메뉴 건너뛰기




Volumn 25, Issue 6, 2004, Pages 1033-1043

UV radiation-induced XPC translocation within chromatin is mediated by damaged-DNA binding protein, DDB2

Author keywords

[No Author keywords available]

Indexed keywords

CYCLOBUTANE; DNA BINDING PROTEIN; PROTEIN P53; PYRIMIDINE; TRANSCRIPTION FACTOR; TUMOR SUPPRESSOR PROTEIN; DDB2 PROTEIN, HUMAN; XPC PROTEIN, HUMAN;

EID: 3042780229     PISSN: 01433334     EISSN: None     Source Type: Journal    
DOI: 10.1093/carcin/bgh085     Document Type: Article
Times cited : (93)

References (64)
  • 1
    • 0033118354 scopus 로고    scopus 로고
    • Molecular mechanism of nucleotide excision repair
    • De Laat,W.L., Jaspers,N.G. and Hoeijmakers,J.H. (1999) Molecular mechanism of nucleotide excision repair. Genes Dev., 13, 768-785.
    • (1999) Genes Dev. , vol.13 , pp. 768-785
    • De Laat, W.L.1    Jaspers, N.G.2    Hoeijmakers, J.H.3
  • 2
    • 0037115936 scopus 로고    scopus 로고
    • Subpathways of nucleotide excision repair and their regulation
    • Hanawalt,P.C. (2002) Subpathways of nucleotide excision repair and their regulation. Oncogene, 21, 8949-8956.
    • (2002) Oncogene , vol.21 , pp. 8949-8956
    • Hanawalt, P.C.1
  • 3
    • 0032716382 scopus 로고    scopus 로고
    • Nucleotide excision repair: From E.coli to man
    • Petit,C. and Sancar,A. (1999) Nucleotide excision repair: from E.coli to man. Biochimie, 81, 15-25.
    • (1999) Biochimie , vol.81 , pp. 15-25
    • Petit, C.1    Sancar, A.2
  • 4
    • 0242605710 scopus 로고    scopus 로고
    • Nucleotide excision repair of DNA with recombinant human proteins: Definition of the minimal set of factors, active forms of TFIIH, and modulation by CAK
    • Araujo,S.J., Tirode,F., Coin,F., Pospiech,H., Syvaoja,J.E., Stucki,M., Hubscher,U., Egly,J.M. and Wood,R.D. (2000) Nucleotide excision repair of DNA with recombinant human proteins: definition of the minimal set of factors, active forms of TFIIH, and modulation by CAK. Genes Dev., 14, 349-359.
    • (2000) Genes Dev. , vol.14 , pp. 349-359
    • Araujo, S.J.1    Tirode, F.2    Coin, F.3    Pospiech, H.4    Syvaoja, J.E.5    Stucki, M.6    Hubscher, U.7    Egly, J.M.8    Wood, R.D.9
  • 5
    • 0035282109 scopus 로고    scopus 로고
    • A multistep damage recognition mechanism for global genomic nucleotide excision repair
    • Sugasawa,K., Okamoto,T., Shimizu,Y., Masutani,C., Iwai,S. and Hanaoka,F. (2001) A multistep damage recognition mechanism for global genomic nucleotide excision repair. Genes Dev., 15, 507-521.
    • (2001) Genes Dev. , vol.15 , pp. 507-521
    • Sugasawa, K.1    Okamoto, T.2    Shimizu, Y.3    Masutani, C.4    Iwai, S.5    Hanaoka, F.6
  • 8
    • 0034737426 scopus 로고    scopus 로고
    • The Xeroderma pigmentosum group C protein complex XPC-HR23B plays an important role in the recruitment of transcription factor IIH to damaged DNA
    • Yokoi,M., Masutani,C., Maekawa,T., Sugasawa,K., Ohkuma,Y. and Hanaoka,F. (2000) The Xeroderma pigmentosum group C protein complex XPC-HR23B plays an important role in the recruitment of transcription factor IIH to damaged DNA. J. Biol. Chem., 275, 9870-9875.
    • (2000) J. Biol. Chem. , vol.275 , pp. 9870-9875
    • Yokoi, M.1    Masutani, C.2    Maekawa, T.3    Sugasawa, K.4    Ohkuma, Y.5    Hanaoka, F.6
  • 9
    • 0032518911 scopus 로고    scopus 로고
    • Release of normal bases from intact DNA by a native DNA repair enzyme
    • Berdal,K.G., Johansen,R.F. and Seeberg,E. (1998) Release of normal bases from intact DNA by a native DNA repair enzyme. EMBO .J., 17, 363-367.
