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Volumn 108, Issue 3, 2015, Pages 748-757

Structural analysis of adenovirus VAI RNA defines the mechanism of inhibition of PKR

Author keywords

[No Author keywords available]

Indexed keywords

ADENOVIRIDAE;

EID: 84947202001     PISSN: 00063495     EISSN: 15420086     Source Type: Journal    
DOI: 10.1016/j.bpj.2014.12.014     Document Type: Article
Times cited : (25)

References (58)
  • 1
    • 84881027832 scopus 로고    scopus 로고
    • Innate immune detection of microbial nucleic acids
    • C. Gürtler, and A.G. Bowie Innate immune detection of microbial nucleic acids Trends Microbiol. 21 2013 413 420
    • (2013) Trends Microbiol. , vol.21 , pp. 413-420
    • Gürtler, C.1    Bowie, A.G.2
  • 2
    • 56749133272 scopus 로고    scopus 로고
    • Viral evasion and subversion of pattern-recognition receptor signalling
    • A.G. Bowie, and L. Unterholzner Viral evasion and subversion of pattern-recognition receptor signalling Nat. Rev. Immunol. 8 2008 911 922
    • (2008) Nat. Rev. Immunol. , vol.8 , pp. 911-922
    • Bowie, A.G.1    Unterholzner, L.2
  • 3
    • 33646805444 scopus 로고    scopus 로고
    • Inhibition of PKR by RNA and DNA viruses
    • J.O. Langland, and J.M. Cameron B.L. Jacobs Inhibition of PKR by RNA and DNA viruses Virus Res. 119 2006 100 110
    • (2006) Virus Res. , vol.119 , pp. 100-110
    • Langland, J.O.1    Cameron, J.M.2    Jacobs, B.L.3
  • 4
    • 58149234074 scopus 로고    scopus 로고
    • Rapid evolution of protein kinase PKR alters sensitivity to viral inhibitors
    • S. Rothenburg, and E.J. Seo K. Dittmar Rapid evolution of protein kinase PKR alters sensitivity to viral inhibitors Nat. Struct. Mol. Biol. 16 2009 63 70
    • (2009) Nat. Struct. Mol. Biol. , vol.16 , pp. 63-70
    • Rothenburg, S.1    Seo, E.J.2    Dittmar, K.3
  • 5
    • 58749102026 scopus 로고    scopus 로고
    • Protein kinase R reveals an evolutionary model for defeating viral mimicry
    • N.C. Elde, and S.J. Child H.S. Malik Protein kinase R reveals an evolutionary model for defeating viral mimicry Nature 457 2009 485 489
    • (2009) Nature , vol.457 , pp. 485-489
    • Elde, N.C.1    Child, S.J.2    Malik, H.S.3
  • 6
    • 33846700754 scopus 로고    scopus 로고
    • Activation of PKR: An open and shut case?
