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Volumn 287, Issue 4, 2012, Pages 2819-2829

Role of human DNA glycosylase Nei-like 2 (NEIL2) and single strand break repair protein polynucleotide kinase 3′-phosphatase in maintenance of mitochondrial genome

Author keywords

[No Author keywords available]

Indexed keywords

CHROMATIN IMMUNOPRECIPITATION ANALYSIS; COLOCALIZATION; CYTOCHROME C OXIDASE; DNA GLYCOSYLASE; DNA POLYMERASE; GENOMIC INTEGRITY; HEK293 CELLS; MITOCHONDRIAL GENES; MITOCHONDRIAL GENOMES; NUCLEAR GENOMES; POLYNUCLEOTIDES; PROTEIN CYTOCHROME C; REACTIVE OXYGEN; SINGLE-STRAND BREAK REPAIRS; SINGLE-STRAND BREAKS;

EID: 84856070741     PISSN: 00219258     EISSN: 1083351X     Source Type: Journal    
DOI: 10.1074/jbc.M111.272179     Document Type: Article
Times cited : (81)

References (62)
  • 1
    • 0028927261 scopus 로고
    • Reactions of oxyl radicals with DNA
    • Breen, A. P., and Murphy, J. A. (1995) Reactions of oxyl radicals with DNA. Free Radic. Biol. Med. 18, 1033-1077
    • (1995) Free Radic. Biol. Med. , vol.18 , pp. 1033-1077
    • Breen, A.P.1    Murphy, J.A.2
  • 2
    • 0031200869 scopus 로고    scopus 로고
    • Free radicals and the pathobiology of brain dopamine systems
    • DOI 10.1016/S0197-0186(97)00031-4, PII S0197018697000314
    • Cadet, J. L., and Brannock, C. (1998) Free radicals and the pathobiology of brain dopamine systems. Neurochem. Int. 32, 117-131 (Pubitemid 28105298)
    • (1998) Neurochemistry International , vol.32 , Issue.2 , pp. 117-131
    • Cadet, J.L.1    Brannock, C.2
  • 3
    • 38049112778 scopus 로고    scopus 로고
    • Early steps in the DNA base excision/single-strand interruption repair pathway in mammalian cells
    • Hegde, M. L., Hazra, T. K., and Mitra, S. (2008) Early steps in the DNA base excision/single-strand interruption repair pathway in mammalian cells. Cell Res. 18, 27-47
    • (2008) Cell Res. , vol.18 , pp. 27-47
    • Hegde, M.L.1    Hazra, T.K.2    Mitra, S.3
  • 4
    • 0028604549 scopus 로고
    • Unified catalytic mechanism for DNA glycosylases
    • Dodson, M. L., Michaels, M. L., and Lloyd, R. S. (1994) Unified catalytic mechanism for DNA glycosylases. J. Biol. Chem. 269, 32709 -32712
    • (1994) J. Biol. Chem. , vol.269 , pp. 32709-32712
    • Dodson, M.L.1    Michaels, M.L.2    Lloyd, R.S.3
  • 6
    • 41249094475 scopus 로고    scopus 로고
    • Interaction of the human DNA glycosylase NEIL1 with proliferating cell nuclear antigen. The potential for replication-associated repair of oxidized bases in mammalian genomes
    • Dou, H., Theriot, C. A., Das, A., Hegde, M. L., Matsumoto, Y., Boldogh, I., Hazra, T. K., Bhakat, K. K., and Mitra, S. (2008) Interaction of the human DNA glycosylase NEIL1 with proliferating cell nuclear antigen. The potential for replication-associated repair of oxidized bases in mammalian genomes. J. Biol. Chem. 283, 3130-3140
    • (2008) J. Biol. Chem. , vol.283 , pp. 3130-3140
    • Dou, H.1    Theriot, C.A.2    Das, A.3    Hegde, M.L.4    Matsumoto, Y.5    Boldogh, I.6    Hazra, T.K.7    Bhakat, K.K.8    Mitra, S.9
  • 11
    • 0019848907 scopus 로고
    • Bleomycin-induced strand-scission of DNA. Mechanism of deoxyribose cleavage
    • Giloni, L., Takeshita, M., Johnson, F., Iden, C., and Grollman, A. P. (1981) Bleomycin-induced strand-scission of DNA. Mechanism of deoxyribose cleavage. J. Biol. Chem. 256, 8608-8615 (Pubitemid 12254808)
