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Volumn 40, Issue 19, 2012, Pages 9825-9835

Nucleoside analog studies indicate mechanistic differences between RNA-editing adenosine deaminases

Author keywords

[No Author keywords available]

Indexed keywords

ADENOSINE DEAMINASE; ADENOSINE DEAMINASE ACTING ON RNA 1; ADENOSINE DEAMINASE ACTING ON RNA 2; AMINO ACID; NUCLEOSIDE DERIVATIVE; RNA EDITING ADENOSINE DEAMINASE; UNCLASSIFIED DRUG;

EID: 84868088487     PISSN: 03051048     EISSN: 13624962     Source Type: Journal    
DOI: 10.1093/nar/gks752     Document Type: Article
Times cited : (23)

References (82)
  • 1
    • 84862185370 scopus 로고    scopus 로고
    • SpliceDisease database: Linking RNA splicing and disease
    • Wang, J., Zhang, J., Li, K., Zhao, W. and Cui, Q. (2012) SpliceDisease database: linking RNA splicing and disease. Nucleic Acids Res., 40, D1055-D1059.
    • (2012) Nucleic Acids Res. , vol.40
    • Wang, J.1    Zhang, J.2    Li, K.3    Zhao, W.4    Cui, Q.5
  • 2
    • 84867597592 scopus 로고    scopus 로고
    • Human mitochondrial diseases caused by lack of taurine modification in mitochondrial tRNAs
    • Suzuki, T., Nagao, A. and Suzuki, T. (2011) Human mitochondrial diseases caused by lack of taurine modification in mitochondrial tRNAs. Wiley Interdiscip. Rev. RNA, 2, 376-386.
    • (2011) Wiley Interdiscip. Rev. RNA , vol.2 , pp. 376-386
    • Suzuki, T.1    Nagao, A.2    Suzuki, T.3
  • 3
    • 0037428129 scopus 로고    scopus 로고
    • Dyskeratosis congenita and cancer in mice deficient in ribosomal RNA modification
    • DOI 10.1126/science.1079447
    • Ruggero, D., Grisendi, S., Piazza, F., Rego, E., Mari, F., Rao, P.H., Cordon-Cardo, C. and Pandolfi, P.P. (2003) Dyskeratosis congenita and cancer in mice deficient in ribosomal RNA modification. Science, 299, 259-262. (Pubitemid 36125213)
    • (2003) Science , vol.299 , Issue.5604 , pp. 259-262
    • Ruggero, D.1    Grisendi, S.2    Piazza, F.3    Rego, E.4    Mari, F.5    Rao, P.H.6    Cordon-Cardo, C.7    Pandolfi, P.P.8
  • 4
    • 0038645126 scopus 로고    scopus 로고
    • RNA editing of serotonin 2C receptor in human postmortem brains of major mental disorders
    • DOI 10.1016/S0304-3940(03)00608-6
    • Iwamoto, K. and Kato, T. (2003) RNA editing of serotonin 2C receptor in human postmortem brains of major mental disorders. Neurosci. Lett., 346, 169-172. (Pubitemid 36829288)
    • (2003) Neuroscience Letters , vol.346 , Issue.3 , pp. 169-172
    • Iwamoto, K.1    Kato, T.2
  • 5
    • 1542378930 scopus 로고    scopus 로고
    • Glutamate receptors: RNA editing and death of motor neurons
    • Kawahara, Y., Ito, K., Sun, H., Aizawa, H., Kanazawa, I. and Kwak, S. (2004) Glutamate receptors: RNA editing and death of motor neurons. Nature, 427, 801.
