메뉴 건너뛰기




Volumn 10, Issue 11, 1999, Pages 3583-3594

The ATPase domain but not the acidic region of Cockayne syndrome group B gene product is essential for DNA repair

Author keywords

[No Author keywords available]

Indexed keywords

ADENOSINE TRIPHOSPHATASE; GENE PRODUCT;

EID: 0344614604     PISSN: 10591524     EISSN: None     Source Type: Journal    
DOI: 10.1091/mbc.10.11.3583     Document Type: Article
Times cited : (44)

References (63)
  • 1
    • 0030902253 scopus 로고    scopus 로고
    • Reduced RNA polymerase II transcription in intact and permeabilized Cockayne syndrome group B cells
    • Balajee, A.S., May, A., Dianov, G.L., Friedberg, E.C., and Bohr, V.A. (1997). Reduced RNA polymerase II transcription in intact and permeabilized Cockayne syndrome group B cells. Proc. Natl. Acad. Sci. USA 94, 4306-4311.
    • (1997) Proc. Natl. Acad. Sci. USA , vol.94 , pp. 4306-4311
    • Balajee, A.S.1    May, A.2    Dianov, G.L.3    Friedberg, E.C.4    Bohr, V.A.5
  • 2
    • 0033561043 scopus 로고    scopus 로고
    • Continuous and widespread roles for the Swi-Snf complex in transcription
    • Biggar, S.R., and Crabtree, G.R. (1999). Continuous and widespread roles for the Swi-Snf complex in transcription. EMBO J. 18, 2254-2264.
    • (1999) EMBO J. , vol.18 , pp. 2254-2264
    • Biggar, S.R.1    Crabtree, G.R.2
  • 3
    • 0001534466 scopus 로고
    • Analysis of pyrmidine dimers in defined genes
    • ed. E.C. Friedberg and P.C. Hanawalt, New York: Marcel Dekker
    • Bohr, V.A., and Okumoto, D.S. (1988). Analysis of pyrmidine dimers in defined genes. In: A Laboratory Manual of Research Procedures, ed. E.C. Friedberg and P.C. Hanawalt, New York: Marcel Dekker, 347-366.
    • (1988) A Laboratory Manual of Research Procedures , pp. 347-366
    • Bohr, V.A.1    Okumoto, D.S.2
  • 4
    • 0021905437 scopus 로고
    • DNA repair in an active gene: Removal of pyrimidine dimers from the DHFR gene of CHO cells is much more efficient than in the genome overall
    • Bohr, V.A., Smith, C.A., Okumoto, D.S., and Hanawalt, P.C. (1985). DNA repair in an active gene: removal of pyrimidine dimers from the DHFR gene of CHO cells is much more efficient than in the genome overall. Cell 40, 359-369.
    • (1985) Cell , vol.40 , pp. 359-369
    • Bohr, V.A.1    Smith, C.A.2    Okumoto, D.S.3    Hanawalt, P.C.4
  • 5
    • 0029620994 scopus 로고
    • Mutations in motif II of Escherichia coli DNA helicase II render the enzyme nonfunctional in both mismatch repair and excision repair with differential effects on the unwinding reaction
    • Brosh, R.M.J., and Matson, S.W. (1995). Mutations in motif II of Escherichia coli DNA helicase II render the enzyme nonfunctional in both mismatch repair and excision repair with differential effects on the unwinding reaction. J. Bacteriol. 177, 5612-5621.
    • (1995) J. Bacteriol. , vol.177 , pp. 5612-5621
    • Brosh, R.M.J.1    Matson, S.W.2
  • 6
    • 0032496215 scopus 로고    scopus 로고
    • Biochemical and biological characterization of wild-type and ATPase-deficient Cockayne syndrome B repair protein
    • Citterio, E., Rademakers, S., van der Horst, G.T., van Gool, A.J., Hoeijmakers, J.H., and Vermeulen, W. (1998). Biochemical and biological characterization of wild-type and ATPase-deficient Cockayne syndrome B repair protein. J. Biol. Chem. 273, 11844-11851.