    • (1998) EMBO .J. , vol.17 , pp. 363-367
    • Berdal, K.G.1    Johansen, R.F.2    Seeberg, E.3
  • 10
    • 0031013308 scopus 로고    scopus 로고
    • Open complex formation around a lesion during nucleotide excision repair provides a structure for cleavage by human XPG protein
    • Evans,E., Fellows,J., Coffer,A. and Wood,R.D. (1997) Open complex formation around a lesion during nucleotide excision repair provides a structure for cleavage by human XPG protein. EMBO J., 16, 625-638.
    • (1997) EMBO J. , vol.16 , pp. 625-638
    • Evans, E.1    Fellows, J.2    Coffer, A.3    Wood, R.D.4
  • 11
    • 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. (1995) 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, 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
  • 12
    • 0032928317 scopus 로고    scopus 로고
    • Influence of p53 tumor suppressor protein on bias of DNA repair and apoptotic response in human cells
    • Wani,M.A., Zhu,Q.Z., El-Mahdy,M.A. and Wani,A.A. (1999) Influence of p53 tumor suppressor protein on bias of DNA repair and apoptotic response in human cells. Carcinogenesis, 20, 765-772.
    • (1999) Carcinogenesis , vol.20 , pp. 765-772
    • Wani, M.A.1    Zhu, Q.Z.2    El-Mahdy, M.A.3    Wani, A.A.4
  • 13
    • 0034646620 scopus 로고    scopus 로고
    • Decreased DNA repair efficiency by loss or disruption of p53 function preferentially affects removal of cyclobutane pyrimidine dimers from non-transcribed strand and slow repair sites in transcribed strand
    • Zhu,Q.Z., Wani,M.A., El-mahdy,M. and Wani,A.A. (2000) Decreased DNA repair efficiency by loss or disruption of p53 function preferentially affects removal of cyclobutane pyrimidine dimers from non-transcribed strand and slow repair sites in transcribed strand. J. Biol. Chem., 275, 11492-11497.
    • (2000) J. Biol. Chem. , vol.275 , pp. 11492-11497
    • Zhu, Q.Z.1    Wani, M.A.2    El-mahdy, M.3    Wani, A.A.4
  • 14
    • 0030853074 scopus 로고    scopus 로고
    • Expression of wild-type p53 is required for efficient global genomic nucleotide excision repair in UV-irradiated human fibroblasts
    • Ford,J.M. and Hanawalt,P.C. (1997) Expression of wild-type p53 is required for efficient global genomic nucleotide excision repair in UV-irradiated human fibroblasts. J. Biol. Chem., 272, 28073-28080.
    • (1997) J. Biol. Chem. , vol.272 , pp. 28073-28080
    • Ford, J.M.1    Hanawalt, P.C.2
  • 15
    • 0029029741 scopus 로고
    • Li-Fraumeni syndrome fibroblasts homozygous for p53 mutations are deficient in global DNA repair but exhibit normal transcription-coupled repair and enhanced UV resistance
    • Ford,J.M. and Hanawalt,P.C. (1995) Li-Fraumeni syndrome fibroblasts homozygous for p53 mutations are deficient in global DNA repair but exhibit normal transcription-coupled repair and enhanced UV resistance. Proc. Natl Acad. Sci. USA, 92, 8876-8880.
    • (1995) Proc. Natl Acad. Sci. USA , vol.92 , pp. 8876-8880
    • Ford, J.M.1    Hanawalt, P.C.2
  • 16
    • 0037435411 scopus 로고    scopus 로고
    • Tumor supressor p53 dependent recruitment of nucleotide excision repair factors XPC and TFIIH to DNA damage
    • Wang,Q., Zhu,Q., Wani,M.A., Wani,G., Chen,J. and Wani,A.A. (2003) Tumor supressor p53 dependent recruitment of nucleotide excision repair factors XPC and TFIIH to DNA damage. DNA Rep., 2, 483-499.
