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Volumn 14, Issue 2, 2006, Pages 345-355

Structure and specific RNA binding of ADAR2 double-stranded RNA binding motifs

Author keywords

[No Author keywords available]

Indexed keywords

DOUBLE STRANDED RNA;

EID: 32044468729     PISSN: 09692126     EISSN: None     Source Type: Journal    
DOI: 10.1016/j.str.2005.11.013     Document Type: Article
Times cited : (98)

References (67)
  • 1
    • 0034672094 scopus 로고    scopus 로고
    • Molecular basis of sequence-specific recognition of pre-ribosomal RNA by nucleolin
    • F.H. Allain, P. Bouvet, T. Dieckmann, and J. Feigon Molecular basis of sequence-specific recognition of pre-ribosomal RNA by nucleolin EMBO J. 19 2000 6870 6881
    • (2000) EMBO J. , vol.19 , pp. 6870-6881
    • Allain, F.H.1    Bouvet, P.2    Dieckmann, T.3    Feigon, J.4
  • 2
    • 0033962272 scopus 로고    scopus 로고
    • A phylogenetic analysis reveals an unusual sequence conservation within introns involved in RNA editing
    • P.J. Aruscavage, and B.L. Bass A phylogenetic analysis reveals an unusual sequence conservation within introns involved in RNA editing RNA 6 2000 257 269
    • (2000) RNA , vol.6 , pp. 257-269
    • Aruscavage, P.J.1    Bass, B.L.2
  • 3
    • 12344300804 scopus 로고    scopus 로고
    • Widespread A-to-I RNA editing of Alu-containing mRNAs in the human transcriptome
    • A. Athanasiadis, A. Rich, and S. Maas Widespread A-to-I RNA editing of Alu-containing mRNAs in the human transcriptome PLoS Biol. 2 2004 e391
    • (2004) PLoS Biol. , vol.2 , pp. 391
    • Athanasiadis, A.1    Rich, A.2    Maas, S.3
  • 4
    • 0033654297 scopus 로고    scopus 로고
    • Generalized born models of macromolecular solvation effects
    • D. Bashford, and D.A. Case Generalized born models of macromolecular solvation effects Annu. Rev. Phys. Chem. 51 2000 129 152
    • (2000) Annu. Rev. Phys. Chem. , vol.51 , pp. 129-152
    • Bashford, D.1    Case, D.A.2
  • 5
    • 0035997389 scopus 로고    scopus 로고
    • RNA editing by adenosine deaminases that act on RNA
    • B.L. Bass RNA editing by adenosine deaminases that act on RNA Annu. Rev. Biochem. 71 2002 817 846
    • (2002) Annu. Rev. Biochem. , vol.71 , pp. 817-846
    • Bass, B.L.1
  • 6
    • 0024233053 scopus 로고
    • An unwinding activity that covalently modifies its double-stranded RNA substrate
    • B.L. Bass, and H. Weintraub An unwinding activity that covalently modifies its double-stranded RNA substrate Cell 55 1988 1089 1098
    • (1988) Cell , vol.55 , pp. 1089-1098
    • Bass, B.L.1    Weintraub, H.2
  • 7
    • 4744347763 scopus 로고    scopus 로고
    • Control of human potassium channel inactivation by editing of a small mRNA hairpin
    • T. Bhalla, J.J. Rosenthal, M. Holmgren, and R. Reenan Control of human potassium channel inactivation by editing of a small mRNA hairpin Nat. Struct. Mol. Biol. 11 2004 950 956
    • (2004) Nat. Struct. Mol. Biol. , vol.11 , pp. 950-956
    • Bhalla, T.1    Rosenthal, J.J.2    Holmgren, M.3    Reenan, R.4
  • 11
    • 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
    • M. Bycroft, S. Grunert, A.G. Murzin, M. Proctor, and D. Stjohnston 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 1995 3563 3571
