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Volumn 2, Issue 1-2, 2008, Pages 25-45

Enzymes used in molecular biology: A useful guide

Author keywords

Enzymes; Molecular biology; Molecular cloning

Indexed keywords

ALKALINE PHOSPHATASE; BAL 31 NUCLEASE; CEREUS RIBONUCLEASE; DAM METHYLTRANSFERASE; DCM METHYLTRANSFERASE; DEOXYRIBONUCLEASE; DEOXYRIBONUCLEASE I; DNA DIRECTED DNA POLYMERASE; DNA DIRECTED DNA POLYMERASE BETA; DNA NUCLEOTIDYLEXOTRANSFERASE; DNA POLYMERASE; DNA TOPOISOMERASE; ENZYME; EXODEOXYRIBONUCLEASE III; EXODEOXYRIBONUCLEASE VII; INORGANIC PYROPHOSPHATASE; LIGASE; METHYLTRANSFERASE; MUNG BEAN NUCLEASE; NUCLEASE; NUCLEASE S1; PANCREATIC RIBONUCLEASE; PHOSPHATASE; POLYDEOXYRIBONUCLEOTIDE SYNTHASE; RIBONUCLEASE; RNA DIRECTED DNA POLYMERASE; RNA LIGASE; TELOMERASE; TOBACCO ACID PYROPHOSPHATASE; UNCLASSIFIED DRUG;

EID: 54949128606     PISSN: 18739601     EISSN: 1873961X     Source Type: Journal    
DOI: 10.1007/s12079-008-0026-2     Document Type: Review
Times cited : (73)

References (165)
  • 1
    • 0038473989 scopus 로고    scopus 로고
    • OB-fold: Growing bigger with functional consistency
    • doi: 10.2174/1389203033487207
    • Agrawal V, Kishan KV (2003) OB-fold: Growing bigger with functional consistency. Curr Protein Pept Sci 4:195-206 doi: 10.2174/ 1389203033487207
    • (2003) Curr Protein Pept Sci , vol.4 , pp. 195-206
    • Agrawal, V.1    Kishan, K.V.2
  • 2
    • 0014020901 scopus 로고
    • A nuclease specific for heat-denatured DNA in isolated from a product of Aspergillus oryzae
    • Ando T (1966) A nuclease specific for heat-denatured DNA in isolated from a product of Aspergillus oryzae. Biochim Biophys Acta 114:158-168
    • (1966) Biochim Biophys Acta , vol.114 , pp. 158-168
    • Ando, T.1
  • 3
    • 54949089311 scopus 로고
    • The ribonucleases, occurrence, structure and properties
    • In: Boyer PD, Lardy H, Myrback K (eds) 2nd edn. Academic, New-York
    • Anfinsen CB, White FHJ (1961) The ribonucleases, occurrence, structure and properties. In: Boyer PD, Lardy H, Myrback K (eds) The enzymes. 2nd edn. Academic, New-York, pp 95-122
    • (1961) The Enzymes , pp. 95-122
    • Anfinsen, C.B.1    White, F.H.J.2
  • 4
    • 26944443861 scopus 로고    scopus 로고
    • Identification and characterization of small RNAs involved in RNA silencing
    • doi: 10.1016/j.febslet.2005.08.009
    • Aravin A, Tuschl T (2005) Identification and characterization of small RNAs involved in RNA silencing. FEBS Lett 579:5830-5840 doi: 10.1016/ j.febslet.2005.08.009
    • (2005) FEBS Lett , vol.579 , pp. 5830-5840
    • Aravin, A.1    Tuschl, T.2
  • 5
    • 0036913982 scopus 로고    scopus 로고
    • OB-fold domains: A snapshot of the evolution of sequence, structure and function
    • doi: 10.1016/S0959-440X(02)00392-5
    • Arcus V (2002) OB-fold domains: A snapshot of the evolution of sequence, structure and function. Curr Opin Struct Biol 12:794-801 doi: 10.1016/ S0959-440X(02)00392-5
    • (2002) Curr Opin Struct Biol , vol.12 , pp. 794-801
    • Arcus, V.1
  • 6
    • 33845443896 scopus 로고    scopus 로고
    • Escherichia coli DNA polymerase III epsilon subunit increases Moloney murine leukemia virus reverse transcriptase fidelity and accuracy of RT-PCR procedures
    • doi: 10.1016/j.ab.2006.10.009
    • Arezi B, Hogrefe HH (2007) Escherichia coli DNA polymerase III epsilon subunit increases Moloney murine leukemia virus reverse transcriptase fidelity and accuracy of RT-PCR procedures. Anal Biochem 360:84-91 doi: 10.1016/j.ab.2006.10.009
    • (2007) Anal Biochem , vol.360 , pp. 84-91
    • Arezi, B.1    Hogrefe, H.H.2
  • 7
    • 22144473328 scopus 로고    scopus 로고
    • Etoposide, topoisomerase II and cancer
    • doi: 10.2174/1568011054222364
    • Baldwin EL, Osheroff N (2005) Etoposide, topoisomerase II and cancer. Curr Med Chem Anticancer Agents 5:363-372 doi: 10.2174/1568011054222364
    • (2005) Curr Med Chem Anticancer Agents , vol.5 , pp. 363-372
    • Baldwin, E.L.1    Osheroff, N.2
  • 8
    • 0014964654 scopus 로고
    • RNA-dependent DNA polymerase in virions of RNA tumour viruses
    • doi: 10.1038/2261209a0
    • Baltimore D (1970) RNA-dependent DNA polymerase in virions of RNA tumour viruses. Nature 226:1209-1211 doi: 10.1038/2261209a0
    • (1970) Nature , vol.226 , pp. 1209-1211
    • Baltimore, D.1
  • 9
    • 0020649911 scopus 로고
    • Avian myeloblastosis virus: A model for the generation of viral oncogenes from potentially oncogenic cellular genetic elements
    • Baluda MA, Perbal B, Rushlow KE, Papas TS (1983) Avian myeloblastosis virus: A model for the generation of viral oncogenes from potentially oncogenic cellular genetic elements. Folia Biol (Praha) 29:18-34
    • (1983) Folia Biol (Praha) , vol.29 , pp. 18-34
    • Baluda, M.A.1    Perbal, B.2    Rushlow, K.E.3    Papas, T.S.4
  • 10
    • 0015738909 scopus 로고
    • Cleavage of circular, superhelical simian virus 40 DNA to a linear duplex by S1 nuclease
    • Beard P, Morrow JF, Berg P (1973) Cleavage of circular, superhelical simian virus 40 DNA to a linear duplex by S1 nuclease. J Virol 12:1303-1313
    • (1973) J Virol , vol.12 , pp. 1303-1313
    • Beard, P.1    Morrow, J.F.2    Berg, P.3
  • 11
    • 0019568339 scopus 로고
    • DNA breakage and closure by rat liver type 1 topoisomerase: Separation of the half-reactions by using a single-stranded DNA substrate
    • doi: 10.1073/pnas.78.5.2883
    • Been MD, Champoux JJ (1981) DNA breakage and closure by rat liver type 1 topoisomerase: Separation of the half-reactions by using a single-stranded DNA substrate. Proc Natl Acad Sci USA 78:2883-2887 doi: 10.1073/pnas.78.5.2883
    • (1981) Proc Natl Acad Sci USA , vol.78 , pp. 2883-2887
    • Been, M.D.1    Champoux, J.J.2
  • 12
    • 0021099452 scopus 로고
    • Reverse transcriptase and its associated ribonuclease H: Interplay of two enzyme activities controls the yield of single-stranded complementary deoxyribonucleic acid
    • doi: 10.1021/bi00279a010
    • Berger SL, Wallace DM, Puskas RS, Eschenfeldt WH (1983) Reverse transcriptase and its associated ribonuclease H: Interplay of two enzyme activities controls the yield of single-stranded complementary deoxyribonucleic acid. Biochemistry 22:2365-2372 doi: 10.1021/bi00279a010
    • (1983) Biochemistry , vol.22 , pp. 2365-2372
    • Berger, S.L.1    Wallace, D.M.2    Puskas, R.S.3    Eschenfeldt, W.H.4
  • 13
    • 0018848177 scopus 로고
    • Polynucleotide kinase exchange as an assay for class II restriction endonucleases
    • doi: 10.1016/S0076-6879(80)65007-1
    • Berkner KL, Folk WR (1980) Polynucleotide kinase exchange as an assay for class II restriction endonucleases. Methods Enzymol 65:28-36 doi: 10.1016/S0076-6879(80)65007-1
    • (1980) Methods Enzymol , vol.65 , pp. 28-36
    • Berkner, K.L.1    Folk, W.R.2
  • 14
    • 0015851235 scopus 로고
    • Isolation and characterization of an endonuclease from Escherichia coli specific for ribonucleic acid in ribonucleic acid-deoxyribonucleic acid hybrid structures
    • Berkower I, Leis J, Hurwitz J (1973) Isolation and characterization of an endonuclease from Escherichia coli specific for ribonucleic acid in ribonucleic acid-deoxyribonucleic acid hybrid structures. J Biol Chem 248:5914-5921
    • (1973) J Biol Chem , vol.248 , pp. 5914-5921
    • Berkower, I.1    Leis, J.2    Hurwitz, J.3
  • 15
    • 0033013881 scopus 로고    scopus 로고
    • Nucleotide sequence, heterologous expression and novel purification of DNA ligase from Bacillus stearothermophilus(1)
    • Brannigan JA, Ashford SR, Doherty AJ, Timson DJ, Wigley DB (1999) Nucleotide sequence, heterologous expression and novel purification of DNA ligase from Bacillus stearothermophilus(1). Biochim Biophys Acta 1432:413-418
    • (1999) Biochim Biophys Acta , vol.1432 , pp. 413-418
    • Brannigan, J.A.1    Ashford, S.R.2    Doherty, A.J.3    Timson, D.J.4    Wigley, D.B.5
  • 16
    • 0014501198 scopus 로고
    • Thermus aquaticus gen. n. and sp. n., a nonsporulating extreme thermophile
    • doi: 10.1002/path.1710980409
    • Brock TD, Freeze H (1969) Thermus aquaticus gen. n. and sp. n., a nonsporulating extreme thermophile. J Bacteriol 98:289-297 doi: 10.1002/ path.1710980409
    • (1969) J Bacteriol , vol.98 , pp. 289-297
    • Brock, T.D.1    Freeze, H.2
  • 17
    • 0001403311 scopus 로고
    • A topoisomerase from Escherichia coli related to DNA gyrase
    • doi: 10.1073/pnas.76.12.6110
    • Brown PO, Peebles CL, Cozzarelli NR (1979) A topoisomerase from Escherichia coli related to DNA gyrase. Proc Natl Acad Sci USA 76:6110-6114 doi: 10.1073/pnas.76.12.6110
    • (1979) Proc Natl Acad Sci USA , vol.76 , pp. 6110-6114
    • Brown, P.O.1    Peebles, C.L.2    Cozzarelli, N.R.3
  • 18
    • 0020326042 scopus 로고
