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Volumn , Issue , 2009, Pages 377-391

Enzymatic formation of the 7-deazaguanosine hypermodified nucleosides of tRNA

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EID: 71849095615     PISSN: None     EISSN: None     Source Type: Book    
DOI: None     Document Type: Chapter
Times cited : (14)

References (114)
  • 1
    • 0016804870 scopus 로고
    • Structure of the modified nucleoside q isolated from escherichia coli transfer ribonucleic acid. 7-(4,5-cis-dihydroxy-1-cyclopenten-3-ylaminomethyl)-7-deazaguanosine
    • Kasai H, Ohashi Z, Harada F et al Structure of the modified nucleoside Q isolated from Escherichia coli transfer ribonucleic acid. 7-(4,5-cis-Dihydroxy-1-cyclopenten-3-ylaminomethyl)-7-deazaguanosine. Biochemistry 1975; 14(19):4198-4208.
    • (1975) Biochemistry , vol.14 , Issue.19 , pp. 4198-4208
    • Kasai, H.1    Ohashi, Z.2    Harada, F.3
  • 2
    • 0000525868 scopus 로고
    • Total synthesis of optically pure nucleoside q. Determination of absolute configuration of natural nucleoside q
    • Ohgi T, Kondo T, Goto T. Total synthesis of optically pure nucleoside Q. Determination of absolute configuration of natural nucleoside Q. J Am Chem Soc 1979; 101:3629-3633.
    • (1979) J am Chem Soc , vol.101 , pp. 3629-3633
    • Ohgi, T.1    Kondo, T.2    Goto, T.3
  • 3
    • 0027191379 scopus 로고
    • Structure of archaeal transfer rna nucleoside g*-15 (2-amino-4,7-dihydro-4-oxo-7-β-d-ribofuranosyl-1h-pyrrolo[2,3-d]pyrimidine'5'carboiimidamide (ar-chaeosine))
    • Gregson JM, Crain PF, Edmonds CG et al. Structure of archaeal transfer RNA nucleoside G*-15 (2-Amino-4,7-dihydro-4-oxo-7-β-D-ribofuranosyl-1H-pyrrolo[2,3-d]pyrimidine'5'Carboiimidamide (Ar-chaeosine)). J Biol Chem 1993; 268(14):10076-10086.
    • (1993) J Biol Chem , vol.268 , Issue.14 , pp. 10076-10086
    • Gregson, J.M.1    Crain, P.F.2    Edmonds, C.G.3
  • 4
    • 0017298136 scopus 로고
    • The structure of q* nucleoside isolated from rabbit liver transfer ribonucleic acid
    • Kasai H, Nakanishi K, Macfarlane RD et al The structure of Q* nucleoside isolated from rabbit liver transfer ribonucleic acid. J Am Chem Soc 1976; 98(16):5044-5046.
    • (1976) J am Chem Soc , vol.98 , Issue.16 , pp. 5044-5046
    • Kasai, H.1    Nakanishi, K.2    Macfarlane, R.D.3
  • 5
    • 0017459030 scopus 로고
    • Isolation of mammalian trnaasp and trnatyr by lectin-sep-harose affinity column chromatography
    • Okada N, Shindo-Okada N, Nishimura S. Isolation of mammalian tRNAAsp and tRNATyr by lectin-Sep-harose affinity column chromatography. Nucleic Acids Res 1977; 4(2):415-423.
    • (1977) Nucleic Acids Res , vol.4 , Issue.2 , pp. 415-423
    • Okada, N.1    Shindo-Okada, N.2    Nishimura, S.3
  • 6
    • 2442709155 scopus 로고    scopus 로고
    • A minimalist glutamyl-trna synthetase dedicated to aminoacylation of the trnaasp quo anticodon
    • Blaise M, Becker HD, Keith G et al A minimalist glutamyl-tRNA synthetase dedicated to aminoacylation of the tRNAAsp QUO anticodon. Nucleic Acids Res 2004; 32(9):2768-2775.
    • (2004) Nucleic Acids Res , vol.32 , Issue.9 , pp. 2768-2775
    • Blaise, M.1    Becker, H.D.2    Keith, G.3
  • 7
    • 1842642896 scopus 로고    scopus 로고
    • A truncated aminoacyl-trna synthetase modifies rna
    • Salazar JC, Ambrogelly A, Crain PF et al. A truncated aminoacyl-tRNA synthetase modifies RNA. Proc Natl Acad Sci USA 2004; 101(20):7536-7541.
    • (2004) Proc Natl Acad Sci USA , vol.101 , Issue.20 , pp. 7536-7541
    • Salazar, J.C.1    Ambrogelly, A.2    Crain, P.F.3
  • 8
    • 85012592477 scopus 로고
    • Biosynthesis and function of queuine and queuosine trnas
    • Gehrke CW, Kuo KCT, eds., Amsterdam: Elsevier
    • Kcrstcn H, Kersten W. Biosynthesis and function of queuine and queuosine tRNAs. In: Gehrke CW, Kuo KCT, eds. Chromatography and Modification of Nucleosides Part B. Amsterdam: Elsevier, 1990:B69-B108.
    • (1990) Chromatography and Modification of Nucleosides Part B , pp. BB69-B108
    • Kcrstcn, H.1    Kersten, W.2
  • 9
    • 1642445245 scopus 로고
    • Detection of unique trna species in tumor tissues by e. Coli guanine insertion enzyme
    • Okada N, Shindo-Okada N, Sato S et al Detection of unique tRNA species in tumor tissues by E. coli guanine insertion enzyme. Proc Natl Acad Sci USA 1978; 75:4247-4251.
    • (1978) Proc Natl Acad Sci USA , vol.75 , pp. 4247-4251
    • Okada, N.1    Shindo-Okada, N.2    Sato, S.3
  • 10
    • 0018582874 scopus 로고
    • Alteration of the q family of transfer rnas in adult drosophila as a function of age, nutrition and genotype
    • Owenby RK, Stulberg MB, Jacobson KB. Alteration of the Q family of transfer RNAs in adult Drosophila as a function of age, nutrition and genotype. Mcch Age Develop 1979; 11:91-103.
    • (1979) Mcch Age Develop , vol.11 , pp. 91-103
    • Owenby, R.K.1    Stulberg, M.B.2    Jacobson, K.B.3
  • 11
    • 0015924554 scopus 로고
    • Activity of a transfer rna modifying enzyme during the development of drosophila and its relationship to the su(S) locus
    • White BN, Tener GM, Holden J et al Activity of a transfer RNA modifying enzyme during the development of Drosophila and its relationship to the su(s) locus. J Mol Biol 1973; 74:635-651.
    • (1973) J Mol Biol , vol.74 , pp. 635-651
    • White, B.N.1    Tener, G.M.2    Holden, J.3
  • 12
    • 0022408375 scopus 로고
    • Relationship of queuine-lacking trnas to the grade of malignancy in human leukemias and lymphomas
    • Emmerich B, Zubrod E, Weber H et al Relationship of queuine-lacking tRNAs to the grade of malignancy in human leukemias and lymphomas. Cancer Res 1985; 45:4308-4314.
    • (1985) Cancer Res , vol.45 , pp. 4308-4314
    • Emmerich, B.1    Zubrod, E.2    Weber, H.3
  • 13
    • 0026737277 scopus 로고
    • Relationship of the queuine content of trna to histopathological grading and survival in human lung cancer
    • Huang B-S, Wu R-T, Chien K-W. Relationship of the queuine content of tRNA to histopathological grading and survival in human lung cancer. Cancer Res 1992; 52:4696-4700.
