메뉴 건너뛰기




Volumn 135, Issue 7, 2008, Pages 1213-1223

Structural Basis of UV DNA-Damage Recognition by the DDB1-DDB2 Complex

Author keywords

DNA; PROTEINS

Indexed keywords

DNA BINDING PROTEIN; PROTEIN DDB1; PROTEIN DDB2; UBIQUITIN PROTEIN LIGASE; UNCLASSIFIED DRUG;

EID: 57749198023     PISSN: 00928674     EISSN: None     Source Type: Journal    
DOI: 10.1016/j.cell.2008.10.045     Document Type: Article
Times cited : (347)

References (59)
  • 2
    • 33749535905 scopus 로고    scopus 로고
    • Molecular architecture and assembly of the DDB1-CUL4A ubiquitin ligase machinery
    • Angers S., Li T., Yi X., MacCoss M.J., Moon R.T., and Zheng N. Molecular architecture and assembly of the DDB1-CUL4A ubiquitin ligase machinery. Nature 443 (2006) 590-593
    • (2006) Nature , vol.443 , pp. 590-593
    • Angers, S.1    Li, T.2    Yi, X.3    MacCoss, M.J.4    Moon, R.T.5    Zheng, N.6
  • 4
    • 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. Stable binding of human XPC complex to irradiated DNA confers strong discrimination for damaged sites. J. Mol. Biol. 300 (2000) 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
  • 5
    • 21744452376 scopus 로고    scopus 로고
    • Cancer in xeroderma pigmentosum and related disorders of DNA repair
    • Cleaver J.E. Cancer in xeroderma pigmentosum and related disorders of DNA repair. Nat. Rev. Cancer 5 (2005) 564-573
    • (2005) Nat. Rev. Cancer , vol.5 , pp. 564-573
    • Cleaver, J.E.1
  • 6
    • 0028103275 scopus 로고
    • The CCP4 suite: programs for protein crystallography
    • Collaborative Computational Project, Number 4
    • Collaborative Computational Project, Number 4. The CCP4 suite: programs for protein crystallography. Acta Crystallogr. 50 (1994) 760-763
    • (1994) Acta Crystallogr. , vol.50 , pp. 760-763
  • 7
    • 0037143629 scopus 로고    scopus 로고
    • DNA-dependent divalent cation binding in the nucleosome core particle
    • Davey C.A., and Richmond T.J. DNA-dependent divalent cation binding in the nucleosome core particle. Proc. Natl. Acad. Sci. USA 99 (2002) 11169-11174
    • (2002) Proc. Natl. Acad. Sci. USA , vol.99 , pp. 11169-11174
    • Davey, C.A.1    Richmond, T.J.2
  • 8
    • 0031058188 scopus 로고    scopus 로고
    • Maximum-likelihood heavy-atom parameter refinement for multiple isomorphous replacement and multiwavelength anomalous diffraction methods
    • delaFortelle E., and Bricogne G. Maximum-likelihood heavy-atom parameter refinement for multiple isomorphous replacement and multiwavelength anomalous diffraction methods. Macromol. Crystallogr. A 276 (1997) 472-494
    • (1997) Macromol. Crystallogr. A , vol.276 , pp. 472-494
    • delaFortelle, E.1    Bricogne, G.2
  • 9
    • 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. 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 (1995) 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
  • 10
    • 33744958177 scopus 로고    scopus 로고
    • Cullin 4A-mediated proteolysis of DDB2 protein at DNA damage sites regulates in vivo lesion recognition by XPC
    • El-Mahdy M.A., Zhu Q., Wang Q.E., Wani G., Praetorius-Ibba M., and Wani A.A. Cullin 4A-mediated proteolysis of DDB2 protein at DNA damage sites regulates in vivo lesion recognition by XPC. J. Biol. Chem. 281 (2006) 13404-13411
    • (2006) J. Biol. Chem. , vol.281 , pp. 13404-13411
    • El-Mahdy, M.A.1    Zhu, Q.2    Wang, Q.E.3    Wani, G.4    Praetorius-Ibba, M.5    Wani, A.A.6
  • 12
    • 0017115180 scopus 로고
    • A DNA binding protein from human placenta specific for ultraviolet damaged DNA
    • Feldberg R.S., and Grossman L. A DNA binding protein from human placenta specific for ultraviolet damaged DNA. Biochemistry 15 (1976) 2402-2408
    • (1976) Biochemistry , vol.15 , pp. 2402-2408
    • Feldberg, R.S.1    Grossman, L.2
  • 13
    • 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. In vivo recruitment of XPC to UV-induced cyclobutane pyrimidine dimers by the DDB2 gene product. J. Biol. Chem. 278 (2003) 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