    • (2003) DNA Rep. , vol.2 , pp. 483-499
    • Wang, Q.1    Zhu, Q.2    Wani, M.A.3    Wani, G.4    Chen, J.5    Wani, A.A.6
  • 17
    • 0029880959 scopus 로고    scopus 로고
    • Functional interaction between p53 and TFIIH complex are affected by tumour-associated mutations
    • Leveillard,T., Andrea,L., Bissonnette,N., Schaeffer,L., Bracco,L., Egly,J.-M. and Wasylyk,B. (1996) Functional interaction between p53 and TFIIH complex are affected by tumour-associated mutations. EMBO J., 15, 1615-1624.
    • (1996) EMBO J. , vol.15 , pp. 1615-1624
    • Leveillard, T.1    Andrea, L.2    Bissonnette, N.3    Schaeffer, L.4    Bracco, L.5    Egly, J.-M.6    Wasylyk, B.7
  • 19
    • 0037972287 scopus 로고    scopus 로고
    • p53 responsive nucleotide excision repair gene products p48 and XPC, but not p53, localize to sites of UV-irradiation-induced DNA damage, in vivo
    • Fitch,M.E., Cross,I.V. and Ford,J.M. (2003) p53 responsive nucleotide excision repair gene products p48 and XPC, but not p53, localize to sites of UV-irradiation-induced DNA damage, in vivo. Carcinogenesis, 24, 843-850.
    • (2003) Carcinogenesis , vol.24 , pp. 843-850
    • Fitch, M.E.1    Cross, I.V.2    Ford, J.M.3
  • 21
    • 0000516293 scopus 로고    scopus 로고
    • Expression of the p48 xeroderma pigmentosum gene is p53-dependent and is involved in global genomic repair
    • Hwang,B.J., Ford,J.M., Hanawalt,P.C. and Chu,G. (1999) Expression of the p48 xeroderma pigmentosum gene is p53-dependent and is involved in global genomic repair. Proc. Natl Acad. Sci. USA, 96, 424-428.
    • (1999) Proc. Natl Acad. Sci. USA , vol.96 , pp. 424-428
    • Hwang, B.J.1    Ford, J.M.2    Hanawalt, P.C.3    Chu, G.4
  • 23
    • 0023803543 scopus 로고
    • Xeroderma pigmentosum group E cells lack a nuclear factor that binds to damaged DNA
    • Chu,G. and Chang,E. (1988) Xeroderma pigmentosum group E cells lack a nuclear factor that binds to damaged DNA. Science, 242, 564-567.
    • (1988) Science , vol.242 , pp. 564-567
    • Chu, G.1    Chang, E.2
  • 24
    • 0027442869 scopus 로고
    • Characterization of a human DNA damage binding protein implicated in xeroderma pigmentosum
    • Keeney,S., Chang,G.J. and Linn,S. (1993) Characterization of a human DNA damage binding protein implicated in xeroderma pigmentosum E. J. Biol. Chem., 268, 21293-21300.
    • (1993) E. J. Biol. Chem. , vol.268 , pp. 21293-21300
    • Keeney, S.1    Chang, G.J.2    Linn, S.3
  • 25
    • 0029165064 scopus 로고
    • Chromosomal localization and cDNA cloning of the genes (DDB1 and DDB2) for the p127 and p48 subunits of a human damage-specific DNA binding protein
    • Dualan,R., Brody,T., Keeney,S., Nichols,A.F., Admon,A. and Linn,S. (1995) Chromosomal localization and cDNA cloning of the genes (DDB1 and DDB2) for the p127 and p48 subunits of a human damage-specific DNA binding protein. Genomics, 29, 62-69.
    • (1995) Genomics , vol.29 , pp. 62-69
    • Dualan, R.1    Brody, T.2    Keeney, S.3    Nichols, A.F.4    Admon, A.5    Linn, S.6
  • 26
    • 0001232093 scopus 로고    scopus 로고
    • p48 Activates a UV-damaged-DNA binding factor and is defective in xeroderma pigmentosum group E cells that lack binding activity
    • Hwang,B.J., Toering,S., Francke,U. and Chu,G. (1998) p48 Activates a UV-damaged-DNA binding factor and is defective in xeroderma pigmentosum group E cells that lack binding activity. Mol. Cell Biol., 18, 4391-4399.
    • (1998) Mol. Cell Biol. , vol.18 , pp. 4391-4399
    • Hwang, B.J.1    Toering, S.2    Francke, U.3    Chu, G.4
  • 27
    • 0029768095 scopus 로고    scopus 로고
    • Mutations specific to the xeroderma pigmentosum group E Ddb-phenotype
    • Nichols,A.F., Ong,P. and Linn,S. (1996) Mutations specific to the xeroderma pigmentosum group E Ddb-phenotype. J. Biol. Chem., 271, 24317-24320.
