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Volumn 9, Issue 12, 2010, Pages 2317-2329

Mechanistic and biological aspects of helicase action on damaged DNA

Author keywords

DNA damage; DNA repair; FANCJ; Fanconi anemia; Helicase; Nucleotide excision repair; Replication; Replication protein A; Werner syndrome; Xeroderma pigmentosum

Indexed keywords

ADENOSINE TRIPHOSPHATASE; DNA BASE; HELICASE; NUCLEIC ACID; POLYCYCLIC AROMATIC HYDROCARBON; PYRIMIDINE DIMER; REPLICATION FACTOR A; SUGAR PHOSPHATE; XERODERMA PIGMENTOSUM GROUP D PROTEIN;

EID: 77954146394     PISSN: 15384101     EISSN: 15514005     Source Type: Journal    
DOI: 10.4161/cc.9.12.11902     Document Type: Review
Times cited : (20)

References (112)
  • 1
    • 42449141601 scopus 로고    scopus 로고
    • Non-hexameric DNA helicases and translocases: Mechanisms and regulation
    • Lohman TM, Tomko EJ, Wu CG. Non-hexameric DNA helicases and translocases: mechanisms and regulation. Nat Rev Mol Cell Biol 2008; 9:391-401.
    • (2008) Nat Rev Mol Cell Biol , vol.9 , pp. 391-401
    • Lohman, T.M.1    Tomko, E.J.2    Wu, C.G.3
  • 2
    • 33745823112 scopus 로고    scopus 로고
    • Mechanisms of helicases
    • Patel SS, Donmez I. Mechanisms of helicases. J Biol Chem 2006; 281:18625-8.
    • (2006) J Biol Chem , vol.281 , pp. 18625-18628
    • Patel, S.S.1    Donmez, I.2
  • 3
    • 48249113056 scopus 로고    scopus 로고
    • Translocation and unwinding mechanisms of RNA and DNA helicases
    • Pyle AM. Translocation and unwinding mechanisms of RNA and DNA helicases. Annu Rev Biophys 2008; 37:317-36.
    • (2008) Annu Rev Biophys , vol.37 , pp. 317-336
    • Pyle, A.M.1
  • 4
    • 34548638261 scopus 로고    scopus 로고
    • Structure and mechanism of helicases and nucleic acid translocases
    • Singleton MR, Dillingham MS, Wigley DB. Structure and mechanism of helicases and nucleic acid translocases. Annu Rev Biochem 2007; 76:23-50.
    • (2007) Annu Rev Biochem , vol.76 , pp. 23-50
    • Singleton, M.R.1    Dillingham, M.S.2    Wigley, D.B.3
  • 5
    • 27544445683 scopus 로고    scopus 로고
    • The DNA damage response during DNA replication 1
    • Branzei D, Foiani M. The DNA damage response during DNA replication 1. Curr Opin Cell Biol 2005; 17:568-75.
    • (2005) Curr Opin Cell Biol , vol.17 , pp. 568-575
    • Branzei, D.1    Foiani, M.2
  • 6
    • 0032738023 scopus 로고    scopus 로고
    • Effect of DNA lesions on transcription elongation
    • Tornaletti S, Hanawalt PC. Effect of DNA lesions on transcription elongation. Biochimie 1999; 81:139-46.
    • (1999) Biochimie , vol.81 , pp. 139-146
    • Tornaletti, S.1    Hanawalt, P.C.2
  • 7
    • 62349130094 scopus 로고    scopus 로고
    • DNA repair in mammalian cells: Transcription-coupled DNA repair: directing your effort where it's most needed
    • Tornaletti S. DNA repair in mammalian cells: Transcription-coupled DNA repair: directing your effort where it's most needed. Cell Mol Life Sci 2009; 66:1010-20.
    • (2009) Cell Mol Life Sci , vol.66 , pp. 1010-1020
    • Tornaletti, S.1
  • 8
    • 0036628726 scopus 로고    scopus 로고
    • Biological consequences of free radicaldamaged DNA bases
    • Wallace SS. Biological consequences of free radicaldamaged DNA bases. Free Radic Biol Med 2002; 33:1-14.
    • (2002) Free Radic Biol Med , vol.33 , pp. 1-14
    • Wallace, S.S.1
  • 9
    • 33646768613 scopus 로고    scopus 로고
    • Poor base stacking at DNA lesions may initiate recognition by many repair proteins
    • Amst
    • Yang W. Poor base stacking at DNA lesions may initiate recognition by many repair proteins. DNA Repair (Amst) 2006; 5:654-66.
    • (2006) DNA Repair , vol.5 , pp. 654-666
    • Yang, W.1
  • 11
    • 33644619706 scopus 로고    scopus 로고
    • Prokaryotic nucleotide excision repair: The UvrABC system
    • Truglio JJ, Croteau DL, Van Houten B, Kisker C. Prokaryotic nucleotide excision repair: the UvrABC system. Chem Rev 2006; 106:233-52.
    • (2006) Chem Rev , vol.106 , pp. 233-252
    • Truglio, J.J.1    Croteau, D.L.2    Van Houten, B.3    Kisker, C.4
  • 12
    • 24044438506 scopus 로고    scopus 로고
    • 'Close-fitting sleeves': DNA damage recognition by the UvrABC nuclease system
    • Van Houten B, Croteau DL, DellaVecchia MJ, Wang H, Kisker C. 'Close-fitting sleeves': DNA damage recognition by the UvrABC nuclease system. Mutat Res 2005; 577:92-117.
    • (2005) Mutat Res , vol.577 , pp. 92-117
    • Van Houten, B.1    Croteau, D.L.2    Dellavecchia, M.J.3    Wang, H.4    Kisker, C.5
  • 13
    • 69149100489 scopus 로고    scopus 로고
    • DNA wrapping is required for DNA damage recognition in the Escherichia coli DNA nucleotide excision repair pathway
    • Wang H, Lu M, Tang MS, Van Houten B, Ross JB, Weinfeld M, et al. DNA wrapping is required for DNA damage recognition in the Escherichia coli DNA nucleotide excision repair pathway. Proc Natl Acad Sci USA 2009; 106:12849-54.
    • (2009) Proc Natl Acad Sci USA , vol.106 , pp. 12849-12854
    • Wang, H.1    Lu, M.2    Tang, M.S.3    Van Houten, B.4    Ross, J.B.5    Weinfeld, M.6
  • 14
    • 0035503314 scopus 로고    scopus 로고
    • Clue to damage recognition by UvrB: Residues in the beta-hairpin structure prevent binding to non-damaged DNA
    • Moolenaar GF, Hoglund L, Goosen N. Clue to damage recognition by UvrB: residues in the beta-hairpin structure prevent binding to non-damaged DNA. EMBO J 2001; 20:6140-9.
