메뉴 건너뛰기




Volumn 38, Issue 7, 2013, Pages 364-371

From keys to bulldozers: Expanding roles for winged helix domains in nucleic-acid-binding proteins

Author keywords

Helicase; Helix turn helix; Protein DNA interaction; RecQ; RNA; Z DNA

Indexed keywords

BLOOM SYNDROME HELICASE; CYCLIC AMP BINDING PROTEIN; DNA Z; DOUBLE STRANDED DNA; ELONGATION FACTOR; HELICASE; HEPATOCYTE NUCLEAR FACTOR 3GAMMA; INTERFERON REGULATORY FACTOR; LA ANTIGEN; LAMBDA EXCISION A REPRESSOR; MESSENGER RNA; METHYLATED DNA PROTEIN CYSTEINE METHYLTRANSFERASE; NUCLEIC ACID BINDING PROTEIN; RECQ HELICASE; RECQ1 HELICASE; RECQ5 HELICASE; REPLICATION FACTOR A; REPRESSOR PROTEIN; RNA HELICASE; ROTHMUND THOMSON SYNDROME HELICASE; SHORT HAIRPIN RNA; SINGLE STRANDED RNA; SKI2 RNA HELICASE; TRANSCRIPTION FACTOR E2F4; TRANSLATION ELONGATION FACTOR SELB; UNCLASSIFIED DRUG; WERNER SYNDROME PROTEIN; WINGED HELIX TRANSCRIPTION FACTOR;

EID: 84879424236     PISSN: 09680004     EISSN: None     Source Type: Journal    
DOI: 10.1016/j.tibs.2013.04.006     Document Type: Review
Times cited : (69)

References (73)
  • 1
    • 15944379232 scopus 로고    scopus 로고
    • The many faces of the helix-turn-helix domain: transcription regulation and beyond
    • Aravind L., et al. The many faces of the helix-turn-helix domain: transcription regulation and beyond. FEMS Microbiol. Rev. 2005, 29:231-262.
    • (2005) FEMS Microbiol. Rev. , vol.29 , pp. 231-262
    • Aravind, L.1
  • 2
    • 0027270989 scopus 로고
    • Co-crystal structure of the HNF-3/fork head DNA-recognition motif resembles histone H5
    • Clark K.L., et al. Co-crystal structure of the HNF-3/fork head DNA-recognition motif resembles histone H5. Nature 1993, 364:412-420.
    • (1993) Nature , vol.364 , pp. 412-420
    • Clark, K.L.1
  • 4
    • 0034708205 scopus 로고    scopus 로고
    • Structure of the winged-helix protein hRFX1 reveals a new mode of DNA binding
    • Gajiwala K.S., et al. Structure of the winged-helix protein hRFX1 reveals a new mode of DNA binding. Nature 2000, 403:916-921.
    • (2000) Nature , vol.403 , pp. 916-921
    • Gajiwala, K.S.1
  • 5
    • 0000445736 scopus 로고    scopus 로고
    • The structure of a CAP-DNA complex having two cAMP molecules bound to each monomer
    • Passner J.M., Steitz T.A. The structure of a CAP-DNA complex having two cAMP molecules bound to each monomer. Proc. Natl. Acad. Sci. U.S.A. 1997, 94:2843-2847.
    • (1997) Proc. Natl. Acad. Sci. U.S.A. , vol.94 , pp. 2843-2847
    • Passner, J.M.1    Steitz, T.A.2
  • 6
    • 29544449398 scopus 로고    scopus 로고
    • Structural basis for recognition and sequestration of UUU(OH) 3' temini of nascent RNA polymerase III transcripts by La, a rheumatic disease autoantigen
    • Teplova M., et al. Structural basis for recognition and sequestration of UUU(OH) 3' temini of nascent RNA polymerase III transcripts by La, a rheumatic disease autoantigen. Mol. Cell 2006, 21:75-85.
    • (2006) Mol. Cell , vol.21 , pp. 75-85
    • Teplova, M.1
  • 7
    • 79956294799 scopus 로고    scopus 로고
    • Forkhead transcription factors: key players in health and disease
    • Benayoun B.A., et al. Forkhead transcription factors: key players in health and disease. Trends Genet. 2011, 27:224-232.