    • (1995) EMBO J. , vol.14 , pp. 3563-3571
    • Bycroft, M.1    Grunert, S.2    Murzin, A.G.3    Proctor, M.4    Stjohnston, D.5
  • 12
    • 0042838304 scopus 로고    scopus 로고
    • Recognition of double-stranded RNA by proteins and small molecules
    • C.B. Carlson, O.M. Stephens, and P.A. Beal Recognition of double-stranded RNA by proteins and small molecules Biopolymers 70 2003 86 102
    • (2003) Biopolymers , vol.70 , pp. 86-102
    • Carlson, C.B.1    Stephens, O.M.2    Beal, P.A.3
  • 14
    • 0037592977 scopus 로고    scopus 로고
    • Requirement of dimerization for RNA editing activity of adenosine deaminases acting on RNA
    • D.S. Cho, W. Yang, J.T. Lee, R. Shiekhattar, J.M. Murray, and K. Nishikura Requirement of dimerization for RNA editing activity of adenosine deaminases acting on RNA J. Biol. Chem. 278 2003 17093 17102
    • (2003) J. Biol. Chem. , vol.278 , pp. 17093-17102
    • Cho, D.S.1    Yang, W.2    Lee, J.T.3    Shiekhattar, R.4    Murray, J.M.5    Nishikura, K.6
  • 16
    • 1042289731 scopus 로고    scopus 로고
    • Structure and sequence determinants required for the RNA editing of ADAR2 substrates
    • T.R. Dawson, C.L. Sansam, and R.B. Emeson Structure and sequence determinants required for the RNA editing of ADAR2 substrates J. Biol. Chem. 279 2004 4941 4951
    • (2004) J. Biol. Chem. , vol.279 , pp. 4941-4951
    • Dawson, T.R.1    Sansam, C.L.2    Emeson, R.B.3
  • 18
    • 0033578927 scopus 로고    scopus 로고
    • Recognition of polyadenylate RNA by the poly(A)-binding protein
    • R.C. Deo, J.B. Bonanno, N. Sonenberg, and S.K. Burley Recognition of polyadenylate RNA by the poly(A)-binding protein Cell 98 1999 835 845
    • (1999) Cell , vol.98 , pp. 835-845
    • Deo, R.C.1    Bonanno, J.B.2    Sonenberg, N.3    Burley, S.K.4
  • 19
    • 0037442962 scopus 로고    scopus 로고
    • HADDOCK: A protein-protein docking approach based on biochemical or biophysical information
    • C. Dominguez, R. Boelens, and A.M. Bonvin HADDOCK: a protein-protein docking approach based on biochemical or biophysical information J. Am. Chem. Soc. 125 2003 1731 1737
    • (2003) J. Am. Chem. Soc. , vol.125 , pp. 1731-1737
    • Dominguez, C.1    Boelens, R.2    Bonvin, A.M.3
  • 20
    • 0036966283 scopus 로고    scopus 로고
    • New and old roles of the double-stranded RNA-binding domain
    • M. Doyle, and M.F. Jantsch New and old roles of the double-stranded RNA-binding domain J. Struct. Biol. 140 2002 147 153
    • (2002) J. Struct. Biol. , vol.140 , pp. 147-153
    • Doyle, M.1    Jantsch, M.F.2
  • 21
    • 0027339321 scopus 로고
    • 2+ permeability of unedited and edited versions of the kainate selective glutamate receptor GluR6
    • 2+ permeability of unedited and edited versions of the kainate selective glutamate receptor GluR6 Proc. Natl. Acad. Sci. USA 90 1993 755 759
    • (1993) Proc. Natl. Acad. Sci. USA , vol.90 , pp. 755-759
    • Egebjerg, J.1    Heinemann, S.F.2
  • 22
    • 0000200738 scopus 로고    scopus 로고
    • Adenosine to inosine RNA editing: Substrates and consequences
    • B.L. Bass Oxford University Press London
    • R.B. Emeson, and M. Singh Adenosine to inosine RNA editing: substrates and consequences B.L. Bass RNA Editing: Frontiers in Molecular Biology 2000 Oxford University Press London 109 138