  • 15
    • 0034765256 scopus 로고    scopus 로고
    • Identification of basic residues in RAG2 critical for DNA binding by the RAG1-RAG2 complex
    • Fugmann S.D., and Schatz D.G. Identification of basic residues in RAG2 critical for DNA binding by the RAG1-RAG2 complex. Mol. Cell 8 (2001) 899-910
    • (2001) Mol. Cell , vol.8 , pp. 899-910
    • Fugmann, S.D.1    Schatz, D.G.2
  • 16
    • 0033538572 scopus 로고    scopus 로고
    • Characterization of DNA recognition by the human UV-damaged DNA-binding protein
    • Fujiwara Y., Masutani C., Mizukoshi T., Kondo J., Hanaoka F., and Iwai S. Characterization of DNA recognition by the human UV-damaged DNA-binding protein. J. Biol. Chem. 274 (1999) 20027-20033
    • (1999) J. Biol. Chem. , vol.274 , pp. 20027-20033
    • Fujiwara, Y.1    Masutani, C.2    Mizukoshi, T.3    Kondo, J.4    Hanaoka, F.5    Iwai, S.6
  • 17
    • 0005001210 scopus 로고
    • UV-induced formation of pyrimidine dimers in nucleosome core DNA is strongly modulated with a period of 10.3 bases
    • Gale J.M., Nissen K.A., and Smerdon M.J. UV-induced formation of pyrimidine dimers in nucleosome core DNA is strongly modulated with a period of 10.3 bases. Proc. Natl. Acad. Sci. USA 84 (1987) 6644-6648
    • (1987) Proc. Natl. Acad. Sci. USA , vol.84 , pp. 6644-6648
    • Gale, J.M.1    Nissen, K.A.2    Smerdon, M.J.3
  • 18
    • 0032580979 scopus 로고    scopus 로고
    • NMR solution structure of a DNA dodecamer duplex containing a cis-diammineplatinum(II) d(GpG) intrastrand cross-link, the major adduct of the anticancer drug cisplatin
    • Gelasco A., and Lippard S.J. NMR solution structure of a DNA dodecamer duplex containing a cis-diammineplatinum(II) d(GpG) intrastrand cross-link, the major adduct of the anticancer drug cisplatin. Biochemistry 37 (1998) 9230-9239
    • (1998) Biochemistry , vol.37 , pp. 9230-9239
    • Gelasco, A.1    Lippard, S.J.2
  • 19
    • 32644450616 scopus 로고    scopus 로고
    • Molecular mechanisms of mammalian global genome nucleotide excision repair
    • Gillet L.C., and Scharer O.D. Molecular mechanisms of mammalian global genome nucleotide excision repair. Chem. Rev. 106 (2006) 253-276
    • (2006) Chem. Rev. , vol.106 , pp. 253-276
    • Gillet, L.C.1    Scharer, O.D.2
  • 20
    • 0037509859 scopus 로고    scopus 로고
    • The ubiquitin ligase activity in the DDB2 and CSA complexes is differentially regulated by the COP9 signalosome in response to DNA damage
    • Groisman R., Polanowska J., Kuraoka I., Sawada J., Saijo M., Drapkin R., Kisselev A.F., Tanaka K., and Nakatani Y. The ubiquitin ligase activity in the DDB2 and CSA complexes is differentially regulated by the COP9 signalosome in response to DNA damage. Cell 113 (2003) 357-367
    • (2003) Cell , vol.113 , pp. 357-367
    • Groisman, R.1    Polanowska, J.2    Kuraoka, I.3    Sawada, J.4    Saijo, M.5    Drapkin, R.6    Kisselev, A.F.7    Tanaka, K.8    Nakatani, Y.9
  • 21
    • 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. 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 (1998) 4391-4399
    • (1998) Mol. Cell. Biol. , vol.18 , pp. 4391-4399
    • Hwang, B.J.1    Toering, S.2    Francke, U.3    Chu, G.4
  • 22
    • 0029777391 scopus 로고    scopus 로고
    • Synthesis of a phosphoramidite coupling unit of the pyrimidine (6-4) pyrimidone photoproduct and its incorporation into oligodeoxynucleotides
    • Iwai S., Shimizu M., Kamiya H., and Ohtsuka E. Synthesis of a phosphoramidite coupling unit of the pyrimidine (6-4) pyrimidone photoproduct and its incorporation into oligodeoxynucleotides. J. Am. Chem. Soc. 118 (1996) 7642-7643
    • (1996) J. Am. Chem. Soc. , vol.118 , pp. 7642-7643
    • Iwai, S.1    Shimizu, M.2    Kamiya, H.3    Ohtsuka, E.4
  • 23
    • 0032529296 scopus 로고    scopus 로고
    • Thermodynamic and base-pairing studies of matched and mismatched DNA dodecamer duplexes containing cis-syn, (6-4) and Dewar photoproducts of TT
