메뉴 건너뛰기




Volumn 426, Issue 12, 2014, Pages 2313-2327

The crystal structure of the anti-σ factor CnrY in complex with the σ factor CnrH shows a new structural class of anti-σ factors targeting extracytoplasmic function σ factors

Author keywords

bacterial transcription; metal resistance; protein:protein interaction; sigma factor; transmembrane signaling

Indexed keywords

SIGMA FACTOR; SIGMA FACTOR CNRH; SIGMA FACTOR CNRY; UNCLASSIFIED DRUG;

EID: 84901198801     PISSN: 00222836     EISSN: 10898638     Source Type: Journal    
DOI: 10.1016/j.jmb.2014.04.003     Document Type: Article
Times cited : (30)

References (61)
  • 1
    • 27644560257 scopus 로고    scopus 로고
    • Sigma and RNA polymerase: An on-again, off-again relationship?
    • R.A. Mooney, S.A. Darst, and R. Landick Sigma and RNA polymerase: an on-again, off-again relationship? Mol Cell 20 2005 335 345
    • (2005) Mol Cell , vol.20 , pp. 335-345
    • Mooney, R.A.1    Darst, S.A.2    Landick, R.3
  • 2
    • 84895899939 scopus 로고    scopus 로고
    • Structural basis for - 10 promoter element melting by environmentally induced sigma factors
    • S. Campagne, M.E. Marsh, G. Capitani, J.A. Vorholt, and F.H. Allain Structural basis for - 10 promoter element melting by environmentally induced sigma factors Nat Struct Mol Biol 21 2014 269 276
    • (2014) Nat Struct Mol Biol , vol.21 , pp. 269-276
    • Campagne, S.1    Marsh, M.E.2    Capitani, G.3    Vorholt, J.A.4    Allain, F.H.5
  • 3
    • 0026612797 scopus 로고
    • The sigma 70 family: Sequence conservation and evolutionary relationships
    • M. Lonetto, M. Gribskov, and C.A. Gross The sigma 70 family: sequence conservation and evolutionary relationships J Bacteriol 174 1992 3843 3849
    • (1992) J Bacteriol , vol.174 , pp. 3843-3849
    • Lonetto, M.1    Gribskov, M.2    Gross, C.A.3
  • 4
    • 0035985580 scopus 로고    scopus 로고
    • The extracytoplasmic function (ECF) sigma factors
    • J.D. Helmann The extracytoplasmic function (ECF) sigma factors Adv Microb Physiol 46 2002 47 110
    • (2002) Adv Microb Physiol , vol.46 , pp. 47-110
    • Helmann, J.D.1
  • 5
    • 0028018104 scopus 로고
    • Analysis of the Streptomyces coelicolor sigE gene reveals the existence of a subfamily of eubacterial RNA polymerase sigma factors involved in the regulation of extracytoplasmic functions
    • M.A. Lonetto, K.L. Brown, K.E. Rudd, and M.J. Buttner Analysis of the Streptomyces coelicolor sigE gene reveals the existence of a subfamily of eubacterial RNA polymerase sigma factors involved in the regulation of extracytoplasmic functions Proc Natl Acad Sci U S A 91 1994 7573 7577
    • (1994) Proc Natl Acad Sci U S A , vol.91 , pp. 7573-7577
    • Lonetto, M.A.1    Brown, K.L.2    Rudd, K.E.3    Buttner, M.J.4
  • 6
    • 0242692671 scopus 로고    scopus 로고
    • Multiple sigma subunits and the partitioning of bacterial transcription space
    • T.M. Gruber, and C.A. Gross Multiple sigma subunits and the partitioning of bacterial transcription space Annu Rev Microbiol 57 2003 441 466
    • (2003) Annu Rev Microbiol , vol.57 , pp. 441-466
    • Gruber, T.M.1    Gross, C.A.2
  • 7
    • 0037308665 scopus 로고    scopus 로고
    • Bacterial RNA polymerases: The wholo story