    • (2011) Trends Genet. , vol.27 , pp. 224-232
    • Benayoun, B.A.1
  • 8
    • 0033559030 scopus 로고    scopus 로고
    • Structural basis of DNA recognition by the heterodimeric cell cycle transcription factor E2F-DP
    • Zheng N., et al. Structural basis of DNA recognition by the heterodimeric cell cycle transcription factor E2F-DP. Genes Dev. 1999, 13:666-674.
    • (1999) Genes Dev. , vol.13 , pp. 666-674
    • Zheng, N.1
  • 9
    • 77955602256 scopus 로고    scopus 로고
    • Structure of the LexA-DNA complex and implications for SOS box measurement
    • Zhang A.P.P., et al. Structure of the LexA-DNA complex and implications for SOS box measurement. Nature 2010, 466:883-886.
    • (2010) Nature , vol.466 , pp. 883-886
    • Zhang, A.P.P.1
  • 10
    • 0035515347 scopus 로고    scopus 로고
    • The ETS-domain transcription factor family
    • Sharrocks A.D. The ETS-domain transcription factor family. Nat. Rev. Mol. Cell Biol. 2001, 2:827-837.
    • (2001) Nat. Rev. Mol. Cell Biol. , vol.2 , pp. 827-837
    • Sharrocks, A.D.1
  • 11
    • 84867319935 scopus 로고    scopus 로고
    • Crystal structure and mechanism of action of the N6-methyladenine-dependent type IIM restriction endonuclease R.DpnI
    • Siwek W., et al. Crystal structure and mechanism of action of the N6-methyladenine-dependent type IIM restriction endonuclease R.DpnI. Nucleic Acids Res. 2012, 40:7563-7572.
    • (2012) Nucleic Acids Res. , vol.40 , pp. 7563-7572
    • Siwek, W.1
  • 12
    • 3543029188 scopus 로고    scopus 로고
    • DNA binding and nucleotide flipping by the human DNA repair protein AGT
    • Daniels D.S., et al. DNA binding and nucleotide flipping by the human DNA repair protein AGT. Nat. Struct. Mol. Biol. 2004, 11:714-720.
    • (2004) Nat. Struct. Mol. Biol. , vol.11 , pp. 714-720
    • Daniels, D.S.1
  • 13
    • 34347205992 scopus 로고    scopus 로고
    • Z-DNA, an active element in the genome
    • Wang G., Vasquez K.M. Z-DNA, an active element in the genome. Front. Biosci. 2007, 12:4424-4438.
    • (2007) Front. Biosci. , vol.12 , pp. 4424-4438
    • Wang, G.1    Vasquez, K.M.2
  • 14
    • 0033546005 scopus 로고    scopus 로고
    • Crystal structure of the Zalpha domain of the human editing enzyme ADAR1 bound to left-handed Z-DNA
    • Schwartz T., et al. Crystal structure of the Zalpha domain of the human editing enzyme ADAR1 bound to left-handed Z-DNA. Science 1999, 284:1841-1845.
    • (1999) Science , vol.284 , pp. 1841-1845
    • Schwartz, T.1
  • 15
    • 34047263964 scopus 로고    scopus 로고
    • A left-handed RNA double helix bound by the Z alpha domain of the RNA-editing enzyme ADAR1
    • Placido D., et al. A left-handed RNA double helix bound by the Z alpha domain of the RNA-editing enzyme ADAR1. Structure 2007, 15:395-404.
    • (2007) Structure , vol.15 , pp. 395-404
    • Placido, D.1
  • 16
    • 0034870407 scopus 로고    scopus 로고
    • Structure of the DLM-1-Z-DNA complex reveals a conserved family of Z-DNA-binding proteins
    • Schwartz T., et al. Structure of the DLM-1-Z-DNA complex reveals a conserved family of Z-DNA-binding proteins. Nat. Struct. Biol. 2001, 8:761-765.
    • (2001) Nat. Struct. Biol. , vol.8 , pp. 761-765
    • Schwartz, T.1
  • 17
    • 1542267839 scopus 로고    scopus 로고
    • The solution structure of the N-terminal domain of E3L shows a tyrosine conformation that may explain its reduced affinity to Z-DNA in vitro
    • Kahmann J.D., et al. The solution structure of the N-terminal domain of E3L shows a tyrosine conformation that may explain its reduced affinity to Z-DNA in vitro. Proc. Natl. Acad. Sci. U.S.A. 2004, 101:2712-2717.