    • (1992) Cancer Res , vol.52 , pp. 4696-4700
    • Huang, B.-S.1    Wu, R.-T.2    Chien, K.-W.3
  • 14
    • 0028068635 scopus 로고
    • Deficiency of queuine, a highly modified purine base, in transfer rnas from primary and metastatic ovarian malignant tumors in women
    • Baranowski W, Dirheimer G, Jakowicki JA et al. Deficiency of queuine, a highly modified purine base, in transfer RNAs from primary and metastatic ovarian malignant tumors in women. Cancer Res 1994; 54:4468-4471.
    • (1994) Cancer Res , vol.54 , pp. 4468-4471
    • Baranowski, W.1    Dirheimer, G.2    Jakowicki, J.A.3
  • 15
    • 3042815958 scopus 로고    scopus 로고
    • Elevated expression level of 60-kda subunit of trna-guanine transglycosylase in colon cancer
    • Ishiwata S, Ozawa Y, Katayama J et al Elevated expression level of 60-kDa subunit of tRNA-guanine transglycosylase in colon cancer. Cancer Lett 2004; 212(1):113-119.
    • (2004) Cancer Lett , vol.212 , Issue.1 , pp. 113-119
    • Ishiwata, S.1    Ozawa, Y.2    Katayama, J.3
  • 16
    • 0035130319 scopus 로고    scopus 로고
    • Increased expression of queuosine synthesizing enzyme, trna-guanine transglycosylase and queuosine levels in trna of leukemic cells
    • Ishiwata S, Katayama J, Shindo H et al Increased expression of queuosine synthesizing enzyme, tRNA-guanine transglycosylase and queuosine levels in tRNA of leukemic cells. J Biochem 2001; 129(1):13-17.
    • (2001) J Biochem , vol.129 , Issue.1 , pp. 13-17
    • Ishiwata, S.1    Katayama, J.2    Shindo, H.3
  • 17
    • 0031566184 scopus 로고    scopus 로고
    • Effects of a diet deficient in tyrosine and queuine on germfree mice
    • Marks T, Farkas WR. Effects of a diet deficient in tyrosine and queuine on germfree mice. Biochem Biophys Res Commun 1997; 230(2):233-237.
    • (1997) Biochem Biophys Res Commun , vol.230 , Issue.2 , pp. 233-237
    • Marks, T.1    Farkas, W.R.2
  • 19
    • 0034728277 scopus 로고    scopus 로고
    • Yeast asparagine (Asn) trna without q base promotes eukaryotic frameshifting more efficiently than mammalian asn trnas with or without q base
    • Carlson BA, Kwon SY, Lee BJ et al Yeast asparagine (Asn) tRNA without Q base promotes eukaryotic frameshifting more efficiently than mammalian Asn tRNAs with or without Q base. Mol Cells 2000; 10(1):113-118.
    • (2000) Mol Cells , vol.10 , Issue.1 , pp. 113-118
    • Carlson, B.A.1    Kwon, S.Y.2    Lee, B.J.3
  • 20
    • 0345624489 scopus 로고    scopus 로고
    • Transfer rna modification status influences retroviral ribosomal frameshifting
    • Carlson BA, Kwon SY, Chamorro M et al Transfer RNA modification status influences retroviral ribosomal frameshifting. Virology 1999; 255(l):2-8.
    • (1999) Virology , vol.255 , Issue.1 , pp. 2-8
    • Carlson, B.A.1    Kwon, S.Y.2    Chamorro, M.3
  • 21
    • 0024789601 scopus 로고
    • Chromatographic analysis of the aminoacyl-trnas which are required for translation of codons at and around the ribosomal frameshift sites of hiv, htlv-1 and blv
    • Hatfield D, Feng Y-X, Lee BJ et al Chromatographic analysis of the aminoacyl-tRNAs which are required for translation of codons at and around the ribosomal frameshift sites of HIV, HTLV-1 and BLV. Virology 1989; 173:736-742.
    • (1989) Virology , vol.173 , pp. 736-742
    • Hatfield, D.1    Feng, Y.-X.2    Lee, B.J.3
  • 22
    • 0024277965 scopus 로고
    • Signals for ribosomal frameshifting in the rous sarcoma virus gag-pol region
    • Jacks T, Madhani HD, Masiarz FR et al Signals for ribosomal frameshifting in the rous sarcoma virus gag-pol region. Cell 1988; 55:447-458.
    • (1988) Cell , vol.55 , pp. 447-458
    • Jacks, T.1    Madhani, H.D.2    Masiarz, F.R.3
  • 23
    • 0033965439 scopus 로고    scopus 로고
    • Transfer rna modification, temperature and dna superhelicity have a common target in the regulatory network of the virulence of shigella flcxncri: The expression of the virf gene
    • Durand JM, Dagberg B, Uhlin BE et al. Transfer RNA modification, temperature and DNA superhelicity have a common target in the regulatory network of the virulence of Shigella flcxncri: the expression of the virF gene. Mol Microbiol 2000; 35(4):924-935.
    • (2000) Mol Microbiol , vol.35 , Issue.4 , pp. 924-935
    • Durand, J.M.1    Dagberg, B.2    Uhlin, B.E.3
  • 24
    • 0028041249 scopus 로고
    • Vacc, a virulence-associated chromosomal locus of shigella flexneri, is homologous to tgt, a gene encoding trna-guanine transglycosylase (Tgt) of e. coli k-12
    • Durand J, Okada N, Tobe T et al. vacC, a virulence-associated chromosomal locus of shigella flexneri, is homologous to tgt, a gene encoding tRNA-guanine transglycosylase (Tgt) of E. coli K-12. J Bacteriol1994; 176(15):4627-4634.
    • (1994) J Bacteriol , vol.176 , Issue.15 , pp. 4627-4634
    • Durand, J.1    Okada, N.2    Tobe, T.3
  • 25
    • 0022036496 scopus 로고
    • Queuosine modification of the wobble base in trna-his influences in vivo decoding properties
    • 24b. Meier F, Surer B, Grosjean H et al. Queuosine modification of the wobble base in tRNA-His influences in vivo decoding properties. The EMBO J 1985; 4:823-827.
    • (1985) The EMBO J , vol.4 , pp. 823-827
    • Meier, F.1    Surer, B.2    Grosjean, H.3
  • 26
    • 0019310310 scopus 로고
    • Distinctive sequence of human mitochondrial ribosomal rna genes
    • Eperon IC, Anderson S, Nierlich DP. Distinctive sequence of human mitochondrial ribosomal RNA genes. Nature 1980; 286(5772):460-467.
    • (1980) Nature , vol.286 , Issue.5772 , pp. 460-467
    • Eperon, I.C.1    Erson, S.2    Nierlich, D.P.3
  • 27
    • 0028353466 scopus 로고
    • The nutrient factor queuine protects hclc cells from hypoxic stress and improves metabolic adaptation to oxygen availability
    • Reisser T, Langgut W, Kersten H. The nutrient factor queuine protects HcLc cells from hypoxic stress and improves metabolic adaptation to oxygen availability. Eur J Biochem 1994; 221:979-986.
    • (1994) Eur J Biochem , vol.221 , pp. 979-986
    • Reisser, T.1    Langgut, W.2    Kersten, H.3
  • 28
    • 42549162439 scopus 로고    scopus 로고
    • Modulation in the activity of lactate dehydrogenase and level of c-myc and c-fos by modified base queuine in cancer
    • Pathak C, Jaiswal YK, Vinayak M. Modulation in the activity of lactate dehydrogenase and level of c-Myc and c-Fos by modified base queuine in cancer. Cancer Biol Ther 2008; 7(1):85-91.