    • (1996) J. Biol. Chem. , vol.271 , pp. 24317-24320
    • Nichols, A.F.1    Ong, P.2    Linn, S.3
  • 28
    • 0023103919 scopus 로고
    • Defect in UV-induced unscheduled DNA synthesis in cultured epidermal keratinocytes from xeroderma pigmentosum
    • Kondo,S., Satoh,Y. and Kuroki,T. (1987) Defect in UV-induced unscheduled DNA synthesis in cultured epidermal keratinocytes from xeroderma pigmentosum. Mutat. Res., 183, 95-101.
    • (1987) Mutat. Res. , vol.183 , pp. 95-101
    • Kondo, S.1    Satoh, Y.2    Kuroki, T.3
  • 29
    • 0024592895 scopus 로고
    • Reduced levels of UV-induced unscheduled DNA synthesis in epidermal keratinocytes of patients with xeroderma pigmentosum and correlation with development of skin neoplasms
    • Kondo,S., Satoh,Y. and Kuroki,T. (1989) Reduced levels of UV-induced unscheduled DNA synthesis in epidermal keratinocytes of patients with xeroderma pigmentosum and correlation with development of skin neoplasms. Cancer Res., 49, 1927-1930.
    • (1989) Cancer Res. , vol.49 , pp. 1927-1930
    • Kondo, S.1    Satoh, Y.2    Kuroki, T.3
  • 30
    • 0025123926 scopus 로고
    • Defective DNA repair in cultured melanocytes from xeroderma pigmentosum patients
    • Yamaguchi,J., Mamada,A., Kondo,S. and Satoh,Y. (1990) Defective DNA repair in cultured melanocytes from xeroderma pigmentosum patients. J. Dermatol., 17, 465-472.
    • (1990) J. Dermatol. , vol.17 , pp. 465-472
    • Yamaguchi, J.1    Mamada, A.2    Kondo, S.3    Satoh, Y.4
  • 31
    • 0029133226 scopus 로고
    • DNA repair in human cells: Quantitative assessment of bulky anti-BPDE DNA adducts by non-competitive immunoassays
    • Venkatachalam,S., Denissenko,M.F. and Wani,A.A. (1995) DNA repair in human cells: quantitative assessment of bulky anti-BPDE DNA adducts by non-competitive immunoassays. Carcinogenesis, 16, 2029-2036.
    • (1995) Carcinogenesis , vol.16 , pp. 2029-2036
    • Venkatachalam, S.1    Denissenko, M.F.2    Wani, A.A.3
  • 32
    • 0035794163 scopus 로고    scopus 로고
    • Stable histone deacetylase complexes distinguished by the presence of SANT domain proteins CoREST/kiaa0071 and Mta-L1
    • Humphrey,G.W., Wang,Y., Russanova,V.R., Hirai,T., Qin,J., Nakatani,Y. and Howard,B.H. (2001) Stable histone deacetylase complexes distinguished by the presence of SANT domain proteins CoREST/kiaa0071 and Mta-L1. J. Biol. Chem., 276, 6817-6824.
    • (2001) J. Biol. Chem. , vol.276 , pp. 6817-6824
    • Humphrey, G.W.1    Wang, Y.2    Russanova, V.R.3    Hirai, T.4    Qin, J.5    Nakatani, Y.6    Howard, B.H.7
  • 33
    • 0036606551 scopus 로고    scopus 로고
    • Sequential binding of UV DNA damage binding factor and degradation of the p48 subunit as early events after UV irradiation
    • Rapic-Otrin,V., McLenigan,M.P., Bisi,D.C., Gonzalez,M. and Levine,A.S. (2002) Sequential binding of UV DNA damage binding factor and degradation of the p48 subunit as early events after UV irradiation. Nucleic Acids Res., 30, 2588-2598.
    • (2002) Nucleic Acids Res. , vol.30 , pp. 2588-2598
    • Rapic-Otrin, V.1    McLenigan, M.P.2    Bisi, D.C.3    Gonzalez, M.4    Levine, A.S.5
  • 34
    • 0025270026 scopus 로고
    • Core filaments of the nuclear matrix
    • He,D., Nickerson,J.A. and Penamn,S. (1990) Core filaments of the nuclear matrix. J. Cell Biol., 110, 569-580.