    • Bacteriophage SP6-specific RNA polymerase. I. Isolation and characterization of the enzyme
    • Butler ET, Chamberlin MJ (1982) Bacteriophage SP6-specific RNA polymerase. I. Isolation and characterization of the enzyme. J Biol Chem 257:5772-5778
    • (1982) J Biol Chem , vol.257 , pp. 5772-5778
    • Butler, E.T.1    Chamberlin, M.J.2
  • 19
    • 0017757667 scopus 로고
    • 3′-Phosphatase activity in T4 polynucleotide kinase
    • doi: 10.1021/bi00642a027
    • Cameron V, Uhlenbeck OC (1977) 3′-Phosphatase activity in T4 polynucleotide kinase. Biochemistry 16:5120-5126 doi: 10.1021/bi00642a027
    • (1977) Biochemistry , vol.16 , pp. 5120-5126
    • Cameron, V.1    Uhlenbeck, O.C.2
  • 20
    • 0017883477 scopus 로고
    • Polynucleotide kinase from a T4 mutant which lacks the 3′ phosphatase activity
    • doi: 10.1093/nar/5.3.825
    • Cameron V, Soltis D, Uhlenbeck OC (1978) Polynucleotide kinase from a T4 mutant which lacks the 3′ phosphatase activity. Nucleic Acids Res 5:825-833 doi: 10.1093/nar/5.3.825
    • (1978) Nucleic Acids Res , vol.5 , pp. 825-833
    • Cameron, V.1    Soltis, D.2    Uhlenbeck, O.C.3
  • 21
    • 0019332501 scopus 로고
    • The effect of divalent cations on the mode of action of DNase I. The initial reaction products produced from covalently closed circular DNA
    • Campbell VW, Jackson DA (1980) The effect of divalent cations on the mode of action of DNase I. The initial reaction products produced from covalently closed circular DNA. J Biol Chem 255:3726-3735
    • (1980) J Biol Chem , vol.255 , pp. 3726-3735
    • Campbell, V.W.1    Jackson, D.A.2
  • 22
    • 0018815075 scopus 로고
    • 5′-32P labeling of RNA and DNA restriction fragments
    • doi: 10.1016/S0076-6879(80)65012-5
    • Chaconas G, van de Sande JH (1980) 5′-32P labeling of RNA and DNA restriction fragments. Methods Enzymol 65:75-85 doi: 10.1016/ S0076-6879(80)65012-5
    • (1980) Methods Enzymol , vol.65 , pp. 75-85
    • Chaconas, G.1    van de Sande, J.H.2
  • 23
    • 0014953125 scopus 로고
    • New RNA polymerase from Escherichia coli infected with bacteriophage T7
    • doi: 10.1038/228227a0
    • Chamberlin M, McGrath J, Waskell L (1970) New RNA polymerase from Escherichia coli infected with bacteriophage T7. Nature 228:227-231 doi: 10.1038/228227a0
    • (1970) Nature , vol.228 , pp. 227-231
    • Chamberlin, M.1    McGrath, J.2    Waskell, L.3
  • 24
    • 0017832205 scopus 로고
    • Proteins that affect DNA conformation
    • doi: 10.1146/annurev.bi.47.070178.002313
    • Champoux JJ (1978) Proteins that affect DNA conformation. Annu Rev Biochem 47:449-479 doi: 10.1146/annurev.bi.47.070178.002313
    • (1978) Annu Rev Biochem , vol.47 , pp. 449-479
    • Champoux, J.J.1
  • 25
    • 0034923502 scopus 로고    scopus 로고
    • DNA topoisomerases: Structure, function, and mechanism
    • doi: 10.1146/annurev.biochem.70.1.369
    • Champoux JJ (2001) DNA topoisomerases: Structure, function, and mechanism. Annu Rev Biochem 70:369-413 doi: 10.1146/ annurev.biochem.70.1.369
    • (2001) Annu Rev Biochem , vol.70 , pp. 369-413
    • Champoux, J.J.1
  • 26
    • 0016166828 scopus 로고
    • Exonuclease VII of Escherichia coli. Mechanism of action
    • Chase JW, Richardson CC (1974a) Exonuclease VII of Escherichia coli. Mechanism of action. J Biol Chem 249:4553-4561
    • (1974) J Biol Chem , vol.249 , pp. 4553-4561
    • Chase, J.W.1    Richardson, C.C.2
  • 27
    • 0016258294 scopus 로고
    • Exonuclease VII of Escherichia coli. Purification and properties
    • Chase JW, Richardson CC (1974b) Exonuclease VII of Escherichia coli. Purification and properties. J Biol Chem 249:4545-4552
    • (1974) J Biol Chem , vol.249 , pp. 4545-4552
    • Chase, J.W.1    Richardson, C.C.2
  • 28
    • 0017108645 scopus 로고
    • Deoxyribonucleic acid polymerase from the extreme thermophile Thermus aquaticus
    • Chien A, Edgar DB, Trela JM (1976) Deoxyribonucleic acid polymerase from the extreme thermophile Thermus aquaticus. J Bacteriol 127:1550-1557
    • (1976) J Bacteriol , vol.127 , pp. 1550-1557
    • Chien, A.1    Edgar, D.B.2    Trela, J.M.3
  • 29
    • 70449209123 scopus 로고
    • On protein synthesis
    • Crick FH (1958) On protein synthesis. Symp Soc Exp Biol 12:138-163
    • (1958) Symp Soc Exp Biol , vol.12 , pp. 138-163
    • Crick, F.H.1
  • 30
    • 0028342951 scopus 로고
    • Repair of oxidative damage to DNA: Enzymology and biology
    • doi: 10.1146/annurev.bi.63.070194.004411
    • Demple B, Harrison L (1994) Repair of oxidative damage to DNA: enzymology and biology. Annu Rev Biochem 63:915-948 doi: 10.1146/ annurev.bi.63.070194.004411
    • (1994) Annu Rev Biochem , vol.63 , pp. 915-948
    • Demple, B.1    Harrison, L.2
  • 31
    • 0016616136 scopus 로고
    • Characterization of a new class of deletions of the D region of the bacteriophage T4 genome
    • doi: 10.1016/0042-6822(75)90086-0
    • Depew RE, Snopek TJ, Cozzarelli NR (1975) Characterization of a new class of deletions of the D region of the bacteriophage T4 genome. Virology 64:144-145 doi: 10.1016/0042-6822(75)90086-0
    • (1975) Virology , vol.64 , pp. 144-145
    • Depew, R.E.1    Snopek, T.J.2    Cozzarelli, N.R.3
  • 32
    • 0033534370 scopus 로고    scopus 로고
    • Functional domains of an ATP-dependent DNA ligase
    • doi: 10.1006/jmbi.1998.2301
    • Doherty AJ, Wigley DB (1999) Functional domains of an ATP-dependent DNA ligase. J Mol Biol 285:63-71 doi: 10.1006/jmbi.1998.2301
    • (1999) J Mol Biol , vol.285 , pp. 63-71
    • Doherty, A.J.1    Wigley, D.B.2
  • 33
    • 0019332777 scopus 로고
    • Phy M: An RNase activity specific for U and A residues useful in RNA sequence analysis
    • doi: 10.1093/nar/8.14.3133
    • Donis-Keller H (1980) Phy M: An RNase activity specific for U and A residues useful in RNA sequence analysis. Nucleic Acids Res 8:3133-3142 doi: 10.1093/nar/8.14.3133
    • (1980) Nucleic Acids Res , vol.8 , pp. 3133-3142
    • Donis-Keller, H.1
  • 34
    • 0031929789 scopus 로고    scopus 로고
    • The pnk/pnl gene (ORF 86) of Autographa californica nucleopolyhedrovirus is a non-essential, immediate early gene
    • Durantel D, Croizier L, Ayres MD, Croizier G, Possee RD, Lopez-Ferber M (1998) The pnk/pnl gene (ORF 86) of Autographa californica nucleopolyhedrovirus is a non-essential, immediate early gene. J Gen Virol 79(Pt 3):629-637
    • (1998) J Gen Virol , vol.79 , Issue.PART 3 , pp. 629-637
    • Durantel, D.1    Croizier, L.2    Ayres, M.D.3    Croizier, G.4    Possee, R.D.5    Lopez-Ferber, M.6
  • 35
    • 0019884371 scopus 로고
    • 5-Methylcytosine in eukaryotic DNA
    • doi: 10.1126/science.6262918
    • Ehrlich M, Wang RY (1981) 5-Methylcytosine in eukaryotic DNA. Science 212:1350-1357 doi: 10.1126/science.6262918
    • (1981) Science , vol.212 , pp. 1350-1357
    • Ehrlich, M.1    Wang, R.Y.2
  • 36
    • 0015239517 scopus 로고
    • Analysis of nucleotide sequences at 3′ termini of duplex deoxyribonucleic acid with the use of the T4 deoxyribonucleic acid polymerase
    • Englund PT (1971) Analysis of nucleotide sequences at 3′ termini of duplex deoxyribonucleic acid with the use of the T4 deoxyribonucleic acid polymerase. J Biol Chem 246:3269-3276
    • (1971) J Biol Chem , vol.246 , pp. 3269-3276
    • Englund, P.T.1
  • 37
    • 0024505998 scopus 로고
    • Eukaryotic transposable elements and genome evolution
    • doi: 10.1016/0168-9525(89)90039-5
    • Finnegan DJ (1989) Eukaryotic transposable elements and genome evolution. Trends Genet 5:103-107 doi: 10.1016/0168-9525(89)90039-5
    • (1989) Trends Genet , vol.5 , pp. 103-107
    • Finnegan, D.J.1
  • 38
    • 0043066735 scopus 로고    scopus 로고
    • DNA replication: A complex matter
    • doi: 10.1038/sj.embor.embor886
    • Frouin I, Montecucco A, Spadari S, Maga G (2003) DNA replication: A complex matter. EMBO Rep 4:666-670 doi: 10.1038/sj.embor.embor886
    • (2003) EMBO Rep , vol.4 , pp. 666-670
    • Frouin, I.1    Montecucco, A.2    Spadari, S.3    Maga, G.4
  • 39
    • 0018199224 scopus 로고
    • DNAse footprinting: A simple method for the detection of protein-DNA binding specificity
    • doi: 10.1093/nar/5.9.3157
    • Galas DJ, Schmitz A (1978) DNAse footprinting: A simple method for the detection of protein-DNA binding specificity. Nucleic Acids Res 5:3157-3170 doi: 10.1093/nar/5.9.3157
    • (1978) Nucleic Acids Res , vol.5 , pp. 3157-3170
    • Galas, D.J.1    Schmitz, A.2
  • 40
    • 18044384092 scopus 로고    scopus 로고
    • DNA polymerases that propagate the eukaryotic DNA replication fork
    • doi: 10.1080/10409230590935433
    • Garg P, Burgers PM (2005) DNA polymerases that propagate the eukaryotic DNA replication fork. Crit Rev Biochem Mol Biol 40:115-128 doi: 10.1080/ 10409230590935433