    • K.S. Murakami, and S.A. Darst Bacterial RNA polymerases: the wholo story Curr Opin Struct Biol 13 2003 31 39
    • (2003) Curr Opin Struct Biol , vol.13 , pp. 31-39
    • Murakami, K.S.1    Darst, S.A.2
  • 9
    • 84877013872 scopus 로고    scopus 로고
    • Signaling diversity and evolution of extracytoplasmic function (ECF) σ factors
    • T. Mascher Signaling diversity and evolution of extracytoplasmic function (ECF) σ factors Curr Opin Microbiol 16 2013 148 155
    • (2013) Curr Opin Microbiol , vol.16 , pp. 148-155
    • Mascher, T.1
  • 10
    • 70350432754 scopus 로고    scopus 로고
    • The third pillar of bacterial signal transduction: Classification of the extracytoplasmic function (ECF) sigma factor protein family
    • A. Staroń, H.J. Sofia, S. Dietrich, L.E. Ulrich, H. Liesegang, and T. Mascher The third pillar of bacterial signal transduction: classification of the extracytoplasmic function (ECF) sigma factor protein family Mol Microbiol 74 2009 557 581
    • (2009) Mol Microbiol , vol.74 , pp. 557-581
    • Staroń, A.1    Sofia, H.J.2    Dietrich, S.3    Ulrich, L.E.4    Liesegang, H.5    Mascher, T.6
  • 11
    • 34548252292 scopus 로고    scopus 로고
    • A conserved structural module regulates transcriptional responses to diverse stress signals in bacteria
    • E.A. Campbell, R. Greenwell, J.R. Anthony, S. Wang, L. Lim, and K. Das et al. A conserved structural module regulates transcriptional responses to diverse stress signals in bacteria Mol Cell 27 2007 793 805
    • (2007) Mol Cell , vol.27 , pp. 793-805
    • Campbell, E.A.1    Greenwell, R.2    Anthony, J.R.3    Wang, S.4    Lim, L.5    Das, K.6
  • 12
    • 0342751307 scopus 로고    scopus 로고
    • Regulation of the cnr cobalt and nickel resistance determinant from Ralstonia sp strain CH34
    • G. Grass, C. Grosse, and D.H. Nies Regulation of the cnr cobalt and nickel resistance determinant from Ralstonia sp. strain CH34 J Bacteriol 182 2000 1390 1398
    • (2000) J Bacteriol , vol.182 , pp. 1390-1398
    • Grass, G.1    Grosse, C.2    Nies, D.H.3
  • 13
    • 0033950956 scopus 로고    scopus 로고
    • Regulation of the cnr cobalt and nickel resistance determinant of Ralstonia eutropha (Alcaligenes eutrophus) CH34
    • C. Tibazarwa, S. Wuertz, M. Mergeay, L. Wyns, and D. van Der Lelie Regulation of the cnr cobalt and nickel resistance determinant of Ralstonia eutropha (Alcaligenes eutrophus) CH34 J Bacteriol 182 2000 1399 1409
    • (2000) J Bacteriol , vol.182 , pp. 1399-1409
    • Tibazarwa, C.1    Wuertz, S.2    Mergeay, M.3    Wyns, L.4    Van Der Lelie, D.5
  • 15
    • 84893263725 scopus 로고    scopus 로고
    • Metal sensing and signal transduction by CnrX from Cupriavidus metallidurans CH34: Role of the only methionine assessed by a functional, spectroscopic, and theoretical study
    • J. Trepreau, C. Grosse, J.M. Mouesca, G. Sarret, E. Girard, and I. Petit-Haertlein et al. Metal sensing and signal transduction by CnrX from Cupriavidus metallidurans CH34: role of the only methionine assessed by a functional, spectroscopic, and theoretical study Metallomics 6 2013 263 273
    • (2013) Metallomics , vol.6 , pp. 263-273
    • Trepreau, J.1    Grosse, C.2    Mouesca, J.M.3    Sarret, G.4    Girard, E.5    Petit-Haertlein, I.6
  • 17
    • 84861427602 scopus 로고    scopus 로고
