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Volumn 461, Issue 2, 2000, Pages 83-108

Going APE over ref-1

Author keywords

AP endonuclease; Ape1 Ref 1; Redox; Redox effector factor 1

Indexed keywords

BLEOMYCIN; CARMUSTINE; DNA (APURINIC OR APYRIMIDINIC SITE) LYASE; ENDONUCLEASE; HYDROGEN PEROXIDE; MENADIONE; MESYLIC ACID METHYL ESTER; NIMUSTINE; PARAQUAT; PROTEIN; TRANSCRIPTION FACTOR;

EID: 0034676227     PISSN: 09218777     EISSN: None     Source Type: Journal    
DOI: 10.1016/S0921-8777(00)00046-X     Document Type: Article
Times cited : (517)

References (158)
  • 1
    • 0025077481 scopus 로고
    • Redox regulation of Fos and Jun DNA-binding activity in vitro
    • Abate C., Patel L., Rauscher F.J.D., Curran T. Redox regulation of Fos and Jun DNA-binding activity in vitro. Science. 249:1990;1157-1161.
    • (1990) Science , vol.249 , pp. 1157-1161
    • Abate, C.1    Patel, L.2    Rauscher, F.J.D.3    Curran, T.4
  • 2
    • 0030903691 scopus 로고    scopus 로고
    • Redox regulation of the DNA binding activity in transcription factor PEBP2. The roles of two conserved cysteine residues
    • Akamatsu Y., Ohno T., Hirota K., Kagoshima H., Yodoi J., Shigesada K. Redox regulation of the DNA binding activity in transcription factor PEBP2. The roles of two conserved cysteine residues. J. Biol. Chem. 272:1997;14497-14500.
    • (1997) J. Biol. Chem. , vol.272 , pp. 14497-14500
    • Akamatsu, Y.1    Ohno, T.2    Hirota, K.3    Kagoshima, H.4    Yodoi, J.5    Shigesada, K.6
  • 3
    • 0028023142 scopus 로고
    • Structure, promoter analysis and chromosomal assignment of the human APEX gene
    • Akiyama K., Seki S., Oshida T., Yoshida M.C. Structure, promoter analysis and chromosomal assignment of the human APEX gene. Biochim. Biophys. Acta. 1219:1994;15-25.
    • (1994) Biochim. Biophys. Acta , vol.1219 , pp. 15-25
    • Akiyama, K.1    Seki, S.2    Oshida, T.3    Yoshida, M.C.4
  • 4
    • 0031560954 scopus 로고    scopus 로고
    • Increase in Ref-1 mRNA and protein by thyrotropin in rat thyroid FRTL-5 cells
    • Asai T., Kambe F., Kikumori T., Seo H. Increase in Ref-1 mRNA and protein by thyrotropin in rat thyroid FRTL-5 cells. Biochem. Biophys. Res. Commun. 236:1997;71-74.
    • (1997) Biochem. Biophys. Res. Commun. , vol.236 , pp. 71-74
    • Asai, T.1    Kambe, F.2    Kikumori, T.3    Seo, H.4
  • 5
    • 0028343506 scopus 로고
    • The Arabidopsis thaliana apurinic endonuclease Arp reduces human transcription factors Fos and Jun
    • Babiychuk E., Kushnir S., Van Montagu M., Inze D. The Arabidopsis thaliana apurinic endonuclease Arp reduces human transcription factors Fos and Jun. Proc. Natl. Acad. Sci. U. S. A. 91:1994;3299-3303.
    • (1994) Proc. Natl. Acad. Sci. U. S. A. , vol.91 , pp. 3299-3303
    • Babiychuk, E.1    Kushnir, S.2    Van Montagu, M.3    Inze, D.4
  • 6
    • 0029347105 scopus 로고
    • Structure and function of apurinic/apyrimidinic endonucleases
    • Barzilay G., Hickson I.D. Structure and function of apurinic/apyrimidinic endonucleases. Bioessays. 17:1995;713-719.
    • (1995) Bioessays , vol.17 , pp. 713-719
    • Barzilay, G.1    Hickson, I.D.2
  • 8
    • 0029010778 scopus 로고
    • Site-directed mutagenesis of the human DNA repair enzyme HAP1: Identification of residues important for AP endonuclease and RNase H activity
    • Barzilay G., Walker L.J., Robson C.N., Hickson I.D. Site-directed mutagenesis of the human DNA repair enzyme HAP1: identification of residues important for AP endonuclease and RNase H activity. Nucleic Acids Res. 23:1995;1544-1550.
    • (1995) Nucleic Acids Res. , vol.23 , pp. 1544-1550
    • Barzilay, G.1    Walker, L.J.2    Robson, C.N.3    Hickson, I.D.4
  • 9
    • 0030740948 scopus 로고    scopus 로고
    • Interaction of human apurinic endonuclease and DNA polymerase β in the base excision repair pathway
    • Bennett R.A., Wilson D.M. III, Wong D., Demple B. Interaction of human apurinic endonuclease and DNA polymerase β in the base excision repair pathway. Proc. Natl. Acad. Sci. U. S. A. 94:1997;7166-7169.
    • (1997) Proc. Natl. Acad. Sci. U. S. A. , vol.94 , pp. 7166-7169
    • Bennett, R.A.1    Wilson D.M. III2    Wong, D.3    Demple, B.4
  • 10
    • 0029131399 scopus 로고
    • Partial characterization of the human CYP1A1 negatively acting transcription factor and mutational analysis of its cognate DNA recognition sequence
    • Boucher P.D., Piechocki M.P., Hines R.N. Partial characterization of the human CYP1A1 negatively acting transcription factor and mutational analysis of its cognate DNA recognition sequence. Mol. Cell. Biol. 15:1995;5144-5151.
    • (1995) Mol. Cell. Biol. , vol.15 , pp. 5144-5151
    • Boucher, P.D.1    Piechocki, M.P.2    Hines, R.N.3
  • 11
    • 0033986948 scopus 로고    scopus 로고
    • Redox-regulated recruitment of the transcriptional coactivators CREB-binding protein and SRC-1 to hypoxia-inducible factor 1α
    • Carrero P., Okamoto K., Coumailleau P., O'Brien S., Tanaka H., Poellinger L. Redox-regulated recruitment of the transcriptional coactivators CREB-binding protein and SRC-1 to hypoxia-inducible factor 1α Mol. Cell. Biol. 20:2000;402-415.
    • (2000) Mol. Cell. Biol. , vol.20 , pp. 402-415
    • Carrero, P.1    Okamoto, K.2    Coumailleau, P.3    O'Brien, S.4    Tanaka, H.5    Poellinger, L.6
  • 12
    • 0028859503 scopus 로고
    • Induction of double-strand breaks by S1 nuclease, mung bean nuclease and nuclease P1 in DNA containing abasic sites and nicks
    • Chaudhry M.A., Weinfeld M. Induction of double-strand breaks by S1 nuclease, mung bean nuclease and nuclease P1 in DNA containing abasic sites and nicks. Nucleic Acids Res. 23:1995;3805-3809.
    • (1995) Nucleic Acids Res. , vol.23 , pp. 3805-3809
    • Chaudhry, M.A.1    Weinfeld, M.2
  • 13
    • 0026004662 scopus 로고
    • Two distinct human DNA diesterases that hydrolyze 3′-blocking deoxyribose fragments from oxidized DNA
    • Chen D.S., Herman T., Demple B. Two distinct human DNA diesterases that hydrolyze 3′-blocking deoxyribose fragments from oxidized DNA. Nucleic Acids Res. 19:1991;5907-5914.
    • (1991) Nucleic Acids Res. , vol.19 , pp. 5907-5914
    • Chen, D.S.1    Herman, T.2    Demple, B.3
  • 14
    • 0027497010 scopus 로고
    • Reduction of radiation cytotoxicity by human apurinic endonuclease in a radiation-sensitive Escherichia coli mutant
    • Chen D.S., Law C., Keng P. Reduction of radiation cytotoxicity by human apurinic endonuclease in a radiation-sensitive Escherichia coli mutant. Radiat. Res. 135:1993;405-410.
    • (1993) Radiat. Res. , vol.135 , pp. 405-410
    • Chen, D.S.1    Law, C.2    Keng, P.3
  • 15
    • 0028088601 scopus 로고
    • Biological responses of human apurinic endonuclease to radiation-induced DNA damage
    • Chen D.S., Olkowski Z.L. Biological responses of human apurinic endonuclease to radiation-induced DNA damage. Ann. NY Acad. Sci. 726:1994;306-308.
    • (1994) Ann. NY Acad. Sci. , vol.726 , pp. 306-308
    • Chen, D.S.1    Olkowski, Z.L.2
  • 16
    • 0024391088 scopus 로고
    • DNA binding site of the growth factor-inducible protein Zif268
    • Christy B., Nathans D. DNA binding site of the growth factor-inducible protein Zif268. Proc. Natl. Acad. Sci. U. S. A. 86:1989;8737-8741.