    • (2005) Crit Rev Biochem Mol Biol , vol.40 , pp. 115-128
    • Garg, P.1    Burgers, P.M.2
  • 41
    • 0026648674 scopus 로고
    • Identification of programmed cell death in situ via specific labeling of nuclear DNA fragmentation
    • doi: 10.1083/jcb.119.3.493
    • Gavrieli Y, Sherman Y, Ben-Sasson SA (1992) Identification of programmed cell death in situ via specific labeling of nuclear DNA fragmentation. J Cell Biol 119:493-501 doi: 10.1083/jcb.119.3.493
    • (1992) J Cell Biol , vol.119 , pp. 493-501
    • Gavrieli, Y.1    Sherman, Y.2    Ben-Sasson, S.A.3
  • 42
    • 0018800323 scopus 로고
    • Recognition sequence of the dam methylase of Escherichia coli K12 and mode of cleavage of Dpn I endonuclease
    • Geier GE, Modrich P (1979) Recognition sequence of the dam methylase of Escherichia coli K12 and mode of cleavage of Dpn I endonuclease. J Biol Chem 254:1408-1413
    • (1979) J Biol Chem , vol.254 , pp. 1408-1413
    • Geier, G.E.1    Modrich, P.2
  • 43
    • 0019376425 scopus 로고
    • DNA topoisomerases
    • doi: 10.1146/annurev.bi.50.070181.004311
    • Gellert M (1981) DNA topoisomerases. Annu Rev Biochem 50:879-910 doi: 10.1146/annurev.bi.50.070181.004311
    • (1981) Annu Rev Biochem , vol.50 , pp. 879-910
    • Gellert, M.1
  • 44
    • 0016152013 scopus 로고
    • Characterization of the single-strand-specific nuclease S1 activity on double-stranded supercoiled polyoma DNA
    • doi: 10.1111/j.1432-1033.1974.tb03446.x
    • Germond JE, Vogt VM, Hirt B (1974) Characterization of the single-strand-specific nuclease S1 activity on double-stranded supercoiled polyoma DNA. Eur J Biochem 43:591-600 doi: 10.1111/ j.1432-1033.1974.tb03446.x
    • (1974) Eur J Biochem , vol.43 , pp. 591-600
    • Germond, J.E.1    Vogt, V.M.2    Hirt, B.3
  • 45
    • 0016822851 scopus 로고
    • Specific hydrolysis of the cohesive ends of bacteriophage lambda DNA by three single strand-specific nucleases
    • Ghangas GS, Wu R (1975) Specific hydrolysis of the cohesive ends of bacteriophage lambda DNA by three single strand-specific nucleases. J Biol Chem 250:4601-4606
    • (1975) J Biol Chem , vol.250 , pp. 4601-4606
    • Ghangas, G.S.1    Wu, R.2
  • 46
    • 0015931813 scopus 로고
    • Action of the single-stranded DNA specific nuclease S1 on double-stranded DNA
    • Godson GN (1973) Action of the single-stranded DNA specific nuclease S1 on double-stranded DNA. Biochim Biophys Acta 308:59-67
    • (1973) Biochim Biophys Acta , vol.308 , pp. 59-67
    • Godson, G.N.1
  • 47
    • 0018858591 scopus 로고
    • Targeted deletions of sequences from closed circular DNA
    • doi: 10.1073/pnas.77.5.2455
    • Green C, Tibbetts C (1980) Targeted deletions of sequences from closed circular DNA. Proc Natl Acad Sci USA 77:2455-2459 doi: 10.1073/ pnas.77.5.2455
    • (1980) Proc Natl Acad Sci USA , vol.77 , pp. 2455-2459
    • Green, C.1    Tibbetts, C.2
  • 48
    • 0020522128 scopus 로고
    • Human beta-globin pre-mRNA synthesized in vitro is accurately spliced in Xenopus oocyte nuclei
    • doi: 10.1016/0092-8674(83)90054-5
    • Green MR, Maniatis T, Melton DA (1983) Human beta-globin pre-mRNA synthesized in vitro is accurately spliced in Xenopus oocyte nuclei. Cell 32:681-694 doi: 10.1016/0092-8674(83)90054-5
    • (1983) Cell , vol.32 , pp. 681-694
    • Green, M.R.1    Maniatis, T.2    Melton, D.A.3
  • 49
    • 0017821271 scopus 로고
    • Nucleotide sequence and secondary structure of potato spindle tuber viroid
    • doi: 10.1038/273203a0
    • Gross HJ, Domdey H, Lossow C, Jank P, Raba M, Alberty H et al (1978) Nucleotide sequence and secondary structure of potato spindle tuber viroid. Nature 273:203-208 doi: 10.1038/273203a0
    • (1978) Nature , vol.273 , pp. 203-208
    • Gross, H.J.1    Domdey, H.2    Lossow, C.3    Jank, P.4    Raba, M.5    Alberty, H.6
  • 50
    • 0019878040 scopus 로고
    • Restriction enzyme digestion of hemimethylated
    • doi: 10.1093/nar/9.11.2509
    • Gruenbaum Y, Cedar H, Razin A (1981a) Restriction enzyme digestion of hemimethylated DNA. Nucleic Acids Res 9:2509-2515 doi: 10.1093/nar/ 9.11.2509
    • (1981) DNA. Nucleic Acids Res , vol.9 , pp. 2509-2515
    • Gruenbaum, Y.1    Cedar, H.2    Razin, A.3
  • 51
    • 0019875880 scopus 로고
    • Methylation of CpG sequences in eukaryotic DNA
    • doi: 10.1016/0014-5793(81)80055-5
    • Gruenbaum Y, Stein R, Cedar H, Razin A (1981b) Methylation of CpG sequences in eukaryotic DNA. FEBS Lett 124:67-71 doi: 10.1016/ 0014-5793(81)80055-5
    • (1981) FEBS Lett , vol.124 , pp. 67-71
    • Gruenbaum, Y.1    Stein, R.2    Cedar, H.3    Razin, A.4
  • 52
    • 0035171927 scopus 로고    scopus 로고
    • Characterization of two DNA polymerases from the hyperthermophilic euryarchaeon Pyrococcus abyssi
    • doi: 10.1046/j.0014-2956.2001.02550.x
    • Gueguen Y, Rolland JL, Lecompte O, Azam P, Le Romancer G, Flament D et al (2001) Characterization of two DNA polymerases from the hyperthermophilic euryarchaeon Pyrococcus abyssi. Eur J Biochem 268:5961-5969 doi: 10.1046/j.0014-2956.2001.02550.x
    • (2001) Eur J Biochem , vol.268 , pp. 5961-5969
    • Gueguen, Y.1    Rolland, J.L.2    Lecompte, O.3    Azam, P.4    Le Romancer, G.5    Flament, D.6
  • 53
    • 0020478771 scopus 로고
    • Intra- and intermolecular strand transfer by HeLa DNA topoisomerase I
    • Halligan BD, Davis JL, Edwards KA, Liu LF (1982) Intra- and intermolecular strand transfer by HeLa DNA topoisomerase I. J Biol Chem 257:3995-4000
    • (1982) J Biol Chem , vol.257 , pp. 3995-4000
    • Halligan, B.D.1    Davis, J.L.2    Edwards, K.A.3    Liu, L.F.4
  • 54
    • 0022819365 scopus 로고
    • T4 polynucleotide kinase: Macromolecular crowding increases the efficiency of reaction at DNA termini
    • doi: 10.1016/0003-2697(86)90555-5
    • Harrison B, Zimmerman SB (1986) T4 polynucleotide kinase: Macromolecular crowding increases the efficiency of reaction at DNA termini. Anal Biochem 158:307-315 doi: 10.1016/0003-2697(86)90555-5
    • (1986) Anal Biochem , vol.158 , pp. 307-315
    • Harrison, B.1    Zimmerman, S.B.2
  • 55
    • 0018505056 scopus 로고
    • Removal of thymine-containing pyrimidine dimers from UV light-irradiated DNA by S1 endonuclease
    • doi: 10.1111/j.1751-1097.1979.tb07142.x
    • Heflich RH, Mahoney-Leo E, Maher VM, McCormick JJ (1979) Removal of thymine-containing pyrimidine dimers from UV light-irradiated DNA by S1 endonuclease. Photochem Photobiol 30:247-250 doi: 10.1111/ j.1751-1097.1979.tb07142.x
    • (1979) Photochem Photobiol , vol.30 , pp. 247-250
    • Heflich, R.H.1    Mahoney-Leo, E.2    Maher, V.M.3    McCormick, J.J.4
  • 56
    • 0036790939 scopus 로고    scopus 로고
    • Bacteriophage T4 RNA ligase 2 (gp24.1) exemplifies a family of RNA ligases found in all phylogenetic domains
    • doi: 10.1073/pnas.192184699
    • Ho CK, Shuman S (2002) Bacteriophage T4 RNA ligase 2 (gp24.1) exemplifies a family of RNA ligases found in all phylogenetic domains. Proc Natl Acad Sci USA 99:12709-12714 doi: 10.1073/pnas.192184699
    • (2002) Proc Natl Acad Sci USA , vol.99 , pp. 12709-12714
    • Ho, C.K.1    Shuman, S.2
  • 57
    • 0017133050 scopus 로고
    • Specific excision of the inserted DNA segment from hybrid plasmids constructed by the poly(dA). poly (dT) method
    • Hofstetter H, Schambock A, Van Den Berg J, Weissmann C (1976) Specific excision of the inserted DNA segment from hybrid plasmids constructed by the poly(dA). poly (dT) method. Biochim Biophys Acta 454:587-591
    • (1976) Biochim Biophys Acta , vol.454 , pp. 587-591
    • Hofstetter, H.1    Schambock, A.2    Van Den Berg, J.3    Weissmann, C.4
  • 58
  • 59
    • 0029883357 scopus 로고    scopus 로고
    • Optimization of Dnase I removal of contaminating DNA from RNA for use in quantitative RNA-PCR
    • 1016, 1018-1020
    • Huang Z, Fasco MJ, Kaminsky LS (1996) Optimization of Dnase I removal of contaminating DNA from RNA for use in quantitative RNA-PCR. Biotechniques 20:1012-1014 1016, 1018-1020
    • (1996) Biotechniques , vol.20 , pp. 1012-1014
    • Huang, Z.1    Fasco, M.J.2    Kaminsky, L.S.3
  • 60
    • 0023665337 scopus 로고
    • Escherichia coli thioredoxin stabilizes complexes of bacteriophage T7 DNA polymerase and primed templates
    • Huber HE, Tabor S, Richardson CC (1987) Escherichia coli thioredoxin stabilizes complexes of bacteriophage T7 DNA polymerase and primed templates. J Biol Chem 262:16224-16232
    • (1987) J Biol Chem , vol.262 , pp. 16224-16232
    • Huber, H.E.1    Tabor, S.2    Richardson, C.C.3
  • 61
    • 0014429805 scopus 로고
    • Sugar-unspecific mung bean nuclease I
    • Johnson PH, Laskowski M Sr (1968) Sugar-unspecific mung bean nuclease I. J Biol Chem 243:3421-3424
    • (1968) J Biol Chem , vol.243 , pp. 3421-3424