    • (2004) Proc. Natl. Acad. Sci. U.S.A. , vol.101 , pp. 2712-2717
    • Kahmann, J.D.1
  • 18
    • 13444267286 scopus 로고    scopus 로고
    • A PKR-like eukaryotic initiation factor 2alpha kinase from zebrafish contains Z-DNA binding domains instead of dsRNA binding domains
    • Rothenburg S., et al. A PKR-like eukaryotic initiation factor 2alpha kinase from zebrafish contains Z-DNA binding domains instead of dsRNA binding domains. Proc. Natl. Acad. Sci. U.S.A. 2005, 102:1602-1607.
    • (2005) Proc. Natl. Acad. Sci. U.S.A. , vol.102 , pp. 1602-1607
    • Rothenburg, S.1
  • 19
    • 81855226703 scopus 로고    scopus 로고
    • ADAR proteins: structure and catalytic mechanism
    • Goodman R.A., et al. ADAR proteins: structure and catalytic mechanism. Curr. Top. Microbiol. Immunol. 2012, 353:1-33.
    • (2012) Curr. Top. Microbiol. Immunol. , vol.353 , pp. 1-33
    • Goodman, R.A.1
  • 20
    • 22544461042 scopus 로고    scopus 로고
    • The crystal structure of the Zbeta domain of the RNA-editing enzyme ADAR1 reveals distinct conserved surfaces among Z-domains
    • Athanasiadis A., et al. The crystal structure of the Zbeta domain of the RNA-editing enzyme ADAR1 reveals distinct conserved surfaces among Z-domains. J. Mol. Biol. 2005, 351:496-507.
    • (2005) J. Mol. Biol. , vol.351 , pp. 496-507
    • Athanasiadis, A.1
  • 21
    • 34547143110 scopus 로고    scopus 로고
    • DAI (DLM-1/ZBP1) is a cytosolic DNA sensor and an activator of innate immune response
    • Takaoka A., et al. DAI (DLM-1/ZBP1) is a cytosolic DNA sensor and an activator of innate immune response. Nature 2007, 448:501-505.
    • (2007) Nature , vol.448 , pp. 501-505
    • Takaoka, A.1
  • 22
    • 79955567592 scopus 로고    scopus 로고
    • Solution structure of the Zbeta domain of human DNA-dependent activator of IFN-regulatory factors and its binding modes to B- and Z-DNAs
    • Kim K., et al. Solution structure of the Zbeta domain of human DNA-dependent activator of IFN-regulatory factors and its binding modes to B- and Z-DNAs. Proc. Natl. Acad. Sci. U.S.A. 2011, 108:6921-6926.
    • (2011) Proc. Natl. Acad. Sci. U.S.A. , vol.108 , pp. 6921-6926
    • Kim, K.1
  • 23
    • 58549108193 scopus 로고    scopus 로고
    • The crystal structure of the second Z-DNA binding domain of human DAI (ZBP1) in complex with Z-DNA reveals an unusual binding mode to Z-DNA
    • Ha S.C., et al. The crystal structure of the second Z-DNA binding domain of human DAI (ZBP1) in complex with Z-DNA reveals an unusual binding mode to Z-DNA. Proc. Natl. Acad. Sci. U.S.A. 2008, 105:20671-20676.
    • (2008) Proc. Natl. Acad. Sci. U.S.A. , vol.105 , pp. 20671-20676
    • Ha, S.C.1
  • 24
    • 15544371486 scopus 로고    scopus 로고
    • Structural basis for mRNA recognition by elongation factor SelB
    • Yoshizawa S., et al. Structural basis for mRNA recognition by elongation factor SelB. Nat. Struct. Mol. Biol. 2005, 12:198-203.
    • (2005) Nat. Struct. Mol. Biol. , vol.12 , pp. 198-203
    • Yoshizawa, S.1
  • 25
    • 34250005188 scopus 로고    scopus 로고
    • Structural insight into a molecular switch in tandem winged-helix motifs from elongation factor SelB
    • Soler N., et al. Structural insight into a molecular switch in tandem winged-helix motifs from elongation factor SelB. J. Mol. Biol. 2007, 370:728-741.