    • (1989) Proc. Natl. Acad. Sci. U. S. A. , vol.86 , pp. 8737-8741
    • Christy, B.1    Nathans, D.2
  • 18
    • 0028342951 scopus 로고
    • Repair of oxidative damage to DNA: Enzymology and biology
    • Demple B., Harrison L. Repair of oxidative damage to DNA: enzymology and biology. Annu. Rev. Biochem. 63:1994;915-948.
    • (1994) Annu. Rev. Biochem. , vol.63 , pp. 915-948
    • Demple, B.1    Harrison, L.2
  • 19
    • 0026323008 scopus 로고
    • Cloning and expression of APE, the cDNA encoding the major human apurinic endonuclease: Definition of a family of DNA repair enzymes
    • Demple B., Herman T., Chen D.S. Cloning and expression of APE, the cDNA encoding the major human apurinic endonuclease: definition of a family of DNA repair enzymes. Proc. Natl. Acad. Sci. U. S. A. 88:1991;11450-11454.
    • (1991) Proc. Natl. Acad. Sci. U. S. A. , vol.88 , pp. 11450-11454
    • Demple, B.1    Herman, T.2    Chen, D.S.3
  • 20
    • 0033546417 scopus 로고    scopus 로고
    • Redox factor-1 (Ref-1) mediates the activation of AP-1 in HeLa and NIH 3T3 cells in response to heat shock
    • Diamond D.A., Parsian A., Hunt C.R., Lofgren S., Spitz D.R., Goswami P.C., Gius D. Redox factor-1 (Ref-1) mediates the activation of AP-1 in HeLa and NIH 3T3 cells in response to heat shock. J. Biol. Chem. 274:1999;16959-16964.
    • (1999) J. Biol. Chem. , vol.274 , pp. 16959-16964
    • Diamond, D.A.1    Parsian, A.2    Hunt, C.R.3    Lofgren, S.4    Spitz, D.R.5    Goswami, P.C.6    Gius, D.7
  • 21
    • 0025120572 scopus 로고
    • The enzymology of apurinic/apyrimidinic endonucleases
    • Doetsch P.W., Cunningham R.P. The enzymology of apurinic/apyrimidinic endonucleases. Mutat. Res. 236:1990;173-201.
    • (1990) Mutat. Res. , vol.236 , pp. 173-201
    • Doetsch, P.W.1    Cunningham, R.P.2
  • 22
    • 0028858334 scopus 로고
    • Differential cellular and subcellular expression of the human multifunctional apurinic/apyrimidinic endonuclease (APE/Ref-1) DNA repair enzyme
    • Duguid J.R., Eble J.N., Wilson T.M., Kelley M.R. Differential cellular and subcellular expression of the human multifunctional apurinic/apyrimidinic endonuclease (APE/Ref-1) DNA repair enzyme. Cancer Res. 55:1995;6097-6102.
    • (1995) Cancer Res. , vol.55 , pp. 6097-6102
    • Duguid, J.R.1    Eble, J.N.2    Wilson, T.M.3    Kelley, M.R.4
  • 25
    • 0033118983 scopus 로고    scopus 로고
    • Molecular mechanisms of transcription activation by HLF and HIF-1α in response to hypoxia: Their stabilization and redox signal-induced interaction with CBP/p300
    • Ema M., Hirota K., Mimura J., Abe H., Yodoi J., Sogawa K., Poellinger L., Fujii-Kuriyama Y. Molecular mechanisms of transcription activation by HLF and HIF-1α in response to hypoxia: their stabilization and redox signal-induced interaction with CBP/p300. Embo. J. 18:1999;1905-1914.
    • (1999) Embo. J. , vol.18 , pp. 1905-1914
    • Ema, M.1    Hirota, K.2    Mimura, J.3    Abe, H.4    Yodoi, J.5    Sogawa, K.6    Poellinger, L.7    Fujii-Kuriyama, Y.8
  • 26
    • 84961981834 scopus 로고    scopus 로고
    • Elements in abasic site recognition by the major human and Escherichia coli apurinic/apyrimidinic endonucleases
    • Erzberger J.P., Barsky D., Scharer O.D., Colvin M.E., Wilson D.M. III Elements in abasic site recognition by the major human and Escherichia coli apurinic/apyrimidinic endonucleases. Nucleic Acids Res. 26:1998;2771-2778.
    • (1998) Nucleic Acids Res. , vol.26 , pp. 2771-2778
    • Erzberger, J.P.1    Barsky, D.2    Scharer, O.D.3    Colvin, M.E.4    Wilson D.M. III5
  • 27
    • 0033538343 scopus 로고    scopus 로고
    • 2+ and specific amino acid residues in the catalytic reaction of the major human abasic endonuclease: New insights from EDTA-resistant incision of acyclic abasic site analogs and site-directed mutagenesis
    • 2+ and specific amino acid residues in the catalytic reaction of the major human abasic endonuclease: new insights from EDTA-resistant incision of acyclic abasic site analogs and site-directed mutagenesis. J. Mol. Biol. 290:1999;447-457.
    • (1999) J. Mol. Biol. , vol.290 , pp. 447-457
    • Erzberger, J.P.1    Wilson D.M. III2
  • 28
    • 0022167665 scopus 로고
    • Nucleotide excision repair of DNA in eukaryotes: Comparisons between human cells and yeast
    • Friedberg E.C. Nucleotide excision repair of DNA in eukaryotes: comparisons between human cells and yeast. Cancer Surv. 4:1985;529-555.
    • (1985) Cancer Surv. , vol.4 , pp. 529-555
    • Friedberg, E.C.1
  • 29
    • 0033611583 scopus 로고    scopus 로고
    • Phosphorylation of the DNA repair protein APE/Ref-1 by CKII affects redox regulation of AP-1
    • Fritz G., Kaina B. Phosphorylation of the DNA repair protein APE/Ref-1 by CKII affects redox regulation of AP-1. Oncogene. 18:1999;1033-1040.
    • (1999) Oncogene , vol.18 , pp. 1033-1040
    • Fritz, G.1    Kaina, B.2
  • 31
    • 0033502803 scopus 로고    scopus 로고
    • Early decrease of apurinic/apyrimidinic endonuclease expression after transient focal cerebral ischemia in mice
    • Fujimura M., Morita-Fujimura Y., Kawase M., Chan P.H. Early decrease of apurinic/apyrimidinic endonuclease expression after transient focal cerebral ischemia in mice. J. Cereb. Blood Flow Metab. 19:1999;495-501.
    • (1999) J. Cereb. Blood Flow Metab. , vol.19 , pp. 495-501
    • Fujimura, M.1    Morita-Fujimura, Y.2    Kawase, M.3    Chan, P.H.4
  • 33
    • 0033570048 scopus 로고    scopus 로고
    • Ref-1 regulates the transactivation and pro-apoptotic functions of p53 in vivo
    • Gaiddon C., Moorthy N.C., Prives C. Ref-1 regulates the transactivation and pro-apoptotic functions of p53 in vivo. Embo. J. 18:1999;5609-5621.
    • (1999) Embo. J. , vol.18 , pp. 5609-5621
    • Gaiddon, C.1    Moorthy, N.C.2    Prives, C.3
  • 34
    • 0032702707 scopus 로고    scopus 로고
    • Transcriptional activation by the Myb proteins requires a specific local promoter structure
    • Ganter B., Chao S.T., Lipsick J.S. Transcriptional activation by the Myb proteins requires a specific local promoter structure. FEBS Lett. 460:1999;401-410.
    • (1999) FEBS Lett. , vol.460 , pp. 401-410
    • Ganter, B.1    Chao, S.T.2    Lipsick, J.S.3
  • 35
    • 0040389654 scopus 로고    scopus 로고
    • Expression of nuclear redox factor Ref-1 in the rat hippocampus following global ischemia induced by cardiac arrest
    • Gillardon F., Bottiger B., Hossmann K.A. Expression of nuclear redox factor Ref-1 in the rat hippocampus following global ischemia induced by cardiac arrest. Brain Res. Mol. Brain Res. 52:1997;194-200.
    • (1997) Brain Res. Mol. Brain Res. , vol.52 , pp. 194-200
    • Gillardon, F.1    Bottiger, B.2    Hossmann, K.A.3
  • 36
    • 0030728449 scopus 로고    scopus 로고
    • The crystal structure of the human DNA repair endonuclease HAP1 suggests the recognition of extra-helical deoxyribose at DNA abasic sites
    • Gorman M.A., Morera S., Rothwell D.G., de La Fortelle E., Mol C.D., Tainer J.A., Hickson I.D., Freemont P.S. The crystal structure of the human DNA repair endonuclease HAP1 suggests the recognition of extra-helical deoxyribose at DNA abasic sites. Embo. J. 16:1997;6548-6558.
    • (1997) Embo. J. , vol.16 , pp. 6548-6558
    • Gorman, M.A.1    Morera, S.2    Rothwell, D.G.3    De La Fortelle, E.4    Mol, C.D.5    Tainer, J.A.6    Hickson, I.D.7    Freemont, P.S.8
  • 37
    • 0029980043 scopus 로고    scopus 로고
    • p53 in growth control and neoplasia
    • Gottlieb T.M., Oren M. p53 in growth control and neoplasia. Biochim. Biophys. Acta. 1287:1996;77-102.
