메뉴 건너뛰기




Volumn 12, Issue 9, 2014, Pages

In TFIIH, XPD Helicase Is Exclusively Devoted to DNA Repair

Author keywords

[No Author keywords available]

Indexed keywords

ADENOSINE TRIPHOSPHATASE; HELICASE; PROTEIN P44; SINGLE STRANDED DNA; TRANSCRIPTION FACTOR IIH; UNCLASSIFIED DRUG; XERODERMA PIGMENTOSUM COMPLEMENTATION GROUP D HELICASE; DNA; ERCC2 PROTEIN, HUMAN; FUNGAL PROTEIN; LUCIFERASE; P44 PROTEIN, HUMAN; PROTEIN BINDING; RECOMBINANT PROTEIN; TRANSCRIPTION FACTOR; XERODERMA PIGMENTOSUM GROUP D PROTEIN;

EID: 84920492375     PISSN: 15449173     EISSN: 15457885     Source Type: Journal    
DOI: 10.1371/journal.pbio.1001954     Document Type: Article
Times cited : (71)

References (50)
  • 1
    • 0035176067 scopus 로고    scopus 로고
    • The xeroderma pigmentosum group D (XPD) gene: one gene, two functions, three diseases
    • Lehmann AR, (2001) The xeroderma pigmentosum group D (XPD) gene: one gene, two functions, three diseases. Genes Dev 15: 15–23.
    • (2001) Genes Dev , vol.15 , pp. 15-23
    • Lehmann, A.R.1
  • 2
    • 0027364921 scopus 로고
    • Human xeroderma pigmentosum group D gene encodes a DNA helicase
    • Sung P, Bailly V, Weber C, Thompson LH, Prakash L, et al. (1993) Human xeroderma pigmentosum group D gene encodes a DNA helicase. Nature 365: 852–855 doi:10.1038/365852a0
    • (1993) Nature , vol.365 , pp. 852-855
    • Sung, P.1    Bailly, V.2    Weber, C.3    Thompson, L.H.4    Prakash, L.5
  • 3
    • 45849119445 scopus 로고    scopus 로고
    • Crystal structure of the FeS cluster-containing nucleotide excision repair helicase XPD
    • Wolski SC, Kuper J, Hänzelmann P, Truglio JJ, Croteau DL, et al. (2008) Crystal structure of the FeS cluster-containing nucleotide excision repair helicase XPD. PLoS Biol 6: e149 doi:10.1371/journal.pbio.0060149
    • (2008) PLoS Biol , vol.6 , pp. e149
    • Wolski, S.C.1    Kuper, J.2    Hänzelmann, P.3    Truglio, J.J.4    Croteau, D.L.5
  • 4
    • 33748428875 scopus 로고    scopus 로고
    • The DNA repair helicases XPD and FancJ have essential iron-sulfur domains
    • Rudolf J, Makrantoni V, Ingledew WJ, Stark MJR, White MF, (2006) The DNA repair helicases XPD and FancJ have essential iron-sulfur domains. Mol Cell 23: 801–808 doi:10.1016/j.molcel.2006.07.019
    • (2006) Mol Cell , vol.23 , pp. 801-808
    • Rudolf, J.1    Makrantoni, V.2    Ingledew, W.J.3    Stark, M.J.R.4    White, M.F.5
  • 5
    • 44149094083 scopus 로고    scopus 로고
    • XPD helicase structures and activities: insights into the cancer and aging phenotypes from XPD mutations
    • Fan L, Fuss JO, Cheng QJ, Arvai AS, Hammel M, et al. (2008) XPD helicase structures and activities: insights into the cancer and aging phenotypes from XPD mutations. Cell 133: 789–800 doi:10.1016/j.cell.2008.04.030
    • (2008) Cell , vol.133 , pp. 789-800
    • Fan, L.1    Fuss, J.O.2    Cheng, Q.J.3    Arvai, A.S.4    Hammel, M.5
  • 6
    • 43949110271 scopus 로고    scopus 로고
    • Structure of the DNA repair helicase XPD
    • Liu H, Rudolf J, Johnson KA, McMahon SA, Oke M, et al. (2008) Structure of the DNA repair helicase XPD. Cell 133: 801–812 doi:10.1016/j.cell.2008.04.029
    • (2008) Cell , vol.133 , pp. 801-812
    • Liu, H.1    Rudolf, J.2    Johnson, K.A.3    McMahon, S.A.4    Oke, M.5
  • 7
    • 0028362248 scopus 로고
    • The ERCC2/DNA repair protein is associated with the class II BTF2/TFIIH transcription factor
    • Schaeffer L, Moncollin V, Roy R, Staub A, Mezzina M, et al. (1994) The ERCC2/DNA repair protein is associated with the class II BTF2/TFIIH transcription factor. EMBO J 13: 2388–2392.