    • Johnson, P.H.1    Laskowski Sr., M.2
  • 62
    • 0014961405 scopus 로고
    • Mung bean nuclease I. II. Resistance of double stranded deoxyribonucleic acid and susceptibility of regions rich in adenosine and thymidine to enzymatic hydrolysis
    • Johnson PH, Laskowski M Sr (1970) Mung bean nuclease I. II. Resistance of double stranded deoxyribonucleic acid and susceptibility of regions rich in adenosine and thymidine to enzymatic hydrolysis. J Biol Chem 245:891-898
    • (1970) J Biol Chem , vol.245 , pp. 891-898
    • Johnson, P.H.1    Laskowski Sr., M.2
  • 63
    • 0028605845 scopus 로고
    • Sequence of the DNA ligase-encoding gene from Thermus scotoductus and conserved motifs in DNA ligases
    • doi: 10.1016/0378-1119(94)90652-1
    • Jonsson ZO, Thorbjarnardottir SH, Eggertsson G, Palsdottir A (1994) Sequence of the DNA ligase-encoding gene from Thermus scotoductus and conserved motifs in DNA ligases. Gene 151:177-180 doi: 10.1016/ 0378-1119(94)90652-1
    • (1994) Gene , vol.151 , pp. 177-180
    • Jonsson, Z.O.1    Thorbjarnardottir, S.H.2    Eggertsson, G.3    Palsdottir, A.4
  • 64
    • 0015917611 scopus 로고
    • Studies on bovine pancreatic deoxyribonuclease A. II. The effect of different bivalent metals on the specificity of degradation of DNA
    • Junowicz E, Spencer JH (1973) Studies on bovine pancreatic deoxyribonuclease A. II. The effect of different bivalent metals on the specificity of degradation of DNA. Biochim Biophys Acta 312:85-102
    • (1973) Biochim Biophys Acta , vol.312 , pp. 85-102
    • Junowicz, E.1    Spencer, J.H.2
  • 65
    • 0028833689 scopus 로고
    • Enzymatically produced composite primers: An application of T4 RNA ligase-coupled primers to PCR
    • 186
    • Kaluz S, Kaluzova M, Flint AP (1995) Enzymatically produced composite primers: An application of T4 RNA ligase-coupled primers to PCR. Biotechniques 19:182-184 186
    • (1995) Biotechniques , vol.19 , pp. 182-184
    • Kaluz, S.1    Kaluzova, M.2    Flint, A.P.3
  • 66
    • 0015421991 scopus 로고
    • Degradation of DNA RNA hybrids by ribonuclease H and DNA polymerases of cellular and viral origin
    • doi: 10.1073/pnas.69.11.3360
    • Keller W, Crouch R (1972) Degradation of DNA RNA hybrids by ribonuclease H and DNA polymerases of cellular and viral origin. Proc Natl Acad Sci USA 69:3360-3364 doi: 10.1073/pnas.69.11.3360
    • (1972) Proc Natl Acad Sci USA , vol.69 , pp. 3360-3364
    • Keller, W.1    Crouch, R.2
  • 68
    • 0021100915 scopus 로고
    • BAL 31 nuclease as a probe in concentrated salt for the B-Z DNA junction
    • doi: 10.1093/nar/11.11.3811
    • Kilpatrick MW, Wei CF, Gray HB Jr, Wells RD (1983) BAL 31 nuclease as a probe in concentrated salt for the B-Z DNA junction. Nucleic Acids Res 11:3811-3822 doi: 10.1093/nar/11.11.3811
    • (1983) Nucleic Acids Res , vol.11 , pp. 3811-3822
    • Kilpatrick, M.W.1    Wei, C.F.2    Gray Jr., H.B.3    Wells, R.D.4
  • 69
    • 0030804068 scopus 로고    scopus 로고
    • Fluorescence-, isotope- or biotin-labeling of the 5′-end of single-stranded DNA/RNA using T4 RNA ligase
    • doi: 10.1093/nar/25.18.3747
    • Kinoshita Y, Nishigaki K, Husimi Y (1997) Fluorescence-, isotope- or biotin-labeling of the 5′-end of single-stranded DNA/RNA using T4 RNA ligase. Nucleic Acids Res 25:3747-3748 doi: 10.1093/nar/25.18.3747
    • (1997) Nucleic Acids Res , vol.25 , pp. 3747-3748
    • Kinoshita, Y.1    Nishigaki, K.2    Husimi, Y.3
  • 70
    • 0014708426 scopus 로고
    • Selective elimination of the exonuclease activity of the deoxyribonucleic acid polymerase from Escherichia coli B by limited proteolysis
    • doi: 10.1073/pnas.65.1.168
    • Klenow H, Henningsen I (1970) Selective elimination of the exonuclease activity of the deoxyribonucleic acid polymerase from Escherichia coli B by limited proteolysis. Proc Natl Acad Sci USA 65:168-175 doi: 10.1073/ pnas.65.1.168
    • (1970) Proc Natl Acad Sci USA , vol.65 , pp. 168-175
    • Klenow, H.1    Henningsen, I.2
  • 71
    • 0019322667 scopus 로고
    • Deoxyribonucleic acid gyrase-deoxyribonucleic acid complex containing 140 base pairs of deoxyribonucleic acid and an alpha 2 beta 2 protein core
    • doi: 10.1021/bi00564a012
    • Klevan L, Wang JC (1980) Deoxyribonucleic acid gyrase-deoxyribonucleic acid complex containing 140 base pairs of deoxyribonucleic acid and an alpha 2 beta 2 protein core. Biochemistry 19:5229-5234 doi: 10.1021/ bi00564a012
    • (1980) Biochemistry , vol.19 , pp. 5229-5234
    • Klevan, L.1    Wang, J.C.2
  • 72
    • 0014968433 scopus 로고
    • DNA synthesis in cell-free extracts of a DNA polymerase-defective mutant
    • Kornberg T, Gefter ML (1970) DNA synthesis in cell-free extracts of a DNA polymerase-defective mutant. Biochem Biophys Res Commun 40:1348-1355
    • (1970) Biochem Biophys Res Commun , vol.40 , pp. 1348-1355
    • Kornberg, T.1    Gefter, M.L.2
  • 73
    • 50549179349 scopus 로고
    • Studies on the incorporation of deoxyribonucleic acid
    • doi: 10.1016/0006-3002(62)90842-9
    • Krakow JS, Coutsogeorgopoulos C, Canellakis ES (1962) Studies on the incorporation of deoxyribonucleic acid. Biochim Biophys Acta 55:639-650 doi: 10.1016/0006-3002(62)90842-9
    • (1962) Biochim Biophys Acta , vol.55 , pp. 639-650
    • Krakow, J.S.1    Coutsogeorgopoulos, C.2    Canellakis, E.S.3
  • 74
    • 0021770860 scopus 로고
    • Functional messenger RNAs are produced by SP6 in vitro transcription of cloned cDNAs
    • doi: 10.1093/nar/12.18.7057
    • Krieg PA, Melton DA (1984) Functional messenger RNAs are produced by SP6 in vitro transcription of cloned cDNAs. Nucleic Acids Res 12:7057-7070 doi: 10.1093/nar/12.18.7057
    • (1984) Nucleic Acids Res , vol.12 , pp. 7057-7070
    • Krieg, P.A.1    Melton, D.A.2
  • 75
    • 0017808624 scopus 로고
    • Gene-sized pieces produced by digestion of linear duplex DNA with mung bean nuclease
    • doi: 10.1021/bi00609a010
    • Kroeker WD, Kowalski D (1978) Gene-sized pieces produced by digestion of linear duplex DNA with mung bean nuclease. Biochemistry 17:3236-3243 doi: 10.1021/bi00609a010
    • (1978) Biochemistry , vol.17 , pp. 3236-3243
    • Kroeker, W.D.1    Kowalski, D.2
  • 76
    • 0017202381 scopus 로고
    • Mung bean nuclease I. Terminally directed hydrolysis of native DNA
    • doi: 10.1021/bi00665a020
    • Kroeker WD, Kowalski D, Laskowski M Sr (1976) Mung bean nuclease I. Terminally directed hydrolysis of native DNA. Biochemistry 15:4463-4467 doi: 10.1021/bi00665a020
    • (1976) Biochemistry , vol.15 , pp. 4463-4467
    • Kroeker, W.D.1    Kowalski, D.2    Laskowski Sr., M.3
  • 77
    • 76549250377 scopus 로고
    • Crystalline desoxyribonuclease; isolation and general properties; spectrophotometric method for the measurement of desoxyribonuclease activity
    • doi: 10.1085/jgp.33.4.349
    • Kunitz M (1950) Crystalline desoxyribonuclease; isolation and general properties; spectrophotometric method for the measurement of desoxyribonuclease activity. J Gen Physiol 33:349-362 doi: 10.1085/ jgp.33.4.349
    • (1950) J Gen Physiol , vol.33 , pp. 349-362
    • Kunitz, M.1
  • 78
    • 0017617464 scopus 로고
    • Assembly of SV40 chromatin in a cell-free system from Xenopus eggs
    • doi: 10.1016/0092-8674(77)90217-3
    • Laskey RA, Mills AD, Morris NR (1977) Assembly of SV40 chromatin in a cell-free system from Xenopus eggs. Cell 10:237-243 doi: 10.1016/ 0092-8674(77)90217-3
    • (1977) Cell , vol.10 , pp. 237-243
    • Laskey, R.A.1    Mills, A.D.2    Morris, N.R.3
  • 79
    • 0016273515 scopus 로고
    • DNA ligase: Structure, mechanism, and function
    • doi: 10.1126/science.186.4166.790
    • Lehman IR (1974) DNA ligase: Structure, mechanism, and function. Science 186:790-797 doi: 10.1126/science.186.4166.790
    • (1974) Science , vol.186 , pp. 790-797
    • Lehman, I.R.1
  • 80
    • 0020683627 scopus 로고
    • Mechanism of action of the endonuclease associated with the alpha beta and beta beta forms of avian RNA tumor virus reverse transcriptase
    • Leis J, Duyk G, Johnson S, Longiaru M, Skalka A (1983) Mechanism of action of the endonuclease associated with the alpha beta and beta beta forms of avian RNA tumor virus reverse transcriptase. J Virol 45:727-739
    • (1983) J Virol , vol.45 , pp. 727-739
    • Leis, J.1    Duyk, G.2    Johnson, S.3    Longiaru, M.4    Skalka, A.5
  • 81
    • 0025882629 scopus 로고
    • Eliminating primers from completed polymerase chain reactions with exonuclease VII
    • doi: 10.1093/nar/19.11.3139
    • Li HH, Cui XF, Arnheim N (1991) Eliminating primers from completed polymerase chain reactions with exonuclease VII. Nucleic Acids Res 19:3139-3141 doi: 10.1093/nar/19.11.3139
    • (1991) Nucleic Acids Res , vol.19 , pp. 3139-3141
