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Volumn 9, Issue 2-3, 2012, Pages

The potential of 2-oxoglutarate oxygenases acting on nucleic acids as therapeutic targets

Author keywords

[No Author keywords available]

Indexed keywords

2 OXOGLUTARIC ACID; 5 METHYLCYTOSINE; CISPLATIN; ERYTHROPOIETIN; FTO PROTEIN; HISTONE DEMETHYLASE; HYPOXIA INDUCIBLE FACTOR; MELDONIUM; MEMBRANE PROTEIN; NUCLEIC ACID BASE; NUCLEIC ACID MODIFYING 2 OXOGLUTARIC ACID OXYGENASE; PHOTOFRIN; TET PROTEIN; TRANSFER RNA; UNCLASSIFIED DRUG; VASCULOTROPIN;

EID: 84871464403     PISSN: None     EISSN: 17406773     Source Type: Journal    
DOI: 10.1016/j.ddstr.2012.02.002     Document Type: Review
Times cited : (14)

References (62)
  • 1
    • 78650864017 scopus 로고    scopus 로고
    • Physiological and biochemical aspects of hydroxylations and demethylations catalyzed by human 2-oxoglutarate oxygenases
    • Loenarz, C. et al. (2011) Physiological and biochemical aspects of hydroxylations and demethylations catalyzed by human 2-oxoglutarate oxygenases. Trends Biochem. Sci. 36, 7-18
    • (2011) Trends Biochem. Sci. , vol.36 , pp. 7-18
    • Loenarz, C.1
  • 2
    • 79956220088 scopus 로고    scopus 로고
    • Inhibition of2-oxoglutaratedependent oxygenases
    • Rose, N.R. et al. (2011) Inhibition of2-oxoglutaratedependent oxygenases. Chem. Soc. Rev. 40, 4364-4397
    • (2011) Chem. Soc. Rev. , vol.40 , pp. 4364-4397
    • Rose, N.R.1
  • 3
    • 0347418197 scopus 로고    scopus 로고
    • Collagens, modifying enzymes and their mutations in humans, flies and worms
    • DOI 10.1016/j.tig.2003.11.004
    • Myllyharju, J. et al. (2004) Collagens, modifying enzymes and their mutations in humans, flies and worms. Trends Genet. 20, 33-43 (Pubitemid 38032818)
    • (2004) Trends in Genetics , vol.20 , Issue.1 , pp. 33-43
    • Myllyharju, J.1    Kivirikko, K.I.2
  • 4
    • 77955790529 scopus 로고    scopus 로고
    • Prolyl hydroxylase domain-containing protein inhibitors as stabilizers of hypoxia-inducible factor: Small molecule-based therapeutics for anemia
    • Yan, L. et al. (2010) Prolyl hydroxylase domain-containing protein inhibitors as stabilizers of hypoxia-inducible factor: small molecule-based therapeutics for anemia. Expert Opin. Ther. Pat. 20, 1219-1245
    • (2010) Expert Opin. Ther. Pat. , vol.20 , pp. 1219-1245
    • Yan, L.1
  • 5
    • 78650425625 scopus 로고    scopus 로고
    • Structural and mechanistic studies on g-butyrobetaine hydroxylase
    • Leung, I.K.H. et al. (2010) Structural and mechanistic studies on g-butyrobetaine hydroxylase. Chem. Biol. 17, 1316-1324
    • (2010) Chem. Biol. , vol.17 , pp. 1316-1324
    • Leung, I.K.H.1
  • 6
    • 77955414934 scopus 로고    scopus 로고
    • Crystal structure of human gamma-butyrobetaine hydroxylase
    • Tars, K. et al. (2010) Crystal structure of human gamma-butyrobetaine hydroxylase. Biochem. Biophys. Res. Commun. 398, 634-639
    • (2010) Biochem. Biophys. Res. Commun. , vol.398 , pp. 634-639
    • Tars, K.1
  • 7
    • 59449087016 scopus 로고    scopus 로고
    • Histone modifying enzymes: Structures, mechanisms, and specificities
    • Marmorstein, R. et al. (2009) Histone modifying enzymes: structures, mechanisms, and specificities. Biochim. Biophys. Acta (BBA): Gene Regul. Mech. 1789, 58-68
    • (2009) Biochim. Biophys. Acta (BBA): Gene Regul. Mech. , vol.1789 , pp. 58-68
    • Marmorstein, R.1
  • 8
    • 70349780606 scopus 로고    scopus 로고
    • The emerging therapeutic potential of histone methyltransferase and demethylase inhibitors
