메뉴 건너뛰기




Volumn 351, Issue 3, 2005, Pages 545-561

The structural basis for substrate specificity in DNA topoisomerase IV

Author keywords

ATPase; Decatenation; DNA binding; Supercoiling; pinwheel

Indexed keywords

DIMER; DNA TOPOISOMERASE (ATP HYDROLYSING); DNA TOPOISOMERASE (ATP HYDROLYSING) A; DNA TOPOISOMERASE IV; PROTEIN PARC;

EID: 22544467771     PISSN: 00222836     EISSN: None     Source Type: Journal    
DOI: 10.1016/j.jmb.2005.06.029     Document Type: Article
Times cited : (130)

References (80)
  • 2
    • 0020322130 scopus 로고
    • A topological model for transcription based on unwinding angle analysis of E. coli RNA polymerase binary, initiation and ternary complexes
    • H.B. Gamper, and J.E. Hearst A topological model for transcription based on unwinding angle analysis of E. coli RNA polymerase binary, initiation and ternary complexes Cell 29 1982 81 90
    • (1982) Cell , vol.29 , pp. 81-90
    • Gamper, H.B.1    Hearst, J.E.2
  • 3
    • 0023433855 scopus 로고
    • Supercoiling of the DNA template during transcription
    • L.F. Liu, and J.C. Wang Supercoiling of the DNA template during transcription Proc. Natl Acad. Sci. USA 84 1987 7024 7027
    • (1987) Proc. Natl Acad. Sci. USA , vol.84 , pp. 7024-7027
    • Liu, L.F.1    Wang, J.C.2
  • 4
    • 0019202180 scopus 로고
    • Catenation and supercoiling in the products of bacteriophage lambda integrative recombination in vitro
    • K. Mizuuchi, M. Gellert, R.A. Weisberg, and H.A. Nash Catenation and supercoiling in the products of bacteriophage lambda integrative recombination in vitro J. Mol. Biol. 141 1980 485 494
    • (1980) J. Mol. Biol. , vol.141 , pp. 485-494
    • Mizuuchi, K.1    Gellert, M.2    Weisberg, R.A.3    Nash, H.A.4
  • 5
    • 0022518195 scopus 로고
    • Biochemical topology: Applications to DNA recombination and replication
    • S.A. Wasserman, and N.R. Cozzarelli Biochemical topology: applications to DNA recombination and replication Science 232 1986 951 960
    • (1986) Science , vol.232 , pp. 951-960
    • Wasserman, S.A.1    Cozzarelli, N.R.2
  • 7
    • 2442599792 scopus 로고    scopus 로고
    • Structure, molecular mechanisms, and evolutionary relationships in DNA topoisomerases
    • K.D. Corbett, and J.M. Berger Structure, molecular mechanisms, and evolutionary relationships in DNA topoisomerases Annu. Rev. Biophys. Biomol. Struct. 33 2004 95 118
    • (2004) Annu. Rev. Biophys. Biomol. Struct. , vol.33 , pp. 95-118
    • Corbett, K.D.1    Berger, J.M.2
  • 8
    • 0031695155 scopus 로고    scopus 로고
    • Moving one DNA double helix through another by a type II DNA topoisomerase: The story of a simple molecular machine
    • J.C. Wang Moving one DNA double helix through another by a type II DNA topoisomerase: the story of a simple molecular machine Quart. Rev. Biophys. 31 1998 107 144
    • (1998) Quart. Rev. Biophys. , vol.31 , pp. 107-144
    • Wang, J.C.1
  • 9
    • 0034923502 scopus 로고    scopus 로고
    • DNA topoisomerases: Structure, function, and mechanism
    • J.J. Champoux DNA topoisomerases: structure, function, and mechanism Annu. Rev. Biochem. 70 2001 369 413
    • (2001) Annu. Rev. Biochem. , vol.70 , pp. 369-413
    • Champoux, J.J.1
  • 10
