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Volumn 475, Issue 1, 2011, Pages 30-38

Molecular analysis and functions of p53R2 in zebrafish

Author keywords

DNA damage; DNA synthesis; Genotoxicity; P53R2; Zebrafish

Indexed keywords

CAMPTOTHECIN; COMPLEMENTARY DNA; DNA; MESYLIC ACID METHYL ESTER; PROTEIN P53; PROTEIN P53R2; RIBONUCLEOTIDE REDUCTASE; UNCLASSIFIED DRUG;

EID: 79952003165     PISSN: 03781119     EISSN: None     Source Type: Journal    
DOI: 10.1016/j.gene.2010.12.008     Document Type: Article
Times cited : (7)

References (55)
  • 1
    • 0033984224 scopus 로고    scopus 로고
    • Application of yeast cells transformed with GFP expression constructs containing the RAD54 or RNR2 promoter as a test for the genotoxic potential of chemical substances
    • Afanassiev V., et al. Application of yeast cells transformed with GFP expression constructs containing the RAD54 or RNR2 promoter as a test for the genotoxic potential of chemical substances. Mutat. Res. 2000, 464:297-308.
    • (2000) Mutat. Res. , vol.464 , pp. 297-308
    • Afanassiev, V.1
  • 3
    • 3242886115 scopus 로고    scopus 로고
    • DNA damage responses to oxidative stress
    • Barzilai A., Yamamoto K. DNA damage responses to oxidative stress. DNA Repair 2004, 3:1109-1115.
    • (2004) DNA Repair , vol.3 , pp. 1109-1115
    • Barzilai, A.1    Yamamoto, K.2
  • 4
    • 0033575292 scopus 로고    scopus 로고
    • Identification of cis-regulating elements and trans-acting factors regulating the expression of the gene encoding the small subunit of ribonucleotide reductase in Dictyostelium discoideum
    • Bonfils C., Gaudet P., Tsang A. Identification of cis-regulating elements and trans-acting factors regulating the expression of the gene encoding the small subunit of ribonucleotide reductase in Dictyostelium discoideum. J. Biol. Chem. 1999, 274:20384-20390.
    • (1999) J. Biol. Chem. , vol.274 , pp. 20384-20390
    • Bonfils, C.1    Gaudet, P.2    Tsang, A.3
  • 5
    • 46249089801 scopus 로고    scopus 로고
    • Mitochondrial DNA depletion syndrome due to mutations in the RRM2B gene
    • Bornstein B., et al. Mitochondrial DNA depletion syndrome due to mutations in the RRM2B gene. Neuromuscul. Disord. 2008, 18:453-459.
    • (2008) Neuromuscul. Disord. , vol.18 , pp. 453-459
    • Bornstein, B.1
  • 6
    • 34249811206 scopus 로고    scopus 로고
    • Mutation of RRM2B, encoding p53-controlled ribonucleotide reductase (p53R2), causes severe mitochondrial DNA depletion
    • Bourdon A., et al. Mutation of RRM2B, encoding p53-controlled ribonucleotide reductase (p53R2), causes severe mitochondrial DNA depletion. Nat. Genet. 2007, 39:776-780.
    • (2007) Nat. Genet. , vol.39 , pp. 776-780
    • Bourdon, A.1
  • 7
    • 1642356666 scopus 로고    scopus 로고
    • S Phase-specific transcription of the mouse ribonucleotide reductase R2 gene requires both a proximal repressive E2F-binding site and an upstream promoter activating region
    • Chabes A.L., Bjorklund S., Thelander L. S Phase-specific transcription of the mouse ribonucleotide reductase R2 gene requires both a proximal repressive E2F-binding site and an upstream promoter activating region. J. Biol. Chem. 2004, 279:10796-10807.
    • (2004) J. Biol. Chem. , vol.279 , pp. 10796-10807
    • Chabes, A.L.1    Bjorklund, S.2    Thelander, L.3
  • 8
    • 0242317756 scopus 로고    scopus 로고
    • Mouse ribonucleotide reductase R2 protein: a new target for anaphase-promoting complex-Cdh1-mediated proteolysis
    • Chabes A.L., Pfleger C.M., Kirschner M.W., Thelander L. Mouse ribonucleotide reductase R2 protein: a new target for anaphase-promoting complex-Cdh1-mediated proteolysis. Proc. Natl Acad. Sci. USA 2003, 100:3925-3929.