    • (1981) Journal of Biological Chemistry , vol.256 , Issue.16 , pp. 8608-8615
    • Giloni, L.1    Takeshita, M.2    Johnson, F.3
  • 12
    • 0021045679 scopus 로고
    • Enzyme action at 3′ termini of ionizing radiation-induced DNA strand breaks
    • Henner, W. D., Grunberg, S. M., and Haseltine, W. A. (1983) Enzyme action at 3′ termini of ionizing radiation-induced DNA strand breaks. J. Biol. Chem. 258, 15198-15205
    • (1983) J. Biol. Chem. , vol.258 , pp. 15198-15205
    • Henner, W.D.1    Grunberg, S.M.2    Haseltine, W.A.3
  • 13
    • 79955663428 scopus 로고    scopus 로고
    • Tidying up loose ends: The role of polynucleotide kinase/phosphatase in DNA strand break repair
    • Weinfeld, M., Mani, R. S., Abdou, I., Aceytuno, R. D., and Glover, J. N. (2011) Tidying up loose ends: the role of polynucleotide kinase/phosphatase in DNA strand break repair. Trends Biochem. Sci. 36, 262-271
    • (2011) Trends Biochem. Sci. , vol.36 , pp. 262-271
    • Weinfeld, M.1    Mani, R.S.2    Abdou, I.3    Aceytuno, R.D.4    Glover, J.N.5
  • 14
    • 0035009313 scopus 로고    scopus 로고
    • Mammalian DNA single-strand break repair: An X-ra(y)ted affair
    • Caldecott, K. W. (2001) Mammalian DNA single-strand break repair: an X-ra(y)ted affair. BioEssays 23, 447-455
    • (2001) BioEssays , vol.23 , pp. 447-455
    • Caldecott, K.W.1
  • 15
    • 48249095920 scopus 로고    scopus 로고
    • Single-strand break repair and genetic disease
    • Caldecott, K. W. (2008) Single-strand break repair and genetic disease. Nat. Rev. Genet. 9, 619-631
    • (2008) Nat. Rev. Genet. , vol.9 , pp. 619-631
    • Caldecott, K.W.1
  • 16
    • 0033588161 scopus 로고    scopus 로고
    • Molecular cloning of the human gene, PNKP, encoding a polynucleotide kinase 3′-phosphatase and evidence for its role in repair of DNA strand breaks caused by oxidative damage
    • Jilani, A., Ramotar, D., Slack, C., Ong, C., Yang, X. M., Scherer, S. W., and Lasko, D. D. (1999) Molecular cloning of the human gene, PNKP, encoding a polynucleotide kinase 3′-phosphatase and evidence for its role in repair of DNA strand breaks caused by oxidative damage. J. Biol. Chem. 274, 24176-24186
    • (1999) J. Biol. Chem. , vol.274 , pp. 24176-24186
    • Jilani, A.1    Ramotar, D.2    Slack, C.3    Ong, C.4    Yang, X.M.5    Scherer, S.W.6    Lasko, D.D.7
  • 18
    • 0027164993 scopus 로고
    • Identification of deoxyribonuclease II as an endonuclease involved in apoptosis
    • DOI 10.1006/abbi.1993.1060
    • Barry, M. A., and Eastman, A. (1993) Identification of deoxyribonuclease II as an endonuclease involved in apoptosis. Arch. Biochem. Biophys. 300, 440-450 (Pubitemid 23225769)
    • (1993) Archives of Biochemistry and Biophysics , vol.300 , Issue.1 , pp. 440-450
    • Barry, M.A.1    Eastman, A.2
  • 19
    • 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., and 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 (Pubitemid 26077846)
    • (1996) EMBO Journal , vol.15 , Issue.5 , pp. 1193-1200
    • Pohjanpelto, P.1    Holtta, E.2
  • 21
    • 0023811053 scopus 로고
    • Normal oxidative damage to mitochondrial and nuclear DNA is extensive
    • Richter, C., Park, J. W., and Ames, B. N. (1988) Normal oxidative damage to mitochondrial and nuclear DNA is extensive. Proc. Natl. Acad. Sci. U.S.A. 85, 6465-6467
    • (1988) Proc. Natl. Acad. Sci. U.S.A. , vol.85 , pp. 6465-6467