    • (2001) EMBO J , vol.20 , pp. 6140-6149
    • Moolenaar, G.F.1    Hoglund, L.2    Goosen, N.3
  • 16
    • 33750970284 scopus 로고    scopus 로고
    • Damage detection by the UvrABC pathway: Crystal structure of UvrB bound to fluorescein-adducted DNA
    • Waters TR, Eryilmaz J, Geddes S, Barrett TE. Damage detection by the UvrABC pathway: crystal structure of UvrB bound to fluorescein-adducted DNA. FEBS Lett 2006; 580:6423-7.
    • (2006) FEBS Lett , vol.580 , pp. 6423-6427
    • Waters, T.R.1    Eryilmaz, J.2    Geddes, S.3    Barrett, T.E.4
  • 17
    • 33644855067 scopus 로고    scopus 로고
    • Base flipping in nucleotide excision repair
    • Malta E, Moolenaar GF, Goosen N. Base flipping in nucleotide excision repair. J Biol Chem 2006; 281:2184-94.
    • (2006) J Biol Chem , vol.281 , pp. 2184-2194
    • Malta, E.1    Moolenaar, G.F.2    Goosen, N.3
  • 19
    • 70349774465 scopus 로고    scopus 로고
    • Exploring damage recognition models in prokaryotic nucleotide excision repair with a benzo[a]pyrene-derived lesion in UvrB
    • Jia L, Kropachev K, Ding S, Van Houten B, Geacintov NE, Broyde S. Exploring damage recognition models in prokaryotic nucleotide excision repair with a benzo[a]pyrene-derived lesion in UvrB. Biochemistry 2009; 48:8948-57.
    • (2009) Biochemistry , vol.48 , pp. 8948-8957
    • Jia, L.1    Kropachev, K.2    Ding, S.3    Van Houten, B.4    Geacintov, N.E.5    Broyde, S.6
  • 20
    • 0034721831 scopus 로고    scopus 로고
    • Interactions of DNA helicases with damaged DNA: Possible biological consequences
    • Villani G, Tanguy LG. Interactions of DNA helicases with damaged DNA: possible biological consequences. J Biol Chem 2000; 275:33185-8.
    • (2000) J Biol Chem , vol.275 , pp. 33185-33188
    • Villani, G.1    Tanguy, L.G.2
  • 21
    • 0028110817 scopus 로고
    • Effect of the major DNA adduct of the antitumor drug cis- Diamminedichloroplatinum (II) on the activity of a helicase essential for DNA replication, the herpes simplex virus type-1 origin-binding protein
    • Villani G, Pillaire MJ, Boehmer PE. Effect of the major DNA adduct of the antitumor drug cisdiamminedichloroplatinum (II) on the activity of a helicase essential for DNA replication, the herpes simplex virus type-1 origin-binding protein. J Biol Chem 1994; 269:21676-81. (Pubitemid 24274807)
    • (1994) Journal of Biological Chemistry , vol.269 , Issue.34 , pp. 21676-21681
    • Villani, G.1    Pillaire, M.-J.2    Boehmer, P.E.3
  • 22
    • 0024503684 scopus 로고
    • Benzo[a]pyrene-DNA adducts inhibit translocation by the gene 4 protein of bacteriophage T7
    • Brown WC, Romano LJ. Benzo[a]pyrene-DNA adducts inhibit translocation by the gene 4 protein of bacteriophage T7. J Biol Chem 1989; 264:6748-54.
    • (1989) J Biol Chem , vol.264 , pp. 6748-6754
    • Brown, W.C.1    Romano, L.J.2
  • 23
    • 0030034293 scopus 로고    scopus 로고
    • Benzo[a]pyrene-DNA adducts inhibit the DNA helicase activity of the bacteriophage T7 gene 4 protein
    • Yong Y, Romano LJ. Benzo[a]pyrene-DNA adducts inhibit the DNA helicase activity of the bacteriophage T7 gene 4 protein. Chem Res Toxicol 1996; 9:179-87.
    • (1996) Chem Res Toxicol , vol.9 , pp. 179-187
    • Yong, Y.1    Romano, L.J.2
  • 24
    • 0027422376 scopus 로고
    • Activity of calf thymus DNA helicase e on cis-diamminedichloroplatinum (II)-damaged DNA 1
    • Huang L, Turchi JJ, Wahl AF, Bambara RA. Activity of calf thymus DNA helicase E on cis-diamminedichloroplatinum (II)-damaged DNA 1. J Biol Chem 1993; 268:26731-7.
    • (1993) J Biol Chem , vol.268 , pp. 26731-26737
    • Huang, L.1    Turchi, J.J.2    Wahl, A.F.3    Bambara, R.A.4
  • 25
    • 0027363992 scopus 로고
    • Effects of a single intrastrand d(GpG) platinum adduct on the strand separating activity of the Escherichia coli proteins RecB and RecA
    • DOI 10.1016/0014-5793(93)80380-D
    • Villani G, Cazaux C, Pillaire MJ, Boehmer P. Effects of a single intrastrand d(GpG) platinum adduct on the strand separating activity of the Escherichia coli proteins RecB and RecA. FEBS Lett 1993; 333:89-95. (Pubitemid 23306944)
    • (1993) FEBS Letters , vol.333 , Issue.1-2 , pp. 89-95
    • Villani, G.1    Cazaux, C.2    Pillaire, M.-J.3    Boehmer, P.4
  • 27
    • 0023410816 scopus 로고
    • The RAD3 gene of Saccharomyces cerevisiae encodes a DNA-dependent ATPase
    • Sung P, Prakash L, Weber S, Prakash S. The RAD3 gene of Saccharomyces cerevisiae encodes a DNA-dependent ATPase. Proc Natl Acad Sci USA 1987; 84:6045-9.
    • (1987) Proc Natl Acad Sci USA , vol.84 , pp. 6045-6049
    • Sung, P.1    Prakash, L.2    Weber, S.3    Prakash, S.4
  • 28
    • 0026536763 scopus 로고
    • The DNA helicase and adenosine triphosphatase activities of yeast Rad3 protein are inhibited by DNA damage. A potential mechanism for damage-specific recognition
    • Naegeli H, Bardwell L, Friedberg EC. The DNA helicase and adenosine triphosphatase activities of yeast Rad3 protein are inhibited by DNA damage. A potential mechanism for damage-specific recognition. J Biol Chem 1992; 267:392-8.