    • (2000) RNA Editing: Frontiers in Molecular Biology , pp. 109-138
    • Emeson, R.B.1    Singh, M.2
  • 23
    • 0034192148 scopus 로고    scopus 로고
    • Proteins binding to duplexed RNA: One motif, multiple functions
    • I. Fierro-Monti, and M.B. Mathews Proteins binding to duplexed RNA: one motif, multiple functions Trends Biochem. Sci. 25 2000 241 246
    • (2000) Trends Biochem. Sci. , vol.25 , pp. 241-246
    • Fierro-Monti, I.1    Mathews, M.B.2
  • 24
    • 0037587631 scopus 로고    scopus 로고
    • An ADAR that edits transcripts encoding ion channel subunits functions as a dimer
    • A. Gallo, L.P. Keegan, G.M. Ring, and M.A. O'Connell An ADAR that edits transcripts encoding ion channel subunits functions as a dimer EMBO J. 22 2003 3421 3430
    • (2003) EMBO J. , vol.22 , pp. 3421-3430
    • Gallo, A.1    Keegan, L.P.2    Ring, G.M.3    O'Connell, M.A.4
  • 25
    • 0035369742 scopus 로고    scopus 로고
    • RNA editing by base deamination: More enzymes, more targets, new mysteries
    • A.P. Gerber, and W. Keller RNA editing by base deamination: more enzymes, more targets, new mysteries Trends Biochem. Sci. 26 2001 376 384
    • (2001) Trends Biochem. Sci. , vol.26 , pp. 376-384
    • Gerber, A.P.1    Keller, W.2
  • 27
    • 0031576336 scopus 로고    scopus 로고
    • Torsion angle dynamics for NMR structure calculation with the new program DYANA
    • P. Guntert, C. Mumenthaler, and K. Wuthrich Torsion angle dynamics for NMR structure calculation with the new program DYANA J. Mol. Biol. 273 1997 283 298
    • (1997) J. Mol. Biol. , vol.273 , pp. 283-298
    • Guntert, P.1    Mumenthaler, C.2    Wuthrich, K.3
  • 29
    • 0036308102 scopus 로고    scopus 로고
    • Protein NMR structure determination with automated NOE assignment using the new software CANDID and the torsion angle dynamics algorithm DYANA
    • T. Herrmann, P. Guntert, and K. Wuthrich Protein NMR structure determination with automated NOE assignment using the new software CANDID and the torsion angle dynamics algorithm DYANA J. Mol. Biol. 319 2002 209 227
    • (2002) J. Mol. Biol. , vol.319 , pp. 209-227
    • Herrmann, T.1    Guntert, P.2    Wuthrich, K.3
  • 30
    • 0042528670 scopus 로고    scopus 로고
    • Nervous system targets of RNA editing identified by comparative genomics
    • B. Hoopengardner, T. Bhalla, C. Staber, and R. Reenan Nervous system targets of RNA editing identified by comparative genomics Science 301 2003 832 836
    • (2003) Science , vol.301 , pp. 832-836
    • Hoopengardner, B.1    Bhalla, T.2    Staber, C.3    Reenan, R.4
  • 31
    • 0037020153 scopus 로고    scopus 로고
    • Adenosine to inosine editing by ADAR2 requires formation of a ternary complex on the GluR-B R/G site
    • D.C. Jaikaran, C.H. Collins, and A.M. MacMillan Adenosine to inosine editing by ADAR2 requires formation of a ternary complex on the GluR-B R/G site J. Biol. Chem. 277 2002 37624 37629
    • (2002) J. Biol. Chem. , vol.277 , pp. 37624-37629
    • Jaikaran, D.C.1    Collins, C.H.2    MacMillan, A.M.3
  • 32
    • 32044460445 scopus 로고    scopus 로고
    • Jovine, L. (2003). NUCCYL (http://www.biosci.ki.se/groups/ljo/software/ nuccyl.html).
