메뉴 건너뛰기




Volumn 100, Issue 1, 1998, Pages 1-16

Effect of a 3'→5' exonuclease with a proofreading function on the fidelity of error-prone DNA polymerase α from regenerating liver of aged rats

Author keywords

3' 5' exonuclease; DNA polymerase; DNA replication; Eukaryote; Fidelity of DNA synthesis; Proofreading

Indexed keywords

DEOXYRIBONUCLEASE; DNA DIRECTED DNA POLYMERASE ALPHA; DNA DIRECTED DNA POLYMERASE BETA; EXONUCLEASE; LIVER EXTRACT; MAGNESIUM CHLORIDE; MANGANESE CHLORIDE; NUCLEASE; NUCLEOTIDE; PHOSPHORUS 32; EXODEOXYRIBONUCLEASE; EXODEOXYRIBONUCLEASE V;

EID: 0032509564     PISSN: 00476374     EISSN: None     Source Type: Journal    
DOI: 10.1016/S0047-6374(97)00114-0     Document Type: Article
Times cited : (9)

References (55)
  • 1
    • 0017749060 scopus 로고
    • Recent excitement in the DNA replication problem
    • Alberts B., Sternglanz R. Recent excitement in the DNA replication problem. Nature. 269:1977;655-661.
    • (1977) Nature , vol.269 , pp. 655-661
    • Alberts, B.1    Sternglanz, R.2
  • 2
    • 0027471443 scopus 로고
    • An error-correcting proofreading exonuclease-polymerase that copurifies with DNA-polymerase-α-primase
    • Bialek G., Grosse F. An error-correcting proofreading exonuclease-polymerase that copurifies with DNA-polymerase-α-primase. J. Biol. Chem. 268:1993;6024-6033.
    • (1993) J. Biol. Chem. , vol.268 , pp. 6024-6033
    • Bialek, G.1    Grosse, F.2
  • 3
    • 0024468469 scopus 로고
    • Exonucleolytic proofreading increases the accuracy of DNA synthesis by human lymphocyte DNA polymerase α-DNA primase
    • Bialek G., Nasheuer H.-P., Goetz H., Grosse F. Exonucleolytic proofreading increases the accuracy of DNA synthesis by human lymphocyte DNA polymerase α-DNA primase. EMBO J. 8:1989;1883-1889.
    • (1989) EMBO J. , vol.8 , pp. 1883-1889
    • Bialek, G.1    Nasheuer, H.-P.2    Goetz, H.3    Grosse, F.4
  • 4
    • 0015499993 scopus 로고
    • Enzymatic synthesis of deoxyribonucleic acid. XXXVI. A proofreading function for the 3′→5′ exonuclease activity in deoxyribonucleic acid polymerases
    • Brutlug D., Kornberg A. Enzymatic synthesis of deoxyribonucleic acid. XXXVI. A proofreading function for the 3′→5′ exonuclease activity in deoxyribonucleic acid polymerases. J. Biol. Chem. 247:1972;241-248.
    • (1972) J. Biol. Chem. , vol.247 , pp. 241-248
    • Brutlug, D.1    Kornberg, A.2
  • 5
    • 0017169587 scopus 로고
    • A new mammalian DNA polymerase with 3′ to 5′ exonuclease activity: DNA polymerase δ
    • Byrnes J.J., Downey K.M., Black V.L., So A.G. A new mammalian DNA polymerase with 3′ to 5′ exonuclease activity: DNA polymerase δ Biochemistry. 15:1976;2817-2823.
    • (1976) Biochemistry , vol.15 , pp. 2817-2823
    • Byrnes, J.J.1    Downey, K.M.2    Black, V.L.3    So, A.G.4
  • 6
    • 0021835802 scopus 로고
    • DNase VII of human placenta: Mechanism studies
    • Chen G.L., Grossman L. DNase VII of human placenta: mechanism studies. J. Biol. Chem. 260:1985;5073-5080.
    • (1985) J. Biol. Chem. , vol.260 , pp. 5073-5080
    • Chen, G.L.1    Grossman, L.2
  • 7
    • 0018801559 scopus 로고
    • Mouse DNA polymerase α: Subunit structure and identification of a species with associated exonuclease J
    • Chen Y.-C., Bohn E.W., Planck S.R., Wilson S.H. Mouse DNA polymerase α: subunit structure and identification of a species with associated exonuclease J. Biol. Chem. 254:1979;11678-11687.
