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Volumn 153, Issue 2, 2000, Pages 186-195

Heat-shock proteins associated with base excision repair enzymes in HeLa cells

Author keywords

[No Author keywords available]

Indexed keywords

DNA BASE; DNA POLYMERASE; ENDONUCLEASE; HEAT SHOCK PROTEIN; HEAT SHOCK PROTEIN 27; HEAT SHOCK PROTEIN 70; URACIL DNA GLYCOSYLTRANSFERASE;

EID: 0033955511     PISSN: 00337587     EISSN: None     Source Type: Journal    
DOI: 10.1667/0033-7587(2000)153[0186:HSPAWB]2.0.CO;2     Document Type: Article
Times cited : (48)

References (28)
  • 1
    • 0041121476 scopus 로고    scopus 로고
    • (I. Hickson, Ed.), Landes Bioscicncc and Chapman & Hall, Austin, TX
    • D. G. Rothwell and D. I. Hickson, In Base Excision Repair of DNA Damage (I. Hickson, Ed.), pp. 67-80. Landes Bioscicncc and Chapman & Hall, Austin, TX, 1997.
    • (1997) Base Excision Repair of DNA Damage , pp. 67-80
    • Rothwell, D.G.1    Hickson, D.I.2
  • 2
    • 0031172802 scopus 로고    scopus 로고
    • A mammalian DNA repair enzyme that excises oxidatively damaged guanines maps to a locus frequently lost to lung cancer
    • P. Lu, H. M. Nash and G. L. Verdine, A mammalian DNA repair enzyme that excises oxidatively damaged guanines maps to a locus frequently lost to lung cancer. Curr. Biol. 7, 397-407 (1997).
    • (1997) Curr. Biol. , vol.7 , pp. 397-407
    • Lu, P.1    Nash, H.M.2    Verdine, G.L.3
  • 3
    • 0030738194 scopus 로고    scopus 로고
    • Cloning and characterization of a mammalian 8-oxoguanine DNA glycosylasc
    • T. A. Rosenquist, D. O. Zharkov and A. P. Grollman, Cloning and characterization of a mammalian 8-oxoguanine DNA glycosylasc. Proc. Natl. Acad. Sci. USA 94, 7429-7434 (1997).
    • (1997) Proc. Natl. Acad. Sci. USA , vol.94 , pp. 7429-7434
    • Rosenquist, T.A.1    Zharkov, D.O.2    Grollman, A.P.3
  • 5
    • 0030816108 scopus 로고    scopus 로고
    • Cloning and characterization of the hOGGl, a human homolog of the OGGl gene of Saccharomvces cerevisae
    • J. P. Radicella, C. Dherin, C. Desmaze, M. S. Fox and S. Boiteux, Cloning and characterization of the hOGGl, a human homolog of the OGGl gene of Saccharomvces cerevisae. Proc. Natl. Acad. Sci. USA 94, 8010-8015 (1997).
    • (1997) Proc. Natl. Acad. Sci. USA , vol.94 , pp. 8010-8015
    • Radicella, J.P.1    Dherin, C.2    Desmaze, C.3    Fox, M.S.4    Boiteux, S.5
  • 7
    • 0027171181 scopus 로고
    • Evidence for two DNA repair enzymes for 8-hydroxyguanine (7,8-dihydro-8-oxoguanine) in human cells
    • T. Bessho, K. Tano, H. Kasai, E. Ohtsuka and S. Nishimura, Evidence for two DNA repair enzymes for 8-hydroxyguanine (7,8-dihydro-8-oxoguanine) in human cells. J. Biol. Chem. 268, 19416-19421 (1993).
    • (1993) J. Biol. Chem. , vol.268 , pp. 19416-19421
    • Bessho, T.1    Tano, K.2    Kasai, H.3    Ohtsuka, E.4    Nishimura, S.5
  • 8
    • 0026554433 scopus 로고
    • Human HeLa cell enzymes that remove phosphoglycolate 3′-end groups from DNA
    • T. A. Winters, M. Weinfeld and T. J. Jorgensen, Human HeLa cell enzymes that remove phosphoglycolate 3′-end groups from DNA. Nucleic Acids Res. 20, 2573-2580 (1992).
    • (1992) Nucleic Acids Res. , vol.20 , pp. 2573-2580
    • Winters, T.A.1    Weinfeld, M.2    Jorgensen, T.J.3
  • 9
    • 0029028964 scopus 로고
    • Excision of dcoxyribose phosphate residues by DNA polymerase β during DNA repair
    • Y. Matsumoto and K. Kim, Excision of dcoxyribose phosphate residues by DNA polymerase β during DNA repair. Science 269, 699-702 (1995).
    • (1995) Science , vol.269 , pp. 699-702
    • Matsumoto, Y.1    Kim, K.2
  • 10