    • Spannhoff, A. et al. (2009) The emerging therapeutic potential of histone methyltransferase and demethylase inhibitors. ChemMedChem 4, 1568-1582
    • (2009) ChemMedChem , vol.4 , pp. 1568-1582
    • Spannhoff, A.1
  • 9
    • 70350315800 scopus 로고    scopus 로고
    • Inhibition of the histone lysine demethylase JMJD2A by ejection of structural Zn(II)
    • Sekirnik, R. et al. (2009) Inhibition of the histone lysine demethylase JMJD2A by ejection of structural Zn(II). Chem. Commun. 42, 6376-6378
    • (2009) Chem. Commun. , vol.42 , pp. 6376-6378
    • Sekirnik, R.1
  • 10
    • 0037068433 scopus 로고    scopus 로고
    • AlkB-mediated oxidative demethylation reverses DNA damage in Escherichia coli
    • DOI 10.1038/nature01048
    • Falnes, P.O. et al. (2002) AlkB-mediated oxidative demethylation reverses DNA damage in Escherichia coli. Nature 419, 178-182 (Pubitemid 35025447)
    • (2002) Nature , vol.419 , Issue.6903 , pp. 178-182
    • Falnes, P.O.1    Johansen, R.F.2    Seeberg, E.3
  • 11
    • 0035221419 scopus 로고    scopus 로고
    • The DNA-repair protein AlkB, EGL-9, and leprecan define new families of 2-oxoglutarate-and iron-dependent dioxygenases
    • Aravind, L. et al. (2001) The DNA-repair protein AlkB, EGL-9, and leprecan define new families of 2-oxoglutarate-and iron-dependent dioxygenases. Genome Biol. 2 RESEARCH0007
    • (2001) Genome Biol. , vol.2
    • Aravind, L.1
  • 12
    • 42549128712 scopus 로고    scopus 로고
    • Crystal structures of DNA/RNA repair enzymes AlkB and ABH2 bound to dsDNA
    • Yang, C.G. et al. (2008) Crystal structures of DNA/RNA repair enzymes AlkB and ABH2 bound to dsDNA. Nature 452, 961-965
    • (2008) Nature , vol.452 , pp. 961-965
    • Yang, C.G.1
  • 13
    • 84858068453 scopus 로고    scopus 로고
    • Dynamic combinatorial mass spectrometry leads to inhibitors of a 2-oxoglutarate dependent nucleic acid demethylase
    • Woon, E.C.Y. et al. (2012) Dynamic combinatorial mass spectrometry leads to inhibitors of a 2-oxoglutarate dependent nucleic acid demethylase. J. Med. Chem. 55, 2173-2184
    • (2012) J. Med. Chem. , vol.55 , pp. 2173-2184
    • Woon, E.C.Y.1
  • 19
    • 81355146483 scopus 로고    scopus 로고
    • 6-Methyladenosinein nuclear RNAisa majorsubstrate of the obesity-associated FTO
    • 6-Methyladenosinein nuclear RNAisa majorsubstrate of the obesity-associated FTO. Nat. Chem. Biol. 7, 885-887
    • (2011) Nat. Chem. Biol. , vol.7 , pp. 885-887
    • Jia, G.1
  • 20
    • 77951623073 scopus 로고    scopus 로고
    • Crystal structure of the FTO protein reveals basis for its substrate specificity
    • Han, Z. et al. (2010) Crystal structure of the FTO protein reveals basis for its substrate specificity. Nature 464, 1205-1209
    • (2010) Nature , vol.464 , pp. 1205-1209
    • Han, Z.1
  • 21
    • 66149146320 scopus 로고    scopus 로고
    • Conversion of 5-methylcytosine to 5-hydroxymethylcytosine in mammalian DNA byMLL partner TET1
    • Tahiliani, M. et al. (2009) Conversion of 5-methylcytosine to 5-hydroxymethylcytosine in mammalian DNA byMLL partner TET1. Science 324, 930-935
    • (2009) Science , vol.324 , pp. 930-935
    • Tahiliani, M.1
  • 22
    • 66149123748 scopus 로고    scopus 로고
    • The nuclear DNA base 5-hydroxymethylcytosine is present in Purkinje neurons and the brain
    • Kriaucionis, S. et al. (2009) The nuclear DNA base 5- hydroxymethylcytosine is present in Purkinje neurons and the brain. Science 324, 929-930
    • (2009) Science , vol.324 , pp. 929-930
