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Volumn 408, Issue , 2006, Pages 189-213

Purification and Characterization of Escherichia coli and Human Nucleotide Excision Repair Enzyme Systems

(2)  Reardon, Joyce T a   Sancar, Aziz a  

a NONE

Author keywords

[No Author keywords available]

Indexed keywords

NUCLEASE;

EID: 33645211068     PISSN: 00766879     EISSN: None     Source Type: Book Series    
DOI: 10.1016/S0076-6879(06)08012-8     Document Type: Review
Times cited : (62)

References (58)
  • 1
    • 0030667311 scopus 로고    scopus 로고
    • Initiation of DNA interstrand cross-link repair in humans: The nucleotide excision repair system makes dual incisions 5′ to the cross-linked base and removes a 22- to 28-nucleotide-long damage-free strand
    • Bessho T., Mu D., and Sancar A. Initiation of DNA interstrand cross-link repair in humans: The nucleotide excision repair system makes dual incisions 5′ to the cross-linked base and removes a 22- to 28-nucleotide-long damage-free strand. Mol. Cell. Biol. 17 (1997) 6822-6830
    • (1997) Mol. Cell. Biol. , vol.17 , pp. 6822-6830
    • Bessho, T.1    Mu, D.2    Sancar, A.3
  • 2
    • 0031023182 scopus 로고    scopus 로고
    • Reconstitution of human excision nuclease with recombinant XPF-ERCC1 complex
    • Bessho T., Sancar A., Thompson L.H., and Thelen M.P. Reconstitution of human excision nuclease with recombinant XPF-ERCC1 complex. J. Biol. Chem. 272 (1997) 3833-3837
    • (1997) J. Biol. Chem. , vol.272 , pp. 3833-3837
    • Bessho, T.1    Sancar, A.2    Thompson, L.H.3    Thelen, M.P.4
  • 4
    • 0021100690 scopus 로고
    • Accurate transcription initiation by RNA polymerase II in a soluble extract from isolated mammalian nuclei
    • Dignam J.D., Lebovitz R.M., and Roeder R.G. Accurate transcription initiation by RNA polymerase II in a soluble extract from isolated mammalian nuclei. Nucleic Acids Res. 11 (1983) 1475-1489
    • (1983) Nucleic Acids Res. , vol.11 , pp. 1475-1489
    • Dignam, J.D.1    Lebovitz, R.M.2    Roeder, R.G.3
  • 6
    • 0034865980 scopus 로고    scopus 로고
    • Reconstitution of recombinant TFIIH that can mediate activator-dependent transcription
    • Fukuda A., Yamauchi J., Wu S.-Y., Chiang C.-M., Muramatsu M., and Hisatake K. Reconstitution of recombinant TFIIH that can mediate activator-dependent transcription. Genes Cells 6 (2001) 707-719
    • (2001) Genes Cells , vol.6 , pp. 707-719
    • Fukuda, A.1    Yamauchi, J.2    Wu, S.-Y.3    Chiang, C.-M.4    Muramatsu, M.5    Hisatake, K.6
  • 7
    • 0024283277 scopus 로고
    • DNA and RNA sequence determination based on phosphorothioate chemistry
    • Gish G., and Eckstein F. DNA and RNA sequence determination based on phosphorothioate chemistry. Science 240 (1988) 1520-1522
    • (1988) Science , vol.240 , pp. 1520-1522
    • Gish, G.1    Eckstein, F.2
  • 8
    • 0036785614 scopus 로고    scopus 로고
    • The SWI/SNF chromatin-remodeling factor stimulates repair by human excision nuclease in the mononucleosome core particle
    • Hara R., and Sancar A. The SWI/SNF chromatin-remodeling factor stimulates repair by human excision nuclease in the mononucleosome core particle. Mol. Cell. Biol. 22 (2002) 6779-6787
    • (2002) Mol. Cell. Biol. , vol.22 , pp. 6779-6787