    • (1994) EMBO J , vol.13 , pp. 2388-2392
    • Schaeffer, L.1    Moncollin, V.2    Roy, R.3    Staub, A.4    Mezzina, M.5
  • 8
    • 84861457511 scopus 로고    scopus 로고
    • TFIIH: when transcription met DNA repair
    • Compe E, Egly J-M, (2012) TFIIH: when transcription met DNA repair. Nat Rev Mol Cell Biol 13: 343–354 doi:10.1038/nrm3350
    • (2012) Nat Rev Mol Cell Biol , vol.13 , pp. 343-354
    • Compe, E.1    Egly, J.-M.2
  • 9
    • 0033104514 scopus 로고    scopus 로고
    • Mutations in XPB and XPD helicases found in xeroderma pigmentosum patients impair the transcription function of TFIIH
    • Coin F, Bergmann E, Tremeau-Bravard A, Egly JM, (1999) Mutations in XPB and XPD helicases found in xeroderma pigmentosum patients impair the transcription function of TFIIH. EMBO J 18: 1357–1366 doi:10.1093/emboj/18.5.1357
    • (1999) EMBO J , vol.18 , pp. 1357-1366
    • Coin, F.1    Bergmann, E.2    Tremeau-Bravard, A.3    Egly, J.M.4
  • 10
    • 34247513888 scopus 로고    scopus 로고
    • Distinct roles for the XPB/p52 and XPD/p44 subcomplexes of TFIIH in damaged DNA opening during nucleotide excision repair
    • Coin F, Oksenych V, Egly J-M, (2007) Distinct roles for the XPB/p52 and XPD/p44 subcomplexes of TFIIH in damaged DNA opening during nucleotide excision repair. Mol Cell 26: 245–256 doi:10.1016/j.molcel.2007.03.009
    • (2007) Mol Cell , vol.26 , pp. 245-256
    • Coin, F.1    Oksenych, V.2    Egly, J.-M.3
  • 11
    • 0026052701 scopus 로고
    • Purification and characterization of yeast RNA polymerase II transcription factor b
    • Feaver WJ, Gileadi O, Kornberg RD, (1991) Purification and characterization of yeast RNA polymerase II transcription factor b. J Biol Chem 266: 19000–19005.
    • (1991) J Biol Chem , vol.266 , pp. 19000-19005
    • Feaver, W.J.1    Gileadi, O.2    Kornberg, R.D.3
  • 12
    • 0025787782 scopus 로고
    • Purification and interaction properties of the human RNA polymerase B(II) general transcription factor BTF2
    • Gerard M, Fischer L, Moncollin V, Chipoulet JM, Chambon P, et al. (1991) Purification and interaction properties of the human RNA polymerase B(II) general transcription factor BTF2. J Biol Chem 266: 20940–20945.
    • (1991) J Biol Chem , vol.266 , pp. 20940-20945
    • Gerard, M.1    Fischer, L.2    Moncollin, V.3    Chipoulet, J.M.4    Chambon, P.5
  • 13
    • 0000402041 scopus 로고
    • An RNA polymerase II transcription factor has an associated DNA-dependent ATPase (dATPase) activity strongly stimulated by the TATA region of promoters
    • Conaway RC, Conaway JW, (1989) An RNA polymerase II transcription factor has an associated DNA-dependent ATPase (dATPase) activity strongly stimulated by the TATA region of promoters. Proc Natl Acad Sci USA 86: 7356–7360.