    • Structural basis of a protein partner switch that regulates the general stress response of alpha-proteobacteria
    • J. Herrou, G. Rotskoff, Y. Luo, B. Roux, and S. Crosson Structural basis of a protein partner switch that regulates the general stress response of alpha-proteobacteria Proc Natl Acad Sci U S A 109 2012 E1415 E1423
    • (2012) Proc Natl Acad Sci U S A , vol.109
    • Herrou, J.1    Rotskoff, G.2    Luo, Y.3    Roux, B.4    Crosson, S.5
  • 18
    • 0242579382 scopus 로고    scopus 로고
    • A new class of lanthanide complexes to obtain high-phasing-power heavy-atom derivatives for macromolecular crystallography
    • E. Girard, M. Stelter, J. Vicat, and R. Kahn A new class of lanthanide complexes to obtain high-phasing-power heavy-atom derivatives for macromolecular crystallography Acta Crystallogr Sect D Biol Crystallogr 59 2003 1914 1922
    • (2003) Acta Crystallogr Sect D Biol Crystallogr , vol.59 , pp. 1914-1922
    • Girard, E.1    Stelter, M.2    Vicat, J.3    Kahn, R.4
  • 19
    • 0037071844 scopus 로고    scopus 로고
    • Crystal structure of a bacterial RNA polymerase holoenzyme at 2.6 Å resolution
    • D.G. Vassylyev, S. Sekine, O. Laptenko, J. Lee, M.N. Vassylyeva, and S. Borukhov et al. Crystal structure of a bacterial RNA polymerase holoenzyme at 2.6 Å resolution Nature 417 2002 712 719
    • (2002) Nature , vol.417 , pp. 712-719
    • Vassylyev, D.G.1    Sekine, S.2    Laptenko, O.3    Lee, J.4    Vassylyeva, M.N.5    Borukhov, S.6
  • 20
    • 0036203066 scopus 로고    scopus 로고
    • Structure of the bacterial RNA polymerase promoter specificity sigma subunit
    • E.A. Campbell, O. Muzzin, M. Chlenov, J.L. Sun, C.A. Olson, and O. Weinman et al. Structure of the bacterial RNA polymerase promoter specificity sigma subunit Mol Cell 9 2002 527 539
    • (2002) Mol Cell , vol.9 , pp. 527-539
    • Campbell, E.A.1    Muzzin, O.2    Chlenov, M.3    Sun, J.L.4    Olson, C.A.5    Weinman, O.6
  • 21
    • 83255167029 scopus 로고    scopus 로고
    • Structural basis for promoter - 10 element recognition by the bacterial RNA polymerase sigma subunit
    • A. Feklistov, and S.A. Darst Structural basis for promoter - 10 element recognition by the bacterial RNA polymerase sigma subunit Cell 147 2011 1257 1269
    • (2011) Cell , vol.147 , pp. 1257-1269
    • Feklistov, A.1    Darst, S.A.2
  • 22
    • 0037123602 scopus 로고    scopus 로고
    • Structural basis of transcription initiation: An RNA polymerase holoenzyme-DNA complex
    • K.S. Murakami, S. Masuda, E.A. Campbell, O. Muzzin, and S.A. Darst Structural basis of transcription initiation: an RNA polymerase holoenzyme-DNA complex Science 296 2002 1285 1290
    • (2002) Science , vol.296 , pp. 1285-1290
    • Murakami, K.S.1    Masuda, S.2    Campbell, E.A.3    Muzzin, O.4    Darst, S.A.5
  • 23
    • 0032735991 scopus 로고    scopus 로고
    • The interface of sigma with core RNA polymerase is extensive, conserved, and functionally specialized
    • M.M. Sharp, C.L. Chan, C.Z. Lu, M.T. Marr, S. Nechaev, and E.W. Merritt et al. The interface of sigma with core RNA polymerase is extensive, conserved, and functionally specialized Genes Dev 13 1999 3015 3026
    • (1999) Genes Dev , vol.13 , pp. 3015-3026
    • Sharp, M.M.1    Chan, C.L.2    Lu, C.Z.3    Marr, M.T.4    Nechaev, S.5    Merritt, E.W.6
