메뉴 건너뛰기




Volumn 73, Issue 2, 1999, Pages 188-203

Purification of a polynucleotide kinase from calf thymus, comparison of its 3'-phosphatase domain with T4 polynucleotide kinase, and investigation of its effect on DNA replication in vitro

Author keywords

3' phosphatase; Bovine thymus; DNA phosphorylation; DNA replication; L 2 haloacid dehalogenase fold; Mammalian polynucleotide kinase; T4 polynucleotide kinase

Indexed keywords

DNA; HALOACID; NUCLEIC ACID; POLYNUCLEOTIDE 5' HYDROXYL KINASE;

EID: 0033135662     PISSN: 07302312     EISSN: None     Source Type: Journal    
DOI: 10.1002/(SICI)1097-4644(19990501)73:2<188::AID-JCB5>3.0.CO;2-H     Document Type: Article
Times cited : (22)

References (63)
  • 2
    • 0023388202 scopus 로고
    • Bacteriophage T4 anticodon nuclease, polynucleotide kinase and RNA ligase reprocess the host lysine tRNA
    • Amitsur M, Levitz R, Kaufmann G. 1987. Bacteriophage T4 anticodon nuclease, polynucleotide kinase and RNA ligase reprocess the host lysine tRNA. EMBO J 6:2499-2503.
    • (1987) EMBO J , vol.6 , pp. 2499-2503
    • Amitsur, M.1    Levitz, R.2    Kaufmann, G.3
  • 3
    • 0024445094 scopus 로고
    • In vitro reconstitution of anticodon nuclease from components encoded by phage T4 and Escherichia coli CTr5X
    • Amitsur M, Morad I, Kaufmann G. 1989. In vitro reconstitution of anticodon nuclease from components encoded by phage T4 and Escherichia coli CTr5X. EMBO J 8:2411-2415.
    • (1989) EMBO J , vol.8 , pp. 2411-2415
    • Amitsur, M.1    Morad, I.2    Kaufmann, G.3
  • 4
    • 0025743997 scopus 로고
    • Deletion analysis of a multifunctional yeast tRNA ligase polypeptide
    • Apostol BL, Westaway SK, Abelson J, Greer CL. 1991. Deletion analysis of a multifunctional yeast tRNA ligase polypeptide. J Biol Chem 266:7545-7455.
    • (1991) J Biol Chem , vol.266 , pp. 7545-17455
    • Apostol, B.L.1    Westaway, S.K.2    Abelson, J.3    Greer, C.L.4
  • 5
    • 0031970010 scopus 로고    scopus 로고
    • The catalytic domain of the P-type ATPase has the haloacid dehalogenase fold
    • Aravind L, Galperin MY, Koonin EV. 1998. The catalytic domain of the P-type ATPase has the haloacid dehalogenase fold. Trend Biochem 23:127-129.
    • (1998) Trend Biochem , vol.23 , pp. 127-129
    • Aravind, L.1    Galperin, M.Y.2    Koonin, E.V.3
  • 6
    • 0017797903 scopus 로고
    • Purification and properties of polynucleotide kinase of calf thymus
    • Austin GE, Sirakoff D, Roop B, Moyer GH. 1978. Purification and properties of polynucleotide kinase of calf thymus. Biochim Biophys Acta 522:412-422.
    • (1978) Biochim Biophys Acta , vol.522 , pp. 412-422
    • Austin, G.E.1    Sirakoff, D.2    Roop, B.3    Moyer, G.H.4
  • 7
    • 0028086144 scopus 로고
    • The complete DNA sequence of Autographa californica nuclear polyhedrosis virus
    • Ayres MD, Howard SC, Kuzio J, López-Ferber M, Possee RD. 1994. The complete DNA sequence of Autographa californica nuclear polyhedrosis virus. Virology 202:586-605.
    • (1994) Virology , vol.202 , pp. 586-605
    • Ayres, M.D.1    Howard, S.C.2    Kuzio, J.3    López-Ferber, M.4    Possee, R.D.5
  • 8
    • 0031054051 scopus 로고    scopus 로고
    • Enzymes and reactions at the eukaryotic replication fork
    • Bambara RA, Murante RS, Henricksen LA. 1997. Enzymes and reactions at the eukaryotic replication fork. J Biol Chem 272:4647-4650.