    • Li, H.H.1    Cui, X.F.2    Arnheim, N.3
  • 82
    • 0017622430 scopus 로고
    • Physicochemical properties of T4 polynucleotide kinase
    • doi: 10.1111/j.1432-1033.1977.tb11343.x
    • Lillehaug JR (1977) Physicochemical properties of T4 polynucleotide kinase. Eur J Biochem 73:499-506 doi: 10.1111/j.1432-1033.1977.tb11343.x
    • (1977) Eur J Biochem , vol.73 , pp. 499-506
    • Lillehaug, J.R.1
  • 83
    • 0017178174 scopus 로고
    • Phosphorylation of double-stranded DNAs by T4 polynucleotide kinase
    • doi: 10.1021/bi00654a011
    • Lillehaug JR, Kleppe RK, Kleppe K (1976) Phosphorylation of double-stranded DNAs by T4 polynucleotide kinase. Biochemistry 15:1858-1865 doi: 10.1021/bi00654a011
    • (1976) Biochemistry , vol.15 , pp. 1858-1865
    • Lillehaug, J.R.1    Kleppe, R.K.2    Kleppe, K.3
  • 84
    • 0019087696 scopus 로고
    • The inverted repeat as a recognizable structural feature in supercoiled DNA molecules
    • doi: 10.1073/pnas.77.11.6468
    • Lilley DM (1980) The inverted repeat as a recognizable structural feature in supercoiled DNA molecules. Proc Natl Acad Sci USA 77:6468-6472 doi: 10.1073/pnas.77.11.6468
    • (1980) Proc Natl Acad Sci USA , vol.77 , pp. 6468-6472
    • Lilley, D.M.1
  • 85
    • 0027381917 scopus 로고
    • Mapping the 5′ and 3′ ends of Tetrahymena thermophila mRNAs using RNA ligase mediated amplification of cDNA ends (RLM-RACE)
    • doi: 10.1093/nar/21.21.4954
    • Liu X, Gorovsky MA (1993) Mapping the 5′ and 3′ ends of Tetrahymena thermophila mRNAs using RNA ligase mediated amplification of cDNA ends (RLM-RACE). Nucleic Acids Res 21:4954-4960 doi: 10.1093/nar/ 21.21.4954
    • (1993) Nucleic Acids Res , vol.21 , pp. 4954-4960
    • Liu, X.1    Gorovsky, M.A.2
  • 86
    • 0001498255 scopus 로고
    • Eukaryotic DNA topoisomerases: Two forms of type I DNA topoisomerases from HeLa cell nuclei
    • doi: 10.1073/pnas.78.6.3487
    • Liu LF, Miller KG (1981) Eukaryotic DNA topoisomerases: Two forms of type I DNA topoisomerases from HeLa cell nuclei. Proc Natl Acad Sci USA 78:3487-3491 doi: 10.1073/pnas.78.6.3487
    • (1981) Proc Natl Acad Sci USA , vol.78 , pp. 3487-3491
    • Liu, L.F.1    Miller, K.G.2
  • 88
    • 0015873924 scopus 로고
    • Isolation of deoxyribonucleic acid methylase mutants of Escherichia coli K-12
    • Marinus MG, Morris NR (1973) Isolation of deoxyribonucleic acid methylase mutants of Escherichia coli K-12. J Bacteriol 114:1143-1150
    • (1973) J Bacteriol , vol.114 , pp. 1143-1150
    • Marinus, M.G.1    Morris, N.R.2
  • 89
    • 0008062361 scopus 로고
    • Escherichia coli thioredoxin: A subunit of bacteriophage T7 DNA polymerase
    • doi: 10.1073/pnas.73.3.780
    • Mark DF, Richardson CC (1976) Escherichia coli thioredoxin: A subunit of bacteriophage T7 DNA polymerase. Proc Natl Acad Sci USA 73:780-784 doi: 10.1073/pnas.73.3.780
    • (1976) Proc Natl Acad Sci USA , vol.73 , pp. 780-784
    • Mark, D.F.1    Richardson, C.C.2
  • 90
    • 0036231641 scopus 로고    scopus 로고
    • ATP-dependent DNA ligases
    • Reviews3005
    • Martin IV, MacNeill SA (2002) ATP-dependent DNA ligases. Genome Biol 3(4):REviews3005
    • (2002) Genome Biol , vol.3 , Issue.4
    • Martin, I.V.1    MacNeill, S.A.2
  • 92
    • 2442437949 scopus 로고    scopus 로고
    • Characterization of a baculovirus enzyme with RNA ligase, polynucleotide 5′-kinase, and polynucleotide 3′-phosphatase activities
    • doi: 10.1074/jbc.M313386200
    • Martins A, Shuman S (2004a) Characterization of a baculovirus enzyme with RNA ligase, polynucleotide 5′-kinase, and polynucleotide 3′-phosphatase activities. J Biol Chem 279:18220-18231 doi: 10.1074/jbc.M313386200
    • (2004) J Biol Chem , vol.279 , pp. 18220-18231
    • Martins, A.1    Shuman, S.2
  • 93
    • 9944247546 scopus 로고    scopus 로고
    • An RNA ligase from Deinococcus radiodurans
    • doi: 10.1074/jbc.M407657200
    • Martins A, Shuman S (2004b) An RNA ligase from Deinococcus radiodurans. J Biol Chem 279:50654-50661 doi: 10.1074/jbc.M407657200
    • (2004) J Biol Chem , vol.279 , pp. 50654-50661
    • Martins, A.1    Shuman, S.2
  • 94
    • 0028213438 scopus 로고
    • Oligo-capping: A simple method to replace the cap structure of eukaryotic mRNAs with oligoribonucleotides
    • doi: 10.1016/0378-1119(94)90802-8
    • Maruyama K, Sugano S (1994) Oligo-capping: A simple method to replace the cap structure of eukaryotic mRNAs with oligoribonucleotides. Gene 138:171-174 doi: 10.1016/0378-1119(94)90802-8
    • (1994) Gene , vol.138 , pp. 171-174
    • Maruyama, K.1    Sugano, S.2
  • 95
    • 0016720451 scopus 로고
    • Analysis of bacteriophage deoxyribonucleic acid sequences methylated by host- and R-factor-controlled enzymes
    • May MS, Hattman S (1975) Analysis of bacteriophage deoxyribonucleic acid sequences methylated by host- and R-factor-controlled enzymes. J Bacteriol 123:768-770
    • (1975) J Bacteriol , vol.123 , pp. 768-770
    • May, M.S.1    Hattman, S.2
  • 96
    • 0015698349 scopus 로고
    • Action of the S1 endonuclease from Aspergillus oryzae on simian virus 40 supercoiled component I DNA
    • doi: 10.1016/0006-291X(73)91130-3
    • Mechali M, de Recondo AM, Girard M (1973) Action of the S1 endonuclease from Aspergillus oryzae on simian virus 40 supercoiled component I DNA. Biochem Biophys Res Commun 54:1306-1320 doi: 10.1016/0006-291X(73)91130-3
    • (1973) Biochem Biophys Res Commun , vol.54 , pp. 1306-1320
    • Mechali, M.1    de Recondo, A.M.2    Girard, M.3
  • 97
    • 0021770917 scopus 로고
    • Efficient in vitro synthesis of biologically active RNA and RNA hybridization probes from plasmids containing a bacteriophage SP6 promoter
    • doi: 10.1093/nar/12.18.7035
    • Melton DA, Krieg PA, Rebagliati MR, Maniatis T, Zinn K, Green MR (1984) Efficient in vitro synthesis of biologically active RNA and RNA hybridization probes from plasmids containing a bacteriophage SP6 promoter. Nucleic Acids Res 12:7035-7056 doi: 10.1093/nar/12.18.7035
    • (1984) Nucleic Acids Res , vol.12 , pp. 7035-7056
    • Melton, D.A.1    Krieg, P.A.2    Rebagliati, M.R.3    Maniatis, T.4    Zinn, K.5    Green, M.R.6
  • 98
    • 0018832897 scopus 로고
    • A temperature-sensitive single-stranded DNA-binding protein from Escherichia coli
    • Meyer RR, Glassberg J, Scott JV, Kornberg A (1980) A temperature-sensitive single-stranded DNA-binding protein from Escherichia coli. J Biol Chem 255:2897-2901
    • (1980) J Biol Chem , vol.255 , pp. 2897-2901
    • Meyer, R.R.1    Glassberg, J.2    Scott, J.V.3    Kornberg, A.4
  • 99
    • 0014940314 scopus 로고
    • Mung bean nuclease I. 3. Purification procedure and (3′) omega monophosphatase activity
    • Mikulski AJ, Laskowski M Sr (1970) Mung bean nuclease I. 3. Purification procedure and (3′) omega monophosphatase activity. J Biol Chem 245:5026-5031
    • (1970) J Biol Chem , vol.245 , pp. 5026-5031
    • Mikulski, A.J.1    Laskowski Sr., M.2
  • 100
    • 0016733010 scopus 로고
    • Bacteriophage T7 deoxyribonucleic acid replication invitro. Bacteriophage T7 DNA polymerase: An an emzyme composed of phage- and host-specific subunits
    • Modrich P, Richardson CC (1975) Bacteriophage T7 deoxyribonucleic acid replication invitro. Bacteriophage T7 DNA polymerase: An an emzyme composed of phage- and host-specific subunits. J Biol Chem 250:5515-5522
    • (1975) J Biol Chem , vol.250 , pp. 5515-5522
    • Modrich, P.1    Richardson, C.C.2
  • 101
    • 0016130809 scopus 로고
    • Characterization of reverse transcriptase and RNase H from friend-murine leukemia virus
    • doi: 10.1016/0042-6822(74)90302-X
    • Moelling K (1974) Characterization of reverse transcriptase and RNase H from friend-murine leukemia virus. Virology 62:46-59 doi: 10.1016/ 0042-6822(74)90302-X
    • (1974) Virology , vol.62 , pp. 46-59
    • Moelling, K.1
  • 102
    • 0028923440 scopus 로고
    • Structure and function of the multifunctional DNA-repair enzyme exonuclease III
    • doi: 10.1038/374381a0
    • Mol CD, Kuo CF, Thayer MM, Cunningham RP, Tainer JA (1995) Structure and function of the multifunctional DNA-repair enzyme exonuclease III. Nature 374:381-386 doi: 10.1038/374381a0
    • (1995) Nature , vol.374 , pp. 381-386
    • Mol, C.D.1    Kuo, C.F.2    Thayer, M.M.3    Cunningham, R.P.4    Tainer, J.A.5
  • 103
    • 0033764931 scopus 로고    scopus 로고
    • A DNA ligase from a hyperthermophilic archaeon with unique cofactor specificity
    • doi: 10.1128/JB.182.22.6424-6433.2000
    • Nakatani M, Ezaki S, Atomi H, Imanaka T (2000) A DNA ligase from a hyperthermophilic archaeon with unique cofactor specificity. J Bacteriol 182:6424-6433 doi: 10.1128/JB.182.22.6424-6433.2000
    • (2000) J Bacteriol , vol.182 , pp. 6424-6433