    • (1989) Proc Natl Acad Sci USA , vol.86 , pp. 7356-7360
    • Conaway, R.C.1    Conaway, J.W.2
  • 14
    • 79960377780 scopus 로고    scopus 로고
    • A history of TFIIH: two decades of molecular biology on a pivotal transcription/repair factor
    • Egly J-M, Coin F, (2011) A history of TFIIH: two decades of molecular biology on a pivotal transcription/repair factor. DNA Repair (Amst) 10: 714–721 doi:10.1016/j.dnarep.2011.04.021
    • (2011) DNA Repair (Amst) , vol.10 , pp. 714-721
    • Egly, J.-M.1    Coin, F.2
  • 15
    • 0035313754 scopus 로고    scopus 로고
    • Mechanism of transcription initiation and promoter escape by RNA polymerase II
    • Dvir A, Conaway JW, Conaway RC, (2001) Mechanism of transcription initiation and promoter escape by RNA polymerase II. Curr Opin Genet Dev 11: 209–214.
    • (2001) Curr Opin Genet Dev , vol.11 , pp. 209-214
    • Dvir, A.1    Conaway, J.W.2    Conaway, R.C.3
  • 16
    • 0033781448 scopus 로고    scopus 로고
    • Mechanism of promoter melting by the xeroderma pigmentosum complementation group B helicase of transcription factor IIH revealed by protein-DNA photo-cross-linking
    • Douziech M, Coin F, Chipoulet JM, Arai Y, Ohkuma Y, et al. (2000) Mechanism of promoter melting by the xeroderma pigmentosum complementation group B helicase of transcription factor IIH revealed by protein-DNA photo-cross-linking. Mol Cell Biol 20: 8168–8177.
    • (2000) Mol Cell Biol , vol.20 , pp. 8168-8177
    • Douziech, M.1    Coin, F.2    Chipoulet, J.M.3    Arai, Y.4    Ohkuma, Y.5
  • 17
    • 0029812863 scopus 로고    scopus 로고
    • Promoter escape by RNA polymerase II. A role for an ATP cofactor in suppression of arrest by polymerase at promoter-proximal sites
    • Dvir A, Conaway RC, Conaway JW, (1996) Promoter escape by RNA polymerase II. A role for an ATP cofactor in suppression of arrest by polymerase at promoter-proximal sites. J Biol Chem 271: 23352–23356.
    • (1996) J Biol Chem , vol.271 , pp. 23352-23356
    • Dvir, A.1    Conaway, R.C.2    Conaway, J.W.3
  • 18
    • 0033529635 scopus 로고    scopus 로고
    • A role for the TFIIH XPB DNA helicase in promoter escape by RNA polymerase II
    • Moreland RJ, Tirode F, Yan Q, Conaway JW, Egly JM, et al. (1999) A role for the TFIIH XPB DNA helicase in promoter escape by RNA polymerase II. J Biol Chem 274: 22127–22130.
    • (1999) J Biol Chem , vol.274 , pp. 22127-22130
    • Moreland, R.J.1    Tirode, F.2    Yan, Q.3    Conaway, J.W.4    Egly, J.M.5
  • 19
    • 70350566800 scopus 로고    scopus 로고
    • Molecular insights into the recruitment of TFIIH to sites of DNA damage
    • Oksenych V, de Jesus BB, Zhovmer A, Egly J-M, Coin F, (2009) Molecular insights into the recruitment of TFIIH to sites of DNA damage. EMBO J 28: 2971–2980 doi:10.1038/emboj.2009.230
    • (2009) EMBO J , vol.28 , pp. 2971-2980
    • Oksenych, V.1    de Jesus, B.B.2    Zhovmer, A.3    Egly, J.-M.4    Coin, F.5
  • 20
    • 0027973206 scopus 로고
    • DNA repair. Incisions for excision
    • Hoeijmakers JH, Bootsma D, (1994) DNA repair. Incisions for excision. Nature 371: 654–655 doi:10.1038/371654a0
    • (1994) Nature , vol.371 , pp. 654-655
    • Hoeijmakers, J.H.1    Bootsma, D.2
  • 21
    • 38149019888 scopus 로고    scopus 로고
    • A molecular basis for damage recognition in eukaryotic nucleotide excision repair
    • Schärer OD, (2008) A molecular basis for damage recognition in eukaryotic nucleotide excision repair. Chembiochem 9: 21–23 doi:10.1002/cbic.200700619
    • (2008) Chembiochem , vol.9 , pp. 21-23
    • Schärer, O.D.1
  • 22
    • 0027905008 scopus 로고
    • DNA repair helicase: a component of BTF2 (TFIIH) basic transcription factor
    • Schaeffer L, Roy R, Humbert S, Moncollin V, Vermeulen W, et al. (1993) DNA repair helicase: a component of BTF2 (TFIIH) basic transcription factor. Science 260: 58–63.