    • (1990) J. Cell Biol. , vol.110 , pp. 569-580
    • He, D.1    Nickerson, J.A.2    Penamn, S.3
  • 35
    • 0030971868 scopus 로고    scopus 로고
    • Components of the human SWI/SNF complex are enriched in active chromatin and are associated with the nuclear matrix
    • Reyes,J.C., Muchardt,C. and Yaniv,M. (1997) Components of the human SWI/SNF complex are enriched in active chromatin and are associated with the nuclear matrix. J. Cell Biol., 137, 263-274.
    • (1997) J. Cell Biol. , vol.137 , pp. 263-274
    • Reyes, J.C.1    Muchardt, C.2    Yaniv, M.3
  • 36
    • 0023425741 scopus 로고
    • Quantitation of pyrimidine dimers by immunoslot blot following sublethal UV-irradiation of human cells
    • Wani,A.A., D'Ambrosio,S.M. and Alvi,N.K. (1987) Quantitation of pyrimidine dimers by immunoslot blot following sublethal UV-irradiation of human cells. Photochem. Photobiol., 46, 477-482.
    • (1987) Photochem. Photobiol. , vol.46 , pp. 477-482
    • Wani, A.A.1    D'Ambrosio, S.M.2    Alvi, N.K.3
  • 37
    • 0021513620 scopus 로고
    • Antibodies to UV irradiated DNA: The monitoring of DNA damage by ELISA and indirect immunofluorescence
    • Wani,A.A., Gibson-D'Ambrosio,R.E. and D'Ambrosio,S.M. (1984) Antibodies to UV irradiated DNA: the monitoring of DNA damage by ELISA and indirect immunofluorescence. Photochem. Photobiol., 40, 465-471.
    • (1984) Photochem. Photobiol. , vol.40 , pp. 465-471
    • Wani, A.A.1    Gibson-D'Ambrosio, R.E.2    D'Ambrosio, S.M.3
  • 38
    • 0034647734 scopus 로고    scopus 로고
    • Human damage-specific DNA-binding protein p48 - characterization of XPE mutations and regulation following UV irradiation
    • Nichols,A.F., Itoh,T., Graham,J.A., Liu,W., Yamaizumi,M. and Linn,S. (2000) Human damage-specific DNA-binding protein p48 - characterization of XPE mutations and regulation following UV irradiation. J. Biol. Chem., 275, 21422-21428.
    • (2000) J. Biol. Chem. , vol.275 , pp. 21422-21428
    • Nichols, A.F.1    Itoh, T.2    Graham, J.A.3    Liu, W.4    Yamaizumi, M.5    Linn, S.6
  • 39
    • 0142091500 scopus 로고    scopus 로고
    • Impaired regulation of tumor suppressor p53 caused by mutations in the xeroderma pigmentosum DDB2 gene: Mutual regulatory interactions between p48(DDB2) and p53
    • Itoh,T., O'Shea,C. and Linn,S. (2003) Impaired regulation of tumor suppressor p53 caused by mutations in the xeroderma pigmentosum DDB2 gene: mutual regulatory interactions between p48(DDB2) and p53. Mol. Cell Biol., 23, 7540-7553.
    • (2003) Mol. Cell Biol. , vol.23 , pp. 7540-7553
    • Itoh, T.1    O'Shea, C.2    Linn, S.3
  • 40
    • 0345306615 scopus 로고    scopus 로고
    • In vivo recruitment of XPC to UV-induced cyclobutane pyrimidine dimers by the DDB2 gene product
    • Fitch,M.E., Nakajima,S., Yasui,A. and Ford,J.M. (2003) In vivo recruitment of XPC to UV-induced cyclobutane pyrimidine dimers by the DDB2 gene product. J. Biol. Chem., 278, 46906-46910.
    • (2003) J. Biol. Chem. , vol.278 , pp. 46906-46910
    • Fitch, M.E.1    Nakajima, S.2    Yasui, A.3    Ford, J.M.4
  • 41
    • 0038771963 scopus 로고    scopus 로고
    • The DDB2 nucleotide excision repair gene product p48 enhances global genomic repair in p53 deficient human fibroblasts
    • Fitch,M.E., Cross,I.V., Turner,S.J., Adimoolam,S., Lin,C.X., Williams,K.G. and Ford,J.M. (2003) The DDB2 nucleotide excision repair gene product p48 enhances global genomic repair in p53 deficient human fibroblasts. DNA Rep., 2, 819-826.