    • (1997) J Biol Chem , vol.272 , pp. 4647-4650
    • Bambara, R.A.1    Murante, R.S.2    Henricksen, L.A.3
  • 9
    • 0031897589 scopus 로고    scopus 로고
    • Predicting functions from protein sequences - Where are the bottlenecks?
    • Bork P, Koonin EV. 1998. Predicting functions from protein sequences - Where are the bottlenecks? Nature Genet 18:313-318.
    • (1998) Nature Genet , vol.18 , pp. 313-318
    • Bork, P.1    Koonin, E.V.2
  • 10
    • 0021792074 scopus 로고
    • Purification and properties of polynucleotide kinase from rat testes
    • Bosdal T, Lillehaug JR. 1985. Purification and properties of polynucleotide kinase from rat testes. Biochim Biophys Acta 840:280-286.
    • (1985) Biochim Biophys Acta , vol.840 , pp. 280-286
    • Bosdal, T.1    Lillehaug, J.R.2
  • 11
    • 0026338995 scopus 로고
    • Use of polyethyleneimine in purification of DNA-binding proteins
    • Burgess R. 1991. Use of polyethyleneimine in purification of DNA-binding proteins. Methods Enzymol 208:2-9.
    • (1991) Methods Enzymol , vol.208 , pp. 2-9
    • Burgess, R.1
  • 12
    • 0017184389 scopus 로고
    • A rapid and sensitive method for the quantitation of microgram quantities of protein utilizing the principle of protein dye-binding
    • Bradford MM. 1976. A rapid and sensitive method for the quantitation of microgram quantities of protein utilizing the principle of protein dye-binding. Anal Biochem 72: 248-254.
    • (1976) Anal Biochem , vol.72 , pp. 248-254
    • Bradford, M.M.1
  • 13
    • 0017757667 scopus 로고
    • 3′-Phosphatase activity in T4 polynucelotide kinase
    • Cameron V, Uhlenbeck OC. 1977. 3′-Phosphatase activity in T4 polynucelotide kinase. Biochemistry 16:5120-5126.
    • (1977) Biochemistry , vol.16 , pp. 5120-5126
    • Cameron, V.1    Uhlenbeck, O.C.2
  • 14
    • 0032486282 scopus 로고    scopus 로고
    • A new class of phosphotransferases phosphorylated on an aspartate residue in an amino-terminal DXDX(T/V) motif
    • Collet J-F, Strooban V, Pirard M, Delpierre G, Van Schaftingen E. 1998. A new class of phosphotransferases phosphorylated on an aspartate residue in an amino-terminal DXDX(T/V) motif. J Biol Chem 273:14107-14112.
    • (1998) J Biol Chem , vol.273 , pp. 14107-14112
    • Collet, J.-F.1    Strooban, V.2    Pirard, M.3    Delpierre, G.4    Van Schaftingen, E.5
  • 15
    • 0015674244 scopus 로고
    • Strand breaks and 5′ end-groups in DNA of irradiated thymocytes
    • Coquerelle T, Bop A, Kessler B, Hagen U. 1973. Strand breaks and 5′ end-groups in DNA of irradiated thymocytes. Int J Radiat Biol 24:397-404.
    • (1973) Int J Radiat Biol , vol.24 , pp. 397-404
    • Coquerelle, T.1    Bop, A.2    Kessler, B.3    Hagen, U.4
  • 16
    • 0028342951 scopus 로고
    • Repair of oxidative damage to DNA: Enzymology and biology
    • Demple B, Harrison L. 1994. Repair of oxidative damage to DNA: Enzymology and biology. Annu Rev Biochem 63: 915-948.
    • (1994) Annu Rev Biochem , vol.63 , pp. 915-948
    • Demple, B.1    Harrison, L.2
  • 17
    • 0016378791 scopus 로고
    • Genetics and physiology of bacteriophage T4 3′-phosphatase: Evidence for involvement of the enzyme in T4 DNA metabolism
    • Depew RE, Cozzarelli NR. 1974. Genetics and physiology of bacteriophage T4 3′-phosphatase: Evidence for involvement of the enzyme in T4 DNA metabolism. J Virol 13:888-897.