    • (1993) Science , vol.260 , pp. 58-63
    • Schaeffer, L.1    Roy, R.2    Humbert, S.3    Moncollin, V.4    Vermeulen, W.5
  • 23
    • 0031666241 scopus 로고    scopus 로고
    • Mutations in the XPD helicase gene result in XP and TTD phenotypes, preventing interaction between XPD and the p44 subunit of TFIIH
    • Coin F, Marinoni JC, Rodolfo C, Fribourg S, Pedrini AM, et al. (1998) Mutations in the XPD helicase gene result in XP and TTD phenotypes, preventing interaction between XPD and the p44 subunit of TFIIH. Nat Genet 20: 184–188 doi:10.1038/2491
    • (1998) Nat Genet , vol.20 , pp. 184-188
    • Coin, F.1    Marinoni, J.C.2    Rodolfo, C.3    Fribourg, S.4    Pedrini, A.M.5
  • 24
    • 0028606403 scopus 로고
    • Mechanisms of DNA excision repair
    • Sancar A, (1994) Mechanisms of DNA excision repair. Science 266: 1954–1956.
    • (1994) Science , vol.266 , pp. 1954-1956
    • Sancar, A.1
  • 25
    • 0033010723 scopus 로고    scopus 로고
    • Reconstitution of the transcription factor TFIIH: assignment of functions for the three enzymatic subunits, XPB, XPD, and cdk7
    • Tirode F, Busso D, Coin F, Egly JM, (1999) Reconstitution of the transcription factor TFIIH: assignment of functions for the three enzymatic subunits, XPB, XPD, and cdk7. Mol Cell 3: 87–95.
    • (1999) Mol Cell , vol.3 , pp. 87-95
    • Tirode, F.1    Busso, D.2    Coin, F.3    Egly, J.M.4
  • 26
    • 0038094503 scopus 로고    scopus 로고
    • Basal transcription defect discriminates between xeroderma pigmentosum and trichothiodystrophy in XPD patients
    • Dubaele S, Proietti De Santis L, Bienstock RJ, et al. (2003) Basal transcription defect discriminates between xeroderma pigmentosum and trichothiodystrophy in XPD patients. Mol Cell 11: 1635–1646.
    • (2003) Mol Cell , vol.11 , pp. 1635-1646
    • Dubaele, S.1    Proietti De Santis, L.2    Bienstock, R.J.3
  • 27
    • 70449717367 scopus 로고    scopus 로고
    • Two-step recognition of DNA damage for mammalian nucleotide excision repair: directional binding of the XPC complex and DNA strand scanning
    • Sugasawa K, Akagi J-I, Nishi R, Iwai S, Hanaoka F, (2009) Two-step recognition of DNA damage for mammalian nucleotide excision repair: directional binding of the XPC complex and DNA strand scanning. Mol Cell 36: 642–653 doi:10.1016/j.molcel.2009.09.035
    • (2009) Mol Cell , vol.36 , pp. 642-653
    • Sugasawa, K.1    Akagi, J.-I.2    Nishi, R.3    Iwai, S.4    Hanaoka, F.5
  • 28
    • 0035929594 scopus 로고    scopus 로고
    • A yeast four-hybrid system identifies Cdk-activating kinase as a regulator of the XPD helicase, a subunit of transcription factor IIH
    • Sandrock B, Egly JM, (2001) A yeast four-hybrid system identifies Cdk-activating kinase as a regulator of the XPD helicase, a subunit of transcription factor IIH. J Biol Chem 276: 35328–35333 doi:10.1074/jbc.M105570200
    • (2001) J Biol Chem , vol.276 , pp. 35328-35333
    • Sandrock, B.1    Egly, J.M.2
  • 29
    • 75749154031 scopus 로고    scopus 로고
    • Dynamic two-stage mechanism of versatile DNA damage recognition by xeroderma pigmentosum group C protein
    • Clement FC, Camenisch U, Fei J, Kaczmarek N, Mathieu N, et al. (2010) Dynamic two-stage mechanism of versatile DNA damage recognition by xeroderma pigmentosum group C protein. Mutat Res 685: 21–28 doi:10.1016/j.mrfmmm.2009.08.005
    • (2010) Mutat Res , vol.685 , pp. 21-28
    • Clement, F.C.1    Camenisch, U.2    Fei, J.3    Kaczmarek, N.4    Mathieu, N.5
  • 30
    • 3042784988 scopus 로고    scopus 로고
    • Xpd, a structural bridge and a functional link
    • Chen J, Suter B, (2003) Xpd, a structural bridge and a functional link. Cell Cycle 2: 503–506.