    • (2003) Proc. Natl Acad. Sci. USA , vol.100 , pp. 3925-3929
    • Chabes, A.L.1    Pfleger, C.M.2    Kirschner, M.W.3    Thelander, L.4
  • 9
    • 57449084374 scopus 로고    scopus 로고
    • ATM-mediated serine 72 phosphorylation stabilizes ribonucleotide reductase small subunit p53R2 protein against MDM2 to DNA damage
    • Chang L., et al. ATM-mediated serine 72 phosphorylation stabilizes ribonucleotide reductase small subunit p53R2 protein against MDM2 to DNA damage. Proc. Natl Acad. Sci. USA 2008, 105:18519-18524.
    • (2008) Proc. Natl Acad. Sci. USA , vol.105 , pp. 18519-18524
    • Chang, L.1
  • 10
    • 0042121237 scopus 로고    scopus 로고
    • Multiple sequence alignment with the Clustal series of programs
    • Chenna R., et al. Multiple sequence alignment with the Clustal series of programs. Nucleic Acids Res. 2003, 31:3497-3500.
    • (2003) Nucleic Acids Res. , vol.31 , pp. 3497-3500
    • Chenna, R.1
  • 11
    • 0035578385 scopus 로고    scopus 로고
    • Apoptosis in the developing zebrafish embryo
    • Cole L.K., Ross L.S. Apoptosis in the developing zebrafish embryo. Dev. Biol. 2001, 240:123-142.
    • (2001) Dev. Biol. , vol.240 , pp. 123-142
    • Cole, L.K.1    Ross, L.S.2
  • 12
    • 0026582672 scopus 로고
    • Ribonucleotide reductase: regulation, regulation, regulation
    • Elledge S.J., Zhou Z., Allen J.B. Ribonucleotide reductase: regulation, regulation, regulation. Trends Biochem. Sci. 1992, 17:119-123.
    • (1992) Trends Biochem. Sci. , vol.17 , pp. 119-123
    • Elledge, S.J.1    Zhou, Z.2    Allen, J.B.3
  • 13
    • 0027605113 scopus 로고
    • DNA damage and cell cycle regulation of ribonucleotide reductase
    • Elledge S.J., Zhou Z., Allen J.B., Navas T.A. DNA damage and cell cycle regulation of ribonucleotide reductase. Bioessays 1993, 15:333-339.
    • (1993) Bioessays , vol.15 , pp. 333-339
    • Elledge, S.J.1    Zhou, Z.2    Allen, J.B.3    Navas, T.A.4
  • 14
    • 0022260274 scopus 로고
    • Cell cycle-dependent expression of mammalian ribonucleotide reductase. Differential regulation of the two subunits
    • Engstrom Y., et al. Cell cycle-dependent expression of mammalian ribonucleotide reductase. Differential regulation of the two subunits. J. Biol. Chem. 1985, 260:9114-9116.
    • (1985) J. Biol. Chem. , vol.260 , pp. 9114-9116
    • Engstrom, Y.1
  • 15
    • 0035864176 scopus 로고    scopus 로고
    • Inducible expression of exogenous genes in Dictyostelium discoideum using the ribonucleotide reductase promoter
    • Gaudet P., MacWilliams H., Tsang A. Inducible expression of exogenous genes in Dictyostelium discoideum using the ribonucleotide reductase promoter. Nucleic Acids Res. 2001, 29:E5.
    • (2001) Nucleic Acids Res. , vol.29
    • Gaudet, P.1    MacWilliams, H.2    Tsang, A.3
  • 16
    • 33646359442 scopus 로고    scopus 로고
    • Regulation of mammalian ribonucleotide reduction and dNTP pools after DNA damage and in resting cells
    • Hakansson P., Hofer A., Thelander L. Regulation of mammalian ribonucleotide reduction and dNTP pools after DNA damage and in resting cells. J. Biol. Chem. 2006, 281:7834-7841.
    • (2006) J. Biol. Chem. , vol.281 , pp. 7834-7841
    • Hakansson, P.1    Hofer, A.2    Thelander, L.3
  • 17
    • 2942708047 scopus 로고    scopus 로고
    • The mosquito ribonucleotide reductase R2 gene: ultraviolet light induces expression of a novel R2 variant with an internal amino acid deletion
    • Jayachandran G., Fallon A.M. The mosquito ribonucleotide reductase R2 gene: ultraviolet light induces expression of a novel R2 variant with an internal amino acid deletion. Insect Mol. Biol. 2004, 13:231-239.