    • (1974) J Virol , vol.13 , pp. 888-897
    • Depew, R.E.1    Cozzarelli, N.R.2
  • 18
    • 0029952480 scopus 로고    scopus 로고
    • Application of an in vitro system in the study of chemotherapeutic drug effects on DNA replication
    • Diaz-Perez MJ, Wainer IW, Zannis-Hadjopoulos M, Price GB. 1996. Application of an in vitro system in the study of chemotherapeutic drug effects on DNA replication. J Cell Biochem 61:444-451.
    • (1996) J Cell Biochem , vol.61 , pp. 444-451
    • Diaz-Perez, M.J.1    Wainer, I.W.2    Zannis-Hadjopoulos, M.3    Price, G.B.4
  • 19
    • 0031929789 scopus 로고    scopus 로고
    • The pnk/pnl gene (ORF 86) of Autographa californica nucleopolyhedrosis virus is a non-essential, immediate early gene
    • Durantel D, Croizer L, Ayres MD, Croizier G, Possee RD, López-Ferber M. 1998. The pnk/pnl gene (ORF 86) of Autographa californica nucleopolyhedrosis virus is a non-essential, immediate early gene. J Gen Virol 79:629-637.
    • (1998) J Gen Virol , vol.79 , pp. 629-637
    • Durantel, D.1    Croizer, L.2    Ayres, M.D.3    Croizier, G.4    Possee, R.D.5    López-Ferber, M.6
  • 21
    • 0021110060 scopus 로고
    • The DNA 3′-phosphatase and 5′-hydroxyl kinase of rat liver chromatin
    • Habraken Y, Verly WG. 1983. The DNA 3′-phosphatase and 5′-hydroxyl kinase of rat liver chromatin. FEBS Lett 160:46-50.
    • (1983) FEBS Lett , vol.160 , pp. 46-50
    • Habraken, Y.1    Verly, W.G.2
  • 22
    • 0023056245 scopus 로고
    • Chromatin 3′-phosphatase/ 5′-OH kinase cannot transfer phosphate from 3′ to 5′ across a strand nick in DNA
    • Habraken Y, Verly WG. 1986. Chromatin 3′-phosphatase/ 5′-OH kinase cannot transfer phosphate from 3′ to 5′ across a strand nick in DNA. Nucleic Acids Res 14: 8103-8110.
    • (1986) Nucleic Acids Res , vol.14 , pp. 8103-8110
    • Habraken, Y.1    Verly, W.G.2
  • 23
    • 0023839662 scopus 로고
    • Further purification and characterization of the DNA 3′ phosphatase from rat-liver chromatin which is also a polynucleotide 5′-hydroxyl kinase
    • Habraken Y, Verly WG. 1988. Further purification and characterization of the DNA 3′ phosphatase from rat-liver chromatin which is also a polynucleotide 5′-hydroxyl kinase. Eur J Biochem 171:59-66.
    • (1988) Eur J Biochem , vol.171 , pp. 59-66
    • Habraken, Y.1    Verly, W.G.2
  • 24
    • 0030699278 scopus 로고    scopus 로고
    • Ribonuclease H renaturation gel assay using a fluorescent-labeled substrate
    • Han LY, Ma WP, Crouch RJ. 1997. Ribonuclease H renaturation gel assay using a fluorescent-labeled substrate. Biotechniques 23:920-926.
    • (1997) Biotechniques , vol.23 , pp. 920-926
    • Han, L.Y.1    Ma, W.P.2    Crouch, R.J.3
  • 25
    • 0029786674 scopus 로고    scopus 로고
    • Crystal structure of L-2-haloacid dehalogenase from Pseudomonas sp. YL. An a/b hydrolase structure that is different from the a/b hydrolase fold
    • Hisano T, Hata Y, Fujii T, Liu J-Q, Kurihara T, Esaki N, Soda K. 1996. Crystal structure of L-2-haloacid dehalogenase from Pseudomonas sp. YL. An a/b hydrolase structure that is different from the a/b hydrolase fold. J Biol Chem 271:20322-20330.
    • (1996) J Biol Chem , vol.271 , pp. 20322-20330
    • Hisano, T.1    Hata, Y.2    Fujii, T.3    Liu, J.-Q.4    Kurihara, T.5    Esaki, N.6    Soda, K.7
  • 26
    • 0031031032 scopus 로고    scopus 로고
    • Purification and substrate specificity of polydeoxyribonucleotide kinases isolated from calf thymus and rat liver
    • Karimi-Busheri F, Weinfeld M. 1997. Purification and substrate specificity of polydeoxyribonucleotide kinases isolated from calf thymus and rat liver. J Cell Biochem 64:258-272.