    • Hara, R.1    Sancar, A.2
  • 9
    • 0038656433 scopus 로고    scopus 로고
    • Effect of damage type on stimulation of human excision nuclease by SWI/SNF chromatin remodeling factor
    • Hara R., and Sancar A. Effect of damage type on stimulation of human excision nuclease by SWI/SNF chromatin remodeling factor. Mol. Cell. Biol. 23 (2003) 4121-4125
    • (2003) Mol. Cell. Biol. , vol.23 , pp. 4121-4125
    • Hara, R.1    Sancar, A.2
  • 10
    • 0028245269 scopus 로고
    • Recombinant replication protein A: Expression, complex formation, and functional characterization
    • Henricksen L.A., Umbricht C.B., and Wold M.S. Recombinant replication protein A: Expression, complex formation, and functional characterization. J. Biol. Chem. 269 (1994) 11121-11132
    • (1994) J. Biol. Chem. , vol.269 , pp. 11121-11132
    • Henricksen, L.A.1    Umbricht, C.B.2    Wold, M.S.3
  • 11
    • 0026508487 scopus 로고
    • Human nucleotide excision nuclease removes thymine dimers from DNA by incising the 22nd phosphodiester bond 5′ and the 6th phosphodiester bond 3′ to the photodimer
    • Huang J.-C., Svoboda D.L., Reardon J.T., and Sancar A. Human nucleotide excision nuclease removes thymine dimers from DNA by incising the 22nd phosphodiester bond 5′ and the 6th phosphodiester bond 3′ to the photodimer. Proc. Natl. Acad. Sci. USA 89 (1992) 3664-3668
    • (1992) Proc. Natl. Acad. Sci. USA , vol.89 , pp. 3664-3668
    • Huang, J.-C.1    Svoboda, D.L.2    Reardon, J.T.3    Sancar, A.4
  • 12
    • 0027944087 scopus 로고
    • Substrate spectrum of human excinuclease: Repair of abasic sites, methylated bases, mismatches, and bulky adducts
    • Huang J.-C., Hsu D.S., Kazantsev A., and Sancar A. Substrate spectrum of human excinuclease: Repair of abasic sites, methylated bases, mismatches, and bulky adducts. Proc. Natl. Acad. Sci. USA 91 (1994) 12213-12217
    • (1994) Proc. Natl. Acad. Sci. USA , vol.91 , pp. 12213-12217
    • Huang, J.-C.1    Hsu, D.S.2    Kazantsev, A.3    Sancar, A.4
  • 13
    • 0040581590 scopus 로고
    • Effect of DNA polymerase I and DNA helicase II on the turnover rate of UvrABC excision nuclease
    • Husain I., Van Houten B., Thomas D.C., Abdel-Moncar M., and Sancar A. Effect of DNA polymerase I and DNA helicase II on the turnover rate of UvrABC excision nuclease. Proc. Natl. Acad. Sci. USA 82 (1985) 6774-6778
    • (1985) Proc. Natl. Acad. Sci. USA , vol.82 , pp. 6774-6778
    • Husain, I.1    Van Houten, B.2    Thomas, D.C.3    Abdel-Moncar, M.4    Sancar, A.5
  • 16
    • 0141427930 scopus 로고    scopus 로고
    • Reduced sulfhydryls maintain specific incision of BPDE-DNA adducts by recombinant thermoresistant Bacillus caldotenax UvrABC endonuclease
    • Jiang G.H., Skorvaga M., Van Houten B., and States J.C. Reduced sulfhydryls maintain specific incision of BPDE-DNA adducts by recombinant thermoresistant Bacillus caldotenax UvrABC endonuclease. Protein Expression Purif. 31 (2003) 88-98
    • (2003) Protein Expression Purif. , vol.31 , pp. 88-98
    • Jiang, G.H.1    Skorvaga, M.2    Van Houten, B.3    States, J.C.4
  • 17
    • 0027442869 scopus 로고
    • Characterization of a human DNA damage binding protein implicated in xeroderma pigmentosum E