    • (2003) Cell Cycle , vol.2 , pp. 503-506
    • Chen, J.1    Suter, B.2
  • 31
    • 35549000640 scopus 로고    scopus 로고
    • Neurological defects in trichothiodystrophy reveal a coactivator function of TFIIH
    • Compe E, Malerba M, Soler L, Marescaux J, Borrelli E, et al. (2007) Neurological defects in trichothiodystrophy reveal a coactivator function of TFIIH. Nat Neurosci 10: 1414–1422 doi:10.1038/nn1990
    • (2007) Nat Neurosci , vol.10 , pp. 1414-1422
    • Compe, E.1    Malerba, M.2    Soler, L.3    Marescaux, J.4    Borrelli, E.5
  • 32
    • 84874257935 scopus 로고    scopus 로고
    • ARCH domain of XPD, an anchoring platform for CAK that conditions TFIIH DNA repair and transcription activities
    • Abdulrahman W, Iltis I, Radu L, Braun C, Maglott-Roth A, et al. (2013) ARCH domain of XPD, an anchoring platform for CAK that conditions TFIIH DNA repair and transcription activities. Proc Natl Acad Sci U S A 110 (8) E633–E642 doi:10.1073/pnas.1213981110
    • (2013) Proc Natl Acad Sci U S A , vol.110 , Issue.8 , pp. E633-E642
    • Abdulrahman, W.1    Iltis, I.2    Radu, L.3    Braun, C.4    Maglott-Roth, A.5
  • 33
    • 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
    • Araújo SJ, Tirode F, Coin F, Pospiech H, Syväoja JE, et al. (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
    • Araújo, S.J.1    Tirode, F.2    Coin, F.3    Pospiech, H.4    Syväoja, J.E.5
  • 34
    • 0028140494 scopus 로고
    • DNA repair gene RAD3 of S. cerevisiae is essential for transcription by RNA polymerase II
    • Guzder SN, Qiu H, Sommers CH, Sung P, Prakash L, et al. (1994) DNA repair gene RAD3 of S. cerevisiae is essential for transcription by RNA polymerase II. Nature 367: 91–94 doi:10.1038/367091a0
    • (1994) Nature , vol.367 , pp. 91-94
    • Guzder, S.N.1    Qiu, H.2    Sommers, C.H.3    Sung, P.4    Prakash, L.5
  • 35
    • 0033544966 scopus 로고    scopus 로고
    • Dual roles for transcription factor IIF in promoter escape by RNA polymerase II
    • Yan Q, Moreland RJ, Conaway JW, Conaway RC, (1999) Dual roles for transcription factor IIF in promoter escape by RNA polymerase II. J Biol Chem 274: 35668–35675.