    • (1997) J Cell Biochem , vol.64 , pp. 258-272
    • Karimi-Busheri, F.1    Weinfeld, M.2
  • 27
    • 0032189831 scopus 로고    scopus 로고
    • Repair of DNA strand gaps and nicks containing 3′-phosphate and 5′-hydroxyl termini by purified mammalian enzymes
    • Karimi-Busheri F, Lee J, Tomkinson AE, Weinfeld M. 1998. Repair of DNA strand gaps and nicks containing 3′-phosphate and 5′-hydroxyl termini by purified mammalian enzymes. Nucleic Acids Res 26:4395-4400.
    • (1998) Nucleic Acids Res , vol.26 , pp. 4395-4400
    • Karimi-Busheri, F.1    Lee, J.2    Tomkinson, A.E.3    Weinfeld, M.4
  • 28
    • 0021969355 scopus 로고
    • Cloning of nascent monkey DNA synthesized early in the cell cycle
    • Kaufmann G, Zannis-Hadjopoulos M, Martin RG. 1985. Cloning of nascent monkey DNA synthesized early in the cell cycle. Mol Cell Biol 5:721-727.
    • (1985) Mol Cell Biol , vol.5 , pp. 721-727
    • Kaufmann, G.1    Zannis-Hadjopoulos, M.2    Martin, R.G.3
  • 29
    • 0025321141 scopus 로고
    • Related domains in yeast tRNA ligase, bacteriophage T4 polynucleotide kinase and RNA ligase, and mammalian myelin 2′,3′-cyclic nucleotide phosphohydrolase revealed by amino acid sequence comparison
    • Koonin EV, Gorbalenya AE. 1990. Related domains in yeast tRNA ligase, bacteriophage T4 polynucleotide kinase and RNA ligase, and mammalian myelin 2′,3′-cyclic nucleotide phosphohydrolase revealed by amino acid sequence comparison. FEBS Lett 268:231-234.
    • (1990) FEBS Lett , vol.268 , pp. 231-234
    • Koonin, E.V.1    Gorbalenya, A.E.2
  • 30
    • 0028116826 scopus 로고
    • Computer analysis of bacterial haloacid dehalogenases defines a large superfamily of hydrolases with diverse specificity
    • Koonin EV, Tatusov RL. 1994. Computer analysis of bacterial haloacid dehalogenases defines a large superfamily of hydrolases with diverse specificity. J Mol Biol 244:125-132.
    • (1994) J Mol Biol , vol.244 , pp. 125-132
    • Koonin, E.V.1    Tatusov, R.L.2
  • 31
    • 0014949207 scopus 로고
    • Cleavage of structural proteins during the assembly of the head of bacteriophage T4
    • Laemmli UK 1970) Cleavage of structural proteins during the assembly of the head of bacteriophage T4. Nature 227:680-685.
    • (1970) Nature , vol.227 , pp. 680-685
    • Laemmli, U.K.1
  • 32
    • 0016747439 scopus 로고
    • Oxygen-effect on strand breaks and specific end-groups in DNA of irradiated thymocytes
    • Lennartz M, Coquerelle T, Bopp A, Hagen U. 1975. Oxygen-effect on strand breaks and specific end-groups in DNA of irradiated thymocytes. Int J Radiat Biol 27:577-587.
    • (1975) Int J Radiat Biol , vol.27 , pp. 577-587
    • Lennartz, M.1    Coquerelle, T.2    Bopp, A.3    Hagen, U.4
  • 33
    • 0017225980 scopus 로고
    • A deoxyribonucleic acid kinase from nuclei of rat liver. Purification and properties
    • Levin CJ, Zimmerman SB. 1976. A deoxyribonucleic acid kinase from nuclei of rat liver. Purification and properties. J Biol Chem 251:1767-1774.