    • 0036085460 scopus 로고    scopus 로고
    • Cellular roles of topoisomerases: A molecular perspective
    • J.C. Wang Cellular roles of topoisomerases: a molecular perspective Nature Rev. Mol. Cell. Biol. 3 2002 430 440
    • (2002) Nature Rev. Mol. Cell. Biol. , vol.3 , pp. 430-440
    • Wang, J.C.1
  • 12
    • 0023664708 scopus 로고
    • In vitro assembly of a prepriming complex at the origin of the Escherichia coli chromosome
    • B.E. Funnell, T.A. Baker, and A. Kornberg In vitro assembly of a prepriming complex at the origin of the Escherichia coli chromosome J. Biol. Chem. 262 1987 10327 10334
    • (1987) J. Biol. Chem. , vol.262 , pp. 10327-10334
    • Funnell, B.E.1    Baker, T.A.2    Kornberg, A.3
  • 14
    • 0024578495 scopus 로고
    • DNA supercoiling and prokaryotic transcription
    • G.J. Pruss, and K. Drlica DNA supercoiling and prokaryotic transcription Cell 56 1989 521 523
    • (1989) Cell , vol.56 , pp. 521-523
    • Pruss, G.J.1    Drlica, K.2
  • 16
    • 0028858007 scopus 로고
    • Roles of topoisomerase IV and DNA gyrase in DNA unlinking during replication in Escherichia coli
    • E.L. Zechiedrich, and N.R. Cozzarelli Roles of topoisomerase IV and DNA gyrase in DNA unlinking during replication in Escherichia coli Genes Dev. 9 1995 2859 2869
    • (1995) Genes Dev. , vol.9 , pp. 2859-2869
    • Zechiedrich, E.L.1    Cozzarelli, N.R.2
  • 17
    • 0026712869 scopus 로고
    • The role of topoisomerase IV in partitioning bacterial replicons and the structure of catenated intermediates in DNA replication
    • D.E. Adams, E.M. Shekhtman, E.L. Zechiedrich, M.B. Schmid, and N.R. Cozzarelli The role of topoisomerase IV in partitioning bacterial replicons and the structure of catenated intermediates in DNA replication Cell 71 1992 277 288
    • (1992) Cell , vol.71 , pp. 277-288
    • Adams, D.E.1    Shekhtman, E.M.2    Zechiedrich, E.L.3    Schmid, M.B.4    Cozzarelli, N.R.5
  • 18
    • 0025027077 scopus 로고
    • New topoisomerase essential for chromosome segregation in E. coli
    • J. Kato, Y. Nishimura, R. Imamura, H. Niki, S. Hiraga, and H. Suzuki New topoisomerase essential for chromosome segregation in E. coli Cell 63 1990 393 404
    • (1990) Cell , vol.63 , pp. 393-404
    • Kato, J.1    Nishimura, Y.2    Imamura, R.3    Niki, H.4    Hiraga, S.5    Suzuki, H.6
  • 20
    • 0017968152 scopus 로고
    • Micrococcus luteus DNA gyrase: Active components and a model for its supercoiling of DNA
    • L.F. Liu, and J.C. Wang Micrococcus luteus DNA gyrase: active components and a model for its supercoiling of DNA Proc. Natl Acad. Sci. USA 75 1978 2098 2102
    • (1978) Proc. Natl Acad. Sci. USA , vol.75 , pp. 2098-2102
    • Liu, L.F.1    Wang, J.C.2
  • 21
    • 0038782340 scopus 로고
    • DNA gyrase: Subunit structure and ATPase activity of the purified enzyme
    • K. Mizuuchi, M.H. O'Dea, and M. Gellert DNA gyrase: subunit structure and ATPase activity of the purified enzyme Proc. Natl Acad. Sci. USA 75 1978 5960 5963
    • (1978) Proc. Natl Acad. Sci. USA , vol.75 , pp. 5960-5963
    • Mizuuchi, K.1    O'Dea, M.H.2    Gellert, M.3
  • 22
    • 0001949962 scopus 로고    scopus 로고
    • Bacterial diversity based on type II DNA topoisomerase genes