    • (2007) J. Mol. Biol. , vol.370 , pp. 728-741
    • Soler, N.1
  • 27
    • 1842577742 scopus 로고    scopus 로고
    • Structural analysis of cooperative RNA binding by the La motif and central RRM domain of human La protein
    • Alfano C., et al. Structural analysis of cooperative RNA binding by the La motif and central RRM domain of human La protein. Nat. Struct. Mol. Biol. 2004, 11:323-329.
    • (2004) Nat. Struct. Mol. Biol. , vol.11 , pp. 323-329
    • Alfano, C.1
  • 28
    • 78149434190 scopus 로고    scopus 로고
    • The RecQ DNA helicases in DNA repair
    • Bernstein K.A., et al. The RecQ DNA helicases in DNA repair. Annu. Rev. Genet. 2010, 44:393-417.
    • (2010) Annu. Rev. Genet. , vol.44 , pp. 393-417
    • Bernstein, K.A.1
  • 29
    • 84873667075 scopus 로고    scopus 로고
    • RecQ helicases: conserved guardians of genomic integrity
    • Larsen N.B., Hickson I.D. RecQ helicases: conserved guardians of genomic integrity. Adv. Exp. Med. Biol. 2013, 767:161-184.
    • (2013) Adv. Exp. Med. Biol. , vol.767 , pp. 161-184
    • Larsen, N.B.1    Hickson, I.D.2
  • 30
    • 79953158070 scopus 로고    scopus 로고
    • A prominent β-hairpin structure in the winged-helix domain of RECQ1 is required for DNA unwinding and oligomer formation
    • Lucic B., et al. A prominent β-hairpin structure in the winged-helix domain of RECQ1 is required for DNA unwinding and oligomer formation. Nucleic Acids Res. 2011, 39:1703-1717.
    • (2011) Nucleic Acids Res. , vol.39 , pp. 1703-1717
    • Lucic, B.1
  • 31
    • 59049103795 scopus 로고    scopus 로고
    • Structure of the human RECQ1 helicase reveals a putative strand-separation pin
    • Pike A.C.W., et al. Structure of the human RECQ1 helicase reveals a putative strand-separation pin. Proc. Natl. Acad. Sci. U.S.A. 2009, 106:1039-1044.
    • (2009) Proc. Natl. Acad. Sci. U.S.A. , vol.106 , pp. 1039-1044
    • Pike, A.C.W.1
  • 32
    • 75849122854 scopus 로고    scopus 로고
    • Structural basis for DNA strand separation by the unconventional winged-helix domain of RecQ helicase WRN
    • Kitano K., et al. Structural basis for DNA strand separation by the unconventional winged-helix domain of RecQ helicase WRN. Structure 2010, 18:177-187.
    • (2010) Structure , vol.18 , pp. 177-187
    • Kitano, K.1
  • 33
    • 33646100776 scopus 로고    scopus 로고
    • A conserved G4 DNA binding domain in RecQ family helicases
    • Huber M.D., et al. A conserved G4 DNA binding domain in RecQ family helicases. J. Mol. Biol. 2006, 358:1071-1080.
    • (2006) J. Mol. Biol. , vol.358 , pp. 1071-1080
    • Huber, M.D.1
  • 34
    • 84864974044 scopus 로고    scopus 로고
    • DNA binding residues in the RQC domain of Werner protein are critical for its catalytic activities
    • Tadokoro T., et al. DNA binding residues in the RQC domain of Werner protein are critical for its catalytic activities. Aging 2012, 4:417-429.
    • (2012) Aging , vol.4 , pp. 417-429
    • Tadokoro, T.1
  • 35
    • 29444432958 scopus 로고    scopus 로고
    • Solution structure of a multifunctional DNA- and protein-binding motif of human Werner syndrome protein
    • Hu J.S., et al. Solution structure of a multifunctional DNA- and protein-binding motif of human Werner syndrome protein. Proc. Natl. Acad. Sci. U.S.A. 2005, 102:18379-18384.