    • J.L. Cole Activation of PKR: an open and shut case? Trends Biochem. Sci. 32 2007 57 62
    • (2007) Trends Biochem. Sci. , vol.32 , pp. 57-62
    • Cole, J.L.1
  • 7
    • 25144502820 scopus 로고    scopus 로고
    • Higher-order substrate recognition of eIF2α by the RNA-dependent protein kinase PKR
    • A.C. Dar, T.E. Dever, and F. Sicheri Higher-order substrate recognition of eIF2α by the RNA-dependent protein kinase PKR Cell 122 2005 887 900
    • (2005) Cell , vol.122 , pp. 887-900
    • Dar, A.C.1    Dever, T.E.2    Sicheri, F.3
  • 8
    • 25144477805 scopus 로고    scopus 로고
    • Mechanistic link between PKR dimerization, autophosphorylation, and eIF2alpha substrate recognition
    • M. Dey, and C. Cao T.E. Dever Mechanistic link between PKR dimerization, autophosphorylation, and eIF2alpha substrate recognition Cell 122 2005 901 913
    • (2005) Cell , vol.122 , pp. 901-913
    • Dey, M.1    Cao, C.2    Dever, T.E.3
  • 9
    • 0026713151 scopus 로고
    • Interactions between double-stranded RNA regulators and the protein kinase DAI
    • L. Manche, and S.R. Green M.B. Mathews Interactions between double-stranded RNA regulators and the protein kinase DAI Mol. Cell. Biol. 12 1992 5238 5248
    • (1992) Mol. Cell. Biol. , vol.12 , pp. 5238-5248
    • Manche, L.1    Green, S.R.2    Mathews, M.B.3
  • 11
    • 79551687500 scopus 로고    scopus 로고
    • Regulation of innate immunity through RNA structure and the protein kinase PKR
    • S.R. Nallagatla, R. Toroney, and P.C. Bevilacqua Regulation of innate immunity through RNA structure and the protein kinase PKR Curr. Opin. Struct. Biol. 21 2011 119 127
    • (2011) Curr. Opin. Struct. Biol. , vol.21 , pp. 119-127
    • Nallagatla, S.R.1    Toroney, R.2    Bevilacqua, P.C.3
  • 12
    • 0025361887 scopus 로고
    • Interaction of adenovirus VA RNAl with the protein kinase DAI: Nonequivalence of binding and function
    • K.H. Mellits, M. Kostura, and M.B. Mathews Interaction of adenovirus VA RNAl with the protein kinase DAI: nonequivalence of binding and function Cell 61 1990 843 852
    • (1990) Cell , vol.61 , pp. 843-852
    • Mellits, K.H.1    Kostura, M.2    Mathews, M.B.3
  • 13
  • 14
    • 0029258446 scopus 로고
    • Interactions between the double-stranded RNA binding motif and RNA: Definition of the binding site for the interferon-induced protein kinase DAI (PKR) on adenovirus VA RNA
    • P.A. Clarke, and M.B. Mathews Interactions between the double-stranded RNA binding motif and RNA: definition of the binding site for the interferon-induced protein kinase DAI (PKR) on adenovirus VA RNA RNA 1 1995 7 20
    • (1995) RNA , vol.1 , pp. 7-20
    • Clarke, P.A.1    Mathews, M.B.2
  • 15
    • 0035836464 scopus 로고    scopus 로고
    • Selective binding by the RNA binding domain of PKR revealed by affinity cleavage
    • R.J. Spanggord, and P.A. Beal Selective binding by the RNA binding domain of PKR revealed by affinity cleavage Biochemistry 40 2001 4272 4280
    • (2001) Biochemistry , vol.40 , pp. 4272-4280
    • Spanggord, R.J.1    Beal, P.A.2
  • 16
    • 0037046161 scopus 로고    scopus 로고
    • Identification of binding sites for both dsRBMs of PKR on kinase-activating and kinase-inhibiting RNA ligands
    • R.J. Spanggord, M. Vuyisich, and P.A. Beal Identification of binding sites for both dsRBMs of PKR on kinase-activating and kinase-inhibiting RNA ligands Biochemistry 41 2002 4511 4520