    • Kriaucionis, S.1
  • 23
    • 80052461558 scopus 로고    scopus 로고
    • Tet proteins can convert 5-methylcytosine to 5-formylcytosine and 5-carboxylcytosine
    • Ito, S. et al. (2011) Tet proteins can convert 5-methylcytosine to 5-formylcytosine and 5-carboxylcytosine. Science 333, 1300-1303
    • (2011) Science , vol.333 , pp. 1300-1303
    • Ito, S.1
  • 24
    • 80052495940 scopus 로고    scopus 로고
    • Tet-mediated formation of 5-carboxylcytosine and its excision by TDG in mammalian DNA
    • He, Y.F. et al. (2011) Tet-mediated formation of 5-carboxylcytosine and its excision by TDG in mammalian DNA. Science 333, 1303-1307
    • (2011) Science , vol.333 , pp. 1303-1307
    • He, Y.F.1
  • 25
    • 79954597550 scopus 로고    scopus 로고
    • Hydroxylation of methylated CpG dinucleotides reverses stabilisation of DNA duplexes by cytosine 5-methylation
    • Thalhammer, A. et al. (2011) Hydroxylation of methylated CpG dinucleotides reverses stabilisation of DNA duplexes by cytosine 5-methylation. Chem. Commun. 47, 5325-5327
    • (2011) Chem. Commun. , vol.47 , pp. 5325-5327
    • Thalhammer, A.1
  • 26
    • 77953037018 scopus 로고    scopus 로고
    • Mutations of the TET2 and CBL genes: Novel molecular markers in myeloid malignancies
    • Bacher, U. et al. (2010) Mutations of the TET2 and CBL genes: novel molecular markers in myeloid malignancies. Ann. Hematol. 89, 643-652
    • (2010) Ann. Hematol. , vol.89 , pp. 643-652
    • Bacher, U.1
  • 28
    • 33646778831 scopus 로고    scopus 로고
    • Repair deficient mice reveal mABH2 as the primary oxidative demethylase for repairing 1meA and 3meC lesions in DNA
    • Ringvoll, J. et al. (2006) Repair deficient mice reveal mABH2 as the primary oxidative demethylase for repairing 1meA and 3meC lesions in DNA. EMBO J. 25, 2189-2198
    • (2006) EMBO J , vol.25 , pp. 2189-2198
    • Ringvoll, J.1
  • 29
    • 68949136580 scopus 로고    scopus 로고
    • Pediatric brain tumors: Mutations of two dioxygenases (hABH2 and hABH3) that directly repair alkylation damage
    • Cetica, V. et al. (2009) Pediatric brain tumors: mutations of two dioxygenases (hABH2 and hABH3) that directly repair alkylation damage. J. Neuro-Oncol. 94, 195-201
    • (2009) J. Neuro-Oncol. , vol.94 , pp. 195-201
    • Cetica, V.1
  • 30
    • 77955027910 scopus 로고    scopus 로고
    • TP53 regulates human AlkB homologue 2 expression in glioma resistance to Photofrin-mediated photodynamic therapy
    • Lee, S.Y. et al. (2010) TP53 regulates human AlkB homologue 2 expression in glioma resistance to Photofrin-mediated photodynamic therapy. Br. J. Cancer 103, 362-369
    • (2010) Br. J. Cancer , vol.103 , pp. 362-369
    • Lee, S.Y.1
  • 31
    • 79952396926 scopus 로고    scopus 로고
    • Down-regulation of ALKBH2 increases cisplatin sensitivity in H1299 lung cancer cells
    • Wu, S.S. et al. (2011) Down-regulation of ALKBH2 increases cisplatin sensitivity in H1299 lung cancer cells. Acta Pharm. Sin. 32, 393-398
    • (2011) Acta Pharm. Sin. , vol.32 , pp. 393-398
    • Wu, S.S.1
  • 32
    • 80555127349 scopus 로고    scopus 로고
    • DNA unwinding by ASCC3 helicase is coupled to ALKBH3-dependent DNA alkylation repair and cancer cell proliferation
    • Dango, S. et al. (2011) DNA unwinding by ASCC3 helicase is coupled to ALKBH3-dependent DNA alkylation repair and cancer cell proliferation. Mol. Cell 44, 373-384
    • (2011) Mol. Cell , vol.44 , pp. 373-384
    • Dango, S.1
  • 33
    • 78449233126 scopus 로고    scopus 로고