    • (2008) Cancer Biol Ther , vol.7 , Issue.1 , pp. 85-91
    • Pathak, C.1    Jaiswal, Y.K.2    Vinayak, M.3
  • 29
    • 25444452879 scopus 로고    scopus 로고
    • Modulation of lactate dehydrogenase isozymes by modified base queuine
    • Pathak C, Vinayak M. Modulation of lactate dehydrogenase isozymes by modified base queuine. Mol Biol Rep 2005; 32(3):191-196.
    • (2005) Mol Biol Rep , vol.32 , Issue.3 , pp. 191-196
    • Pathak, C.1    Vinayak, M.2
  • 30
    • 48249144817 scopus 로고    scopus 로고
    • Queuine mediated inhibition in phosphorylation of tyrosine phospho-proteins in cancer
    • Pathak C, Jaiswal YK, Vinayak M. Queuine mediated inhibition in phosphorylation of tyrosine phospho-proteins in cancer. Mol Biol Rep 2008; 35(3):369-374.
    • (2008) Mol Biol Rep , vol.35 , Issue.3 , pp. 369-374
    • Pathak, C.1    Jaiswal, Y.K.2    Vinayak, M.3
  • 31
    • 0027446680 scopus 로고
    • Modulation of epidermal growth factor receptor activity and related responses by the 7-deazaguanine derivative, queuine
    • Langgut W, Reisser T, Kersten H et al Modulation of epidermal growth factor receptor activity and related responses by the 7-deazaguanine derivative, queuine. Oncogene 1993; 8:3141-3147.
    • (1993) Oncogene , vol.8 , pp. 3141-3147
    • Langgut, W.1    Reisser, T.2    Kersten, H.3
  • 32
    • 0025173473 scopus 로고
    • Possible involvement of queuine in control mechanisms of protein synthesis and protein phosphorylation in eukaryotes
    • Mahr U, Bohm P, Kersten H. Possible involvement of queuine in control mechanisms of protein synthesis and protein phosphorylation in eukaryotes. BioFactors 1990; 2(3):185-192.
    • (1990) Biofactors , vol.2 , Issue.3 , pp. 185-192
    • Mahr, U.1    Bohm, P.2    Kersten, H.3
  • 33
    • 36549029244 scopus 로고    scopus 로고
    • Possible involvement of queuine in regulation of cell proliferation
    • Pathak C, Jaiswal YK, Vinayak M. Possible involvement of queuine in regulation of cell proliferation. Biofactors 2007; 29(4):159-173.
    • (2007) Biofactors , vol.29 , Issue.4 , pp. 159-173
    • Pathak, C.1    Jaiswal, Y.K.2    Vinayak, M.3
  • 34
    • 0028908903 scopus 로고
    • Regulation of signalling by receptor tyrosine kinases in hela cells involves the q-base
    • Langgut W. Regulation of signalling by receptor tyrosine kinases in heLa cells involves the q-base. Biochem Biophy Res Comm 1995; 207(1):306-311.
    • (1995) Biochem Biophy Res Comm , vol.207 , Issue.1 , pp. 306-311
    • Langgut, W.1
  • 35
    • 0027379152 scopus 로고
    • Modulation of mammalian cell proliferation by a modified trna base of bacterial origin
    • Langgut W, Reisser T, Nishimura S et al Modulation of mammalian cell proliferation by a modified tRNA base of bacterial origin. FEBS Lett 1993; 336(1):137-142.
    • (1993) FEBS Lett , vol.336 , Issue.1 , pp. 137-142
    • Langgut, W.1    Reisser, T.2    Nishimura, S.3
  • 36
    • 0025370590 scopus 로고
    • The deazaguanine-derivative, queuine, affects cell proliferation, protein phosphorylation and the expression of the proto pncogenes c-fbs and c-myc in hela cells
    • Langgut W, Kersten H. The deazaguanine-derivative, queuine, affects cell proliferation, protein phosphorylation and the expression of the proto pncogenes c-fbs and c-myc in HeLa cells. FEBS Lett 1990; 265:33-36.
    • (1990) FEBS Lett , vol.265 , pp. 33-36
    • Langgut, W.1    Kersten, H.2
  • 37
    • 0025977143 scopus 로고
    • Queuine, a trna anticodon wobble base, maintains the proliferative and pluripotent potential of hl-60 cells in the presence of the differentiating agent 6-thioguanine
    • French BT, Patrick DE, Grever MR et al Queuine, a tRNA anticodon wobble base, maintains the proliferative and pluripotent potential of HL-60 cells in the presence of the differentiating agent 6-thioguanine. Proc Natl Acad Sci USA 1991; 88:370-374.
    • (1991) Proc Natl Acad Sci USA , vol.88 , pp. 370-374
    • French, B.T.1    Patrick, D.E.2    Grever, M.R.3
  • 38
    • 0018588082 scopus 로고
    • Naturally occurring nucleoside and nucleotide antibiotics
    • Suhadolnik RJ. Naturally occurring nucleoside and nucleotide antibiotics. Prog Nucleic Acid Res Mol Biol1979; 22:193-291.
    • (1979) Prog Nucleic Acid Res Mol Biol , vol.22 , pp. 193-291
    • Suhadolnik, R.J.1
  • 39
    • 0001968230 scopus 로고
    • Primary, secondary and tertiary structure of trnas
    • Soil D, RajBhandary UL, eds., Washington D.C.: ASM Press
    • Dirheimer G, Keith G, Dumas P et al Primary, secondary and tertiary structure of tRNAs. In: Soil D, RajBhandary UL, eds. tRNA: Structure, Biosynthesis and Function. Washington D.C.: ASM Press, 1995:93-126.
    • (1995) Trna: Structure, Biosynthesis and Function , pp. 93-126
    • Dirheimer, G.1    Keith, G.2    Dumas, P.3
  • 40
    • 0017295709 scopus 로고
    • Conformational changes of transfer rna. The role of magnesium(ii)
    • Stein A, Crothers DM. Conformational changes of transfer RNA. The role of magnesium(II). Biochemistry1976; 15(1):160-168.
    • (1976) Biochemistry , vol.15 , Issue.1 , pp. 160-168
    • Stein, A.1    Crothers, D.M.2
  • 41
    • 0017055057 scopus 로고
    • Crystallographic refinement of yeast phenylalanine transfer rna at 2-5a resolution
    • Jack A, Ladner JE, Klug A. Crystallographic refinement of yeast phenylalanine transfer RNA at 2-5A resolution. J Mol Biol 1976; 108(4):619-649.
    • (1976) J Mol Biol , vol.108 , Issue.4 , pp. 619-649
    • Jack, A.1    Ladner, J.E.2    Klug, A.3
  • 42
    • 0033862354 scopus 로고    scopus 로고
    • The crystal structure of yeast phenylalanine trna at 1.93 a resolution: A classic structure revisited
    • Shi H, Moore PB. The crystal structure of yeast phenylalanine tRNA at 1.93 A resolution: a classic structure revisited. RNA 2000; 6(8):1091-1105.
    • (2000) RNA , vol.6 , Issue.8 , pp. 1091-1105
    • Shi, H.1    Moore, P.B.2
  • 43
    • 34548353962 scopus 로고    scopus 로고
    • Mg2+ binding and archaeosine modification stabilize the g15 c48 levitt base pair in trnas
    • Oliva R, Tramontano A, Cavallo L. Mg2+ binding and archaeosine modification stabilize the G15 C48 Levitt base pair in tRNAs. RNA 2007; 13(9):1427-1436.