    • (2005) Proc. Natl. Acad. Sci. U.S.A. , vol.102 , pp. 18379-18384
    • Hu, J.S.1
  • 36
    • 0347362703 scopus 로고    scopus 로고
    • Werner syndrome protein contains three structure-specific DNA binding domains
    • von Kobbe C., et al. Werner syndrome protein contains three structure-specific DNA binding domains. J. Biol. Chem. 2003, 278:52997-53006.
    • (2003) J. Biol. Chem. , vol.278 , pp. 52997-53006
    • von Kobbe, C.1
  • 37
    • 0033515425 scopus 로고    scopus 로고
    • Crystal structures of complexes of PcrA DNA helicase with a DNA substrate indicate an inchworm mechanism
    • Velankar S.S., et al. Crystal structures of complexes of PcrA DNA helicase with a DNA substrate indicate an inchworm mechanism. Cell 1999, 97:75-84.
    • (1999) Cell , vol.97 , pp. 75-84
    • Velankar, S.S.1
  • 38
    • 33845657428 scopus 로고    scopus 로고
    • UvrD helicase unwinds DNA one base pair at a time by a two-part power stroke
    • Lee J.Y., Yang W. UvrD helicase unwinds DNA one base pair at a time by a two-part power stroke. Cell 2006, 127:1349-1360.
    • (2006) Cell , vol.127 , pp. 1349-1360
    • Lee, J.Y.1    Yang, W.2
  • 39
    • 0030740262 scopus 로고    scopus 로고
    • Major domain swiveling revealed by the crystal structures of complexes of E. coli Rep helicase bound to single-stranded DNA and ADP
    • Korolev S., et al. Major domain swiveling revealed by the crystal structures of complexes of E. coli Rep helicase bound to single-stranded DNA and ADP. Cell 1997, 90:635-647.
    • (1997) Cell , vol.90 , pp. 635-647
    • Korolev, S.1
  • 40
    • 66149148295 scopus 로고    scopus 로고
    • Mechanistic basis of 5'-3' translocation in SF1B helicases
    • Saikrishnan K., et al. Mechanistic basis of 5'-3' translocation in SF1B helicases. Cell 2009, 137:849-859.
    • (2009) Cell , vol.137 , pp. 849-859
    • Saikrishnan, K.1
  • 41
    • 34447132375 scopus 로고    scopus 로고
    • Structural basis for DNA duplex separation by a superfamily-2 helicase
    • Büttner K., et al. Structural basis for DNA duplex separation by a superfamily-2 helicase. Nat. Struct. Mol. Biol. 2007, 14:647-652.
    • (2007) Nat. Struct. Mol. Biol. , vol.14 , pp. 647-652
    • Büttner, K.1
  • 42
    • 0141865522 scopus 로고    scopus 로고
    • High-resolution structure of the E. coli RecQ helicase catalytic core
    • Bernstein D.A., et al. High-resolution structure of the E. coli RecQ helicase catalytic core. EMBO J. 2003, 22:4910-4921.
    • (2003) EMBO J. , vol.22 , pp. 4910-4921
    • Bernstein, D.A.1
  • 43
    • 84861395477 scopus 로고    scopus 로고
    • Complex activities of the human Bloom's syndrome helicase are encoded in a core region comprising the RecA and Zn-binding domains
    • Gyimesi M., et al. Complex activities of the human Bloom's syndrome helicase are encoded in a core region comprising the RecA and Zn-binding domains. Nucleic Acids Res. 2012, 40:3952-3963.
    • (2012) Nucleic Acids Res. , vol.40 , pp. 3952-3963
    • Gyimesi, M.1
  • 44
    • 30344477373 scopus 로고    scopus 로고
    • Biochemical characterization of the RECQ4 protein, mutated in Rothmund-Thomson syndrome
    • Macris M.A., et al. Biochemical characterization of the RECQ4 protein, mutated in Rothmund-Thomson syndrome. DNA Repair (Amst.) 2006, 5:172-180.
    • (2006) DNA Repair (Amst.) , vol.5 , pp. 172-180
    • Macris, M.A.1
  • 45
    • 62049085034 scopus 로고    scopus 로고
    • Dual DNA unwinding activities of the Rothmund-Thomson syndrome protein, RECQ4
    • Xu X., Liu Y. Dual DNA unwinding activities of the Rothmund-Thomson syndrome protein, RECQ4. EMBO J. 2009, 28:568-577.