    • The AlkB domain of mammalian ABH8 catalyzes hydroxylation of 5-methoxycarbonylmethyluridine at the wobble position of tRNA
    • Fu, Y. et al. (2010) The AlkB domain of mammalian ABH8 catalyzes hydroxylation of 5-methoxycarbonylmethyluridine at the wobble position of tRNA. Angew. Chem. Int. Ed. 49, 8885-8888
    • (2010) Angew. Chem. Int. Ed. , vol.49 , pp. 8885-8888
    • Fu, Y.1
  • 34
    • 79551582659 scopus 로고    scopus 로고
    • ALKBH8-mediated formation of a novel diastereomeric pair of wobble nucleosides in mammalian tRNA
    • van den Born, E. et al. (2011) ALKBH8-mediated formation of a novel diastereomeric pair of wobble nucleosides in mammalian tRNA. Nat. Commun. 2, 172
    • (2011) Nat. Commun. , vol.2 , pp. 172
    • Van Den Born, E.1
  • 36
    • 77949376153 scopus 로고    scopus 로고
    • Mammalian ALKBH8 possesses tRNA methyltransferase activity required for the biogenesis of multiple wobble uridine modifications implicated in translational decoding
    • Songe-Moller, L. et al. (2010) Mammalian ALKBH8 possesses tRNA methyltransferase activity required for the biogenesis of multiple wobble uridine modifications implicated in translational decoding. Mol. Cell Biol. 30, 1814-1827
    • (2010) Mol. Cell Biol. , vol.30 , pp. 1814-1827
    • Songe-Moller, L.1
  • 37
    • 77951981033 scopus 로고    scopus 로고
    • Human AlkB homolog ABH8 is a tRNA methyltransferase required for wobble uridine modification and DNA damage survival
    • Fu, D. et al. (2010) Human AlkB homolog ABH8 is a tRNA methyltransferase required for wobble uridine modification and DNA damage survival. Mol. Cell Biol. 30, 2449-2459
    • (2010) Mol. Cell Biol. , vol.30 , pp. 2449-2459
    • Fu, D.1
  • 38
    • 0345060040 scopus 로고    scopus 로고
    • Novel Methyltransferase for Modified Uridine Residues at the Wobble Position of tRNA
    • DOI 10.1128/MCB.23.24.9283-9292.2003
    • Kalhor, H.R. et al. (2003) Novel methyltransferase for modified uridine residues at the wobble position of tRNA. Mol. Cell Biol. 23, 9283-9292 (Pubitemid 37499815)
    • (2003) Molecular and Cellular Biology , vol.23 , Issue.24 , pp. 9283-9292
    • Kalhor, H.R.1    Clarke, S.2
  • 39
    • 33846269602 scopus 로고    scopus 로고
    • TRNA's Wobble Decoding of the Genome: 40 Years of Modification
    • DOI 10.1016/j.jmb.2006.11.046, PII S0022283606015865
    • Agris, P.F. et al. (2007) tRNA's wobble decoding of the genome: 40 years of modification. J. Mol. Biol. 366, 1-13 (Pubitemid 46123342)
    • (2007) Journal of Molecular Biology , vol.366 , Issue.1 , pp. 1-13
    • Agris, P.F.1    Vendeix, F.A.P.2    Graham, W.D.3
  • 40
    • 78049396647 scopus 로고    scopus 로고
    • Expanding role of the Jumonji C domain as an RNA hydroxylase
    • Noma, A. et al. (2010) Expanding role of the Jumonji C domain as an RNA hydroxylase. J. Biol. Chem. 285, 34503-34507
    • (2010) J. Biol. Chem. , vol.285 , pp. 34503-34507
    • Noma, A.1
  • 41
    • 79952328235 scopus 로고    scopus 로고
    • Crystal structure of a novel JmjC-domain-containing protein, TYW5, involved in tRNA modification
    • Kato, M. et al. (2011) Crystal structure of a novel JmjC-domain- containing protein, TYW5, involved in tRNA modification. Nucl. Acids Res. 39, 1576-1585
    • (2011) Nucl. Acids Res. , vol.39 , pp. 1576-1585
    • Kato, M.1
  • 42
    • 67650072604 scopus 로고    scopus 로고
    • Jmjd6 catalyses lysyl-hydroxylation of U2AF65, a protein associated with RNA splicing
