메뉴 건너뛰기




Volumn 767, Issue , 2013, Pages 123-144

DNA helicases associated with genetic instability, cancer, and aging

Author keywords

[No Author keywords available]

Indexed keywords

BLOOM SYNDROME HELICASE; DDX11 HELICASE; ENZYME INHIBITOR; FANCONI ANEMIA GROUP J PROTEIN; FANCONI ANEMIA PROTEIN; HELICASE; MITOCHONDRIAL DNA; POLYDEOXYRIBONUCLEOTIDE SYNTHASE; RECQ HELICASE; RECQL4 HELICASE; TWINKLE HELICASE; UNCLASSIFIED DRUG; WERNER SYNDROME PROTEIN; XERODERMA PIGMENTOSUM GROUP D PROTEIN; IRON SULFUR PROTEIN; UNCLASSIFIED ENZYME; DNA HELICASE;

EID: 84873646761     PISSN: 00652598     EISSN: None     Source Type: Book Series    
DOI: 10.1007/978-1-4614-5037-5_6     Document Type: Article
Times cited : (34)

References (108)
  • 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
    • 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
  • 3
    • 38049075962 scopus 로고    scopus 로고
    • Human premature aging DNA repair and RecQ helicases
    • Brosh Jr RM, 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
  • 4
    • 0029893874 scopus 로고    scopus 로고
    • Mechanisms of helicase-catalyzed DNA unwinding
    • Lohman TM, Bjornson KP. Mechanisms of helicase-catalyzed DNA unwinding. Annu Rev Biochem. 1996;65:169-214.
    • (1996) Annu Rev Biochem , vol.65 , pp. 169-214
    • Lohman, T.M.1    Bjornson, K.P.2
  • 5
    • 33745823112 scopus 로고    scopus 로고
    • Mechanisms of helicases
    • Patel SS, Donmez I. Mechanisms of helicases. J Biol Chem. 2006;281:18265-8.
    • (2006) J Biol Chem , vol.281 , pp. 18265-18268
    • Patel, S.S.1    Donmez, I.2
  • 6
    • 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
  • 8
    • 79953187302 scopus 로고    scopus 로고
    • Superfamily I. helicases as modular components of DNA-processing machines
    • Dillingham MS, Superfamily I. helicases as modular components of DNA-processing machines. Biochem Soc Trans. 2011;39:413-23.
    • (2011) Biochem Soc Trans , vol.39 , pp. 413-423
    • Dillingham, M.S.1
  • 9
    • 84864499620 scopus 로고    scopus 로고
    • RecQ helicases in DNA double strand break repair and telomere maintenance
    • Singh DK, Ghosh AK, Croteau DL, Bohr VA. RecQ helicases in DNA double strand break repair and telomere maintenance. Mutat Res. 2012;736:15-24.
    • (2012) Mutat Res , vol.736 , pp. 15-24
    • Singh, D.K.1    Ghosh, A.K.2    Croteau, D.L.3    Bohr, V.A.4
  • 10
    • 63449109208 scopus 로고    scopus 로고
    • Welcome the family of FANCJ-like helicases to the block of genome stability maintenance proteins
    • Wu Y, Suhasini AN, Brosh RM. Welcome the family of FANCJ-like helicases to the block of genome stability maintenance proteins. Cell Mol Life Sci. 2009;66:1209-22.
    • (2009) Cell Mol Life Sci , vol.66 , pp. 1209-1222
    • Wu, Y.1    Suhasini, A.N.2    Brosh, R.M.3
  • 11
    • 84870323168 scopus 로고    scopus 로고
    • Structure, function and evolution of the XPD family of iron-sulfur-containing 5 ¢ ->3 ¢ DNA helicases
    • White MF. Structure, function and evolution of the XPD family of iron-sulfur-containing 5 ¢ ->3 ¢ DNA helicases. Biochem Soc Trans. 2009;37:547-51.
    • (2009) Biochem Soc Trans , vol.37 , pp. 547-551
    • White, M.F.1
  • 12
    • 84857029886 scopus 로고    scopus 로고
    • Iron-sulphur clusters in nucleic acid processing enzymes
    • White MF, Dillingham MS. Iron-sulphur clusters in nucleic acid processing enzymes. Curr Opin Struct Biol. 2012;22:94-100.
    • (2012) Curr Opin Struct Biol , vol.22 , pp. 94-100
    • White, M.F.1    Dillingham, M.S.2
  • 13
    • 84857041145 scopus 로고    scopus 로고
    • Shining a light on xeroderma pigmentosum
    • Digiovanna JJ, Kraemer KH. Shining a light on xeroderma pigmentosum. J Invest Dermatol. 2012;132:785-96.
    • (2012) J Invest Dermatol , vol.132 , pp. 785-796
    • Digiovanna, J.J.1    Kraemer, K.H.2
  • 14
    • 79960377780 scopus 로고    scopus 로고
    • A history of TFIIH: Two decades of molecular biology on a pivotal transcription/repair factor
    • Egly JM, Coin F. A history of TFIIH: two decades of molecular biology on a pivotal transcription/repair factor. DNA Repair (Amst). 2011;10:714-21.
    • (2011) DNA Repair (Amst) , vol.10 , pp. 714-721
    • Egly, J.M.1    Coin, F.2
  • 15
    • 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.
    • (2010) Cell Cycle , vol.9 , pp. 90-96
    • Oksenych, V.1    Coin, F.2
  • 16
    • 82755184119 scopus 로고    scopus 로고
    • The Fanconi anaemia pathway orchestrates incisions at sites of crosslinked DNA
    • Crossan GP, Patel KJ. The Fanconi anaemia pathway orchestrates incisions at sites of crosslinked DNA. J Pathol. 2012;226:326-37.
    • (2012) J Pathol , vol.226 , pp. 326-337
    • Crossan, G.P.1    Patel, K.J.2
  • 17
    • 79959635260 scopus 로고    scopus 로고
    • DNA interstrand crosslink repair and cancer
    • Deans AJ, West SC. DNA interstrand crosslink repair and cancer. Nat Rev Cancer. 2011;11:467-80.
