메뉴 건너뛰기




Volumn 6, Issue 11, 2007, Pages 1629-1641

Human endonuclease VIII-like (NEIL) proteins in the giant DNA Mimivirus

Author keywords

Endonuclease VIII like; Human NEIL1; Mimivirus; Oxidative DNA damage

Indexed keywords

5',2 DEOXYRIBOSE 5 PHOSPHATE LYASE; DNA FORMAMIDOPYRIMIDINE GLYCOSYLASE; ENDONUCLEASE; ENDONUCLEASE VIII; HYDANTOIN; LYASE; NEIL1 PROTEIN; SINGLE STRANDED DNA; UNCLASSIFIED DRUG;

EID: 35348954360     PISSN: 15687864     EISSN: None     Source Type: Journal    
DOI: 10.1016/j.dnarep.2007.05.011     Document Type: Article
Times cited : (37)

References (52)
  • 1
    • 0030861915 scopus 로고    scopus 로고
    • DNA glycosylases in the base excision repair of DNA
    • Krokan H.E., Standal R., and Slupphaug G. DNA glycosylases in the base excision repair of DNA. Biochem. J. 325 Pt 1 (1997) 1-16
    • (1997) Biochem. J. , vol.325 , Issue.PART 1 , pp. 1-16
    • Krokan, H.E.1    Standal, R.2    Slupphaug, G.3
  • 2
    • 0032836651 scopus 로고    scopus 로고
    • Initiation of base excision repair: glycosylase mechanisms and structures
    • McCullough A.K., Dodson M.L., and Lloyd R.S. Initiation of base excision repair: glycosylase mechanisms and structures. Annu. Rev. Biochem. 68 (1999) 255-285
    • (1999) Annu. Rev. Biochem. , vol.68 , pp. 255-285
    • McCullough, A.K.1    Dodson, M.L.2    Lloyd, R.S.3
  • 4
    • 0001473891 scopus 로고    scopus 로고
    • Chemistry of glycosylases and endonucleases involved in base-excision repair
    • David S.S., and Williams S.D. Chemistry of glycosylases and endonucleases involved in base-excision repair. Chem. Rev. 98 (1998) 1221-1262
    • (1998) Chem. Rev. , vol.98 , pp. 1221-1262
    • David, S.S.1    Williams, S.D.2
  • 5
    • 0033610478 scopus 로고    scopus 로고
    • Mechanism-based DNA-protein cross-linking of MutY via oxidation of 8-oxoguanosine (communication)
    • Hickerson R.P., Chepanoske C.L., Williams S.D., David S.S., and Burrows C.J. Mechanism-based DNA-protein cross-linking of MutY via oxidation of 8-oxoguanosine (communication). J. Am. Chem. Soc. 121 (1999) 9901-9902
    • (1999) J. Am. Chem. Soc. , vol.121 , pp. 9901-9902
    • Hickerson, R.P.1    Chepanoske, C.L.2    Williams, S.D.3    David, S.S.4    Burrows, C.J.5
  • 6
    • 0001965216 scopus 로고
    • Redox chemistry of guanine and 8-oxyguanine and a comparison of the peroxidase-catalyzed and electrochemical oxidation of 8-oxyguanine
    • Goyal R.N., and Dryhurst G. Redox chemistry of guanine and 8-oxyguanine and a comparison of the peroxidase-catalyzed and electrochemical oxidation of 8-oxyguanine. J. Electoranal. Chem. 135 (1982) 75-91
    • (1982) J. Electoranal. Chem. , vol.135 , pp. 75-91
    • Goyal, R.N.1    Dryhurst, G.2
  • 7
    • 0034624588 scopus 로고    scopus 로고
    • Characterization of spiroiminodihydantoin as a product of one-electron oxidation of 8-oxo-7,8-dihydroguanosine
    • Luo W., Muller J.G., Rachlin E.M., and Burrows C.J. Characterization of spiroiminodihydantoin as a product of one-electron oxidation of 8-oxo-7,8-dihydroguanosine. Org. Lett. 2 (2000) 613-616
    • (2000) Org. Lett. , vol.2 , pp. 613-616
    • Luo, W.1    Muller, J.G.2    Rachlin, E.M.3    Burrows, C.J.4
  • 8
    • 0036801449 scopus 로고    scopus 로고
    • Guanine and 7,8-dihydro-8-oxo-guanine-specific oxidation in DNA by chromium(V)
    • Sugden K.D., and Martin B.D. Guanine and 7,8-dihydro-8-oxo-guanine-specific oxidation in DNA by chromium(V). Environ. Health Perspect. 110 Suppl. 5 (2002) 725-728