    • (2003) DNA Rep. , vol.2 , pp. 819-826
    • Fitch, M.E.1    Cross, I.V.2    Turner, S.J.3    Adimoolam, S.4    Lin, C.X.5    Williams, K.G.6    Ford, J.M.7
  • 42
    • 0035850238 scopus 로고    scopus 로고
    • The p48 subunit of the damaged-DNA binding protein DDB associates with the CBP/p300 family of histone acetyltransferase
    • Datta,A., Bagchi,S., Nag,A., Shiyanov,P., Adami,G.R., Yoon,T. and Raychaudhuri,P. (2001) The p48 subunit of the damaged-DNA binding protein DDB associates with the CBP/p300 family of histone acetyltransferase. Mutat. Res., 486, 89-97.
    • (2001) Mutat. Res. , vol.486 , pp. 89-97
    • Datta, A.1    Bagchi, S.2    Nag, A.3    Shiyanov, P.4    Adami, G.R.5    Yoon, T.6    Raychaudhuri, P.7
  • 43
    • 0034812915 scopus 로고    scopus 로고
    • Human STAGA complex is a chromatin-acetylating transcription coactivator that interacts with pre-mRNA splicing and DNA damage-binding factors in vivo
    • Martinez,E., Palhan,V.B., Tjernberg,A., Lymar,E.S., Gamper,A.M., Kundu,T.K., Chait,B.T. and Roeder,R.G. (2001) Human STAGA complex is a chromatin-acetylating transcription coactivator that interacts with pre-mRNA splicing and DNA damage-binding factors in vivo. Mol. Cell Biol., 21, 6782-6795.
    • (2001) Mol. Cell Biol. , vol.21 , pp. 6782-6795
    • Martinez, E.1    Palhan, V.B.2    Tjernberg, A.3    Lymar, E.S.4    Gamper, A.M.5    Kundu, T.K.6    Chait, B.T.7    Roeder, R.G.8
  • 44
    • 0017886958 scopus 로고
    • Sodium butyrate inhibits histone deacetylation in cultured cells
    • Candido,E.P., Reeves,R. and Davie,J.R. (1978) Sodium butyrate inhibits histone deacetylation in cultured cells. Cell, 14, 105-113.
    • (1978) Cell , vol.14 , pp. 105-113
    • Candido, E.P.1    Reeves, R.2    Davie, J.R.3
  • 45
    • 0017898940 scopus 로고
    • Suppression of histone deacetylation in vivo and in vitro by sodium butyrate
    • Boffa,L.C., Vidali,G., Mann,R.S. and Allfrey,V.G. (1978) Suppression of histone deacetylation in vivo and in vitro by sodium butyrate. J. Biol. Chem., 253, 3364-3366.
    • (1978) J. Biol. Chem. , vol.253 , pp. 3364-3366
    • Boffa, L.C.1    Vidali, G.2    Mann, R.S.3    Allfrey, V.G.4
  • 46
    • 0017864644 scopus 로고
    • The effect of sodium butyrate on histone modification
    • Sealy,L. and Chalkley,R. (1978) The effect of sodium butyrate on histone modification. Cell, 14, 115-121.
    • (1978) Cell , vol.14 , pp. 115-121
    • Sealy, L.1    Chalkley, R.2
  • 47
    • 0018751050 scopus 로고
    • Sodium butyrate induces new gene expression in Friend erythroleukemic cells
    • Reeves,R. and Cserjesi,P. (1979) Sodium butyrate induces new gene expression in Friend erythroleukemic cells. J. Biol. Chem., 254, 4283-4290.
    • (1979) J. Biol. Chem. , vol.254 , pp. 4283-4290
    • Reeves, R.1    Cserjesi, P.2
  • 48
    • 0030817140 scopus 로고    scopus 로고
    • DNA damage recognition by XPA protein promotes efficient recruitment of transcription factor II H
    • Nocentini,S., Coin,F., Saijo,M., Tanaka,K. and Egly,J.M. (1997) DNA damage recognition by XPA protein promotes efficient recruitment of transcription factor II H. J. Biol. Chem., 272, 22991-22994.