    • Nakatani, M.1    Ezaki, S.2    Atomi, H.3    Imanaka, T.4
  • 104
    • 6344289396 scopus 로고    scopus 로고
    • How an RNA ligase discriminates RNA versus DNA damage
    • doi: 10.1016/j.molcel.2004.09.022
    • Nandakumar J, Shuman S (2004) How an RNA ligase discriminates RNA versus DNA damage. Mol Cell 16:211-221 doi: 10.1016/j.molcel.2004.09.022
    • (2004) Mol Cell , vol.16 , pp. 211-221
    • Nandakumar, J.1    Shuman, S.2
  • 105
    • 3843051369 scopus 로고    scopus 로고
    • RNA substrate specificity and structure-guided mutational analysis of bacteriophage T4 RNA ligase 2
    • doi: 10.1074/jbc.M402394200
    • Nandakumar J, Ho CK, Lima CD, Shuman S (2004) RNA substrate specificity and structure-guided mutational analysis of bacteriophage T4 RNA ligase 2. J Biol Chem 279:31337-31347 doi: 10.1074/jbc.M402394200
    • (2004) J Biol Chem , vol.279 , pp. 31337-31347
    • Nandakumar, J.1    Ho, C.K.2    Lima, C.D.3    Shuman, S.4
  • 106
    • 0021760543 scopus 로고
    • Alteration of apparent restriction endonuclease recognition specificities by DNA methylases
    • doi: 10.1093/nar/12.13.5165
    • Nelson M, Christ C, Schildkraut I (1984) Alteration of apparent restriction endonuclease recognition specificities by DNA methylases. Nucleic Acids Res 12:5165-5173 doi: 10.1093/nar/12.13.5165
    • (1984) Nucleic Acids Res , vol.12 , pp. 5165-5173
    • Nelson, M.1    Christ, C.2    Schildkraut, I.3
  • 107
    • 0019350114 scopus 로고
    • Cruciform structures in supercoiled DNA
    • doi: 10.1038/289466a0
    • Panayotatos N, Wells RD (1981) Cruciform structures in supercoiled DNA. Nature 289:466-470 doi: 10.1038/289466a0
    • (1981) Nature , vol.289 , pp. 466-470
    • Panayotatos, N.1    Wells, R.D.2
  • 108
    • 0015712190 scopus 로고
    • Physical characterization and simultaneous purification of bacteriophage T4 induced polynucleotide kinase, polynucleotide ligase, and deoxyribonucleic acid polymerase
    • doi: 10.1021/bi00749a003
    • Panet A, van de Sande JH, Loewen PC, Khorana HG, Raae AJ, Lillehaug JR et al (1973) Physical characterization and simultaneous purification of bacteriophage T4 induced polynucleotide kinase, polynucleotide ligase, and deoxyribonucleic acid polymerase. Biochemistry 12:5045-5050 doi: 10.1021/bi00749a003
    • (1973) Biochemistry , vol.12 , pp. 5045-5050
    • Panet, A.1    van de Sande, J.H.2    Loewen, P.C.3    Khorana, H.G.4    Raae, A.J.5    Lillehaug, J.R.6
  • 109
    • 0019870039 scopus 로고
    • Sequence dependence of the helical repeat of DNA in solution
    • doi: 10.1038/292375a0
    • Peck LJ, Wang JC (1981) Sequence dependence of the helical repeat of DNA in solution. Nature 292:375-378 doi: 10.1038/292375a0
    • (1981) Nature , vol.292 , pp. 375-378
    • Peck, L.J.1    Wang, J.C.2
  • 110
    • 47349089911 scopus 로고    scopus 로고
    • Avian Myeoloblastosis Virus (AMV): Only one side of the coin
    • doi: 10.1186/1742-4690-5-49
    • Perbal B (2008) Avian Myeoloblastosis Virus (AMV): Only one side of the coin. Retrovirology 5:49 doi: 10.1186/1742-4690-5-49
    • (2008) Retrovirology , vol.5 , pp. 49
    • Perbal, B.1
  • 112
    • 0017164347 scopus 로고
    • Two restriction endonucleases from Bacillus globiggi
    • Pirrotta V (1976) Two restriction endonucleases from Bacillus globiggi. Nucleic Acids Res 3:1747-1760
    • (1976) Nucleic Acids Res , vol.3 , pp. 1747-1760
    • Pirrotta, V.1
  • 113
    • 0019164715 scopus 로고
    • Analysis of covalent complexes formed between calf thymus DNA topoisomerase and single-stranded DNA
    • doi: 10.1111/j.1432-1033.1980.tb04734.x
    • Prell B, Vosberg HP (1980) Analysis of covalent complexes formed between calf thymus DNA topoisomerase and single-stranded DNA. Eur J Biochem 108:389-398 doi: 10.1111/j.1432-1033.1980.tb04734.x
    • (1980) Eur J Biochem , vol.108 , pp. 389-398
    • Prell, B.1    Vosberg, H.P.2
  • 114
    • 41449105355 scopus 로고    scopus 로고
    • Telomere length, telomeric proteins and genomic instability during the multistep carcinogenic process
    • doi: 10.1016/j.critrevonc.2007.11.006
    • Raynaud CM, Sabatier L, Philipot O, Olaussen KA, Soria JC (2008) Telomere length, telomeric proteins and genomic instability during the multistep carcinogenic process. Crit Rev Oncol Hematol 66:99-117 doi: 10.1016/j.critrevonc.2007.11.006
    • (2008) Crit Rev Oncol Hematol , vol.66 , pp. 99-117
    • Raynaud, C.M.1    Sabatier, L.2    Philipot, O.3    Olaussen, K.A.4    Soria, J.C.5
  • 115
    • 0011923583 scopus 로고
    • Distribution of 5-methylcytosine in chromatin
    • doi: 10.1073/pnas.74.7.2725
    • Razin A, Cedar H (1977) Distribution of 5-methylcytosine in chromatin. Proc Natl Acad Sci USA 74:2725-2728 doi: 10.1073/pnas.74.7.2725
    • (1977) Proc Natl Acad Sci USA , vol.74 , pp. 2725-2728
    • Razin, A.1    Cedar, H.2
  • 116
    • 0019318994 scopus 로고
    • DNA methylation and gene function
    • doi: 10.1126/science.6254144
    • Razin A, Riggs AD (1980) DNA methylation and gene function. Science 210:604-610 doi: 10.1126/science.6254144
    • (1980) Science , vol.210 , pp. 604-610
    • Razin, A.1    Riggs, A.D.2
  • 117
    • 0019811680 scopus 로고
    • Primary and secondary structure of U2 snRNA
    • doi: 10.1093/nar/9.21.5645
    • Reddy R, Henning D, Epstein P, Busch H (1981) Primary and secondary structure of U2 snRNA. Nucleic Acids Res 9:5645-5658 doi: 10.1093/nar/ 9.21.5645
    • (1981) Nucleic Acids Res , vol.9 , pp. 5645-5658
    • Reddy, R.1    Henning, D.2    Epstein, P.3    Busch, H.4
  • 118
    • 0015207594 scopus 로고
    • Conformational isomers of alkaline phosphatase in the mechanism of hydrolysis
    • doi: 10.1021/bi00793a016
    • Reid TW, Wilson IB (1971) Conformational isomers of alkaline phosphatase in the mechanism of hydrolysis. Biochemistry 10:380-387 doi: 10.1021/ bi00793a016
    • (1971) Biochemistry , vol.10 , pp. 380-387
    • Reid, T.W.1    Wilson, I.B.2
  • 119
    • 0019316884 scopus 로고
    • Enzymatic synthesis of deoxyribonucleic acid by the avian retrovirus reverse transcriptase in vitro: Optimum conditions required for transcription of large ribonucleic acid templates
    • doi: 10.1021/bi00544a019
    • Retzel EF, Collett MS, Faras AJ (1980) Enzymatic synthesis of deoxyribonucleic acid by the avian retrovirus reverse transcriptase in vitro: Optimum conditions required for transcription of large ribonucleic acid templates. Biochemistry 19:513-518 doi: 10.1021/ bi00544a019
    • (1980) Biochemistry , vol.19 , pp. 513-518
    • Retzel, E.F.1    Collett, M.S.2    Faras, A.J.3
  • 120
    • 0000973807 scopus 로고
    • A deoxyribonucleic acid phosphatase-exonuclease from Escherichia Coli. I. Purification of the enzyme and characterization of the phosphatase activity
    • Richardson CC, Kornberg A (1964) A deoxyribonucleic acid phosphatase-exonuclease from Escherichia Coli. I. Purification of the enzyme and characterization of the phosphatase activity. J Biol Chem 239:242-250
    • (1964) J Biol Chem , vol.239 , pp. 242-250
    • Richardson, C.C.1    Kornberg, A.2
  • 121
    • 0000973806 scopus 로고
    • A deoxyribonucleic acid phosphatase-exonuclease from Escherichia Coli. Ii. Characterization of the exonuclease activity
    • Richardson CC, Lehman IR, Kornberg A (1964) A deoxyribonucleic acid phosphatase-exonuclease from Escherichia Coli. Ii. Characterization of the exonuclease activity. J Biol Chem 239:251-258
    • (1964) J Biol Chem , vol.239 , pp. 251-258
    • Richardson, C.C.1    Lehman, I.R.2    Kornberg, A.3
  • 122
    • 0032568248 scopus 로고    scopus 로고
    • Resistance and cross-resistance with saquinavir and other HIV protease inhibitors: Theory and practice
    • doi: 10.1097/00002030-199805000-00005
    • Roberts NA, Craig JC, Sheldon J (1998) Resistance and cross-resistance with saquinavir and other HIV protease inhibitors: Theory and practice. AIDS 12:453-460 doi: 10.1097/00002030-199805000-00005
    • (1998) AIDS , vol.12 , pp. 453-460
    • Roberts, N.A.1    Craig, J.C.2    Sheldon, J.3
  • 123
    • 0019142844 scopus 로고
    • Cloning of the exonuclease III gene of Escherichia coli
    • doi: 10.1016/0378-1119(80)90059-1
    • Rogers SG, Weiss B (1980) Cloning of the exonuclease III gene of Escherichia coli. Gene 11:187-195 doi: 10.1016/0378-1119(80)90059-1
    • (1980) Gene , vol.11 , pp. 187-195
    • Rogers, S.G.1    Weiss, B.2
  • 124
    • 3142564389 scopus 로고    scopus 로고
    • Characterization of a thermophilic DNA ligase from the archaeon Thermococcus fumicolans
    • doi: 10.1111/j.1574-6968.2004.tb09657.x
    • Rolland JL, Gueguen Y, Persillon C, Masson JM, Dietrich J (2004) Characterization of a thermophilic DNA ligase from the archaeon Thermococcus fumicolans. FEMS Microbiol Lett 236:267-273 doi: 10.1111/ j.1574-6968.2004.tb09657.x