    • (1996) Biochim. Biophys. Acta , vol.1287 , pp. 77-102
    • Gottlieb, T.M.1    Oren, M.2
  • 38
    • 0030025773 scopus 로고    scopus 로고
    • Hypoxia-mediated selection of cells with diminished apoptotic potential in solid tumours (see comments)
    • Graeber T.G., Osmanian C., Jacks T., Housman D.E., Koch C.J., Lowe S.W., Giaccia A.J. Hypoxia-mediated selection of cells with diminished apoptotic potential in solid tumours (see comments). Nature. 379:1996;88-91.
    • (1996) Nature , vol.379 , pp. 88-91
    • Graeber, T.G.1    Osmanian, C.2    Jacks, T.3    Housman, D.E.4    Koch, C.J.5    Lowe, S.W.6    Giaccia, A.J.7
  • 39
    • 0032188756 scopus 로고    scopus 로고
    • Apurinic endonuclease (Ref-1) is induced in mammalian cells by oxidative stress and involved in clastogenic adaptation
    • Grosch S., Fritz G., Kaina B. Apurinic endonuclease (Ref-1) is induced in mammalian cells by oxidative stress and involved in clastogenic adaptation. Cancer Res. 58:1998;4410-4416.
    • (1998) Cancer Res. , vol.58 , pp. 4410-4416
    • Grosch, S.1    Fritz, G.2    Kaina, B.3
  • 40
    • 0344980129 scopus 로고    scopus 로고
    • Transcriptional activation of apurinic/apyrimidinic endonuclease (Ape, Ref-1) by oxidative stress requires CREB
    • Grosch S., Kaina B. Transcriptional activation of apurinic/apyrimidinic endonuclease (Ape, Ref-1) by oxidative stress requires CREB. Biochem. Biophys. Res. Commun. 261:1999;859-863.
    • (1999) Biochem. Biophys. Res. Commun. , vol.261 , pp. 859-863
    • Grosch, S.1    Kaina, B.2
  • 42
    • 0032588585 scopus 로고    scopus 로고
    • HIF-1α and p53 promote hypoxia-induced delayed neuronal death in models of CNS ischemia
    • Halterman M.W., Federoff H.J. HIF-1α and p53 promote hypoxia-induced delayed neuronal death in models of CNS ischemia. Exp. Neurol. 159:1999;65-72.
    • (1999) Exp. Neurol. , vol.159 , pp. 65-72
    • Halterman, M.W.1    Federoff, H.J.2
  • 43
    • 0031984661 scopus 로고    scopus 로고
    • Creation of a fully functional human chimeric DNA repair protein. Combining O6-methylguanine DNA methyltransferase (MGMT) and AP endonuclease (APE/redox effector factor 1 (Ref-1)) DNA repair proteins
    • Hansen W.K., Deutsch W.A., Yacoub A., Xu Y., Williams D.A., Kelley M.R. Creation of a fully functional human chimeric DNA repair protein. Combining O6-methylguanine DNA methyltransferase (MGMT) and AP endonuclease (APE/redox effector factor 1 (Ref-1)) DNA repair proteins. J. Biol. Chem. 273:1998;756-762.
    • (1998) J. Biol. Chem. , vol.273 , pp. 756-762
    • Hansen, W.K.1    Deutsch, W.A.2    Yacoub, A.3    Xu, Y.4    Williams, D.A.5    Kelley, M.R.6
  • 45
    • 0031414852 scopus 로고    scopus 로고
    • Comparison of the promoters of the mouse (APEX) and human (APE) apurinic endonuclease genes
    • Harrison L., Ascione A.G., Takiguchi Y., Wilson D.M. III, Chen D.J., Demple B. Comparison of the promoters of the mouse (APEX) and human (APE) apurinic endonuclease genes. Mutat. Res. 385:1997;159-172.
    • (1997) Mutat. Res. , vol.385 , pp. 159-172
    • Harrison, L.1    Ascione, A.G.2    Takiguchi, Y.3    Wilson D.M. III4    Chen, D.J.5    Demple, B.6
  • 46
    • 0028918766 scopus 로고
    • Characterization of the promoter region of the human apurinic endonuclease gene (APE)
    • Harrison L., Ascione A.G., Wilson D.M. III, Demple B. Characterization of the promoter region of the human apurinic endonuclease gene (APE). J. Biol. Chem. 270:1995;5556-5564.
    • (1995) J. Biol. Chem. , vol.270 , pp. 5556-5564
    • Harrison, L.1    Ascione, A.G.2    Wilson D.M. III3    Demple, B.4
  • 48
    • 0029939856 scopus 로고    scopus 로고
    • Regulated expression of APE apurinic endonuclease mRNA during wound healing in porcine epidermis
    • Harrison L., Galanopoulos T., Ascione A.G., Antoniades H.N., Demple B. Regulated expression of APE apurinic endonuclease mRNA during wound healing in porcine epidermis. Carcinogenesis. 17:1996;377-381.
    • (1996) Carcinogenesis , vol.17 , pp. 377-381
    • Harrison, L.1    Galanopoulos, T.2    Ascione, A.G.3    Antoniades, H.N.4    Demple, B.5
  • 51
  • 52
    • 0029753008 scopus 로고    scopus 로고
    • Activation of hypoxia-inducible transcription factor depends primarily upon redox-sensitive stabilization of its α subunit
    • Huang L.E., Arany Z., Livingston D.M., Bunn H.F. Activation of hypoxia-inducible transcription factor depends primarily upon redox-sensitive stabilization of its α subunit. J. Biol. Chem. 271:1996;32253-32259.
    • (1996) J. Biol. Chem. , vol.271 , pp. 32253-32259
    • Huang, L.E.1    Arany, Z.2    Livingston, D.M.3    Bunn, H.F.4
  • 53
    • 0027456704 scopus 로고
    • Characterization of the DNA-binding properties of the early growth response-1 (Egr-1) transcription factor: Evidence for modulation by a redox mechanism
    • Huang R.P., Adamson E.D. Characterization of the DNA-binding properties of the early growth response-1 (Egr-1) transcription factor: evidence for modulation by a redox mechanism. DNA Cell Biol. 12:1993;265-273.
    • (1993) DNA Cell Biol. , vol.12 , pp. 265-273
    • Huang, R.P.1    Adamson, E.D.2
  • 56
    • 0026465075 scopus 로고
    • Overexpression of human DNA repair protein N-methylpurine-DNA glycosylase results in the increased removal of N-methylpurines in DNA without a concomitant increase in resistance to alkylating agents in Chinese hamster ovary cells
    • Ibeanu G., Hartenstein B., Dunn W.C., Chang L.Y., Hofmann E., Coquerelle T., Mitra S., Kaina B. Overexpression of human DNA repair protein N-methylpurine-DNA glycosylase results in the increased removal of N-methylpurines in DNA without a concomitant increase in resistance to alkylating agents in Chinese hamster ovary cells. Carcinogenesis. 13:1992;1989-1995.
    • (1992) Carcinogenesis , vol.13 , pp. 1989-1995
    • Ibeanu, G.1    Hartenstein, B.2    Dunn, W.C.3    Chang, L.Y.4    Hofmann, E.5    Coquerelle, T.6    Mitra, S.7    Kaina, B.8
  • 57
    • 0030478864 scopus 로고    scopus 로고
    • Negative regulation of the major human AP-endonuclease, a multifunctional protein
    • Izumi T., Henner W.D., Mitra S. Negative regulation of the major human AP-endonuclease, a multifunctional protein. Biochemistry. 35:1996;14679-14683.
    • (1996) Biochemistry , vol.35 , pp. 14679-14683
    • Izumi, T.1    Henner, W.D.2    Mitra, S.3
  • 58
    • 0033583089 scopus 로고    scopus 로고
    • Intragenic suppression of an active site mutation in the human apurinic/apyrimidinic endonuclease
    • Izumi T., Malecki J., Chaudhry M.A., Weinfeld M., Hill J.H., Lee J.C., Mitra S. Intragenic suppression of an active site mutation in the human apurinic/apyrimidinic endonuclease. J. Mol. Biol. 287:1999;47-57.
    • (1999) J. Mol. Biol. , vol.287 , pp. 47-57
    • Izumi, T.1    Malecki, J.2    Chaudhry, M.A.3    Weinfeld, M.4    Hill, J.H.5    Lee, J.C.6    Mitra, S.7
  • 59
    • 0031901923 scopus 로고    scopus 로고
    • Deletion analysis of human AP-endonuclease: Minimum sequence required for the endonuclease activity
    • Izumi T., Mitra S. Deletion analysis of human AP-endonuclease: minimum sequence required for the endonuclease activity. Carcinogenesis. 19:1998;525-527.