    • (1992) J Biol Chem , vol.267 , pp. 392-398
    • Naegeli, H.1    Bardwell, L.2    Friedberg, E.C.3
  • 29
    • 0027159787 scopus 로고
    • The DNA helicase activities of Rad3 protein of Saccharomyces cerevisiae and helicase II of Escherichia coli are differentially inhibited by covalent and noncovalent DNA modifications
    • Naegeli H, Modrich P, Friedberg EC. The DNA helicase activities of Rad3 protein of Saccharomyces cerevisiae and helicase II of Escherichia coli are differentially inhibited by covalent and noncovalent DNA modifications. J Biol Chem 1993; 268:10386-92.
    • (1993) J Biol Chem , vol.268 , pp. 10386-10392
    • Naegeli, H.1    Modrich, P.2    Friedberg, E.C.3
  • 30
    • 0027391296 scopus 로고
    • Inhibition of Rad3 DNA helicase activity by DNA adducts and abasic sites: Implications for the role of a DNA helicase in damage-specific incision of DNA
    • Naegeli H, Bardwell L, Friedberg EC. Inhibition of Rad3 DNA helicase activity by DNA adducts and abasic sites: implications for the role of a DNA helicase in damage-specific incision of DNA. Biochemistry 1993; 32:613-21.
    • (1993) Biochemistry , vol.32 , pp. 613-621
    • Naegeli, H.1    Bardwell, L.2    Friedberg, E.C.3
  • 31
    • 0942268166 scopus 로고    scopus 로고
    • DNA repair-deficient diseases, xeroderma pigmentosum, Cockayne syndrome and trichothiodystrophy
    • Lehmann AR. DNA repair-deficient diseases, xeroderma pigmentosum, Cockayne syndrome and trichothiodystrophy. Biochimie 2003; 85:1101-11.
    • (2003) Biochimie , vol.85 , pp. 1101-1111
    • Lehmann, A.R.1
  • 32
    • 33750922149 scopus 로고    scopus 로고
    • Phenotypic heterogeneity in the XPB DNA helicase gene (ERCC3): Xeroderma pigmentosum without and with Cockayne syndrome
    • Oh KS, Khan SG, Jaspers NG, Raams A, Ueda T, Lehmann A, et al. Phenotypic heterogeneity in the XPB DNA helicase gene (ERCC3): xeroderma pigmentosum without and with Cockayne syndrome. Hum Mutat 2006; 27:1092-103.
    • (2006) Hum Mutat , vol.27 , pp. 1092-1103
    • Oh, K.S.1    Khan, S.G.2    Jaspers, N.G.3    Raams, A.4    Ueda, T.5    Lehmann, A.6
  • 33
    • 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 JM. Distinct roles for the XPB/p52 and XPD/p44 subcomplexes of TFIIH in damaged DNA opening during nucleotide excision repair. Mol Cell 2007; 26:245-56.
    • (2007) Mol Cell , vol.26 , pp. 245-256
    • Coin, F.1    Oksenych, V.2    Egly, J.M.3
  • 34
    • 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, Sarasin A, et al. The ERCC2/DNA repair protein is associated with the class II BTF2/TFIIH transcription factor. EMBO J 1994; 13:2388-92.
    • (1994) EMBO J , vol.13 , pp. 2388-2392
    • Schaeffer, L.1    Moncollin, V.2    Roy, R.3    Staub, A.4    Mezzina, M.5    Sarasin, A.6
  • 35
    • 0028232284 scopus 로고
    • RAD25 is a DNA helicase required for DNA repair and RNA polymerase II transcription
    • DOI 10.1038/369578a0
    • Guzder SN, Sung P, Bailly V, Prakash L, Prakash S. RAD25 is a DNA helicase required for DNA repair and RNA polymerase II transcription. Nature 1994; 369:578-81. (Pubitemid 24192529)
    • (1994) Nature , vol.369 , Issue.6481 , pp. 578-581
    • Guzder, S.N.1    Sung, P.2    Bailly, V.3    Prakash, L.4    Prakash, S.5
  • 36
    • 0024095589 scopus 로고
    • Mutation of lysine-48 to arginine in the yeast RAD3 protein abolishes its ATPase and DNA helicase activities but not the ability to bind ATP
    • Sung P, Higgins D, Prakash L, Prakash S. Mutation of lysine-48 to arginine in the yeast RAD3 protein abolishes its ATPase and DNA helicase activities but not the ability to bind ATP. EMBO J 1988; 7:3263-9.
    • (1988) EMBO J , vol.7 , pp. 3263-3269
    • Sung, P.1    Higgins, D.2    Prakash, L.3    Prakash, S.4
  • 37
    • 22144482360 scopus 로고    scopus 로고
    • TFIIH XPB mutants suggest a unified bacterial-like mechanism for promoter opening but not escape
    • Lin YC, Choi WS, Gralla JD. TFIIH XPB mutants suggest a unified bacterial-like mechanism for promoter opening but not escape. Nat Struct Mol Biol 2005; 12:603-7.
    • (2005) Nat Struct Mol Biol , vol.12 , pp. 603-607
    • Lin, Y.C.1    Choi, W.S.2    Gralla, J.D.3
  • 38
    • 74549171725 scopus 로고    scopus 로고
    • The long unwinding road: XPB and XPD helicases in damaged DNA opening
    • Oksenych V, Coin F. The long unwinding road: XPB and XPD helicases in damaged DNA opening. Cell Cycle 2010; 9:90-6.
    • Cell Cycle , vol.2010 , Issue.9 , pp. 90-96
    • Oksenych, V.1    Coin, F.2
  • 39
    • 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. Reconstitution of the transcription factor TFIIH: assignment of functions for the three enzymatic subunits, XPB XPD, and cdk7. Mol Cell 1999; 3:87-95.
    • (1999) Mol Cell , vol.3 , pp. 87-95
    • Tirode, F.1    Busso, D.2    Coin, F.3    Egly, J.M.4
  • 40
    • 0040435451 scopus 로고    scopus 로고
    • TFIIH with inactive XPD helicase functions in transcription initiation but is defective in DNA repair
    • Winkler GS, Araujo SJ, Fiedler U, Vermeulen W, Coin F, Egly JM, et al. TFIIH with inactive XPD helicase functions in transcription initiation but is defective in DNA repair. J Biol Chem 2000; 275:4258-66.
    • (2000) J Biol Chem , vol.275 , pp. 4258-4266
    • Winkler, G.S.1    Araujo, S.J.2    Fiedler, U.3    Vermeulen, W.4    Coin, F.5    Egly, J.M.6
  • 41
    • 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, Nishi R, Iwai S, Hanaoka F. Two-step recognition of DNA damage for mammalian nucleotide excision repair: Directional binding of the XPC complex and DNA strand scanning. Mol Cell 2009; 36:642-53.