    • Richter, C.1    Park, J.W.2    Ames, B.N.3
  • 22
    • 0032432767 scopus 로고    scopus 로고
    • The sensitivity to DNA single strand breakage in mitochondria, but not in nuclei, of Chinese hamster V79 and variant cells correlates with their cellular sensitivity to hydrogen peroxide
    • DOI 10.1016/S0378-4274(98)00132-5, PII S0378427498001325
    • Kaneko, M., and Inoue, F. (1998) The sensitivity to DNA single strand breakage in mitochondria, but not in nuclei, of Chinese hamster V79 and variant cells correlates with their cellular sensitivity to hydrogen peroxide. Toxicol. Lett. 99, 15-22 (Pubitemid 29027834)
    • (1998) Toxicology Letters , vol.99 , Issue.1 , pp. 15-22
    • Kaneko, M.1    Inoue, F.2
  • 23
    • 0036361291 scopus 로고    scopus 로고
    • Animal models for mitochondrial disease
    • Wallace, D. C. (2002) Animal models for mitochondrial disease. Methods Mol. Biol. 197, 3-54
    • (2002) Methods Mol. Biol. , vol.197 , pp. 3-54
    • Wallace, D.C.1
  • 24
    • 77955245660 scopus 로고    scopus 로고
    • Understanding heterogeneous diseases in mtDNA maintenance
    • Copeland, W. C. (2010) Understanding heterogeneous diseases in mtDNA maintenance. Methods 51, 363
    • (2010) Methods , vol.51 , pp. 363
    • Copeland, W.C.1
  • 26
    • 0036570012 scopus 로고    scopus 로고
    • Repair of oxidative DNA damage in nuclear and mitochondrial DNA, and some changes with aging in mammalian cells
    • Bohr, V. A. (2002) Repair of oxidative DNA damage in nuclear and mitochondrial DNA, and some changes with aging in mammalian cells. Free Radic. Biol. Med. 32, 804-812
    • (2002) Free Radic. Biol. Med. , vol.32 , pp. 804-812
    • Bohr, V.A.1
  • 28
    • 33645928711 scopus 로고    scopus 로고
    • Identification and characterization of mitochondrial abasic (AP)-endonuclease in mammalian cells
    • DOI 10.1093/nar/gkl177
    • Chattopadhyay, R., Wiederhold, L., Szczesny, B., Boldogh, I., Hazra, T. K., Izumi, T., and Mitra, S. (2006) Identification and characterization of mitochondrial abasic (AP)-endonuclease in mammalian cells. Nucleic Acids Res. 34, 2067-2076 (Pubitemid 44314205)
    • (2006) Nucleic Acids Research , vol.34 , Issue.7 , pp. 2067-2076
    • Chattopadhyay, R.1    Wiederhold, L.2    Szczesny, B.3    Boldogh, I.4    Hazra, T.K.5    Izumi, T.6    Mitra, S.7
  • 29
    • 0032514627 scopus 로고    scopus 로고
    • Identification of 5′-deoxyribose phosphate lyase activity in human DNA polymerase γ and its role in mitochondrial base excision repair in vitro
    • Longley, M. J., Prasad, R., Srivastava, D. K., Wilson, S. H., and Copeland, W. C. (1998) Identification of 5′-deoxyribose phosphate lyase activity in human DNA polymerase γ and its role in mitochondrial base excision repair in vitro. Proc. Natl. Acad. Sci. U.S.A. 95, 12244-12248
    • (1998) Proc. Natl. Acad. Sci. U.S.A. , vol.95 , pp. 12244-12248
    • Longley, M.J.1    Prasad, R.2    Srivastava, D.K.3    Wilson, S.H.4    Copeland, W.C.5
  • 30
    • 77956545422 scopus 로고    scopus 로고
    • Specific Inhibition of NEIL-initiated repair of oxidized base damage in human genome by copper and iron: Potential etiological linkage to neurodegenerative diseases
    • Hegde, M. L., Hegde, P. M., Holthauzen, L. M., Hazra, T. K., Rao, K. S., and Mitra, S. (2010) Specific Inhibition of NEIL-initiated repair of oxidized base damage in human genome by copper and iron: potential etiological linkage to neurodegenerative diseases. J. Biol. Chem. 285, 28812-28825