    • (2004) FEMS Microbiol Lett , vol.236 , pp. 267-273
    • Rolland, J.L.1    Gueguen, Y.2    Persillon, C.3    Masson, J.M.4    Dietrich, J.5
  • 125
    • 0017277566 scopus 로고
    • Terminal labeling and addition of homopolymer tracts to duplex DNA fragments by terminal deoxynucleotidyl transferase
    • Roychoudhury R, Jay E, Wu R (1976) Terminal labeling and addition of homopolymer tracts to duplex DNA fragments by terminal deoxynucleotidyl transferase. Nucleic Acids Res 3:863-877
    • (1976) Nucleic Acids Res , vol.3 , pp. 863-877
    • Roychoudhury, R.1    Jay, E.2    Wu, R.3
  • 126
    • 0021813995 scopus 로고
    • DNA polymerases from the extremely thermophilic bacterium Thermus thermophilus HB-8
    • doi: 10.1111/j.1432-1033.1985.tb08890.x
    • Ruttimann C, Cotoras M, Zaldivar J, Vicuna R (1985) DNA polymerases from the extremely thermophilic bacterium Thermus thermophilus HB-8. Eur J Biochem 149:41-46 doi: 10.1111/j.1432-1033.1985.tb08890.x
    • (1985) Eur J Biochem , vol.149 , pp. 41-46
    • Ruttimann, C.1    Cotoras, M.2    Zaldivar, J.3    Vicuna, R.4
  • 127
    • 0022423551 scopus 로고
    • A novel transcription property of SP6 and T7 RNA polymerases: Dependence on template structure
    • doi: 10.1093/nar/13.17.6223
    • Schenborn ET, Mierendorf RC Jr (1985) A novel transcription property of SP6 and T7 RNA polymerases: Dependence on template structure. Nucleic Acids Res 13:6223-6236 doi: 10.1093/nar/13.17.6223
    • (1985) Nucleic Acids Res , vol.13 , pp. 6223-6236
    • Schenborn, E.T.1    Mierendorf Jr., R.C.2
  • 128
    • 0034057803 scopus 로고    scopus 로고
    • Hepatitis B virus biology
    • doi: 10.1128/MMBR.64.1.51-68.2000
    • Seeger C, Mason WS (2000) Hepatitis B virus biology. Microbiol Mol Biol Rev 64:51-68 doi: 10.1128/MMBR.64.1.51-68.2000
    • (2000) Microbiol Mol Biol Rev , vol.64 , pp. 51-68
    • Seeger, C.1    Mason, W.S.2
  • 129
    • 0016323383 scopus 로고
    • Mapping of mutational alterations in DNA with S1 nuclease: The location of deletions, insertions and temperature-sensitive mutations in SV40
    • Shenk TE, Rhodes C, Rigby PW, Berg P (1975) Mapping of mutational alterations in DNA with S1 nuclease: The location of deletions, insertions and temperature-sensitive mutations in SV40. Cold Spring Harb Symp Quant Biol 39(Pt 1):61-67
    • (1975) Cold Spring Harb Symp Quant Biol , vol.39 , Issue.PART 1 , pp. 61-67
    • Shenk, T.E.1    Rhodes, C.2    Rigby, P.W.3    Berg, P.4
  • 130
    • 0007852992 scopus 로고
    • Location of S1 nuclease-cleavage sites on circular, superhelical DNAs between polyoma virus and simian virus 40
    • Shishido K (1979) Location of S1 nuclease-cleavage sites on circular, superhelical DNAs between polyoma virus and simian virus 40. Agric Biol Chem 43:1093-1102
    • (1979) Agric Biol Chem , vol.43 , pp. 1093-1102
    • Shishido, K.1
  • 131
    • 0016197728 scopus 로고
    • Cleavage of ultraviolet light-irradiated DNA by single strand-specific S1 endonuclease
    • doi: 10.1016/0006-291X(74)90466-5
    • Shishido K, Ando T (1974) Cleavage of ultraviolet light-irradiated DNA by single strand-specific S1 endonuclease. Biochem Biophys Res Commun 59:1380-1388 doi: 10.1016/0006-291X(74)90466-5
    • (1974) Biochem Biophys Res Commun , vol.59 , pp. 1380-1388
    • Shishido, K.1    Ando, T.2
  • 132
    • 0016665307 scopus 로고
    • Site-specific fragmentation of bacteriophage T5 DNA by single-strand-specific S1 endonuclease
    • Shishido K, Ando T (1975) Site-specific fragmentation of bacteriophage T5 DNA by single-strand-specific S1 endonuclease. Biochim Biophys Acta 390:125-132
    • (1975) Biochim Biophys Acta , vol.390 , pp. 125-132
    • Shishido, K.1    Ando, T.2
  • 133
    • 0002571496 scopus 로고
    • Single-strand-specific nucleases
    • In: Linn S, Roberts R (eds) Cold Spring Harbor Laboratory, Cold Spring Harbor
    • Shishido K, Ando T (1982) Single-strand-specific nucleases. In: Linn S, Roberts R (eds) Nucleases. Cold Spring Harbor Laboratory, Cold Spring Harbor, pp 155-185
    • (1982) Nucleases , pp. 155-185
    • Shishido, K.1    Ando, T.2
  • 134
    • 0014803154 scopus 로고
    • Some properties of the polynucleotide segments isolated from heat-denatured DNA by digestion with a nuclease specific for single stranded DNA
    • Shishido K, Ikeda Y (1970) Some properties of the polynucleotide segments isolated from heat-denatured DNA by digestion with a nuclease specific for single stranded DNA. J Biochem 67:759-765
    • (1970) J Biochem , vol.67 , pp. 759-765
    • Shishido, K.1    Ikeda, Y.2
  • 135
    • 0015242818 scopus 로고
    • Isolation of double-helical regions rich in adenine-thymine base pairing from bacteriophage f1 DNA
    • doi: 10.1016/0022-2836(71)90200-2
    • Shishido K, Ikeda Y (1971) Isolation of double-helical regions rich in adenine-thymine base pairing from bacteriophage f1 DNA. J Mol Biol 55:287-291 doi: 10.1016/0022-2836(71)90200-2
    • (1971) J Mol Biol , vol.55 , pp. 287-291
    • Shishido, K.1    Ikeda, Y.2
  • 136
    • 0015408606 scopus 로고
    • Purification and properties of bacteriophage T4-induced RNA ligase
    • doi: 10.1073/pnas.69.10.3009
    • Silber R, Malathi VG, Hurwitz J (1972) Purification and properties of bacteriophage T4-induced RNA ligase. Proc Natl Acad Sci USA 69:3009-3013 doi: 10.1073/pnas.69.10.3009
    • (1972) Proc Natl Acad Sci USA , vol.69 , pp. 3009-3013
    • Silber, R.1    Malathi, V.G.2    Hurwitz, J.3
  • 137
    • 2442549510 scopus 로고    scopus 로고
    • S-Adenosyl-L-methionine-dependent restriction enzymes
    • doi: 10.1080/10409230490440532
    • Sistla S, Rao DN (2004) S-Adenosyl-L-methionine-dependent restriction enzymes. Crit Rev Biochem Mol Biol 39:1-19 doi: 10.1080/10409230490440532
    • (2004) Crit Rev Biochem Mol Biol , vol.39 , pp. 1-19
    • Sistla, S.1    Rao, D.N.2
  • 138
    • 0019793550 scopus 로고
    • Nucleotide sequence of the cloned gene for bacteriophage T7 RNA polymerase
    • doi: 10.1016/0022-2836(81)90187-X
    • Stahl SJ, Zinn K (1981) Nucleotide sequence of the cloned gene for bacteriophage T7 RNA polymerase. J Mol Biol 148:481-485 doi: 10.1016/ 0022-2836(81)90187-X
    • (1981) J Mol Biol , vol.148 , pp. 481-485
    • Stahl, S.J.1    Zinn, K.2
  • 139
    • 0014427513 scopus 로고
    • Studies of the deoxyribonucleic acid from mesophilic and thermophilic bacteria
    • Stenesh J, Roe BA, Snyder TL (1968) Studies of the deoxyribonucleic acid from mesophilic and thermophilic bacteria. Biochim Biophys Acta 161:442-454
    • (1968) Biochim Biophys Acta , vol.161 , pp. 442-454
    • Stenesh, J.1    Roe, B.A.2    Snyder, T.L.3
  • 140
    • 0017333769 scopus 로고
    • Bacteriophage T4 RNA ligase. Reaction intermediates and interaction of substrates
    • Sugino A, Snoper TJ, Cozzarelli NR (1977) Bacteriophage T4 RNA ligase. Reaction intermediates and interaction of substrates. J Biol Chem 252:1732-1738
    • (1977) J Biol Chem , vol.252 , pp. 1732-1738
    • Sugino, A.1    Snoper, T.J.2    Cozzarelli, N.R.3
  • 141
    • 0001161168 scopus 로고
    • A nuclease from mung bean sprouts
    • Sung SC, Laskowski M Sr (1962) A nuclease from mung bean sprouts. J Biol Chem 237:506-511
    • (1962) J Biol Chem , vol.237 , pp. 506-511
    • Sung, S.C.1    Laskowski Sr., M.2
  • 142
    • 0018837047 scopus 로고
    • Methylation of integrated adenovirus type 12 DNA sequences in transformed cells is inversely correlated with viral gene expression
    • doi: 10.1073/pnas.77.1.253
    • Sutter D, Doerfler W (1980) Methylation of integrated adenovirus type 12 DNA sequences in transformed cells is inversely correlated with viral gene expression. Proc Natl Acad Sci USA 77:253-256 doi: 10.1073/ pnas.77.1.253
    • (1980) Proc Natl Acad Sci USA , vol.77 , pp. 253-256
    • Sutter, D.1    Doerfler, W.2
  • 143
    • 0023371227 scopus 로고
    • DNA sequence analysis with a modified bacteriophage T7 DNA polymerase
    • doi: 10.1073/pnas.84.14.4767
    • Tabor S, Richardson CC (1987) DNA sequence analysis with a modified bacteriophage T7 DNA polymerase. Proc Natl Acad Sci USA 84:4767-4771 doi: 10.1073/pnas.84.14.4767
    • (1987) Proc Natl Acad Sci USA , vol.84 , pp. 4767-4771
    • Tabor, S.1    Richardson, C.C.2
  • 144
    • 0024596736 scopus 로고
    • Selective inactivation of the exonuclease activity of bacteriophage T7 DNA polymerase by in vitro mutagenesis
    • Tabor S, Richardson CC (1989) Selective inactivation of the exonuclease activity of bacteriophage T7 DNA polymerase by in vitro mutagenesis. J Biol Chem 264:6447-6458
    • (1989) J Biol Chem , vol.264 , pp. 6447-6458
    • Tabor, S.1    Richardson, C.C.2
  • 145
    • 0023665251 scopus 로고