    • (2011) Nat Rev Cancer , vol.11 , pp. 467-480
    • Deans, A.J.1    West, S.C.2
  • 18
    • 79952162878 scopus 로고    scopus 로고
    • Hereditary breast cancer and the BRCA1-associated FANCJ/ BACH1/BRIP1
    • Cantor SB, Guillemette S. Hereditary breast cancer and the BRCA1-associated FANCJ/ BACH1/BRIP1. Future Oncol. 2011;7:253-61.
    • (2011) Future Oncol , vol.7 , pp. 253-261
    • Cantor, S.B.1    Guillemette, S.2
  • 19
    • 20644461718 scopus 로고    scopus 로고
    • BACH1, a novel helicase-like protein, interacts directly with BRCA1 and contributes to its DNA repair function
    • Cantor SB, Bell DW, Ganesan S, et al. BACH1, a novel helicase-like protein, interacts directly with BRCA1 and contributes to its DNA repair function. Cell. 2001;105:149-60.
    • (2001) Cell , vol.105 , pp. 149-160
    • Cantor, S.B.1    Bell, D.W.2    Ganesan, S.3
  • 20
    • 61349135721 scopus 로고    scopus 로고
    • FANCJ is a structure-speci fi c DNA helicase associated with the maintenance of genomic G/C tracts
    • London TB, Barber LJ, Mosedale G, et al. FANCJ is a structure-speci fi c DNA helicase associated with the maintenance of genomic G/C tracts. J Biol Chem. 2008;283:36132-9.
    • (2008) J Biol Chem , vol.283 , pp. 36132-36139
    • London, T.B.1    Barber, L.J.2    Mosedale, G.3
  • 21
    • 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 Jr RM. 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
  • 22
    • 76049096485 scopus 로고    scopus 로고
    • Warsaw breakage syndrome, a cohesinopathy associated with mutations in the XPD helicase family member DDX11/ChlR1
    • van der LP, Chrzanowska KH, Godthelp BC, et al. Warsaw breakage syndrome, a cohesinopathy associated with mutations in the XPD helicase family member DDX11/ChlR1. Am J Hum Genet. 2010;86:262-6.
    • (2010) Am J Hum Genet , vol.86 , pp. 262-266
    • Van Der, L.P.1    Chrzanowska, K.H.2    Godthelp, B.C.3
  • 23
    • 1642360837 scopus 로고    scopus 로고
    • Chl1p, a DNA helicase-like protein in budding yeast, functions in sister-chromatid cohesion
    • Skibbens RV. Chl1p, a DNA helicase-like protein in budding yeast, functions in sister-chromatid cohesion. Genetics. 2004;166:33-42.
    • (2004) Genetics , vol.166 , pp. 33-42
    • Skibbens, R.V.1
  • 24
    • 34548251989 scopus 로고    scopus 로고
    • Loss of ChlR1 helicase in mouse causes lethality due to the accumulation of aneuploid cells generated by cohesion defects and placental malformation
    • Inoue A, Li T, Roby SK, et al. Loss of ChlR1 helicase in mouse causes lethality due to the accumulation of aneuploid cells generated by cohesion defects and placental malformation. Cell Cycle. 2007;6:1646-54.
    • (2007) Cell Cycle , vol.6 , pp. 1646-1654
    • Inoue, A.1    Li, T.2    Roby, S.K.3
  • 25
    • 33845657930 scopus 로고    scopus 로고
    • The DNA helicase ChlR1 is required for sister chromatid cohesion in mammalian cells
    • Parish JL, Rosa J, Wang X, Lahti JM, Doxsey SJ, Androphy EJ. The DNA helicase ChlR1 is required for sister chromatid cohesion in mammalian cells. J Cell Sci. 2006;119:4857-65.
    • (2006) J Cell Sci , vol.119 , pp. 4857-4865
    • Parish, J.L.1    Rosa, J.2    Wang, X.3    Lahti, J.M.4    Doxsey, S.J.5    Androphy, E.J.6
  • 26
    • 80052607856 scopus 로고    scopus 로고
    • Mammalian ChlR1 has a role in heterochromatin organization
    • Inoue A, Hyle J, Lechner MS, Lahti JM. Mammalian ChlR1 has a role in heterochromatin organization. Exp Cell Res. 2011;317:2522-35.
    • (2011) Exp Cell Res , vol.317 , pp. 2522-2535
    • Inoue, A.1    Hyle, J.2    Lechner, M.S.3    Lahti, J.M.4
  • 27
    • 0028785586 scopus 로고
    • The Bloom's syndrome gene product is homologous to RecQ helicases
    • Ellis NA, Groden J, Ye TZ, et al. The Bloom's syndrome gene product is homologous to RecQ helicases. Cell. 1995;83:655-66.
    • (1995) Cell , vol.83 , pp. 655-666
    • Ellis, N.A.1    Groden, J.2    Ye, T.Z.3
  • 28
    • 0346351375 scopus 로고
    • A manyfold increase in sister chromatid exchanges in Bloom's syndrome lymphocytes
    • Chaganti RS, Schonberg S, German J. A manyfold increase in sister chromatid exchanges in Bloom's syndrome lymphocytes. Proc Natl Acad Sci USA. 1974;71:4508-12.
    • (1974) Proc Natl Acad Sci USA , vol.71 , pp. 4508-4512
    • Chaganti, R.S.1    Schonberg, S.2    German, J.3
  • 29
    • 73949138091 scopus 로고    scopus 로고
    • Dissolution of double Holliday junctions by the concerted action of BLM and topoisomerase IIIalpha
    • Bachrati CZ, Hickson ID. Dissolution of double Holliday junctions by the concerted action of BLM and topoisomerase IIIalpha. Methods Mol Biol. 2009;582:91-102.