    • (2007) RNA , vol.13 , Issue.9 , pp. 1427-1436
    • Oliva, R.1    Tramontano, A.2    Cavallo, L.3
  • 44
    • 0037310429 scopus 로고    scopus 로고
    • Biosynthesis of the 7-deazaguanosine hypermodified nucleosides of transfer rna
    • Iwata-Reuyl D. Biosynthesis of the 7-deazaguanosine hypermodified nucleosides of transfer RNA. Bioorg Chem 2003; 31(1):24-43.
    • (2003) Bioorg Chem , vol.31 , Issue.1 , pp. 24-43
    • Iwata-Reuyl, D.1
  • 45
    • 0017230764 scopus 로고
    • Biosynthesis of the modified nucleoside q in transfer rna
    • Kuchino Y, Kasai H, Nihei K et al Biosynthesis of the modified nucleoside Q in transfer RNA. Nucleic Acids Research 1976; 3:393-398.
    • (1976) Nucleic Acids Research , vol.3 , pp. 393-398
    • Kuchino, Y.1    Kasai, H.2
  • 46
    • 0018497447 scopus 로고
    • A factor in serum and amniotic fluid is a substrate for the trna-modifying enzyme trna-guanine transferase
    • Katze JR, Farkas WR. A factor in serum and amniotic fluid is a substrate for the tRNA-modifying enzyme tRNA-guanine transferase. Proc Natl Acad Sci USA 1979; 76(7):3271-3275.
    • (1979) Proc Natl Acad Sci USA , vol.76 , Issue.7 , pp. 3271-3275
    • Katze, J.R.1    Farkas, W.R.2
  • 47
    • 0018800830 scopus 로고
    • Novel mechanism of posttranscriptional modification of trna. insertion of bases of q precursors into trna by a specific trna transglycosylasc reaction
    • Okada N, Noguchi S, Kasai H et al Novel mechanism of posttranscriptional modification of tRNA. Insertion of bases of Q precursors into tRNA by a specific tRNA transglycosylasc reaction. J Biol Chem1979; 254(8):3067-3073.
    • (1979) J Biol Chem , vol.254 , Issue.8 , pp. 3067-3073
    • Okada, N.1    Noguchi, S.2    Kasai, H.3
  • 48
    • 0020485425 scopus 로고
    • Salvage of the nucleic acid base queuine from queuine-containing trna by animal cells
    • Gunduz U, Katzc JR. Salvage of the nucleic acid base queuine from queuine-containing tRNA by animal cells. Biochem Biophys Res Comm 1982; 109(1):159-167.
    • (1982) Biochem Biophys Res Comm , vol.109 , Issue.1 , pp. 159-167
    • Gunduz, U.1    Katzc, J.R.2
  • 49
    • 0024197850 scopus 로고
    • Novel salvage of queuine from queuosine and absence of queuine synthesis in chlorella pyrenoidosa and chlamydomonas rcinhardtii
    • Kirtland GM, Morris TD, Moore PH et al Novel salvage of queuine from queuosine and absence of queuine synthesis in chlorella pyrenoidosa and chlamydomonas rcinhardtii. J Bacteriol 1988; 170(12):5633-5641.
    • (1988) J Bacteriol , vol.170 , Issue.12 , pp. 5633-5641
    • Kirtland, G.M.1    Morris, T.D.2    Moore, P.H.3
  • 50
    • 57349131670 scopus 로고    scopus 로고
    • The biosynthesis of the 7-deazaguanosinc modified trna nucleosides: A new role for gtp cyclohydrolase-i
    • Phillips G, Yacoubi BE, Lyons B et al The biosynthesis of the 7-deazaguanosinc modified tRNA nucleosides: A new role for GTP cyclohydrolase-I. J Bacteriol 2008:7876-84.
    • (2008) J Bacteriol , pp. 7876-7884
    • Phillips, G.1    Yacoubi, B.E.2    Lyons, B.3
  • 51
    • 34249874032 scopus 로고    scopus 로고
    • Characterization of fe(2+)-dependent archaeal-specific gtp cyclohydrolase, mpta, from methanocaldococcus jannaschii
    • 49b. Grochowski LL, Xu H, Leung K et al Characterization of Fe(2+)-dependent archaeal-specific GTP cyclohydrolase, MptA, from methanocaldococcus jannaschii. Biochemistry 2007; 46(22):6658-6667.
    • (2007) Biochemistry , vol.46 , Issue.22 , pp. 6658-6667
    • Grochowski, L.L.1    Xu, H.2    Leung, K.3
  • 52
    • 0036011084 scopus 로고    scopus 로고
    • Synthesis and turnover of folates in plants
    • Hanson AD, Gregory JF, 3rd. Synthesis and turnover of folates in plants. Cure Opin Plant Biol 2002; 5(3):244-249.
    • (2002) Cure Opin Plant Biol , vol.5 , Issue.3 , pp. 244-249
    • Hanson, A.D.1    Gregory, J.F.2
  • 53
    • 0035996799 scopus 로고    scopus 로고
    • The folic add biosynthesis pathway in bacteria: Evaluation of potential for antibacterial drug discovery
    • Bermingham A, Derrick JP. The folic add biosynthesis pathway in bacteria: evaluation of potential for antibacterial drug discovery. Bioessays 2002; 24(7):637-648.
    • (2002) Bioessays , vol.24 , Issue.7 , pp. 637-648
    • Bermingham, A.1    Derrick, J.P.2
  • 54
    • 0034176921 scopus 로고    scopus 로고
    • Tereahydrobiopterin biosynthesis, regeneration and functions
    • Thony B, Auerbach G, Blau N. Tereahydrobiopterin biosynthesis, regeneration and functions. Biochem J2000; 347(Pt 1):1-16.
    • (2000) Biochem J , vol.347 , pp. 1-16
    • Thony, B.1    Auerbach, G.2    Blau, N.3
  • 55
    • 1342325436 scopus 로고    scopus 로고
    • Identification of four genes necessary for biosynthesis of the modified nucleoside queuosine
    • Reader JS, Metzgar D, Schimmel P et al Identification of four genes necessary for biosynthesis of the modified nucleoside queuosine. J Biol Chem 2004; 279(8):6280-6285.
    • (2004) J Biol Chem , vol.279 , Issue.8 , pp. 6280-6285
    • Reader, J.S.1    Metzgar, D.2    Schimmel, P.3
  • 56
    • 0037125195 scopus 로고    scopus 로고
    • Escherichia coli 6-pynivoyltctrahydroptcrin synthase ortholog encoded by ygcm has a new catalytic activity for conversion of sepiapterin to 7,8-dihydropterin
    • Woo HJ, Hwang YK, Kim YJ et al Escherichia coli 6-pynivoyltctrahydroptcrin synthase ortholog encoded by ygcM has a new catalytic activity for conversion of sepiapterin to 7,8-dihydropterin. FEBS Lett 2002; 523(1-3):234-238.
    • (2002) FEBS Lett , vol.523 , Issue.1-3 , pp. 234-238
    • Woo, H.J.1    Hwang, Y.K.2    Kim, Y.J.3
  • 58
    • 0035282866 scopus 로고    scopus 로고
    • Radical sam, a novel protein superfamily linking unresolved steps in familiar biosynthetic pathways with radical mechanisms: Functional characterization using new analysis and information visualization methods
    • Sofia HJ, Chen G, Hetzler BG et al Radical SAM, a novel protein superfamily linking unresolved steps in familiar biosynthetic pathways with radical mechanisms: functional characterization using new analysis and information visualization methods. Nucleic Adds Res 2001; 29(5):1097-1106.