    • (2010) J. Biol. Chem. , vol.285 , pp. 28812-28825
    • Hegde, M.L.1    Hegde, P.M.2    Holthauzen, L.M.3    Hazra, T.K.4    Rao, K.S.5    Mitra, S.6
  • 31
    • 27644582893 scopus 로고    scopus 로고
    • Probing tumor phenotypes using stable and regulated synthetic microRNA precursors
    • DOI 10.1038/ng1651, PII N1651
    • Dickins, R. A., Hemann, M. T., Zilfou, J. T., Simpson, D. R., Ibarra, I., Hannon, G. J., and Lowe, S. W. (2005) Probing tumor phenotypes using stable and regulated synthetic microRNA precursors. Nat. Genet. 37, 1289-1295 (Pubitemid 41568715)
    • (2005) Nature Genetics , vol.37 , Issue.11 , pp. 1289-1295
    • Dickins, R.A.1    Hemann, M.T.2    Zilfou, J.T.3    Simpson, D.R.4    Ibarra, I.5    Hannon, G.J.6    Lowe, S.W.7
  • 34
    • 59449105405 scopus 로고    scopus 로고
    • Transcriptional synergy mediated by SAF-1 and AP-1: Critical role of N-terminal polyalanine and two zinc finger domains of SAF-1
    • Kumar, D., Ray, A., and Ray, B. K. (2009) Transcriptional synergy mediated by SAF-1 and AP-1: critical role of N-terminal polyalanine and two zinc finger domains of SAF-1. J. Biol. Chem. 284, 1853-1862
    • (2009) J. Biol. Chem. , vol.284 , pp. 1853-1862
    • Kumar, D.1    Ray, A.2    Ray, B.K.3
  • 36
    • 0037162995 scopus 로고    scopus 로고
    • Identification and characterization of a novel human DNA glycosylase for repair of cytosine-derived lesions
    • DOI 10.1074/jbc.C200355200
    • Hazra, T. K., Kow, Y. W., Hatahet, Z., Imhoff, B., Boldogh, I., Mokkapati, S. K., Mitra, S., and Izumi, T. (2002) Identification and characterization of a novel human DNA glycosylase for repair of cytosine-derived lesions. J. Biol. Chem. 277, 30417-30420 (Pubitemid 34970730)
    • (2002) Journal of Biological Chemistry , vol.277 , Issue.34 , 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
  • 37
    • 3242739284 scopus 로고    scopus 로고
    • Reconstitution of a minimal mtDNA replisome in vitro
    • DOI 10.1038/sj.emboj.7600257
    • Korhonen, J. A., Pham, X. H., Pellegrini, M., and Falkenberg, M. (2004) Reconstitution of a minimal mtDNA replisome in vitro. EMBO J. 23, 2423-2429 (Pubitemid 38954849)
    • (2004) EMBO Journal , vol.23 , Issue.12 , pp. 2423-2429
    • Korhonen, J.A.1    Pham, X.H.2    Pellegrini, M.3    Falkenberg, M.4
  • 38
    • 0034666329 scopus 로고    scopus 로고
    • The DNA ligase III zinc finger stimulates binding to DNA secondary structure and promotes end joining
    • Taylor, R. M., Whitehouse, C. J., and Caldecott, K. W. (2000) The DNA ligase III zinc finger stimulates binding to DNA secondary structure and promotes end joining. Nucleic Acids Res. 28, 3558-3563
    • (2000) Nucleic Acids Res. , vol.28 , pp. 3558-3563
    • Taylor, R.M.1    Whitehouse, C.J.2    Caldecott, K.W.3
  • 39
    • 0035846899 scopus 로고    scopus 로고
    • XRCC1 stimulates human polynucleotide kinase activity at damaged DNA termini and accelerates DNA single-strand break repair
    • DOI 10.1016/S0092-8674(01)00195-7
    • Whitehouse, C. J., Taylor, R. M., Thistlethwaite, A., Zhang, H., Karimi- Busheri, F., Lasko, D. D., Weinfeld, M., and Caldecott, K. W. (2001) XRCC1 stimulates human polynucleotide kinase activity at damaged DNA termini and accelerates DNA single-strand break repair. Cell 104, 107-117 (Pubitemid 32144976)