    • (1997) J. Biol. Chem. , vol.272 , pp. 22991-22994
    • Nocentini, S.1    Coin, F.2    Saijo, M.3    Tanaka, K.4    Egly, J.M.5
  • 49
    • 0027483739 scopus 로고
    • Preferential binding of the xeroderma pigmentosum group A complementing protein to damaged DNA
    • Jones,C.J. and Wood,R.D. (1993) Preferential binding of the xeroderma pigmentosum group A complementing protein to damaged DNA. Biochemistry, 32, 12096-12104.
    • (1993) Biochemistry , vol.32 , pp. 12096-12104
    • Jones, C.J.1    Wood, R.D.2
  • 50
    • 0033603338 scopus 로고    scopus 로고
    • Order of assembly of human DNA repair excision nuclease
    • Wakasugi,M. and Sancar,A. (1999) Order of assembly of human DNA repair excision nuclease. J. Biol. Chem., 274, 18759-18768.
    • (1999) J. Biol. Chem. , vol.274 , pp. 18759-18768
    • Wakasugi, M.1    Sancar, A.2
  • 51
    • 0034616963 scopus 로고    scopus 로고
    • Stable binding of human XPC complex to irradiated DNA confers strong discrimination for damaged sites
    • Batty,D., Rapic'-Otrin,V., Levine,A.S. and Wood,R.D. (2000) Stable binding of human XPC complex to irradiated DNA confers strong discrimination for damaged sites. J. Mol. Biol., 300, 275-290.
    • (2000) J. Mol. Biol. , vol.300 , pp. 275-290
    • Batty, D.1    Rapic'-Otrin, V.2    Levine, A.S.3    Wood, R.D.4
  • 52
    • 0037039443 scopus 로고    scopus 로고
    • Translocation of Cockayne syndrome group A protein to the nuclear matrix: Possible relevance to transcription-coupled DNA repair
    • Kamiuchi,S., Saijo,M., Citterio,E., de Jager,M., Hoeijmakers,J.H. and Tanaka,K. (2002) Translocation of Cockayne syndrome group A protein to the nuclear matrix: possible relevance to transcription-coupled DNA repair. Proc. Natl Acad. Sci. USA, 99, 201-206.
    • (2002) Proc. Natl Acad. Sci. USA , vol.99 , pp. 201-206
    • Kamiuchi, S.1    Saijo, M.2    Citterio, E.3    de Jager, M.4    Hoeijmakers, J.H.5    Tanaka, K.6
  • 53
    • 0030971289 scopus 로고    scopus 로고
    • Translocation of a UV-damaged DNA binding protein into a tight association with chromatin after treatment of mammalian cells with UV light
    • Otrin,V.R., McLenigan,M., Takao,M., Levine,A.S. and Protic,M. (1997) Translocation of a UV-damaged DNA binding protein into a tight association with chromatin after treatment of mammalian cells with UV light. J. Cell Sci., 110 (Pt 10), 1159-1168.
    • (1997) J. Cell Sci., , vol.110 , Issue.PART 10 , pp. 1159-1168
    • Otrin, V.R.1    McLenigan, M.2    Takao, M.3    Levine, A.S.4    Protic, M.5
  • 54
    • 0037127293 scopus 로고    scopus 로고
    • DDB accumulates at DNA damage sites immediately after UV irradiation and directly stimulates nucleotide excision repair
    • Wakasugi,M., Kawashima,A., Morioka,H., Linn,S., Sancar,A., Mori,T., Nikaido,O. and Matsunaga,T. (2002) DDB accumulates at DNA damage sites immediately after UV irradiation and directly stimulates nucleotide excision repair. J. Biol. Chem., 277, 1637-1640.
    • (2002) J. Biol. Chem. , vol.277 , pp. 1637-1640
    • Wakasugi, M.1    Kawashima, A.2    Morioka, H.3    Linn, S.4    Sancar, A.5    Mori, T.6    Nikaido, O.7    Matsunaga, T.8
  • 55
    • 0037450761 scopus 로고    scopus 로고
    • p53 is a chromatin accessibility factor for nucleotide excision repair of DNA damage
    • Rubbi,C.P. and Milner,J. (2003) p53 is a chromatin accessibility factor for nucleotide excision repair of DNA damage. EMBO J., 22, 975-986.