    • (1979) Biol. Chem. , vol.254 , pp. 11678-11687
    • Chen, Y.-C.1    Bohn, E.W.2    Planck, S.R.3    Wilson, S.H.4
  • 8
    • 0022614929 scopus 로고
    • Heteroduplex deoxyribonucleic acid base mismatch repair in bacteria
    • Claverys J.-P., Lacks S.A. Heteroduplex deoxyribonucleic acid base mismatch repair in bacteria. Microbiol. Rev. 50:1986;133-165.
    • (1986) Microbiol. Rev. , vol.50 , pp. 133-165
    • Claverys, J.-P.1    Lacks, S.A.2
  • 9
    • 0021333232 scopus 로고
    • The interaction of DNA polymerase III and the product of the Escherichia coli mutator gene, mutD
    • DiFrancesco R., Bhatnagar S.K., Brown A., Bessman M.J. The interaction of DNA polymerase III and the product of the Escherichia coli mutator gene, mutD. J. Biol. Chem. 259:1984;5567-5573.
    • (1984) J. Biol. Chem. , vol.259 , pp. 5567-5573
    • Difrancesco, R.1    Bhatnagar, S.K.2    Brown, A.3    Bessman, M.J.4
  • 10
    • 36949055511 scopus 로고
    • Comparaaative rates of spontaneous mutation
    • Drake J.W. Comparaaative rates of spontaneous mutation. Nature. 221:1969;1132.
    • (1969) Nature , vol.221 , pp. 1132
    • Drake, J.W.1
  • 11
    • 0024299216 scopus 로고
    • Do DNA polymerases δ and α act coordinately as leading and lagging strand replicases?
    • Focher F., Ferrari E., Spadari S., Hubscher U. Do DNA polymerases δ and α act coordinately as leading and lagging strand replicases? FEBS Lett. 229:1988;6-10.
    • (1988) FEBS Lett. , vol.229 , pp. 6-10
    • Focher, F.1    Ferrari, E.2    Spadari, S.3    Hubscher, U.4
  • 12
    • 0016292997 scopus 로고
    • Mutational specificity of a conditional Escherichia coli mutator, mutD5
    • Fowler R.G., Degnen G.E., Cox E.C. Mutational specificity of a conditional Escherichia coli mutator, mutD5. Mol. Gen. Genet. 133:1974;179-191.
    • (1974) Mol. Gen. Genet. , vol.133 , pp. 179-191
    • Fowler, R.G.1    Degnen, G.E.2    Cox, E.C.3
  • 13
    • 0023661092 scopus 로고
    • Identification of DNA polymerase δ in CV-1 cells: Studies implicating both DNA polymerase δ and DNA polymerase α in DNA replication
    • Hammond R.A., Byrnes J.J., Miller M.R. Identification of DNA polymerase δ in CV-1 cells: studies implicating both DNA polymerase δ and DNA polymerase α in DNA replication. Biochemistry. 26:1987;6817-6824.
    • (1987) Biochemistry , vol.26 , pp. 6817-6824
    • Hammond, R.A.1    Byrnes, J.J.2    Miller, M.R.3
  • 14
    • 0025162255 scopus 로고
    • Effect of DNA polymerase inhibitors on DNA repair in intact and permeable human fibroblasts: Evidence that DNA polymerase δ and β are involved in DNA repair synthesis induced N-methyl-N′-nitro-N-nitrosoguanidine
    • Hammond R.A., McClung J.K., Miller M.R. Effect of DNA polymerase inhibitors on DNA repair in intact and permeable human fibroblasts: evidence that DNA polymerase δ and β are involved in DNA repair synthesis induced N-methyl-N′-nitro-N-nitrosoguanidine. Biochemistry. 29:1990;286-291.
    • (1990) Biochemistry , vol.29 , pp. 286-291
    • Hammond, R.A.1    McClung, J.K.2    Miller, M.R.3
  • 15
    • 0019835717 scopus 로고
    • Purification and characterization of DNase VII, a 3′→5′-directed exonuclease from human placenta
    • Hollis G.F., Grossman L. Purification and characterization of DNase VII, a 3′→5′-directed exonuclease from human placenta. J. Biol. Chem. 256:1981;8074-8079.