    • (2003) NUCCYL
    • Jovine, L.1
  • 33
    • 0344012481 scopus 로고    scopus 로고
    • ADAR2 A→I editing: Site selectivity and editing efficiency are separate events
    • A.M. Kallman, M. Sahlin, and M. Ohman ADAR2 A→I editing: site selectivity and editing efficiency are separate events Nucleic Acids Res. 31 2003 4874 4881
    • (2003) Nucleic Acids Res. , vol.31 , pp. 4874-4881
    • Kallman, A.M.1    Sahlin, M.2    Ohman, M.3
  • 35
    • 0029058994 scopus 로고
    • Structure of the Dsrna binding domain of Escherichia coli Rnase-Iii
    • A. Kharrat, M.J. Macias, T.J. Gibson, M. Nilges, and A. Pastore Structure of the Dsrna binding domain of Escherichia coli Rnase-Iii EMBO J. 14 1995 3572 3584
    • (1995) EMBO J. , vol.14 , pp. 3572-3584
    • Kharrat, A.1    MacIas, M.J.2    Gibson, T.J.3    Nilges, M.4    Pastore, A.5
  • 36
    • 0037705633 scopus 로고    scopus 로고
    • Biochemical analysis and scanning force microscopy reveal productive and nonproductive ADAR2 binding to RNA substrates
    • Y. Klaue, A.M. Kallman, M. Bonin, W. Nellen, and M. Ohman Biochemical analysis and scanning force microscopy reveal productive and nonproductive ADAR2 binding to RNA substrates RNA 9 2003 839 846
    • (2003) RNA , vol.9 , pp. 839-846
    • Klaue, Y.1    Kallman, A.M.2    Bonin, M.3    Nellen, W.4    Ohman, M.5
  • 37
    • 0027339892 scopus 로고
    • 2+ permeability in both TM1 and TM2 of high affinity kainate receptor channels: Diversity by RNA editing
    • 2+ permeability in both TM1 and TM2 of high affinity kainate receptor channels: diversity by RNA editing Neuron 10 1993 491 500
    • (1993) Neuron , vol.10 , pp. 491-500
    • Kohler, M.1    Burnashev, N.2    Sakmann, B.3    Seeburg, P.H.4
  • 38
    • 0030339738 scopus 로고    scopus 로고
    • AQUA and PROCHECK-NMR: Programs for checking the quality of protein structures solved by NMR
    • R.A. Laskowski, J.A. Rullmannn, M.W. MacArthur, R. Kaptein, and J.M. Thornton AQUA and PROCHECK-NMR: programs for checking the quality of protein structures solved by NMR J. Biomol. NMR 8 1996 477 486
    • (1996) J. Biomol. NMR , vol.8 , pp. 477-486
    • Laskowski, R.A.1    Rullmannn, J.A.2    MacArthur, M.W.3    Kaptein, R.4    Thornton, J.M.5
  • 42
    • 0242581682 scopus 로고    scopus 로고
    • Crystal structure of a zinc-finger-RNA complex reveals two modes of molecular recognition
    • D. Lu, M.A. Searles, and A. Klug Crystal structure of a zinc-finger-RNA complex reveals two modes of molecular recognition Nature 426 2003 96 100
    • (2003) Nature , vol.426 , pp. 96-100
    • Lu, D.1    Searles, M.A.2    Klug, A.3
  • 43
    • 4644339417 scopus 로고    scopus 로고
    • Evidence for auto-inhibition by the N terminus of hADAR2 and activation by dsRNA binding
    • M.R. Macbeth, A.T. Lingam, and B.L. Bass Evidence for auto-inhibition by the N terminus of hADAR2 and activation by dsRNA binding RNA 10 2004 1563 1571
    • (2004) RNA , vol.10 , pp. 1563-1571
    • MacBeth, M.R.1    Lingam, A.T.2    Bass, B.L.3
  • 44
    • 24644519954 scopus 로고    scopus 로고
    • Inositol hexakisphosphate is bound in the ADAR2 core and required for RNA editing