    • (2004) Nature , vol.427 , pp. 801
    • Kawahara, Y.1    Ito, K.2    Sun, H.3    Aizawa, H.4    Kanazawa, I.5    Kwak, S.6
  • 6
    • 15044346521 scopus 로고    scopus 로고
    • Deficient RNA editing of GluR2 and neuronal death in amyotropic lateral sclerosis
    • DOI 10.1007/s00109-004-0599-z
    • Kwak, S. and Kawahara, Y. (2005) Deficient RNA editing of GluR2 and neuronal death in amyotropic lateral sclerosis. J. Mol. Med., 83, 110-120. (Pubitemid 40379299)
    • (2005) Journal of Molecular Medicine , vol.83 , Issue.2 , pp. 110-120
    • Kwak, S.1    Kawahara, Y.2
  • 10
    • 30844442607 scopus 로고    scopus 로고
    • The snoRNA HBII-52 regulates alternative splicing of the serotonin receptor 2C
    • DOI 10.1126/science.1118265
    • Kishore, S. and Stamm, S. (2006) The snoRNA HBII-52 regulates alternative splicing of the serotonin receptor 2C. Science, 311, 230-232. (Pubitemid 43108188)
    • (2006) Science , vol.311 , Issue.5758 , pp. 230-232
    • Kishore, S.1    Stamm, S.2
  • 11
    • 22344445939 scopus 로고    scopus 로고
    • ADAR2-mediated editing of RNA substrates in the nucleolus is inhibited by C/D small nucleolar RNAs
    • DOI 10.1083/jcb.200411129
    • Vitali, P., Basyuk, E., Le Meur, E., Bertrand, E., Muscatelli, F., Cavaillé , J. and Huttenhofer, A. (2005) ADAR2-mediated editing of RNA substrates in the nucleolus is inhibited by C/D small nucleolar RNAs. J. Cell Biol., 169, 745-753. (Pubitemid 41002880)
    • (2005) Journal of Cell Biology , vol.169 , Issue.5 , pp. 745-753
    • Vitali, P.1    Basyuk, E.2    Le Meur, E.3    Bertrand, E.4    Muscatelli, F.5    Cavaille, J.6    Huttenhofer, A.7
  • 14
    • 84855403375 scopus 로고    scopus 로고
    • Deregulation of the A-to-I RNA editing mechanism in psychiatric disorders
    • Silberberg, G., Lundin, D., Navon, R. and Ohman, M. (2012) Deregulation of the A-to-I RNA editing mechanism in psychiatric disorders. Hum. Mol. Genet., 21, 311-321.
    • (2012) Hum. Mol. Genet. , vol.21 , pp. 311-321
    • Silberberg, G.1    Lundin, D.2    Navon, R.3    Ohman, M.4
  • 15
    • 0042888576 scopus 로고    scopus 로고
    • Mutations of the RNA-specific adenosine deaminase gene (DSRAD) are involved in dyschromatosis symmetrica hereditaria
    • DOI 10.1086/378209
    • Miyamura, Y., Suzuki, T., Kono, M., Inagaki, K., Ito, S., Suzuki, N. and Tomita, Y. (2003) Mutations of the RNA-specific adenosine deaminase gene (DSRAD) are involved in dyschromatosis symmetrica hereditaria. Am. J. Hum. Genet., 73, 693-699. (Pubitemid 37076285)
    • (2003) American Journal of Human Genetics , vol.73 , Issue.3 , pp. 693-699
    • Miyamura, Y.1    Suzuki, T.2    Kono, M.3    Inagaki, K.4    Ito, S.5    Suzuki, N.6    Tomita, Y.7
  • 16
    • 42749093007 scopus 로고    scopus 로고
    • Down-regulation of RNA editing in pediatric astrocytomas: ADAR2 editing activity inhibits cell migration and proliferation
    • Cenci, C., Barzotti, R., Galeano, F., Corbelli, S., Rota, R., Massimi, L., Di Rocco, C., O'Connell, M.A. and Gallo, A. (2008) Down-regulation of RNA editing in pediatric astrocytomas: ADAR2 editing activity inhibits cell migration and proliferation. J. Biol. Chem., 283, 7251-7260.
    • (2008) J. Biol. Chem. , vol.283 , pp. 7251-7260
    • Cenci, C.1    Barzotti, R.2    Galeano, F.3    Corbelli, S.4    Rota, R.5    Massimi, L.6    Di Rocco, C.7    O'Connell, M.A.8    Gallo, A.9
  • 21
    • 0037171846 scopus 로고    scopus 로고
    • Altered editing of serotonin 2C receptor pre-mRNA in the prefrontal cortex of depressed suicide victims
    • DOI 10.1016/S0896-6273(02)00660-8
    • Gurevich, I., Tamir, H., Arango, V., Dwork, A.J., Mann, J.J. and Schmauss, C. (2002) Altered editing of serotonin 2C receptor pre-mRNA in the prefrontal cortex of depressed suicide victims. Neuron., 34, 349-356. (Pubitemid 34465494)
    • (2002) Neuron , vol.34 , Issue.3 , pp. 349-356
    • Gurevich, I.1    Tamir, H.2    Arango, V.3    Dwork, A.J.4    Mann, J.J.5    Schmauss, C.6
  • 23
    • 0036966283 scopus 로고    scopus 로고
    • New and old roles of the doublestranded RNA-binding domain
    • Doyle, M. and Jantsch, M.F. (2003) New and old roles of the doublestranded RNA-binding domain. J. Struct. Biol., 140, 147-153.