  • 24
    • 0012837562 scopus 로고    scopus 로고
    • Crystal structure of Escherichia coli sigmaE with the cytoplasmic domain of its anti-sigma RseA
    • E.A. Campbell, J.L. Tupy, T.M. Gruber, S. Wang, M.M. Sharp, and C.A. Gross et al. Crystal structure of Escherichia coli sigmaE with the cytoplasmic domain of its anti-sigma RseA Mol Cell 11 2003 1067 1078
    • (2003) Mol Cell , vol.11 , pp. 1067-1078
    • Campbell, E.A.1    Tupy, J.L.2    Gruber, T.M.3    Wang, S.4    Sharp, M.M.5    Gross, C.A.6
  • 25
    • 0030980926 scopus 로고    scopus 로고
    • The C-terminal half of the anti-sigma factor FlgM, becomes structured when bound to its target, sigma 28
    • G.W. Daughdrill, M.S. Chadsey, J.E. Karlinsey, K.T. Hughes, and F.W. Dahlquist The C-terminal half of the anti-sigma factor FlgM, becomes structured when bound to its target, sigma 28 Nat Struct Biol 4 1997 285 291
    • (1997) Nat Struct Biol , vol.4 , pp. 285-291
    • Daughdrill, G.W.1    Chadsey, M.S.2    Karlinsey, J.E.3    Hughes, K.T.4    Dahlquist, F.W.5
  • 27
    • 0034725649 scopus 로고    scopus 로고
    • 70 binding site located on Escherichia coli core RNA polymerase
    • 70 binding site located on Escherichia coli core RNA polymerase J Biol Chem 275 2000 23113 23119
    • (2000) J Biol Chem , vol.275 , pp. 23113-23119
    • Arthur, T.M.1    Anthony, L.C.2    Burgess, R.R.3
  • 28
    • 4744373193 scopus 로고    scopus 로고
    • A hydrophobic patch on the flap-tip helix of E coli RNA polymerase mediates sigma(70) region 4 function
    • K. Geszvain, T.M. Gruber, R.A. Mooney, C.A. Gross, and R. Landick A hydrophobic patch on the flap-tip helix of E coli RNA polymerase mediates sigma(70) region 4 function J Mol Biol 343 2004 569 587
    • (2004) J Mol Biol , vol.343 , pp. 569-587
    • Geszvain, K.1    Gruber, T.M.2    Mooney, R.A.3    Gross, C.A.4    Landick, R.5
  • 29
    • 56049087926 scopus 로고    scopus 로고
    • X-ray structure of the metal-sensor CnrX in both the apo- and copper-bound forms
    • G. Pompidor, A.P. Maillard, E. Girard, S. Gambarelli, R. Kahn, and J. Coves X-ray structure of the metal-sensor CnrX in both the apo- and copper-bound forms FEBS Lett 582 2008 3954 3958
    • (2008) FEBS Lett , vol.582 , pp. 3954-3958
    • Pompidor, G.1    Maillard, A.P.2    Girard, E.3    Gambarelli, S.4    Kahn, R.5    Coves, J.6
  • 30
    • 35048813675 scopus 로고    scopus 로고
    • Plasmids pMOL28 and pMOL30 of Cupriavidus metallidurans are specialized in the maximal viable response to heavy metals
    • S. Monchy, M.A. Benotmane, P. Janssen, T. Vallaeys, S. Taghavi, and D. van der Lelie et al. Plasmids pMOL28 and pMOL30 of Cupriavidus metallidurans are specialized in the maximal viable response to heavy metals J Bacteriol 189 2007 7417 7425
    • (2007) J Bacteriol , vol.189 , pp. 7417-7425
    • Monchy, S.1    Benotmane, M.A.2    Janssen, P.3    Vallaeys, T.4    Taghavi, S.5    Van Der Lelie, D.6
  • 31
    • 68449097696 scopus 로고    scopus 로고
    • Cupriavidus metallidurans: Evolution of a metal-resistant bacterium
    • T. von Rozycki, and D.H. Nies Cupriavidus metallidurans: evolution of a metal-resistant bacterium Antonie Van Leeuwenhoek 96 2009 115 139
    • (2009) Antonie Van Leeuwenhoek , vol.96 , pp. 115-139