    • 0026761183 scopus 로고
    • Enhanced excision repair activity in mammalian cells after ionizing radiation
    • R. Bases, W. A. Franklin, T. Moy and F. Mendez, Enhanced excision repair activity in mammalian cells after ionizing radiation. Int. J. Radiat. Biol. 62, 427-441 (1992).
    • (1992) Int. J. Radiat. Biol. , vol.62 , pp. 427-441
    • Bases, R.1    Franklin, W.A.2    Moy, T.3    Mendez, F.4
  • 12
  • 13
    • 0029974576 scopus 로고    scopus 로고
    • Nucleotide excision repair in yeast is mediated hy sequential assembly of repair factors and not by a pre-assembled repairosome
    • S. N. Guzder, P. Sung, L. Prakash and S. Prakash, Nucleotide excision repair in yeast is mediated hy sequential assembly of repair factors and not by a pre-assembled repairosome. J. Biol. Chem. 271, 8903-8910 (1996).
    • (1996) J. Biol. Chem. , vol.271 , pp. 8903-8910
    • Guzder, S.N.1    Sung, P.2    Prakash, L.3    Prakash, S.4
  • 14
    • 0030018848 scopus 로고    scopus 로고
    • Specific interaction of DNA polymerase β and DNA ligase I in a multiprotein base excision repair complex from bovine testis
    • R. Prasad, R. K. Singhal, D. K. Srivastava, J. T. Molina, A. E. Tomkinson and S. H. Wilson, Specific interaction of DNA polymerase β and DNA ligase I in a multiprotein base excision repair complex from bovine testis. J. Biol Chem. 271, 16000-16007 (1996).
    • (1996) J. Biol Chem. , vol.271 , pp. 16000-16007
    • Prasad, R.1    Singhal, R.K.2    Srivastava, D.K.3    Molina, J.T.4    Tomkinson, A.E.5    Wilson, S.H.6
  • 15
    • 0032557562 scopus 로고    scopus 로고
    • Involvement of molecular chaperonins in nucleotide excision repair
    • Y. Zou, J. Crowley and B. Van Houten, Involvement of molecular chaperonins in nucleotide excision repair. J. Biol. Chem. 273, 12887-12892 (1998).
    • (1998) J. Biol. Chem. , vol.273 , pp. 12887-12892
    • Zou, Y.1    Crowley, J.2    Van Houten, B.3
  • 16
    • 0017184389 scopus 로고
    • A rapid and sensitive method for the quantitation of microgram quantities of protein utilizing the principle of protein-dye binding
    • M. M. Bradford, A rapid and sensitive method for the quantitation of microgram quantities of protein utilizing the principle of protein-dye binding. Anal. Biochem. 72, 248-254 (1976).
    • (1976) Anal. Biochem. , vol.72 , pp. 248-254
    • Bradford, M.M.1
  • 17
    • 0029810085 scopus 로고    scopus 로고
    • Characterization of the DNA polymerase requirement of human base excision repair
    • K. Nealon, I. D. Nicholl and M. K. Kenny, Characterization of the DNA polymerase requirement of human base excision repair. Nucleic Acids Res. 24, 3763-3770 (1996).
    • (1996) Nucleic Acids Res. , vol.24 , pp. 3763-3770
    • Nealon, K.1    Nicholl, I.D.2    Kenny, M.K.3
  • 18
    • 0028933306 scopus 로고
    • Properties of a recombinant human uracil-DNA glycosylase from the UNG gene and evidence that UNG encodes the major uracil-DNA glycosylase
    • G. Slupphaug, I. Eftedal, B. Kavli, S. Bharati, N. M. Helle, T. Haug, D. W. Levine and H. E. Krokan, Properties of a recombinant human uracil-DNA glycosylase from the UNG gene and evidence that UNG encodes the major uracil-DNA glycosylase. Biochemistry 34, 128-138 (1995).
    • (1995) Biochemistry , vol.34 , pp. 128-138
    • Slupphaug, G.1    Eftedal, I.2    Kavli, B.3    Bharati, S.4    Helle, N.M.5    Haug, T.6    Levine, D.W.7    Krokan, H.E.8
  • 20
    • 0030841051 scopus 로고    scopus 로고
    • Nuclear and mitochondrial uracil-DNA glycosylases are generated by alternative splicing and transcription from different positions in the UNG gene