    • (2009) Methods Mol Biol , vol.582 , pp. 91-102
    • Bachrati, C.Z.1    Hickson, I.D.2
  • 30
    • 0347987856 scopus 로고    scopus 로고
    • The Bloom's syndrome helicase suppresses crossing over during homologous recombination
    • Wu L, Hickson ID. The Bloom's syndrome helicase suppresses crossing over during homologous recombination. Nature. 2003;426:870-4.
    • (2003) Nature , vol.426 , pp. 870-874
    • Wu, L.1    Hickson, I.D.2
  • 31
    • 77955919033 scopus 로고    scopus 로고
    • BLM has early and late functions in homologous recombination repair in mouse embryonic stem cells
    • Chu WK, Hanada K, Kanaar R, Hickson ID. BLM has early and late functions in homologous recombination repair in mouse embryonic stem cells. Oncogene. 2010;29:4705-14.
    • (2010) Oncogene , vol.29 , pp. 4705-4714
    • Chu, W.K.1    Hanada, K.2    Kanaar, R.3    Hickson, I.D.4
  • 32
    • 79951688343 scopus 로고    scopus 로고
    • BLM-DNA2-RPA-MRN and EXO1-BLMRPA- MRN constitute two DNA end resection machineries for human DNA break repair
    • Nimonkar AV, Genschel J, Kinoshita E, et al. BLM-DNA2-RPA-MRN and EXO1-BLMRPA- MRN constitute two DNA end resection machineries for human DNA break repair. Genes Dev. 2011;25:350-62.
    • (2011) Genes Dev , vol.25 , pp. 350-362
    • Nimonkar, A.V.1    Genschel, J.2    Kinoshita, E.3
  • 33
    • 67349227137 scopus 로고    scopus 로고
    • Replication stress induces sister-chromatid bridging at fragile site loci in mitosis
    • Chan KL, Palmai-Pallag T, Ying S, Hickson ID. Replication stress induces sister-chromatid bridging at fragile site loci in mitosis. Nat Cell Biol. 2009;11:753-60.
    • (2009) Nat Cell Biol , vol.11 , pp. 753-760
    • Chan, K.L.1    Palmai-Pallag, T.2    Ying, S.3    Hickson, I.D.4
  • 34
    • 78649467087 scopus 로고    scopus 로고
    • Human RECQ helicases: Roles in DNA metabolism, mutagenesis and cancer biology
    • Monnat Jr RJ. Human RECQ helicases: roles in DNA metabolism, mutagenesis and cancer biology. Semin Cancer Biol. 2010;20:329-39.
    • (2010) Semin Cancer Biol , vol.20 , pp. 329-339
    • Monnat Jr., R.J.1
  • 35
    • 76749168005 scopus 로고    scopus 로고
    • Roles of Werner syndrome protein in protection of genome integrity
    • Rossi ML, Ghosh AK, Bohr VA. Roles of Werner syndrome protein in protection of genome integrity. DNA Repair (Amst). 2010;9:331-44.
    • (2010) DNA Repair (Amst) , vol.9 , pp. 331-344
    • Rossi, M.L.1    Ghosh, A.K.2    Bohr, V.A.3
  • 37
    • 32944476196 scopus 로고    scopus 로고
    • Revisiting the craniosynostosis-radial ray hypoplasia association: Baller-Gerold syndrome caused by mutations in the RECQL4 gene
    • Van Maldergem L, Siitonen HA, Jalkh N, et al. Revisiting the craniosynostosis-radial ray hypoplasia association: Baller-Gerold syndrome caused by mutations in the RECQL4 gene. J Med Genet. 2006;43:148-52.
    • (2006) J Med Genet , vol.43 , pp. 148-152
    • Van Maldergem, L.1    Siitonen, H.A.2    Jalkh, N.3
  • 38
    • 77956707391 scopus 로고    scopus 로고
    • The involvement of human RECQL4 in DNA double-strand break repair
    • Singh DK, Karmakar P, Aamann M, et al. The involvement of human RECQL4 in DNA double-strand break repair. Aging Cell. 2010;9:358-71.
    • (2010) Aging Cell , vol.9 , pp. 358-371
    • Singh, D.K.1    Karmakar, P.2    Aamann, M.3
  • 39
    • 84855266777 scopus 로고    scopus 로고
    • RECQL4, the protein mutated in Rothmund-Thomson syndrome, functions in telomere maintenance
    • Ghosh AK, Rossi ML, Singh DK, et al. RECQL4, the protein mutated in Rothmund-Thomson syndrome, functions in telomere maintenance. J Biol Chem. 2012;287:196-209.
    • (2012) J Biol Chem , vol.287 , pp. 196-209
    • Ghosh, A.K.1    Rossi, M.L.2    Singh, D.K.3
  • 40
    • 84862782942 scopus 로고    scopus 로고
    • RECQL4 localizes to mitochondria and preserves mitochondrial DNA integrity
    • Croteau DL, Rossi ML, Canugovi C, et al. RECQL4 localizes to mitochondria and preserves mitochondrial DNA integrity. Aging Cell. 2012;11(3):456-66.
    • (2012) Aging Cell , vol.11 , Issue.3 , pp. 456-466
    • Croteau, D.L.1    Rossi, M.L.2    Canugovi, C.3
  • 41
    • 84864804909 scopus 로고    scopus 로고
    • RECQL4 is essential for the transport of p53 to mitochondria in normal human cells in the absence of exogenous stress
    • De S, Kumari J, Mudgal R, et al. RECQL4 is essential for the transport of p53 to mitochondria in normal human cells in the absence of exogenous stress. J Cell Sci. 2012;125:2509-22.
    • (2012) J Cell Sci , vol.125 , pp. 2509-2522
    • De S Kumari, J.1    Mudgal, R.2
  • 42
    • 33748744378 scopus 로고    scopus 로고
    • Mechanisms of RecQ helicases in pathways of DNA metabolism and maintenance of genomic stability
    • Sharma S, Doherty KM, Brosh Jr RM. 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
  • 43
    • 33847228012 scopus 로고    scopus 로고
    • RECQL, a member of the RecQ family of DNA helicases, suppresses chromosomal instability
    • Sharma S, Stumpo DJ, Balajee AS, et al. RECQL, a member of the RecQ family of DNA helicases, suppresses chromosomal instability. Mol Cell Biol. 2007;27:1784-94.