    • (2004) Insect Mol. Biol. , vol.13 , pp. 231-239
    • Jayachandran, G.1    Fallon, A.M.2
  • 18
    • 0030580112 scopus 로고    scopus 로고
    • The three-dimensional structure of mammalian ribonucleotide reductase protein R2 reveals a more-accessible iron-radical site than Escherichia coli R2
    • Kauppi B., et al. The three-dimensional structure of mammalian ribonucleotide reductase protein R2 reveals a more-accessible iron-radical site than Escherichia coli R2. J. Mol. Biol. 1996, 262:706-720.
    • (1996) J. Mol. Biol. , vol.262 , pp. 706-720
    • Kauppi, B.1
  • 20
    • 0042166135 scopus 로고    scopus 로고
    • Impaired function of p53R2 in Rrm2b-null mice causes severe renal failure through attenuation of dNTP pools
    • Kimura T., et al. Impaired function of p53R2 in Rrm2b-null mice causes severe renal failure through attenuation of dNTP pools. Nat. Genet. 2003, 34:440-445.
    • (2003) Nat. Genet. , vol.34 , pp. 440-445
    • Kimura, T.1
  • 22
    • 59149091263 scopus 로고    scopus 로고
    • A novel homozygous RRM2B missense mutation in association with severe mtDNA depletion
    • Kollberg G., et al. A novel homozygous RRM2B missense mutation in association with severe mtDNA depletion. Neuromuscul. Disord. 2009, 19:147-150.
    • (2009) Neuromuscul. Disord. , vol.19 , pp. 147-150
    • Kollberg, G.1
  • 23
    • 0036898541 scopus 로고    scopus 로고
    • Zebrafish as a model organism for the identification and characterization of drugs and genes affecting p53 signaling
    • Langheinrich U., Hennen E., Stott G., Vacun G. Zebrafish as a model organism for the identification and characterization of drugs and genes affecting p53 signaling. Curr. Biol. 2002, 12:2023-2028.
    • (2002) Curr. Biol. , vol.12 , pp. 2023-2028
    • Langheinrich, U.1    Hennen, E.2    Stott, G.3    Vacun, G.4
  • 24
    • 25644455941 scopus 로고    scopus 로고
    • The ribonucleotide reductase subunit M2B subcellular localization and functional importance for DNA replication in physiological growth of KB cells
    • Liu X., et al. The ribonucleotide reductase subunit M2B subcellular localization and functional importance for DNA replication in physiological growth of KB cells. Biochem. Pharmacol. 2005, 70:1288-1297.
    • (2005) Biochem. Pharmacol. , vol.70 , pp. 1288-1297
    • Liu, X.1
  • 25
    • 0035710746 scopus 로고    scopus 로고
    • Analysis of relative gene expression data using real-time quantitative PCR and the 2(-Delta Delta C(T)) method
    • Livak K.J., Schmittgen T.D. Analysis of relative gene expression data using real-time quantitative PCR and the 2(-Delta Delta C(T)) method. Methods 2001, 25:402-408.
    • (2001) Methods , vol.25 , pp. 402-408
    • Livak, K.J.1    Schmittgen, T.D.2
  • 26
    • 0034594895 scopus 로고    scopus 로고
    • P53 sends nucleotides to repair DNA
    • Lozano G., Elledge S.J. p53 sends nucleotides to repair DNA. Nature 2000, 404:24-25.
    • (2000) Nature , vol.404 , pp. 24-25
    • Lozano, G.1    Elledge, S.J.2
  • 27
    • 33746539166 scopus 로고    scopus 로고
    • DNA precursor metabolism and genomic stability
    • Mathews C.K. DNA precursor metabolism and genomic stability. FASEB J. 2006, 20:1300-1314.
    • (2006) FASEB J. , vol.20 , pp. 1300-1314
    • Mathews, C.K.1
  • 28
    • 0030440607 scopus 로고    scopus 로고
    • Cloning and sequencing of cDNAs encoding ribonucleotide reductase from zebrafish Danio rerio
    • Mathews C.Z., Sjoberg B.M., Karlsson M. Cloning and sequencing of cDNAs encoding ribonucleotide reductase from zebrafish Danio rerio. Mol. Mar. Biol. Biotechnol. 1996, 5:284-287.