    • (2003) J. Struct. Biol. , vol.140 , pp. 147-153
    • Doyle, M.1    Jantsch, M.F.2
  • 24
    • 0034711082 scopus 로고    scopus 로고
    • Double-stranded RNA adenosine deaminases ADAR1 and ADAR2 have overlapping specificities
    • Lehmann, K.A. and Bass, B.L. (2000) Double-stranded RNA adenosine deaminases ADAR1 and ADAR2 have overlapping specificities. Biochemistry, 39, 12875-12884.
    • (2000) Biochemistry , vol.39 , pp. 12875-12884
    • Lehmann, K.A.1    Bass, B.L.2
  • 25
    • 0029164692 scopus 로고
    • Expression and regulation by interferon of a double-stranded-RNA-specific adenosine deaminase from human cells: Evidence for two forms of the deaminase
    • Patterson, J.B. and Samuel, C.E. (1995) Expression and regulation by interferon of a double-stranded-RNA-specific adenosine deaminase from human cells: evidence for two forms of the deaminase. Mol. Cell. Biol., 15, 5376-5388.
    • (1995) Mol. Cell. Biol. , vol.15 , pp. 5376-5388
    • Patterson, J.B.1    Samuel, C.E.2
  • 26
    • 0034779253 scopus 로고    scopus 로고
    • CRM1 mediates the export of ADAR1 through a nuclear export signal within the Z-DNA binding domain
    • DOI 10.1128/MCB.21.22.7862-7871.2001
    • Poulsen, H., Nilsson, J., Damgaard, C.K., Egebjerg, J. and Kjems, J. (2001) CRM1 mediates the export of ADAR1 through a nuclear export signal within the Z-DNA binding domain. Mol. Cell. Biol., 21, 7862-7871. (Pubitemid 32988794)
    • (2001) Molecular and Cellular Biology , vol.21 , Issue.22 , pp. 7862-7871
    • Poulsen, H.1    Nilsson, J.2    Damgaard, C.K.3    Egebjerg, J.4    Kjems, J.5
  • 29
    • 0035150231 scopus 로고    scopus 로고
    • The human but not the Xenopus RNA-editing enzyme ADAR1 has an atypical nuclear localization signal and displays the characteristics of a shuttling protein
    • Eckmann, C.R., Neunteufl, A., Pfaffstetter, L. and Jantsch, M.F. (2001) The human but not the Xenopus RNA-editing enzyme ADAR1 has an atypical nuclear localization signal and displays the characteristics of a shuttling protein. Mol. Biol. Cell, 12, 1911-1924. (Pubitemid 33049688)
    • (2001) Molecular Biology of the Cell , vol.12 , Issue.7 , pp. 1911-1924
    • Eckmann, C.R.1    Neunteufl, A.2    Pfaffstetter, L.3    Jantsch, M.F.4
  • 30
    • 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
    • DOI 10.1091/mbc.E02-03-0161
    • Strehblow, A., Hallegger, M. and Jantsch, M.F. (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, 3822-3835. (Pubitemid 35398551)
    • (2002) Molecular Biology of the Cell , vol.13 , Issue.11 , pp. 3822-3835
    • Strehblow, A.1    Hallegger, M.2    Jantsch, M.F.3
  • 31
    • 0033580386 scopus 로고    scopus 로고
    • Characterization of the 5'-flanking region of the human RNA-specific adenosine deaminase ADAR1 gene and identification of an interferon-inducible ADAR1 promoter
    • DOI 10.1016/S0378-1119(99)00017-7, PII S0378111999000177
    • George, C.X. and Samuel, C.E. (1999) Characterization of the 5'-flanking region of the human RNA-specific adenosine deaminase ADAR1 gene and identification of an interferon-inducible ADAR1 promoter. Gene, 229, 203-213. (Pubitemid 29148324)
    • (1999) Gene , vol.229 , Issue.1-2 , pp. 203-213
    • George, C.X.1    Samuel, C.E.2
  • 32
    • 0033551050 scopus 로고    scopus 로고
    • Human RNA-specific adenosine deaminase ADAR1 transcripts possess alternative exon 1 structures that initiate from different promoters, one constitutively active and the other interferon inducible
    • DOI 10.1073/pnas.96.8.4621
    • George, C.X. and Samuel, C.E. (1999) Human RNA-specific adenosine deaminase ADAR1 transcripts possess alternative exon 1 structures that initiate from different promoters, one constitutively active and the other interferon inducible. Proc. Natl Acad. Sci. USA, 96, 4621-4626. (Pubitemid 29190386)
    • (1999) Proceedings of the National Academy of Sciences of the United States of America , vol.96 , Issue.8 , pp. 4621-4626
    • George, C.X.1    Samuel, C.E.2
  • 33
    • 0034722628 scopus 로고    scopus 로고
    • Human RNA-specific adenosine deaminase (ADAR1) gene specifies transcripts that initiate from a constitutively active alternative promoter
    • Kawakubo, K. and Samuel, C.E. (2000) Human RNA-specific adenosine deaminase (ADAR1) gene specifies transcripts that initiate from a constitutively active alternative promoter. Gene, 258, 165-172.
