    • Bevilacqua, P.C.1    Cech, T.R.2
  • 86
    • 0025047647 scopus 로고
    • Architecture of ribosomal RNA: Constraints on the sequence of "tetra-loops
    • 2236056 1:CAS:528:DyaK3MXhvFKjsQ%3D%3D 10.1073/pnas.87.21.8467
    • CR Woese S Winker RR Gutell 1990 Architecture of ribosomal RNA: constraints on the sequence of "tetra-loops" Proc Natl Acad Sci USA 87 21 8467 8471 2236056 1:CAS:528:DyaK3MXhvFKjsQ%3D%3D 10.1073/pnas.87.21.8467
    • (1990) Proc Natl Acad Sci USA , vol.87 , Issue.21 , pp. 8467-8471
    • Woese, C.R.1    Winker, S.2    Gutell, R.R.3
  • 87
    • 0029121733 scopus 로고
    • Exceptionally stable nucleic acid hairpins
    • 7545040 1:CAS:528:DyaK2MXmt1amsLk%3D 10.1146/annurev.bb.24.060195.002115
    • G Varani 1995 Exceptionally stable nucleic acid hairpins Annu Rev Biophys Biomol Struct 24 379 404 7545040 1:CAS:528:DyaK2MXmt1amsLk%3D 10.1146/annurev.bb.24.060195.002115
    • (1995) Annu Rev Biophys Biomol Struct , vol.24 , pp. 379-404
    • Varani, G.1
  • 88
    • 0142153880 scopus 로고    scopus 로고
    • Conservation of RNase III processing pathways and specificity in hemiascomycetes
    • 14555472 1:CAS:528:DC%2BD3sXos1GktLk%3D 10.1128/EC.2.5.901-909.2003
    • G Chanfreau 2003 Conservation of RNase III processing pathways and specificity in hemiascomycetes Eukaryot Cell 2 5 901 909 14555472 1:CAS:528:DC%2BD3sXos1GktLk%3D 10.1128/EC.2.5.901-909.2003
    • (2003) Eukaryot Cell , vol.2 , Issue.5 , pp. 901-909
    • Chanfreau, G.1
  • 89
    • 0034724279 scopus 로고    scopus 로고
    • Recognition of a conserved class of RNA tetraloops by Saccharomyces cerevisiae RNase III
    • 10716739 1:CAS:528:DC%2BD3cXitlWqsr0%3D 10.1073/pnas.97.7.3142
    • G Chanfreau M Buckle A Jacquier 2000 Recognition of a conserved class of RNA tetraloops by Saccharomyces cerevisiae RNase III Proc Natl Acad Sci USA 97 7 3142 3147 10716739 1:CAS:528:DC%2BD3cXitlWqsr0%3D 10.1073/pnas.97.7.3142
    • (2000) Proc Natl Acad Sci USA , vol.97 , Issue.7 , pp. 3142-3147
    • Chanfreau, G.1    Buckle, M.2    Jacquier, A.3
  • 90
    • 0033868624 scopus 로고    scopus 로고
    • Substrate recognition by a eukaryotic RNase III: The double-stranded RNA-binding domain of Rnt1p selectively binds RNA containing a 5′-AGNN-3′ tetraloop
    • 10943893 1:CAS:528:DC%2BD3cXls1yqsLo%3D 10.1017/S1355838200000431
    • R Nagel M Ares Jr 2000 Substrate recognition by a eukaryotic RNase III: the double-stranded RNA-binding domain of Rnt1p selectively binds RNA containing a 5′-AGNN-3′ tetraloop RNA 6 8 1142 1156 10943893 1:CAS:528:DC%2BD3cXls1yqsLo%3D 10.1017/S1355838200000431
    • (2000) RNA , vol.6 , Issue.8 , pp. 1142-1156
    • Nagel, R.1    Ares, Jr.M.2
  • 91
    • 0037126626 scopus 로고    scopus 로고
    • A novel family of RNA tetraloop structure forms the recognition site for Saccharomyces cerevisiae RNase III
    • 11743000 1:CAS:528:DC%2BD38XpsF2j 10.1093/emboj/20.24.7240