    • Von Rozycki, T.1    Nies, D.H.2
  • 33
  • 34
    • 48449106792 scopus 로고    scopus 로고
    • The Jpred 3 secondary structure prediction server
    • C. Cole, J.D. Barber, and G.J. Barton The Jpred 3 secondary structure prediction server Nucleic Acids Res 36 2008 W197 W201
    • (2008) Nucleic Acids Res , vol.36
    • Cole, C.1    Barber, J.D.2    Barton, G.J.3
  • 35
    • 42049122814 scopus 로고    scopus 로고
    • Regulation of bacterial RNA polymerase sigma factor activity: A structural perspective
    • E.A. Campbell, L.F. Westblade, and S.A. Darst Regulation of bacterial RNA polymerase sigma factor activity: a structural perspective Curr Opin Microbiol 11 2008 121 127
    • (2008) Curr Opin Microbiol , vol.11 , pp. 121-127
    • Campbell, E.A.1    Westblade, L.F.2    Darst, S.A.3
  • 36
    • 1842766125 scopus 로고    scopus 로고
    • Crystal structure of the flagellar sigma/anti-sigma complex sigma(28)/FlgM reveals an intact sigma factor in an inactive conformation
    • M.K. Sorenson, S.S. Ray, and S.A. Darst Crystal structure of the flagellar sigma/anti-sigma complex sigma(28)/FlgM reveals an intact sigma factor in an inactive conformation Mol Cell 14 2004 127 138
    • (2004) Mol Cell , vol.14 , pp. 127-138
    • Sorenson, M.K.1    Ray, S.S.2    Darst, S.A.3
  • 37
    • 34548153206 scopus 로고    scopus 로고
    • Crystal structure of the Escherichia coli regulator of sigma70, Rsd, in complex with sigma70 domain 4
    • G.A. Patikoglou, L.F. Westblade, E.A. Campbell, V. Lamour, W.J. Lane, and S.A. Darst Crystal structure of the Escherichia coli regulator of sigma70, Rsd, in complex with sigma70 domain 4 J Mol Biol 372 2007 649 659
    • (2007) J Mol Biol , vol.372 , pp. 649-659
    • Patikoglou, G.A.1    Westblade, L.F.2    Campbell, E.A.3    Lamour, V.4    Lane, W.J.5    Darst, S.A.6
  • 38
    • 55349117114 scopus 로고    scopus 로고
    • Rsd family proteins make simultaneous interactions with regions 2 and 4 of the primary sigma factor
    • A.H. Yuan, B.D. Gregory, J.S. Sharp, K.D. McCleary, S.L. Dove, and A. Hochschild Rsd family proteins make simultaneous interactions with regions 2 and 4 of the primary sigma factor Mol Microbiol 70 2008 1136 1151
    • (2008) Mol Microbiol , vol.70 , pp. 1136-1151
    • Yuan, A.H.1    Gregory, B.D.2    Sharp, J.S.3    McCleary, K.D.4    Dove, S.L.5    Hochschild, A.6
  • 39
    • 14644435825 scopus 로고    scopus 로고
    • Intrinsically unstructured proteins and their functions
    • H.J. Dyson, and P.E. Wright Intrinsically unstructured proteins and their functions Nat Rev Mol Cell Biol 6 2005 197 208
    • (2005) Nat Rev Mol Cell Biol , vol.6 , pp. 197-208
    • Dyson, H.J.1    Wright, P.E.2
  • 40
    • 77949916296 scopus 로고    scopus 로고
    • Understanding protein non-folding
    • V.N. Uversky, and A.K. Dunker Understanding protein non-folding Biochim Biophys Acta 1804 2010 1231 1264
    • (2010) Biochim Biophys Acta , vol.1804 , pp. 1231-1264
    • Uversky, V.N.1    Dunker, A.K.2
  • 41
    • 50049100893 scopus 로고    scopus 로고
    • Signaling mechanisms for activation of extracytoplasmic function (ECF) sigma factors
    • B.E. Brooks, and S.K. Buchanan Signaling mechanisms for activation of extracytoplasmic function (ECF) sigma factors Biochim Biophys Acta 1778 2008 1930 1945