    • (2007) Mol Cell Biol , vol.27 , pp. 1784-1794
    • Sharma, S.1    Stumpo, D.J.2    Balajee, A.S.3
  • 44
    • 40249083431 scopus 로고    scopus 로고
    • Human RECQ1 is a DNA damage responsive protein required for genotoxic stress resistance and suppression of sister chromatid exchanges
    • Sharma S, Brosh Jr RM. Human RECQ1 is a DNA damage responsive protein required for genotoxic stress resistance and suppression of sister chromatid exchanges. PLoS One. 2007;2:e1297.
    • (2007) PLoS One , vol.2
    • Sharma, S.1    Brosh Jr., R.M.2
  • 45
    • 77749330814 scopus 로고    scopus 로고
    • The human RECQ1 and RECQ4 helicases play distinct roles in DNA replication initiation
    • Thangavel S, Mendoza-Maldonado R, Tissino E, et al. The human RECQ1 and RECQ4 helicases play distinct roles in DNA replication initiation. Mol Cell Biol. 2010;30:1382-96.
    • (2010) Mol Cell Biol , vol.30 , pp. 1382-1396
    • Thangavel, S.1    Mendoza-Maldonado, R.2    Tissino, E.3
  • 46
    • 47249100637 scopus 로고    scopus 로고
    • A RECQ5-RNA polymerase II association identi fi ed by targeted proteomic analysis of human chromatin
    • Aygun O, Svejstrup J, Liu Y. A RECQ5-RNA polymerase II association identi fi ed by targeted proteomic analysis of human chromatin. Proc Natl Acad Sci USA. 2008;105:8580-4.
    • (2008) Proc Natl Acad Sci USA , vol.105 , pp. 8580-8584
    • Aygun, O.1    Svejstrup, J.2    Liu, Y.3
  • 47
    • 77958595004 scopus 로고    scopus 로고
    • RECQ5 helicase associates with the C-terminal repeat domain of RNA polymerase II during productive elongation phase of transcription
    • Kanagaraj R, Huehn D, MacKellar A, et al. RECQ5 helicase associates with the C-terminal repeat domain of RNA polymerase II during productive elongation phase of transcription. Nucleic Acids Res. 2010;38:8131-40.
    • (2010) Nucleic Acids Res , vol.38 , pp. 8131-8140
    • Kanagaraj, R.1    Huehn, D.2    MacKellar, A.3
  • 48
    • 84857854718 scopus 로고    scopus 로고
    • RECQL5 cooperates with topoisomerase II alpha in DNA decatenation and cell cycle progression
    • Ramamoorthy M, Tadokoro T, Rybanska I, et al. RECQL5 cooperates with topoisomerase II alpha in DNA decatenation and cell cycle progression. Nucleic Acids Res. 2012;40:1621-35.
    • (2012) Nucleic Acids Res , vol.40 , pp. 1621-1635
    • Ramamoorthy, M.1    Tadokoro, T.2    Rybanska, I.3
  • 49
    • 83755205842 scopus 로고    scopus 로고
    • Defects in mitochondrial DNA replication and human disease
    • Copeland WC. Defects in mitochondrial DNA replication and human disease. Crit Rev Biochem Mol Biol. 2012;47:64-74.
    • (2012) Crit Rev Biochem Mol Biol , vol.47 , pp. 64-74
    • Copeland, W.C.1
  • 50
    • 1542677230 scopus 로고    scopus 로고
    • TWINKLE Has 5 ¢ -> 3 ¢ DNA helicase activity and is speci fi cally stimulated by mitochondrial single-stranded DNA-binding protein
    • Korhonen JA, Gaspari M, Falkenberg M. TWINKLE Has 5 ¢ -> 3 ¢ DNA helicase activity and is speci fi cally stimulated by mitochondrial single-stranded DNA-binding protein. J Biol Chem. 2003;278:48627-32.
    • (2003) J Biol Chem , vol.278 , pp. 48627-48632
    • Korhonen, J.A.1    Gaspari, M.2    Falkenberg, M.3
  • 51
    • 84860379072 scopus 로고    scopus 로고
    • The human mitochondrial DNA helicase TWINKLE is both an unwinding and an annealing helicase
    • Sen D, Nandakumar D, Tang GQ, Patel SS. The human mitochondrial DNA helicase TWINKLE is both an unwinding and an annealing helicase. J Biol Chem. 2012;287(18):14545-56.
    • (2012) J Biol Chem , vol.287 , Issue.18 , pp. 14545-14556
    • Sen, D.1    Nandakumar, D.2    Tang, G.Q.3    Patel, S.S.4
  • 53
    • 0038094503 scopus 로고    scopus 로고
    • Basal transcription defect discriminates between xeroderma pigmentosum and trichothiodystrophy in XPD patients
    • Dubaele S, De Proietti SL, Bienstock RJ, et al. Basal transcription defect discriminates between xeroderma pigmentosum and trichothiodystrophy in XPD patients. Mol Cell. 2003;11:1635-46.
    • (2003) Mol Cell , vol.11 , pp. 1635-1646
    • Dubaele, S.1    De Proietti, S.L.2    Bienstock, R.J.3
  • 54
    • 53149104726 scopus 로고    scopus 로고
    • XPD structure reveals its secrets
    • Lehmann AR. XPD structure reveals its secrets. DNA Repair (Amst). 2008;7:1912-5.