    • H Wu PK Yang SE Butcher S Kang G Chanfreau J Feigon 2001 A novel family of RNA tetraloop structure forms the recognition site for Saccharomyces cerevisiae RNase III EMBO J 20 24 7240 7249 11743000 1:CAS:528:DC%2BD38XpsF2j 10.1093/emboj/20.24.7240
    • (2001) EMBO J , vol.20 , Issue.24 , pp. 7240-7249
    • Wu, H.1    Yang, P.K.2    Butcher, S.E.3    Kang, S.4    Chanfreau, G.5    Feigon, J.6
  • 92
    • 0037126621 scopus 로고    scopus 로고
    • Solution structure of conserved AGNN tetraloops: Insights into Rnt1p RNA processing
    • 11743001 1:CAS:528:DC%2BD38XpsF2i 10.1093/emboj/20.24.7250
    • I Lebars B Lamontagne S Yoshizawa S Aboul-Elela D Fourmy 2001 Solution structure of conserved AGNN tetraloops: insights into Rnt1p RNA processing EMBO J 20 24 7250 7258 11743001 1:CAS:528:DC%2BD38XpsF2i 10.1093/emboj/20.24.7250
    • (2001) EMBO J , vol.20 , Issue.24 , pp. 7250-7258
    • Lebars, I.1    Lamontagne, B.2    Yoshizawa, S.3    Aboul-Elela, S.4    Fourmy, D.5
  • 93
    • 0024282180 scopus 로고
    • Cis-acting sequences responsible for anterior localization of bicoid mRNA in Drosophila embryos
    • 3143913 1:CAS:528:DyaL1MXlt1aluw%3D%3D 10.1038/336595a0
    • PM Macdonald G Struhl 1988 Cis-acting sequences responsible for anterior localization of bicoid mRNA in Drosophila embryos Nature 336 6199 595 598 3143913 1:CAS:528:DyaL1MXlt1aluw%3D%3D 10.1038/336595a0
    • (1988) Nature , vol.336 , Issue.6199 , pp. 595-598
    • MacDonald, P.M.1    Struhl, G.2
  • 94
    • 0027203592 scopus 로고
    • Multiple RNA regulatory elements mediate distinct steps in localization of oskar mRNA
    • 8275853 1:CAS:528:DyaK2cXivFWhsbg%3D
    • J Kim-Ha PJ Webster JL Smith PM Macdonald 1993 Multiple RNA regulatory elements mediate distinct steps in localization of oskar mRNA Development 119 1 169 178 8275853 1:CAS:528:DyaK2cXivFWhsbg%3D
    • (1993) Development , vol.119 , Issue.1 , pp. 169-178
    • Kim-Ha, J.1    Webster, P.J.2    Smith, J.L.3    MacDonald, P.M.4
  • 95
    • 0035955296 scopus 로고    scopus 로고
    • Dimerization of the 3′UTR of bicoid mRNA involves a two-step mechanism
    • 11676536 1:CAS:528:DC%2BD3MXnslCrsbs%3D 10.1006/jmbi.2001.5057
    • C Wagner I Palacios L Jaeger D St Johnston B Ehresmann C Ehresmann C Brunel 2001 Dimerization of the 3′UTR of bicoid mRNA involves a two-step mechanism J Mol Biol 313 3 511 524 11676536 1:CAS:528:DC%2BD3MXnslCrsbs%3D 10.1006/jmbi.2001.5057
    • (2001) J Mol Biol , vol.313 , Issue.3 , pp. 511-524
    • Wagner, C.1    Palacios, I.2    Jaeger, L.3    St Johnston, D.4    Ehresmann, B.5    Ehresmann, C.6    Brunel, C.7
  • 96
    • 0032545926 scopus 로고    scopus 로고
    • Staufen-dependent localization of prospero mRNA contributes to neuroblast daughter-cell fate
    • 9486649 1:CAS:528:DyaK1cXhtlCjtLo%3D 10.1038/35861
    • J Broadus S Fuerstenberg CQ Doe 1998 Staufen-dependent localization of prospero mRNA contributes to neuroblast daughter-cell fate Nature 391 6669 792 795 9486649 1:CAS:528:DyaK1cXhtlCjtLo%3D 10.1038/35861