    • (2000) Gene , vol.258 , pp. 165-172
    • Kawakubo, K.1    Samuel, C.E.2
  • 36
    • 1042278125 scopus 로고    scopus 로고
    • Liver disintegration in the mouse embryo caused by deficiency in the RNA-editing Enzyme ADAR1
    • DOI 10.1074/jbc.M311347200
    • Hartner, J.C., Schmittwolf, C., Kispert, A., Müller, A.M., Higuchi, M. and Seeburg, P.H. (2004) Liver disintegration in the mouse embryo caused by deficiency in the RNA-editing enzyme ADAR1. J. Biol. Chem., 279, 4894-4902. (Pubitemid 38199085)
    • (2004) Journal of Biological Chemistry , vol.279 , Issue.6 , pp. 4894-4902
    • Hartner, J.C.1    Schmittwolf, C.2    Kispert, A.3    Muller, A.M.4    Higuchi, M.5    Seeburg, P.H.6
  • 37
    • 57849136005 scopus 로고    scopus 로고
    • ADAR1 is essential for the maintenance of hematopoiesis and suppression of interferon signaling
    • Hartner, J.C., Walkley, C.R., Lu, J. and Orkin, S.H. (2009) ADAR1 is essential for the maintenance of hematopoiesis and suppression of interferon signaling. Nat. Immunol., 10, 109-115.
    • (2009) Nat. Immunol. , vol.10 , pp. 109-115
    • Hartner, J.C.1    Walkley, C.R.2    Lu, J.3    Orkin, S.H.4
  • 40
    • 0034612640 scopus 로고    scopus 로고
    • Point mutation in an AMPA receptor gene rescues lethality in mice deficient in the RNA-editing enzyme ADAR2
    • DOI 10.1038/35017558
    • Higuchi, M., Maas, S., Single, F.N., Hartner, J., Rozov, A., Burnashev, N., Feldmeyer, D., Sprengel, R. and Seeburg, P.H. (2000) Point mutation in an AMPA receptor gene rescues lethality in mice deficient in the RNA-editing enzyme ADAR2. Nature, 406, 78-81. (Pubitemid 30460214)
    • (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
  • 41
    • 77955549933 scopus 로고    scopus 로고
    • Mutational spectrum of the ADAR1 gene in dyschromatosis symmetrica hereditaria
    • Li, M., Yang, L., Li, C., Jin, C., Lai, M., Zhang, G., Hu, Y., Ji, J. and Yao, Z. (2010) Mutational spectrum of the ADAR1 gene in dyschromatosis symmetrica hereditaria. Arch. Dermatol. Res., 302, 469-476.
    • (2010) Arch. Dermatol. Res. , vol.302 , pp. 469-476
    • Li, M.1    Yang, L.2    Li, C.3    Jin, C.4    Lai, M.5    Zhang, G.6    Hu, Y.7    Ji, J.8    Yao, Z.9
  • 42
    • 81855172263 scopus 로고    scopus 로고
    • ADARs: Viruses and innate immunity
    • Samuel, C.E. (2012) ADARs: viruses and innate immunity. Curr. Top. Microbiol. Immunol., 353, 163-195.