    • Keeney S., Chang G.J., and Linn S. Characterization of a human DNA damage binding protein implicated in xeroderma pigmentosum E. J. Biol. Chem. 268 (1993) 21293-21300
    • (1993) J. Biol. Chem. , vol.268 , pp. 21293-21300
    • Keeney, S.1    Chang, G.J.2    Linn, S.3
  • 18
    • 27644510072 scopus 로고    scopus 로고
    • Xeroderma pigmentosom complementation group E protein (XPE/DDB2): Purification of various complexes of XPE and analyses of their damaged DNA binding and putative DNA repair properties
    • Kulaksiz G., Reardon J.T., and Sancar A. Xeroderma pigmentosom complementation group E protein (XPE/DDB2): Purification of various complexes of XPE and analyses of their damaged DNA binding and putative DNA repair properties. Mol. Cell. Biol. 25 (2005) 9784-9792
    • (2005) Mol. Cell. Biol. , vol.25 , pp. 9784-9792
    • Kulaksiz, G.1    Reardon, J.T.2    Sancar, A.3
  • 19
    • 0026100191 scopus 로고
    • An in vitro transcription analysis of early responses of the human immunodeficiency virus type 1 long terminal repeat to different transcriptional activators
    • Li Y., Ross J., Scheppler J.A., and Franza Jr. B.R. An in vitro transcription analysis of early responses of the human immunodeficiency virus type 1 long terminal repeat to different transcriptional activators. Mol. Cell. Biol. 11 (1991) 1883-1893
    • (1991) Mol. Cell. Biol. , vol.11 , pp. 1883-1893
    • Li, Y.1    Ross, J.2    Scheppler, J.A.3    Franza Jr., B.R.4
  • 20
    • 0026077576 scopus 로고
    • The C-terminal half of UvrC protein is sufficient to reconstitute (A)BC excinuclease
    • Lin J.-J., and Sancar A. The C-terminal half of UvrC protein is sufficient to reconstitute (A)BC excinuclease. Proc. Natl. Acad. Sci. USA 88 (1991) 6824-6828
    • (1991) Proc. Natl. Acad. Sci. USA , vol.88 , pp. 6824-6828
    • Lin, J.-J.1    Sancar, A.2
  • 21
    • 0026754657 scopus 로고
    • (A)BC excinuclease: The Escherichia coli nucleotide excision repair enzyme
    • Lin J.J., and Sancar A. (A)BC excinuclease: The Escherichia coli nucleotide excision repair enzyme. Mol. Microbiol. 6 (1992) 2219-2224
    • (1992) Mol. Microbiol. , vol.6 , pp. 2219-2224
    • Lin, J.J.1    Sancar, A.2
  • 23
    • 0242689439 scopus 로고
    • DNA-dependent transcription of adenovirus genes in a soluble whole-cell extract
    • Manley J.L., Fire A., Cano A., Sharp P.A., and Gefter M.L. DNA-dependent transcription of adenovirus genes in a soluble whole-cell extract. Proc. Natl. Acad. Sci. USA 77 (1980) 3855-3859
    • (1980) Proc. Natl. Acad. Sci. USA , vol.77 , pp. 3855-3859
    • Manley, J.L.1    Fire, A.2    Cano, A.3    Sharp, P.A.4    Gefter, M.L.5
  • 25
    • 0029132176 scopus 로고
    • Human DNA repair excision nuclease: Analysis of the roles of the subunits involved in dual incisions by using anti-XPG and anti-ERCC1 antibodies
    • Matsunaga T., Mu D., Park C.-H., Reardon J.T., and Sancar A. Human DNA repair excision nuclease: Analysis of the roles of the subunits involved in dual incisions by using anti-XPG and anti-ERCC1 antibodies. J. Biol. Chem. 270 (1995) 20862-20869
    • (1995) J. Biol. Chem. , vol.270 , pp. 20862-20869
    • Matsunaga, T.1    Mu, D.2    Park, C.-H.3    Reardon, J.T.4    Sancar, A.5
  • 26
    • 17544367892 scopus 로고    scopus 로고