    • (2003) EMBO J. , vol.22 , pp. 975-986
    • Rubbi, C.P.1    Milner, J.2
  • 58
    • 0031814129 scopus 로고    scopus 로고
    • Relationship of the xeroderma pigmentosum group E DNA repair defect to the chromatin and DNA binding proteins UV-DDB and replication protein A
    • Otrin,V.R., Kuraoka,I., Nardo,T., McLenigan,M., Eker,A.P., Stefanini,M., Levine,A.S. and Wood,R.D. (1998) Relationship of the xeroderma pigmentosum group E DNA repair defect to the chromatin and DNA binding proteins UV-DDB and replication protein A. Mol. Cell. Biol., 18, 3182-3190.
    • (1998) Mol. Cell. Biol. , vol.18 , pp. 3182-3190
    • Otrin, V.R.1    Kuraoka, I.2    Nardo, T.3    McLenigan, M.4    Eker, A.P.5    Stefanini, M.6    Levine, A.S.7    Wood, R.D.8
  • 59
    • 0020356008 scopus 로고
    • Sodium butyrate stimulates DNA repair in UV-irradiated normal and xeroderma pigmentosum human fibroblasts
    • Smerdon,M.J., Lan,S.Y., Calza,R.E. and Reeves,R. (1982) Sodium butyrate stimulates DNA repair in UV-irradiated normal and xeroderma pigmentosum human fibroblasts. J. Biol. Chem., 257, 13441-13447.
    • (1982) J. Biol. Chem. , vol.257 , pp. 13441-13447
    • Smerdon, M.J.1    Lan, S.Y.2    Calza, R.E.3    Reeves, R.4
  • 60
    • 0030716255 scopus 로고    scopus 로고
    • Characterization of reaction intermediates of human excision repair nuclease
    • Mu,D., Wakasugi,M., Hsu,D.S. and Sancar,A. (1997) Characterization of reaction intermediates of human excision repair nuclease. J. Biol. Chem., 272, 28971-28979.
    • (1997) J. Biol. Chem. , vol.272 , pp. 28971-28979
    • Mu, D.1    Wakasugi, M.2    Hsu, D.S.3    Sancar, A.4
  • 61
    • 0029870677 scopus 로고    scopus 로고
    • Reaction mechanism of human DNA repair excision nuclease
    • Mu,D., Hsu,D.S. and Sancar,A. (1996) Reaction mechanism of human DNA repair excision nuclease. J. Biol. Chem., 271, 8285-8294.
    • (1996) J. Biol. Chem. , vol.271 , pp. 8285-8294
    • Mu, D.1    Hsu, D.S.2    Sancar, A.3
  • 62
    • 0032933141 scopus 로고    scopus 로고
    • Specific acetylation of chromosomal protein HMG-17 by PCAF alters its interaction with nucleosomes
    • Herrera,J.E., Sakaguchi,K., Bergel,M., Trieschmann,L., Nakatani,Y. and Bustin,M. (1999) Specific acetylation of chromosomal protein HMG-17 by PCAF alters its interaction with nucleosomes. Mol. Cell Biol., 19, 3466-3473.
    • (1999) Mol. Cell Biol. , vol.19 , pp. 3466-3473
    • Herrera, J.E.1    Sakaguchi, K.2    Bergel, M.3    Trieschmann, L.4    Nakatani, Y.5    Bustin, M.6
  • 63
    • 0032186185 scopus 로고    scopus 로고
    • Acetylation of HMG I(Y) by CBP turns off IFN beta expression by disrupting the enhanceosome
    • Munshi,N., Merika,M., Yie,J., Senger,K., Chen,G. and Thanos,D. (1998) Acetylation of HMG I(Y) by CBP turns off IFN beta expression by disrupting the enhanceosome. Mol. Cell, 2, 457-467.
    • (1998) Mol. Cell , vol.2 , pp. 457-467
    • Munshi, N.1    Merika, M.2    Yie, J.3    Senger, K.4    Chen, G.5    Thanos, D.6
  • 64
    • 0018801554 scopus 로고
    • Studies of acetylation and deacetylation in high mobility group proteins. Identification of the sites of acetylation in HMG-1
    • Sterner,R., Vidali,G. and Allfrey,V.G. (1979) Studies of acetylation and deacetylation in high mobility group proteins. Identification of the sites of acetylation in HMG-1. J. Biol. Chem., 254, 11577-11583.
    • (1979) J. Biol. Chem. , vol.254 , pp. 11577-11583
    • Sterner, R.1    Vidali, G.2    Allfrey, V.G.3


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.