    • (2002) Environ. Health Perspect. , vol.110 , Issue.SUPPL. 5 , pp. 725-728
    • Sugden, K.D.1    Martin, B.D.2
  • 9
    • 0033555373 scopus 로고    scopus 로고
    • Insertion of dGMP and dAMP during in vitro DNA synthesis opposite an oxidized form of 7,8-dihydro-8-oxoguanine
    • Duarte V., Muller J.G., and Burrows C.J. Insertion of dGMP and dAMP during in vitro DNA synthesis opposite an oxidized form of 7,8-dihydro-8-oxoguanine. Nucleic Acids Res. 27 (1999) 496-502
    • (1999) Nucleic Acids Res. , vol.27 , pp. 496-502
    • Duarte, V.1    Muller, J.G.2    Burrows, C.J.3
  • 10
    • 0037154121 scopus 로고    scopus 로고
    • Oxidation of 7,8-dihydro-8-oxoguanine affords lesions that are potent sources of replication errors in vivo
    • Henderson P.T., Delaney J.C., Gu F., Tannenbaum S.R., and Essigmann J.M. Oxidation of 7,8-dihydro-8-oxoguanine affords lesions that are potent sources of replication errors in vivo. Biochemistry 41 (2002) 914-921
    • (2002) Biochemistry , vol.41 , pp. 914-921
    • Henderson, P.T.1    Delaney, J.C.2    Gu, F.3    Tannenbaum, S.R.4    Essigmann, J.M.5
  • 11
    • 0034610403 scopus 로고    scopus 로고
    • Removal of hydantoin products of 8-oxoguanine oxidation by the Escherichia coli DNA repair enzyme, FPG
    • Leipold M.D., Muller J.G., Burrows C.J., and David S.S. Removal of hydantoin products of 8-oxoguanine oxidation by the Escherichia coli DNA repair enzyme, FPG. Biochemistry 39 (2000) 14984-14992
    • (2000) Biochemistry , vol.39 , pp. 14984-14992
    • Leipold, M.D.1    Muller, J.G.2    Burrows, C.J.3    David, S.S.4
  • 12
    • 0035339684 scopus 로고    scopus 로고
    • Repair of hydantoins, one electron oxidation product of 8-oxoguanine, by DNA glycosylases of Escherichia coli
    • Hazra T.K., Muller J.G., Manuel R.C., Burrows C.J., Lloyd R.S., and Mitra S. Repair of hydantoins, one electron oxidation product of 8-oxoguanine, by DNA glycosylases of Escherichia coli. Nucleic Acids Res. 29 (2001) 1967-1974
    • (2001) Nucleic Acids Res. , vol.29 , pp. 1967-1974
    • Hazra, T.K.1    Muller, J.G.2    Manuel, R.C.3    Burrows, C.J.4    Lloyd, R.S.5    Mitra, S.6
  • 16
    • 0037125133 scopus 로고    scopus 로고
    • A novel human DNA glycosylase that removes oxidative DNA damage and is homologous to Escherichia coli endonuclease VIII
    • Bandaru V., Sunkara S., Wallace S.S., and Bond J.P. A novel human DNA glycosylase that removes oxidative DNA damage and is homologous to Escherichia coli endonuclease VIII. DNA Repair (Amst.) 1 (2002) 517-529
    • (2002) DNA Repair (Amst.) , vol.1 , pp. 517-529
    • Bandaru, V.1    Sunkara, S.2    Wallace, S.S.3    Bond, J.P.4
  • 18
    • 0037162995 scopus 로고    scopus 로고
    • Identification and characterization of a novel human DNA glycosylase for repair of cytosine-derived lesions
    • Hazra T.K., Kow Y.W., Hatahet Z., Imhoff B., Boldogh I., Mokkapati S.K., Mitra S., and Izumi T. Identification and characterization of a novel human DNA glycosylase for repair of cytosine-derived lesions. J. Biol. Chem. 277 (2002) 30417-30420
    • (2002) J. Biol. Chem. , vol.277 , pp. 30417-30420
    • Hazra, T.K.1    Kow, Y.W.2    Hatahet, Z.3    Imhoff, B.4    Boldogh, I.5    Mokkapati, S.K.6    Mitra, S.7    Izumi, T.8
  • 19
    • 0037112668 scopus 로고    scopus 로고