    • (2008) Biochim Biophys Acta , vol.1778 , pp. 1930-1945
    • Brooks, B.E.1    Buchanan, S.K.2
  • 42
    • 83355162691 scopus 로고    scopus 로고
    • Differential proteolysis of sigma regulators controls cell-surface signalling in Pseudomonas aeruginosa
    • R.C. Draper, L.W. Martin, P.A. Beare, and I.L. Lamont Differential proteolysis of sigma regulators controls cell-surface signalling in Pseudomonas aeruginosa Mol Microbiol 82 2011 1444 1453
    • (2011) Mol Microbiol , vol.82 , pp. 1444-1453
    • Draper, R.C.1    Martin, L.W.2    Beare, P.A.3    Lamont, I.L.4
  • 43
    • 84880017963 scopus 로고    scopus 로고
    • The activity of sigmaV, an extracytoplasmic function sigma factor of Bacillus subtilis, is controlled by regulated proteolysis of the anti-sigma factor RsiV
    • J.L. Hastie, K.B. Williams, and C.D. Ellermeier The activity of sigmaV, an extracytoplasmic function sigma factor of Bacillus subtilis, is controlled by regulated proteolysis of the anti-sigma factor RsiV J Bacteriol 195 2013 3135 3144
    • (2013) J Bacteriol , vol.195 , pp. 3135-3144
    • Hastie, J.L.1    Williams, K.B.2    Ellermeier, C.D.3
  • 44
    • 71749105254 scopus 로고    scopus 로고
    • Regulated intramembrane proteolysis in the control of extracytoplasmic function sigma factors
    • J. Heinrich, and T. Wiegert Regulated intramembrane proteolysis in the control of extracytoplasmic function sigma factors Res Microbiol 160 2009 696 703
    • (2009) Res Microbiol , vol.160 , pp. 696-703
    • Heinrich, J.1    Wiegert, T.2
  • 45
    • 34250821713 scopus 로고    scopus 로고
    • Contribution of extracytoplasmic function sigma factors to transition metal homeostasis in Cupriavidus metallidurans strain CH34
    • C. Grosse, S. Friedrich, and D.H. Nies Contribution of extracytoplasmic function sigma factors to transition metal homeostasis in Cupriavidus metallidurans strain CH34 J Mol Microbiol Biotechnol 12 2007 227 240
    • (2007) J Mol Microbiol Biotechnol , vol.12 , pp. 227-240
    • Grosse, C.1    Friedrich, S.2    Nies, D.H.3
  • 46
    • 77956398098 scopus 로고    scopus 로고
    • The complete genome sequence of Cupriavidus metallidurans strain CH34, a master survivalist in harsh and anthropogenic environments
    • P.J. Janssen, R. Van Houdt, H. Moors, P. Monsieurs, N. Morin, and A. Michaux et al. The complete genome sequence of Cupriavidus metallidurans strain CH34, a master survivalist in harsh and anthropogenic environments PLoS One 5 2010 e10433
    • (2010) PLoS One , vol.5 , pp. 10433
    • Janssen, P.J.1    Van Houdt, R.2    Moors, H.3    Monsieurs, P.4    Morin, N.5    Michaux, A.6
  • 47
    • 59449102308 scopus 로고    scopus 로고
    • NetPhosBac - A predictor for Ser/Thr phosphorylation sites in bacterial proteins
    • M.L. Miller, B. Soufi, C. Jers, N. Blom, B. Macek, and I. Mijakovic NetPhosBac - a predictor for Ser/Thr phosphorylation sites in bacterial proteins Proteomics 9 2009 116 125
    • (2009) Proteomics , vol.9 , pp. 116-125
    • Miller, M.L.1    Soufi, B.2    Jers, C.3    Blom, N.4    Macek, B.5    Mijakovic, I.6
  • 48
    • 0024361623 scopus 로고
    • Cloning and expression of plasmid genes encoding resistances to chromate and cobalt in Alcaligenes eutrophus