    • (2009) EMBO J. , vol.28 , pp. 568-577
    • Xu, X.1    Liu, Y.2
  • 46
    • 3543007196 scopus 로고    scopus 로고
    • Human RECQ5beta, a protein with DNA helicase and strand-annealing activities in a single polypeptide
    • Garcia P.L., et al. Human RECQ5beta, a protein with DNA helicase and strand-annealing activities in a single polypeptide. EMBO J. 2004, 23:2882-2891.
    • (2004) EMBO J. , vol.23 , pp. 2882-2891
    • Garcia, P.L.1
  • 47
    • 78649877700 scopus 로고    scopus 로고
    • Structure and function of the regulatory HRDC domain from human Bloom syndrome protein
    • Kim Y.M., Choi B.S. Structure and function of the regulatory HRDC domain from human Bloom syndrome protein. Nucleic Acids Res. 2010, 38:7764-7777.
    • (2010) Nucleic Acids Res. , vol.38 , pp. 7764-7777
    • Kim, Y.M.1    Choi, B.S.2
  • 48
    • 34047267832 scopus 로고    scopus 로고
    • Crystal structure of the HRDC domain of human Werner syndrome protein, WRN
    • Kitano K., et al. Crystal structure of the HRDC domain of human Werner syndrome protein, WRN. J. Biol. Chem. 2007, 282:2717-2728.
    • (2007) J. Biol. Chem. , vol.282 , pp. 2717-2728
    • Kitano, K.1
  • 49
    • 1842861596 scopus 로고    scopus 로고
    • Three-dimensional structural views of branch migration and resolution in DNA homologous recombination
    • Yamada K., et al. Three-dimensional structural views of branch migration and resolution in DNA homologous recombination. Curr. Opin. Struct. Biol. 2004, 14:130-137.
    • (2004) Curr. Opin. Struct. Biol. , vol.14 , pp. 130-137
    • Yamada, K.1
  • 50
    • 24044482592 scopus 로고    scopus 로고
    • Structure-function analysis of the three domains of RuvB DNA motor protein
    • Ohnishi T., et al. Structure-function analysis of the three domains of RuvB DNA motor protein. J. Biol. Chem. 2005, 280:30504-30510.
    • (2005) J. Biol. Chem. , vol.280 , pp. 30504-30510
    • Ohnishi, T.1
  • 51
    • 18644379392 scopus 로고    scopus 로고
    • Crystal structure of the RuvA-RuvB complex: a structural basis for the Holliday junction migrating motor machinery
    • Yamada K., et al. Crystal structure of the RuvA-RuvB complex: a structural basis for the Holliday junction migrating motor machinery. Mol. Cell 2002, 10:671-681.
    • (2002) Mol. Cell , vol.10 , pp. 671-681
    • Yamada, K.1
  • 52
    • 0030790696 scopus 로고    scopus 로고
    • Structure of the multimodular endonuclease FokI bound to DNA
    • Wah D.A., et al. Structure of the multimodular endonuclease FokI bound to DNA. Nature 1997, 388:97-100.
    • (1997) Nature , vol.388 , pp. 97-100
    • Wah, D.A.1
  • 53
    • 35748971020 scopus 로고    scopus 로고
    • Structure of the full-length human RPA14/32 complex gives insights into the mechanism of DNA binding and complex formation
    • Deng X., et al. Structure of the full-length human RPA14/32 complex gives insights into the mechanism of DNA binding and complex formation. J. Mol. Biol. 2007, 374:865-876.
    • (2007) J. Mol. Biol. , vol.374 , pp. 865-876
    • Deng, X.1
  • 54
    • 62549112552 scopus 로고    scopus 로고
    • Atomic structures and functional implications of the archaeal RecQ-like helicase Hjm
    • Oyama T., et al. Atomic structures and functional implications of the archaeal RecQ-like helicase Hjm. BMC Struct. Biol. 2009, 9:2.