    • Human DNA glycosylases of the bacterial Fpg/MutM superfamily: an alternative pathway for the repair of 8-oxoguanine and other oxidation products in DNA
    • Morland I., Rolseth V., Luna L., Rognes T., Bjoras M., and Seeberg E. Human DNA glycosylases of the bacterial Fpg/MutM superfamily: an alternative pathway for the repair of 8-oxoguanine and other oxidation products in DNA. Nucleic Acids Res. 30 (2002) 4926-4936
    • (2002) Nucleic Acids Res. , vol.30 , pp. 4926-4936
    • Morland, I.1    Rolseth, V.2    Luna, L.3    Rognes, T.4    Bjoras, M.5    Seeberg, E.6
  • 20
  • 22
    • 33745200736 scopus 로고    scopus 로고
    • Oxidative DNA glycosylases: recipes from cloning to characterization
    • Bandaru V., Blaisdell J.O., and Wallace S.S. Oxidative DNA glycosylases: recipes from cloning to characterization. Methods Enzymol. 408 (2006) 15-33
    • (2006) Methods Enzymol. , vol.408 , pp. 15-33
    • Bandaru, V.1    Blaisdell, J.O.2    Wallace, S.S.3
  • 23
    • 0037168491 scopus 로고    scopus 로고
    • In vitro nucleotide misinsertion opposite the oxidized guanosine lesions spiroiminodihydantoin and guanidinohydantoin and DNA synthesis past the lesions using Escherichia coli DNA polymerase I (Klenow fragment)
    • Kornyushyna O., Berges A.M., Muller J.G., and Burrows C.J. In vitro nucleotide misinsertion opposite the oxidized guanosine lesions spiroiminodihydantoin and guanidinohydantoin and DNA synthesis past the lesions using Escherichia coli DNA polymerase I (Klenow fragment). Biochemistry 41 (2002) 15304-15314
    • (2002) Biochemistry , vol.41 , pp. 15304-15314
    • Kornyushyna, O.1    Berges, A.M.2    Muller, J.G.3    Burrows, C.J.4
  • 24
    • 0035860767 scopus 로고    scopus 로고
    • Identification of an intrinsic 5′- deoxyribose-5-phosphate lyase activity in human DNA polymerase lambda: a possible role in base excision repair
    • Garcia-Diaz M., Bebenek K., Kunkel T.A., and Blanco L. Identification of an intrinsic 5′- deoxyribose-5-phosphate lyase activity in human DNA polymerase lambda: a possible role in base excision repair. J. Biol. Chem. 276 (2001) 34659-34663
    • (2001) J. Biol. Chem. , vol.276 , pp. 34659-34663
    • Garcia-Diaz, M.1    Bebenek, K.2    Kunkel, T.A.3    Blanco, L.4
  • 25
    • 0347379928 scopus 로고    scopus 로고
    • Repair of oxidized bases in DNA bubble structures by human DNA glycosylases NEIL1 and NEIL2
    • Dou H., Mitra S., and Hazra T.K. Repair of oxidized bases in DNA bubble structures by human DNA glycosylases NEIL1 and NEIL2. J. Biol. Chem. 278 (2003) 49679-49684
    • (2003) J. Biol. Chem. , vol.278 , pp. 49679-49684
    • Dou, H.1    Mitra, S.2    Hazra, T.K.3
  • 26
    • 0344815737 scopus 로고
    • Extent of N-terminal methionine excision from Escherichia coli proteins is governed by the side-chain length of the penultimate amino acid
    • Hirel P.H., Schmitter M.J., Dessen P., Fayat G., and Blanquet S. Extent of N-terminal methionine excision from Escherichia coli proteins is governed by the side-chain length of the penultimate amino acid. Proc. Natl. Acad. Sci. U. S. A. 86 (1989) 8247-8251
    • (1989) Proc. Natl. Acad. Sci. U. S. A. , vol.86 , pp. 8247-8251
    • Hirel, P.H.1    Schmitter, M.J.2    Dessen, P.3    Fayat, G.4    Blanquet, S.5
  • 28
    • 7944222565 scopus 로고    scopus 로고
    • Recognition of the oxidized lesions spiroiminodihydantoin and guanidinohydantoin in DNA by the mammalian base excision repair glycosylases NEIL1 and NEIL2