    • (1996) Mol. Mar. Biol. Biotechnol. , vol.5 , pp. 284-287
    • Mathews, C.Z.1    Sjoberg, B.M.2    Karlsson, M.3
  • 29
    • 57049147881 scopus 로고    scopus 로고
    • Characterization of housekeeping genes in zebrafish: male-female differences and effects of tissue type, developmental stage and chemical treatment
    • McCurley A.T., Callard G.V. Characterization of housekeeping genes in zebrafish: male-female differences and effects of tissue type, developmental stage and chemical treatment. BMC Mol. Biol. 2008, 9:102.
    • (2008) BMC Mol. Biol. , vol.9 , pp. 102
    • McCurley, A.T.1    Callard, G.V.2
  • 30
    • 0034738967 scopus 로고    scopus 로고
    • A ribonucleotide reductase gene is a transcriptional target of p53 and p73
    • Nakano K., Balint E., Ashcroft M., Vousden K.H. A ribonucleotide reductase gene is a transcriptional target of p53 and p73. Oncogene 2000, 19:4283-4289.
    • (2000) Oncogene , vol.19 , pp. 4283-4289
    • Nakano, K.1    Balint, E.2    Ashcroft, M.3    Vousden, K.H.4
  • 32
    • 53249113140 scopus 로고    scopus 로고
    • A genotoxicity test system based on p53R2 gene expression in human cells: assessment of its reactivity to various classes of genotoxic chemicals
    • Ohno K., Ishihata K., Tanaka-Azuma Y., Yamada T. A genotoxicity test system based on p53R2 gene expression in human cells: assessment of its reactivity to various classes of genotoxic chemicals. Mutat. Res. 2008, 656:27-35.
    • (2008) Mutat. Res. , vol.656 , pp. 27-35
    • Ohno, K.1    Ishihata, K.2    Tanaka-Azuma, Y.3    Yamada, T.4
  • 33
    • 27744581861 scopus 로고    scopus 로고
    • Genotoxicity test system based on p53R2 gene expression in human cells: examination with 80 chemicals
    • Ohno K., Tanaka-Azuma Y., Yoneda Y., Yamada T. Genotoxicity test system based on p53R2 gene expression in human cells: examination with 80 chemicals. Mutat. Res. 2005, 588:47-57.
    • (2005) Mutat. Res. , vol.588 , pp. 47-57
    • Ohno, K.1    Tanaka-Azuma, Y.2    Yoneda, Y.3    Yamada, T.4
  • 34
    • 56649111359 scopus 로고    scopus 로고
    • Ribonucleotide reduction is a cytosolic process in mammalian cells independently of DNA damage
    • Pontarin G., et al. Ribonucleotide reduction is a cytosolic process in mammalian cells independently of DNA damage. Proc. Natl Acad. Sci. USA 2008, 105:17801-17806.
    • (2008) Proc. Natl Acad. Sci. USA , vol.105 , pp. 17801-17806
    • Pontarin, G.1
  • 35
    • 14644442937 scopus 로고    scopus 로고
    • Rapid development of glomerular injury and renal failure in mice lacking p53R2
    • Powell D.R., et al. Rapid development of glomerular injury and renal failure in mice lacking p53R2. Pediatr. Nephrol. 2005, 20:432-440.
    • (2005) Pediatr. Nephrol. , vol.20 , pp. 432-440
    • Powell, D.R.1
  • 36
    • 0033588374 scopus 로고    scopus 로고
    • Evidence by mutagenesis that Tyr(370) of the mouse ribonucleotide reductase R2 protein is the connecting link in the intersubunit radical transfer pathway
    • Rova U., Adrait A., Potsch S., Graslund A., Thelander L. Evidence by mutagenesis that Tyr(370) of the mouse ribonucleotide reductase R2 protein is the connecting link in the intersubunit radical transfer pathway. J. Biol. Chem. 1999, 274:23746-23751.