    • (1998) J. Biol. Chem. , vol.273 , pp. 11844-11851
    • Citterio, E.1    Rademakers, S.2    Van Der Horst, G.T.3    Van Gool, A.J.4    Hoeijmakers, J.H.5    Vermeulen, W.6
  • 7
    • 0027941742 scopus 로고
    • Defective repair of ionizing radiation damage in Cockayne's syndrome and xeroderma pigmentosum group G
    • Cooper, P.K., and Leadon, S.A. (1994). Defective repair of ionizing radiation damage in Cockayne's syndrome and xeroderma pigmentosum group G. Ann. NY Acad. Sci. 726, 330-332.
    • (1994) Ann. NY Acad. Sci. , vol.726 , pp. 330-332
    • Cooper, P.K.1    Leadon, S.A.2
  • 8
    • 0031025997 scopus 로고    scopus 로고
    • Defective transcription-coupled., repair of oxidative base damage in Cockayne syndrome patients from XP group G
    • Cooper, P.K., Nouspikel, T., Clarkson, S.G., and Leadon, S.A. (1997). Defective transcription-coupled., repair of oxidative base damage in Cockayne syndrome patients from XP group G. Science 275, 990-993.
    • (1997) Science , vol.275 , pp. 990-993
    • Cooper, P.K.1    Nouspikel, T.2    Clarkson, S.G.3    Leadon, S.A.4
  • 9
    • 0033545960 scopus 로고    scopus 로고
    • Inhibition of RNA polymerase II transcription in human cell extracts by cisplatin DNA damage
    • Cullinane, C., Mazur, S.J., Essigmann, J.M., Phillips, D.R., and Bohr, V.A. (1999). Inhibition of RNA polymerase II transcription in human cell extracts by cisplatin DNA damage. Biochemistry 38, 6204-6212.
    • (1999) Biochemistry , vol.38 , pp. 6204-6212
    • Cullinane, C.1    Mazur, S.J.2    Essigmann, J.M.3    Phillips, D.R.4    Bohr, V.A.5
  • 10
    • 0029157378 scopus 로고
    • Evolution of the SNF2 family of proteins: Subfamilies with distinct sequences and functions
    • Eisen, J.A., Sweder, K.S., and Hanawalt, P.C. (1995). Evolution of the SNF2 family of proteins: subfamilies with distinct sequences and functions. Nucleic Acids Res. 23, 2715-2723.
    • (1995) Nucleic Acids Res. , vol.23 , pp. 2715-2723
    • Eisen, J.A.1    Sweder, K.S.2    Hanawalt, P.C.3
  • 11
    • 0028297860 scopus 로고
    • Gene-specific DNA repair of UV-induced cyclobutane pyrimidine dimers in some cancer-prone and premature-aging human syndromes
    • Evans, M.K., and Bohr, V.A. (1994). Gene-specific DNA repair of UV-induced cyclobutane pyrimidine dimers in some cancer-prone and premature-aging human syndromes. Mutat. Res. 314, 221-231.
    • (1994) Mutat. Res. , vol.314 , pp. 221-231
    • Evans, M.K.1    Bohr, V.A.2
  • 12
    • 0029850732 scopus 로고    scopus 로고
    • Cockayne syndrome - A primary defect in DNA repair, transcription, both or neither?
    • Friedberg, E.C. (1996). Cockayne syndrome - a primary defect in DNA repair, transcription, both or neither? Bioessays 18, 731-738.
    • (1996) Bioessays , vol.18 , pp. 731-738
    • Friedberg, E.C.1
  • 14
    • 0021998243 scopus 로고
    • Adducts from in vivo action of the carcinogen 4-hydroxyaminoquinoline 1-oxide in rats and from in vitro reaction of 4-acetoxyaminoquinoline 1-oxide with DNA and polynucleotides
    • Galiegue-Zouitina, S., Bailleul, B., and Loucheux-Lefebvre, M.H. (1985). Adducts from in vivo action of the carcinogen 4-hydroxyaminoquinoline 1-oxide in rats and from in vitro reaction of 4-acetoxyaminoquinoline 1-oxide with DNA and polynucleotides. Cancer Res. 45, 520-525.