    • (2002) Biochemistry , vol.41 , pp. 4511-4520
    • Spanggord, R.J.1    Vuyisich, M.2    Beal, P.A.3
  • 17
    • 84894569469 scopus 로고    scopus 로고
    • Domain interactions in adenovirus VAI RNA mediate high-affinity PKR binding
    • K. Launer-Felty, and J.L. Cole Domain interactions in adenovirus VAI RNA mediate high-affinity PKR binding J. Mol. Biol. 426 2014 1285 1295
    • (2014) J. Mol. Biol. , vol.426 , pp. 1285-1295
    • Launer-Felty, K.1    Cole, J.L.2
  • 18
    • 47749109063 scopus 로고    scopus 로고
    • Systematic deletion of the adenovirus-associated RNAI terminal stem reveals a surprisingly active RNA inhibitor of double-stranded RNA-activated protein kinase
    • A.M. Wahid, V.K. Coventry, and G.L. Conn Systematic deletion of the adenovirus-associated RNAI terminal stem reveals a surprisingly active RNA inhibitor of double-stranded RNA-activated protein kinase J. Biol. Chem. 283 2008 17485 17493
    • (2008) J. Biol. Chem. , vol.283 , pp. 17485-17493
    • Wahid, A.M.1    Coventry, V.K.2    Conn, G.L.3
  • 19
    • 77956937785 scopus 로고    scopus 로고
    • Magnesium-dependent interaction of PKR with adenovirus VAI
    • K. Launer-Felty, and C.J. Wong J.L. Cole Magnesium-dependent interaction of PKR with adenovirus VAI J. Mol. Biol. 402 2010 638 644
    • (2010) J. Mol. Biol. , vol.402 , pp. 638-644
    • Launer-Felty, K.1    Wong, C.J.2    Cole, J.L.3
  • 20
    • 0029903806 scopus 로고    scopus 로고
    • Secondary and tertiary structure in the central domain of adenovirus type 2 VA RNA i
    • Y. Ma, and M.B. Mathews Secondary and tertiary structure in the central domain of adenovirus type 2 VA RNA I RNA 2 1996 937 951
    • (1996) RNA , vol.2 , pp. 937-951
    • Ma, Y.1    Mathews, M.B.2
  • 21
    • 84905970441 scopus 로고    scopus 로고
    • Dissection of the adenoviral VA RNAI central domain structure reveals minimum requirements for RNA-mediated inhibition of PKR
    • J.L. Wilson, and V.K. Vachon G.L. Conn Dissection of the adenoviral VA RNAI central domain structure reveals minimum requirements for RNA-mediated inhibition of PKR J. Biol. Chem. 289 2014 23233 23245
    • (2014) J. Biol. Chem. , vol.289 , pp. 23233-23245
    • Wilson, J.L.1    Vachon, V.K.2    Conn, G.L.3
  • 22
    • 84891034536 scopus 로고    scopus 로고
    • Solution conformation of adenovirus virus associated RNA-I and its interaction with PKR
    • E. Dzananovic, and T.R. Patel S.A. McKenna Solution conformation of adenovirus virus associated RNA-I and its interaction with PKR J. Struct. Biol. 185 2014 48 57
    • (2014) J. Struct. Biol. , vol.185 , pp. 48-57
    • Dzananovic, E.1    Patel, T.R.2    McKenna, S.A.3
  • 23
    • 80855131662 scopus 로고    scopus 로고
    • Heparin activates PKR by inducing dimerization
    • E. Anderson, and W.S. Pierre-Louis J.L. Cole Heparin activates PKR by inducing dimerization J. Mol. Biol. 413 2011 973 984
    • (2011) J. Mol. Biol. , vol.413 , pp. 973-984
    • Anderson, E.1    Pierre-Louis, W.S.2    Cole, J.L.3
  • 24
    • 23144463133 scopus 로고    scopus 로고
    • Kinefold web server for RNA/DNA folding path and structure prediction including pseudoknots and knots
    • A. Xayaphoummine, T. Bucher, and H. Isambert Kinefold web server for RNA/DNA folding path and structure prediction including pseudoknots and knots Nucleic Acids Res. 33 2005 W605 W610
    • (2005) Nucleic Acids Res. , vol.33 , pp. W605-W610
    • Xayaphoummine, A.1    Bucher, T.2    Isambert, H.3