    • (2001) Cell , vol.104 , Issue.1 , pp. 107-117
    • Whitehouse, C.J.1    Taylor, R.M.2    Thistlethwaite, A.3    Zhang, H.4    Karimi-Busheri, F.5    Lasko, D.D.6    Weinfeld, M.7    Caldecott, K.W.8
  • 40
    • 0032533794 scopus 로고    scopus 로고
    • The presence of two distinct 8-oxoguanine repair enzymes in human cells: Their potential complementary roles in preventing mutation
    • Hazra, T. K., Izumi, T., Maidt, L., Floyd, R. A., and Mitra, S. (1998) The presence of two distinct 8-oxoguanine repair enzymes in human cells: their potential complementary roles in preventing mutation. Nucleic Acids Res. 26, 5116-5122 (Pubitemid 28517567)
    • (1998) Nucleic Acids Research , vol.26 , Issue.22 , pp. 5116-5122
    • Hazra, T.K.1    Izumi, T.2    Maidt, L.3    Floyd, R.A.4    Mitra, S.5
  • 41
    • 0042708011 scopus 로고    scopus 로고
    • Mismatch repair in human nuclear extracts. Effects of internal DNA-hairpin structures between mismatches and excision-initiation nicks on mismatch correction and mismatch-provoked excision
    • DOI 10.1074/jbc.M302844200
    • Wang, H., and Hays, J. B. (2003) Mismatch repair in human nuclear extracts: effects of internal DNA-hairpin structures between mismatches and excision-initiation nicks on mismatch correction and mismatch-provoked excision. J. Biol. Chem. 278, 28686-28693 (Pubitemid 36935775)
    • (2003) Journal of Biological Chemistry , vol.278 , Issue.31 , pp. 28686-28693
    • Wang, H.1    Hays, J.B.2
  • 42
    • 33744721699 scopus 로고    scopus 로고
    • Quantitative PCR-based measurement of nuclear and mitochondrial DNA damage and repair in mammalian cells
    • Santos, J. H., Meyer, J. N., Mandavilli, B. S., and Van Houten, B. (2006) Quantitative PCR-based measurement of nuclear and mitochondrial DNA damage and repair in mammalian cells. Methods Mol. Biol. 314, 183-199
    • (2006) Methods Mol. Biol. , vol.314 , pp. 183-199
    • Santos, J.H.1    Meyer, J.N.2    Mandavilli, B.S.3    Van Houten, B.4
  • 43
  • 44
    • 0347379928 scopus 로고    scopus 로고
    • Repair of Oxidized Bases in DNA Bubble Structures by Human DNA Glycosylases NEIL1 and NEIL2
    • DOI 10.1074/jbc.M308658200
    • Dou, H., Mitra, S., and Hazra, T. K. (2003) Repair of oxidized bases inDNA bubble structures by human DNA glycosylases NEIL1 and NEIL2. J. Biol. Chem. 278, 49679-49684 (Pubitemid 37548799)
    • (2003) Journal of Biological Chemistry , vol.278 , Issue.50 , pp. 49679-49684
    • Dou, H.1    Mitra, S.2    Hazra, T.K.3
  • 45
    • 0035874485 scopus 로고    scopus 로고
    • Self-association and precursor protein binding of Saccharomyces cerevisiae Tom40p, the core component of the protein translocation channel of the mitochondrial outer membrane
    • DOI 10.1042/0264-6021:3560207
    • Gordon, D. M., Wang, J., Amutha, B., and Pain, D. (2001) Self-association and precursor protein binding of Saccharomyces cerevisiae Tom40p, the core component of the protein translocation channel of the mitochondrial outer membrane. Biochem. J. 356, 207-215 (Pubitemid 34275722)
    • (2001) Biochemical Journal , vol.356 , Issue.1 , pp. 207-215
    • Gordon, D.M.1    Wang, J.2    Amutha, B.3    Pain, D.4
  • 46
    • 55049124777 scopus 로고    scopus 로고
    • Long patch base excision repair in mammalian mitochondrial genomes