    • (1999) J. Biol. Chem. , vol.274 , pp. 23746-23751
    • Rova, U.1    Adrait, A.2    Potsch, S.3    Graslund, A.4    Thelander, L.5
  • 37
    • 0032555497 scopus 로고    scopus 로고
    • Kinetic evidence that a radical transfer pathway in protein R2 of mouse ribonucleotide reductase is involved in generation of the tyrosyl free radical. J. of Bio. Chem.
    • Schmidt, P. P., Rova, U., Katterle, B., Thelander, L., Graslund, A., 1998. Kinetic evidence that a radical transfer pathway in protein R2 of mouse ribonucleotide reductase is involved in generation of the tyrosyl free radical. J. of Bio. Chem. 273, 21463-21472.
    • (1998) , vol.273 , pp. 21463-21472
    • Schmidt, P.P.1    Rova, U.2    Katterle, B.3    Thelander, L.4    Graslund, A.5
  • 38
    • 1642453838 scopus 로고    scopus 로고
    • In vitro characterization of enzymatic properties and inhibition of the p53R2 subunit of human ribonucleotide reductase
    • Shao J., et al. In vitro characterization of enzymatic properties and inhibition of the p53R2 subunit of human ribonucleotide reductase. Cancer Res. 2004, 64:1-6.
    • (2004) Cancer Res. , vol.64 , pp. 1-6
    • Shao, J.1
  • 39
    • 72749119232 scopus 로고    scopus 로고
    • 2.6Å X-ray crystal structure of human p53R2, a p53-inducible ribonucleotide reductase
    • Smith P., et al. 2.6Å X-ray crystal structure of human p53R2, a p53-inducible ribonucleotide reductase. Biochemistry 2009, 48:11134-11141.
    • (2009) Biochemistry , vol.48 , pp. 11134-11141
    • Smith, P.1
  • 40
    • 0043240183 scopus 로고    scopus 로고
    • Cancer genetics and drug discovery in the zebrafish
    • Stern H.M., Zon L.I. Cancer genetics and drug discovery in the zebrafish. Nat. Rev. Cancer 2003, 3:533-539.
    • (2003) Nat. Rev. Cancer , vol.3 , pp. 533-539
    • Stern, H.M.1    Zon, L.I.2
  • 41
    • 0034594978 scopus 로고    scopus 로고
    • A ribonucleotide reductase gene involved in a p53-dependent cell-cycle checkpoint for DNA damage
    • Tanaka H., et al. A ribonucleotide reductase gene involved in a p53-dependent cell-cycle checkpoint for DNA damage. Nature 2000, 404:42-49.
    • (2000) Nature , vol.404 , pp. 42-49
    • Tanaka, H.1
  • 42
    • 38149126474 scopus 로고    scopus 로고
    • High-resolution in situ hybridization to whole-mount zebrafish embryos
    • Thisse C., Thisse B. High-resolution in situ hybridization to whole-mount zebrafish embryos. Nat. Protoc. 2008, 3:59-69.
    • (2008) Nat. Protoc. , vol.3 , pp. 59-69
    • Thisse, C.1    Thisse, B.2
  • 43
    • 3042615152 scopus 로고    scopus 로고
    • A new approach to 'megaprimer' polymerase chain reaction mutagenesis without an intermediate gel purification step
    • Tyagi R., Lai R., Duggleby R.G. A new approach to 'megaprimer' polymerase chain reaction mutagenesis without an intermediate gel purification step. BMC Biotechnol. 2004, 4:2.
    • (2004) BMC Biotechnol. , vol.4 , pp. 2
    • Tyagi, R.1    Lai, R.2    Duggleby, R.G.3
  • 44
    • 59649115646 scopus 로고    scopus 로고
    • Mouse models of mitochondrial DNA defects and their relevance for human disease
    • Tyynismaa H., Suomalainen A. Mouse models of mitochondrial DNA defects and their relevance for human disease. EMBO Rep. 2009, 10:137-143.
    • (2009) EMBO Rep. , vol.10 , pp. 137-143
    • Tyynismaa, H.1    Suomalainen, A.2
  • 45
    • 68249118218 scopus 로고    scopus 로고
    • A heterozygous truncating mutation in RRM2B causes autosomal-dominant progressive external ophthalmoplegia with multiple mtDNA deletions
    • Tyynismaa H., et al. A heterozygous truncating mutation in RRM2B causes autosomal-dominant progressive external ophthalmoplegia with multiple mtDNA deletions. Am. J. Hum. Genet. 2009, 85:290-295.