    • (2012) Curr. Top. Microbiol. Immunol. , vol.353 , pp. 163-195
    • Samuel, C.E.1
  • 43
    • 24644519954 scopus 로고    scopus 로고
    • Structural biology: Inositol hexakisphosphate is bound in the ADAR2 core and required for RNA editing
    • DOI 10.1126/science.1113150
    • Macbeth, M.R., Schubert, H.L., Vandemark, A.P., Lingam, A.T., Hill, C.P. and Bass, B.L. (2005) Inositol hexakisphosphate is bound in the ADAR2 core and required for RNA editing. Science, 309, 1534-1539. (Pubitemid 41266474)
    • (2005) Science , vol.309 , Issue.5740 , pp. 1534-1539
    • Macbeth, M.R.1    Schubert, H.L.2    VanDemark, A.F.3    Lingam, A.T.4    Hill, C.P.5    Bass, B.L.6
  • 44
    • 0033565664 scopus 로고    scopus 로고
    • Synthetic substrate analogs for the RNA-editing adenosine deaminase ADAR-2
    • DOI 10.1093/nar/27.14.2912
    • Yi-Brunozzi, H.Y., Easterwood, L.M., Kamilar, G.M. and Beal, P.A. (1999) Synthetic substrate analogs for the RNA-editing adenosine deaminase ADAR-2. Nucleic Acids Res., 27, 2912-2917. (Pubitemid 29335712)
    • (1999) Nucleic Acids Research , vol.27 , Issue.14 , pp. 2912-2917
    • Yi-Brunozzi, H.Y.1    Easterwood, L.M.2    Kamilar, G.M.3    Beal, P.A.4
  • 45
    • 0034703723 scopus 로고    scopus 로고
    • Demethylation of 6-O-methylinosine by an RNA-editing adenosine deaminase
    • Easterwood, L.M., Véliz, E.A. and Beal, P.A. (2000) Demethylation of 6-O-methylinosine by an RNA-editing adenosine deaminase. J. Am. Chem. Soc., 122, 11537-11538.
    • (2000) J. Am. Chem. Soc. , vol.122 , pp. 11537-11538
    • Easterwood, L.M.1    Véliz, E.A.2    Beal, P.A.3
  • 46
    • 0034633941 scopus 로고    scopus 로고
    • Analysis of the RNA-editing reaction of ADAR2 with structural and fluorescent analogues of the GluR-B R/G editing site
    • Stephens, O.M., Yi-Brunozzi, H.Y. and Beal, P.A. (2000) Analysis of the RNA-editing reaction of ADAR2 with structural and fluorescent analogues of the GluR-B R/G editing site. Biochemistry, 39, 12243-12251.
    • (2000) Biochemistry , vol.39 , pp. 12243-12251
    • Stephens, O.M.1    Yi-Brunozzi, H.Y.2    Beal, P.A.3
  • 47
    • 0035851115 scopus 로고    scopus 로고
    • Conformational changes that occur during an RNA-editing adenosine deamination reaction
    • Yi-Brunozzi, H.Y., Stephens, O.M. and Beal, P.A. (2001) Conformational changes that occur during an RNA-editing adenosine deamination reaction. J. Biol. Chem., 276, 37827-37833.
    • (2001) J. Biol. Chem. , vol.276 , pp. 37827-37833
    • Yi-Brunozzi, H.Y.1    Stephens, O.M.2    Beal, P.A.3
  • 48
    • 0042734808 scopus 로고    scopus 로고
    • Substrate analogues for an RNA-editing adenosine deaminase: Mechanistic investigation and inhibitor design
    • DOI 10.1021/ja029742d
    • Vé liz, E.A., Easterwood, L.M. and Beal, P.A. (2003) Substrate analogues for an RNA-editing adenosine deaminase: mechanistic investigation and inhibitor design. J. Am. Chem. Soc., 125, 10867-10876. (Pubitemid 37087544)
    • (2003) Journal of the American Chemical Society , vol.125 , Issue.36 , pp. 10867-10876
    • Veliz, E.A.1    Easterwood, L.M.2    Beal, P.A.3
  • 50
    • 33748627443 scopus 로고    scopus 로고
    • C6-substituted analogues of 8-azanebularine: Probes of an RNA-editing enzyme active site
    • DOI 10.1021/ol061354j
    • Maydanovych, O. and Beal, P.A. (2006) C6-substituted analogues of 8-azanebularine: probes of an RNA-editing enzyme active site. Org. Lett., 8, 3753-3756. (Pubitemid 44378355)
    • (2006) Organic Letters , vol.8 , Issue.17 , pp. 3753-3756
    • Maydanovych, O.1    Beal, P.A.2
  • 51
    • 61649112213 scopus 로고    scopus 로고
    • Synthesis and evaluation of an RNA editing substrate bearing 2'-deoxy-2'-mercaptoadenosine
    • Jayalath, P., Pokharel, S., Vé liz, E. and Beal, P.A. (2009) Synthesis and evaluation of an RNA editing substrate bearing 2'-deoxy-2'-mercaptoadenosine. Nucleos. Nucleot. Nucl., 28, 78-88.
    • (2009) Nucleos. Nucleot. Nucl. , vol.28 , pp. 78-88
    • Jayalath, P.1    Pokharel, S.2    Vé Liz, E.3    Beal, P.A.4
  • 54
    • 78650542645 scopus 로고    scopus 로고
    • RNA editing changes the lesion specificity for the DNA repair enzyme NEIL1
    • Yeo, J., Goodman, R.A., Schirle, N.T., David, S.S. and Beal, P.A. (2010) RNA editing changes the lesion specificity for the DNA repair enzyme NEIL1. Proc. Natl Acad. Sci. USA, 107, 20715-20719.