    • (1999) J Biol Chem , vol.274 , pp. 35668-35675
    • Yan, Q.1    Moreland, R.J.2    Conaway, J.W.3    Conaway, R.C.4
  • 36
    • 79960766105 scopus 로고    scopus 로고
    • Insight into structure and assembly of the nuclear pore complex by utilizing the genome of a eukaryotic thermophile
    • Amlacher S, Sarges P, Flemming D, van Noort V, Kunze R, et al. (2011) Insight into structure and assembly of the nuclear pore complex by utilizing the genome of a eukaryotic thermophile. Cell 146: 277–289 doi:10.1016/j.cell.2011.06.039
    • (2011) Cell , vol.146 , pp. 277-289
    • Amlacher, S.1    Sarges, P.2    Flemming, D.3    van Noort, V.4    Kunze, R.5
  • 37
    • 84857195289 scopus 로고    scopus 로고
    • Functional and structural studies of the nucleotide excision repair helicase XPD suggest a polarity for DNA translocation
    • Kuper J, Wolski SC, Michels G, Kisker C, (2012) Functional and structural studies of the nucleotide excision repair helicase XPD suggest a polarity for DNA translocation. EMBO J 31 (2) 494–502 doi:10.1038/emboj.2011.374
    • (2012) EMBO J , vol.31 , Issue.2 , pp. 494-502
    • Kuper, J.1    Wolski, S.C.2    Michels, G.3    Kisker, C.4
  • 38
    • 84857194573 scopus 로고    scopus 로고
    • Regulation of translocation polarity by helicase domain 1 in SF2B helicases
    • Pugh RA, Wu CG, Spies M, (2012) Regulation of translocation polarity by helicase domain 1 in SF2B helicases. EMBO J 31: 503–514 doi:10.1038/emboj.2011.412
    • (2012) EMBO J , vol.31 , pp. 503-514
    • Pugh, R.A.1    Wu, C.G.2    Spies, M.3
  • 39
    • 34548638261 scopus 로고    scopus 로고
    • Structure and mechanism of helicases and nucleic acid translocases
    • Singleton MR, Dillingham MS, Wigley DB, (2007) Structure and mechanism of helicases and nucleic acid translocases. Annu Rev Biochem 76: 23–50 doi:10.1146/annurev.biochem.76.052305.115300
    • (2007) Annu Rev Biochem , vol.76 , pp. 23-50
    • Singleton, M.R.1    Dillingham, M.S.2    Wigley, D.B.3
  • 40
    • 0022273627 scopus 로고
    • Xeroderma pigmentosum D-HeLa hybrids with low and high ultraviolet sensitivity associated with normal and diminished DNA repair ability, respectively
    • Johnson RT, Squires S, Elliott GC, Koch GL, Rainbow AJ, (1985) Xeroderma pigmentosum D-HeLa hybrids with low and high ultraviolet sensitivity associated with normal and diminished DNA repair ability, respectively. J Cell Sci 76: 115–133.
    • (1985) J Cell Sci , vol.76 , pp. 115-133
    • Johnson, R.T.1    Squires, S.2    Elliott, G.C.3    Koch, G.L.4    Rainbow, A.J.5
  • 41
    • 0029095126 scopus 로고
    • Requirement for TFIIH kinase activity in transcription by RNA polymerase II
    • Akoulitchev S, Mäkelä TP, Weinberg RA, Reinberg D, (1995) Requirement for TFIIH kinase activity in transcription by RNA polymerase II. Nature 377: 557–560 doi:10.1038/377557a0
    • (1995) Nature , vol.377 , pp. 557-560
    • Akoulitchev, S.1    Mäkelä, T.P.2    Weinberg, R.A.3    Reinberg, D.4
  • 42
    • 0030667826 scopus 로고    scopus 로고
    • Promoter escape by RNA polymerase II. Formation of an escape-competent transcriptional intermediate is a prerequisite for exit of polymerase from the promoter
    • Dvir A, Tan S, Conaway JW, Conaway RC, (1997) Promoter escape by RNA polymerase II. Formation of an escape-competent transcriptional intermediate is a prerequisite for exit of polymerase from the promoter. J Biol Chem 272: 28175–28178.
    • (1997) J Biol Chem , vol.272 , pp. 28175-28178
    • Dvir, A.1    Tan, S.2    Conaway, J.W.3    Conaway, R.C.4
  • 43
    • 0030740233 scopus 로고    scopus 로고
    • A role for TFIIH in controlling the activity of early RNA polymerase II elongation complexes
    • Dvir A, Conaway RC, Conaway JW, (1997) A role for TFIIH in controlling the activity of early RNA polymerase II elongation complexes. Proc Natl Acad Sci USA 94: 9006–9010.