    • (1998) Carcinogenesis , vol.19 , pp. 525-527
    • Izumi, T.1    Mitra, S.2
  • 62
  • 65
    • 0032909814 scopus 로고    scopus 로고
    • Reduction of apurinic/apyrimidinic endonuclease expression after transient global cerebral ischemia in rats: Implication of the failure of DNA repair in neuronal apoptosis
    • Kawase M., Fujimura M., Morita-Fujimura Y., Chan P.H. Reduction of apurinic/apyrimidinic endonuclease expression after transient global cerebral ischemia in rats: implication of the failure of DNA repair in neuronal apoptosis. Stroke. 30:1999;441-449.
    • (1999) Stroke , vol.30 , pp. 441-449
    • Kawase, M.1    Fujimura, M.2    Morita-Fujimura, Y.3    Chan, P.H.4
  • 67
    • 0002912067 scopus 로고    scopus 로고
    • The multifunctional DNA base excision repair and redox protein, AP endonuclease (APE/Ref-1), and its role in germ cell tumors
    • (Eds.), Jonh Libbey and Co., London, UK
    • M.R. Kelley, Y. Xu, R. Tritt, K.A. Robertson (Eds.), The multifunctional DNA base excision repair and redox protein, AP endonuclease (APE/Ref-1), and its role in germ cell tumors, in: Germ Cell Tumors, Vol. IV, Jonh Libbey and Co., London, UK, 1998, pp. 81-86.
    • (1998) In: Germ Cell Tumors , vol.4 , pp. 81-86
    • Kelley, M.R.1    Xu, Y.2    Tritt, R.3    Robertson, K.A.4
  • 68
    • 0029073989 scopus 로고
    • Implication of mammalian ribosomal protein S3 in the processing of DNA damage
    • Kim J., Chubatsu L.S., Admon A., Stahl J., Fellous R., Linn S. Implication of mammalian ribosomal protein S3 in the processing of DNA damage. J. Biol. Chem. 270:1995;13620-13629.
    • (1995) J. Biol. Chem. , vol.270 , pp. 13620-13629
    • Kim, J.1    Chubatsu, L.S.2    Admon, A.3    Stahl, J.4    Fellous, R.5    Linn, S.6
  • 69
    • 0030916372 scopus 로고    scopus 로고
    • Evidence of reduced DNA repair in amyotrophic lateral sclerosis brain tissue
    • Kisby G.E., Milne J., Sweatt C. Evidence of reduced DNA repair in amyotrophic lateral sclerosis brain tissue. Neuroreport. 8:1997;1337-1340.
    • (1997) Neuroreport , vol.8 , pp. 1337-1340
    • Kisby, G.E.1    Milne, J.2    Sweatt, C.3
  • 70
    • 0030957997 scopus 로고    scopus 로고
    • Second pathway for completion of human DNA base excision-repair: Reconstitution with purified proteins and requirement for DNase IV (FEN1)
    • Klungland A., Lindahl T. Second pathway for completion of human DNA base excision-repair: reconstitution with purified proteins and requirement for DNase IV (FEN1). Embo. J. 16:1997;3341-3348.
    • (1997) Embo. J. , vol.16 , pp. 3341-3348
    • Klungland, A.1    Lindahl, T.2
  • 71
    • 0034681378 scopus 로고    scopus 로고
    • A redox mechanism controls differential DNA binding activities of hypoxia-inducible factor (HIF) 1α and the HIF-like factor
    • Lando D., Pongratz I., Poellinger L., Whitelaw M.L. A redox mechanism controls differential DNA binding activities of hypoxia-inducible factor (HIF) 1α and the HIF-like factor. J. Biol. Chem. 275:2000;4618-4627.
    • (2000) J. Biol. Chem. , vol.275 , pp. 4618-4627
    • Lando, D.1    Pongratz, I.2    Poellinger, L.3    Whitelaw, M.L.4
  • 72
    • 0030941458 scopus 로고    scopus 로고
    • p53 the cellular gatekeeper for growth and division
    • Levine A.J. p53 the cellular gatekeeper for growth and division. Cell. 88:1997;323-331.
    • (1997) Cell , vol.88 , pp. 323-331
    • Levine, A.J.1
  • 73
    • 0015504248 scopus 로고
    • Rate of depurination of native deoxyribonucleic acid
    • Lindahl T., Nyberg B. Rate of depurination of native deoxyribonucleic acid. Biochemistry. 11:1972;3610-3618.
    • (1972) Biochemistry , vol.11 , pp. 3610-3618
    • Lindahl, T.1    Nyberg, B.2
  • 74
    • 0023015325 scopus 로고
    • Mutagenesis by apurinic/apyrimidinic sites
    • Loeb L.A., Preston B.D. Mutagenesis by apurinic/apyrimidinic sites. Annu. Rev. Genet. 20:1986;201-230.
    • (1986) Annu. Rev. Genet. , vol.20 , pp. 201-230
    • Loeb, L.A.1    Preston, B.D.2
  • 75
    • 0033586728 scopus 로고    scopus 로고
    • Single-turnover analysis of mutant human apurinic/apyrimidinic endonuclease
    • Lucas J.A., Masuda Y., Bennett R.A., Strauss N.S., Strauss P.R. Single-turnover analysis of mutant human apurinic/apyrimidinic endonuclease. Biochemistry. 38:1999;4958-4964.
    • (1999) Biochemistry , vol.38 , pp. 4958-4964
    • Lucas, J.A.1    Masuda, Y.2    Bennett, R.A.3    Strauss, N.S.4    Strauss, P.R.5
  • 76
    • 0025115303 scopus 로고
    • Immunoelectron microscopic studies on the location of ribosomal proteins on the surface of the 40S ribosomal subunit from rat liver
    • Lutsch G., Stahl J., Kargel H.J., Noll F., Bielka H. Immunoelectron microscopic studies on the location of ribosomal proteins on the surface of the 40S ribosomal subunit from rat liver. Eur. J. Cell. Biol. 51:1990;140-150.
    • (1990) Eur. J. Cell. Biol. , vol.51 , pp. 140-150
    • Lutsch, G.1    Stahl, J.2    Kargel, H.J.3    Noll, F.4    Bielka, H.5
  • 77
    • 0029804576 scopus 로고    scopus 로고
    • Thioredoxin: A redox-regulating cellular cofactor for glucocorticoid hormone action. Cross talk between endocrine control of stress response and cellular antioxidant defense system
    • Makino Y., Okamoto K., Yoshikawa N., Aoshima M., Hirota K., Yodoi J., Umesono K., Makino I., Tanaka H. Thioredoxin: a redox-regulating cellular cofactor for glucocorticoid hormone action. Cross talk between endocrine control of stress response and cellular antioxidant defense system. J. Clin. Invest. 98:1996;2469-2477.
    • (1996) J. Clin. Invest. , vol.98 , pp. 2469-2477
    • Makino, Y.1    Okamoto, K.2    Yoshikawa, N.3    Aoshima, M.4    Hirota, K.5    Yodoi, J.6    Umesono, K.7    Makino, I.8    Tanaka, H.9
  • 78
    • 0030560994 scopus 로고    scopus 로고
    • Pax genes and their roles in cell differentiation and development
    • Mansouri A., Hallonet M., Gruss P. Pax genes and their roles in cell differentiation and development. Curr. Opinion Cell. Biol. 8:1996;851-857.
    • (1996) Curr. Opinion Cell. Biol. , vol.8 , pp. 851-857
    • Mansouri, A.1    Hallonet, M.2    Gruss, P.3
  • 79
    • 0032515143 scopus 로고    scopus 로고
    • Dynamics of the interaction of human apurinic endonuclease (Ape1) with its substrate and product
    • Masuda Y., Bennett R.A., Demple B. Dynamics of the interaction of human apurinic endonuclease (Ape1) with its substrate and product. J. Biol. Chem. 273:1998;30352-30359.
    • (1998) J. Biol. Chem. , vol.273 , pp. 30352-30359
    • Masuda, Y.1    Bennett, R.A.2    Demple, B.3
  • 80
    • 0032515067 scopus 로고    scopus 로고
    • Rapid dissociation of human apurinic endonuclease (Ape1) from incised DNA induced by magnesium
    • Masuda Y., Bennett R.A., Demple B. Rapid dissociation of human apurinic endonuclease (Ape1) from incised DNA induced by magnesium. J. Biol. Chem. 273:1998;30360-30365.
    • (1998) J. Biol. Chem. , vol.273 , pp. 30360-30365
    • Masuda, Y.1    Bennett, R.A.2    Demple, B.3
  • 82
    • 0029028964 scopus 로고
    • Excision of deoxyribose phosphate residues by DNA polymerase β during DNA repair
    • Matsumoto Y., Kim K. Excision of deoxyribose phosphate residues by DNA polymerase β during DNA repair. Science. 269:1995;699-702.
    • (1995) Science , vol.269 , pp. 699-702
    • Matsumoto, Y.1    Kim, K.2
  • 83
    • 0027963233 scopus 로고
    • Two different cellular redox systems regulate the DNA-binding activity of the p50 subunit of NF-κB in vitro
    • Mitomo K., Nakayama K., Fujimoto K., Sun X., Seki S., Yamamoto K. Two different cellular redox systems regulate the DNA-binding activity of the p50 subunit of NF-κB in vitro. Gene. 145:1994;197-203.