    • Webby, C.J. et al. (2009) Jmjd6 catalyses lysyl-hydroxylation of U2AF65, a protein associated with RNA splicing. Science 325, 90-93
    • (2009) Science , vol.325 , pp. 90-93
    • Webby, C.J.1
  • 43
    • 66149156967 scopus 로고    scopus 로고
    • A novel human AlkB homologue, ALKBH8, contributes to human bladder cancer progression
    • Shimada, K. et al. (2009) A novel human AlkB homologue, ALKBH8, contributes to human bladder cancer progression. Cancer Res. 69, 3157-3164
    • (2009) Cancer Res. , vol.69 , pp. 3157-3164
    • Shimada, K.1
  • 44
    • 54049092869 scopus 로고    scopus 로고
    • Human AlkB homolog 1 is a mitochondrial protein that demethylates 3-methylcytosine in DNA and RNA
    • Westbye, M.P. et al. (2008) Human AlkB homolog 1 is a mitochondrial protein that demethylates 3-methylcytosine in DNA and RNA. J. Biol. Chem. 283, 25046-25056
    • (2008) J. Biol. Chem. , vol.283 , pp. 25046-25056
    • Westbye, M.P.1
  • 45
    • 72949087952 scopus 로고    scopus 로고
    • Human AlkB homologue 1 (ABH1) exhibits DNA lyase activity at abasic sites
    • Muller, T.A. et al. (2010) Human AlkB homologue 1 (ABH1) exhibits DNA lyase activity at abasic sites. DNA Repair 9, 58-65
    • (2010) DNA Repair , vol.9 , pp. 58-65
    • Muller, T.A.1
  • 46
    • 79251588745 scopus 로고    scopus 로고
    • Human AlkB homologue 5 is a nuclear 2-oxoglutarate dependent oxygenase and a direct target of hypoxia-inducible factor 1alpha (HIF-1alpha
    • Thalhammer, A. et al. (2011) Human AlkB homologue 5 is a nuclear 2-oxoglutarate dependent oxygenase and a direct target of hypoxia-inducible factor 1alpha (HIF-1alpha). PLoS ONE 6, e16210
    • (2011) PLoS ONE , vol.6
    • Thalhammer, A.1
  • 47
    • 67650733537 scopus 로고    scopus 로고
    • Direct analysis of enzyme-catalyzed DNA demethylation
    • Karkhanina, A.A. et al. (2009) Direct analysis of enzyme-catalyzed DNA demethylation. Anal. Chem. 81, 5871-5875
    • (2009) Anal. Chem. , vol.81 , pp. 5871-5875
    • Karkhanina, A.A.1
  • 48
    • 79955755461 scopus 로고    scopus 로고
    • Inborn and acquired metabolic defects in cancer
    • Frezza, C. et al. (2011) Inborn and acquired metabolic defects in cancer. J. Mol. Med. 89, 213-220
    • (2011) J. Mol. Med. , vol.89 , pp. 213-220
    • Frezza, C.1
  • 49
    • 79955547561 scopus 로고    scopus 로고
    • The oncometabolite 2-hydroxyglutarate inhibits histone lysine demethylases
    • Chowdhury, R. et al. (2011) The oncometabolite 2-hydroxyglutarate inhibits histone lysine demethylases. EMBO Rep. 12, 463-469
    • (2011) EMBO Rep. , vol.12 , pp. 463-469
    • Chowdhury, R.1
  • 50
    • 78651463452 scopus 로고    scopus 로고
    • Oncometabolite 2-hydroxyglutarate is a competitive inhibitor of a-ketoglutarate-dependent dioxygenases
    • Xu, W. et al. (2011) Oncometabolite 2-hydroxyglutarate is a competitive inhibitor of a-ketoglutarate-dependent dioxygenases. Cancer Cell 19, 17-30
    • (2011) Cancer Cell , vol.19 , pp. 17-30
    • Xu, W.1
  • 51
    • 34548032087 scopus 로고    scopus 로고
    • Genome-wide association studies provide new insights into type 2 diabetes aetiology
    • DOI 10.1038/nrg2178, PII NRG2178
    • Frayling, T.M. (2007) Genome-wide association studies provide new insights into type 2 diabetes aetiology. Nat. Rev. Genet. 8, 657-662 (Pubitemid 47281993)
    • (2007) Nature Reviews Genetics , vol.8 , Issue.9 , pp. 657-662
    • Frayling, T.M.1
  • 52
    • 78650175023 scopus 로고    scopus 로고
    • Impaired hydroxylation of 5-methylcytosine in myeloid cancers with mutant TET2