    • Jing Y., Kao J.F., and Taylor J.S. Thermodynamic and base-pairing studies of matched and mismatched DNA dodecamer duplexes containing cis-syn, (6-4) and Dewar photoproducts of TT. Nucleic Acids Res. 26 (1998) 3845-3853
    • (1998) Nucleic Acids Res. , vol.26 , pp. 3845-3853
    • Jing, Y.1    Kao, J.F.2    Taylor, J.S.3
  • 24
    • 0027879008 scopus 로고
    • Automatic processing of rotation diffraction data from crystals of initially unknown symmetry and cell constants
    • Kabsch W. Automatic processing of rotation diffraction data from crystals of initially unknown symmetry and cell constants. J. Appl. Cryst. 26 (1993) 795-800
    • (1993) J. Appl. Cryst. , vol.26 , pp. 795-800
    • Kabsch, W.1
  • 25
    • 33644536070 scopus 로고    scopus 로고
    • The DDB1-CUL4ADDB2 ubiquitin ligase is deficient in xeroderma pigmentosum group E and targets histone H2A at UV-damaged DNA sites
    • Kapetanaki M.G., Guerrero-Santoro J., Bisi D.C., Hsieh C.L., Rapic-Otrin V., and Levine A.S. The DDB1-CUL4ADDB2 ubiquitin ligase is deficient in xeroderma pigmentosum group E and targets histone H2A at UV-damaged DNA sites. Proc. Natl. Acad. Sci. USA 103 (2006) 2588-2593
    • (2006) Proc. Natl. Acad. Sci. USA , vol.103 , pp. 2588-2593
    • Kapetanaki, M.G.1    Guerrero-Santoro, J.2    Bisi, D.C.3    Hsieh, C.L.4    Rapic-Otrin, V.5    Levine, A.S.6
  • 26
    • 30344460705 scopus 로고    scopus 로고
    • Structure of DDB1 in complex with a paramyxovirus V protein: viral hijack of a propeller cluster in ubiquitin ligase
    • Li T., Chen X., Garbutt K.C., Zhou P., and Zheng N. Structure of DDB1 in complex with a paramyxovirus V protein: viral hijack of a propeller cluster in ubiquitin ligase. Cell 124 (2006) 105-117
    • (2006) Cell , vol.124 , pp. 105-117
    • Li, T.1    Chen, X.2    Garbutt, K.C.3    Zhou, P.4    Zheng, N.5
  • 27
    • 50349085962 scopus 로고    scopus 로고
    • 3DNA: a versatile, integrated software system for the analysis, rebuilding and visualization of three-dimensional nucleic-acid structures
    • Lu X.J., and Olson W.K. 3DNA: a versatile, integrated software system for the analysis, rebuilding and visualization of three-dimensional nucleic-acid structures. Nat. Protocols 3 (2008) 1213-1227
    • (2008) Nat. Protocols , vol.3 , pp. 1213-1227
    • Lu, X.J.1    Olson, W.K.2
  • 29
    • 33644626078 scopus 로고    scopus 로고
    • NMR structures of damaged DNA
    • Lukin M., and de Los Santos C. NMR structures of damaged DNA. Chem. Rev. 106 (2006) 607-686
    • (2006) Chem. Rev. , vol.106 , pp. 607-686
    • Lukin, M.1    de Los Santos, C.2
  • 32
    • 34948892722 scopus 로고    scopus 로고
    • Recognition of DNA damage by the Rad4 nucleotide excision repair protein
    • Min J.H., and Pavletich N.P. Recognition of DNA damage by the Rad4 nucleotide excision repair protein. Nature 449 (2007) 570-575
    • (2007) Nature , vol.449 , pp. 570-575
    • Min, J.H.1    Pavletich, N.P.2
  • 33
    • 16244423719 scopus 로고    scopus 로고
    • The UV-damaged DNA binding protein mediates efficient targeting of the nucleotide excision repair complex to UV-induced photo lesions
    • Moser J., Volker M., Kool H., Alekseev S., Vrieling H., Yasui A., van Zeeland A.A., and Mullenders L.H. The UV-damaged DNA binding protein mediates efficient targeting of the nucleotide excision repair complex to UV-induced photo lesions. DNA Repair (Amst.) 4 (2005) 571-582
    • (2005) DNA Repair (Amst.) , vol.4 , pp. 571-582
    • Moser, J.1    Volker, M.2    Kool, H.3    Alekseev, S.4    Vrieling, H.5    Yasui, A.6    van Zeeland, A.A.7    Mullenders, L.H.8
  • 35
    • 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. Human damage-specific DNA-binding protein p48. Characterization of XPE mutations and regulation following UV irradiation. J. Biol. Chem. 275 (2000) 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
  • 36
    • 33847727050 scopus 로고    scopus 로고
    • Ubiquitin proteasome system (UPS): what can chromatin do for you?