    • W.M. Huang Bacterial diversity based on type II DNA topoisomerase genes Annu. Rev. Genet. 30 1996 79 107
    • (1996) Annu. Rev. Genet. , vol.30 , pp. 79-107
    • Huang, W.M.1
  • 23
    • 0023664670 scopus 로고
    • DNA gyrase-catalyzed decatenation of multiply linked DNA dimers
    • K.J. Marians DNA gyrase-catalyzed decatenation of multiply linked DNA dimers J. Biol. Chem. 262 1987 10362 10368
    • (1987) J. Biol. Chem. , vol.262 , pp. 10362-10368
    • Marians, K.J.1
  • 24
    • 0029856729 scopus 로고    scopus 로고
    • Contrasting enzymatic activities of topoisomerase IV and DNA gyrase from Escherichia coli
    • C. Ullsperger, and N.R. Cozzarelli Contrasting enzymatic activities of topoisomerase IV and DNA gyrase from Escherichia coli J. Biol. Chem. 271 1996 31549 31555
    • (1996) J. Biol. Chem. , vol.271 , pp. 31549-31555
    • Ullsperger, C.1    Cozzarelli, N.R.2
  • 25
    • 0025758726 scopus 로고
    • The C-terminal domain of the Escherichia coli DNA gyrase a subunit is a DNA-binding protein
    • R.J. Reece, and A. Maxwell The C-terminal domain of the Escherichia coli DNA gyrase A subunit is a DNA-binding protein Nucl. Acids Res. 19 1991 1399 1405
    • (1991) Nucl. Acids Res. , vol.19 , pp. 1399-1405
    • Reece, R.J.1    Maxwell, A.2
  • 26
    • 0029955899 scopus 로고    scopus 로고
    • Conversion of DNA gyrase into a conventional type II topoisomerase
    • S.C. Kampranis, and A. Maxwell Conversion of DNA gyrase into a conventional type II topoisomerase Proc. Natl Acad. Sci. USA 93 1996 14416 14421
    • (1996) Proc. Natl Acad. Sci. USA , vol.93 , pp. 14416-14421
    • Kampranis, S.C.1    Maxwell, A.2
  • 27
    • 2442611949 scopus 로고    scopus 로고
    • The C-terminal domain of DNA gyrase a adopts a DNA-bending β-pinwheel fold
    • K.D. Corbett, R.K. Shultzaberger, and J.M. Berger The C-terminal domain of DNA gyrase A adopts a DNA-bending β-pinwheel fold Proc. Natl Acad. Sci. USA 101 2004 7293 7298
    • (2004) Proc. Natl Acad. Sci. USA , vol.101 , pp. 7293-7298
    • Corbett, K.D.1    Shultzaberger, R.K.2    Berger, J.M.3
  • 28
    • 22544447404 scopus 로고    scopus 로고
    • A superhelical spiral in the Escherichia coli DNA gyrase a C-terminal domain imparts unidirectional supercoiling bias
    • A.J. Ruthenburg, D.M. Graybosch, J.C. Huetsch, and G.L. Verdine A superhelical spiral in the Escherichia coli DNA gyrase A C-terminal domain imparts unidirectional supercoiling bias J. Biol. Chem 2005 In the press
    • (2005) J. Biol. Chem
    • Ruthenburg, A.J.1    Graybosch, D.M.2    Huetsch, J.C.3    Verdine, G.L.4
  • 29
    • 16344371468 scopus 로고    scopus 로고
    • Computational analysis of DNA gyrase action
    • A. Vologodskii Computational analysis of DNA gyrase action Biophys. J. 87 2004 3066 3073
    • (2004) Biophys. J. , vol.87 , pp. 3066-3073
    • Vologodskii, A.1
  • 30
    • 0018666498 scopus 로고
    • A sign inversion mechanism for enzymatic supercoiling of DNA
    • P.O. Brown, and N.R. Cozzarelli A sign inversion mechanism for enzymatic supercoiling of DNA Science 206 1979 1081 1083
    • (1979) Science , vol.206 , pp. 1081-1083
    • Brown, P.O.1    Cozzarelli, N.R.2
  • 31
    • 0027490939 scopus 로고
    • Escherichia coli topoisomerase IV. Purification, characterization, subunit structure, and subunit interactions