    • M.R. Macbeth, H.L. Schubert, A.P. Vandemark, A.T. Lingam, C.P. Hill, and B.L. Bass Inositol hexakisphosphate is bound in the ADAR2 core and required for RNA editing Science 309 2005 1534 1539
    • (2005) Science , vol.309 , pp. 1534-1539
    • MacBeth, M.R.1    Schubert, H.L.2    Vandemark, A.P.3    Lingam, A.T.4    Hill, C.P.5    Bass, B.L.6
  • 45
    • 0033022121 scopus 로고    scopus 로고
    • Long RNA hairpins that contain inosine are present in Caenorhabditis elegans poly(A)+ RNA
    • D.P. Morse, and B.L. Bass Long RNA hairpins that contain inosine are present in Caenorhabditis elegans poly(A)+ RNA Proc. Natl. Acad. Sci. USA 96 1999 6048 6053
    • (1999) Proc. Natl. Acad. Sci. USA , vol.96 , pp. 6048-6053
    • Morse, D.P.1    Bass, B.L.2
  • 46
    • 0037062438 scopus 로고    scopus 로고
    • RNA hairpins in noncoding regions of human brain and Caenorhabditis elegans mRNA are edited by adenosine deaminases that act on RNA
    • D.P. Morse, P.J. Aruscavage, and B.L. Bass RNA hairpins in noncoding regions of human brain and Caenorhabditis elegans mRNA are edited by adenosine deaminases that act on RNA Proc. Natl. Acad. Sci. USA 99 2002 7906 7911
    • (2002) Proc. Natl. Acad. Sci. USA , vol.99 , pp. 7906-7911
    • Morse, D.P.1    Aruscavage, P.J.2    Bass, B.L.3
  • 47
    • 0033543577 scopus 로고    scopus 로고
    • Altered flexibility in the substrate-binding site of related native and engineered high-alkaline Bacillus subtilisins
    • F.A. Mulder, D. Schipper, R. Bott, and R. Boelens Altered flexibility in the substrate-binding site of related native and engineered high-alkaline Bacillus subtilisins J. Mol. Biol. 292 1999 111 123
    • (1999) J. Mol. Biol. , vol.292 , pp. 111-123
    • Mulder, F.A.1    Schipper, D.2    Bott, R.3    Boelens, R.4
  • 48
    • 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
    • S. Nanduri, B.W. Carpick, Y.W. Yang, B.R.G. Williams, and J. Qin 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 1998 5458 5465
    • (1998) EMBO J. , vol.17 , pp. 5458-5465
    • Nanduri, S.1    Carpick, B.W.2    Yang, Y.W.3    Williams, B.R.G.4    Qin, J.5
  • 49
    • 0342748466 scopus 로고    scopus 로고
    • In vitro analysis of the binding of ADAR2 to the pre-mRNA encoding the GluR-B R/G site
    • M. Ohman, A.M. Kallman, and B.L. Bass In vitro analysis of the binding of ADAR2 to the pre-mRNA encoding the GluR-B R/G site RNA 6 2000 687 697
    • (2000) RNA , vol.6 , pp. 687-697
    • Ohman, M.1    Kallman, A.M.2    Bass, B.L.3
  • 50
    • 0036755397 scopus 로고    scopus 로고
    • Refinement of d(GCGAAGC) hairpin structure using one- and two-bond residual dipolar couplings
    • P. Padrta, R. Stefl, L. Kralik, L. Zidek, and V. Sklenar Refinement of d(GCGAAGC) hairpin structure using one- and two-bond residual dipolar couplings J. Biomol. NMR 24 2002 1 14
    • (2002) J. Biomol. NMR , vol.24 , pp. 1-14
    • Padrta, P.1    Stefl, R.2    Kralik, L.3    Zidek, L.4    Sklenar, V.5
  • 51
    • 1242340502 scopus 로고    scopus 로고
    • New applications of 2D filtered/edited NOESY for assignment and structure elucidation of RNA and RNA-protein complexes