    • Ko, M. et al. (2010) Impaired hydroxylation of 5-methylcytosine in myeloid cancers with mutant TET2. Nature 468, 839-843
    • (2010) Nature , vol.468 , pp. 839-843
    • Ko, M.1
  • 53
    • 77955983722 scopus 로고    scopus 로고
    • Origin and evolution of peptide-modifying dioxygenases and identification of the wybutosine hydroxylase/hydroperoxidase
    • Iyer, L.M. et al. (2010) Origin and evolution of peptide-modifying dioxygenases and identification of the wybutosine hydroxylase/hydroperoxidase. Nucl. Acids Res. 38, 5261-5279
    • (2010) Nucl. Acids Res. , vol.38 , pp. 5261-5279
    • Iyer, L.M.1
  • 54
    • 13444280435 scopus 로고    scopus 로고
    • Repair of 3-methylthymine and 1-methylguanine lesions by bacterial and human AlkB proteins
    • DOI 10.1093/nar/gkh964
    • Falnes, P.O. (2004) Repair of 3-methylthymine and 1-methylguanine lesions by bacterial and human AlkB proteins. Nucl. Acids Res. 32, 6260-6267 (Pubitemid 40202084)
    • (2004) Nucleic Acids Research , vol.32 , Issue.21 , pp. 6260-6267
    • Falnes, P.O.1
  • 55
    • 37549024986 scopus 로고    scopus 로고
    • Kinetic studies of Escherichia coli AlkB using a new fluorescence-based assay for DNA demethylation
    • Roy, T.W. et al. (2007) Kinetic studies of Escherichia coli AlkB using a new fluorescence-based assay for DNA demethylation. Nucl. Acids Res. 35, e147
    • (2007) Nucl. Acids Res. , vol.35
    • Roy, T.W.1
  • 57
    • 33745198199 scopus 로고    scopus 로고
    • Direct removal of alkylation damage from DNA by AlkB and related DNA dioxygenases
    • Sedgwick, B. et al. (2006) Direct removal of alkylation damage from DNA by AlkB and related DNA dioxygenases. Methods Enzymol. 408, 108-120
    • (2006) Methods Enzymol. , vol.408 , pp. 108-120
    • Sedgwick, B.1
  • 58
    • 78649825211 scopus 로고    scopus 로고
    • TET1 is a DNA-binding protein that modulates DNA methylation and gene transcription via hydroxylation of 5-methylcytosine
    • Zhang, H.K. et al. (2010) TET1 is a DNA-binding protein that modulates DNA methylation and gene transcription via hydroxylation of 5-methylcytosine. Cell Res. 20, 1390-1393
    • (2010) Cell Res. , vol.20 , pp. 1390-1393
    • Zhang, H.K.1
  • 60
    • 77956189495 scopus 로고    scopus 로고
    • Role of Tet proteins in 5mC to5hmC conversion, ES-cell self-renewal and inner cell mass specification
    • Ito, S. et al. (2010) Role of Tet proteins in 5mC to5hmC conversion, ES-cell self-renewal and inner cell mass specification. Nature 466, 1129-1133
    • (2010) Nature , vol.466 , pp. 1129-1133
    • Ito, S.1
  • 61
    • 80053210330 scopus 로고    scopus 로고
    • Roles of Trm9-and ALKBH8-like proteins in the formation of modified wobble uridines in Arabidopsis tRNA
    • Leihne, V. et al. (2011) Roles of Trm9-and ALKBH8-like proteins in the formation of modified wobble uridines in Arabidopsis tRNA. Nucl. Acids Res. 39, 7688-7701
    • (2011) Nucl. Acids Res. , vol.39 , pp. 7688-7701
    • Leihne, V.1
  • 62
    • 70149118360 scopus 로고    scopus 로고
    • Enzymological and structural studies of the mechanism of promiscuous substrate recognition by the oxidative DNA repair enzyme AlkB
    • Yu, B. et al. (2009) Enzymological and structural studies of the mechanism of promiscuous substrate recognition by the oxidative DNA repair enzyme AlkB. Proc. Natl. Acad. Sci. U. S. A. 106, 14315-14320
    • (2009) Proc. Natl. Acad. Sci. U. S. A. , vol.106 , pp. 14315-14320
    • Yu, B.1


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