    • (1985) Cancer Res. , vol.45 , pp. 520-525
    • Galiegue-Zouitina, S.1    Bailleul, B.2    Loucheux-Lefebvre, M.H.3
  • 15
    • 0028047403 scopus 로고
    • A dominant negative allele of the Escherichia coli uvrD gene encoding DNA helicase II. A biochemical and genetic characterization
    • George, J.W., Brosh, R.M.J., and Matson, S.W. (1994). A dominant negative allele of the Escherichia coli uvrD gene encoding DNA helicase II. A biochemical and genetic characterization. J. Mol. Biol. 235, 424-435.
    • (1994) J. Mol. Biol. , vol.235 , pp. 424-435
    • George, J.W.1    Brosh, R.M.J.2    Matson, S.W.3
  • 16
    • 0029984256 scopus 로고    scopus 로고
    • Characterization of the interaction between the acidic activation domain of VP16 and the RNA polymerase II initiation factor TFIIB
    • Gupta, R., Emili, A., Pan, G., Xiao, H., Shales, M., Greenblatt, J., and Ingles, C.J. (1996). Characterization of the interaction between the acidic activation domain of VP16 and the RNA polymerase II initiation factor TFIIB. Nucleic Acids Res. 24, 2324-2330.
    • (1996) Nucleic Acids Res. , vol.24 , pp. 2324-2330
    • Gupta, R.1    Emili, A.2    Pan, G.3    Xiao, H.4    Shales, M.5    Greenblatt, J.6    Ingles, C.J.7
  • 17
    • 0023923585 scopus 로고
    • Structural and functional characterization of the short acidic transcriptional activation region of yeast GCN4 protein
    • Hope, I.A., Mahadevan, S., and Struhl, K. (1988). Structural and functional characterization of the short acidic transcriptional activation region of yeast GCN4 protein. Nature 333, 635-640.
    • (1988) Nature , vol.333 , pp. 635-640
    • Hope, I.A.1    Mahadevan, S.2    Struhl, K.3
  • 18
    • 0016440294 scopus 로고
    • The major cause of inactivation and mutation by 4-nitroquinoline 1-oxide in Escherichia coli: Excisable 4NQO-purine adducts
    • Ikenaga, M., Ichikawa-Ryo, H., and Kondo, S. (1975). The major cause of inactivation and mutation by 4-nitroquinoline 1-oxide in Escherichia coli: excisable 4NQO-purine adducts. J. Mol. Biol. 92, 341-356.
    • (1975) J. Mol. Biol. , vol.92 , pp. 341-356
    • Ikenaga, M.1    Ichikawa-Ryo, H.2    Kondo, S.3
  • 19
    • 0028136544 scopus 로고
    • Mutations in the NTP-binding motif of minute virus of mice (MVM) NS-1 protein uncouple ATPase and DNA helicase functions
    • Jindal, H.K., Yong, C.B., Wilson, G.M., Tam, P., and Astell, C.R. (1994). Mutations in the NTP-binding motif of minute virus of mice (MVM) NS-1 protein uncouple ATPase and DNA helicase functions. J. Biol. Chem. 269, 3283-3289.
    • (1994) J. Biol. Chem. , vol.269 , pp. 3283-3289
    • Jindal, H.K.1    Yong, C.B.2    Wilson, G.M.3    Tam, P.4    Astell, C.R.5
  • 20
    • 0023669671 scopus 로고
    • Formation of 8-hydroxyguanine residues in DNA treated with 4-hydroxyaminoquinoline 1-oxide and its related compounds in the presence of seryl-AMP
    • Kohda, K., Tada, M., Hakura, A., Kasai, H., and Kawazoe, Y. (1987). Formation of 8-hydroxyguanine residues in DNA treated with 4-hydroxyaminoquinoline 1-oxide and its related compounds in the presence of seryl-AMP. Biochem. Biophys. Res. Commun. 149, 1141-1148.