    • H. Peng, and K.J. Marians Escherichia coli topoisomerase IV. Purification, characterization, subunit structure, and subunit interactions J. Biol. Chem. 268 1993 24481 24490
    • (1993) J. Biol. Chem. , vol.268 , pp. 24481-24490
    • Peng, H.1    Marians, K.J.2
  • 32
    • 0242582268 scopus 로고    scopus 로고
    • A physical and functional interaction between Escherichia coli FtsK and topoisomerase IV
    • O. Espeli, C. Lee, and K.J. Marians A physical and functional interaction between Escherichia coli FtsK and topoisomerase IV J. Biol. Chem. 278 2003 44639 44644
    • (2003) J. Biol. Chem. , vol.278 , pp. 44639-44644
    • Espeli, O.1    Lee, C.2    Marians, K.J.3
  • 33
    • 0342377454 scopus 로고    scopus 로고
    • Bipolar localization of Bacillus subtilis topoisomerase IV, an enzyme required for chromosome segregation
    • W.M. Huang, J.L. Libbey, P. van der Hoeven, and S.X. Yu Bipolar localization of Bacillus subtilis topoisomerase IV, an enzyme required for chromosome segregation Proc. Natl Acad. Sci. USA 95 1998 4652 4657
    • (1998) Proc. Natl Acad. Sci. USA , vol.95 , pp. 4652-4657
    • Huang, W.M.1    Libbey, J.L.2    Van Der Hoeven, P.3    Yu, S.X.4
  • 34
    • 3042634753 scopus 로고    scopus 로고
    • The topoisomerase IV ParC subunit colocalizes with the Caulobacter replisome and is required for polar localization of replication origins
    • S.C. Wang, and L. Shapiro The topoisomerase IV ParC subunit colocalizes with the Caulobacter replisome and is required for polar localization of replication origins Proc. Natl Acad. Sci. USA 101 2004 9251 9256
    • (2004) Proc. Natl Acad. Sci. USA , vol.101 , pp. 9251-9256
    • Wang, S.C.1    Shapiro, L.2
  • 35
    • 0034669232 scopus 로고    scopus 로고
    • Preferential relaxation of positively supercoiled DNA by E. coli topoisomerase IV in single-molecule and ensemble measurements
    • N.J. Crisona, T.R. Strick, D. Bensimon, V. Croquette, and N.R. Cozzarelli Preferential relaxation of positively supercoiled DNA by E. coli topoisomerase IV in single-molecule and ensemble measurements Genes Dev. 14 2000 2881 2892
    • (2000) Genes Dev. , vol.14 , pp. 2881-2892
    • Crisona, N.J.1    Strick, T.R.2    Bensimon, D.3    Croquette, V.4    Cozzarelli, N.R.5
  • 37
    • 0043194014 scopus 로고    scopus 로고
    • Single-molecule study of DNA unlinking by eukaryotic and prokaryotic type-II topoisomerases
    • G. Charvin, D. Bensimon, and V. Croquette Single-molecule study of DNA unlinking by eukaryotic and prokaryotic type-II topoisomerases Proc. Natl Acad. Sci. USA 100 2003 9820 9825
    • (2003) Proc. Natl Acad. Sci. USA , vol.100 , pp. 9820-9825
    • Charvin, G.1    Bensimon, D.2    Croquette, V.3
  • 38
    • 0028806614 scopus 로고
    • The interaction of Escherichia coli topoisomerase IV with DNA
    • H. Peng, and K.J. Marians The interaction of Escherichia coli topoisomerase IV with DNA J. Biol. Chem. 270 1995 25286 25290
    • (1995) J. Biol. Chem. , vol.270 , pp. 25286-25290
    • Peng, H.1    Marians, K.J.2
  • 39
    • 11244308067 scopus 로고    scopus 로고
    • Structure of the topoisomerase IV C-terminal domain: A broken β-propeller implies a role as geometry facilitator in catalysis