    • (1981) J. Biol. Chem. , vol.256 , pp. 8074-8079
    • Hollis, G.F.1    Grossman, L.2
  • 16
    • 0015523028 scopus 로고
    • On the exonuclease activity of phage T4 deoxyribonucleic acid polymerase
    • Huang W.M., Lehman I.R. On the exonuclease activity of phage T4 deoxyribonucleic acid polymerase. J. Biol. Chem. 247:1972;3139-3146.
    • (1972) J. Biol. Chem. , vol.247 , pp. 3139-3146
    • Huang, W.M.1    Lehman, I.R.2
  • 17
    • 0023657423 scopus 로고
    • Eukaryotic DNA replication: A complex picture partially clarified
    • Huberman J.A. Eukaryotic DNA replication: a complex picture partially clarified. Cell. 48:1987;7-8.
    • (1987) Cell , vol.48 , pp. 7-8
    • Huberman, J.A.1
  • 18
    • 0021174104 scopus 로고
    • The DNA polymerase-primase from Drosophila melanogaster embryos: Rate and fidelity of polymerization on single-stranded DNA templates
    • Kaguni L.S., DiFrancesco R.A., Lehman I.R. The DNA polymerase-primase from Drosophila melanogaster embryos: rate and fidelity of polymerization on single-stranded DNA templates. J. Biol. Chem. 259:1984;9314-9319.
    • (1984) J. Biol. Chem. , vol.259 , pp. 9314-9319
    • Kaguni, L.S.1    Difrancesco, R.A.2    Lehman, I.R.3
  • 20
    • 0003890119 scopus 로고
    • W.H. Freeman, San Francisco
    • Kornberg, A., 1980. DNA replication. W.H. Freeman, San Francisco, pp. 101-200.
    • (1980) DNA Replication , pp. 101-200
    • Kornberg, A.1
  • 21
    • 0019861198 scopus 로고
    • Fidelity of mammalian DNA polymerases
    • Kunkel T.A., Loeb L.A. Fidelity of mammalian DNA polymerases. Science. 213:1981;765-767.
    • (1981) Science , vol.213 , pp. 765-767
    • Kunkel, T.A.1    Loeb, L.A.2
  • 23
    • 0023121219 scopus 로고
    • Human placental DNA polymerase δ: Identification of a 170-kilodalton polypeptide by activity staining and immunoblotting
    • Lee M.Y.W.T., Toomey N.L. Human placental DNA polymerase δ: identification of a 170-kilodalton polypeptide by activity staining and immunoblotting. Biochemistry. 26:1987;1076-1085.
    • (1987) Biochemistry , vol.26 , pp. 1076-1085
    • Lee, M.Y.W.T.1    Toomey, N.L.2
  • 24
    • 0005913439 scopus 로고
    • Synthesis of DNA containing the simian virus 40 origin of replication by the combined action of DNA polymerase α and δ
    • Lee S.-H., Eki T., Hurwitz J. Synthesis of DNA containing the simian virus 40 origin of replication by the combined action of DNA polymerase α and δ Proc. Natl. Acad. Sci. USA. 86:1989;7361-7365.
    • (1989) Proc. Natl. Acad. Sci. USA , vol.86 , pp. 7361-7365
    • Lee, S.-H.1    Eki, T.2    Hurwitz, J.3
  • 25
    • 0014690918 scopus 로고
    • Properties of deoxyribonuclease III from mammalian tissues
    • Lindahl T., Gally J.A., Edelman G.M. Properties of deoxyribonuclease III from mammalian tissues. J. Biol. Chem. 244:1969;5014-5019.
    • (1969) J. Biol. Chem. , vol.244 , pp. 5014-5019
    • Lindahl, T.1    Gally, J.A.2    Edelman, G.M.3
  • 27
    • 0016719055 scopus 로고
    • Nuclear deoxyribonucleic acid polymerases of liver
    • Lynch W.E., Surrey S., Lieberman I. Nuclear deoxyribonucleic acid polymerases of liver. J. Biol. Chem. 250:1975;8179-8183.
    • (1975) J. Biol. Chem. , vol.250 , pp. 8179-8183
    • Lynch, W.E.1    Surrey, S.2    Lieberman, I.3
  • 28
    • 0023369230 scopus 로고
    • Proofreading by DNA polymerase III of Escherichia coli depends on cooperative interaction of the polymerase and exonuclease subunit
    • Maki H., Kornberg A. Proofreading by DNA polymerase III of Escherichia coli depends on cooperative interaction of the polymerase and exonuclease subunit. Proc. Natl. Acad. Sci. USA. 84:1987;4389-4392.