    • A. Nies, D.H. Nies, and S. Silver Cloning and expression of plasmid genes encoding resistances to chromate and cobalt in Alcaligenes eutrophus J Bacteriol 171 1989 5065 5070
    • (1989) J Bacteriol , vol.171 , pp. 5065-5070
    • Nies, A.1    Nies, D.H.2    Silver, S.3
  • 49
    • 75149132523 scopus 로고    scopus 로고
    • RseA, the SigE specific anti-sigma factor of Mycobacterium tuberculosis, is inactivated by phosphorylation-dependent ClpC1P2 proteolysis
    • S. Barik, K. Sureka, P. Mukherjee, J. Basu, and M. Kundu RseA, the SigE specific anti-sigma factor of Mycobacterium tuberculosis, is inactivated by phosphorylation-dependent ClpC1P2 proteolysis Mol Microbiol 75 2010 592 606
    • (2010) Mol Microbiol , vol.75 , pp. 592-606
    • Barik, S.1    Sureka, K.2    Mukherjee, P.3    Basu, J.4    Kundu, M.5
  • 52
    • 77950793231 scopus 로고    scopus 로고
    • Experimental phasing with SHELXC/D/E: Combining chain tracing with density modification
    • G.M. Sheldrick Experimental phasing with SHELXC/D/E: combining chain tracing with density modification Acta Crystallogr Sect D Biol Crystallogr 66 2010 479 485
    • (2010) Acta Crystallogr Sect D Biol Crystallogr , vol.66 , pp. 479-485
    • Sheldrick, G.M.1
  • 54
    • 84860285553 scopus 로고    scopus 로고
    • Completion of autobuilt protein models using a database of protein fragments
    • K. Cowtan Completion of autobuilt protein models using a database of protein fragments Acta Crystallogr Sect D Biol Crystallogr 68 2012 328 335
    • (2012) Acta Crystallogr Sect D Biol Crystallogr , vol.68 , pp. 328-335
    • Cowtan, K.1
  • 57
    • 33645158291 scopus 로고    scopus 로고
    • TLSMD web server for the generation of multi-group TLS models
    • J. Painter, and E.A. Merritt TLSMD web server for the generation of multi-group TLS models J Appl Crystallogr 39 2006 109 111
    • (2006) J Appl Crystallogr , vol.39 , pp. 109-111
    • Painter, J.1    Merritt, E.A.2
  • 59
    • 45949107473 scopus 로고    scopus 로고
    • Recent developments in the MAFFT multiple sequence alignment program
    • K. Katoh, and H. Toh Recent developments in the MAFFT multiple sequence alignment program Brief Bioinform 9 2008 286 298
    • (2008) Brief Bioinform , vol.9 , pp. 286-298
    • Katoh, K.1    Toh, H.2
  • 60
    • 65449188232 scopus 로고    scopus 로고
    • Jalview Version 2 - A multiple sequence alignment editor and analysis workbench
    • A.M. Waterhouse, J.B. Procter, D.M. Martin, M. Clamp, and G.J. Barton Jalview Version 2 - a multiple sequence alignment editor and analysis workbench Bioinformatics 25 2009 1189 1191
    • (2009) Bioinformatics , vol.25 , pp. 1189-1191
    • Waterhouse, A.M.1    Procter, J.B.2    Martin, D.M.3    Clamp, M.4    Barton, G.J.5
  • 61
    • 77950806408 scopus 로고    scopus 로고
    • New algorithms and methods to estimate maximum-likelihood phylogenies: Assessing the performance of PhyML 3.0
    • S. Guindon, J.F. Dufayard, V. Lefort, M. Anisimova, W. Hordijk, and O. Gascuel New algorithms and methods to estimate maximum-likelihood phylogenies: assessing the performance of PhyML 3.0 Syst Biol 59 2010 307 321
    • (2010) Syst Biol , vol.59 , pp. 307-321
    • Guindon, S.1    Dufayard, J.F.2    Lefort, V.3    Anisimova, M.4    Hordijk, W.5    Gascuel, O.6


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.