    • (2009) BMC Struct. Biol. , vol.9 , pp. 2
    • Oyama, T.1
  • 55
    • 67650296697 scopus 로고    scopus 로고
    • Structural evidence for consecutive Hel308-like modules in the spliceosomal ATPase Brr2
    • Zhang L., et al. Structural evidence for consecutive Hel308-like modules in the spliceosomal ATPase Brr2. Nat. Struct. Mol. Biol. 2009, 16:731-739.
    • (2009) Nat. Struct. Mol. Biol. , vol.16 , pp. 731-739
    • Zhang, L.1
  • 56
    • 37549033817 scopus 로고    scopus 로고
    • Crystal structure of an archaeal Ski2p-like protein from Pyrococcus horikoshii OT3
    • Zhang X., et al. Crystal structure of an archaeal Ski2p-like protein from Pyrococcus horikoshii OT3. Protein Sci. 2008, 17:136-145.
    • (2008) Protein Sci. , vol.17 , pp. 136-145
    • Zhang, X.1
  • 57
    • 84055217962 scopus 로고    scopus 로고
    • The crystal structure of S. cerevisiae Ski2, a DExH helicase associated with the cytoplasmic functions of the exosome
    • Halbach F., et al. The crystal structure of S. cerevisiae Ski2, a DExH helicase associated with the cytoplasmic functions of the exosome. RNA 2012, 18:124-134.
    • (2012) RNA , vol.18 , pp. 124-134
    • Halbach, F.1
  • 58
    • 77954952539 scopus 로고    scopus 로고
    • The crystal structure of Mtr4 reveals a novel arch domain required for rRNA processing
    • Jackson R.N., et al. The crystal structure of Mtr4 reveals a novel arch domain required for rRNA processing. EMBO J. 2010, 29:2205-2216.
    • (2010) EMBO J. , vol.29 , pp. 2205-2216
    • Jackson, R.N.1
  • 59
    • 79551503145 scopus 로고    scopus 로고
    • Winged helix domains with unknown function in Hel308 and related helicases
    • Woodman I.L., Bolt E.L. Winged helix domains with unknown function in Hel308 and related helicases. Biochem. Soc. Trans. 2011, 39:140-144.
    • (2011) Biochem. Soc. Trans. , vol.39 , pp. 140-144
    • Woodman, I.L.1    Bolt, E.L.2
  • 60
    • 84869469029 scopus 로고    scopus 로고
    • Structural analysis of the C-terminal domain of the spliceosomal helicase Prp22
    • Kudlinzki D., et al. Structural analysis of the C-terminal domain of the spliceosomal helicase Prp22. Biol. Chem. 2012, 393:1131-1140.
    • (2012) Biol. Chem. , vol.393 , pp. 1131-1140
    • Kudlinzki, D.1
  • 61
    • 77954958169 scopus 로고    scopus 로고
    • Prp43p contains a processive helicase structural architecture with a specific regulatory domain
    • Walbott H., et al. Prp43p contains a processive helicase structural architecture with a specific regulatory domain. EMBO J. 2010, 29:2194-2204.
    • (2010) EMBO J. , vol.29 , pp. 2194-2204
    • Walbott, H.1
  • 62
    • 84869227939 scopus 로고    scopus 로고
    • Roles of individual domains in the function of DHX29, an essential factor required for translation of structured mammalian mRNAs
    • Dhote V., et al. Roles of individual domains in the function of DHX29, an essential factor required for translation of structured mammalian mRNAs. Proc. Natl. Acad. Sci. U.S.A. 2012, 109:E3150-E3159.
    • (2012) Proc. Natl. Acad. Sci. U.S.A. , vol.109
    • Dhote, V.1
  • 63
    • 59649104376 scopus 로고    scopus 로고
    • Identification of the SSB binding site on E. coli RecQ reveals a conserved surface for binding SSB's C terminus
    • Shereda R.D., et al. Identification of the SSB binding site on E. coli RecQ reveals a conserved surface for binding SSB's C terminus. J. Mol. Biol. 2009, 386:612-625.
    • (2009) J. Mol. Biol. , vol.386 , pp. 612-625
    • Shereda, R.D.1
  • 64
    • 10944225939 scopus 로고    scopus 로고
    • Pathways and functions of the Werner syndrome protein
    • Lee J.W., et al. Pathways and functions of the Werner syndrome protein. Mech. Ageing Dev. 2005, 126:79-86.