  • 25
    • 33947720028 scopus 로고    scopus 로고
    • Selective 2′-hydroxyl acylation analyzed by primer extension (SHAPE): Quantitative RNA structure analysis at single nucleotide resolution
    • K.A. Wilkinson, E.J. Merino, and K.M. Weeks Selective 2′-hydroxyl acylation analyzed by primer extension (SHAPE): quantitative RNA structure analysis at single nucleotide resolution Nat. Protoc. 1 2006 1610 1616
    • (2006) Nat. Protoc. , vol.1 , pp. 1610-1616
    • Wilkinson, K.A.1    Merino, E.J.2    Weeks, K.M.3
  • 26
    • 34247162792 scopus 로고    scopus 로고
    • A fast-acting reagent for accurate analysis of RNA secondary and tertiary structure by SHAPE chemistry
    • S.A. Mortimer, and K.M. Weeks A fast-acting reagent for accurate analysis of RNA secondary and tertiary structure by SHAPE chemistry J. Am. Chem. Soc. 129 2007 4144 4145
    • (2007) J. Am. Chem. Soc. , vol.129 , pp. 4144-4145
    • Mortimer, S.A.1    Weeks, K.M.2
  • 27
    • 13944278373 scopus 로고    scopus 로고
    • SAFA: Semi-automated footprinting analysis software for high-throughput quantification of nucleic acid footprinting experiments
    • R. Das, and A. Laederach R.B. Altman SAFA: semi-automated footprinting analysis software for high-throughput quantification of nucleic acid footprinting experiments RNA 11 2005 344 354
    • (2005) RNA , vol.11 , pp. 344-354
    • Das, R.1    Laederach, A.2    Altman, R.B.3
  • 28
    • 77949447172 scopus 로고    scopus 로고
    • RNAstructure: Software for RNA secondary structure prediction and analysis
    • J.S. Reuter, and D.H. Mathews RNAstructure: software for RNA secondary structure prediction and analysis BMC Bioinformatics 11 2010 129
    • (2010) BMC Bioinformatics , vol.11 , pp. 129
    • Reuter, J.S.1    Mathews, D.H.2
  • 29
    • 77957139491 scopus 로고    scopus 로고
    • SHAPE-directed RNA secondary structure prediction
    • J.T. Low, and K.M. Weeks SHAPE-directed RNA secondary structure prediction Methods 52 2010 150 158
    • (2010) Methods , vol.52 , pp. 150-158
    • Low, J.T.1    Weeks, K.M.2
  • 31
    • 0035124442 scopus 로고    scopus 로고
    • Automated matching of high- and low-resolution structural models
    • M.B. Kozin, and D.I. Svergun Automated matching of high- and low-resolution structural models J. Appl. Crystallogr. 34 2001 33 41
    • (2001) J. Appl. Crystallogr. , vol.34 , pp. 33-41
    • Kozin, M.B.1    Svergun, D.I.2
  • 32
    • 33745216899 scopus 로고    scopus 로고
    • Improved methods for fitting sedimentation coefficient distributions derived by time-derivative techniques
    • J.S. Philo Improved methods for fitting sedimentation coefficient distributions derived by time-derivative techniques Anal. Biochem. 354 2006 238 246
    • (2006) Anal. Biochem. , vol.354 , pp. 238-246
    • Philo, J.S.1
  • 33
    • 1642368109 scopus 로고    scopus 로고
    • Analysis of heterologous interacting systems by sedimentation velocity: Curve fitting algorithms for estimation of sedimentation coefficients, equilibrium and kinetic constants
    • W.F. Stafford, and P.J. Sherwood Analysis of heterologous interacting systems by sedimentation velocity: curve fitting algorithms for estimation of sedimentation coefficients, equilibrium and kinetic constants Biophys. Chem. 108 2004 231 243
    • (2004) Biophys. Chem. , vol.108 , pp. 231-243
    • Stafford, W.F.1    Sherwood, P.J.2
  • 34
    • 0001229341 scopus 로고    scopus 로고