    • Hailer M.K., Slade P.G., Martin B.D., Rosenquist T.A., and Sugden K.D. Recognition of the oxidized lesions spiroiminodihydantoin and guanidinohydantoin in DNA by the mammalian base excision repair glycosylases NEIL1 and NEIL2. DNA Repair (Amst.) 4 (2005) 41-50
    • (2005) DNA Repair (Amst.) , vol.4 , pp. 41-50
    • Hailer, M.K.1    Slade, P.G.2    Martin, B.D.3    Rosenquist, T.A.4    Sugden, K.D.5
  • 29
    • 0026751221 scopus 로고
    • Excision of 5′-terminal deoxyribose phosphate from damaged DNA is catalyzed by the Fpg protein of Escherichia coli
    • Graves R.J., Felzenszwalb I., Laval J., and O'Connor T.R. Excision of 5′-terminal deoxyribose phosphate from damaged DNA is catalyzed by the Fpg protein of Escherichia coli. J. Biol. Chem. 267 (1992) 14429-14435
    • (1992) J. Biol. Chem. , vol.267 , pp. 14429-14435
    • Graves, R.J.1    Felzenszwalb, I.2    Laval, J.3    O'Connor, T.R.4
  • 30
    • 7944227532 scopus 로고    scopus 로고
    • DNA glycosylase activities for thymine residues oxidized in the methyl group are functions of the hNEIL1 and hNTHl enzymes in human cells
    • Zhang Q.M., Yonekura S., Takao M., Yasui A., Sugiyama H., and Yonei S. DNA glycosylase activities for thymine residues oxidized in the methyl group are functions of the hNEIL1 and hNTHl enzymes in human cells. DNA Repair (Amst.) 4 (2005) 71-79
    • (2005) DNA Repair (Amst.) , vol.4 , pp. 71-79
    • Zhang, Q.M.1    Yonekura, S.2    Takao, M.3    Yasui, A.4    Sugiyama, H.5    Yonei, S.6
  • 31
    • 33749318279 scopus 로고    scopus 로고
    • Catalytic mechanism of Escherichia coli endonuclease VIII: roles of the intercalation loop and the zinc finger
    • Kropachev K.Y., Zharkov D.O., and Grollman A.P. Catalytic mechanism of Escherichia coli endonuclease VIII: roles of the intercalation loop and the zinc finger. Biochemistry 45 (2006) 12039-12049
    • (2006) Biochemistry , vol.45 , pp. 12039-12049
    • Kropachev, K.Y.1    Zharkov, D.O.2    Grollman, A.P.3
  • 32
    • 33747808676 scopus 로고    scopus 로고
    • Structure of T4 pyrimidine dimer glycosylase in a reduced imine covalent complex with abasic site-containing DNA
    • Golan G., Zharkov D.O., Grollman A.P., Dodson M.L., McCullough A.K., Lloyd R.S., and Shoham G. Structure of T4 pyrimidine dimer glycosylase in a reduced imine covalent complex with abasic site-containing DNA. J. Mol. Biol. 362 (2006) 241-258
    • (2006) J. Mol. Biol. , vol.362 , pp. 241-258
    • Golan, G.1    Zharkov, D.O.2    Grollman, A.P.3    Dodson, M.L.4    McCullough, A.K.5    Lloyd, R.S.6    Shoham, G.7
  • 33
    • 0036788148 scopus 로고    scopus 로고
    • Roles of uracil-DNA glycosylase and dUTPase in virus replication
    • Chen R., Wang H., and Mansky L.M. Roles of uracil-DNA glycosylase and dUTPase in virus replication. J. Gen. Virol. 83 (2002) 2339-2345
    • (2002) J. Gen. Virol. , vol.83 , pp. 2339-2345
    • Chen, R.1    Wang, H.2    Mansky, L.M.3
  • 34
    • 33645047654 scopus 로고    scopus 로고
    • Genomic and evolutionary aspects of Mimivirus
    • Suzan-Monti M., La Scola B., and Raoult D. Genomic and evolutionary aspects of Mimivirus. Virus Res. 117 (2006) 145-155
    • (2006) Virus Res. , vol.117 , pp. 145-155
    • Suzan-Monti, M.1    La Scola, B.2    Raoult, D.3
  • 35
    • 26844477403 scopus 로고    scopus 로고
    • Mimivirus gene promoters exhibit an unprecedented conservation among all eukaryotes