    • (1998) Nature , vol.391 , Issue.6669 , pp. 792-795
    • Broadus, J.1    Fuerstenberg, S.2    Doe, C.Q.3
  • 97
    • 80052235798 scopus 로고    scopus 로고
    • Mechanisms of dendritic mRNA transport and its role in synaptic tagging
    • 21878995 1:CAS:528:DC%2BC3MXhtFSltb%2FN 10.1038/emboj.2011.278
    • M Doyle MA Kiebler 2011 Mechanisms of dendritic mRNA transport and its role in synaptic tagging EMBO J 30 17 3540 3552 21878995 1:CAS:528: DC%2BC3MXhtFSltb%2FN 10.1038/emboj.2011.278
    • (2011) EMBO J , vol.30 , Issue.17 , pp. 3540-3552
    • Doyle, M.1    Kiebler, M.A.2
  • 98
    • 0034612640 scopus 로고    scopus 로고
    • Point mutation in an AMPA receptor gene rescues lethality in mice deficient in the RNA-editing enzyme ADAR2
    • 10894545 1:STN:280:DC%2BD3czltFSnsQ%3D%3D 10.1038/35017558
    • M Higuchi S Maas FN Single J Hartner A Rozov N Burnashev D Feldmeyer R Sprengel PH Seeburg 2000 Point mutation in an AMPA receptor gene rescues lethality in mice deficient in the RNA-editing enzyme ADAR2 Nature 406 6791 78 81 10894545 1:STN:280:DC%2BD3czltFSnsQ%3D%3D 10.1038/35017558
    • (2000) Nature , vol.406 , Issue.6791 , pp. 78-81
    • Higuchi, M.1    Maas, S.2    Single, F.N.3    Hartner, J.4    Rozov, A.5    Burnashev, N.6    Feldmeyer, D.7    Sprengel, R.8    Seeburg, P.H.9
  • 99
    • 81855226661 scopus 로고    scopus 로고
    • Role of ADARs in mouse development
    • 21725896 1:CAS:528:DC%2BC38XhsFCqsL7F 10.1007/82-2011-150
    • CR Walkley B Liddicoat JC Hartner 2012 Role of ADARs in mouse development Curr Top Microbiol Immunol 353 197 220 21725896 1:CAS:528:DC%2BC38XhsFCqsL7F 10.1007/82-2011-150
    • (2012) Curr Top Microbiol Immunol , vol.353 , pp. 197-220
    • Walkley, C.R.1    Liddicoat, B.2    Hartner, J.C.3
  • 100
    • 0034682706 scopus 로고    scopus 로고
    • A-to-I pre-mRNA editing in Drosophila is primarily involved in adult nervous system function and integrity
    • 10966106 1:CAS:528:DC%2BD3cXmtFOrsL0%3D 10.1016/S0092-8674(00)00049-0
    • MJ Palladino LP Keegan MA O'Connell RA Reenan 2000 A-to-I pre-mRNA editing in Drosophila is primarily involved in adult nervous system function and integrity Cell 102 4 437 449 10966106 1:CAS:528:DC%2BD3cXmtFOrsL0%3D 10.1016/S0092-8674(00)00049-0
    • (2000) Cell , vol.102 , Issue.4 , pp. 437-449
    • Palladino, M.J.1    Keegan, L.P.2    O'Connell, M.A.3    Reenan, R.A.4
  • 101
    • 21844472772 scopus 로고    scopus 로고
    • Tuning of RNA editing by ADAR is required in Drosophila
    • 15920480 1:CAS:528:DC%2BD2MXltFWrurs%3D 10.1038/sj.emboj.7600691
    • LP Keegan J Brindle A Gallo A Leroy RA Reenan MA O'Connell 2005 Tuning of RNA editing by ADAR is required in Drosophila EMBO J 24 12 2183 2193 15920480 1:CAS:528:DC%2BD2MXltFWrurs%3D 10.1038/sj.emboj.7600691
    • (2005) EMBO J , vol.24 , Issue.12 , pp. 2183-2193
    • Keegan, L.P.1    Brindle, J.2    Gallo, A.3    Leroy, A.4    Reenan, R.A.5    O'Connell, M.A.6