    • (1987) Biochem. Biophys. Res. Commun. , vol.149 , pp. 1141-1148
    • Kohda, K.1    Tada, M.2    Hakura, A.3    Kasai, H.4    Kawazoe, Y.5
  • 21
    • 0014243348 scopus 로고
    • Photoreactivation of mutation and killing in Escherichia coli
    • Kondo, S., and Kato, T. (1968). Photoreactivation of mutation and killing in Escherichia coli. Adv. Biol. Med. Phys. 12, 283-298.
    • (1968) Adv. Biol. Med. Phys. , vol.12 , pp. 283-298
    • Kondo, S.1    Kato, T.2
  • 22
    • 0030740262 scopus 로고    scopus 로고
    • Major domain swiveling revealed by the crystal structures of complexes of E. coli Rep helicase bound to single-stranded DNA and ADP
    • Korolev, S., Hsieh, J., Gauss, G.H., Lohman, T.M., and Waksman, G. (1997). Major domain swiveling revealed by the crystal structures of complexes of E. coli Rep helicase bound to single-stranded DNA and ADP. Cell 90, 635-647.
    • (1997) Cell , vol.90 , pp. 635-647
    • Korolev, S.1    Hsieh, J.2    Gauss, G.H.3    Lohman, T.M.4    Waksman, G.5
  • 23
    • 0025888264 scopus 로고
    • Efficient site-directed mutagenesis using uracil-containing DNA
    • Kunkel, T.A., Bebenek, K., and McClary, J. (1991). Efficient site-directed mutagenesis using uracil-containing DNA. Methods Enzymol. 204, 125-139.
    • (1991) Methods Enzymol. , vol.204 , pp. 125-139
    • Kunkel, T.A.1    Bebenek, K.2    McClary, J.3
  • 24
    • 0342446581 scopus 로고
    • Nucleolin, the major nucleolar protein of growing eukaryotic cells: An unusual protein structure revealed by the nucleotide sequence
    • Lapeyre, B., Bourbon, H., and Amalric, F. (1987). Nucleolin, the major nucleolar protein of growing eukaryotic cells: an unusual protein structure revealed by the nucleotide sequence. Proc. Natl. Acad. Sci. USA 84, 1472-1476.
    • (1987) Proc. Natl. Acad. Sci. USA , vol.84 , pp. 1472-1476
    • Lapeyre, B.1    Bourbon, H.2    Amalric, F.3
  • 25
    • 0027295019 scopus 로고
    • The yeast SNF2/ SWI2 protein has DNA-stimulated ATPase activity required for transcriptional activation
    • Laurent, B.C., Treich, I., and Carlson, M. (1993). The yeast SNF2/ SWI2 protein has DNA-stimulated ATPase activity required for transcriptional activation. Genes & Dev. 7, 583-591.
    • (1993) Genes & Dev. , vol.7 , pp. 583-591
    • Laurent, B.C.1    Treich, I.2    Carlson, M.3
  • 26
    • 0027379353 scopus 로고
    • Preferential repair of ionizing radiation-induced damage in the transcribed strand of an active human gene is defective in Cockayne syndrome
    • Leadon, S.A., and Cooper, P.K. (1993). Preferential repair of ionizing radiation-induced damage in the transcribed strand of an active human gene is defective in Cockayne syndrome. Proc. Natl. Acad. Sci. USA 90, 10499-10503.
    • (1993) Proc. Natl. Acad. Sci. USA , vol.90 , pp. 10499-10503
    • Leadon, S.A.1    Cooper, P.K.2
  • 27
    • 0020374786 scopus 로고
    • Three complementation groups in Cockayne syndrome
    • Lehmann, A.R. (1982). Three complementation groups in Cockayne syndrome. Mutat. Res. 106, 347-356.