    • H. Nilsen, M. Otterlei, T. Haug, K. Solum, T. A. Nagelhus, F. Skorpen and H. E. Krokan, Nuclear and mitochondrial uracil-DNA glycosylases are generated by alternative splicing and transcription from different positions in the UNG gene. Nucleic Acids Res. 25, 750-755 (1997).
    • (1997) Nucleic Acids Res. , vol.25 , pp. 750-755
    • Nilsen, H.1    Otterlei, M.2    Haug, T.3    Solum, K.4    Nagelhus, T.A.5    Skorpen, F.6    Krokan, H.E.7
  • 21
    • 0029836226 scopus 로고    scopus 로고
    • Determinants of RNA polymerase a subunit for interaction with β, β′, and σ subunits: Hydroxyl-radical protein footprinting
    • T. Heyduk, E. Heyduk, K. Severinov, H. Tang and R. H. Ebright, Determinants of RNA polymerase a subunit for interaction with β, β′, and σ subunits: hydroxyl-radical protein footprinting. Proc. Natl. Acad. Sci. USA 93, 10162-10166 (1996).
    • (1996) Proc. Natl. Acad. Sci. USA , vol.93 , pp. 10162-10166
    • Heyduk, T.1    Heyduk, E.2    Severinov, K.3    Tang, H.4    Ebright, R.H.5
  • 22
    • 0027931824 scopus 로고
    • Mapping protein domains involved in macromolecular interactions: A novel protein foot-printing approach
    • E. Heyduk and T. Heyduk, Mapping protein domains involved in macromolecular interactions: A novel protein foot-printing approach. Biochemistry 33, 9643-9650 (1994).
    • (1994) Biochemistry , vol.33 , pp. 9643-9650
    • Heyduk, E.1    Heyduk, T.2
  • 23
    • 0026651978 scopus 로고
    • Ethidium bromide provides a simple tool for identifying genuine DNA-independent protein associations
    • J-S. Lai and W. Herr, Ethidium bromide provides a simple tool for identifying genuine DNA-independent protein associations. Proc. Natl. Acad. Sci. USA 89, 6958-6962 (1992).
    • (1992) Proc. Natl. Acad. Sci. USA , vol.89 , pp. 6958-6962
    • Lai, J.-S.1    Herr, W.2
  • 24
    • 0030939690 scopus 로고    scopus 로고
    • Reconstitution of human base excision repair with purified proteins
    • I. D. Nicholl, K. Nealon and M. K. Kenny, Reconstitution of human base excision repair with purified proteins. Biochemistry 36, 7557-7566 (1997).
    • (1997) Biochemistry , vol.36 , pp. 7557-7566
    • Nicholl, I.D.1    Nealon, K.2    Kenny, M.K.3
  • 25
    • 0030740948 scopus 로고    scopus 로고
    • Interaction of human apurinic endonuclease and DNA polymerase β in the base excision pathway
    • R. A. O. Bennett, D. Wilson, III, D. Wong and B. Demple, Interaction of human apurinic endonuclease and DNA polymerase β in the base excision pathway. Proc. Natl. Acad Sci. USA 94, 7166-7169 (1997).
    • (1997) Proc. Natl. Acad Sci. USA , vol.94 , pp. 7166-7169
    • Bennett, R.A.O.1    Wilson D. III2    Wong, D.3    Demple, B.4
  • 27
    • 0032951710 scopus 로고    scopus 로고
    • Human thymine DNA glycosylase binds to apurinic sites in DNA but is displaced by human apurinic endonuclease I
    • T. R. Waters, P. Gallinari, J. Jiricny and P. F. Swann, Human thymine DNA glycosylase binds to apurinic sites in DNA but is displaced by human apurinic endonuclease I. J. Biol. Chem. 274, 67-74 (1999).
    • (1999) J. Biol. Chem. , vol.274 , pp. 67-74
    • Waters, T.R.1    Gallinari, P.2    Jiricny, J.3    Swann, P.F.4
  • 28
    • 0033555665 scopus 로고    scopus 로고
    • Intranuclear targeted delivery of functional NF-κB by 70 kDa heat shock protein
    • S. M. Fujihara and S. G. Nadler, Intranuclear targeted delivery of functional NF-κB by 70 kDa heat shock protein. EMBO J. 18, 411-419 (1999).
    • (1999) EMBO J. , vol.18 , pp. 411-419
    • Fujihara, S.M.1    Nadler, S.G.2


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.