  • 102
    • 81855172227 scopus 로고    scopus 로고
    • Regulation and functions of ADAR in drosophila
    • 21761288 1:CAS:528:DC%2BC38XhsFCqsL%2FN 10.1007/82-2011-152
    • S Paro X Li MA O'Connell LP Keegan 2012 Regulation and functions of ADAR in drosophila Curr Top Microbiol Immunol 353 221 236 21761288 1:CAS:528:DC%2BC38XhsFCqsL%2FN 10.1007/82-2011-152
    • (2012) Curr Top Microbiol Immunol , vol.353 , pp. 221-236
    • Paro, S.1    Li, X.2    O'Connell, M.A.3    Keegan, L.P.4
  • 103
    • 84889676816 scopus 로고    scopus 로고
    • Ribonuclease III and the role of double-stranded RNA processing in bacterial systems
    • doi: 10.1007/978-3-642-21078-5-11 Nicholson AW (2011) Ribonuclease III and the role of double-stranded RNA processing in bacterial systems. Nucl Acids Mol Biol 26:269-297. doi: 10.1007/978-3-642-21078-5-11
    • Nicholson AW (2011) Ribonuclease III and the role of double-stranded RNA processing in bacterial systems. Nucl Acids Mol Biol 26:269-297. doi: 10.1007/978-3-642-21078-5-11
    • (2011) Nucl Acids Mol Biol , vol.26 , pp. 269-297
    • Nicholson, A.W.1
  • 104
    • 0035155389 scopus 로고    scopus 로고
    • The RNase III family: A conserved structure and expanding functions in eukaryotic dsRNA metabolism
    • 11719970 1:CAS:528:DC%2BD3MXptVCru7c%3D
    • B Lamontagne S Larose J Boulanger SA Elela 2001 The RNase III family: a conserved structure and expanding functions in eukaryotic dsRNA metabolism Curr Issues Mol Biol 3 4 71 78 11719970 1:CAS:528:DC%2BD3MXptVCru7c%3D
    • (2001) Curr Issues Mol Biol , vol.3 , Issue.4 , pp. 71-78
    • Lamontagne, B.1    Larose, S.2    Boulanger, J.3    Elela, S.A.4
  • 105
    • 0029071516 scopus 로고
    • Protein-RNA recognition
    • 7574494 1:CAS:528:DyaK2MXmsl2qtrw%3D 10.1146/annurev.bi.64.070195.003113
    • DE Draper 1995 Protein-RNA recognition Annu Rev Biochem 64 593 620 7574494 1:CAS:528:DyaK2MXmsl2qtrw%3D 10.1146/annurev.bi.64.070195.003113
    • (1995) Annu Rev Biochem , vol.64 , pp. 593-620
    • Draper, D.E.1
  • 106
    • 0032727991 scopus 로고    scopus 로고
    • Themes in RNA-protein recognition
    • 10550207 1:CAS:528:DyaK1MXms12rt7k%3D 10.1006/jmbi.1999.2991
    • DE Draper 1999 Themes in RNA-protein recognition J Mol Biol 293 2 255 270 10550207 1:CAS:528:DyaK1MXms12rt7k%3D 10.1006/jmbi.1999.2991
    • (1999) J Mol Biol , vol.293 , Issue.2 , pp. 255-270
    • Draper, D.E.1
  • 107
    • 33749151151 scopus 로고    scopus 로고
    • Structure of an AAGU tetraloop and its contribution to substrate selection by yeast RNase III
    • 16979185 1:CAS:528:DC%2BD28XhtVajsLvJ 10.1016/j.jmb.2006.08.029
    • C Gaudin G Ghazal S Yoshizawa SA Elela D Fourmy 2006 Structure of an AAGU tetraloop and its contribution to substrate selection by yeast RNase III J Mol Biol 363 2 322 331 16979185 1:CAS:528:DC%2BD28XhtVajsLvJ 10.1016/j.jmb.2006.08. 029
    • (2006) J Mol Biol , vol.363 , Issue.2 , pp. 322-331