    • Suhre K., Audic S., and Claverie J.M. Mimivirus gene promoters exhibit an unprecedented conservation among all eukaryotes. Proc. Natl. Acad. Sci. U. S. A. 102 (2005) 14689-14693
    • (2005) Proc. Natl. Acad. Sci. U. S. A. , vol.102 , pp. 14689-14693
    • Suhre, K.1    Audic, S.2    Claverie, J.M.3
  • 37
    • 84900614807 scopus 로고    scopus 로고
    • Response to Comment on "The 1.2- Megabase Genome Sequence of Mimivirus"
    • Ogata H., Abergel C., Raoult D., and Claverie J.M. Response to Comment on "The 1.2- Megabase Genome Sequence of Mimivirus". Science 308 (2005) 1114B
    • (2005) Science , vol.308
    • Ogata, H.1    Abergel, C.2    Raoult, D.3    Claverie, J.M.4
  • 38
    • 2042522697 scopus 로고    scopus 로고
    • Microorganisms resistant to free-living amoebae
    • Greub G., and Raoult D. Microorganisms resistant to free-living amoebae. Clin. Microbiol. Rev. 17 (2004) 413-433
    • (2004) Clin. Microbiol. Rev. , vol.17 , pp. 413-433
    • Greub, G.1    Raoult, D.2
  • 40
    • 23944516801 scopus 로고    scopus 로고
    • Mimivirus relatives in the Sargasso sea
    • Ghedin E., and Claverie J.M. Mimivirus relatives in the Sargasso sea. Virol. J. 2 (2005) 62
    • (2005) Virol. J. , vol.2 , pp. 62
    • Ghedin, E.1    Claverie, J.M.2
  • 41
    • 4243178226 scopus 로고    scopus 로고
    • Free-living amoebae as opportunistic and non-opportunistic pathogens of humans and animals
    • Schuster F.L., and Visvesvara G.S. Free-living amoebae as opportunistic and non-opportunistic pathogens of humans and animals. Int. J. Parasitol. 34 (2004) 1001-1027
    • (2004) Int. J. Parasitol. , vol.34 , pp. 1001-1027
    • Schuster, F.L.1    Visvesvara, G.S.2
  • 42
    • 0017966479 scopus 로고
    • The occurrence of amphizoic Amebae in domestic animals
    • Kadlec V. The occurrence of amphizoic Amebae in domestic animals. J. Protozool. 25 (1978) 235-237
    • (1978) J. Protozool. , vol.25 , pp. 235-237
    • Kadlec, V.1
  • 43
    • 0034254724 scopus 로고    scopus 로고
    • Crystal structure of a repair enzyme of oxidatively damaged DNA, MutM (Fpg), from an extreme thermophile, Thermus thermophilus HB8
    • Sugahara M., Mikawa T., Kumasaka T., Yamamoto M., Kato R., Fukuyama K., Inoue Y., and Kuramitsu S. Crystal structure of a repair enzyme of oxidatively damaged DNA, MutM (Fpg), from an extreme thermophile, Thermus thermophilus HB8. EMBO J. 19 (2000) 3857-3869
    • (2000) EMBO J. , vol.19 , pp. 3857-3869
    • Sugahara, M.1    Mikawa, T.2    Kumasaka, T.3    Yamamoto, M.4    Kato, R.5    Fukuyama, K.6    Inoue, Y.7    Kuramitsu, S.8
  • 44
    • 3142702720 scopus 로고    scopus 로고
    • The crystal structure of human endonuclease VIII-like 1 (NEIL1) reveals a zincless finger motif required for glycosylase activity
    • Doublié S., Bandaru V., Bond J.P., and Wallace S.S. The crystal structure of human endonuclease VIII-like 1 (NEIL1) reveals a zincless finger motif required for glycosylase activity. Proc. Natl. Acad. Sci. U. S. A. 101 (2004) 10284-10289
    • (2004) Proc. Natl. Acad. Sci. U. S. A. , vol.101 , pp. 10284-10289
    • Doublié, S.1    Bandaru, V.2    Bond, J.P.3    Wallace, S.S.4
  • 45
    • 8744262953 scopus 로고    scopus 로고
    • Identification of a zinc finger domain in the human NEIL2 (Nei-like-2) protein
    • Das A., Rajagopalan L., Mathura V.S., Rigby S.J., Mitra S., and Hazra T.K. Identification of a zinc finger domain in the human NEIL2 (Nei-like-2) protein. J. Biol. Chem. 279 (2004) 47132-47138