    • (1982) Mutat. Res. , vol.106 , pp. 347-356
    • Lehmann, A.R.1
  • 28
    • 0018611921 scopus 로고
    • Abnormal kinetics of DNA synthesis in UV light-irradiated cells from patients with Cockayne's syndrome
    • Lehmann, A.R., Kirk-Bell, S., and Mayne, L. (1979). Abnormal kinetics of DNA synthesis in UV light-irradiated cells from patients with Cockayne's syndrome. Cancer Res. 39, 4237-4241.
    • (1979) Cancer Res. , vol.39 , pp. 4237-4241
    • Lehmann, A.R.1    Kirk-Bell, S.2    Mayne, L.3
  • 29
    • 0023652389 scopus 로고
    • Deletion analysis of GAL4 defines two transcriptional activating segments
    • Ma, J., and Ptashne, M. (1987). Deletion analysis of GAL4 defines two transcriptional activating segments. Cell 48, 847-853.
    • (1987) Cell , vol.48 , pp. 847-853
    • Ma, J.1    Ptashne, M.2
  • 31
    • 0027444169 scopus 로고
    • Repair of individual DNA strands in the hamster dihydrofolate reductase gene after treatment with UV light, alkylating agents, and cisplatin
    • May, A., Nairn, R.S., Okumoto, D.S., Wassermann, K., Stevnsner, T., Jones, J.C., and Bohr, V.A. (1993). Repair of individual DNA strands in the hamster dihydrofolate reductase gene after treatment with UV light, alkylating agents, and cisplatin. J. Biol. Chem. 268, 1650-1657.
    • (1993) J. Biol. Chem. , vol.268 , pp. 1650-1657
    • May, A.1    Nairn, R.S.2    Okumoto, D.S.3    Wassermann, K.4    Stevnsner, T.5    Jones, J.C.6    Bohr, V.A.7
  • 32
    • 0020066520 scopus 로고
    • Failure of RNA synthesis to recover after UV irradiation: An early defect in cells from individuals with Cockayne's syndrome and xeroderma pigmentosum
    • Mayne, L.V., and Lehmann, A.R. (1982). Failure of RNA synthesis to recover after UV irradiation: an early defect in cells from individuals with Cockayne's syndrome and xeroderma pigmentosum. Cancer Res. 42, 1473-1478.
    • (1982) Cancer Res. , vol.42 , pp. 1473-1478
    • Mayne, L.V.1    Lehmann, A.R.2
  • 34
    • 0024284028 scopus 로고
    • A simple salting out procedure for extracting DNA from human nucleated cells
    • Miller, S.A., Dykes, D.D., and Polesky, H.F. (1988). A simple salting out procedure for extracting DNA from human nucleated cells. Nucleic Acids Res. 26, 1215.
    • (1988) Nucleic Acids Res. , vol.26 , pp. 1215
    • Miller, S.A.1    Dykes, D.D.2    Polesky, H.F.3
  • 35
    • 0024675824 scopus 로고
    • The biology of the (6-4) photoproduct
    • Mitchell, D.L., and Nairn, R.S. (1989). The biology of the (6-4) photoproduct. Photochem. Photobiol. 49, 805-819.
    • (1989) Photochem. Photobiol. , vol.49 , pp. 805-819
    • Mitchell, D.L.1    Nairn, R.S.2
  • 36
    • 0029810361 scopus 로고    scopus 로고
    • The human CSB (ERCC6) gene corrects the transcription-coupled repair defect in the CHO cell mutant UV61
    • Orren, D.K., Dianov, G.L., and Bohr, V.A. (1996). The human CSB (ERCC6) gene corrects the transcription-coupled repair defect in the CHO cell mutant UV61. Nucleic Acids Res. 24, 3317-3322.
    • (1996) Nucleic Acids Res. , vol.24 , pp. 3317-3322
    • Orren, D.K.1    Dianov, G.L.2    Bohr, V.A.3
  • 37
    • 0026680746 scopus 로고
    • Mutational analysis of a DEAD box RNA helicase: The mammalian translation initiation factor eIF-4A
    • Pause, A., and Sonenberg, N. (1992). Mutational analysis of a DEAD box RNA helicase: the mammalian translation initiation factor eIF-4A. EMBO J. 11, 2543-2654.