    • (2010) Proc. Natl Acad. Sci. USA , vol.107 , pp. 20715-20719
    • Yeo, J.1    Goodman, R.A.2    Schirle, N.T.3    David, S.S.4    Beal, P.A.5
  • 56
    • 63849246525 scopus 로고    scopus 로고
    • Protein structure prediction on the Web: A case study using the Phyre server
    • Kelley, L.A. and Sternberg, M.J.E. (2009) Protein structure prediction on the Web: a case study using the Phyre server. Nat. Protocols, 4, 363-371.
    • (2009) Nat. Protocols , vol.4 , pp. 363-371
    • Kelley, L.A.1    Sternberg, M.J.E.2
  • 58
    • 4644339417 scopus 로고    scopus 로고
    • Evidence for auto-inhibition by the N terminus of hADAR2 and activation by dsRNA binding
    • DOI 10.1261/rna.7920904
    • Macbeth, M.R., Lingam, A.T. and Bass, B.L. (2004) Evidence for auto-inhibition by the N terminus of hADAR2 and activation by dsRNA binding. RNA, 10, 1563-1571. (Pubitemid 39288191)
    • (2004) RNA , vol.10 , Issue.10 , pp. 1563-1571
    • Macbeth, M.R.1    Lingam, A.T.2    Bass, B.L.3
  • 59
    • 79956271523 scopus 로고    scopus 로고
    • Predicting sites of ADAR editing in double-stranded RNA
    • Eggington, J.M., Greene, T. and Bass, B.L. (2011) Predicting sites of ADAR editing in double-stranded RNA. Nat. Commun., 2, 319.
    • (2011) Nat. Commun. , vol.2 , pp. 319
    • Eggington, J.M.1    Greene, T.2    Bass, B.L.3
  • 60
    • 77957919940 scopus 로고    scopus 로고
    • Selective inhibition of ADAR2-catalyzed editing of the serotonin 2c receptor pre-mRNA by a helix-threading peptide
    • Schirle, N.T., Goodman, R.A., Krishnamurthy, M. and Beal, P.A. (2010) Selective inhibition of ADAR2-catalyzed editing of the serotonin 2c receptor pre-mRNA by a helix-threading peptide. Org. Biomol. Chem., 8, 4898-4904.
    • (2010) Org. Biomol. Chem. , vol.8 , pp. 4898-4904
    • Schirle, N.T.1    Goodman, R.A.2    Krishnamurthy, M.3    Beal, P.A.4
  • 61
    • 33749254843 scopus 로고    scopus 로고
    • An accurate fluorescent assay for quantifying the extent of RNA editing
    • DOI 10.1261/rna.166906
    • Roberson, L.M. and Rosenthal, J.J.C. (2006) An accurate fluorescent assay for quantifying the extent of RNA editing. RNA, 12, 1907-1912. (Pubitemid 44484263)
    • (2006) RNA , vol.12 , Issue.10 , pp. 1907-1912
    • Roberson, L.M.1    Rosenthal, J.J.C.2
  • 63
    • 0026620322 scopus 로고
    • Kinetics of intermolecular cleavage by hammerhead ribozymes
    • DOI 10.1021/bi00163a012
    • Fedor, M.J. and Uhlenbeck, O.C. (1992) Kinetics of intermolecular cleavage by hammerhead ribozymes. Biochemistry, 31, 12042-12054. (Pubitemid 23011347)
    • (1992) Biochemistry , vol.31 , Issue.48 , pp. 12042-12054
    • Fedor, M.J.1    Uhlenbeck, O.C.2
  • 64
    • 0026680843 scopus 로고
    • Site-specific modification of pre-mRNA: The 2'-hydroxyl groups at the splice sites
    • Moore, M.J. and Sharp, P.A. (1992) Site-specific modification of pre-mRNA: the 2'-hydroxyl groups at the splice sites. Science, 256, 992-997.