    • (2004) J. Biol. Chem. , vol.279 , pp. 47132-47138
    • Das, A.1    Rajagopalan, L.2    Mathura, V.S.3    Rigby, S.J.4    Mitra, S.5    Hazra, T.K.6
  • 46
    • 0028847687 scopus 로고
    • Involvement of glutamic acid 23 in the catalytic mechanism of T4 endonuclease V
    • Manuel R.C., Latham K.A., Dodson M.L., and Lloyd R.S. Involvement of glutamic acid 23 in the catalytic mechanism of T4 endonuclease V. J. Biol. Chem. 270 (1995) 2652-2661
    • (1995) J. Biol. Chem. , vol.270 , pp. 2652-2661
    • Manuel, R.C.1    Latham, K.A.2    Dodson, M.L.3    Lloyd, R.S.4
  • 47
    • 1842289240 scopus 로고    scopus 로고
    • Characterization of an African swine fever virus 20-kDa DNA polymerase involved in DNA repair
    • Oliveros M., Yanez R.J., Salas M.L., Salas J., Vinuela E., and Blanco L. Characterization of an African swine fever virus 20-kDa DNA polymerase involved in DNA repair. J. Biol. Chem. 272 (1997) 30899-30910
    • (1997) J. Biol. Chem. , vol.272 , pp. 30899-30910
    • Oliveros, M.1    Yanez, R.J.2    Salas, M.L.3    Salas, J.4    Vinuela, E.5    Blanco, L.6
  • 48
    • 33644687604 scopus 로고    scopus 로고
    • Contributions of an endonuclease IV homologue to DNA repair in the African swine fever virus
    • Lamarche B.J., and Tsai M.D. Contributions of an endonuclease IV homologue to DNA repair in the African swine fever virus. Biochemistry 45 (2006) 2790-2803
    • (2006) Biochemistry , vol.45 , pp. 2790-2803
    • Lamarche, B.J.1    Tsai, M.D.2
  • 49
    • 33747883756 scopus 로고    scopus 로고
    • Characterization of mimivirus NAD+-dependent DNA ligase
    • Benarroch D., and Shuman S. Characterization of mimivirus NAD+-dependent DNA ligase. Virology 353 (2006) 133-143
    • (2006) Virology , vol.353 , pp. 133-143
    • Benarroch, D.1    Shuman, S.2
  • 50
    • 0032516831 scopus 로고    scopus 로고
    • Mammalian abasic site base excision repair. Identification of the reaction sequence and rate-determining steps
    • Srivastava D.K., Berg B.J., Prasad R., Molina J.T., Beard W.A., Tomkinson A.E., and Wilson S.H. Mammalian abasic site base excision repair. Identification of the reaction sequence and rate-determining steps. J. Biol. Chem. 273 (1998) 21203-21209
    • (1998) J. Biol. Chem. , vol.273 , pp. 21203-21209
    • Srivastava, D.K.1    Berg, B.J.2    Prasad, R.3    Molina, J.T.4    Beard, W.A.5    Tomkinson, A.E.6    Wilson, S.H.7
  • 51
    • 0029892846 scopus 로고    scopus 로고
    • Evidence for an imino intermediate in the DNA polymerase beta deoxyribose phosphate excision reaction
    • Piersen C.E., Prasad R., Wilson S.H., and Lloyd R.S. Evidence for an imino intermediate in the DNA polymerase beta deoxyribose phosphate excision reaction. J. Biol. Chem. 271 (1996) 17811-17815
    • (1996) J. Biol. Chem. , vol.271 , pp. 17811-17815
    • Piersen, C.E.1    Prasad, R.2    Wilson, S.H.3    Lloyd, R.S.4
  • 52
    • 33747845656 scopus 로고    scopus 로고
    • Deoxyribophosphate lyase activity of mammalian endonuclease VHI-like proteins
    • Grin I.R., Khodyreva S.N., Nevinsky G.A., and Zharkov D.O. Deoxyribophosphate lyase activity of mammalian endonuclease VHI-like proteins. FEBS Lett. 580 (2006) 4916-4922
    • (2006) FEBS Lett. , vol.580 , pp. 4916-4922
    • Grin, I.R.1    Khodyreva, S.N.2    Nevinsky, G.A.3    Zharkov, D.O.4


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.