    • (2008) DNA Repair (Amst) , vol.7 , pp. 1912-1915
    • Lehmann, A.R.1
  • 55
    • 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
  • 56
    • 0034927859 scopus 로고    scopus 로고
    • Cerebro-oculo-facio-skeletal syndrome with a nucleotide excision-repair defect and a mutated XPD gene, with prenatal diagnosis in a triplet pregnancy
    • Graham Jr JM, Nyane-Yeboa K, Raams A, et al. Cerebro-oculo-facio-skeletal syndrome with a nucleotide excision-repair defect and a mutated XPD gene, with prenatal diagnosis in a triplet pregnancy. Am J Hum Genet. 2001;69:291-300.
    • (2001) Am J Hum Genet , vol.69 , pp. 291-300
    • Graham Jr., J.M.1    Nyane-Yeboa, K.2    Raams, A.3
  • 57
    • 34447318130 scopus 로고    scopus 로고
    • The FANCJ/MutLalpha interaction is required for correction of the cross-link response in FA-J cells
    • Peng M, Litman R, Xie J, Sharma S, Brosh Jr RM, Cantor SB. The FANCJ/MutLalpha interaction is required for correction of the cross-link response in FA-J cells. EMBO J. 2007;26:3238-49.
    • (2007) EMBO J , vol.26 , pp. 3238-3249
    • Peng, M.1    Litman, R.2    Xie, J.3    Sharma, S.4    Brosh Jr., R.M.5    Cantor, S.B.6
  • 58
    • 25144497571 scopus 로고    scopus 로고
    • The BRCA1-interacting helicase BRIP1 is de fi cient in Fanconi anemia
    • Levran O, Attwooll C, Henry RT, et al. The BRCA1-interacting helicase BRIP1 is de fi cient in Fanconi anemia. Nat Genet. 2005;37:931-3.
    • (2005) Nat Genet , vol.37 , pp. 931-933
    • Levran, O.1    Attwooll, C.2    Henry, R.T.3
  • 59
    • 77958512174 scopus 로고    scopus 로고
    • Fanconi anemia Group J mutation abolishes its DNA repair function by uncoupling DNA translocation from helicase activity or disruption of protein-DNA complexes
    • Wu Y, Sommers JA, Suhasini AN, et al. Fanconi anemia Group J mutation abolishes its DNA repair function by uncoupling DNA translocation from helicase activity or disruption of protein-DNA complexes. Blood. 2010;116:3780-91.
    • (2010) Blood , vol.116 , pp. 3780-3791
    • Wu, Y.1    Sommers, J.A.2    Suhasini, A.N.3
  • 60
    • 0142147272 scopus 로고    scopus 로고
    • The BRCT domain is a phospho-protein binding domain
    • Yu X, Chini CC, He M, Mer G, Chen J. The BRCT domain is a phospho-protein binding domain. Science. 2003;302:639-42.
    • (2003) Science , vol.302 , pp. 639-642
    • Yu, X.1    Chini, C.C.2    He, M.3    Mer, G.4    Chen, J.5
  • 61
    • 77951878399 scopus 로고    scopus 로고
    • Targeting the FANCJ-BRCA1 interaction promotes a switch from recombination to poleta-dependent bypass
    • Xie J, Litman R, Wang S, et al. Targeting the FANCJ-BRCA1 interaction promotes a switch from recombination to poleta-dependent bypass. Oncogene. 2010;29:2499-508.
    • (2010) Oncogene , vol.29 , pp. 2499-2508
    • Xie, J.1    Litman, R.2    Wang, S.3
  • 62
    • 51049121966 scopus 로고    scopus 로고
    • Studies with the human cohesin establishment factor, ChlR1. Association of ChlR1 with Ctf18-RFC and Fen1
    • Farina A, Shin JH, Kim DH, et al. Studies with the human cohesin establishment factor, ChlR1. Association of ChlR1 with Ctf18-RFC and Fen1. J Biol Chem. 2008;283:20925-36.
    • (2008) J Biol Chem , vol.283 , pp. 20925-20936
    • Farina, A.1    Shin, J.H.2    Kim, D.H.3
  • 63
    • 0034651623 scopus 로고    scopus 로고
    • Characterization of the enzymatic activity of hChlR1, a novel human DNA helicase
    • Hirota Y, Lahti JM. Characterization of the enzymatic activity of hChlR1, a novel human DNA helicase. Nucleic Acids Res. 2000;28:917-24.
    • (2000) Nucleic Acids Res , vol.28 , pp. 917-924
    • Hirota, Y.1    Lahti, J.M.2
  • 65
    • 34247562576 scopus 로고    scopus 로고
    • Syndrome-causing mutations of the BLM gene in persons in the Bloom's Syndrome Registry
    • German J, Sanz MM, Ciocci S, Ye TZ, Ellis NA. Syndrome-causing mutations of the BLM gene in persons in the Bloom's Syndrome Registry. Hum Mutat. 2007;28:743-53.
    • (2007) Hum Mutat , vol.28 , pp. 743-753
    • German, J.1    Sanz, M.M.2    Ciocci, S.3    Ye, T.Z.4    Ellis, N.A.5
  • 66
    • 0032964641 scopus 로고    scopus 로고
    • The DNA helicase activity of BLM is necessary for the correction of the genomic instability of bloom syndrome cells
    • Neff NF, Ellis NA, Ye TZ, et al. The DNA helicase activity of BLM is necessary for the correction of the genomic instability of bloom syndrome cells. Mol Biol Cell. 1999;10:665-76.
    • (1999) Mol Biol Cell , vol.10 , pp. 665-676
    • Neff, N.F.1    Ellis, N.A.2    Ye, T.Z.3
  • 67
    • 0032547953 scopus 로고    scopus 로고
    • Point mutations causing Bloom's syndrome abolish ATPase and DNA helicase activities of the BLM protein
    • Bahr A, De Graeve F, Kedinger C, Chatton B. Point mutations causing Bloom's syndrome abolish ATPase and DNA helicase activities of the BLM protein. Oncogene. 1998;17:2565-71.