    • (1987) Proc. Natl. Acad. Sci. USA , vol.84 , pp. 4389-4392
    • Maki, H.1    Kornberg, A.2
  • 29
    • 0021041357 scopus 로고
    • Structure and expression of the dnaQ mutator and the RNase H genes of Escherichia coli: Overlap of the promorter regions
    • Maki H., Horiuchi T., Sekiguchi M. Structure and expression of the dnaQ mutator and the RNase H genes of Escherichia coli: overlap of the promorter regions. Proc. Natl. Acad. Sci. USA. 80:1983;7137-7141.
    • (1983) Proc. Natl. Acad. Sci. USA , vol.80 , pp. 7137-7141
    • Maki, H.1    Horiuchi, T.2    Sekiguchi, M.3
  • 30
    • 0023517589 scopus 로고
    • Cell cycle dependent activities of DNA polymerase α and δ in chinese hamster ovary cells
    • Marraccino R.L., Wahl A.F., Keng P.C., Lord E.M., Bambara R.A. Cell cycle dependent activities of DNA polymerase α and δ in chinese hamster ovary cells. Biochemistry. 26:1987;7864-7870.
    • (1987) Biochemistry , vol.26 , pp. 7864-7870
    • Marraccino, R.L.1    Wahl, A.F.2    Keng, P.C.3    Lord, E.M.4    Bambara, R.A.5
  • 31
    • 0018786252 scopus 로고
    • DNA polymerase III of Escherichia coli: Purification and identification of subunits
    • McHenry C., Crow W. DNA polymerase III of Escherichia coli: purification and identification of subunits. J. Biol. Chem. 254:1979;1748-1753.
    • (1979) J. Biol. Chem. , vol.254 , pp. 1748-1753
    • McHenry, C.1    Crow, W.2
  • 32
    • 0019320874 scopus 로고
    • Eukaryotic DNA polymerase a: Structural analysis of the enzyme from regenerating rat liver
    • Mechali M., Abadiedebat J., Recondo A.-M. Eukaryotic DNA polymerase a: structural analysis of the enzyme from regenerating rat liver. J. Biol. Chem. 255:1980;2114-2122.
    • (1980) J. Biol. Chem. , vol.255 , pp. 2114-2122
    • Mechali, M.1    Abadiedebat, J.2    Recondo, A.-M.3
  • 33
    • 0015530249 scopus 로고
    • 1 ribonuclease digestion by gel electrophoresis and two-dimensional thin-layer chromatography
    • 1 ribonuclease digestion by gel electrophoresis and two-dimensional thin-layer chromatography. J. Mol. Biol. 72:1972;633-643.
    • (1972) J. Mol. Biol. , vol.72 , pp. 633-643
    • Mirzabekov, A.D.1    Griffin, B.E.2
  • 34
    • 0019182084 scopus 로고
    • Interaction of mammalian deoxyribonuclease V, a double strand 3′→5′ and 5′→3′ exonuclease, with deoxyribonucleic acid polymerase-β From the Novikoff hepatoma
    • Mosbaugh D.W., Meyer R.R. Interaction of mammalian deoxyribonuclease V, a double strand 3′→5′ and 5′→3′ exonuclease, with deoxyribonucleic acid polymerase-β from the Novikoff hepatoma. J. Biol. Chem. 255:1980;10239-10247.
    • (1980) J. Biol. Chem. , vol.255 , pp. 10239-10247
    • Mosbaugh, D.W.1    Meyer, R.R.2
  • 35
    • 0019880374 scopus 로고
    • Increased error frequency of DNA polymerases from senescent human fibroblasts
    • Murray V., Holliday R. Increased error frequency of DNA polymerases from senescent human fibroblasts. J. Mol. Biol. 146:1981;55-76.
    • (1981) J. Mol. Biol. , vol.146 , pp. 55-76
    • Murray, V.1    Holliday, R.2
  • 36
    • 0021131819 scopus 로고
    • Mammalian DNA polymerase α holoenzymes with possible functions at the leading and lagging strand of the replication fork
    • Ottiger H.-P., Hubscher U. Mammalian DNA polymerase α holoenzymes with possible functions at the leading and lagging strand of the replication fork. Proc. Natl. Acad. Sci. USA. 81:1984;3993-3997.