    • (1994) Gene , vol.145 , pp. 197-203
    • Mitomo, K.1    Nakayama, K.2    Fujimoto, K.3    Sun, X.4    Seki, S.5    Yamamoto, K.6
  • 85
    • 0027351670 scopus 로고
    • Regulation of repair of alkylation damage in mammalian genomes
    • Mitra S., Kaina B. Regulation of repair of alkylation damage in mammalian genomes. Prog. Nucleic Acid Res. Mol. Biol. 44:1993;109-142.
    • (1993) Prog. Nucleic Acid Res. Mol. Biol. , vol.44 , pp. 109-142
    • Mitra, S.1    Kaina, B.2
  • 86
    • 0034719372 scopus 로고    scopus 로고
    • DNA-bound structures and mutants reveal abasic DNA binding by APE1 DNA repair and coordination
    • Mol C.D., Izumi T., Mitra S., Tainer J.A. DNA-bound structures and mutants reveal abasic DNA binding by APE1 DNA repair and coordination. Nature. 403:2000;451-456.
    • (2000) Nature , vol.403 , pp. 451-456
    • Mol, C.D.1    Izumi, T.2    Mitra, S.3    Tainer, J.A.4
  • 87
    • 0028923440 scopus 로고
    • Structure and function of the multifunctional DNA-repair enzyme exonuclease III
    • Mol C.D., Kuo C.F., Thayer M.M., Cunningham R.P., Tainer J.A. Structure and function of the multifunctional DNA-repair enzyme exonuclease III. Nature. 374:1995;381-386.
    • (1995) Nature , vol.374 , pp. 381-386
    • Mol, C.D.1    Kuo, C.F.2    Thayer, M.M.3    Cunningham, R.P.4    Tainer, J.A.5
  • 88
    • 0033961301 scopus 로고    scopus 로고
    • Alterations in the expression of the DNA repair/redox enzyme APE/Ref-1 in epithelial ovarian cancers
    • Moore D.H., Michael H., Tritt R., Parsons S.H., Kelley M.R. Alterations in the expression of the DNA repair/redox enzyme APE/Ref-1 in epithelial ovarian cancers. Clin. Cancer Res. 6:2000;602-609.
    • (2000) Clin. Cancer Res. , vol.6 , pp. 602-609
    • Moore, D.H.1    Michael, H.2    Tritt, R.3    Parsons, S.H.4    Kelley, M.R.5
  • 89
    • 0032801797 scopus 로고    scopus 로고
    • Early decrease in apurinic/apyrimidinic endonuclease is followed by DNA fragmentation after cold injury-induced brain trauma in mice
    • Morita-Fujimura Y., Fujimura M., Kawase M., Chan P.H. Early decrease in apurinic/apyrimidinic endonuclease is followed by DNA fragmentation after cold injury-induced brain trauma in mice. Neuroscience. 93:1999;1465-1473.
    • (1999) Neuroscience , vol.93 , pp. 1465-1473
    • Morita-Fujimura, Y.1    Fujimura, M.2    Kawase, M.3    Chan, P.H.4
  • 90
    • 0033152195 scopus 로고    scopus 로고
    • Endogenous apurinic/apyrimidinic sites in genomic DNA of mammalian tissues
    • Nakamura J., Swenberg J.A. Endogenous apurinic/apyrimidinic sites in genomic DNA of mammalian tissues. Cancer Res. 59:1999;2522-2526.
    • (1999) Cancer Res. , vol.59 , pp. 2522-2526
    • Nakamura, J.1    Swenberg, J.A.2
  • 91
    • 0031984807 scopus 로고    scopus 로고
    • Highly sensitive apurinic/apyrimidinic site assay can detect spontaneous and chemically induced depurination under physiological conditions
    • Nakamura J., Walker V.E., Upton P.B., Chiang S.Y., Kow Y.W., Swenberg J.A. Highly sensitive apurinic/apyrimidinic site assay can detect spontaneous and chemically induced depurination under physiological conditions. Cancer Res. 58:1998;222-225.
    • (1998) Cancer Res. , vol.58 , pp. 222-225
    • Nakamura, J.1    Walker, V.E.2    Upton, P.B.3    Chiang, S.Y.4    Kow, Y.W.5    Swenberg, J.A.6
  • 92
    • 0029804314 scopus 로고    scopus 로고
    • Subunit association and DNA binding activity of the heterotrimeric transcription factor NF-Y is regulated by cellular redox
    • Nakshatri H., Bhat-Nakshatri P., Currie R.A. Subunit association and DNA binding activity of the heterotrimeric transcription factor NF-Y is regulated by cellular redox. J. Biol. Chem. 271:1996;28784-28791.
    • (1996) J. Biol. Chem. , vol.271 , pp. 28784-28791
    • Nakshatri, H.1    Bhat-Nakshatri, P.2    Currie, R.A.3
  • 93
    • 0024239413 scopus 로고
    • The avian cellular homolog of the oncogene Jun
    • Nishimura T., Vogt P.K. The avian cellular homolog of the oncogene Jun. Oncogene. 3:1988;659-663.
    • (1988) Oncogene , vol.3 , pp. 659-663
    • Nishimura, T.1    Vogt, P.K.2
  • 95
    • 0027506460 scopus 로고
    • Escape from redox regulation enhances the transforming activity of Fos
    • Okuno H., Akahori A., Sato H., Xanthoudakis S., Curran T., Iba H. Escape from redox regulation enhances the transforming activity of Fos. Oncogene. 8:1993;695-701.
    • (1993) Oncogene , vol.8 , pp. 695-701
    • Okuno, H.1    Akahori, A.2    Sato, H.3    Xanthoudakis, S.4    Curran, T.5    Iba, H.6
  • 96
    • 0032567807 scopus 로고    scopus 로고
    • Mutant AP endonuclease in patients with amyotrophic lateral sclerosis
    • Olkowski Z.L. Mutant AP endonuclease in patients with amyotrophic lateral sclerosis. Neuroreport. 9:1998;239-242.
    • (1998) Neuroreport , vol.9 , pp. 239-242
    • Olkowski, Z.L.1
  • 97
    • 0028244814 scopus 로고
    • Stable expression in rat glioma cells of sense and antisense nucleic acids to a human multifunctional DNA repair enzyme APEX nuclease
    • Ono Y., Furuta T., Ohmoto T., Akiyama K., Seki S. Stable expression in rat glioma cells of sense and antisense nucleic acids to a human multifunctional DNA repair enzyme APEX nuclease. Mutat. Res. 315:1994;55-63.
    • (1994) Mutat. Res. , vol.315 , pp. 55-63
    • Ono, Y.1    Furuta, T.2    Ohmoto, T.3    Akiyama, K.4    Seki, S.5
  • 98
    • 0028823440 scopus 로고
    • Relationship between expression of a major apurinic/apyrimidinic endonuclease (APEX nuclease) and susceptibility to genotoxic agents in human glioma cell lines
    • Ono Y., Matsumoto K., Furuta T., Ohmoto T., Akiyama K., Seki S. Relationship between expression of a major apurinic/apyrimidinic endonuclease (APEX nuclease) and susceptibility to genotoxic agents in human glioma cell lines. J. Neurooncol. 25:1995;183-192.
    • (1995) J. Neurooncol. , vol.25 , pp. 183-192
    • Ono, Y.1    Matsumoto, K.2    Furuta, T.3    Ohmoto, T.4    Akiyama, K.5    Seki, S.6
  • 100
    • 0032817022 scopus 로고    scopus 로고
    • Post-translational regulation of AP-1 transcription factor DNA-binding activity in the rat conceptus
    • Ozolins T.R., Hales B.F. Post-translational regulation of AP-1 transcription factor DNA-binding activity in the rat conceptus. Mol. Pharmacol. 56:1999;537-544.
    • (1999) Mol. Pharmacol. , vol.56 , pp. 537-544
    • Ozolins, T.R.1    Hales, B.F.2
  • 102
    • 0032167424 scopus 로고    scopus 로고
    • Base excision repair initiation revealed by crystal structures and binding kinetics of human uracil-DNA glycosylase with DNA
    • Parikh S.S., Mol C.D., Slupphaug G., Bharati S., Krokan H.E., Tainer J.A. Base excision repair initiation revealed by crystal structures and binding kinetics of human uracil-DNA glycosylase with DNA. Embo. J. 17:1998;5214-5226.