    • T.-J. Hsieh, L. Farh, W.M. Huang, and N.L. Chan Structure of the topoisomerase IV C-terminal domain: a broken β-propeller implies a role as geometry facilitator in catalysis J. Biol. Chem. 279 2004 55587 55593
    • (2004) J. Biol. Chem. , vol.279 , pp. 55587-55593
    • Hsieh, T.-J.1    Farh, L.2    Huang, W.M.3    Chan, N.L.4
  • 40
    • 0030664213 scopus 로고    scopus 로고
    • Requirement of topoisomerase IV parC and parE genes for cell cycle progression and developmental regulation in Caulobacter crescentus
    • D. Ward, and A. Newton Requirement of topoisomerase IV parC and parE genes for cell cycle progression and developmental regulation in Caulobacter crescentus Mol. Microbiol. 26 1997 897 910
    • (1997) Mol. Microbiol. , vol.26 , pp. 897-910
    • Ward, D.1    Newton, A.2
  • 42
  • 43
    • 0032947158 scopus 로고    scopus 로고
    • Quaternary changes in topoisomerase II may direct orthogonal movement of two DNA strands
    • D. Fass, C.E. Bogden, and J.M. Berger Quaternary changes in topoisomerase II may direct orthogonal movement of two DNA strands Nature Struct. Biol. 6 1999 322 326
    • (1999) Nature Struct. Biol. , vol.6 , pp. 322-326
    • Fass, D.1    Bogden, C.E.2    Berger, J.M.3
  • 44
    • 0021930326 scopus 로고
    • DNA gyrase and its complexes with DNA: Direct observation by electron microscopy
    • T. Kirchhausen, J.C. Wang, and S.C. Harrison DNA gyrase and its complexes with DNA: direct observation by electron microscopy Cell 41 1985 933 943
    • (1985) Cell , vol.41 , pp. 933-943
    • Kirchhausen, T.1    Wang, J.C.2    Harrison, S.C.3
  • 45
    • 13844275625 scopus 로고    scopus 로고
    • Small-angle X-ray scattering reveals the solution structure of the full-length DNA gyrase a subunit
    • L. Costenaro, J.G. Grossmann, C. Ebel, and A. Maxwell Small-angle X-ray scattering reveals the solution structure of the full-length DNA gyrase A subunit Structure 13 2005 287 295
    • (2005) Structure , vol.13 , pp. 287-295
    • Costenaro, L.1    Grossmann, J.G.2    Ebel, C.3    Maxwell, A.4
  • 46
    • 0026536335 scopus 로고
    • Solution structure of a calmodulin-target peptide complex by multidimensional NMR
    • M. Ikura, G.M. Clore, A.M. Gronenborn, G. Zhu, C.B. Klee, and A. Bax Solution structure of a calmodulin-target peptide complex by multidimensional NMR Science 256 1992 632 638
    • (1992) Science , vol.256 , pp. 632-638
    • Ikura, M.1    Clore, G.M.2    Gronenborn, A.M.3    Zhu, G.4    Klee, C.B.5    Bax, A.6
  • 47
    • 0032563163 scopus 로고    scopus 로고
    • Crystal structure of the signal sequence binding subunit of the signal recognition particle
    • R.J. Keenan, D.M. Freymann, P. Walter, and R.M. Stroud Crystal structure of the signal sequence binding subunit of the signal recognition particle Cell 94 1998 181 191
    • (1998) Cell , vol.94 , pp. 181-191
    • Keenan, R.J.1    Freymann, D.M.2    Walter, P.3    Stroud, R.M.4
  • 48
    • 0018835270 scopus 로고
    • Formation and resolution of DNA catenanes by DNA gyrase
    • K.N. Kreuzer, and N.R. Cozzarelli Formation and resolution of DNA catenanes by DNA gyrase Cell 20 1980 245 254
    • (1980) Cell , vol.20 , pp. 245-254
    • Kreuzer, K.N.1    Cozzarelli, N.R.2