    • Replication protein A confers structure-specific endonuclease activities to the XPF-ERCC1 and XPG subunits of human DNA repair excision nuclease
    • Matsunaga T., Park C.-H., Bessho T., Mu D., and Sancar A. Replication protein A confers structure-specific endonuclease activities to the XPF-ERCC1 and XPG subunits of human DNA repair excision nuclease. J. Biol. Chem. 271 (1996) 11047-11050
    • (1996) J. Biol. Chem. , vol.271 , pp. 11047-11050
    • Matsunaga, T.1    Park, C.-H.2    Bessho, T.3    Mu, D.4    Sancar, A.5
  • 27
    • 0029870677 scopus 로고    scopus 로고
    • Reaction mechanism of human DNA repair excision nuclease
    • Mu D., Hsu D.S., and Sancar A. Reaction mechanism of human DNA repair excision nuclease. J. Biol. Chem. 271 (1996) 8285-8294
    • (1996) J. Biol. Chem. , vol.271 , pp. 8285-8294
    • Mu, D.1    Hsu, D.S.2    Sancar, A.3
  • 28
    • 0028896837 scopus 로고
    • Reconstitution of human DNA repair excision nuclease in a highly defined system
    • Mu D., Park C.-H., Matsunaga T., Hsu D.S., Reardon J.T., and Sancar A. Reconstitution of human DNA repair excision nuclease in a highly defined system. J. Biol. Chem. 270 (1995) 2415-2418
    • (1995) J. Biol. Chem. , vol.270 , pp. 2415-2418
    • Mu, D.1    Park, C.-H.2    Matsunaga, T.3    Hsu, D.S.4    Reardon, J.T.5    Sancar, A.6
  • 33
    • 0028932889 scopus 로고
    • The general transcription-repair factor TFIIH is recruited to the excision repair complex by the XPA protein independent of the TFIIE transcription factor
    • Park C.-H., Mu D., Reardon J.T., and Sancar A. The general transcription-repair factor TFIIH is recruited to the excision repair complex by the XPA protein independent of the TFIIE transcription factor. J. Biol. Chem. 270 (1995) 4896-4902
    • (1995) J. Biol. Chem. , vol.270 , pp. 4896-4902
    • Park, C.-H.1    Mu, D.2    Reardon, J.T.3    Sancar, A.4
  • 34
    • 0027426754 scopus 로고
    • Reconstitution of mammalian excision repair activity with mutant cell-free extracts and XPAC and ERCC1 proteins expressed in Escherichia coli
    • Park C.-H., and Sancar A. Reconstitution of mammalian excision repair activity with mutant cell-free extracts and XPAC and ERCC1 proteins expressed in Escherichia coli. Nucleic Acids Res. 21 (1993) 5110-5116
    • (1993) Nucleic Acids Res. , vol.21 , pp. 5110-5116
    • Park, C.-H.1    Sancar, A.2
  • 35
    • 0030745912 scopus 로고    scopus 로고
    • In vitro repair of oxidative DNA damage by human nucleotide excision repair system: Possible explanation for neurodegeneration in Xeroderma pigmentosum patients
    • Reardon J.T., Bessho T., Kung H.C., Bolton P.H., and Sancar A. In vitro repair of oxidative DNA damage by human nucleotide excision repair system: Possible explanation for neurodegeneration in Xeroderma pigmentosum patients. Proc. Natl. Acad. Sci. USA 94 (1997) 9463-9468
    • (1997) Proc. Natl. Acad. Sci. USA , vol.94 , pp. 9463-9468
    • Reardon, J.T.1    Bessho, T.2    Kung, H.C.3    Bolton, P.H.4    Sancar, A.5
  • 36
    • 0029741027 scopus 로고    scopus 로고
    • Overproduction, purification, and characterization of the XPC subunit of the human DNA repair excision nuclease
    • Reardon J.T., Mu D., and Sancar A. Overproduction, purification, and characterization of the XPC subunit of the human DNA repair excision nuclease. J. Biol. Chem. 271 (1996) 19451-19456