    • (2009) Am. J. Hum. Genet. , vol.85 , pp. 290-295
    • Tyynismaa, H.1
  • 46
    • 60249091269 scopus 로고    scopus 로고
    • Regulation of p53R2 and its role as potential target for cancer therapy
    • Wang X., Zhenchuk A., Wiman K.G., Albertioni F. Regulation of p53R2 and its role as potential target for cancer therapy. Cancer Lett. 2009, 276:1-7.
    • (2009) Cancer Lett. , vol.276 , pp. 1-7
    • Wang, X.1    Zhenchuk, A.2    Wiman, K.G.3    Albertioni, F.4
  • 48
    • 0037374051 scopus 로고    scopus 로고
    • Wild-type p53 regulates human ribonucleotide reductase by protein-protein interaction with p53R2 as well as hRRM2 subunits
    • Xue L., et al. Wild-type p53 regulates human ribonucleotide reductase by protein-protein interaction with p53R2 as well as hRRM2 subunits. Cancer Res. 2003, 63:980-986.
    • (2003) Cancer Res. , vol.63 , pp. 980-986
    • Xue, L.1
  • 49
    • 0035890408 scopus 로고    scopus 로고
    • P53R2-dependent pathway for DNA synthesis in a p53-regulated cell cycle checkpoint
    • Yamaguchi T., et al. p53R2-dependent pathway for DNA synthesis in a p53-regulated cell cycle checkpoint. Cancer Res. 2001, 61:8256-8262.
    • (2001) Cancer Res. , vol.61 , pp. 8256-8262
    • Yamaguchi, T.1
  • 50
    • 18844430787 scopus 로고    scopus 로고
    • Silencing of the p53R2 gene by RNA interference inhibits growth and enhances 5-fluorouracil sensitivity of oral cancer cells
    • Yanamoto S., et al. Silencing of the p53R2 gene by RNA interference inhibits growth and enhances 5-fluorouracil sensitivity of oral cancer cells. Cancer Lett. 2005, 223:67-76.
    • (2005) Cancer Lett. , vol.223 , pp. 67-76
    • Yanamoto, S.1
  • 51
    • 38449101066 scopus 로고    scopus 로고
    • Improvement in radiosensitivity using small interfering RNA targeting p53R2 in esophageal squamous cell carcinoma
    • Yokomakura N., et al. Improvement in radiosensitivity using small interfering RNA targeting p53R2 in esophageal squamous cell carcinoma. Oncol. Rep. 2007, 18:561-567.
    • (2007) Oncol. Rep. , vol.18 , pp. 561-567
    • Yokomakura, N.1
  • 52
    • 0025236555 scopus 로고
    • Tumor necrosis factor alpha and interferon gamma inhibit proliferation and alkaline phosphatase activity of human osteoblastic SaOS-2 cell line
    • Yoshihara R., Shiozawa S., Imai Y., Fujita T. Tumor necrosis factor alpha and interferon gamma inhibit proliferation and alkaline phosphatase activity of human osteoblastic SaOS-2 cell line. Lymphokine Res. 1990, 9:59-66.
    • (1990) Lymphokine Res. , vol.9 , pp. 59-66
    • Yoshihara, R.1    Shiozawa, S.2    Imai, Y.3    Fujita, T.4
  • 53
    • 0142250911 scopus 로고    scopus 로고
    • The human ribonucleotide reductase subunit hRRM2 complements p53R2 in response to UV-induced DNA repair in cells with mutant p53
    • Zhou B., et al. The human ribonucleotide reductase subunit hRRM2 complements p53R2 in response to UV-induced DNA repair in cells with mutant p53. Cancer Res. 2003, 63:6583-6594.
    • (2003) Cancer Res. , vol.63 , pp. 6583-6594
    • Zhou, B.1
  • 54
    • 0142250911 scopus 로고    scopus 로고
    • The human ribonucleotide reductase subunit hRRM2 complements p53R2 in response to UV-induced DNA repair in cells with mutant p53
    • Zhou B., et al. The human ribonucleotide reductase subunit hRRM2 complements p53R2 in response to UV-induced DNA repair in cells with mutant p53. Cancer Res. 2003, 63:6583-6594.
    • (2003) Cancer Res. , vol.63 , pp. 6583-6594
    • Zhou, B.1
  • 55


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