  • 49
    • 0019321213 scopus 로고
    • Decatenation of kinetoplast DNA by topoisomerases
    • J.C. Marini, K.G. Miller, and P.T. Englund Decatenation of kinetoplast DNA by topoisomerases J. Biol. Chem. 255 1980 4976 4979
    • (1980) J. Biol. Chem. , vol.255 , pp. 4976-4979
    • Marini, J.C.1    Miller, K.G.2    Englund, P.T.3
  • 50
    • 0028844115 scopus 로고
    • The structure and replication of kinetoplast DNA
    • T.A. Shapiro, and P.T. Englund The structure and replication of kinetoplast DNA Annu. Rev. Microbiol. 49 1995 117 143
    • (1995) Annu. Rev. Microbiol. , vol.49 , pp. 117-143
    • Shapiro, T.A.1    Englund, P.T.2
  • 51
    • 0018039318 scopus 로고
    • DNA-DNA gyrase complex: The wrapping of the DNA duplex outside the enzyme
    • L.F. Liu, and J.C. Wang DNA-DNA gyrase complex: the wrapping of the DNA duplex outside the enzyme Cell 15 1978 979 984
    • (1978) Cell , vol.15 , pp. 979-984
    • Liu, L.F.1    Wang, J.C.2
  • 55
    • 3242754359 scopus 로고    scopus 로고
    • DNA disentangling by type-2 topoisomerases
    • G.R. Buck, and E.L. Zechiedrich DNA disentangling by type-2 topoisomerases J. Mol. Biol. 340 2004 933 939
    • (2004) J. Mol. Biol. , vol.340 , pp. 933-939
    • Buck, G.R.1    Zechiedrich, E.L.2
  • 56
    • 0030758268 scopus 로고    scopus 로고
    • Simplification of DNA topology below equilibrium values by type II topoisomerases
    • V.V. Rybenkov, C. Ullsperger, A.V. Vologodskii, and N.R. Cozzarelli Simplification of DNA topology below equilibrium values by type II topoisomerases Science 277 1997 690 693
    • (1997) Science , vol.277 , pp. 690-693
    • Rybenkov, V.V.1    Ullsperger, C.2    Vologodskii, A.V.3    Cozzarelli, N.R.4
  • 59
    • 0037396976 scopus 로고    scopus 로고
    • Impact of genotypic studies on mycobacterial taxonomy: The new mycobacteria of the 1990s
    • E. Tortoli Impact of genotypic studies on mycobacterial taxonomy: the new mycobacteria of the 1990s Clin. Microbiol. Rev. 16 2003 319 354
    • (2003) Clin. Microbiol. Rev. , vol.16 , pp. 319-354
    • Tortoli, E.1
  • 60
    • 0032787876 scopus 로고    scopus 로고
    • Escherichia coli maltose-binding protein is uncommonly effective at promoting the solubility of polypeptides to which it is fused
    • R.B. Kapust, and D.S. Waugh Escherichia coli maltose-binding protein is uncommonly effective at promoting the solubility of polypeptides to which it is fused Protein Sci. 8 1999 1668 1674
    • (1999) Protein Sci. , vol.8 , pp. 1668-1674
    • Kapust, R.B.1    Waugh, D.S.2
  • 61
    • 0027439390 scopus 로고
    • Atomic structures of the human immunophilin FKBP-12 complexes with FK506 and rapamycin
    • G.D. Van Duyne, R.F. Standaert, P.A. Karplus, S.L. Schreiber, and J. Clardy Atomic structures of the human immunophilin FKBP-12 complexes with FK506 and rapamycin J. Mol. Biol. 229 1993 105 124
    • (1993) J. Mol. Biol. , vol.229 , pp. 105-124
    • Van Duyne, G.D.1    Standaert, R.F.2    Karplus, P.A.3    Schreiber, S.L.4    Clardy, J.5
  • 63
    • 0031059866 scopus 로고    scopus 로고
    • Processing of X-ray diffraction data collected in oscillation mode
    • Z. Otwinowski, and W. Minor Processing of X-ray diffraction data collected in oscillation mode Methods Enzymol. 276 1997 472 494