    • (1998) Oncogene , vol.17 , pp. 2565-2571
    • Bahr, A.1    De Graeve, F.2    Kedinger, C.3    Chatton, B.4
  • 68
    • 19844372703 scopus 로고    scopus 로고
    • Structural and functional characterizations reveal the importance of a zinc binding domain in Bloom's syndrome helicase
    • Guo RB, Rigolet P, Zargarian L, Fermandjian S, Xi XG. Structural and functional characterizations reveal the importance of a zinc binding domain in Bloom's syndrome helicase. Nucleic Acids Res. 2005;33(10):3109-24.
    • (2005) Nucleic Acids Res , vol.33 , Issue.10 , pp. 3109-3124
    • Guo, R.B.1    Rigolet, P.2    Zargarian, L.3    Fermandjian, S.4    Xi, X.G.5
  • 69
    • 35648999125 scopus 로고    scopus 로고
    • Structural and functional analyses of disease-causing missense mutations in Bloom syndrome protein
    • Guo RB, Rigolet P, Ren H, et al. Structural and functional analyses of disease-causing missense mutations in Bloom syndrome protein. Nucleic Acids Res. 2007;35:6297-310.
    • (2007) Nucleic Acids Res , vol.35 , pp. 6297-6310
    • Guo, R.B.1    Rigolet, P.2    Ren, H.3
  • 70
    • 0035980070 scopus 로고    scopus 로고
    • Functional interaction of p53 and BLM DNA helicase in apoptosis
    • Wang XW, Tseng A, Ellis NA, et al. Functional interaction of p53 and BLM DNA helicase in apoptosis. J Biol Chem. 2001;276:32948-55.
    • (2001) J Biol Chem , vol.276 , pp. 32948-32955
    • Wang, X.W.1    Tseng, A.2    Ellis, N.A.3
  • 71
    • 15844409553 scopus 로고    scopus 로고
    • Positional cloning of the Werner's syndrome gene
    • Yu CE, Oshima J, Fu YH, et al. Positional cloning of the Werner's syndrome gene. Science. 1996;272:258-62.
    • (1996) Science , vol.272 , pp. 258-262
    • Yu, C.E.1    Oshima, J.2    Fu, Y.H.3
  • 72
    • 0035799620 scopus 로고    scopus 로고
    • Diverged nuclear localization of Werner helicase in human and mouse cells
    • Suzuki T, Shiratori M, Furuichi Y, Matsumoto T. Diverged nuclear localization of Werner helicase in human and mouse cells. Oncogene. 2001;20:2551-8.
    • (2001) Oncogene , vol.20 , pp. 2551-2558
    • Suzuki, T.1    Shiratori, M.2    Furuichi, Y.3    Matsumoto, T.4
  • 73
    • 77954025436 scopus 로고    scopus 로고
    • WRN mutations in Werner syndrome patients: Genomic rearrangements, unusual intronic mutations and ethnic-speci fi c alterations
    • Friedrich K, Lee L, Leistritz DF, et al. WRN mutations in Werner syndrome patients: genomic rearrangements, unusual intronic mutations and ethnic-speci fi c alterations. Hum Genet. 2010;128:103-11.
    • (2010) Hum Genet , vol.128 , pp. 103-111
    • Friedrich, K.1    Lee, L.2    Leistritz, D.F.3
  • 74
    • 33744990645 scopus 로고    scopus 로고
    • The spectrum of WRN mutations in Werner syndrome patients
    • Huang S, Lee L, Hanson NB, et al. The spectrum of WRN mutations in Werner syndrome patients. Hum Mutat. 2006;27:558-67.
    • (2006) Hum Mutat , vol.27 , pp. 558-567
    • Huang, S.1    Lee, L.2    Hanson, N.B.3
  • 75
    • 33746763080 scopus 로고    scopus 로고
    • Werner syndrome and mutations of the WRN and LMNA genes in France
    • Uhrhammer NA, Lafarge L, Dos SL, et al. Werner syndrome and mutations of the WRN and LMNA genes in France. Hum Mutat. 2006;27:718-9.
    • (2006) Hum Mutat , vol.27 , pp. 718-719
    • Uhrhammer, N.A.1    Lafarge, L.2    Dos, S.L.3
  • 76
    • 1842685207 scopus 로고    scopus 로고
    • The Werner syndrome protein has separable recombination and survival functions
    • (Amst)
    • Swanson C, Saintigny Y, Emond MJ, Monnat Jr RJ. The Werner syndrome protein has separable recombination and survival functions. DNA Repair (Amst). 2004;3:475-82.
    • (2004) DNA Repair , vol.3 , pp. 475-482
    • Swanson, C.1    Saintigny, Y.2    Emond, M.J.3    Monnat Jr., R.J.4
  • 77
    • 0141740425 scopus 로고    scopus 로고
    • WRN the protein de fi cient in Werner syndrome plays a critical structural role in optimizing DNA repair
    • Chen L, Huang S, Lee L, et al. WRN, the protein de fi cient in Werner syndrome, plays a critical structural role in optimizing DNA repair. Aging Cell. 2003;2:191-9.
    • (2003) Aging Cell , vol.2 , pp. 191-199
    • Chen, L.1    Huang, S.2    Lee, L.3
  • 78
    • 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, 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
  • 79
    • 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, 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
  • 80
    • 16944363270 scopus 로고    scopus 로고
    • A mutation in the XPB/ERCC3 DNA repair transcription gene, associated with trichothiodystrophy
    • Weeda G, Eveno E, Donker I, et al. A mutation in the XPB/ERCC3 DNA repair transcription gene, associated with trichothiodystrophy. Am J Hum Genet. 1997;60:320-9.
    • (1997) Am J Hum Genet , vol.60 , pp. 320-329
    • Weeda, G.1    Eveno, E.2    Donker, I.3
  • 81
    • 0033010376 scopus 로고    scopus 로고
    • The relative expression of mutated XPB genes results in xeroderma pigmentosum/Cockayne's syndrome or trichothiodystrophy cellular phenotypes
    • Riou L, Zeng L, Chevallier-Lagente O, et al. The relative expression of mutated XPB genes results in xeroderma pigmentosum/Cockayne's syndrome or trichothiodystrophy cellular phenotypes. Hum Mol Genet. 1999;8:1125-33.