    • (2005) Mech. Ageing Dev. , vol.126 , pp. 79-86
    • Lee, J.W.1
  • 65
    • 1642324918 scopus 로고    scopus 로고
    • Stimulation of flap endonuclease-1 by the Bloom's syndrome protein
    • Sharma S., et al. Stimulation of flap endonuclease-1 by the Bloom's syndrome protein. J. Biol. Chem. 2004, 279:9847-9856.
    • (2004) J. Biol. Chem. , vol.279 , pp. 9847-9856
    • Sharma, S.1
  • 66
    • 84892445196 scopus 로고    scopus 로고
    • A kulcstól a bulldózerig: szárnyas hélix domének funkcionális adaptációja DNS-köto fehérjékben
    • Harami G., et al. A kulcstól a bulldózerig: szárnyas hélix domének funkcionális adaptációja DNS-köto fehérjékben. Biokémia 2012, 36:30-42.
    • (2012) Biokémia , vol.36 , pp. 30-42
    • Harami, G.1
  • 67
    • 0032522789 scopus 로고    scopus 로고
    • RecQ helicase, in concert with RecA and SSB proteins, initiates and disrupts DNA recombination
    • Harmon F.G., Kowalczykowski S.C. RecQ helicase, in concert with RecA and SSB proteins, initiates and disrupts DNA recombination. Genes Dev. 1998, 12:1134-1144.
    • (1998) Genes Dev. , vol.12 , pp. 1134-1144
    • Harmon, F.G.1    Kowalczykowski, S.C.2
  • 68
    • 0035870569 scopus 로고    scopus 로고
    • Substrate-specific inhibition of RecQ helicase
    • Wu X., Maizels N. Substrate-specific inhibition of RecQ helicase. Nucleic Acids Res. 2001, 29:1765-1771.
    • (2001) Nucleic Acids Res. , vol.29 , pp. 1765-1771
    • Wu, X.1    Maizels, N.2
  • 69
    • 23044517287 scopus 로고    scopus 로고
    • Biochemical analysis of the DNA unwinding and strand annealing activities catalyzed by human RECQ1
    • Sharma S., et al. Biochemical analysis of the DNA unwinding and strand annealing activities catalyzed by human RECQ1. J. Biol. Chem. 2005, 280:28072-28084.
    • (2005) J. Biol. Chem. , vol.280 , pp. 28072-28084
    • Sharma, S.1
  • 70
    • 0035393720 scopus 로고    scopus 로고
    • The Bloom's and Werner's syndrome proteins are DNA structure-specific helicases
    • Mohaghegh P., et al. The Bloom's and Werner's syndrome proteins are DNA structure-specific helicases. Nucleic Acids Res. 2001, 29:2843-2849.
    • (2001) Nucleic Acids Res. , vol.29 , pp. 2843-2849
    • Mohaghegh, P.1
  • 71
    • 33646843592 scopus 로고    scopus 로고
    • Mobile D-loops are a preferred substrate for the Bloom's syndrome helicase
    • Bachrati C.Z., et al. Mobile D-loops are a preferred substrate for the Bloom's syndrome helicase. Nucleic Acids Res. 2006, 34:2269-2279.
    • (2006) Nucleic Acids Res. , vol.34 , pp. 2269-2279
    • Bachrati, C.Z.1
  • 72
    • 49649099084 scopus 로고    scopus 로고
    • The Human RecQ helicases, BLM and RECQ1, display distinct DNA substrate specificities
    • Popuri V., et al. The Human RecQ helicases, BLM and RECQ1, display distinct DNA substrate specificities. J. Biol. Chem. 2008, 283:17766-17776.
    • (2008) J. Biol. Chem. , vol.283 , pp. 17766-17776
    • Popuri, V.1
  • 73
    • 62849091779 scopus 로고    scopus 로고
    • The Werner syndrome helicase/exonuclease processes mobile D-loops through branch migration and degradation
    • Opresko P.L., et al. The Werner syndrome helicase/exonuclease processes mobile D-loops through branch migration and degradation. PLoS ONE 2009, 4:e4825.
    • (2009) PLoS ONE , vol.4
    • Opresko, P.L.1


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.