    • (1976) J Biol Chem , vol.251 , pp. 1767-1774
    • Levin, C.J.1    Zimmerman, S.B.2
  • 34
    • 0030991370 scopus 로고    scopus 로고
    • Detection of higher-order 50-and 10-kbp DNA fragments before apoptotic internucleosomal cleavage after transient cerebral ischemia
    • MacManus JP Rasquinha I, Tuor U, Preston E. 1997. Detection of higher-order 50-and 10-kbp DNA fragments before apoptotic internucleosomal cleavage after transient cerebral ischemia. J Cereb Blood Flow Metab 17:376-387.
    • (1997) J Cereb Blood Flow Metab , vol.17 , pp. 376-387
    • MacManus, J.P.1    Rasquinha, I.2    Tuor, U.3    Preston, E.4
  • 35
    • 0032032935 scopus 로고    scopus 로고
    • Oct-1 enhances the in vitro replication of a mammalian autonomously replicating sequence
    • Matheos DD, Ruiz MT, Price GB, Zannis-Hadjopoulos M. 1998. Oct-1 enhances the in vitro replication of a mammalian autonomously replicating sequence. J Cell Biochem 68:309-327.
    • (1998) J Cell Biochem , vol.68 , pp. 309-327
    • Matheos, D.D.1    Ruiz, M.T.2    Price, G.B.3    Zannis-Hadjopoulos, M.4
  • 36
    • 0022137932 scopus 로고
    • T4 polynucleotide kinase; cloning of the gene (pseT) and amplification of its product
    • Midgley CA, Murray NE. 1985. T4 polynucleotide kinase; cloning of the gene (pseT) and amplification of its product. EMBO J 4:2695-2703.
    • (1985) EMBO J , vol.4 , pp. 2695-2703
    • Midgley, C.A.1    Murray, N.E.2
  • 37
    • 0014027646 scopus 로고
    • The enzymatic phosphorylation of ribonucleic acid and deoxyribonucleic acid. I. Phosphorylation at 5′-hydroxyl termini
    • Novogrodsky A, Hurwitz J. 1966. The enzymatic phosphorylation of ribonucleic acid and deoxyribonucleic acid. I. Phosphorylation at 5′-hydroxyl termini. J Biol Chem 241:2923-2932.
    • (1966) J Biol Chem , vol.241 , pp. 2923-2932
    • Novogrodsky, A.1    Hurwitz, J.2
  • 38
    • 0014027742 scopus 로고
    • The enzymatic phosphorylation of ribonucleic acid and deoxyribonucleic acid. II. Further properties of the 5′-hydroxyl polynucleotide kinase
    • Novogrodsky A, Tal M, Traub A, Hurwitz J. 1966. The enzymatic phosphorylation of ribonucleic acid and deoxyribonucleic acid. II. Further properties of the 5′-hydroxyl polynucleotide kinase J Biol Chem 241:2933-2943.
    • (1966) J Biol Chem , vol.241 , pp. 2933-2943
    • Novogrodsky, A.1    Tal, M.2    Traub, A.3    Hurwitz, J.4
  • 39
    • 0025946276 scopus 로고
    • Plasmids bearing mammalian DNA-replication origin-enriched (ors) fragments initiate semiconservative replication in a cell-free system
    • Pearson CE, Frappier L, Zannis-Hadjopoulos M. 1991. Plasmids bearing mammalian DNA-replication origin-enriched (ors) fragments initiate semiconservative replication in a cell-free system. Biochim Biophys Acta 1090:156-166.
    • (1991) Biochim Biophys Acta , vol.1090 , pp. 156-166
    • Pearson, C.E.1    Frappier, L.2    Zannis-Hadjopoulos, M.3
  • 40
    • 0020494636 scopus 로고
    • 3′-Phosphatase activity of the DNA kinase from rat liver
    • Pheiffer BH, Zimmerman SB. 1982. 3′-Phosphatase activity of the DNA kinase from rat liver. Biochem Biophys Res Commun 109:1297-1302.
    • (1982) Biochem Biophys Res Commun , vol.109 , pp. 1297-1302
    • Pheiffer, B.H.1    Zimmerman, S.B.2
  • 41
    • 0027392502 scopus 로고
    • Pre-tRNA splicing: Variation on a theme or exception to the rule?
    • Phizicky EM, Greer CL. 1993. Pre-tRNA splicing: Variation on a theme or exception to the rule? Trends Biochem Sci 18:31-34.