    • Gaudin, C.1    Ghazal, G.2    Yoshizawa, S.3    Elela, S.A.4    Fourmy, D.5
  • 108
    • 33749135948 scopus 로고    scopus 로고
    • Characterization of the reactivity determinants of a novel hairpin substrate of yeast RNase III
    • 16962133 1:CAS:528:DC%2BD28XhtVajsLvK 10.1016/j.jmb.2006.08.028
    • G Ghazal SA Elela 2006 Characterization of the reactivity determinants of a novel hairpin substrate of yeast RNase III J Mol Biol 363 2 332 344 16962133 1:CAS:528:DC%2BD28XhtVajsLvK 10.1016/j.jmb.2006.08.028
    • (2006) J Mol Biol , vol.363 , Issue.2 , pp. 332-344
    • Ghazal, G.1    Elela, S.A.2
  • 109
    • 0031470503 scopus 로고    scopus 로고
    • Regulation of ribonuclease III processing by double-helical sequence antideterminants
    • 9391043 1:CAS:528:DyaK2sXotVamtbY%3D 10.1073/pnas.94.25.13437
    • K Zhang AW Nicholson 1997 Regulation of ribonuclease III processing by double-helical sequence antideterminants Proc Natl Acad Sci USA 94 25 13437 13441 9391043 1:CAS:528:DyaK2sXotVamtbY%3D 10.1073/pnas.94.25.13437
    • (1997) Proc Natl Acad Sci USA , vol.94 , Issue.25 , pp. 13437-13441
    • Zhang, K.1    Nicholson, A.W.2
  • 110
    • 33747038694 scopus 로고    scopus 로고
    • Characterization of RNA sequence determinants and antideterminants of processing reactivity for a minimal substrate of Escherichia coli ribonuclease III
    • 16896014 1:CAS:528:DC%2BD28Xps1yjtbs%3D 10.1093/nar/gkl459
    • AV Pertzev AW Nicholson 2006 Characterization of RNA sequence determinants and antideterminants of processing reactivity for a minimal substrate of Escherichia coli ribonuclease III Nucleic Acids Res 34 13 3708 3721 16896014 1:CAS:528:DC%2BD28Xps1yjtbs%3D 10.1093/nar/gkl459
    • (2006) Nucleic Acids Res , vol.34 , Issue.13 , pp. 3708-3721
    • Pertzev, A.V.1    Nicholson, A.W.2
  • 111
    • 77955702062 scopus 로고    scopus 로고
    • Thermotoga maritima ribonuclease III. Characterization of thermostable biochemical behavior and analysis of conserved base pairs that function as reactivity epitopes for the Thermotoga 23S rRNA precursor
    • 20677811 1:CAS:528:DC%2BC3cXpsFKjt78%3D 10.1021/bi100930u
    • L Nathania AW Nicholson 2010 Thermotoga maritima ribonuclease III. Characterization of thermostable biochemical behavior and analysis of conserved base pairs that function as reactivity epitopes for the Thermotoga 23S rRNA precursor Biochemistry 49 33 7164 7178 20677811 1:CAS:528:DC%2BC3cXpsFKjt78%3D 10.1021/bi100930u
    • (2010) Biochemistry , vol.49 , Issue.33 , pp. 7164-7178
    • Nathania, L.1    Nicholson, A.W.2
  • 112
    • 79954586093 scopus 로고    scopus 로고
    • Characterization of Aquifex aeolicus ribonuclease III and the reactivity epitopes of its pre-ribosomal RNA substrates
    • 21138964 1:CAS:528:DC%2BC3MXkvFansbY%3D 10.1093/nar/gkq1030
    • Z Shi RH Nicholson R Jaggi AW Nicholson 2011 Characterization of Aquifex aeolicus ribonuclease III and the reactivity epitopes of its pre-ribosomal RNA substrates Nucleic Acids Res 39 7 2756 2768 21138964 1:CAS:528: DC%2BC3MXkvFansbY%3D 10.1093/nar/gkq1030