    • (1992) EMBO J. , vol.11 , pp. 2543-2654
    • Pause, A.1    Sonenberg, N.2
  • 38
    • 0030986934 scopus 로고    scopus 로고
    • SWI2/SNF2 and related proteins: ATP-driven motors that disrupt protein-DNA interactions?
    • Pazin, M.J., and Kadonaga, J.T. (1997). SWI2/SNF2 and related proteins: ATP-driven motors that disrupt protein-DNA interactions? Cell 88, 737-740.
    • (1997) Cell , vol.88 , pp. 737-740
    • Pazin, M.J.1    Kadonaga, J.T.2
  • 39
    • 0023683667 scopus 로고
    • How eukaryotic transcriptional activators work
    • Ptashne, M. (1988). How eukaryotic transcriptional activators work. Nature 335, 683-689.
    • (1988) Nature , vol.335 , pp. 683-689
    • Ptashne, M.1
  • 40
    • 0029809505 scopus 로고    scopus 로고
    • Functional analysis of the DNA-stimulated ATPase domain of yeast SWI2/SNF2
    • Richmond, E., and Peterson, C.L. (1996). Functional analysis of the DNA-stimulated ATPase domain of yeast SWI2/SNF2. Nucleic Acids Res. 24, 3685-3692.
    • (1996) Nucleic Acids Res. , vol.24 , pp. 3685-3692
    • Richmond, E.1    Peterson, C.L.2
  • 41
    • 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. (1997). RNA polymerase II stalled at a thymine dimer: footprint and effect on excision repair. Nucleic Acids Res. 25, 787-793.
    • (1997) Nucleic Acids Res. , vol.25 , pp. 787-793
    • Selby, C.P.1    Drapkin, R.2    Reinberg, D.3    Sancar, A.4
  • 42
    • 0030822591 scopus 로고    scopus 로고
    • Cockayne syndrome group B protein enhances by polymerase II
    • Selby, C.P., and Sancar, A. (1997a). Cockayne syndrome group B protein enhances by polymerase II. Proc. Natl. Acad. Sci. USA 94, 11205-11209.
    • (1997) Proc. Natl. Acad. Sci. USA , vol.94 , pp. 11205-11209
    • Selby, C.P.1    Sancar, A.2
  • 43
    • 0030822591 scopus 로고    scopus 로고
    • Cockayne syndrome group B protein enhances elongation by RNA polymerase II
    • Selby, C.P., and Sancar, A. (1997b) Cockayne syndrome group B protein enhances elongation by RNA polymerase II. Proc. Natl. Acad. Sci. USA 94, 11205-11209.
    • (1997) Proc. Natl. Acad. Sci. USA , vol.94 , pp. 11205-11209
    • Selby, C.P.1    Sancar, A.2
  • 44
    • 0026672644 scopus 로고
    • Gene- and strand-specific damage and repair in Chinese hamster ovary cells treated with 4-nitroquinoline 1-oxide
    • Snyderwine, E.G., and Bohr, V.A. (1992). Gene- and strand-specific damage and repair in Chinese hamster ovary cells treated with 4-nitroquinoline 1-oxide. Cancer Res. 52, 4183-4189.
    • (1992) Cancer Res. , vol.52 , pp. 4183-4189
    • Snyderwine, E.G.1    Bohr, V.A.2
  • 45
    • 0025345242 scopus 로고
    • Direct and selective binding of an acidic transcriptional activation domain to the TATA-box factor TFIID
    • Stringer, K.F., Ingles, C.J., and Greenblatt, J. (1990). Direct and selective binding of an acidic transcriptional activation domain to the TATA-box factor TFIID. Nature 345, 783-786.