    • (1984) Proc. Natl. Acad. Sci. USA , vol.81 , pp. 3993-3997
    • Ottiger, H.-P.1    Hubscher, U.2
  • 38
    • 0028338562 scopus 로고
    • Studies of gapped DNA substrate binding by mammalian DNA polymerase β: Dependence on 5′-phosphate group
    • Prasad R., Beard W.A., Wilson S.H. Studies of gapped DNA substrate binding by mammalian DNA polymerase β: dependence on 5′-phosphate group. J. Biol. Chem. 269:1994;18096-18101.
    • (1994) J. Biol. Chem. , vol.269 , pp. 18096-18101
    • Prasad, R.1    Beard, W.A.2    Wilson, S.H.3
  • 39
    • 0017775949 scopus 로고
    • Studies on the biochemical basis of mutation: Effect of amino acid substitution on the enzymatic and biological properties of bacteriophage T4 DNA polymerase
    • Reha-Krantz L.J., Bessman M.J. Studies on the biochemical basis of mutation: effect of amino acid substitution on the enzymatic and biological properties of bacteriophage T4 DNA polymerase. J. Mol. Biol. 116:1977;99-113.
    • (1977) J. Mol. Biol. , vol.116 , pp. 99-113
    • Reha-Krantz, L.J.1    Bessman, M.J.2
  • 40
    • 0020981110 scopus 로고
    • Identification of the ε-subunit of Escherichia coli DNA polymerase III holoenzyme as the dnaQ gene product: A fidelity subunit for DNA replication
    • Scheuermann R., Tam S., Burgers P.M.J., Lu C., Echols H. Identification of the ε-subunit of Escherichia coli DNA polymerase III holoenzyme as the dnaQ gene product: a fidelity subunit for DNA replication. Proc. Natl. Acad. Sci. USA. 80:1983;7085-7089.
    • (1983) Proc. Natl. Acad. Sci. USA , vol.80 , pp. 7085-7089
    • Scheuermann, R.1    Tam, S.2    Burgers, P.M.J.3    Lu, C.4    Echols, H.5
  • 41
    • 0015499898 scopus 로고
    • Deoxyribonucleic acid polymerase: Two distinct enzymes in one polypeptide. I. A proteolytic fragment containing the polymerase and 3′→5′ exonuclease functions
    • Setlow P., Brutrug D., Kornberg A. Deoxyribonucleic acid polymerase: Two distinct enzymes in one polypeptide. I. A proteolytic fragment containing the polymerase and 3′→5′ exonuclease functions. J. Biol. Chem. 247:1972;224-231.
    • (1972) J. Biol. Chem. , vol.247 , pp. 224-231
    • Setlow, P.1    Brutrug, D.2    Kornberg, A.3
  • 42
    • 0028966181 scopus 로고
    • DNA polymerase β conducts the gap-filling step in uracil-initiated base excision repair in a bovine testis nuclear extract
    • Singhal R.K., Prasad R., Wilson S.M. DNA polymerase β conducts the gap-filling step in uracil-initiated base excision repair in a bovine testis nuclear extract. J. Biol. Chem. 270:1995;949-957.
    • (1995) J. Biol. Chem. , vol.270 , pp. 949-957
    • Singhal, R.K.1    Prasad, R.2    Wilson, S.M.3
  • 43
    • 0022971471 scopus 로고
    • Exonuclease activity associated with a multiprotein form of HeLa cell DNA polymerase α
    • Skarnes W., Bonin P., Baril E. Exonuclease activity associated with a multiprotein form of HeLa cell DNA polymerase α J. Biol. Chem. 261:1986;6629-6636.
    • (1986) J. Biol. Chem. , vol.261 , pp. 6629-6636
    • Skarnes, W.1    Bonin, P.2    Baril, E.3
  • 44
    • 0024298834 scopus 로고
    • Mammalian DNA polymerase α and δ: Current status in DNA replication
    • So A.G., Downey K.M. Mammalian DNA polymerase α and δ: current status in DNA replication. Biochemistry. 27:1988;4591-4595.