    • O'Connell B.C., and Harper J.W. Ubiquitin proteasome system (UPS): what can chromatin do for you?. Curr. Opin. Cell Biol. 19 (2007) 206-214
    • (2007) Curr. Opin. Cell Biol. , vol.19 , pp. 206-214
    • O'Connell, B.C.1    Harper, J.W.2
  • 37
    • 35548951922 scopus 로고    scopus 로고
    • Base flipping of the thymine dimer in duplex DNA
    • O'Neil L.L., Grossfield A., and Wiest O. Base flipping of the thymine dimer in duplex DNA. J. Phys. Chem. B 111 (2007) 11843-11849
    • (2007) J. Phys. Chem. B , vol.111 , pp. 11843-11849
    • O'Neil, L.L.1    Grossfield, A.2    Wiest, O.3
  • 38
    • 0031059866 scopus 로고    scopus 로고
    • Processing of X-ray diffraction data collected in oscillation mode
    • Otwinowski Z., and Minor W. Processing of X-ray diffraction data collected in oscillation mode. Macromol. Crystallogr. A 276 (1997) 307-326
    • (1997) Macromol. Crystallogr. A , vol.276 , pp. 307-326
    • Otwinowski, Z.1    Minor, W.2
  • 39
    • 0027989651 scopus 로고
    • Xeroderma pigmentosum group E binding factor recognizes a broad spectrum of DNA damage
    • Payne A., and Chu G. Xeroderma pigmentosum group E binding factor recognizes a broad spectrum of DNA damage. Mutat. Res. 310 (1994) 89-102
    • (1994) Mutat. Res. , vol.310 , pp. 89-102
    • Payne, A.1    Chu, G.2
  • 40
    • 0038105065 scopus 로고    scopus 로고
    • True XP group E patients have a defective UV-damaged DNA binding protein complex and mutations in DDB2 which reveal the functional domains of its p48 product
    • Rapic-Otrin V., Navazza V., Nardo T., Botta E., McLenigan M., Bisi D.C., Levine A.S., and Stefanini M. True XP group E patients have a defective UV-damaged DNA binding protein complex and mutations in DDB2 which reveal the functional domains of its p48 product. Hum. Mol. Genet. 12 (2003) 1507-1522
    • (2003) Hum. Mol. Genet. , vol.12 , pp. 1507-1522
    • Rapic-Otrin, V.1    Navazza, V.2    Nardo, T.3    Botta, E.4    McLenigan, M.5    Bisi, D.C.6    Levine, A.S.7    Stefanini, M.8
  • 41
    • 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
    • Rapic Otrin V., Kuraoka I., Nardo T., McLenigan M., Eker A.P., Stefanini M., Levine A.S., and Wood R.D. 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 (1998) 3182-3190
    • (1998) Mol. Cell. Biol. , vol.18 , pp. 3182-3190
    • Rapic Otrin, V.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
  • 42
    • 0027445650 scopus 로고
    • Comparative analysis of binding of human damaged DNA-binding protein (XPE) and Escherichia coli damage recognition protein (UvrA) to the major ultraviolet photoproducts: T[c,s]T, T[t,s]T, T[6-4]T, and T[Dewar]T
    • Reardon J.T., Nichols A.F., Keeney S., Smith C.A., Taylor J.S., Linn S., and Sancar A. Comparative analysis of binding of human damaged DNA-binding protein (XPE) and Escherichia coli damage recognition protein (UvrA) to the major ultraviolet photoproducts: T[c,s]T, T[t,s]T, T[6-4]T, and T[Dewar]T. J. Biol. Chem. 268 (1993) 21301-21308
    • (1993) J. Biol. Chem. , vol.268 , pp. 21301-21308
    • Reardon, J.T.1    Nichols, A.F.2    Keeney, S.3    Smith, C.A.4    Taylor, J.S.5    Linn, S.6    Sancar, A.7
  • 43