    • (1990) Nature , vol.345 , pp. 783-786
    • Stringer, K.F.1    Ingles, C.J.2    Greenblatt, J.3
  • 47
    • 0024117989 scopus 로고
    • The RAD6 protein of Saccharomyces cerevisiae polyubiquitinates histones, and its acidic domain mediates this activity
    • Sung, P., Prakash, S., and Prakash, L. (1988). The RAD6 protein of Saccharomyces cerevisiae polyubiquitinates histones, and its acidic domain mediates this activity. Genes & Dev. 2, 1476-1485.
    • (1988) Genes & Dev. , vol.2 , pp. 1476-1485
    • Sung, P.1    Prakash, S.2    Prakash, L.3
  • 48
    • 0015338027 scopus 로고
    • High sensitivity of xeroderma pigmentosum cells to the carcinogen 4-nitroguinoline-1-oxide
    • Takebe, H., Furuyama, J.I., Miki, Y., and Kondo, S. (1972). High sensitivity of xeroderma pigmentosum cells to the carcinogen 4-nitroguinoline-1-oxide. Mutat. Res. 15, 98-100.
    • (1972) Mutat. Res. , vol.15 , pp. 98-100
    • Takebe, H.1    Furuyama, J.I.2    Miki, Y.3    Kondo, S.4
  • 50
    • 0032561475 scopus 로고    scopus 로고
    • RNA polymerase II elongation complexes containing the Cockayne syndrome group B protein interact with a molecular complex containing the transcription factor IIH components xeroderma pigmentosum B and p62
    • Tantin, D. (1998). RNA polymerase II elongation complexes containing the Cockayne syndrome group B protein interact with a molecular complex containing the transcription factor IIH components xeroderma pigmentosum B and p62. J. Biol. Chem. 273, 27794-27799.
    • (1998) J. Biol. Chem. , vol.273 , pp. 27794-27799
    • Tantin, D.1
  • 51
    • 0030667078 scopus 로고    scopus 로고
    • Recruitment of the putative transcription-repair coupling factor CSB/ERCC6 to RNA polymerase II elongation complexes
    • Tantin, D., Kansal, A., and Carey, M. (1997). Recruitment of the putative transcription-repair coupling factor CSB/ERCC6 to RNA polymerase II elongation complexes. Mol. Cell. Biol. 17, 6803-6814.
    • (1997) Mol. Cell. Biol. , vol.17 , pp. 6803-6814
    • Tantin, D.1    Kansal, A.2    Carey, M.3
  • 53
    • 0026465665 scopus 로고
    • ERCC6, a member of a subfamily of putative helicases, is involved in Cockayne's syndrome and preferential repair of active genes
    • Troelstra, C., van Gool, A., de Wit, J., Vermeulen, W., Bootsma, D., and Hoeijmakers, J.H. (1992). ERCC6, a member of a subfamily of putative helicases, is involved in Cockayne's syndrome and preferential repair of active genes. Cell 71, 939-953.
    • (1992) Cell , vol.71 , pp. 939-953
    • Troelstra, C.1    Van Gool, A.2    De Wit, J.3    Vermeulen, W.4    Bootsma, D.5    Hoeijmakers, J.H.6
  • 56
    • 0032577452 scopus 로고    scopus 로고
    • Lack of transcription-coupled repair of acetylaminofluorene DNA adducts in human fibroblasts contrasts their efficient inhibition of transcription
    • van Oosterwijk, M.F., Filon, R., de Groot, A.J., van Zeeland, A.A., and Mullenders, L.H. (1998). Lack of transcription-coupled repair of acetylaminofluorene DNA adducts in human fibroblasts contrasts their efficient inhibition of transcription. J. Biol. Chem. 273, 13599-13604.