    • (2001) Nucleic Adds Res , vol.29 , Issue.5 , pp. 1097-1106
    • Sofia, H.J.1    Chen, G.2    Hetzler, B.G.3
  • 60
    • 4644367918 scopus 로고    scopus 로고
    • S-adenosylmethionine radical enzymes
    • Marsh EN, Patwardhan A, Huhta MS. S-adenosylmethionine radical enzymes. Bioorg Chem 2004; 32(5):326-340.
    • (2004) Bioorg Chem , vol.32 , Issue.5 , pp. 326-340
    • Marsh, E.N.1    Patwardhan, A.2    Huhta, M.S.3
  • 61
    • 15444381025 scopus 로고    scopus 로고
    • From cyclohydrolase to oxidoreductase: Discovery of nitrile reductase activity in a common fold
    • Van Lanen SG, Reader JS, Swairjo MA et al From cyclohydrolase to oxidoreductase: discovery of nitrile reductase activity in a common fold. Proc Natl Acad Sd USA 2005; 102(12):4264-4269.
    • (2005) Proc Natl Acad Sd USA , vol.102 , Issue.12 , pp. 4264-4269
    • Van Lanen, S.G.1    Reader, J.S.2    Swairjo, M.A.3
  • 62
    • 0023903154 scopus 로고
    • New function of vitamin bi2: Cobamide-dependent redaction of epoxyqueuosine to queuosine in trnas of escherichia coli and salmonella typhimurium
    • 2: Cobamide-dependent redaction of epoxyqueuosine to queuosine in tRNAs of Escherichia coli and salmonella typhimurium. J Bacteriol1988; 170(5):2078-2082.
    • (1988) J Bacteriol , vol.170 , Issue.5 , pp. 2078-2082
    • Frey, B.1    McCloskey, J.A.2    Kersten, W.3
  • 63
    • 0017390969 scopus 로고
    • Enzymatic synthesis of q* nucleoside containing mannose in the anticodon of trna: Isolation of a novel mannosyltransferase from a cell-free extract of rat liver
    • Okada N, Nishimura S. Enzymatic synthesis of Q* nucleoside containing mannose in the anticodon of tRNA: Isolation of a novel mannosyltransferase from a cell-free extract of Rat Liver. Nucleic Acids Research1977; 4(8):2931-2937.
    • (1977) Nucleic Acids Research , vol.4 , Issue.8 , pp. 2931-2937
    • Okada, N.1    Nishimura, S.2
  • 64
    • 0034665997 scopus 로고    scopus 로고
    • Hypermodification of trna in thermophilic archaea. Cloning, overexpression and characterization of trna-guanine transglycosylase from methanococcus jannaschii
    • Bai Y, Fox DT, Lacy JA et al. Hypermodification of tRNA in Thermophilic archaea. Cloning, overexpression and characterization of tRNA-guanine transglycosylase from Methanococcus jannaschii. J Biol Chcm2000; 275(37):28731-28738.
    • (2000) J Biol Chcm , vol.275 , Issue.37 , pp. 28731-28738
    • Bai, Y.1    Fox, D.T.2    Lacy, J.A.3
  • 65
    • 0030792095 scopus 로고    scopus 로고
    • Biosynthesis of archaeosinc, a novel derivative of 7-deazaguanosine specific to archaeal trna, proceeds via a pathway involving base replacement of the trna polynucleotide chain
    • Watanabe M, Matsuo M, Tanaka S et al Biosynthesis of archaeosinc, a novel derivative of 7-deazaguanosine specific to archaeal tRNA, proceeds via a pathway involving base replacement of the tRNA polynucleotide chain. J Biol Chem 1997; 272(32):20146-20151.
    • (1997) J Biol Chem , vol.272 , Issue.32 , pp. 20146-20151
    • Watanabe, M.1    Matsuo, M.2    Tanaka, S.3
  • 66
    • 0034192571 scopus 로고    scopus 로고
    • Sequence and structural features of the t-fbld, an original tunnelling building unit
    • Colloc’h N, Poupon A, Momon JP. Sequence and structural features of the T-fbld, an original tunnelling building unit. Proteins 2000; 39(2):142-154.
    • (2000) Proteins , vol.39 , Issue.2 , pp. 142-154
    • Colloc’h, N.1    Poupon, A.2    Momon, J.P.3
  • 67
    • 40449139687 scopus 로고    scopus 로고
    • Purification, crystallization and preliminary crystallographic analysis of a 6-pyruvoyltetrahydropterin synthase homologue from esherichia coli. Acta crystallogr sect f
    • Seo KH, Supangat, Kim HL et al. Purification, crystallization and preliminary crystallographic analysis of a 6-pyruvoyltetrahydropterin synthase homologue from Esherichia coli. Acta Crystallogr Sect F Struct Biol Cryst Commun 2008; 64(Pt 2): 105-107.
    • (2008) Struct Biol Cryst Commun , vol.64 , pp. 105-107
    • Seo, K.H.1    Supangat, K.H.2
  • 68
    • 40449121240 scopus 로고    scopus 로고
    • Crystallization and preliminary x-ray characterization of qued from bacillus subtilis, an enzyme involved in queuosine biosynthesis
    • Cicmil N, Shi L. Crystallization and preliminary X-ray characterization of queD from Bacillus subtilis, an enzyme involved in queuosine biosynthesis. Acta Crystallogr Sect F Struct Biol Cryst Commun 2008; 64(Pt 2):119-122.
    • (2008) Acta Crystallogr Sect F Struct Biol Cryst Commun , vol.64 , pp. 119-122
    • Cicmil, N.1    Shi, L.2
  • 69
    • 33744489086 scopus 로고    scopus 로고
    • Crystallization and preliminary x-ray characterization of the nitrile reducatse quef- a queuosine biosynthesis enzyme
    • Swairjo MA, Reddy RP, Lee B et al. Crystallization and preliminary X-ray characterization of the nitrile reducatse QueF- a queuosine biosynthesis enzyme. Acta Crystallogr D Biol Crystallogr 2005; F61:945-948.
    • (2005) Acta Crystallogr D Biol Crystallogr , vol.F61 , pp. 945-948
    • Swairjo, M.A.1    Reddy, R.P.2    Lee, B.3
  • 70
    • 0028264849 scopus 로고
    • Three-dimensional structure of 6-pyruvoyl tetrahydropterin synthase, an enzyme involved in tetrahydrobiopterin biosynthesis
    • Nar H, Huber R, Heizmann CW et al Three-dimensional structure of 6-pyruvoyl tetrahydropterin synthase, an enzyme involved in tetrahydrobiopterin biosynthesis. EMBO J 1994; 13(6):1255-1262.
    • (1994) EMBO J , vol.13 , Issue.6 , pp. 1255-1262
    • Nar, H.1    Huber, R.2    Heizmann, C.W.3
  • 71
    • 0030663655 scopus 로고    scopus 로고
    • Crystal structure of the protein drug urate oxidase-inhibitor complex at 2.05 a resolution
    • Colloc’h N, el Hajji M, Bachet B et al Crystal structure of the protein drug urate oxidase-inhibitor complex at 2.05 A resolution. Nat Struct Biol 1997; 4(11):947-952.