    • (1998) Embo. J. , vol.17 , pp. 5214-5226
    • Parikh, S.S.1    Mol, C.D.2    Slupphaug, G.3    Bharati, S.4    Krokan, H.E.5    Tainer, J.A.6
  • 103
    • 0029892846 scopus 로고    scopus 로고
    • Evidence for an imino intermediate in the DNA polymerase β deoxyribose phosphate excision reaction
    • Piersen C.E., Prasad R., Wilson S.H., Lloyd R.S. Evidence for an imino intermediate in the DNA polymerase β 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
  • 104
    • 0033065390 scopus 로고    scopus 로고
    • Overexpression of the human HAP1 protein sensitizes cells to the lethal effect of bioreductive drugs
    • Prieto-Alamo M.J., Laval F. Overexpression of the human HAP1 protein sensitizes cells to the lethal effect of bioreductive drugs. Carcinogenesis. 20:1999;415-419.
    • (1999) Carcinogenesis , vol.20 , pp. 415-419
    • Prieto-Alamo, M.J.1    Laval, F.2
  • 105
    • 0032763809 scopus 로고    scopus 로고
    • Molecular cloning, sequence and structure analysis of hamster apurinic/apyrimidinic endonuclease (chAPE1) gene
    • Purohit S., Arenaz P. Molecular cloning, sequence and structure analysis of hamster apurinic/apyrimidinic endonuclease (chAPE1) gene. Mutat. Res. 435:1999;215-224.
    • (1999) Mutat. Res. , vol.435 , pp. 215-224
    • Purohit, S.1    Arenaz, P.2
  • 106
    • 0030585150 scopus 로고    scopus 로고
    • The solution structure of human thioredoxin complexed with its target from Ref-1 reveals peptide chain reversal
    • Qin J., Clore G.M., Kennedy W.P., Kuszewski J., Gronenborn A.M. The solution structure of human thioredoxin complexed with its target from Ref-1 reveals peptide chain reversal. Structure. 4:1996;613-620.
    • (1996) Structure , vol.4 , pp. 613-620
    • Qin, J.1    Clore, G.M.2    Kennedy, W.P.3    Kuszewski, J.4    Gronenborn, A.M.5
  • 107
    • 0032574770 scopus 로고    scopus 로고
    • Activation of apurinic/apyrimidinic endonuclease in human cells by reactive oxygen species and its correlation with their adaptive response to genotoxicity of free radicals
    • Ramana C.V., Boldogh I., Izumi T., Mitra S. Activation of apurinic/apyrimidinic endonuclease in human cells by reactive oxygen species and its correlation with their adaptive response to genotoxicity of free radicals. Proc. Natl. Acad. Sci. U. S. A. 95:1998;5061-5066.
    • (1998) Proc. Natl. Acad. Sci. U. S. A. , vol.95 , pp. 5061-5066
    • Ramana, C.V.1    Boldogh, I.2    Izumi, T.3    Mitra, S.4
  • 108
    • 0028007266 scopus 로고
    • Expression of a multifunctional DNA repair enzyme gene, apurinic/apyrimidinic endonuclease (APE supraoptic Ref-1) in the suprachiasmatic and paraventricular nuclei
    • Rivkees S.A., Kelley M.R. Expression of a multifunctional DNA repair enzyme gene, apurinic/apyrimidinic endonuclease (APE supraoptic Ref-1) in the suprachiasmatic and paraventricular nuclei. Brain Res. 666:1994;137-142.
    • (1994) Brain Res. , vol.666 , pp. 137-142
    • Rivkees, S.A.1    Kelley, M.R.2
  • 109
    • 0026078249 scopus 로고
    • Two interdependent basic domains in nucleoplasmin nuclear targeting sequence: Identification of a class of bipartite nuclear targeting sequence
    • Robbins J., Dilworth S.M., Laskey R.A., Dingwall C. Two interdependent basic domains in nucleoplasmin nuclear targeting sequence: identification of a class of bipartite nuclear targeting sequence. Cell. 64:1991;615-623.
    • (1991) Cell , vol.64 , pp. 615-623
    • Robbins, J.1    Dilworth, S.M.2    Laskey, R.A.3    Dingwall, C.4
  • 110
    • 0030954254 scopus 로고    scopus 로고
    • Down-regulation of apurinic/apyrimidinic endonuclease expression is associated with the induction of apoptosis in differentiating myeloid leukemia cells
    • Robertson K.A., Hill D.P., Xu Y., Liu L., Van Epps S., Hockenbery D.M., Park J.R., Wilson T.M., Kelley M.R. Down-regulation of apurinic/apyrimidinic endonuclease expression is associated with the induction of apoptosis in differentiating myeloid leukemia cells. Cell Growth Differ. 8:1997;443-449.
    • (1997) Cell Growth Differ. , vol.8 , pp. 443-449
    • Robertson, K.A.1    Hill, D.P.2    Xu, Y.3    Liu, L.4    Van Epps, S.5    Hockenbery, D.M.6    Park, J.R.7    Wilson, T.M.8    Kelley, M.R.9
  • 111
    • 0025936119 scopus 로고
    • Isolation of cDNA clones encoding a human apurinic/apyrimidinic endonuclease that corrects DNA repair and mutagenesis defects in E. coli xth (exonuclease III) mutants
    • Robson C.N., Hickson I.D. Isolation of cDNA clones encoding a human apurinic/apyrimidinic endonuclease that corrects DNA repair and mutagenesis defects in E. coli xth (exonuclease III) mutants. Nucleic Acids Res. 19:1991;5519-5523.
    • (1991) Nucleic Acids Res. , vol.19 , pp. 5519-5523
    • Robson, C.N.1    Hickson, I.D.2
  • 112
  • 113
    • 0033991183 scopus 로고    scopus 로고
    • Analysis of repair of abasic sites in early onset breast cancer patients
    • Rossi O., Carrozzino F., Cappelli E., Carli F., Frosina G. Analysis of repair of abasic sites in early onset breast cancer patients. Int. J. Cancer. 85:2000;21-26.
    • (2000) Int. J. Cancer , vol.85 , pp. 21-26
    • Rossi, O.1    Carrozzino, F.2    Cappelli, E.3    Carli, F.4    Frosina, G.5
  • 114
    • 0029972312 scopus 로고    scopus 로고
    • Asparagine 212 is essential for abasic site recognition by the human DNA repair endonuclease HAP1
    • Rothwell D.G., Hickson I.D. Asparagine 212 is essential for abasic site recognition by the human DNA repair endonuclease HAP1. Nucleic Acids Res. 24:1996;4217-4221.
    • (1996) Nucleic Acids Res. , vol.24 , pp. 4217-4221
    • Rothwell, D.G.1    Hickson, I.D.2
  • 116
    • 0030878398 scopus 로고    scopus 로고
    • The Drosophila ribosomal protein S3 contains a DNA deoxyribophosphodiesterase (dRpase) activity
    • Sandigursky M., Yacoub A., Kelley M.R., Deutsch W.A., Franklin W.A. The Drosophila ribosomal protein S3 contains a DNA deoxyribophosphodiesterase (dRpase) activity. J. Biol. Chem. 272:1997;17480-17484.
    • (1997) J. Biol. Chem. , vol.272 , pp. 17480-17484
    • Sandigursky, M.1    Yacoub, A.2    Kelley, M.R.3    Deutsch, W.A.4    Franklin, W.A.5
  • 117
    • 0032813088 scopus 로고    scopus 로고
    • Repair of DNA damage in mitochondria
    • Sawyer D.E., Van Houten B. Repair of DNA damage in mitochondria. Mutat. Res. 434:1999;161-176.
    • (1999) Mutat. Res. , vol.434 , pp. 161-176
    • Sawyer, D.E.1    Van Houten, B.2
  • 118
  • 119
    • 0025718595 scopus 로고
    • CDNA and deduced amino acid sequence of a mouse DNA repair enzyme (APEX nuclease) with significant homology to Escherichia coli exonuclease III
    • Seki S., Akiyama K., Watanabe S., Hatsushika M., Ikeda S., Tsutsui K. cDNA and deduced amino acid sequence of a mouse DNA repair enzyme (APEX nuclease) with significant homology to Escherichia coli exonuclease III. J. Biol. Chem. 266:1991;20797-20802.
    • (1991) J. Biol. Chem. , vol.266 , pp. 20797-20802
    • Seki, S.1    Akiyama, K.2    Watanabe, S.3    Hatsushika, M.4    Ikeda, S.5    Tsutsui, K.6
  • 120
    • 0033233243 scopus 로고    scopus 로고
    • Regulation of mammalian O2 homeostasis by hypoxia-inducible factor 1
    • Semenza G.L. Regulation of mammalian O2 homeostasis by hypoxia-inducible factor 1. Annu. Rev. Cell. Dev. Biol. 15:1999;551-578.
    • (1999) Annu. Rev. Cell. Dev. Biol. , vol.15 , pp. 551-578
    • Semenza, G.L.1
  • 121
    • 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.H. 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.H.3
  • 122
    • 0029904839 scopus 로고    scopus 로고
    • A nucleotide-flipping mechanism from the structure of human uracil-DNA glycosylase bound to DNA (see comments)
    • Slupphaug G., Mol C.D., Kavli B., Arvai A.S., Krokan H.E., Tainer J.A. A nucleotide-flipping mechanism from the structure of human uracil-DNA glycosylase bound to DNA (see comments). Nature. 384:1996;87-92.