    • (1998) J. Biol. Chem. , vol.273 , pp. 13599-13604
    • Van Oosterwijk, M.F.1    Filon, R.2    De Groot, A.J.3    Van Zeeland, A.A.4    Mullenders, L.H.5
  • 57
    • 0029941444 scopus 로고    scopus 로고
    • The sensitivity of Cockayne's syndrome cells to DNA-damaging agents is not due to defective transcription-coupled repair of active genes
    • van Oosterwijk, M.F., Versteeg, A., Filon, R., van Zeeland, A.A., and Mullenders, L.H. (1996). The sensitivity of Cockayne's syndrome cells to DNA-damaging agents is not due to defective transcription-coupled repair of active genes. Mol. Cell. Biol. 16, 4436-4444.
    • (1996) Mol. Cell. Biol. , vol.16 , pp. 4436-4444
    • Van Oosterwijk, M.F.1    Versteeg, A.2    Filon, R.3    Van Zeeland, A.A.4    Mullenders, L.H.5
  • 58
    • 0025341294 scopus 로고
    • The genetic defect in Cockayne syndrome is associated with a defect in repair of UV-induced DNA damage in transcriptionally active DNA
    • Venema, J., Mullenders, L.H., Natarajan, AT., van Zeeland, A.A., and Mayne, L.V. (1990). The genetic defect in Cockayne syndrome is associated with a defect in repair of UV-induced DNA damage in transcriptionally active DNA. Proc. Natl. Acad. Sci. USA 87, 4707-4711.
    • (1990) Proc. Natl. Acad. Sci. USA , vol.87 , pp. 4707-4711
    • Venema, J.1    Mullenders, L.H.2    Natarajan, A.T.3    Van Zeeland, A.A.4    Mayne, L.V.5
  • 60
    • 0018328670 scopus 로고
    • Effects of DNA damaging agents on cultured fibroblasts derived from patients with Cockayne syndrome
    • Wade, M.H., and Chu, E.H. (1979). Effects of DNA damaging agents on cultured fibroblasts derived from patients with Cockayne syndrome. Mutat. Res. 59, 49-60.
    • (1979) Mutat. Res. , vol.59 , pp. 49-60
    • Wade, M.H.1    Chu, E.H.2
  • 61
    • 10244263498 scopus 로고    scopus 로고
    • Biochemical analysis of mutant T7 primase/helicase proteins defective in DNA binding, nucleotide hydrolysis, and the coupling of hydrolysis with DNA unwinding
    • Washington, M.T., Rosenberg, A.H., Griffin, K., Studier, F.W., and Patel, S.S. (1996). Biochemical analysis of mutant T7 primase/helicase proteins defective in DNA binding, nucleotide hydrolysis, and the coupling of hydrolysis with DNA unwinding. J. Biol. Chem. 271, 26825-26834.
    • (1996) J. Biol. Chem. , vol.271 , pp. 26825-26834
    • Washington, M.T.1    Rosenberg, A.H.2    Griffin, K.3    Studier, F.W.4    Patel, S.S.5
  • 62
    • 0024590341 scopus 로고
    • A human placental cDNA clone that encodes nonhistone chromosomal protein HMG-1
    • Wen, L., Huang, J.K., Johnson, B.H., and Reeck, G.R. (1989). A human placental cDNA clone that encodes nonhistone chromosomal protein HMG-1. Nucleic Acids Res. 17, 1197-1214.
    • (1989) Nucleic Acids Res. , vol.17 , pp. 1197-1214
    • Wen, L.1    Huang, J.K.2    Johnson, B.H.3    Reeck, G.R.4
  • 63
    • 0031943276 scopus 로고    scopus 로고
    • Yeast RNA polymerase II transcription in vitro is inhibited in the presence of nucleotide excision repair: Complementation of inhibition by HoloTFIIH and requirement for RAD26
    • You, Z., Feaver, W.J., and Friedberg, E.C. (1998). Yeast RNA polymerase II transcription in vitro is inhibited in the presence of nucleotide excision repair: complementation of inhibition by HoloTFIIH and requirement for RAD26. Mol. Cell. Biol. 18, 2668-2676.
    • (1998) Mol. Cell. Biol. , vol.18 , pp. 2668-2676
    • You, Z.1    Feaver, W.J.2    Friedberg, E.C.3


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.