    • (1997) Nat Struct Biol , vol.4 , Issue.11 , pp. 947-952
    • Colloc’h, N.1    El Hajji, M.2    Bachet, B.3
  • 72
    • 0032066057 scopus 로고    scopus 로고
    • Crystal structure and reaction mechanism of 7,8-dihydroneopterin aldolase from staphylococcus aureus
    • Hennig M, D’Arcy A, Hampele IC et al Crystal structure and reaction mechanism of 7,8-dihydroneopterin aldolase from Staphylococcus aureus. Nat Struct Biol 1998; 5(5):357-362.
    • (1998) Nat Struct Biol , vol.5 , Issue.5 , pp. 357-362
    • Hennig, M.1    D’Arcy, A.2    Hampele, I.C.3
  • 73
    • 0029644734 scopus 로고
    • Atomic structure of gtp cyclohydrolase i
    • Nar H, Huber R, Meining W et al. Atomic structure of GTP cyclohydrolase I. Structure 1995; 3(5):459-466.
    • (1995) Structure , vol.3 , Issue.5 , pp. 459-466
    • Nar, H.1    Huber, R.2    Meining, W.3
  • 74
    • 0037022228 scopus 로고    scopus 로고
    • Crystal structure of the stimulatory complex of gtp cyclohydrolase i and its feedback regulatory protein gfrp
    • Maira N, Okada K, Hatakeyama K et al Crystal structure of the stimulatory complex of GTP cyclohydrolase I and its feedback regulatory protein GFRP. Proc Natl Acad Sci USA 2002; 99(3):1212-1217.
    • (2002) Proc Natl Acad Sci USA , vol.99 , Issue.3 , pp. 1212-1217
    • Maira, N.1    Okada, K.2    Hatakeyama, K.3
  • 75
    • 33845985292 scopus 로고    scopus 로고
    • Discovery of a new prokaryotic type i gtp cyclohydrolasc family
    • El Yacoubi B, Bonnett S, Anderson JN et al Discovery of a new prokaryotic type I GTP cyclohydrolasc family. J Biol Chem 2006; 281(49):37586-37593.
    • (2006) J Biol Chem , vol.281 , Issue.49 , pp. 37586-37593
    • El Yacoubi, B.1    Bonnett, S.2    Anderson, J.N.3
  • 76
    • 0037126007 scopus 로고    scopus 로고
    • Folate synthesis in plants: The first step of the pterin branch is mediated by a unique bimodular gtp cyclohydrolase i
    • Basset G, Quinlivan EP, Ziemak MJ et al. Folate synthesis in plants: the first step of the pterin branch is mediated by a unique bimodular GTP cyclohydrolase I. Proc Natl Acad Sci USA 2002; 99(19):12489-12494.
    • (2002) Proc Natl Acad Sci USA , vol.99 , Issue.19 , pp. 12489-12494
    • Basset, G.1    Quinlivan, E.P.2    Ziemak, M.J.3
  • 77
    • 85075282602 scopus 로고    scopus 로고
    • Zinc-independent folate biosynthesis: Structural biochemical and genetic investigations reveal new metal dependence for gtp cyclohydrolase ib
    • Sankaran B, Bonnett S, Shah K et al Zinc-independent folate biosynthesis: structuraL biochemical and genetic investigations reveal new metal dependence for GTP cyclohydrolase IB. Manuscript Under Review2008.
    • (2008) Manuscript under Review
    • Sankaran, B.1    Bonnett, S.2    Shah, K.3
  • 78
    • 12944300456 scopus 로고    scopus 로고
    • Zinc plays a key role in human and bacterial gtp cyclohydrolase i
    • Auerbach G, Herrmann A, Bracher A et al Zinc plays a key role in human and bacterial GTP cyclohydrolase I. Proc Natl Acad Sci USA 2000; 97(25):13567-13572.
    • (2000) Proc Natl Acad Sci USA , vol.97 , Issue.25 , pp. 13567-13572
    • Auerbach, G.1    Herrmann, A.2    Bracher, A.3
  • 79
    • 35848965494 scopus 로고    scopus 로고
    • Mechanistic studies of bacillus subtilis quef, the nitrile oxidoreductase involved in queuosine biosynthesis
    • Lee BW, Lanen SG, Iwata-Reuyl D. Mechanistic studies of bacillus subtilis QueF, the nitrile oxidoreductase involved in queuosine biosynthesis. Biochemistry 2007; 46(44):12844-12854.
    • (2007) Biochemistry , vol.46 , Issue.44 , pp. 12844-12854
    • Lee, B.W.1    Lanen, S.G.2    Iwata-Reuyl, D.3
  • 80
    • 27744479717 scopus 로고    scopus 로고
    • Mechanism and substrate specificity of trna-guanine transglycosylases (Tgts): Trna-modifying enzymes from the three different kingdoms of life share a common catalytic mechanism
    • Stengl B, Reuter K, Klebe G. Mechanism and substrate specificity of tRNA-guanine transglycosylases (TGTs): tRNA-modifying enzymes from the three different kingdoms of life share a common catalytic mechanism. Chembiochem 2005; 6(11):1926-1939.
    • (2005) Chembiochem , vol.6 , Issue.11 , pp. 1926-1939
    • Stengl, B.1    Reuter, K.2    Klebe, G.3
  • 81
    • 18844429219 scopus 로고    scopus 로고
    • Transglycosylation: A mechanism for rna modification (and editing?)
    • Garcia GA, Kittendotf JD. Transglycosylation: a mechanism for RNA modification (and editing?). Bioorg Chem 2005; 33(3):229-251.
    • (2005) Bioorg Chem , vol.33 , Issue.3 , pp. 229-251
    • Garcia, G.A.1    Kittendotf, J.D.2
  • 82
    • 0003634460 scopus 로고    scopus 로고
    • Structural basis of base exchange by trna-guanine transglycosylases
    • Grosjean H, Benne R, eds., Washington, D.C.: ASM Press
    • Romier C, Ficner R, Suck D. Structural basis of base exchange by tRNA-guanine transglycosylases. In: Grosjean H, Benne R, eds. Modification and Editing of RNA. Washington, D.C.: ASM Press, 1998:169-182.
    • (1998) Modification and Editing of RNA , pp. 169-182
    • Romier, C.1    Ficner, R.2    Suck, D.3
  • 83
    • 0003634460 scopus 로고    scopus 로고
    • Mechanisms of rna-modifying and editing enzymes
    • Grosjean H, Benne R, eds, Washington, D.C.: ASM Press
    • Garcia GA, Goodenough-Lashua M. Mechanisms of RNA-Modifying and Editing Enzymes. In: Grosjean H, Benne R, eds. Modification and Editing of RNA. Washington, D.C.: ASM Press, 1998:135-168.
    • (1998) Modification and Editing of RNA , pp. 135-168
    • Garcia, G.A.1    Goodenough-Lashua, M.2
  • 84
    • 0028989621 scopus 로고
    • Trna-guanine transglycosylase from bovine liver. Purification of the enzyme to homogeneity and biochemical characterization
    • Slany RK, Muller SO. tRNA-guanine transglycosylase from bovine liver. Purification of the enzyme to homogeneity and biochemical characterization. Eur J Biochem 1995; 230(1):221-228.
    • (1995) Eur J Biochem , vol.230 , Issue.1 , pp. 221-228
    • Slany, R.K.1    Muller, S.O.2
  • 85
    • 0020491382 scopus 로고
    • Purification and properties of guanine, qucuinc-trna transglycosylase from wheat germ
    • Walden TLJ, Howes N, Farkas WR. Purification and properties of guanine, qucuinc-tRNA transglycosylase from wheat germ. J Biol Chem 1982; 257(22):13218-13222.