    • (2009) Mol Cell , vol.36 , pp. 642-653
    • Sugasawa, K.1    Akagi, J.2    Nishi, R.3    Iwai, S.4    Hanaoka, F.5
  • 42
    • 77950366206 scopus 로고    scopus 로고
    • The helicase XPD unwinds bubble structures and is not stalled by DNA lesions removed by the nucleotide excision repair pathway
    • Rudolf J, Rouillon C, Schwarz-Linek U, White MF. The helicase XPD unwinds bubble structures and is not stalled by DNA lesions removed by the nucleotide excision repair pathway. Nucleic Acids Res 2009; 38:931-41.
    • (2009) Nucleic Acids Res , vol.38 , pp. 931-941
    • Rudolf, J.1    Rouillon, C.2    Schwarz-Linek, U.3    White, M.F.4
  • 43
    • 57349157777 scopus 로고    scopus 로고
    • RecBCD enzyme and the repair of double-stranded DNA breaks
    • Dillingham MS, Kowalczykowski SC. RecBCD enzyme and the repair of double-stranded DNA breaks. Microbiol Mol Biol Rev 2008; 72:642-71.
    • (2008) Microbiol Mol Biol Rev , vol.72 , pp. 642-671
    • Dillingham, M.S.1    Kowalczykowski, S.C.2
  • 45
    • 72149090671 scopus 로고    scopus 로고
    • FANCM connects the genome instability disorders Bloom's Syndrome and Fanconi Anemia
    • Deans AJ, West SC. FANCM connects the genome instability disorders Bloom's Syndrome and Fanconi Anemia. Mol Cell 2009; 36:943-53.
    • (2009) Mol Cell , vol.36 , pp. 943-953
    • Deans, A.J.1    West, S.C.2
  • 46
    • 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, Roberts VA, et al. XPD helicase structures and activities: insights into the cancer and aging phenotypes from XPD mutations. Cell 2008; 133:789-800.
    • (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    Roberts, V.A.6
  • 49
    • 13844296708 scopus 로고    scopus 로고
    • Bumps in the road: How replicative DNA polymerases see DNA damage
    • Hogg M, Wallace SS, Doublie S. Bumps in the road: how replicative DNA polymerases see DNA damage. Curr Opin Struct Biol 2005; 15:86-93.
    • (2005) Curr Opin Struct Biol , vol.15 , pp. 86-93
    • Hogg, M.1    Wallace, S.S.2    Doublie, S.3
  • 50
    • 0037310493 scopus 로고    scopus 로고
    • Damage repair DNA polymerases Y
    • Yang W. Damage repair DNA polymerases Y. Curr Opin Struct Biol 2003; 13:23-30.
    • (2003) Curr Opin Struct Biol , vol.13 , pp. 23-30
    • Yang, W.1
  • 51
    • 53149104726 scopus 로고    scopus 로고
    • XPD structure reveals its secrets
    • Amst
    • Lehmann AR. XPD structure reveals its secrets. DNA Repair (Amst) 2008; 7:1912-5.
    • (2008) DNA Repair , vol.7 , pp. 1912-1915
    • Lehmann, A.R.1
  • 52
    • 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, Tainer JA. Conserved XPB core structure and motifs for DNA unwinding: implications for pathway selection of transcription or excision repair. Mol Cell 2006; 22:27-37.
    • (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    Tainer, J.A.6
  • 53
    • 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 JM, Coin F. Molecular insights into the recruitment of TFIIH to sites of DNA damage. EMBO J 2009; 28:2971-80.
    • (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
  • 54
    • 0034679815 scopus 로고    scopus 로고
    • Uncoupling DNA translocation and helicase activity in PcrA: Direct evidence for an active mechanism
    • Soultanas P, Dillingham MS, Wiley P, Webb MR, Wigley DB. Uncoupling DNA translocation and helicase activity in PcrA: direct evidence for an active mechanism. EMBO J 2000; 19:3799-810. (Pubitemid 30462137)
    • (2000) EMBO Journal , vol.19 , Issue.14 , pp. 3799-3810
    • Soultanas, P.1    Dillingham, M.S.2    Wiley, P.3    Webb, M.R.4    Wigley, D.B.5
  • 55
    • 38049075962 scopus 로고    scopus 로고
    • Human premature aging, DNA repair and RecQ helicases
    • Brosh RM Jr, Bohr VA. Human premature aging, DNA repair and RecQ helicases. Nucleic Acids Res 2007; 35:7527-44.
    • (2007) Nucleic Acids Res , vol.35 , pp. 7527-7544
    • Brosh Jr., R.M.1    Bohr, V.A.2
  • 56
    • 0003887169 scopus 로고
    • Committee on the Biologic Effects of Atmospheric Pollutants National Academy of Sciences, Washington DC
    • Committee on the Biologic Effects of Atmospheric Pollutants) Particulate Polycyclic Organic Matter. National Academy of Sciences, Washington DC. 1972.
    • (1972) Particulate Polycyclic Organic Matter
  • 57
    • 33748744378 scopus 로고    scopus 로고
    • Mechanisms of RecQ helicases in pathways of DNA metabolism and maintenance of genomic stability
    • Sharma S, Doherty KM, Brosh RM Jr. Mechanisms of RecQ helicases in pathways of DNA metabolism and maintenance of genomic stability. Biochem J 2006; 398:319-37.
    • (2006) Biochem J , vol.398 , pp. 319-337
    • Sharma, S.1    Doherty, K.M.2    Brosh Jr., R.M.3
  • 58
    • 69949144385 scopus 로고    scopus 로고
    • Genomic instability and DNA damage responses in progeria arising from defective maturation of prelamin A
    • Musich PR, Zou Z. Genomic instability and DNA damage responses in progeria arising from defective maturation of prelamin A. Aging 2009; 1:28-37.
    • (2009) Aging , vol.1 , pp. 28-37
    • Musich, P.R.1    Zou, Z.2
  • 59
    • 42049116919 scopus 로고    scopus 로고
    • The RecQ helicase WRN is required for normal replication fork progression after DNA damage or replication fork arrest
    • Sidorova JM, Li N, Folch A, Monnat RJ Jr. The RecQ helicase WRN is required for normal replication fork progression after DNA damage or replication fork arrest. Cell Cycle 2008; 7:796-807.
    • (2008) Cell Cycle , vol.7 , pp. 796-807
    • Sidorova, J.M.1    Li, N.2    Folch, A.3    Monnat Jr., R.J.4
  • 60
    • 77649243788 scopus 로고    scopus 로고
    • Sequence-specific processing of telomeric 3' overhangs by the Werner syndrome protein exonuclease activity
    • Li B, Reddy S, Comai L. Sequence-specific processing of telomeric 3' overhangs by the Werner syndrome protein exonuclease activity. Aging 2009; 1:289-302.