    • (1999) Hum Mol Genet , vol.8 , pp. 1125-1133
    • Riou, L.1    Zeng, L.2    Chevallier-Lagente, O.3
  • 82
    • 58149163606 scopus 로고    scopus 로고
    • Twinkle mutations associated with autosomal dominant progressive external ophthalmoplegia lead to impaired helicase function and in vivo mtDNA replication stalling
    • Goffart S, Cooper HM, Tyynismaa H, Wanrooij S, Suomalainen A, Spelbrink JN. Twinkle mutations associated with autosomal dominant progressive external ophthalmoplegia lead to impaired helicase function and in vivo mtDNA replication stalling. Hum Mol Genet. 2009;18:328-40.
    • (2009) Hum Mol Genet , vol.18 , pp. 328-340
    • Goffart, S.1    Cooper, H.M.2    Tyynismaa, H.3    Wanrooij, S.4    Suomalainen, A.5    Spelbrink, J.N.6
  • 83
    • 29144486726 scopus 로고    scopus 로고
    • Mutant mitochondrial helicase Twinkle causes multiple mtDNA deletions and a late-onset mitochondrial disease in mice
    • Tyynismaa H, Mjosund KP, Wanrooij S, et al. Mutant mitochondrial helicase Twinkle causes multiple mtDNA deletions and a late-onset mitochondrial disease in mice. Proc Natl Acad Sci USA. 2005;102:17687-92.
    • (2005) Proc Natl Acad Sci USA , vol.102 , pp. 17687-17692
    • Tyynismaa, H.1    Mjosund, K.P.2    Wanrooij, S.3
  • 84
    • 34250868951 scopus 로고    scopus 로고
    • Expression of catalytic mutants of the mtDNA helicase Twinkle and polymerase POLG causes distinct replication stalling phenotypes
    • Wanrooij S, Goffart S, Pohjoismaki JL, Yasukawa T, Spelbrink JN. Expression of catalytic mutants of the mtDNA helicase Twinkle and polymerase POLG causes distinct replication stalling phenotypes. Nucleic Acids Res. 2007;35:3238-51.
    • (2007) Nucleic Acids Res , vol.35 , pp. 3238-3251
    • Wanrooij, S.1    Goffart, S.2    Pohjoismaki, J.L.3    Yasukawa, T.4    Spelbrink, J.N.5
  • 85
    • 77956912166 scopus 로고    scopus 로고
    • Disease variants of the human mitochondrial DNA helicase encoded by C10orf2 differentially alter protein stability, nucleotide hydrolysis, and helicase activity
    • Longley MJ, Humble MM, Sharief FS, Copeland WC. Disease variants of the human mitochondrial DNA helicase encoded by C10orf2 differentially alter protein stability, nucleotide hydrolysis, and helicase activity. J Biol Chem. 2010;285:29690-702.
    • (2010) J Biol Chem , vol.285 , pp. 29690-29702
    • Longley, M.J.1    Humble, M.M.2    Sharief, F.S.3    Copeland, W.C.4
  • 87
    • 79959941676 scopus 로고    scopus 로고
    • Mutants of the base excision repair glycosylase, endonuclease III: DNA charge transport as a fi rst step in lesion detection
    • Romano CA, Sontz PA, Barton JK. Mutants of the base excision repair glycosylase, endonuclease III: DNA charge transport as a fi rst step in lesion detection. Biochemistry. 2011;50:6133-45.
    • (2011) Biochemistry , vol.50 , pp. 6133-6145
    • Romano, C.A.1    Sontz, P.A.2    Barton, J.K.3
  • 88
    • 43049105313 scopus 로고    scopus 로고
    • Biological contexts for DNA charge transport chemistry
    • Merino EJ, Boal AK, Barton JK. Biological contexts for DNA charge transport chemistry. Curr Opin Chem Biol. 2008;12:229-37.
    • (2008) Curr Opin Chem Biol , vol.12 , pp. 229-237
    • Merino, E.J.1    Boal, A.K.2    Barton, J.K.3
  • 89
    • 84857127226 scopus 로고    scopus 로고
    • DNA charge transport as a fi rst step in coordinating the detection of lesions by repair proteins
    • Sontz PA, Mui TP, Fuss JO, Tainer JA, Barton JK. DNA charge transport as a fi rst step in coordinating the detection of lesions by repair proteins. Proc Natl Acad Sci USA. 2012;109:1856-61.
    • (2012) Proc Natl Acad Sci USA , 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
  • 90
    • 84859747536 scopus 로고    scopus 로고
    • Rescue of replication failure by Fanconi anaemia proteins
    • Constantinou A. Rescue of replication failure by Fanconi anaemia proteins. Chromosoma. 2012;121:21-36.
    • (2012) Chromosoma , vol.121 , pp. 21-36
    • Constantinou, A.1
  • 91
    • 39449085063 scopus 로고    scopus 로고
    • DNA-damage repair; The good, the bad, and the ugly
    • Hakem R. DNA-damage repair; the good, the bad, and the ugly. EMBO J. 2008;27:589-605.
    • (2008) EMBO J , vol.27 , pp. 589-605
    • Hakem, R.1
  • 94
    • 53649090109 scopus 로고    scopus 로고
    • DNA helicases Sgs1 and BLM promote DNA double-strand break resection
    • Gravel S, Chapman JR, Magill C, Jackson SP. DNA helicases Sgs1 and BLM promote DNA double-strand break resection. Genes Dev. 2008;22:2767-72.
    • (2008) Genes Dev , vol.22 , pp. 2767-2772
    • Gravel, S.1    Chapman, J.R.2    Magill, C.3    Jackson, S.P.4
  • 96
    • 79951813659 scopus 로고    scopus 로고
    • Interaction between the helicases genetically linked to Fanconi anemia group J and Bloom's syndrome
    • Suhasini AN, Rawtani NA, Wu Y, et al. Interaction between the helicases genetically linked to Fanconi anemia group J and Bloom's syndrome. EMBO J. 2011;30:692-705.