    • (1988) Biochemistry , vol.27 , pp. 4591-4595
    • So, A.G.1    Downey, K.M.2
  • 45
    • 0026662688 scopus 로고
    • Effects of aging and dietary restriction on DNA polymerases: Gene expression, enzyme fidelity, and DNA excision repair
    • Srivastava V., Tilley R., Miller S., Hart R., Busbee D. Effects of aging and dietary restriction on DNA polymerases: gene expression, enzyme fidelity, and DNA excision repair. Exp. Gerontol. 27:1992;593-613.
    • (1992) Exp. Gerontol. , vol.27 , pp. 593-613
    • Srivastava, V.1    Tilley, R.2    Miller, S.3    Hart, R.4    Busbee, D.5
  • 46
    • 0030595976 scopus 로고    scopus 로고
    • Age-associated changes in the template-reading fidelity of DNA polymerase α from regenerating rat liver
    • Taguchi T., Ohashi M. Age-associated changes in the template-reading fidelity of DNA polymerase α from regenerating rat liver. Mech. Ageing Dev. 92:1996;143-157.
    • (1996) Mech. Ageing Dev. , vol.92 , pp. 143-157
    • Taguchi, T.1    Ohashi, M.2
  • 48
    • 0024851541 scopus 로고
    • Multiple replication factors augment DNA synthesis by the two eukaryotic DNA polymerases, α and δ
    • Tsurimoto T., Stillman B. Multiple replication factors augment DNA synthesis by the two eukaryotic DNA polymerases, α and δ EMBO J. 8:1989;3883-3889.
    • (1989) EMBO J. , vol.8 , pp. 3883-3889
    • Tsurimoto, T.1    Stillman, B.2
  • 49
    • 0018098754 scopus 로고
    • Mechanism of ultraviolet-induced mutagenesis: Extent and fidelity of in vitro DNA synthesis on irradiated templates
    • Villani G., Boiteux S., Radman M. Mechanism of ultraviolet-induced mutagenesis: extent and fidelity of in vitro DNA synthesis on irradiated templates. Proc. Natl. Acad. Sci. USA. 75:1978;3037-3041.
    • (1978) Proc. Natl. Acad. Sci. USA , vol.75 , pp. 3037-3041
    • Villani, G.1    Boiteux, S.2    Radman, M.3
  • 50
    • 0022973861 scopus 로고
    • A multiprotein form of DNA polymerase α from HeLa cells: Resolution of its associated catalytic activities
    • Vishwanatha J.K., Coughlin S.A., Wesolowski-Owen M., Baril E.F. A multiprotein form of DNA polymerase α from HeLa cells: resolution of its associated catalytic activities. J. Biol. Chem. 261:1986;6619-6628.
    • (1986) J. Biol. Chem. , vol.261 , pp. 6619-6628
    • Vishwanatha, J.K.1    Coughlin, S.A.2    Wesolowski-Owen, M.3    Baril, E.F.4
  • 51
    • 0345975560 scopus 로고
    • Hypermutation at the immunoglobulin heavy chain locus in a pre-B-cell line
    • Wabl M., Burrows P.D., Gabain A., Steinberg C. Hypermutation at the immunoglobulin heavy chain locus in a pre-B-cell line. Proc. Natl. Acad. Sci. USA. 82:1985;479-482.
    • (1985) Proc. Natl. Acad. Sci. USA , vol.82 , pp. 479-482
    • Wabl, M.1    Burrows, P.D.2    Gabain, A.3    Steinberg, C.4
  • 52
    • 0028337685 scopus 로고
    • Anatomy of a DNA replication fork revealed by reconstitution of SV 40 DNA replication in vitro
    • Waga S., Stillman B. Anatomy of a DNA replication fork revealed by reconstitution of SV 40 DNA replication in vitro. Nature. 369:1994;207-212.
    • (1994) Nature , vol.369 , pp. 207-212
    • Waga, S.1    Stillman, B.2
  • 53
    • 0015991771 scopus 로고
    • Nuclear deoxyribonucleic acid polymerase: Purification and properties of the homogeneous enzyme from human KB cells
    • Wang T.S.-F., Sedwick W.D., Korn D. Nuclear deoxyribonucleic acid polymerase: purification and properties of the homogeneous enzyme from human KB cells. J. Biol. Chem. 249:1974;841-850.
    • (1974) J. Biol. Chem. , vol.249 , pp. 841-850
    • Wang, T.S.-F.1    Sedwick, W.D.2    Korn, D.3


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.