    • (2009) Aging , vol.1 , pp. 289-302
    • Li, B.1    Reddy, S.2    Comai, L.3
  • 61
    • 2942637828 scopus 로고    scopus 로고
    • The Werner Syndrome helicase and exonuclease cooperate to resolve telomeric D loops in a manner regulated by TRF1 and TRF2
    • Opresko PL, Otterlei M, Graakjaer J, Bruheim O, Dawut L, Kolvraa S, et al. The Werner Syndrome helicase and exonuclease cooperate to resolve telomeric D loops in a manner regulated by TRF1 and TRF2. Mol Cell 2004; 14:763-74.
    • (2004) Mol Cell , vol.14 , pp. 763-774
    • Opresko, P.L.1    Otterlei, M.2    Graakjaer, J.3    Bruheim, O.4    Dawut, L.5    Kolvraa, S.6
  • 62
    • 23744439082 scopus 로고    scopus 로고
    • Gene expression responses to DNA damage are altered in human aging and in Werner Syndrome
    • Kyng KJ, May A, Stevnsner T, Becker KG, Kolvra S, Bohr VA. Gene expression responses to DNA damage are altered in human aging and in Werner Syndrome. Oncogene 2005; 24:5026-42.
    • (2005) Oncogene , vol.24 , pp. 5026-5042
    • Kyng, K.J.1    May, A.2    Stevnsner, T.3    Becker, K.G.4    Kolvra, S.5    Bohr, V.A.6
  • 63
    • 67650523677 scopus 로고    scopus 로고
    • The Werner syndrome protein affects the expression of genes involved in adipogenesis and inflammation in addition to cell cycle and DNA damage responses
    • Turaga RV, Paquet ER, Sild M, Vignard J, Garand C, Johnson FB, et al. The Werner syndrome protein affects the expression of genes involved in adipogenesis and inflammation in addition to cell cycle and DNA damage responses. Cell Cycle 2009; 8:2080-92.
    • (2009) Cell Cycle , vol.8 , pp. 2080-2092
    • Turaga, R.V.1    Paquet, E.R.2    Sild, M.3    Vignard, J.4    Garand, C.5    Johnson, F.B.6
  • 64
    • 68049113833 scopus 로고    scopus 로고
    • WRN helicase defective in the premature aging disorder Werner syndrome genetically interacts with topoisomerase 3 and restores the top3 slow growth phenotype of sgs1 top3
    • Aggarwal M, Brosh RM Jr. WRN helicase defective in the premature aging disorder Werner syndrome genetically interacts with topoisomerase 3 and restores the top3 slow growth phenotype of sgs1 top3. Aging 2009; 1:219-33.
    • (2009) Aging , vol.1 , pp. 219-233
    • Aggarwal, M.1    Brosh Jr., R.M.2
  • 66
    • 33646846505 scopus 로고    scopus 로고
    • Inhibition of Werner Syndrome helicase activity by benzo[a]pyrene diol epoxide adducts can be overcome by Replication Protein A
    • Choudhary S, Doherty KM, Handy CJ, Sayer JM, Yagi H, Jerina DM, et al. Inhibition of Werner Syndrome helicase activity by benzo[a]pyrene diol epoxide adducts can be overcome by Replication Protein A. J Biol Chem 2006; 281:6000-9.
    • (2006) J Biol Chem , vol.281 , pp. 6000-6009
    • Choudhary, S.1    Doherty, K.M.2    Handy, C.J.3    Sayer, J.M.4    Yagi, H.5    Jerina, D.M.6
  • 67
    • 0142071741 scopus 로고    scopus 로고
    • Inhibition of Werner syndrome helicase activity by benzo[c]phenanthrene diol epoxide dA adducts in DNA is both strand-and stereoisomer-dependent
    • Driscoll HC, Matson SW, Sayer JM, Kroth H, Jerna DM, Brosh RM Jr. Inhibition of Werner syndrome helicase activity by benzo[c]phenanthrene diol epoxide dA adducts in DNA is both strand-and stereoisomer-dependent. J Biol Chem 2003; 278:41126-35.
    • (2003) J Biol Chem , vol.278 , pp. 41126-41135
    • Driscoll, H.C.1    Matson, S.W.2    Sayer, J.M.3    Kroth, H.4    Jerna, D.M.5    Brosh Jr., R.M.6
  • 68
    • 0031041812 scopus 로고    scopus 로고
    • NMR solution structures of stereoisometric covalent polycyclic aromatic carcinogen-DNA adduct: Principles, patterns, and diversity
    • Geacintov NE, Cosman M, Hingerty BE, Amin S, Broyde S, Patel DJ. NMR solution structures of stereoisometric covalent polycyclic aromatic carcinogen-DNA adduct: principles, patterns, and diversity. Chem Res Toxicol 1997; 10:111-46.
    • (1997) Chem Res Toxicol , vol.10 , pp. 111-146
    • Geacintov, N.E.1    Cosman, M.2    Hingerty, B.E.3    Amin, S.4    Broyde, S.5    Patel, D.J.6
  • 69
    • 12244283733 scopus 로고    scopus 로고
    • Solution structure of a cis-opened (10R)-N6-deoxyadenosine adduct of (9S,10R)-9,10-epoxy-7,8,9,10-tetrahydrobenzo[a]pyrene in a DNA duplex
    • Volk DE, Thiviyanathan V, Rice JS, Luxon BA, Shah JH, Yagi H, et al. Solution structure of a cis-opened (10R)-N6-deoxyadenosine adduct of (9S,10R)-9,10-epoxy-7,8,9,10-tetrahydrobenzo[a]pyrene in a DNA duplex. Biochemistry 2003; 42:1410-20.
    • (2003) Biochemistry , vol.42 , pp. 1410-1420
    • Volk, D.E.1    Thiviyanathan, V.2    Rice, J.S.3    Luxon, B.A.4    Shah, J.H.5    Yagi, H.6
  • 72
    • 0033258739 scopus 로고    scopus 로고
    • Effect of absolute configuration on the optical and NMR properties of oligonucleotides containing benzo[a]pyrene adducts at N6 of deoxyadenosine
    • Sayer JM, Shah JM, Liang C, Xie G, Kroth H, Yagi H, et al. Effect of absolute configuration on the optical and NMR properties of oligonucleotides containing benzo[a]pyrene adducts at N6 of deoxyadenosine. Polycyclic Aromatic Hydrocarbons 1999; 17:95-104.