    • (2011) Nucleic Acids Res , vol.39 , Issue.7 , pp. 2756-2768
    • Shi, Z.1    Nicholson, R.H.2    Jaggi, R.3    Nicholson, A.W.4
  • 113
    • 80052460364 scopus 로고    scopus 로고
    • Functional conservation in human and Drosophila of Metazoan ADAR2 involved in RNA editing: Loss of ADAR1 in insects
    • 21622951 1:CAS:528:DC%2BC3MXhtFehtr7P 10.1093/nar/gkr423
    • LP Keegan L McGurk JP Palavicini J Brindle S Paro X Li JJ Rosenthal MA O'Connell 2011 Functional conservation in human and Drosophila of Metazoan ADAR2 involved in RNA editing: loss of ADAR1 in insects Nucleic Acids Res 39 16 7249 7262 21622951 1:CAS:528:DC%2BC3MXhtFehtr7P 10.1093/nar/gkr423
    • (2011) Nucleic Acids Res , vol.39 , Issue.16 , pp. 7249-7262
    • Keegan, L.P.1    McGurk, L.2    Palavicini, J.P.3    Brindle, J.4    Paro, S.5    Li, X.6    Rosenthal, J.J.7    O'Connell, M.A.8
  • 115
    • 0035997389 scopus 로고    scopus 로고
    • RNA editing by adenosine deaminases that act on RNA
    • 12045112 1:CAS:528:DC%2BD38Xos1Clt7g%3D 10.1146/annurev.biochem.71. 110601.135501
    • BL Bass 2002 RNA editing by adenosine deaminases that act on RNA Annu Rev Biochem 71 817 846 12045112 1:CAS:528:DC%2BD38Xos1Clt7g%3D 10.1146/annurev. biochem.71.110601.135501
    • (2002) Annu Rev Biochem , vol.71 , pp. 817-846
    • Bass, B.L.1
  • 116
    • 0034711082 scopus 로고    scopus 로고
    • Double-stranded RNA adenosine deaminases ADAR1 and ADAR2 have overlapping specificities
    • 11041852 1:CAS:528:DC%2BD3cXmsl2jsL4%3D 10.1021/bi001383g
    • KA Lehmann BL Bass 2000 Double-stranded RNA adenosine deaminases ADAR1 and ADAR2 have overlapping specificities Biochemistry 39 42 12875 12884 11041852 1:CAS:528:DC%2BD3cXmsl2jsL4%3D 10.1021/bi001383g
    • (2000) Biochemistry , vol.39 , Issue.42 , pp. 12875-12884
    • Lehmann, K.A.1    Bass, B.L.2
  • 117
    • 0024297354 scopus 로고
    • Multiple sequence alignment with hierarchical clustering
    • 2849754 1:CAS:528:DyaL1MXjsVOqtA%3D%3D 10.1093/nar/16.22.10881
    • F Corpet 1988 Multiple sequence alignment with hierarchical clustering Nucleic Acids Res 16 22 10881 10890 2849754 1:CAS:528:DyaL1MXjsVOqtA%3D%3D 10.1093/nar/16.22.10881
    • (1988) Nucleic Acids Res , vol.16 , Issue.22 , pp. 10881-10890
    • Corpet, F.1
  • 118
    • 0034161321 scopus 로고    scopus 로고
    • NPS@: Network protein sequence analysis
    • 10694887 1:CAS:528:DC%2BD3cXhsleiu7Y%3D 10.1016/S0968-0004(99)01540-6
    • C Combet C Blanchet C Geourjon G Deléage 2000 NPS@: network protein sequence analysis Trends Biochem Sci 25 3 147 150 10694887 1:CAS:528:DC%2BD3cXhsleiu7Y%3D 10.1016/S0968-0004(99)01540-6
    • (2000) Trends Biochem Sci , vol.25 , Issue.3 , pp. 147-150
    • Combet, C.1    Blanchet, C.2    Geourjon, C.3    Deléage, G.4


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.