    • (1997) Methods Enzymol. , vol.276 , pp. 472-494
    • Otwinowski, Z.1    Minor, W.2
  • 64
    • 1242274650 scopus 로고    scopus 로고
    • Automated protein crystal structure determination using ELVES
    • J. Holton, and T. Alber Automated protein crystal structure determination using ELVES Proc. Natl Acad. Sci. USA 101 2004 1537 1542
    • (2004) Proc. Natl Acad. Sci. USA , vol.101 , pp. 1537-1542
    • Holton, J.1    Alber, T.2
  • 66
    • 2142689200 scopus 로고    scopus 로고
    • SOLVE and RESOLVE: Automated structure solution, density modification and model building
    • T. Terwilliger SOLVE and RESOLVE: automated structure solution, density modification and model building J. Synchrotron. Radiat. 11 2004 49 52
    • (2004) J. Synchrotron. Radiat. , vol.11 , pp. 49-52
    • Terwilliger, T.1
  • 67
    • 0028103275 scopus 로고
    • The CCP4 suite: Programs for protein crystallography
    • Collaborative Computational Project Number
    • Collaborative Computational Project Number The CCP4 suite: programs for protein crystallography Acta Crystallog. sect. D 50 1994 760 763
    • (1994) Acta Crystallog. Sect. D , vol.50 , pp. 760-763
  • 70
    • 0035182073 scopus 로고    scopus 로고
    • Use of TLS parameters to model anisotropic displacements in macromolecular refinement
    • M.D. Winn, M.N. Isupov, and G.N. Murshudov Use of TLS parameters to model anisotropic displacements in macromolecular refinement Acta Crystallog. sect. D 57 2001 122 133
    • (2001) Acta Crystallog. Sect. D , vol.57 , pp. 122-133
    • Winn, M.D.1    Isupov, M.N.2    Murshudov, G.N.3
  • 74
    • 0012293235 scopus 로고    scopus 로고
    • DeLano Scientific San Carlos, CA
    • W.L. DeLano PyMOL 2002 DeLano Scientific San Carlos, CA
    • (2002) PyMOL
    • Delano, W.L.1
  • 75
    • 0037119393 scopus 로고    scopus 로고
    • Studies of a positive supercoiling machine: Nucleotide hydrolysis and a multifunctional latch in the mechanism of reverse gyrase
    • A.C. Rodriguez Studies of a positive supercoiling machine: nucleotide hydrolysis and a multifunctional latch in the mechanism of reverse gyrase J. Biol. Chem. 277 2002 29865 29873
    • (2002) J. Biol. Chem. , vol.277 , pp. 29865-29873
    • Rodriguez, A.C.1
  • 76
    • 0041935939 scopus 로고    scopus 로고
    • US National Institutes of Health Bethesda, MD
    • W.S. Rasband ImageJ 1997-2005 US National Institutes of Health Bethesda, MD
    • (1997) ImageJ
    • Rasband, W.S.1
  • 77
    • 33044509376 scopus 로고    scopus 로고
    • (Engel, P. C., ed.), chapter 6. BIOS Scientific Publishers and Academic Press, San Diego, CA, USA.
    • Clarke, A. R. (1996). In Enzymology, Labfax (Engel, P. C., ed.), chapter 6. BIOS Scientific Publishers and Academic Press, San Diego, CA, USA.
    • (1996) Enzymology, Labfax
    • Clarke, A.R.1
  • 80
    • 0033578684 scopus 로고    scopus 로고
    • Protein secondary structure prediction based on position-specific scoring matrices
    • D.T. Jones Protein secondary structure prediction based on position-specific scoring matrices J. Mol. Biol. 292 1999 195 202
    • (1999) J. Mol. Biol. , vol.292 , pp. 195-202
    • Jones, D.T.1


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.