    • (1999) Polycyclic Aromatic Hydrocarbons , vol.17 , pp. 95-104
    • Sayer, J.M.1    Shah, J.M.2    Liang, C.3    Xie, G.4    Kroth, H.5    Yagi, H.6
  • 73
    • 0036174219 scopus 로고    scopus 로고
    • Synthesis and characterization of sitespecific and stereoisomeric fjord dibenzo[a,l]pyrene diol epoxide-N(6)-adenine adducts: Unusual thermal stabilization of modified DNA duplexes
    • Ruan Q, Kolbanovskiy A, Zhuang P, Chen J, Krzeminshi J, Amin S, et al. Synthesis and characterization of sitespecific and stereoisomeric fjord dibenzo[a,l]pyrene diol epoxide-N(6)-adenine adducts: unusual thermal stabilization of modified DNA duplexes. Chem Res Toxicol 2002; 15:249-61.
    • (2002) Chem Res Toxicol , vol.15 , pp. 249-261
    • Ruan, Q.1    Kolbanovskiy, A.2    Zhuang, P.3    Chen, J.4    Krzeminshi, J.5    Amin, S.6
  • 74
    • 0027172508 scopus 로고
    • Escherichia coli rep helicase unwinds DNA by an active mechanism
    • Amaratunga M, Lohman TM. Escherichia coli Rep helicase unwinds DNA by an active mechanism. Biochemistry 1993; 32:6815-20. (Pubitemid 23221610)
    • (1993) Biochemistry , vol.32 , Issue.27 , pp. 6815-6820
    • Amaratunga, M.1    Lohman, T.M.2
  • 75
    • 0037129934 scopus 로고    scopus 로고
    • Vinylphosphonate internucleotide linkages inhibit the activity of PcrA DNA helicase
    • Bertram RD, Hayes CJ, Soultanas P. Vinylphosphonate internucleotide linkages inhibit the activity of PcrA DNA helicase. Biochemistry 2002; 41:7725-31.
    • (2002) Biochemistry , vol.41 , pp. 7725-7731
    • Bertram, R.D.1    Hayes, C.J.2    Soultanas, P.3
  • 77
    • 21844445309 scopus 로고    scopus 로고
    • Analysis of the DNA substrate specificity of the human BACH1 helicase associated with breast cancer
    • Gupta R, Sharma S, Sommers JA, Jin Z, Cantor SB, Brosh RM Jr. Analysis of the DNA substrate specificity of the human BACH1 helicase associated with breast cancer. J Biol Chem 2005; 280:25450-60.
    • (2005) J Biol Chem , vol.280 , pp. 25450-25460
    • Gupta, R.1    Sharma, S.2    Sommers, J.A.3    Jin, Z.4    Cantor, S.B.5    Brosh Jr., R.M.6
  • 78
    • 33845871975 scopus 로고    scopus 로고
    • Inhibition of BACH1 (FANCJ) helicase by backbone discontinuity is overcome by increased motor ATPase or length of loading strand
    • Gupta R, Sharma S, Doherty KM, Sommers JA, Cantor SB, Brosh RM Jr. Inhibition of BACH1 (FANCJ) helicase by backbone discontinuity is overcome by increased motor ATPase or length of loading strand. Nucleic Acids Res 2006; 34:6673-83.
    • (2006) Nucleic Acids Res , vol.34 , pp. 6673-6683
    • Gupta, R.1    Sharma, S.2    Doherty, K.M.3    Sommers, J.A.4    Cantor, S.B.5    Brosh Jr., R.M.6
  • 79
    • 12144258604 scopus 로고    scopus 로고
    • Chemically modified DNA substrates implicate the importance of electrostatic interactions for DNA unwinding by Dda helicase
    • Eoff RL, Spurling TL, Raney KD. Chemically modified DNA substrates implicate the importance of electrostatic interactions for DNA unwinding by Dda helicase. Biochemistry 2005; 44:666-74.
    • (2005) Biochemistry , vol.44 , pp. 666-674
    • Eoff, R.L.1    Spurling, T.L.2    Raney, K.D.3
  • 81
    • 2442513338 scopus 로고    scopus 로고
    • The DNA-unwinding mechanism of the ring helicase of bacteriophage T7
    • Jeong YJ, Levin MK, Patel SS. The DNA-unwinding mechanism of the ring helicase of bacteriophage T7. Proc Natl Acad Sci USA 2004; 101:7264-9.
    • (2004) Proc Natl Acad Sci USA , vol.101 , pp. 7264-7269
    • Jeong, Y.J.1    Levin, M.K.2    Patel, S.S.3
  • 82
    • 33646101028 scopus 로고    scopus 로고
    • Robust translocation along a molecular monorail: The NS3 helicase from Hepatitis C Virus traverses unusually large disruptions in its track
    • Beran RK, Bruno MM, Bowers HA, Jankowsky E, Pyle AM. Robust translocation along a molecular monorail: the NS3 helicase from Hepatitis C Virus traverses unusually large disruptions in its track. J Mol Biol 2006; 358:974-82.
    • (2006) J Mol Biol , vol.358 , pp. 974-982
    • Beran, R.K.1    Bruno, M.M.2    Bowers, H.A.3    Jankowsky, E.4    Pyle, A.M.5
  • 83
    • 3342896727 scopus 로고    scopus 로고
    • Periodic cycles of RNA unwinding and pausing by hepatitis C virus NS3 helicase
    • DOI 10.1038/nature02704
    • Serebrov V, Pyle AM. Periodic cycles of RNA unwinding and pausing by hepatitis C virus NS3 helicase. Nature 2004; 430:476-80. (Pubitemid 38987912)
    • (2004) Nature , vol.430 , Issue.6998 , pp. 476-480
    • Serebrov, V.1    Pyle, A.M.2
  • 84
    • 0035863881 scopus 로고    scopus 로고
    • Unwinding of nucleic acids by HCV NS3 helicase is sensitive to the structure of the duplex
    • Tackett AJ, Wei L, Cameron CE, Raney KD. Unwinding of nucleic acids by HCV NS3 helicase is sensitive to the structure of the duplex. Nucleic Acids Res 2001; 29:565-72. (Pubitemid 32060942)
    • (2001) Nucleic Acids Research , vol.29 , Issue.2 , pp. 565-572
    • Tackett, A.J.1    Wei, L.2    Cameron, C.E.3    Raney, K.D.4
  • 85
    • 3142708510 scopus 로고    scopus 로고
    • RPA alleviates the inhibitory effect of vinylphosphonate internucleotide linkages on DNA unwinding by BLM and WRN helicases
    • Garcia PL, Bradley G, Hayes CJ, Krintel S, Soultanas P, Janscak P. RPA alleviates the inhibitory effect of vinylphosphonate internucleotide linkages on DNA unwinding by BLM and WRN helicases. Nucleic Acids Res 2004; 32:3771-8.