    • (2011) EMBO J , vol.30 , pp. 692-705
    • Suhasini, A.N.1    Rawtani, N.A.2    Wu, Y.3
  • 97
    • 24944575242 scopus 로고    scopus 로고
    • BACH1 is critical for homologous recombination and appears to be the Fanconi anemia gene product FANCJ
    • Litman R, Peng M, Jin Z, et al. BACH1 is critical for homologous recombination and appears to be the Fanconi anemia gene product FANCJ. Cancer Cell. 2005;8:255-65.
    • (2005) Cancer Cell , vol.8 , pp. 255-265
    • Litman, R.1    Peng, M.2    Jin, Z.3
  • 98
    • 84655170302 scopus 로고    scopus 로고
    • Fanconi anemia and Bloom's syndrome crosstalk through FANCJ-BLM helicase interaction
    • Suhasini AN, Brosh Jr RM. Fanconi anemia and Bloom's syndrome crosstalk through FANCJ-BLM helicase interaction. Trends Genet. 2012;28:7-13.
    • (2012) Trends Genet , vol.28 , pp. 7-13
    • Suhasini, A.N.1    Brosh Jr., R.M.2
  • 99
    • 33748428875 scopus 로고    scopus 로고
    • The DNA repair helicases XPD and FancJ have essential Iron-Sulfur domains
    • Rudolf J, Makrantoni V, Ingledew WJ, Stark MJ, White MF. The DNA repair helicases XPD and FancJ have essential Iron-Sulfur domains. Mol Cell. 2006;23:801-8.
    • (2006) Mol Cell , vol.23 , pp. 801-808
    • Rudolf, J.1    Makrantoni, V.2    Ingledew, W.J.3    Stark, M.J.4    White, M.F.5
  • 100
    • 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, 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
  • 101
    • 43949110271 scopus 로고    scopus 로고
    • Structure of the DNA repair helicase XPD
    • Liu H, Rudolf J, Johnson KA, et al. Structure of the DNA repair helicase XPD. Cell. 2008;133:801-12.
    • (2008) Cell , vol.133 , pp. 801-812
    • Liu, H.1    Rudolf, J.2    Johnson, K.A.3
  • 102
    • 45849119445 scopus 로고    scopus 로고
    • Crystal structure of the FeS cluster-containing nucleotide excision repair helicase XPD
    • Wolski SC, Kuper J, Hanzelmann P, et al. Crystal structure of the FeS cluster-containing nucleotide excision repair helicase XPD. PLoS Biol. 2008;6:e149.
    • (2008) PLoS Biol , vol.6
    • Wolski, S.C.1    Kuper, J.2    Hanzelmann, P.3
  • 103
    • 38349091095 scopus 로고    scopus 로고
    • The iron-containing domain is essential in Rad3 helicases for coupling of ATP hydrolysis to DNA translocation and for targeting the helicase to the single-stranded DNA-double-stranded DNA junction
    • Pugh RA, Honda M, Leesley H, et al. The iron-containing domain is essential in Rad3 helicases for coupling of ATP hydrolysis to DNA translocation and for targeting the helicase to the single-stranded DNA-double-stranded DNA junction. J Biol Chem. 2008;283:1732-43.
    • (2008) J Biol Chem , vol.283 , pp. 1732-1743
    • Pugh, R.A.1    Honda, M.2    Leesley, H.3
  • 104
    • 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. Functional and structural studies of the nucleotide excision repair helicase XPD suggest a polarity for DNA translocation. EMBO J. 2011;31:494-502.
    • (2011) EMBO J , vol.31 , pp. 494-502
    • Kuper, J.1    Wolski, S.C.2    Michels, G.3    Kisker, C.4
  • 105
    • 84857194573 scopus 로고    scopus 로고
    • Regulation of translocation polarity by helicase domain 1 in SF2B helicases
    • Pugh RA, Wu CG, Spies M. Regulation of translocation polarity by helicase domain 1 in SF2B helicases. EMBO J. 2011;31:503-14.
    • (2011) EMBO J , vol.31 , pp. 503-514
    • Pugh, R.A.1    Wu, C.G.2    Spies, M.3
  • 106
    • 84861551208 scopus 로고    scopus 로고
    • DNA helicase and helicase-nuclease enzymes with a conserved ironsulfur cluster
    • Wu Y, Brosh Jr RM. DNA helicase and helicase-nuclease enzymes with a conserved ironsulfur cluster. Nucleic Acids Res. 2012;40(10):4247-60.
    • (2012) Nucleic Acids Res , vol.40 , Issue.10 , pp. 4247-4260
    • Wu, Y.1    Brosh Jr., R.M.2
  • 107
    • 65349085023 scopus 로고    scopus 로고
    • Hitting the bull's eye: Novel directed cancer therapy through helicase-targeted synthetic lethality
    • Aggarwal M, Brosh Jr RM. Hitting the bull's eye: novel directed cancer therapy through helicase-targeted synthetic lethality. J Cell Biochem. 2009;106:758-63.
    • (2009) J Cell Biochem , vol.106 , pp. 758-763
    • Aggarwal, M.1    Brosh Jr., R.M.2
  • 108
    • 79952127438 scopus 로고    scopus 로고
    • Inhibition of helicase activity by a small molecule impairs Werner syndrome helicase (WRN) function in the cellular response to DNA damage or replication stress
    • Aggarwal M, Sommers JA, Shoemaker RH, Brosh Jr RM. Inhibition of helicase activity by a small molecule impairs Werner syndrome helicase (WRN) function in the cellular response to DNA damage or replication stress. Proc Natl Acad Sci USA. 2011;108:1525-30.
    • (2011) Proc Natl Acad Sci USA , vol.108 , pp. 1525-1530
    • Aggarwal, M.1    Sommers, J.A.2    Shoemaker, R.H.3    Brosh Jr., R.M.4


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.