    • (1993) Trends Biochem Sci , vol.18 , pp. 31-34
    • Phizicky, E.M.1    Greer, C.L.2
  • 42
    • 0029968417 scopus 로고    scopus 로고
    • Phosphorylation of Okazaki-like DNA fragments in mammalian cells and role of polyamines in the processing of this DNA
    • Pohjanpelto P, Hölttä E. 1996. Phosphorylation of Okazaki-like DNA fragments in mammalian cells and role of polyamines in the processing of this DNA. EMBO J 15:1193-1200.
    • (1996) EMBO J , vol.15 , pp. 1193-1200
    • Pohjanpelto, P.1    Hölttä, E.2
  • 43
    • 0029033390 scopus 로고
    • 5′ phosphorylation of DNA in mammalian cells: Identification of a polymin P-precipitable polynucleotide kinase
    • Prinos P, Slack C, Lasko, DD. 1995. 5′ phosphorylation of DNA in mammalian cells: Identification of a polymin P-precipitable polynucleotide kinase. J Cell Biochem 58: 115-131.
    • (1995) J Cell Biochem , vol.58 , pp. 115-131
    • Prinos, P.1    Slack, C.2    Lasko, D.D.3
  • 45
    • 0013791279 scopus 로고
    • Phosphorylation of nucleic acid by an enzyme from T4 bacteriophage-infected E. coli
    • Richardson CC. 1965. Phosphorylation of nucleic acid by an enzyme from T4 bacteriophage-infected E. coli. Proc Natl Acad Sci USA 54:158-165.
    • (1965) Proc Natl Acad Sci USA , vol.54 , pp. 158-165
    • Richardson, C.C.1
  • 46
    • 77956897435 scopus 로고
    • Bacteriophage T4 polynucleotide kinase
    • Boyer PD, editor. New York: Academic Press
    • Richardson CC. 1981. Bacteriophage T4 polynucleotide kinase. In: Boyer PD, editor. The enzymes, Vol XIV. New York: Academic Press, p 299-314.
    • (1981) The Enzymes , vol.14 , pp. 299-314
    • Richardson, C.C.1
  • 49
    • 0030297538 scopus 로고    scopus 로고
    • tRNA ligase is required for regulated mRNA splicing in the unfolded protein response
    • Sidrauski C, Cox JS, Walter P. 1996. tRNA ligase is required for regulated mRNA splicing in the unfolded protein response. Cell 87:405-413.
    • (1996) Cell , vol.87 , pp. 405-413
    • Sidrauski, C.1    Cox, J.S.2    Walter, P.3
  • 50
    • 0030954870 scopus 로고    scopus 로고
    • The transmembrane kinase Ire1p is a site-specific endonuclease that initiates mRNA splicing in the unfolded protein response
    • Sidrauski C, Walter P. 1997. The transmembrane kinase Ire1p is a site-specific endonuclease that initiates mRNA splicing in the unfolded protein response. Cell 90:1031-1039.
    • (1997) Cell , vol.90 , pp. 1031-1039
    • Sidrauski, C.1    Walter, P.2
  • 51
    • 0018098860 scopus 로고
    • A role in true-late gene expression for the bacteriophage 5′ polynucleotide kinase 3′-phosphatase
    • Sirotkin K, Cooley W, Runnels JM, Snyder L. 1978. A role in true-late gene expression for the bacteriophage 5′ polynucleotide kinase 3′-phosphatase. J Mol Biol 123:221-233.
    • (1978) J Mol Biol , vol.123 , pp. 221-233
    • Sirotkin, K.1    Cooley, W.2    Runnels, J.M.3    Snyder, L.4
  • 52
    • 0018801475 scopus 로고
    • 5′-hydroxyl polyribonucleotide kinase from HeLa cell nuclei
    • Shuman S, Hurwitz J. 1979. 5′-hydroxyl polyribonucleotide kinase from HeLa cell nuclei. J Biol Chem 254:10396-10404.
    • (1979) J Biol Chem , vol.254 , pp. 10396-10404
    • Shuman, S.1    Hurwitz, J.2
  • 53
    • 0004056014 scopus 로고
    • T4 polynucleotide kinase and RNA ligase
    • Mathews CK, Kutter EM, Mosig G, Berget PB, editors. Washington, DC: American Society for Microbiology
    • Snyder L. 1983. T4 polynucleotide kinase and RNA ligase. In: Mathews CK, Kutter EM, Mosig G, Berget PB, editors. Bacteriophage T4. Washington, DC: American Society for Microbiology, p 351-355.