    • (1992) Science , vol.256 , pp. 992-997
    • Moore, M.J.1    Sharp, P.A.2
  • 65
    • 0032522283 scopus 로고    scopus 로고
    • Calculation of relative hydration free energy differences for heteroaromatic compounds: Use in the design of adenosine deaminase and cytidine deaminase inhibitors
    • DOI 10.1021/ja972906j
    • Erion, M.D. and Reddy, M.R. (1998) Calculation of relative hydration free energy differences for heteroaromatic compounds: use in the design of adenosine deaminase and cytidine deaminase inhibitors. J. Am. Chem. Soc., 120, 3295-3304. (Pubitemid 28289065)
    • (1998) Journal of the American Chemical Society , vol.120 , Issue.14 , pp. 3295-3304
    • Erion, M.D.1    Reddy, M.R.2
  • 66
    • 0001478794 scopus 로고
    • Covalent hydration in nitrogen heterocycles
    • Albert, A. (1976) Covalent Hydration in Nitrogen Heterocycles. Adv. Heterocycl. Chem., 20, 117-143.
    • (1976) Adv. Heterocycl. Chem. , vol.20 , pp. 117-143
    • Albert, A.1
  • 67
    • 0028263121 scopus 로고
    • Evidence that total substitution of adenine with 7-deazaadenine in the HDV antigenomic ribozyme changes the kinetics of RNA folding
    • DOI 10.1016/S0960-894X(01)80668-5
    • Wieczorek, A., Dinter-Gottlieb, G. and Gottlieb, P.A. (1994) Evidence that total substitution of adenine with 7-deazaadenine in the HDV antigenomic ribozyme changes the kinetics of RNA folding. Bioorg. Med. Chem. Lett., 4, 987-994. (Pubitemid 24121105)
    • (1994) Bioorganic and Medicinal Chemistry Letters , vol.4 , Issue.8 , pp. 987-994
    • Wieczorek, A.1    Dinter-Gottlieb, G.2    Gottlieb, P.A.3
  • 69
    • 0026434561 scopus 로고
    • Atomic structure of adenosine deaminase complexed with a transition-state analog: Understanding catalysis and immunodeficiency mutations
    • Wilson, D.K., Rudolph, F.B. and Quiocho, F.A. (1991) Atomic structure of adenosine deaminase complexed with a transition-state analog: understanding catalysis and immunodeficiency mutations. Science, 252, 1278-1284. (Pubitemid 21917036)
    • (1991) Science , vol.252 , Issue.5010 , pp. 1278-1284
    • Wilson, D.K.1    Rudolph, F.B.2    Quiocho, F.A.3
  • 70
    • 0013878432 scopus 로고
    • Specificity of adenosine deaminase toward adenosine and 2'-deoxyadenosine analogues
    • Frederiksen, S. (1966) Specificity of adenosine deaminase toward adenosine and 2'-deoxyadenosine analogues. Arch. Biochem. Biophys., 113, 383-388.
    • (1966) Arch. Biochem. Biophys. , vol.113 , pp. 383-388
    • Frederiksen, S.1
  • 71
    • 34548339631 scopus 로고    scopus 로고
    • Pyrazolo[3,4-d]pyrimidine ribonucleosides related to 2-aminoadenosine and isoguanosine: Synthesis, deamination and tautomerism
    • DOI 10.1039/b708736e
    • Seela, F. and Xu, K. (2007) Pyrazolo[3, 4-d]pyrimidine ribonucleosides related to 2-aminoadenosine and isoguanosine: synthesis, deamination and tautomerism. Org. Biomol. Chem., 5, 3034-3045. (Pubitemid 47340694)
    • (2007) Organic and Biomolecular Chemistry , vol.5 , Issue.18 , pp. 3034-3045
    • Seela, F.1    Xu, K.2
  • 73
    • 32244445417 scopus 로고    scopus 로고
    • Crystal structure of Staphylococcus aureus tRNA adenosine deaminase TadA in complex with RNA
    • DOI 10.1038/nsmb1047, PII NSMB1047
    • Losey, H.C., Ruthenburg, A.J. and Verdine, G.L. (2006) Crystal structure of Staphylococcus aureus tRNA adenosine deaminase TadA in complex with RNA. Nat. Struct. Mol. Biol., 13, 153-159. (Pubitemid 43214719)
    • (2006) Nature Structural and Molecular Biology , vol.13 , Issue.2 , pp. 153-159
    • Losey, H.C.1    Ruthenburg, A.J.2    Verdine, G.L.3
  • 74
    • 0029905437 scopus 로고    scopus 로고
    • Probing the functional role of two conserved active site aspartates in mouse adenosine deaminase
    • DOI 10.1021/bi952920d
    • Sideraki, V., Mohamedali, K.A., Wilson, D.K., Chang, Z., Kellems, R.E., Quiocho, F.A. and Rudolph, F.B. (1996) Probing the functional role of two conserved active site aspartates in mouse adenosine deaminase. Biochemistry, 35, 7862-7872. (Pubitemid 26202525)
    • (1996) Biochemistry , vol.35 , Issue.24 , pp. 7862-7872
    • Sideraki, V.1    Mohamedali, K.A.2    Wilson, D.K.3    Chang, Z.4    Kellems, R.E.5    Quiocho, F.A.6    Rudolph, F.B.7
  • 75
    • 0015217258 scopus 로고
    • Substrate specificity and aspects of deamination catalyzed by rabbit muscle 50-adenylic acid aminohydrolase
    • Zielke, C.L. and Suelter, C.H. (1971) Substrate specificity and aspects of deamination catalyzed by rabbit muscle 50-adenylic acid aminohydrolase. J. Biol. Chem., 246, 1313-1317.