    • (1996) J. Biol. Chem. , vol.271 , pp. 19451-19456
    • Reardon, J.T.1    Mu, D.2    Sancar, A.3
  • 37
    • 0142059994 scopus 로고    scopus 로고
    • Recognition and repair of the cyclobutane thymine dimer, a major cause of skin cancers, by the human excision nuclease
    • Reardon J.T., and Sancar A. Recognition and repair of the cyclobutane thymine dimer, a major cause of skin cancers, by the human excision nuclease. Genes Dev. 17 (2003) 2539-2551
    • (2003) Genes Dev. , vol.17 , pp. 2539-2551
    • Reardon, J.T.1    Sancar, A.2
  • 38
    • 3843137530 scopus 로고    scopus 로고
    • Thermodynamic cooperativity and kinetic proofreading in DNA damage recognition and repair
    • Reardon J.T., and Sancar A. Thermodynamic cooperativity and kinetic proofreading in DNA damage recognition and repair. Cell Cycle 3 (2004) 141-144
    • (2004) Cell Cycle , vol.3 , pp. 141-144
    • Reardon, J.T.1    Sancar, A.2
  • 40
    • 0030855076 scopus 로고    scopus 로고
    • Rodent UV-sensitive mutant cell lines in complementation groups 6-10 have normal general excision repair activity
    • Reardon J.T., Thompson L.H., and Sancar A. Rodent UV-sensitive mutant cell lines in complementation groups 6-10 have normal general excision repair activity. Nucleic Acids Res. 25 (1997) 1015-1021
    • (1997) Nucleic Acids Res. , vol.25 , pp. 1015-1021
    • Reardon, J.T.1    Thompson, L.H.2    Sancar, A.3
  • 41
    • 0033566758 scopus 로고    scopus 로고
    • Efficient nucleotide excision repair of cisplatin, oxaliplatin, and bis-aceto-ammine-dichloro-cyclohexylamine-platinum(IV) (JM216) platinum intrastrand DNA diadducts
    • Reardon J.T., Vaisman A., Chaney S.G., and Sancar A. Efficient nucleotide excision repair of cisplatin, oxaliplatin, and bis-aceto-ammine-dichloro-cyclohexylamine-platinum(IV) (JM216) platinum intrastrand DNA diadducts. Cancer Res. 59 (1999) 3968-3971
    • (1999) Cancer Res. , vol.59 , pp. 3968-3971
    • Reardon, J.T.1    Vaisman, A.2    Chaney, S.G.3    Sancar, A.4
  • 42
    • 0029001182 scopus 로고
    • Excision repair in mammalian cells
    • Sancar A. Excision repair in mammalian cells. J. Biol. Chem. 270 (1995) 15915-15918
    • (1995) J. Biol. Chem. , vol.270 , pp. 15915-15918
    • Sancar, A.1
  • 43
    • 0020641572 scopus 로고
    • A novel repair enzyme: UVRABC excision nuclease of Escherichia coli cuts a DNA strand on both sides of the damaged region
    • Sancar A., and Rupp W.D. A novel repair enzyme: UVRABC excision nuclease of Escherichia coli cuts a DNA strand on both sides of the damaged region. Cell 33 (1983) 249-260
    • (1983) Cell , vol.33 , pp. 249-260
    • Sancar, A.1    Rupp, W.D.2
  • 44
    • 10044226288 scopus 로고    scopus 로고
    • Nucleotide excision repair in E. coli and man
    • Yang W. (Ed), Elsevier Academic Press, San Diego
    • Sancar A., and Reardon J.T. Nucleotide excision repair in E. coli and man. In: Yang W. (Ed). "Advances in Protein Chemistry" Vol. 69 (2004), Elsevier Academic Press, San Diego 43-71
    • (2004) "Advances in Protein Chemistry" , vol.69 , pp. 43-71
    • Sancar, A.1    Reardon, J.T.2
  • 45
    • 33745218298 scopus 로고    scopus 로고
    • Purification and characterization of DNA photolyases
    • [9] this volume.