    • (1983) Bacteriophage T4 , pp. 351-355
    • Snyder, L.1
  • 54
    • 0019559633 scopus 로고
    • Characterization of DNA kinase from calf thymus
    • Tamura S, Teraoka H, Tsukada K. 1981. Characterization of DNA kinase from calf thymus. Eur J Biochem 115:449-453.
    • (1981) Eur J Biochem , vol.115 , pp. 449-453
    • Tamura, S.1    Teraoka, H.2    Tsukada, K.3
  • 55
    • 0016776738 scopus 로고
    • Polynucleotide kinase from rat-liver nuclei. Purification and properties
    • Teraoka H, Mizuta K, Sato F, Shimoyachi M, Tsukada K. 1975. Polynucleotide kinase from rat-liver nuclei. Purification and properties. Eur J Biochem 58:297-302.
    • (1975) Eur J Biochem , vol.58 , pp. 297-302
    • Teraoka, H.1    Mizuta, K.2    Sato, F.3    Shimoyachi, M.4    Tsukada, K.5
  • 56
    • 0027968068 scopus 로고
    • Clustal W: Improving the sensitivity of progressive multiple sequence alignment through sequence weighting, position-specific gap penalties, and weight matrix choices
    • Thompson JD, Higgins DG, Gibson TJ. 1994. Clustal W: Improving the sensitivity of progressive multiple sequence alignment through sequence weighting, position-specific gap penalties, and weight matrix choices. Nucleic Acids Res 22:4673-4680.
    • (1994) Nucleic Acids Res , vol.22 , pp. 4673-4680
    • Thompson, J.D.1    Higgins, D.G.2    Gibson, T.J.3
  • 57
    • 0028797949 scopus 로고
    • Analysis by deletion mutagenesis of minimal sequence requirements for autonomous replication of ors8, a monkey early-replicating DNA sequence
    • Todd A, Landry S, Pearson CE, Khoury V, Zannis-Hadjopoulos M. 1995. Analysis by deletion mutagenesis of minimal sequence requirements for autonomous replication of ors8, a monkey early-replicating DNA sequence. J Cell Biochem 57:280-289.
    • (1995) J Cell Biochem , vol.57 , pp. 280-289
    • Todd, A.1    Landry, S.2    Pearson, C.E.3    Khoury, V.4    Zannis-Hadjopoulos, M.5
  • 58
    • 0030569504 scopus 로고    scopus 로고
    • Replication factor C recognizes 5′ phosphate ends of telomeres
    • Uchiumi F, Ohta T, Tanuma S. 1996. Replication factor C recognizes 5′ phosphate ends of telomeres. Biochem Biophys Res Commun 229:310-315.
    • (1996) Biochem Biophys Res Commun , vol.229 , pp. 310-315
    • Uchiumi, F.1    Ohta, T.2    Tanuma, S.3
  • 59
    • 0028337685 scopus 로고
    • Anatomy of a DNA replication fork revealed by reconstitution of SV40 DNA replication in vitro
    • Waga S, Stillman B. 1994. Anatomy of a DNA replication fork revealed by reconstitution of SV40 DNA replication in vitro. Nature 369:207-212.
    • (1994) Nature , vol.369 , pp. 207-212
    • Waga, S.1    Stillman, B.2
  • 60
    • 0020106807 scopus 로고
    • Nuclear ligation of RNA 5′ OH kinase products in tRNA
    • Winocov I, Button JD. 1982. Nuclear ligation of RNA 5′ OH kinase products in tRNA. Mol Cell Biol 2:241-249.
    • (1982) Mol Cell Biol , vol.2 , pp. 241-249
    • Winocov, I.1    Button, J.D.2
  • 63
    • 77956945636 scopus 로고
    • Eukaryotic DNA kinase
    • Boyer PD, editor. New York: Academic Press
    • Zimmerman SB, Pheiffer BH. 1981. Eukaryotic DNA kinase. In: Boyer PD, editor. The enzymes, Vol. XIV. New York: Academic Press, p 315-329.
    • (1981) The Enzymes , vol.14 , pp. 315-329
    • Zimmerman, S.B.1    Pheiffer, B.H.2


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.