    • (1982) J Biol Chem , vol.257 , Issue.22 , pp. 13218-13222
    • Walden, T.1    Howes, N.2    Farkas, W.R.3
  • 86
    • 0019330581 scopus 로고
    • Transfer ribonucleic acid guanine transglycosylase isolated from rat liver
    • Shindo-Okada N, Okada N, Ohgi T et al Transfer ribonucleic acid guanine transglycosylase isolated from rat liver. Biochemistry 1980; 19(2):395-400.
    • (1980) Biochemistry , vol.19 , Issue.2 , pp. 395-400
    • Shindo-Okada, N.1    Okada, N.2    Ohgi, T.3
  • 87
    • 0033046425 scopus 로고    scopus 로고
    • Novel predicted rna-binding domains associated with the translation machinery
    • Aravind L, Koonin EV. Novel predicted RNA-binding domains associated with the translation machinery. J Mol Evol 1999; 48(3):291-302.
    • (1999) J Mol Evol , vol.48 , Issue.3 , pp. 291-302
    • Aravind, L.1    Koonin, E.V.2
  • 88
    • 34748912322 scopus 로고    scopus 로고
    • The pua domain—a structural and functional overview
    • Pircz-Arcllano I, Gallego J, Cervera J. The PUA domain—a structural and functional overview. FEBS J2007; 274(19):4972-4984.
    • (2007) FEBS J , vol.274 , Issue.19 , pp. 4972-4984
    • Pircz-Arcllano, I.1    Gallego, J.2    Cervera, J.3
  • 89
    • 0036307766 scopus 로고    scopus 로고
    • Crystal structure of archaeosinc trna-guanine transglycosylase
    • Ishitani R, Nureki O, Fukai S et al. Crystal structure of archaeosinc tRNA-guanine transglycosylase. J Mol Biol 2002; 318(3):665-677.
    • (2002) J Mol Biol , vol.318 , Issue.3 , pp. 665-677
    • Ishitani, R.1    Nureki, O.2    Fukai, S.3
  • 90
    • 0038613099 scopus 로고    scopus 로고
    • Alternative tertiary structure of trna for recognition by a posttranscriptional modification enzyme
    • Ishitani R, Nureki O, Nameki N et al Alternative tertiary structure of tRNA for recognition by a posttranscriptional modification enzyme. Cell 2003; 113(3):383-394.
    • (2003) Cell , vol.113 , Issue.3 , pp. 383-394
    • Ishitani, R.1    Nureki, O.2    Nameki, N.3
  • 91
    • 33646368150 scopus 로고    scopus 로고
    • The rna-binding pua domain of archaeal trna-guanine transglycosylase is not required for archaeosinc formation
    • Sabina J, Soli D. The RNA-binding PUA domain of archaeal tRNA-guanine transglycosylase is not required for archaeosinc formation. J Biol Chcm 2006; 281(11):6993-7001.
    • (2006) J Biol Chcm , vol.281 , Issue.11 , pp. 6993-7001
    • Sabina, J.1    Soli, D.2
  • 92
    • 0029116609 scopus 로고
    • Trna-guanine transglycosylase from escherichia coli. Minimal trna structure and sequence requirements for recognition
    • Cumow AW, Garcia GA. tRNA-guanine transglycosylase from Escherichia coli. Minimal tRNA structure and sequence requirements for recognition. J Biol Chem 1995; 270(29):17264-17267.
    • (1995) J Biol Chem , vol.270 , Issue.29 , pp. 17264-17267
    • Cumow, A.W.1    Garcia, G.A.2
  • 93
    • 0028595685 scopus 로고
    • A ugu sequence in the anticodon loop is a minimum requirement for recognition by e. Coli trna-guanine transglycosylase
    • Nakanishi S, Ueda T, Hori H et al A UGU sequence in the anticodon loop is a minimum requirement for recognition by E. coli tRNA-guanine transglycosylase. J Biol Chem 1994; 269(51):32221-32225.
    • (1994) J Biol Chem , vol.269 , Issue.51 , pp. 32221-32225
    • Nakanishi, S.1    Ueda, T.2    Hori, H.3
  • 94
    • 0028641310 scopus 로고
    • Trna-guanine transglycosylase from escherichia coli: Recognition of dimeric, unmodified trna(tyr)
    • Cumow AW, Garcia GA. tRNA-guanine transglycosylase from Escherichia coli: recognition of dimeric, unmodified tRNA(Tyr). Biochimie 1994; 76(12):1183-1191.
    • (1994) Biochimie , vol.76 , Issue.12 , pp. 1183-1191
    • Cumow, A.W.1    Garcia, G.A.2
  • 95
    • 0036510739 scopus 로고    scopus 로고
    • The escherichia coli trna-guanine transglycosylase can recognize and modify dna
    • Nonekowski ST, Kung FL, Garcia GA. The Escherichia coli tRNA-guanine transglycosylase can recognize and modify DNA. J Biol Chem 2002; 277(9):7178-7182.
    • (2002) J Biol Chem , vol.277 , Issue.9 , pp. 7178-7182
    • Nonekowski, S.T.1    Kung, F.L.2    Garcia, G.A.3
  • 96
    • 34547886845 scopus 로고    scopus 로고
    • Site-specific modification of shigella flexneri virf mrna by trna-guanine ttansglycosylase in vitro
    • Hurt JK, Olgen S, Garcia GA. Site-specific modification of shigella flexneri virF mRNA by tRNA-guanine ttansglycosylase in vitro. Nucleic Acids Res 2007; 35(14):4905-4913.
    • (2007) Nucleic Acids Res , vol.35 , Issue.14 , pp. 4905-4913
    • Hurt, J.K.1    Olgen, S.2    Garcia, G.A.3
  • 97
    • 20444478991 scopus 로고    scopus 로고
    • Riboswitches as versatile gene control elements
    • Tucker BJ, Breaker RR. Riboswitches as versatile gene control elements. Curr Opin Struct Biol 2005; 15(3):342-348.
    • (2005) Curr Opin Struct Biol , vol.15 , Issue.3 , pp. 342-348
    • Tucker, B.J.1    Breaker, R.R.2
  • 98
    • 0033963529 scopus 로고    scopus 로고
    • Glycosidase mechanisms: Anatomy of a finely tuned catalyst
    • Zcchel DL, Withers SG. Glycosidase mechanisms: anatomy of a finely tuned catalyst. Acc Chem Res 2000; 33(1):11-18.
    • (2000) Acc Chem Res , vol.33 , Issue.1 , pp. 11-18
    • Zcchel, D.L.1    Withers, S.G.2
  • 99
    • 0141596159 scopus 로고    scopus 로고
    • Chemical trapping and crystal structure of a catalytic trna guanine transglycosylase covalent intermediate
    • Xie W, Liu X, Huang RH. Chemical trapping and crystal structure of a catalytic tRNA guanine transglycosylase covalent intermediate. Nat Struct Biol 2003; 10(10):781-788.
    • (2003) Nat Struct Biol , vol.10 , Issue.10 , pp. 781-788
    • Xie, W.1    Liu, X.2    Huang, R.H.3
  • 100
    • 2342631335 scopus 로고    scopus 로고
    • S-adenosylmethionine: Nothing goes to waste
    • Fontecave M, Atta M, Mulliez E. S-adenosylmethionine: nothing goes to waste. Trends Biochem Sci 2004; 29(5):243-249.