    • Sancar G.B., and Sancar A. Purification and characterization of DNA photolyases. Methods Enzymol 408 (2006) [9] this volume.
    • (2006) Methods Enzymol , vol.408
    • Sancar, G.B.1    Sancar, A.2
  • 46
    • 33745193942 scopus 로고
    • Purification and properties of UvrABC excision nuclease and its utilization to detect bulky DNA adducts
    • Friedberg E.C., and Hanawalt P.C. (Eds), Dekker, New York
    • Sancar A., Thomas D.C., Van Houten B., Husain I., and Levy M. Purification and properties of UvrABC excision nuclease and its utilization to detect bulky DNA adducts. In: Friedberg E.C., and Hanawalt P.C. (Eds). "DNA Repair: A Laboratory Manual of Research Procedures" Vol. 3 (1988), Dekker, New York 479-508
    • (1988) "DNA Repair: A Laboratory Manual of Research Procedures" , vol.3 , pp. 479-508
    • Sancar, A.1    Thomas, D.C.2    Van Houten, B.3    Husain, I.4    Levy, M.5
  • 47
    • 0027255962 scopus 로고
    • Complementation of the DNA repair defect in xeroderma pigmentosum group G cells by a human cDNA related to yeast RAD2
    • Scherly D., Nouspikel T., Corlet J., Ucla C., Bairoch A., and Clarkson S.G. Complementation of the DNA repair defect in xeroderma pigmentosum group G cells by a human cDNA related to yeast RAD2. Nature 363 (1993) 182-185
    • (1993) Nature , vol.363 , pp. 182-185
    • Scherly, D.1    Nouspikel, T.2    Corlet, J.3    Ucla, C.4    Bairoch, A.5    Clarkson, S.G.6
  • 48
    • 0024547157 scopus 로고
    • In vitro proteolytic cleavage of the Escherichia coli Ada protein by the ompT gene product
    • Sedgwick B. In vitro proteolytic cleavage of the Escherichia coli Ada protein by the ompT gene product. J. Bacteriol. 171 (1989) 2249-2251
    • (1989) J. Bacteriol. , vol.171 , pp. 2249-2251
    • Sedgwick, B.1
  • 49
    • 0030804783 scopus 로고    scopus 로고
    • RNA polymerase II stalled at a thymine dimer: Footprint and effect on excision repair
    • Selby C.P., Drapkin R., Reinberg D., and Sancar A. RNA polymerase II stalled at a thymine dimer: Footprint and effect on excision repair. Nucleic Acids Res. 25 (1997) 787-793
    • (1997) Nucleic Acids Res. , vol.25 , pp. 787-793
    • Selby, C.P.1    Drapkin, R.2    Reinberg, D.3    Sancar, A.4
  • 50
    • 0346275194 scopus 로고    scopus 로고
    • Characterization of transcription-repair coupling factors in E. coli and humans
    • Selby C.P., and Sancar A. Characterization of transcription-repair coupling factors in E. coli and humans. Methods Enzymol. 371 (2003) 300-324
    • (2003) Methods Enzymol. , vol.371 , pp. 300-324
    • Selby, C.P.1    Sancar, A.2
  • 51
    • 0033544942 scopus 로고    scopus 로고
    • Cullin 4A associates with the UV-damaged DNA-binding protein DDB
    • Shiyanov P., Nag A., and Raychaudhuri P. Cullin 4A associates with the UV-damaged DNA-binding protein DDB. J. Biol. Chem. 274 (1999) 35309-35312
    • (1999) J. Biol. Chem. , vol.274 , pp. 35309-35312
    • Shiyanov, P.1    Nag, A.2    Raychaudhuri, P.3
  • 52
    • 0024307545 scopus 로고
    • Human nucleotide excision repair in vitro: Repair of pyrimidine dimers, psoralen and cisplatin adducts by HeLa cell-free extract