    • Szczesny, B., Tann, A. W., Longley, M. J., Copeland, W. C., and Mitra, S. (2008) Long patch base excision repair in mammalian mitochondrial genomes. J. Biol. Chem. 283, 26349-26356
    • (2008) J. Biol. Chem. , vol.283 , pp. 26349-26356
    • Szczesny, B.1    Tann, A.W.2    Longley, M.J.3    Copeland, W.C.4    Mitra, S.5
  • 49
    • 78149434640 scopus 로고    scopus 로고
    • Phosphorylated nucleolin interacts with translationally controlled tumor protein during mitosis and with Oct4 during interphase in ES cells
    • Johansson, H., Svensson, F., Runnberg, R., Simonsson, T., and Simonsson, S. (2010) Phosphorylated nucleolin interacts with translationally controlled tumor protein during mitosis and with Oct4 during interphase in ES cells. PLoS One 5, e13678
    • (2010) PLoS One , vol.5
    • Johansson, H.1    Svensson, F.2    Runnberg, R.3    Simonsson, T.4    Simonsson, S.5
  • 50
  • 51
    • 38049010435 scopus 로고    scopus 로고
    • Nuclear receptors and other nuclear transcription factors in mitochondria: Regulatory molecules in a new environment
    • Psarra, A. M., and Sekeris, C. E. (2008) Nuclear receptors and other nuclear transcription factors in mitochondria: regulatory molecules in a new environment. Biochim. Biophys. Acta 1783, 1-11
    • (2008) Biochim. Biophys. Acta , vol.1783 , pp. 1-11
    • Psarra, A.M.1    Sekeris, C.E.2
  • 52
    • 0034717014 scopus 로고    scopus 로고
    • Death signal-induced localization of p53 protein to mitochondria: A potential role in apoptotic signaling
    • DOI 10.1074/jbc.275.21.16202
    • Marchenko, N. D., Zaika, A., and Moll, U. M. (2000) Death signal-induced localization of p53 protein to mitochondria. A potential role in apoptotic signaling. J. Biol. Chem. 275, 16202-16212 (Pubitemid 30366932)
    • (2000) Journal of Biological Chemistry , vol.275 , Issue.21 , pp. 16202-16212
    • Marchenko, N.D.1    Zaika, A.2    Moll, U.M.3
  • 54
    • 0035877820 scopus 로고    scopus 로고
    • IκB-α, the NF-κB inhibitory subunit, interacts with ANT, the mitochondrial ATP/ADP translocator
    • Bottero, V., Rossi, F., Samson, M., Mari, M., Hofman, P., and Peyron, J. F. (2001) IκB-α, the NF-κB inhibitory subunit, interacts with ANT, the mitochondrial ATP/ADP translocator. J. Biol. Chem. 276, 21317-21324
    • (2001) J. Biol. Chem. , vol.276 , pp. 21317-21324
    • Bottero, V.1    Rossi, F.2    Samson, M.3    Mari, M.4    Hofman, P.5    Peyron, J.F.6
  • 55
    • 0041324898 scopus 로고    scopus 로고
    • The interplay between the glucocorticoid receptor and nuclear factor-kappaB or activator protein-1: Molecular mechanisms for gene repression
    • DOI 10.1210/er.2002-0006
    • De Bosscher, K., Vanden Berghe, W., and Haegeman, G. (2003) The interplay between the glucocorticoid receptor and nuclear factor-κB or activator protein-1: molecular mechanisms for gene repression. Endocr. Rev. 24, 488-522 (Pubitemid 37059110)
    • (2003) Endocrine Reviews , vol.24 , Issue.4 , pp. 488-522
    • De Bosscher, K.1    Vanden, B.W.2    Haegeman, G.3
  • 56
    • 5044232010 scopus 로고    scopus 로고
    • Mitochondrial poly(ADP-ribosylation): From old data to new perspectives
    • Scovassi, A. I. (2004) Mitochondrial poly(ADP-ribosylation): from old data to new perspectives. FASEB J. 18, 1487-1488
    • (2004) FASEB J. , vol.18 , pp. 1487-1488
    • Scovassi, A.I.1
  • 61


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