    • 37549039510 scopus 로고    scopus 로고
    • A short history of SHELX
    • Sheldrick G.M. A short history of SHELX. Acta Crystallogr. A 64 (2008) 112-122
    • (2008) Acta Crystallogr. A , vol.64 , pp. 112-122
    • Sheldrick, G.M.1
  • 44
    • 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
  • 47
    • 0027203512 scopus 로고
    • A 127 kDa component of a UV-damaged DNA-binding complex, which is defective in some xeroderma pigmentosum group E patients, is homologous to a slime mold protein
    • Takao M., Abramic M., Moos Jr. M., Otrin V.R., Wootton J.C., McLenigan M., Levine A.S., and Protic M. A 127 kDa component of a UV-damaged DNA-binding complex, which is defective in some xeroderma pigmentosum group E patients, is homologous to a slime mold protein. Nucleic Acids Res. 21 (1993) 4111-4118
    • (1993) Nucleic Acids Res. , vol.21 , pp. 4111-4118
    • Takao, M.1    Abramic, M.2    Moos Jr., M.3    Otrin, V.R.4    Wootton, J.C.5    McLenigan, M.6    Levine, A.S.7    Protic, M.8
  • 48
    • 0037031210 scopus 로고    scopus 로고
    • Xeroderma pigmentosum complementation group E and UV-damaged DNA-binding protein
    • Tang J., and Chu G. Xeroderma pigmentosum complementation group E and UV-damaged DNA-binding protein. DNA Repair (Amst.) 1 (2002) 601-616
    • (2002) DNA Repair (Amst.) , vol.1 , pp. 601-616
    • Tang, J.1    Chu, G.2
  • 49
    • 0033636515 scopus 로고    scopus 로고
    • Xeroderma pigmentosum p48 gene enhances global genomic repair and suppresses UV-induced mutagenesis
    • Tang J.Y., Hwang B.J., Ford J.M., Hanawalt P.C., and Chu G. Xeroderma pigmentosum p48 gene enhances global genomic repair and suppresses UV-induced mutagenesis. Mol. Cell 5 (2000) 737-744
    • (2000) Mol. Cell , vol.5 , pp. 737-744
    • Tang, J.Y.1    Hwang, B.J.2    Ford, J.M.3    Hanawalt, P.C.4    Chu, G.5
  • 50
    • 21844442362 scopus 로고    scopus 로고
    • Repair of UV lesions in nucleosomes-intrinsic properties and remodeling
    • Thoma F. Repair of UV lesions in nucleosomes-intrinsic properties and remodeling. DNA Repair (Amst.) 4 (2005) 855-869
    • (2005) DNA Repair (Amst.) , vol.4 , pp. 855-869
    • Thoma, F.1
  • 51
    • 0026466831 scopus 로고
    • An ultraviolet light-damaged DNA recognition protein absent in xeroderma pigmentosum group E cells binds selectively to pyrimidine (6-4) pyrimidone photoproducts
    • Treiber D.K., Chen Z., and Essigmann J.M. An ultraviolet light-damaged DNA recognition protein absent in xeroderma pigmentosum group E cells binds selectively to pyrimidine (6-4) pyrimidone photoproducts. Nucleic Acids Res. 20 (1992) 5805-5810
    • (1992) Nucleic Acids Res. , vol.20 , pp. 5805-5810
    • Treiber, D.K.1    Chen, Z.2    Essigmann, J.M.3
  • 52
    • 0000560808 scopus 로고    scopus 로고
    • MOLREP: an automated program for molecular replacement
    • Vagin A., and Teplyakov A. MOLREP: an automated program for molecular replacement. J. Appl. Cryst. 30 (1997) 1022-1025
    • (1997) J. Appl. Cryst. , vol.30 , pp. 1022-1025
    • Vagin, A.1    Teplyakov, A.2
  • 53