    • (1971) J. Biol. Chem. , vol.246 , pp. 1313-1317
    • Zielke, C.L.1    Suelter, C.H.2
  • 77
    • 0027398949 scopus 로고
    • A pre-transition-state mimic of an enzyme: X-ray structure of adenosine deaminase with bound 1-deazaadenosine and zinc-activated water
    • Wilson, D.K. and Quiocho, F.A. (1993) A pre-transition-state mimic of an enzyme: X-ray structure of adenosine deaminase with bound 1-deazaadenosine and zinc-activated water. Biochemistry, 32, 1689-1694. (Pubitemid 23066441)
    • (1993) Biochemistry , vol.32 , Issue.7 , pp. 1689-1694
    • Wilson, D.K.1    Quiocho, F.A.2
  • 78
    • 39749128713 scopus 로고    scopus 로고
    • Transition state structure of E. coli tRNA-specific adenosine deaminase
    • DOI 10.1021/ja078008x
    • Luo, M. and Schramm, V.L. (2008) Transition state structure of E. coli tRNA-specific adenosine deaminase. J. Am. Chem. Soc., 130, 2649-2655. (Pubitemid 351304780)
    • (2008) Journal of the American Chemical Society , vol.130 , Issue.8 , pp. 2649-2655
    • Luo, M.1    Schramm, V.L.2
  • 79
    • 0025242063 scopus 로고
    • Arginine 127 stabilizes the transition state in carboxypeptidase
    • Phillips, M.A., Fletterick, R. and Rutter, W.J. (1990) Arginine 127 stabilizes the transition state in carboxypeptidase. J. Biol. Chem., 265, 20692-20698. (Pubitemid 120014063)
    • (1990) Journal of Biological Chemistry , vol.265 , Issue.33 , pp. 20692-20698
    • Phillips, M.A.1    Fletterick, R.2    Rutter, W.J.3
  • 80
    • 0027049221 scopus 로고
    • Guanidine derivatives restore activity to carboxypeptidase lacking arginine-127
    • Phillips, M.A., Hedstrom, L. and Rutter, W.J. (1992) Guanidine derivatives restore activity to carboxypeptidase lacking arginine-127. Protein Sci., 1, 517-521. (Pubitemid 23016872)
    • (1992) Protein Science , vol.1 , Issue.4 , pp. 517-521
    • Phillips, M.A.1    Hedstrom, L.2    Rutter, W.J.3
  • 81
    • 72749127274 scopus 로고    scopus 로고
    • Arginine 15 stabilizes an S(N)Ar reaction transition state and the binding of anionic ligands at the active site of human glutathione transferase A1-1
    • Gildenhuys, S., Dobreva, M., Kinsley, N., Sayed, Y., Burke, J., Pelly, S., Gordon, G.P., Sayed, M., Sewell, T. and Dirr, H.W. (2010) Arginine 15 stabilizes an S(N)Ar reaction transition state and the binding of anionic ligands at the active site of human glutathione transferase A1-1. Biophys. Chem., 146, 118-125.
    • (2010) Biophys. Chem. , vol.146 , pp. 118-125
    • Gildenhuys, S.1    Dobreva, M.2    Kinsley, N.3    Sayed, Y.4    Burke, J.5    Pelly, S.6    Gordon, G.P.7    Sayed, M.8    Sewell, T.9    Dirr, H.W.10
  • 82
    • 84855209589 scopus 로고
    • Biological and biochemical properties of the analogue antibiotic tubercidin
    • Acs, G., Reich, E. and Mori, M. (1964) Biological and Biochemical Properties of the Analogue Antibiotic Tubercidin. Proc. Natl Acad. Sci. USA, 52, 493-501.
    • (1964) Proc. Natl Acad. Sci. USA , vol.52 , pp. 493-501
    • Acs, G.1    Reich, E.2    Mori, M.3


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