    • (2004) Nucleic Acids Res , vol.32 , pp. 3771-3778
    • Garcia, P.L.1    Bradley, G.2    Hayes, C.J.3    Krintel, S.4    Soultanas, P.5    Janscak, P.6
  • 86
    • 0018190807 scopus 로고
    • DNA phosphotriesters as indicators of cumulative carcinogen-induced damage
    • Shooter KV. DNA phosphotriesters as indicators of cumulative carcinogen-induced damage. Nature 1978; 274:612-4.
    • (1978) Nature , vol.274 , pp. 612-614
    • Shooter, K.V.1
  • 87
    • 0023261982 scopus 로고
    • Comparative inhibition of chloramphenicol acetyltransferase gene expression by antisense oligonucleotide analogues having alkyl phosphotriester, methylphosphonate and phosphorothioate linkages
    • Marcus-Sekura CJ, Woerner AM, Shinozuka K, Zon G, Quinnan GV Jr. Comparative inhibition of chloramphenicol acetyltransferase gene expression by antisense oligonucleotide analogues having alkyl phosphotriester, methylphosphonate and phosphorothioate linkages. Nucleic Acids Res 1987; 15:5749-63.
    • (1987) Nucleic Acids Res , vol.15 , pp. 5749-5763
    • Marcus-Sekura, C.J.1    Woerner, A.M.2    Shinozuka, K.3    Zon, G.4    Quinnan Jr., G.V.5
  • 88
    • 45449100900 scopus 로고    scopus 로고
    • DNA damage, DNA repair, ageing and age-related disease
    • Wilson DM, III, Bohr VA, McKinnon PJ. DNA damage, DNA repair, ageing and age-related disease. Mech Ageing Dev 2008; 129:349-52.
    • (2008) Mech Ageing Dev , vol.129 , pp. 349-352
    • Wilson III, D.M.1    Bohr, V.A.2    McKinnon, P.J.3
  • 89
    • 68349128255 scopus 로고    scopus 로고
    • FANCJ helicase operates in the Fanconi Anemia DNA repair pathway and the response to replicational stress
    • Wu Y, Brosh RM Jr. FANCJ helicase operates in the Fanconi Anemia DNA repair pathway and the response to replicational stress. Curr Mol Med 2009; 9:470-82.
    • (2009) Curr Mol Med , vol.9 , pp. 470-482
    • Wu, Y.1    Brosh Jr., R.M.2
  • 90
    • 67650563908 scopus 로고    scopus 로고
    • FANCJ helicase uniquely senses oxidative base damage in either strand of duplex DNA and is stimulated by Replication Protein a to unwind the damaged DNA substrate in a strand-specific manner
    • Suhasini AN, Sommers JA, Mason AC, Voloshin ON, Camerini-Otero RD, Wold MS, et al. FANCJ helicase uniquely senses oxidative base damage in either strand of duplex DNA and is stimulated by Replication Protein A to unwind the damaged DNA substrate in a strand-specific manner. J Biol Chem 2009; 284:18458-70.
    • (2009) J Biol Chem , vol.284 , pp. 18458-18470
    • Suhasini, A.N.1    Sommers, J.A.2    Mason, A.C.3    Voloshin, O.N.4    Camerini-Otero, R.D.5    Wold, M.S.6
  • 91
    • 0001195990 scopus 로고    scopus 로고
    • Structure of a duplex DNA containing a thymine glycol residue in solution
    • Kung HC, Bolton PH. Structure of a duplex DNA containing a thymine glycol residue in solution. J Biol Chem 1997; 272:9227-36.
    • (1997) J Biol Chem , vol.272 , pp. 9227-9236
    • Kung, H.C.1    Bolton, P.H.2
  • 92
    • 71449125359 scopus 로고    scopus 로고
    • Telomeric D-loops containing 8-oxo-2′-deoxyguanosine are preferred substrates for Werner and Bloom syndrome helicases and are bound by POT1
    • Ghosh A, Rossi ML, Aulds J, Croteau D, Bohr VA. Telomeric D-loops containing 8-oxo-2′-deoxyguanosine are preferred substrates for Werner and Bloom syndrome helicases and are bound by POT1. J Biol Chem 2009; 284:31074-84.
    • (2009) J Biol Chem , vol.284 , pp. 31074-31084
    • Ghosh, A.1    Rossi, M.L.2    Aulds, J.3    Croteau, D.4    Bohr, V.A.5
  • 93
    • 34948855936 scopus 로고    scopus 로고
    • FANCJ (BACH1) helicase forms DNA damage inducible foci with replication protein a and interacts physically and functionally with the single-stranded DNA-binding protein
    • Gupta R, Sharma S, Sommers JA, Kenny MK, Cantor SB, Brosh RM Jr. FANCJ (BACH1) helicase forms DNA damage inducible foci with replication protein A and interacts physically and functionally with the single-stranded DNA-binding protein. Blood 2007; 110:2390-8.
    • (2007) Blood , vol.110 , pp. 2390-2398
    • Gupta, R.1    Sharma, S.2    Sommers, J.A.3    Kenny, M.K.4    Cantor, S.B.5    Brosh Jr., R.M.6
  • 94
    • 2342487313 scopus 로고    scopus 로고
    • Analysis of the unwinding activity of the dimeric RECQ1 helicase in the presence of human Replication Protein A
    • Cui S, Arosio D, Doherty KM, Brosh RM Jr, Falaschi A Vindigni A. Analysis of the unwinding activity of the dimeric RECQ1 helicase in the presence of human Replication Protein A. Nucleic Acids Res 2004; 32:2158-70.
    • (2004) Nucleic Acids Res , vol.32 , pp. 2158-2170
    • Cui, S.1    Arosio, D.2    Doherty, K.M.3    Brosh Jr., R.M.4    Falaschi, A.5    Vindigni, A.6
  • 95
    • 0030908093 scopus 로고    scopus 로고
    • Replication Protein A: A heterotrimeric, single-stranded DNA-binding protein required for eukaryotic DNA metabolism
    • Wold MS. Replication Protein A: a heterotrimeric, single-stranded DNA-binding protein required for eukaryotic DNA metabolism. Annu Rev Biochem 1997; 66:61-92.
    • (1997) Annu Rev Biochem , vol.66 , pp. 61-92
    • Wold, M.S.1
  • 96
    • 68249122027 scopus 로고    scopus 로고
    • The checkpoint response to replication stress
    • Amst
    • Branzei D, Foiani M. The checkpoint response to replication stress. DNA Repair (Amst) 2009; 8:1038-46.