    • 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. DDB accumulates at DNA damage sites immediately after UV irradiation and directly stimulates nucleotide excision repair. J. Biol. Chem. 277 (2002) 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
  • 54
    • 33744781568 scopus 로고    scopus 로고
    • Histone H3 and H4 ubiquitylation by the CUL4-DDB-ROC1 ubiquitin ligase facilitates cellular response to DNA damage
    • Wang H., Zhai L., Xu J., Joo H.Y., Jackson S., Erdjument-Bromage H., Tempst P., Xiong Y., and Zhang Y. Histone H3 and H4 ubiquitylation by the CUL4-DDB-ROC1 ubiquitin ligase facilitates cellular response to DNA damage. Mol. Cell 22 (2006) 383-394
    • (2006) Mol. Cell , vol.22 , pp. 383-394
    • Wang, H.1    Zhai, L.2    Xu, J.3    Joo, H.Y.4    Jackson, S.5    Erdjument-Bromage, H.6    Tempst, P.7    Xiong, Y.8    Zhang, Y.9
  • 56
    • 28944440380 scopus 로고    scopus 로고
    • DDB1-DDB2 (xeroderma pigmentosum group E) protein complex recognizes a cyclobutane pyrimidine dimer, mismatches, apurinic/apyrimidinic sites, and compound lesions in DNA
    • Wittschieben B.O., Iwai S., and Wood R.D. DDB1-DDB2 (xeroderma pigmentosum group E) protein complex recognizes a cyclobutane pyrimidine dimer, mismatches, apurinic/apyrimidinic sites, and compound lesions in DNA. J. Biol. Chem. 280 (2005) 39982-39989
    • (2005) J. Biol. Chem. , vol.280 , pp. 39982-39989
    • Wittschieben, B.O.1    Iwai, S.2    Wood, R.D.3
  • 57
    • 0037756787 scopus 로고    scopus 로고
    • Structure of a beta-TrCP1-Skp1-beta-catenin complex: destruction motif binding and lysine specificity of the SCF(beta-TrCP1) ubiquitin ligase
    • Wu G., Xu G., Schulman B.A., Jeffrey P.D., Harper J.W., and Pavletich N.P. Structure of a beta-TrCP1-Skp1-beta-catenin complex: destruction motif binding and lysine specificity of the SCF(beta-TrCP1) ubiquitin ligase. Mol. Cell 11 (2003) 1445-1456
    • (2003) Mol. Cell , vol.11 , pp. 1445-1456
    • Wu, G.1    Xu, G.2    Schulman, B.A.3    Jeffrey, P.D.4    Harper, J.W.5    Pavletich, N.P.6
  • 58
    • 12344307150 scopus 로고    scopus 로고
    • Nucleosomal structure of undamaged DNA regions suppresses the non-specific DNA binding of the XPC complex
    • Yasuda T., Sugasawa K., Shimizu Y., Iwai S., Shiomi T., and Hanaoka F. Nucleosomal structure of undamaged DNA regions suppresses the non-specific DNA binding of the XPC complex. DNA Repair (Amst.) 4 (2005) 389-395
    • (2005) DNA Repair (Amst.) , vol.4 , pp. 389-395
    • Yasuda, T.1    Sugasawa, K.2    Shimizu, Y.3    Iwai, S.4    Shiomi, T.5    Hanaoka, F.6
  • 59
    • 34748912887 scopus 로고    scopus 로고
    • In vivo destabilization and functional defects of the xeroderma pigmentosum C protein caused by a pathogenic missense mutation
    • Yasuda G., Nishi R., Watanabe E., Mori T., Iwai S., Orioli D., Stefanini M., Hanaoka F., and Sugasawa K. In vivo destabilization and functional defects of the xeroderma pigmentosum C protein caused by a pathogenic missense mutation. Mol. Cell. Biol. 27 (2007) 6606-6614
    • (2007) Mol. Cell. Biol. , vol.27 , pp. 6606-6614
    • Yasuda, G.1    Nishi, R.2    Watanabe, E.3    Mori, T.4    Iwai, S.5    Orioli, D.6    Stefanini, M.7    Hanaoka, F.8    Sugasawa, K.9


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.