    • R.D. Peterson, C.A. Theimer, H. Wu, and J. Feigon New applications of 2D filtered/edited NOESY for assignment and structure elucidation of RNA and RNA-protein complexes J. Biomol. NMR 28 2004 59 67
    • (2004) J. Biomol. NMR , vol.28 , pp. 59-67
    • Peterson, R.D.1    Theimer, C.A.2    Wu, H.3    Feigon, J.4
  • 53
    • 0033529064 scopus 로고    scopus 로고
    • Regulation of alternative splicing by RNA editing
    • S.M. Rueter, T.R. Dawson, and R.B. Emeson Regulation of alternative splicing by RNA editing Nature 399 1999 75 80
    • (1999) Nature , vol.399 , pp. 75-80
    • Rueter, S.M.1    Dawson, T.R.2    Emeson, R.B.3
  • 54
    • 0032535613 scopus 로고    scopus 로고
    • Molecular basis of double-stranded RNA-protein interactions: Structure of a dsRNA-binding domain complexed with dsRNA
    • J.M. Ryter, and S.C. Schultz Molecular basis of double-stranded RNA-protein interactions: structure of a dsRNA-binding domain complexed with dsRNA EMBO J. 17 1998 7505 7513
    • (1998) EMBO J. , vol.17 , pp. 7505-7513
    • Ryter, J.M.1    Schultz, S.C.2
  • 55
    • 0345133268 scopus 로고    scopus 로고
    • Modulation of RNA editing by functional nucleolar sequestration of ADAR2
    • C.L. Sansam, K.S. Wells, and R.B. Emeson Modulation of RNA editing by functional nucleolar sequestration of ADAR2 Proc. Natl. Acad. Sci. USA 100 2003 14018 14023
    • (2003) Proc. Natl. Acad. Sci. USA , vol.100 , pp. 14018-14023
    • Sansam, C.L.1    Wells, K.S.2    Emeson, R.B.3
  • 56
    • 0024380087 scopus 로고
    • Rapid detection of octamer binding proteins with 'mini-extracts,' prepared from a small number of cells
    • E. Schreiber, P. Matthias, M.M. Muller, and W. Schaffner Rapid detection of octamer binding proteins with 'mini-extracts,' prepared from a small number of cells Nucleic Acids Res. 17 1989 6419
    • (1989) Nucleic Acids Res. , vol.17 , pp. 6419
    • Schreiber, E.1    Matthias, P.2    Muller, M.M.3    Schaffner, W.4
  • 57
    • 0032077722 scopus 로고    scopus 로고
    • RNA editing of brain glutamate receptor channels: Mechanism and physiology
    • P.H. Seeburg, M. Higuchi, and R. Sprengel RNA editing of brain glutamate receptor channels: mechanism and physiology Brain Res. Brain Res. Rev. 26 1998 217 229
    • (1998) Brain Res. Brain Res. Rev. , vol.26 , pp. 217-229
    • Seeburg, P.H.1    Higuchi, M.2    Sprengel, R.3
  • 58
    • 0025995296 scopus 로고
    • RNA editing in brain controls a determinant of ion flow in glutamate-gated channels
    • B. Sommer, M. Kohler, R. Sprengel, and P.H. Seeburg RNA editing in brain controls a determinant of ion flow in glutamate-gated channels Cell 67 1991 11 19
    • (1991) Cell , vol.67 , pp. 11-19
    • Sommer, B.1    Kohler, M.2    Sprengel, R.3    Seeburg, P.H.4
  • 59
    • 17844397456 scopus 로고    scopus 로고
    • A novel RNA pentaloop fold involved in targeting ADAR2
    • R. Stefl, and F.H. Allain A novel RNA pentaloop fold involved in targeting ADAR2 RNA 11 2005 592 597
    • (2005) RNA , vol.11 , pp. 592-597
    • Stefl, R.1    Allain, F.H.2
  • 60
    • 17844404891 scopus 로고    scopus 로고
    • RNA sequence- and shape-dependent recognition by proteins in the ribonucleoprotein particle