    • (2009) DNA Repair , vol.8 , pp. 1038-1046
    • Branzei, D.1    Foiani, M.2
  • 98
    • 18244371925 scopus 로고    scopus 로고
    • Functional uncoupling of MCM helicase and DNA polymerase activities activates the ATR-dependent checkpoint
    • Byun TS, Pacek M, Yee MC, Walter JC, Cimprich KA. Functional uncoupling of MCM helicase and DNA polymerase activities activates the ATR-dependent checkpoint. Genes Dev 2005; 19:1040-52.
    • (2005) Genes Dev , vol.19 , pp. 1040-1052
    • Byun, T.S.1    Pacek, M.2    Yee, M.C.3    Walter, J.C.4    Cimprich, K.A.5
  • 99
    • 71449107031 scopus 로고    scopus 로고
    • The Mcm complex: Unwinding the mechanism of a replicative helicase
    • Bochman ML, Schwacha A. The Mcm complex: unwinding the mechanism of a replicative helicase. Microbiol Mol Biol Rev 2009; 73:652-83.
    • (2009) Microbiol Mol Biol Rev , vol.73 , pp. 652-683
    • Bochman, M.L.1    Schwacha, A.2
  • 100
    • 44849128194 scopus 로고    scopus 로고
    • How ATR turns on: TopBP1 goes on ATRIP with ATR
    • Burrows AE, Elledge SJ. How ATR turns on: TopBP1 goes on ATRIP with ATR. Genes Dev 2008; 22:1416-21.
    • (2008) Genes Dev , vol.22 , pp. 1416-1421
    • Burrows, A.E.1    Elledge, S.J.2
  • 101
  • 102
    • 34948889415 scopus 로고    scopus 로고
    • The Rad9-Hus1-Rad1 checkpoint clamp regulates interaction of TopBP1 with ATR
    • Lee J, Kumagai A, Dunphy WG. The Rad9-Hus1-Rad1 checkpoint clamp regulates interaction of TopBP1 with ATR. J Biol Chem 2007; 282:28036-44.
    • (2007) J Biol Chem , vol.282 , pp. 28036-28044
    • Lee, J.1    Kumagai, A.2    Dunphy, W.G.3
  • 103
    • 44849093460 scopus 로고    scopus 로고
    • TopBP1 activates ATR through ATRIP and a PIKK regulatory domain
    • Mordes DA, Glick GG, Zhao R, Cortez D. TopBP1 activates ATR through ATRIP and a PIKK regulatory domain. Genes Dev 2008; 22:1478-89.
    • (2008) Genes Dev , vol.22 , pp. 1478-1489
    • Mordes, D.A.1    Glick, G.G.2    Zhao, R.3    Cortez, D.4
  • 104
    • 75949092280 scopus 로고    scopus 로고
    • BACH1/FANCJ acts with TopBP1 and participates early in DNA replication checkpoint control
    • Gong Z, Kim JE, Leung CC, Glover JN, Chen J. BACH1/FANCJ acts with TopBP1 and participates early in DNA replication checkpoint control. Mol Cell 2010; 37:438-46.
    • (2010) Mol Cell , vol.37 , pp. 438-446
    • Gong, Z.1    Kim, J.E.2    Leung, C.C.3    Glover, J.N.4    Chen, J.5
  • 105
    • 34748890424 scopus 로고    scopus 로고
    • Activation of BRCA1/ BRCA2-associated helicase BACH1 is required for timely progression through S phase
    • Kumaraswamy E, Shiekhattar R. Activation of BRCA1/ BRCA2-associated helicase BACH1 is required for timely progression through S phase. Mol Cell Biol 2007; 27:6733-41.
    • (2007) Mol Cell Biol , vol.27 , pp. 6733-6741
    • Kumaraswamy, E.1    Shiekhattar, R.2
  • 106
    • 44949114282 scopus 로고    scopus 로고
    • FANCJ helicase defective in Fanconia Anemia and breast cancer unwinds G-quadruplex DNA to defend genomic stability
    • Wu Y, Shin-Ya K, Brosh RM Jr. FANCJ helicase defective in Fanconia Anemia and breast cancer unwinds G-quadruplex DNA to defend genomic stability. Mol Cell Biol 2008; 28:4116-28.
    • (2008) Mol Cell Biol , vol.28 , pp. 4116-4128
    • Wu, Y.1    Shin-Ya, K.2    Brosh Jr., R.M.3
  • 108
    • 0042466524 scopus 로고    scopus 로고
    • DNA polymerase stabilization at stalled replication forks requires Mec1 and the RecQ helicase Sgs1
    • Cobb JA, Bjergbaek L, Shimada K, Frei C, Gasser SM. DNA polymerase stabilization at stalled replication forks requires Mec1 and the RecQ helicase Sgs1. EMBO J 2003; 22:4325-36.
    • (2003) EMBO J , vol.22 , pp. 4325-4336
    • Cobb, J.A.1    Bjergbaek, L.2    Shimada, K.3    Frei, C.4    Gasser, S.M.5
  • 109
    • 23844450310 scopus 로고    scopus 로고
    • Physical and functional mapping of the RPA interaction domain of the Werner and Bloom syndrome helicases
    • Doherty KM, Sommers JA, Gray MD, Lee JW, von Kobbe C, Thoma NH, et al. Physical and functional mapping of the RPA interaction domain of the Werner and Bloom syndrome helicases. J Biol Chem 2005; 280:29494-505.
    • (2005) J Biol Chem , vol.280 , pp. 29494-29505
    • Doherty, K.M.1    Sommers, J.A.2    Gray, M.D.3    Lee, J.W.4    Von Kobbe, C.5    Thoma, N.H.6
  • 110
    • 69949138464 scopus 로고    scopus 로고
    • HSSB1 and hSSB2 form similar multiprotein complexes that participate in DNA damage response
    • Li Y, Bolderson E, Kumar R, Muniandy PA, Xue Y, Richard DJ, et al. HSSB1 and hSSB2 form similar multiprotein complexes that participate in DNA damage response. J Biol Chem 2009; 284:23525-31.
    • (2009) J Biol Chem , vol.284 , pp. 23525-23531
    • Li, Y.1    Bolderson, E.2    Kumar, R.3    Muniandy, P.A.4    Xue, Y.5    Richard, D.J.6
  • 112
    • 70350491426 scopus 로고    scopus 로고
    • Multiple human single-stranded DNA binding proteins function in genome maintenance: Structural, biochemical and functional analysis
    • Richard DJ, Bolderson E, Khanna KK. Multiple human single-stranded DNA binding proteins function in genome maintenance: structural, biochemical and functional analysis. Crit Rev Biochem Mol Biol 2000; 44:98-116.
    • (2000) Crit Rev Biochem Mol Biol , vol.44 , pp. 98-116
    • Richard, D.J.1    Bolderson, E.2    Khanna, K.K.3


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