    • (1997) Proc Natl Acad Sci USA , vol.94 , pp. 9006-9010
    • Dvir, A.1    Conaway, R.C.2    Conaway, J.W.3
  • 44
    • 84873408109 scopus 로고    scopus 로고
    • DNA quality control by a lesion sensor pocket of the xeroderma pigmentosum group D helicase subunit of TFIIH
    • Mathieu N, Kaczmarek N, Rüthemann P, Luch A, Naegeli H, (2013) DNA quality control by a lesion sensor pocket of the xeroderma pigmentosum group D helicase subunit of TFIIH. Curr Biol 23: 204–212 doi:10.1016/j.cub.2012.12.032
    • (2013) Curr Biol , vol.23 , pp. 204-212
    • Mathieu, N.1    Kaczmarek, N.2    Rüthemann, P.3    Luch, A.4    Naegeli, H.5
  • 45
    • 84875613843 scopus 로고    scopus 로고
    • Structural visualization of key steps in human transcription initiation
    • He Y, Fang J, Taatjes DJ, Nogales E, (2013) Structural visualization of key steps in human transcription initiation. Nature 495: 481–486 doi:10.1038/nature11991
    • (2013) Nature , vol.495 , pp. 481-486
    • He, Y.1    Fang, J.2    Taatjes, D.J.3    Nogales, E.4
  • 46
    • 84884516365 scopus 로고    scopus 로고
    • Architecture of an RNA polymerase II transcription pre-initiation complex
    • Murakami K, Elmlund H, Kalisman N, Bushnell DA, Adams CM, et al. (2013) Architecture of an RNA polymerase II transcription pre-initiation complex. Science 342: 1238724 doi:10.1126/science.1238724
    • (2013) Science , vol.342 , pp. 1238724
    • Murakami, K.1    Elmlund, H.2    Kalisman, N.3    Bushnell, D.A.4    Adams, C.M.5
  • 47
    • 80054726392 scopus 로고    scopus 로고
    • ATP-stimulated, DNA-mediated redox signaling by XPD, a DNA repair and transcription helicase
    • Mui TP, Fuss JO, Ishida JP, Tainer JA, Barton JK, et al. (2011) ATP-stimulated, DNA-mediated redox signaling by XPD, a DNA repair and transcription helicase. J Am Chem Soc 133: 16378–16381 doi:10.1021/ja207222t
    • (2011) J Am Chem Soc , vol.133 , pp. 16378-16381
    • Mui, T.P.1    Fuss, J.O.2    Ishida, J.P.3    Tainer, J.A.4    Barton, J.K.5
  • 48
    • 84857127226 scopus 로고    scopus 로고
    • DNA charge transport as a first step in coordinating the detection of lesions by repair proteins
    • Sontz PA, Mui TP, Fuss JO, Tainer JA, Barton JK, (2012) DNA charge transport as a first step in coordinating the detection of lesions by repair proteins. Proc Natl Acad Sci U S A 109: 1856–1861 doi:10.1073/pnas.1120063109
    • (2012) Proc Natl Acad Sci U S A , vol.109 , pp. 1856-1861
    • Sontz, P.A.1    Mui, T.P.2    Fuss, J.O.3    Tainer, J.A.4    Barton, J.K.5
  • 49
    • 58149394844 scopus 로고    scopus 로고
    • A set of baculovirus transfer vectors for screening of affinity tags and parallel expression strategies
    • Abdulrahman W, Uhring M, Kolb-Cheynel I, Garnier JM, Moras D, et al. (2009) A set of baculovirus transfer vectors for screening of affinity tags and parallel expression strategies. Anal Biochem 385: 383–385 doi:10.1016/j.ab.2008.10.044
    • (2009) Anal Biochem , vol.385 , pp. 383-385
    • Abdulrahman, W.1    Uhring, M.2    Kolb-Cheynel, I.3    Garnier, J.M.4    Moras, D.5
  • 50
    • 33645988522 scopus 로고    scopus 로고
    • Conserved XPB core structure and motifs for DNA unwinding: implications for pathway selection of transcription or excision repair
    • Fan L, Arvai AS, Cooper PK, Iwai S, Hanaoka F, et al. (2006) Conserved XPB core structure and motifs for DNA unwinding: implications for pathway selection of transcription or excision repair. Mol Cell 22: 27–37 doi:10.1016/j.molcel.2006.02.017
    • (2006) Mol Cell , vol.22 , pp. 27-37
    • Fan, L.1    Arvai, A.S.2    Cooper, P.K.3    Iwai, S.4    Hanaoka, F.5


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.