    • (1996) Nature , vol.384 , pp. 87-92
    • Slupphaug, G.1    Mol, C.D.2    Kavli, B.3    Arvai, A.S.4    Krokan, H.E.5    Tainer, J.A.6
  • 123
    • 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., 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
  • 124
    • 0031021533 scopus 로고    scopus 로고
    • Substrate binding by human apurinic/apyrimidinic endonuclease indicates a Briggs-Haldane mechanism
    • Strauss P.R., Beard W.A., Patterson T.A., Wilson S.H. Substrate binding by human apurinic/apyrimidinic endonuclease indicates a Briggs-Haldane mechanism. J. Biol. Chem. 272:1997;1302-1307.
    • (1997) J. Biol. Chem. , vol.272 , pp. 1302-1307
    • Strauss, P.R.1    Beard, W.A.2    Patterson, T.A.3    Wilson, S.H.4
  • 125
    • 0032486475 scopus 로고    scopus 로고
    • Domain mapping of human apurinic/apyrimidinic endonuclease. Structural and functional evidence for a disordered amino terminus and a tight globular carboxyl domain
    • Strauss P.R., Holt C.M. Domain mapping of human apurinic/apyrimidinic endonuclease. Structural and functional evidence for a disordered amino terminus and a tight globular carboxyl domain. J. Biol. Chem. 273:1998;14435-14441.
    • (1998) J. Biol. Chem. , vol.273 , pp. 14435-14441
    • Strauss, P.R.1    Holt, C.M.2
  • 126
    • 0031938474 scopus 로고    scopus 로고
    • Inductions of immediate early genes (IEGS) and Ref-1 by human chorionic gonadotropin in murine Leydig cell line (MA-10)
    • Suzuki S., Nagaya T., Suganuma N., Tomoda Y., Seo H. Inductions of immediate early genes (IEGS) and Ref-1 by human chorionic gonadotropin in murine Leydig cell line (MA-10). Biochem. Mol. Biol. Int. 44:1998;217-224.
    • (1998) Biochem. Mol. Biol. Int. , vol.44 , pp. 217-224
    • Suzuki, S.1    Nagaya, T.2    Suganuma, N.3    Tomoda, Y.4    Seo, H.5
  • 127
    • 0030075950 scopus 로고    scopus 로고
    • CDNA cloning of rat major AP endonuclease (APEX nuclease) and analyses of its mRNA expression in rat tissues
    • Tan Y., Nakagawa Y., Akiyama K., Wakabayashi H., Sarker A.H., Seki S. cDNA cloning of rat major AP endonuclease (APEX nuclease) and analyses of its mRNA expression in rat tissues. Acta Med. Okayama. 50:1996;53-60.
    • (1996) Acta Med. Okayama , vol.50 , pp. 53-60
    • Tan, Y.1    Nakagawa, Y.2    Akiyama, K.3    Wakabayashi, H.4    Sarker, A.H.5    Seki, S.6
  • 128
    • 0032563635 scopus 로고    scopus 로고
    • Immunohistochemical localization of redox factor-1 (Ref-1) in Alzheimer's hippocampus
    • Tan Z., Sun N., Schreiber S.S. Immunohistochemical localization of redox factor-1 (Ref-1) in Alzheimer's hippocampus. Neuroreport. 9:1998;2749-2752.
    • (1998) Neuroreport , vol.9 , pp. 2749-2752
    • Tan, Z.1    Sun, N.2    Schreiber, S.S.3
  • 129
    • 0024328791 scopus 로고
    • A holistic approach to protein structure alignment
    • Taylor W.R., Orengo C.A. A holistic approach to protein structure alignment. Protein Eng. 2:1989;505-519.
    • (1989) Protein Eng. , vol.2 , pp. 505-519
    • Taylor, W.R.1    Orengo, C.A.2
  • 132
    • 0032566712 scopus 로고    scopus 로고
    • Redox potential controls the structure and DNA binding activity of the paired domain
    • Tell G., Scaloni A., Pellizzari L., Formisano S., Pucillo C., Damante G. Redox potential controls the structure and DNA binding activity of the paired domain. J. Biol. Chem. 273:1998;25062-25072.
    • (1998) J. Biol. Chem. , vol.273 , pp. 25062-25072
    • Tell, G.1    Scaloni, A.2    Pellizzari, L.3    Formisano, S.4    Pucillo, C.5    Damante, G.6
  • 133
    • 0034160089 scopus 로고    scopus 로고
    • An 'environment to nucleus' signaling system operates in B lymphocytes: Redox status modulates BSAP/Pax-5 activation through Ref-1 nuclear translocation
    • Tell G., Zecca A., Pellizzari L., Spessotto P., Colombatti A., Kelley M.R., Damante G., Pucillo C. An 'environment to nucleus' signaling system operates in B lymphocytes: redox status modulates BSAP/Pax-5 activation through Ref-1 nuclear translocation. Nucleic Acids Res. 28:2000;1099-1105.
    • (2000) Nucleic Acids Res. , vol.28 , pp. 1099-1105
    • Tell, G.1    Zecca, A.2    Pellizzari, L.3    Spessotto, P.4    Colombatti, A.5    Kelley, M.R.6    Damante, G.7    Pucillo, C.8
  • 134
    • 0006110610 scopus 로고    scopus 로고
    • Histology-specific expression of a DNA repair protein in pediatric rhabdomyosarcomas
    • in press
    • B. Thompson, R. Tritt, M. Davis, M.R. Kelley, Histology-specific expression of a DNA repair protein in pediatric rhabdomyosarcomas, J. Ped. Oncol., 2000, in press.
    • (2000) J. Ped. Oncol.
    • Thompson, B.1    Tritt, R.2    Davis, M.3    Kelley, M.R.4
  • 135
    • 0030933193 scopus 로고    scopus 로고
    • Expression of yeast but not human apurinic/apyrimidinic endonuclease renders Chinese hamster cells more resistant to DNA damaging agents
    • Tomicic M., Eschbach E., Kaina B. Expression of yeast but not human apurinic/apyrimidinic endonuclease renders Chinese hamster cells more resistant to DNA damaging agents. Mutat. Res. 383:1997;155-165.
    • (1997) Mutat. Res. , vol.383 , pp. 155-165
    • Tomicic, M.1    Eschbach, E.2    Kaina, B.3
  • 137
    • 0028596574 scopus 로고
    • A role for the human DNA repair enzyme HAP1 in cellular protection against DNA damaging agents and hypoxic stress
    • Walker L.J., Craig R.B., Harris A.L., Hickson I.D. A role for the human DNA repair enzyme HAP1 in cellular protection against DNA damaging agents and hypoxic stress. Nucleic Acids Res. 22:1994;4884-4889.
    • (1994) Nucleic Acids Res. , vol.22 , pp. 4884-4889
    • Walker, L.J.1    Craig, R.B.2    Harris, A.L.3    Hickson, I.D.4
  • 138
    • 0027324056 scopus 로고
    • Identification of residues in the human DNA repair enzyme HAP1 (Ref-1) that are essential for redox regulation of Jun DNA binding
    • Walker L.J., Robson C.N., Black E., Gillespie D., Hickson I.D. Identification of residues in the human DNA repair enzyme HAP1 (Ref-1) that are essential for redox regulation of Jun DNA binding. Mol. Cell Biol. 13:1993;5370-5376.
    • (1993) Mol. Cell Biol. , vol.13 , pp. 5370-5376
    • Walker, L.J.1    Robson, C.N.2    Black, E.3    Gillespie, D.4    Hickson, I.D.5
  • 139
    • 0024161399 scopus 로고
    • AP endonucleases and DNA glycosylases that recognize oxidative DNA damage
    • Wallace S.S. AP endonucleases and DNA glycosylases that recognize oxidative DNA damage. Environ. Mol. Mutagen. 12:1988;431-477.
    • (1988) Environ. Mol. Mutagen. , vol.12 , pp. 431-477
    • Wallace, S.S.1
  • 140
    • 0028151464 scopus 로고
    • DNA damages processed by base excision repair: Biological consequences
    • Wallace S.S. DNA damages processed by base excision repair: biological consequences. Int. J. Radiat. Biol. 66:1994;579-589.
    • (1994) Int. J. Radiat. Biol. , vol.66 , pp. 579-589
    • Wallace, S.S.1
  • 141
    • 0031773901 scopus 로고    scopus 로고
    • Enzymatic processing of radiation-induced free radical damage in DNA
    • Wallace S.S. Enzymatic processing of radiation-induced free radical damage in DNA. Radiat. Res. 150:1998;S60-S79.
    • (1998) Radiat. Res. , vol.150
    • Wallace, S.S.1
  • 143
    • 0034142085 scopus 로고    scopus 로고
    • Is CREB a key to neuronal survival?
    • Walton M.R., Dragunow I. Is CREB a key to neuronal survival? Trends Neurosci. 23:2000;48-53.