    • Escherichia coli thioredoxin confers processivity on the DNA polymerase activity of the gene 5 protein of bacteriophage T7
    • Tabor S, Huber HE, Richardson CC (1987) Escherichia coli thioredoxin confers processivity on the DNA polymerase activity of the gene 5 protein of bacteriophage T7. J Biol Chem 262:16212-16223
    • (1987) J Biol Chem , vol.262 , pp. 16212-16223
    • Tabor, S.1    Huber, H.E.2    Richardson, C.C.3
  • 146
    • 3643120086 scopus 로고
    • The Structure and Function of Ribonuclease T1: I. Chromatographic purification and properties of ribonuclease T1
    • Takahashi K (1961) The Structure and Function of Ribonuclease T1: I. Chromatographic purification and properties of ribonuclease T1. J Biochem 49:1-10
    • (1961) J Biochem , vol.49 , pp. 1-10
    • Takahashi, K.1
  • 147
    • 0021229570 scopus 로고
    • Thermophilic DNA ligase. Purification and properties of the enzyme from Thermus thermophilus HB8
    • Takahashi M, Yamaguchi E, Uchida T (1984) Thermophilic DNA ligase. Purification and properties of the enzyme from Thermus thermophilus HB8. J Biol Chem 259:10041-10047
    • (1984) J Biol Chem , vol.259 , pp. 10041-10047
    • Takahashi, M.1    Yamaguchi, E.2    Uchida, T.3
  • 148
    • 0018942291 scopus 로고
    • Eukaryotic signal sequence transports insulin antigen in Escherichia coli
    • doi: 10.1073/pnas.77.6.3369
    • Talmadge K, Stahl S, Gilbert W (1980) Eukaryotic signal sequence transports insulin antigen in Escherichia coli. Proc Natl Acad Sci USA 77:3369-3373 doi: 10.1073/pnas.77.6.3369
    • (1980) Proc Natl Acad Sci USA , vol.77 , pp. 3369-3373
    • Talmadge, K.1    Stahl, S.2    Gilbert, W.3
  • 149
    • 0014964695 scopus 로고
    • RNA-dependent DNA polymerase in virions of Rous sarcoma virus
    • doi: 10.1038/2261211a0
    • Temin HM, Mizutani S (1970) RNA-dependent DNA polymerase in virions of Rous sarcoma virus. Nature 226:1211-1213 doi: 10.1038/2261211a0
    • (1970) Nature , vol.226 , pp. 1211-1213
    • Temin, H.M.1    Mizutani, S.2
  • 150
    • 0022999793 scopus 로고
    • Ligation of single-stranded oligodeoxyribonucleotides by T4 RNA ligase
    • doi: 10.1016/0003-2697(86)90606-8
    • Tessier DC, Brousseau R, Vernet T (1986) Ligation of single-stranded oligodeoxyribonucleotides by T4 RNA ligase. Anal Biochem 158:171-178 doi: 10.1016/0003-2697(86)90606-8
    • (1986) Anal Biochem , vol.158 , pp. 171-178
    • Tessier, D.C.1    Brousseau, R.2    Vernet, T.3
  • 151
    • 0012767432 scopus 로고    scopus 로고
    • Nucleic acid recognition by OB-fold proteins
    • doi: 10.1146/annurev.biophys.32.110601.142506
    • Theobald DL, Mitton-Fry RM, Wuttke DS (2003) Nucleic acid recognition by OB-fold proteins. Annu Rev Biophys Biomol Struct 32:115-133 doi: 10.1146/ annurev.biophys.32.110601.142506
    • (2003) Annu Rev Biophys Biomol Struct , vol.32 , pp. 115-133
    • Theobald, D.L.1    Mitton-Fry, R.M.2    Wuttke, D.S.3
  • 152
    • 0029096564 scopus 로고
    • Cloning and sequence analysis of the DNA ligase-encoding gene of Rhodothermus marinus, and overproduction, purification and characterization of two thermophilic DNA ligases
    • doi: 10.1016/0378-1119(95)00286-F
    • Thorbjarnardottir SH, Jonsson ZO, Andresson OS, Kristjansson JK, Eggertsson G, Palsdottir A (1995) Cloning and sequence analysis of the DNA ligase-encoding gene of Rhodothermus marinus, and overproduction, purification and characterization of two thermophilic DNA ligases. Gene 161:1-6 doi: 10.1016/0378-1119(95)00286-F
    • (1995) Gene , vol.161 , pp. 1-6
    • Thorbjarnardottir, S.H.1    Jonsson, Z.O.2    Andresson, O.S.3    Kristjansson, J.K.4    Eggertsson, G.5    Palsdottir, A.6
  • 153
    • 0033534503 scopus 로고    scopus 로고
    • Functional domains of an NAD+-dependent DNA ligase
    • doi: 10.1006/jmbi.1998.2302
    • Timson DJ, Wigley DB (1999) Functional domains of an NAD+-dependent DNA ligase. J Mol Biol 285:73-83 doi: 10.1006/jmbi.1998.2302
    • (1999) J Mol Biol , vol.285 , pp. 73-83
    • Timson, D.J.1    Wigley, D.B.2
  • 154
    • 0017348683 scopus 로고
    • The reverse transcriptase
    • Verma IM (1977) The reverse transcriptase. Biochim Biophys Acta 473:1-38
    • (1977) Biochim Biophys Acta , vol.473 , pp. 1-38
    • Verma, I.M.1
  • 155
    • 0015924086 scopus 로고
    • Purification and further properties of single-strand-specific nuclease from Aspergillus oryzae
    • doi: 10.1111/j.1432-1033.1973.tb02669.x
    • Vogt VM (1973) Purification and further properties of single-strand-specific nuclease from Aspergillus oryzae. Eur J Biochem 33:192-200 doi: 10.1111/j.1432-1033.1973.tb02669.x
    • (1973) Eur J Biochem , vol.33 , pp. 192-200
    • Vogt, V.M.1
  • 156
    • 0018846634 scopus 로고
    • Purification and properties of S1 nuclease from Aspergillus
    • doi: 10.1016/S0076-6879(80)65034-4
    • Vogt VM (1980) Purification and properties of S1 nuclease from Aspergillus. Methods Enzymol 65:248-255 doi: 10.1016/ S0076-6879(80)65034-4
    • (1980) Methods Enzymol , vol.65 , pp. 248-255
    • Vogt, V.M.1
  • 157
    • 0018370487 scopus 로고
    • Helical repeat of DNA in solution
    • doi: 10.1073/pnas.76.1.200
    • Wang JC (1979) Helical repeat of DNA in solution. Proc Natl Acad Sci USA 76:200-203 doi: 10.1073/pnas.76.1.200
    • (1979) Proc Natl Acad Sci USA , vol.76 , pp. 200-203
    • Wang, J.C.1
  • 158
    • 0021112801 scopus 로고
    • Isolation and comparison of two molecular species of the BAL 31 nuclease from Alteromonas espejiana with distinct kinetic properties
    • Wei CF, Alianell GA, Bencen GH, Gray HB Jr (1983) Isolation and comparison of two molecular species of the BAL 31 nuclease from Alteromonas espejiana with distinct kinetic properties. J Biol Chem 258:13506-13512
    • (1983) J Biol Chem , vol.258 , pp. 13506-13512
    • Wei, C.F.1    Alianell, G.A.2    Bencen, G.H.3    Gray Jr., H.B.4
  • 159
    • 0017255036 scopus 로고
    • Endonuclease II of Escherichia coli is exonuclease III
    • Weiss B (1976) Endonuclease II of Escherichia coli is exonuclease III. J Biol Chem 251:1896-1901
    • (1976) J Biol Chem , vol.251 , pp. 1896-1901
    • Weiss, B.1
  • 160
    • 0016313747 scopus 로고
    • A system for mapping DNA sequences in the chromosomes of Drosophila melanogaster
    • doi: 10.1016/0092-8674(74)90045-2
    • Wensink PC, Finnegan DJ, Donelson JE, Hogness DS (1974) A system for mapping DNA sequences in the chromosomes of Drosophila melanogaster. Cell 3:315-325 doi: 10.1016/0092-8674(74)90045-2
    • (1974) Cell , vol.3 , pp. 315-325
    • Wensink, P.C.1    Finnegan, D.J.2    Donelson, J.E.3    Hogness, D.S.4
  • 161
    • 36249023071 scopus 로고    scopus 로고
    • A unified classification system for eukaryotic transposable elements
    • doi: 10.1038/nrg2165
    • Wicker T, Sabot F, Hua-Van A, Bennetzen JL, Capy P, Chalhoub B et al (2007) A unified classification system for eukaryotic transposable elements. Nat Rev Genet 8:973-982 doi: 10.1038/nrg2165
    • (2007) Nat Rev Genet , vol.8 , pp. 973-982
    • Wicker, T.1    Sabot, F.2    Hua-Van, A.3    Bennetzen, J.L.4    Capy, P.5    Chalhoub, B.6
  • 162
    • 0016589019 scopus 로고
    • Specificity of the S1 nuclease from Aspergillus oryzae
    • Wiegand RC, Godson GN, Radding CM (1975) Specificity of the S1 nuclease from Aspergillus oryzae. J Biol Chem 250:8848-8855
    • (1975) J Biol Chem , vol.250 , pp. 8848-8855
    • Wiegand, R.C.1    Godson, G.N.2    Radding, C.M.3
  • 163
    • 0025801120 scopus 로고
    • Organization of restriction-modification systems
    • doi: 10.1093/nar/19.10.2539
    • Wilson GG (1991) Organization of restriction-modification systems. Nucleic Acids Res 19:2539-2566 doi: 10.1093/nar/19.10.2539
    • (1991) Nucleic Acids Res , vol.19 , pp. 2539-2566
    • Wilson, G.G.1
  • 164
    • 0029868595 scopus 로고    scopus 로고
    • Single-stranded DNA ligation by T4 RNA ligase for PCR cloning of 5′-noncoding fragments and coding sequence of a specific gene
    • doi: 10.1093/nar/24.5.990
    • Zhang XH, Chiang VL (1996) Single-stranded DNA ligation by T4 RNA ligase for PCR cloning of 5′-noncoding fragments and coding sequence of a specific gene. Nucleic Acids Res 24:990-991 doi: 10.1093/nar/24.5.990
    • (1996) Nucleic Acids Res , vol.24 , pp. 990-991
    • Zhang, X.H.1    Chiang, V.L.2
  • 165
    • 0020523431 scopus 로고
    • Identification of two distinct regulatory regions adjacent to the human beta-interferon gene
    • doi: 10.1016/0092-8674(83)90544-5
    • Zinn K, DiMaio D, Maniatis T (1983) Identification of two distinct regulatory regions adjacent to the human beta-interferon gene. Cell 34:865-879 doi: 10.1016/0092-8674(83)90544-5
    • (1983) Cell , vol.34 , pp. 865-879
    • Zinn, K.1    DiMaio, D.2    Maniatis, T.3


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