    • (2004) Trends Biochem Sci , vol.29 , Issue.5 , pp. 243-249
    • Fontecave, M.1    Atta, M.2    Mulliez, E.3
  • 101
    • 0027295625 scopus 로고
    • A new function of s-adenosylmechionine: The ribosyl moiety of adomet is the precursor of the cyclopentenediol moiety of the trna wobble base queuine
    • Slany RK, Bosl M, Crain PF et al A new function of S-adenosylmechionine: The ribosyl moiety of AdoMet is the precursor of the cyclopentenediol moiety of the tRNA wobble base queuine. Biochemistry 1993; 32:7811-7817.
    • (1993) Biochemistry , vol.32 , pp. 7811-7817
    • Slany, R.K.1    Bosl, M.2    Crain, P.F.3
  • 103
    • 0034603906 scopus 로고    scopus 로고
    • Mechanistic studies of the trna-modifying enzyme quea: A chemical imperative for the use of adomet as a “ribosyl” donor
    • Kinzie SD, Them B, frvata-Reuyl D. Mechanistic studies of the tRNA-modifying enzyme QueA: a chemical imperative for the use of AdoMet as a “ribosyl” donor. Org Lett 2000; 2(9):1307-1310.
    • (2000) Org Lett , vol.2 , Issue.9 , pp. 1307-1310
    • Kinzie, S.D.1    Them, B.2    Frvata-Reuyl, D.3
  • 104
    • 0037544102 scopus 로고    scopus 로고
    • Kinetic mechanism of the trna-modifying enzyme s-adenosylmethionine: trna ribosyltransferase-isomerase (quea)
    • Van I alien SG, Iwata-Reuyl D. Kinetic mechanism of the tRNA-modifying enzyme S-adenosylmethionine: tRNA ribosyltransferase-isomerase (QueA). Biochemistry 2003; 42(18):5312-5320.
    • (2003) Biochemistry , vol.42 , Issue.18 , pp. 5312-5320
    • Van I Alien, S.G.1    Iwata-Reuyl, D.2
  • 105
    • 33750702867 scopus 로고    scopus 로고
    • Crystal structure of bacillus subtilis s-adcnosylmethionine: Trna ribosyltransferase-isomerase
    • Grimm C, Ficner R, Sgraja T et al Crystal structure of Bacillus subtilis S-adcnosylmethionine:tRNA ribosyltransferase-isomerase. Biochem Biophys Res Commun 2006; 351(3):695-701.
    • (2006) Biochem Biophys Res Commun , vol.351 , Issue.3 , pp. 695-701
    • Grimm, C.1    Ficner, R.2    Sgraja, T.3
  • 106
    • 21044441789 scopus 로고    scopus 로고
    • Crystal structure of s-adcnosylmethionine: Trna ribosyltransferase-isomerase (quea) from thermotoga maritima at 2.0 a resolution reveals a new fold
    • Mathews L Schwarzenbacher R, McMullan D et al. Crystal structure of S-adcnosylmethionine:tRNA ribosyltransferase-isomerase (QueA) from Thermotoga maritima at 2.0 A resolution reveals a new fold. Proteins 2005; 59(4):869-874.
    • (2005) Proteins , vol.59 , Issue.4 , pp. 869-874
    • Mathews L Schwarzenbacher, R.1    McMullan, D.2
  • 107
    • 10744231159 scopus 로고    scopus 로고
    • The escherichia coli yadb gene product reveals a novel aminoacyl-trna synthetase like activity
    • Campanacci V, Dubois DY, Becker HD et al The Escherichia coli YadB gene product reveals a novel aminoacyl-tRNA synthetase like activity. J Mol Biol 2004; 337(2):273-283.
    • (2004) J Mol Biol , vol.337 , Issue.2 , pp. 273-283
    • Campanacci, V.1    Dubois, D.Y.2    Becker, H.D.3
  • 108
    • 0024415902 scopus 로고
    • Codon recognition patterns as deduced from sequences of the complete set of transfer rna species in mycoplasma capricolum. Resemblance to mitochondria
    • Andachi Y, Yamao F, Muto A et al Codon recognition patterns as deduced from sequences of the complete set of transfer RNA species in Mycoplasma capricolum. Resemblance to mitochondria. J Mol Biol 1989; 209(1):37-54.
    • (1989) J Mol Biol , vol.209 , Issue.1 , pp. 37-54
    • Andachi, Y.1    Yamao, F.2    Muto, A.3
  • 109
    • 0021362106 scopus 로고
    • Queuine salvage in mammalian cells. Evidence that queuine is generated from queuosine 5'-phosphate
    • Gunduz U, Katze JR. Queuine salvage in mammalian cells. Evidence that queuine is generated from queuosine 5'-phosphate. J Biol Chem 1984; 259(2):1110-1113.
    • (1984) J Biol Chem , vol.259 , Issue.2 , pp. 1110-1113
    • Gunduz, U.1    Katze, J.R.2
  • 110
    • 0030832831 scopus 로고    scopus 로고
    • Slight sequence variations of a common fold explain the substrate specificities of trna-guanine transglycosylascs from the three kingdoms
    • Romier C, Meyer JE, Suck D. Slight sequence variations of a common fold explain the substrate specificities of tRNA-guanine transglycosylascs from the three kingdoms. FEBS Lett 1997; 416(1):93-98.
    • (1997) FEBS Lett , vol.416 , Issue.1 , pp. 93-98
    • Romier, C.1    Meyer, J.E.2    Suck, D.3
  • 111
    • 0036716306 scopus 로고    scopus 로고
    • Purine regulon of gamma-proteobacteria: A detailed description
    • Ravcheev DA, Gel’fand MS, Mironov AA et al. Purine regulon of gamma-proteobacteria: a detailed description. Gcnetika 2002; 38(9):1203-1214.
    • (2002) Gcnetika , vol.38 , Issue.9 , pp. 1203-1214
    • Ravcheev, D.A.1    Gel’fand, M.S.2    Mironov, A.A.3
  • 112
    • 2342511433 scopus 로고    scopus 로고
    • New rna motifs suggest an expanded scope for riboswitches in bacterial genetic control
    • Bamck JE, Corbino KA, Winkler WC et al. New RNA motifs suggest an expanded scope for riboswitches in bacterial genetic control. Proc Natl Acad Sci USA 2004; 101(17):6421-6426.
    • (2004) Proc Natl Acad Sci USA , vol.101 , Issue.17 , pp. 6421-6426
    • Bamck, J.E.1    Corbino, K.A.2    Winkler, W.C.3
  • 113
    • 41649108068 scopus 로고    scopus 로고
    • Confirmation of a second natural preql aptamer class in strep-tococcaceae bacteria
    • Meyer MM, Roth A, Chervin SM et al. Confirmation of a second natural preQl aptamer class in Strep-tococcaceae bacteria. RNA 2008; 14(4):685-695.
    • (2008) RNA , vol.14 , Issue.4 , pp. 685-695
    • Meyer, M.M.1    Roth, A.2    Chervin, S.M.3
  • 114
    • 34247181095 scopus 로고    scopus 로고
    • A riboswitch selective for the queuosine precursor preql contains an unusually small aptamer domain
    • Roth A, Winkler WC, Regulski EE et al A riboswitch selective for the queuosine precursor preQl contains an unusually small aptamer domain. Nat Struct Mol Biol 2007; 14(4):308-317
    • (2007) Nat Struct Mol Biol , vol.14 , Issue.4 , pp. 308-317
    • Roth, A.1    Winkler, W.C.2    Regulski, E.E.3


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.