    • (2000) Trends Neurosci. , vol.23 , pp. 48-53
    • Walton, M.R.1    Dragunow, I.2
  • 144
    • 0029572482 scopus 로고
    • Trans-complementation by human apurinic endonuclease (Ape) of hypersensitivity to DNA damage and spontaneous mutator phenotype in apn1-yeast
    • Wilson D.M. III, Bennett R.A., Marquis J.C., Ansari P., Demple B. Trans-complementation by human apurinic endonuclease (Ape) of hypersensitivity to DNA damage and spontaneous mutator phenotype in apn1-yeast. Nucleic Acids Res. 23:1995;5027-5033.
    • (1995) Nucleic Acids Res. , vol.23 , pp. 5027-5033
    • Wilson D.M. III1    Bennett, R.A.2    Marquis, J.C.3    Ansari, P.4    Demple, B.5
  • 145
    • 0029001186 scopus 로고
    • Incision activity of human apurinic endonuclease (Ape) at abasic site analogs in DNA
    • Wilson D.M. III, Takeshita M., Grollman A.P., Demple B. Incision activity of human apurinic endonuclease (Ape) at abasic site analogs in DNA. J. Biol. Chem. 270:1995;16002-16007.
    • (1995) J. Biol. Chem. , vol.270 , pp. 16002-16007
    • Wilson D.M. III1    Takeshita, M.2    Grollman, A.P.3    Demple, B.4
  • 146
    • 0032100860 scopus 로고    scopus 로고
    • Mammalian base excision repair and DNA polymerase β
    • Wilson S.H. Mammalian base excision repair and DNA polymerase β Mutat. Res. 407:1998;203-215.
    • (1998) Mutat. Res. , vol.407 , pp. 203-215
    • Wilson, S.H.1
  • 147
    • 0028275092 scopus 로고
    • Cloning of the multifunctional rat apurinic/apyrimidinic endonuclease (rAPEN)/redox factor from an immature T cell line
    • Wilson T.M., Carney J.P., Kelley M.R. Cloning of the multifunctional rat apurinic/apyrimidinic endonuclease (rAPEN)/redox factor from an immature T cell line. Nucleic Acids Res. 22:1994;530-531.
    • (1994) Nucleic Acids Res. , vol.22 , pp. 530-531
    • Wilson, T.M.1    Carney, J.P.2    Kelley, M.R.3
  • 148
    • 0030004546 scopus 로고    scopus 로고
    • Differential expression of the apurinic/apyrimidinic endonuclease (APE/Ref-1) multifunctional DNA base excision repair gene during fetal development and in adult rat brain and testis
    • Wilson T.M., Rivkees S.A., Deutsch W.A., Kelley M.R. Differential expression of the apurinic/apyrimidinic endonuclease (APE/Ref-1) multifunctional DNA base excision repair gene during fetal development and in adult rat brain and testis. Mutat. Res. 362:1996;237-248.
    • (1996) Mutat. Res. , vol.362 , pp. 237-248
    • Wilson, T.M.1    Rivkees, S.A.2    Deutsch, W.A.3    Kelley, M.R.4
  • 149
    • 0026583944 scopus 로고
    • Identification and characterization of Ref-1, a nuclear protein that facilitates AP-1 DNA-binding activity
    • Xanthoudakis S., Curran T. Identification and characterization of Ref-1, a nuclear protein that facilitates AP-1 DNA-binding activity. Embo. J. 11:1992;653-665.
    • (1992) Embo. J. , vol.11 , pp. 653-665
    • Xanthoudakis, S.1    Curran, T.2
  • 150
    • 0026714672 scopus 로고
    • Redox activation of Fos-Jun DNA binding activity is mediated by a DNA repair enzyme
    • Xanthoudakis S., Miao G., Wang F., Pan Y.C., Curran T. Redox activation of Fos-Jun DNA binding activity is mediated by a DNA repair enzyme. Embo. J. 11:1992;3323-3335.
    • (1992) Embo. J. , vol.11 , pp. 3323-3335
    • Xanthoudakis, S.1    Miao, G.2    Wang, F.3    Pan, Y.C.4    Curran, T.5
  • 151
    • 0028058086 scopus 로고
    • The redox and DNA-repair activities of Ref-1 are encoded by nonoverlapping domains
    • Xanthoudakis S., Miao G.G., Curran T. The redox and DNA-repair activities of Ref-1 are encoded by nonoverlapping domains. Proc. Natl. Acad. Sci. U. S. A. 91:1994;23-27.
    • (1994) Proc. Natl. Acad. Sci. U. S. A. , vol.91 , pp. 23-27
    • Xanthoudakis, S.1    Miao, G.G.2    Curran, T.3
  • 152
    • 0029829265 scopus 로고    scopus 로고
    • The redox/DNA repair protein, Ref-1, is essential for early embryonic development in mice
    • Xanthoudakis S., Smeyne R.J., Wallace J.D., Curran T. The redox/DNA repair protein, Ref-1, is essential for early embryonic development in mice. Proc. Natl. Acad. Sci. U. S. A. 93:1996;8919-8923.
    • (1996) Proc. Natl. Acad. Sci. U. S. A. , vol.93 , pp. 8919-8923
    • Xanthoudakis, S.1    Smeyne, R.J.2    Wallace, J.D.3    Curran, T.4
  • 153
    • 0031439376 scopus 로고    scopus 로고
    • The apurinic/apyrimidinic endonuclease (APE/Ref-1) DNA repair enzyme is elevated in premalignant and malignant cervical cancer
    • Xu Y., Moore D.H., Broshears J., Liu L., Wilson T.M., Kelley M.R. The apurinic/apyrimidinic endonuclease (APE/Ref-1) DNA repair enzyme is elevated in premalignant and malignant cervical cancer. Anticancer Res. 17:1997;3713-3719.
    • (1997) Anticancer Res. , vol.17 , pp. 3713-3719
    • Xu, Y.1    Moore, D.H.2    Broshears, J.3    Liu, L.4    Wilson, T.M.5    Kelley, M.R.6
  • 154
    • 0029956360 scopus 로고    scopus 로고
    • Drosophila ribosomal protein PO contains apurinic/apyrimidinic endonuclease activity
    • Yacoub A., Kelley M.R., Deutsch W.A. Drosophila ribosomal protein PO contains apurinic/apyrimidinic endonuclease activity. Nucleic Acids Res. 24:1996;4298-4303.
    • (1996) Nucleic Acids Res. , vol.24 , pp. 4298-4303
    • Yacoub, A.1    Kelley, M.R.2    Deutsch, W.A.3
  • 155
    • 0031439356 scopus 로고    scopus 로고
    • The DNA repair activity of human redox/repair protein APE/Ref-1 is inactivated by phosphorylation
    • Yacoub A., Kelley M.R., Deutsch W.A. The DNA repair activity of human redox/repair protein APE/Ref-1 is inactivated by phosphorylation. Cancer Res. 57:1997;5457-5459.
    • (1997) Cancer Res. , vol.57 , pp. 5457-5459
    • Yacoub, A.1    Kelley, M.R.2    Deutsch, W.A.3
  • 156
    • 0027936404 scopus 로고
    • Activation of AP-1 and of a nuclear redox factor, Ref-1, in the response of HT29 colon cancer cells to hypoxia
    • Yao K.S., Xanthoudakis S., Curran T., O'Dwyer P.J. Activation of AP-1 and of a nuclear redox factor, Ref-1, in the response of HT29 colon cancer cells to hypoxia. Mol. Cell. Biol. 14:1994;5997-6003.
    • (1994) Mol. Cell. Biol. , vol.14 , pp. 5997-6003
    • Yao, K.S.1    Xanthoudakis, S.2    Curran, T.3    O'Dwyer, P.J.4
  • 157
    • 0026675841 scopus 로고
    • The human gene for apurinic/apyrimidinic endonuclease (HAP1): Sequence and localization to chromosome 14 band q12
    • Zhao B., Grandy D.K., Hagerup J.M., Magenis R.E., Smith L., Chauhan B.C., Henner W.D. The human gene for apurinic/apyrimidinic endonuclease (HAP1): sequence and localization to chromosome 14 band q12. Nucleic Acids Res. 20:1992;4097-4098.
    • (1992) Nucleic Acids Res. , vol.20 , pp. 4097-4098
    • Zhao, B.1    Grandy, D.K.2    Hagerup, J.M.3    Magenis, R.E.4    Smith, L.5    Chauhan, B.C.6    Henner, W.D.7
  • 158
    • 0029079936 scopus 로고
    • Cell cycle regulation of the cyclin A, cdc25C and cdc2 genes is based on a common mechanism of transcriptional repression
    • Zwicker J., Lucibello F.C., Wolfraim L.A., Gross C., Truss M., Engeland K., Muller R. Cell cycle regulation of the cyclin A, cdc25C and cdc2 genes is based on a common mechanism of transcriptional repression. Embo. J. 14:1995;4514-4522.
    • (1995) Embo. J. , vol.14 , pp. 4514-4522
    • Zwicker, J.1    Lucibello, F.C.2    Wolfraim, L.A.3    Gross, C.4    Truss, M.5    Engeland, K.6    Muller, R.7


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