    • Sibghat-Ullah W., Husain I., Carlton W., and Sancar A. Human nucleotide excision repair in vitro: Repair of pyrimidine dimers, psoralen and cisplatin adducts by HeLa cell-free extract. Nucleic Acids Res. 17 (1989) 4471-4484
    • (1989) Nucleic Acids Res. , vol.17 , pp. 4471-4484
    • Sibghat-Ullah, W.1    Husain, I.2    Carlton, W.3    Sancar, A.4
  • 53
    • 0025180836 scopus 로고
    • The repair patch of E. coli (A)BC excinuclease
    • Sibghat-Ullah A., Sancar, and Hearst J.E. The repair patch of E. coli (A)BC excinuclease. Nucleic Acids Res. 18 (1990) 5051-5053
    • (1990) Nucleic Acids Res. , vol.18 , pp. 5051-5053
    • Sibghat-Ullah, A.1    Sancar2    Hearst, J.E.3
  • 54
    • 0027392108 scopus 로고
    • DNA repair by eukaryotic nucleotide excision nuclease: Removal of thymine dimer and psoralen monoadduct by HeLa cell-free extract and of thymine dimer by Xenopus laevis oocytes
    • Svoboda D.L., Taylor J.-., Hearst J.E., and Sancar A. DNA repair by eukaryotic nucleotide excision nuclease: Removal of thymine dimer and psoralen monoadduct by HeLa cell-free extract and of thymine dimer by Xenopus laevis oocytes. J. Biol. Chem. 268 (1993) 1931-1936
    • (1993) J. Biol. Chem. , vol.268 , pp. 1931-1936
    • Svoboda, D.L.1    Taylor, J.-.2    Hearst, J.E.3    Sancar, A.4
  • 55
    • 0021847980 scopus 로고
    • Amplification and purification of UvrA, UvrB, and UvrC proteins of Escherichia coli
    • Thomas D.C., Levy M., and Sancar A. Amplification and purification of UvrA, UvrB, and UvrC proteins of Escherichia coli. J. Biol. Chem. 260 (1985) 9875-9883
    • (1985) J. Biol. Chem. , vol.260 , pp. 9875-9883
    • Thomas, D.C.1    Levy, M.2    Sancar, A.3
  • 56
    • 0033010723 scopus 로고    scopus 로고
    • Reconstitution of the transcription factor TFIIH: Assignment of functions for the three enzymatic subunits, XPB, XPD, and cdk 7
    • Tirode F., Busso D., Coin F., and Egly J.-M. Reconstitution of the transcription factor TFIIH: Assignment of functions for the three enzymatic subunits, XPB, XPD, and cdk 7. Mol. Cell 3 (1999) 87-95
    • (1999) Mol. Cell , vol.3 , pp. 87-95
    • Tirode, F.1    Busso, D.2    Coin, F.3    Egly, J.-M.4
  • 57
    • 0023024986 scopus 로고
    • Construction of DNA substrates modified with psoralen at a unique site and study of the action mechanism of ABC excinuclease on these uniformly modified substrates
    • Van Houten B., Gamper H., Hearst J.E., and Sancar A. Construction of DNA substrates modified with psoralen at a unique site and study of the action mechanism of ABC excinuclease on these uniformly modified substrates. J. Biol. Chem. 261 (1986) 14135-14141
    • (1986) J. Biol. Chem. , vol.261 , pp. 14135-14141
    • Van Houten, B.1    Gamper, H.2    Hearst, J.E.3    Sancar, A.4
  • 58
    • 0023878893 scopus 로고
    • Complementation of the Xeroderma pigmentosum DNA repair defect in cell-free extracts
    • Wood R.D., Robins P., and Lindahl T. Complementation of the Xeroderma pigmentosum DNA repair defect in cell-free extracts. Cell 53 (1988) 97-106
    • (1988) Cell , vol.53 , pp. 97-106
    • Wood, R.D.1    Robins, P.2    Lindahl, T.3


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