    • R. Stefl, L. Skrisovska, and F.H. Allain RNA sequence- and shape-dependent recognition by proteins in the ribonucleoprotein particle EMBO Rep. 6 2005 33 38
    • (2005) EMBO Rep. , vol.6 , pp. 33-38
    • Stefl, R.1    Skrisovska, L.2    Allain, F.H.3
  • 61
    • 22444447868 scopus 로고    scopus 로고
    • Resonance assignments of the double-stranded RNA-binding domains of adenosine deaminase acting on RNA 2 (ADAR2)
    • R. Stefl, L. Skrisovska, M. Xu, R.B. Emeson, and F.H. Allain Resonance assignments of the double-stranded RNA-binding domains of adenosine deaminase acting on RNA 2 (ADAR2) J. Biomol. NMR 31 2005 71 72
    • (2005) J. Biomol. NMR , vol.31 , pp. 71-72
    • Stefl, R.1    Skrisovska, L.2    Xu, M.3    Emeson, R.B.4    Allain, F.H.5
  • 62
    • 4644234057 scopus 로고    scopus 로고
    • The binding selectivity of ADAR2's dsRBMs contributes to RNA-editing selectivity
    • O.M. Stephens, B.L. Haudenschild, and P.A. Beal The binding selectivity of ADAR2's dsRBMs contributes to RNA-editing selectivity Chem. Biol. 11 2004 1239 1250
    • (2004) Chem. Biol. , vol.11 , pp. 1239-1250
    • Stephens, O.M.1    Haudenschild, B.L.2    Beal, P.A.3
  • 63
    • 0344305774 scopus 로고    scopus 로고
    • Mutations in RNAi rescue aberrant chemotaxis of ADAR mutants
    • L.A. Tonkin, and B.L. Bass Mutations in RNAi rescue aberrant chemotaxis of ADAR mutants Science 302 2003 1725
    • (2003) Science , vol.302 , pp. 1725
    • Tonkin, L.A.1    Bass, B.L.2
  • 64
    • 0025913797 scopus 로고
    • Role of biased hypermutation in evolution of subacute sclerosing panencephalitis virus from progenitor acute measles virus
    • T.C. Wong, M. Ayata, S. Ueda, and A. Hirano Role of biased hypermutation in evolution of subacute sclerosing panencephalitis virus from progenitor acute measles virus J. Virol. 65 1991 2191 2199
    • (1991) J. Virol. , vol.65 , pp. 2191-2199
    • Wong, T.C.1    Ayata, M.2    Ueda, S.3    Hirano, A.4
  • 65
    • 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
    • H. Wu, A. Henras, G. Chanfreau, and J. Feigon 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 2004 8307 8312
    • (2004) Proc. Natl. Acad. Sci. USA , vol.101 , pp. 8307-8312
    • Wu, H.1    Henras, A.2    Chanfreau, G.3    Feigon, J.4
  • 66
    • 0035943347 scopus 로고    scopus 로고
    • The fate of dsRNA in the nucleus: A p54(nrb)-containing complex mediates the nuclear retention of promiscuously A-to-I edited RNAs
    • Z. Zhang, and G.G. Carmichael The fate of dsRNA in the nucleus: a p54(nrb)-containing complex mediates the nuclear retention of promiscuously A-to-I edited RNAs Cell 106 2001 465 475
    • (2001) Cell , vol.106 , pp. 465-475
    • Zhang, Z.1    Carmichael, G.G.2
  • 67
    • 0034987544 scopus 로고    scopus 로고
    • A solubility-enhancement tag (SET) for NMR studies of poorly behaving proteins
    • P. Zhou, A.A. Lugovskoy, and G. Wagner A solubility-enhancement tag (SET) for NMR studies of poorly behaving proteins J. Biomol. NMR 20 2001 11 14
    • (2001) J. Biomol. NMR , vol.20 , pp. 11-14
    • Zhou, P.1    Lugovskoy, A.A.2    Wagner, G.3


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