    • Calculation of hydrodynamic properties of globular proteins from their atomic-level structure
    • J. García De La Torre, M.L. Huertas, and B. Carrasco Calculation of hydrodynamic properties of globular proteins from their atomic-level structure Biophys. J. 78 2000 719 730
    • (2000) Biophys. J. , vol.78 , pp. 719-730
    • García De La Torre, J.1    Huertas, M.L.2    Carrasco, B.3
  • 35
    • 0026244044 scopus 로고
    • GNOM - A program package for small-angle scattering data processing
    • A.V. Semenyuk, and D.I. Svergun GNOM - a program package for small-angle scattering data processing J. Appl. Crystallogr. 24 1991 537 540
    • (1991) J. Appl. Crystallogr. , vol.24 , pp. 537-540
    • Semenyuk, A.V.1    Svergun, D.I.2
  • 36
    • 62649139615 scopus 로고    scopus 로고
    • DAMMIF, a program for rapid ab-initio shape determination in small-angle scattering
    • D. Franke, and D.I. Svergun DAMMIF, a program for rapid ab-initio shape determination in small-angle scattering J. Appl. Crystallogr. 42 2009 342 346
    • (2009) J. Appl. Crystallogr. , vol.42 , pp. 342-346
    • Franke, D.1    Svergun, D.I.2
  • 37
    • 0037701585 scopus 로고    scopus 로고
    • Uniqueness of ab initio shape determination in small-angle scattering
    • V.V. Volkov, and D.I. Svergun Uniqueness of ab initio shape determination in small-angle scattering J. Appl. Crystallogr. 36 2003 860 864
    • (2003) J. Appl. Crystallogr. , vol.36 , pp. 860-864
    • Volkov, V.V.1    Svergun, D.I.2
  • 39
    • 0029978646 scopus 로고    scopus 로고
    • Structure, function, and evolution of adenovirus-associated RNA: A phylogenetic approach
    • Y. Ma, and M.B. Mathews Structure, function, and evolution of adenovirus-associated RNA: a phylogenetic approach J. Virol. 70 1996 5083 5099
    • (1996) J. Virol. , vol.70 , pp. 5083-5099
    • Ma, Y.1    Mathews, M.B.2
  • 40
    • 73049091026 scopus 로고    scopus 로고
    • The PKR-binding domain of adenovirus VA RNAI exists as a mixture of two functionally non-equivalent structures
    • A.M. Wahid, V.K. Coventry, and G.L. Conn The PKR-binding domain of adenovirus VA RNAI exists as a mixture of two functionally non-equivalent structures Nucleic Acids Res. 37 2009 5830 5837
    • (2009) Nucleic Acids Res. , vol.37 , pp. 5830-5837
    • Wahid, A.M.1    Coventry, V.K.2    Conn, G.L.3
  • 41
    • 77955787630 scopus 로고    scopus 로고
    • Advances in RNA structure analysis by chemical probing
    • K.M. Weeks Advances in RNA structure analysis by chemical probing Curr. Opin. Struct. Biol. 20 2010 295 304
    • (2010) Curr. Opin. Struct. Biol. , vol.20 , pp. 295-304
    • Weeks, K.M.1
  • 42
    • 84878157779 scopus 로고    scopus 로고
    • Nucleic acid structure characterization by small angle X-ray scattering (SAXS)
    • Serge L. Beaucage, John Wiley & Sons, Inc
    • J.E. Burke, and S.E. Butcher Nucleic acid structure characterization by small angle X-ray scattering (SAXS) Serge L. Beaucage, Current Protocols in Nucleic Acid Chemistry 2012 John Wiley & Sons, Inc.
    • (2012) Current Protocols in Nucleic Acid Chemistry
    • Burke, J.E.1    Butcher, S.E.2
  • 43
    • 77149170364 scopus 로고    scopus 로고
    • Improving small-angle x-ray scattering data for structural analyses of the RNA world
    • R.P. Rambo, and J.A. Tainer Improving small-angle x-ray scattering data for structural analyses of the RNA world RNA 16 2010 638 646
    • (2010) RNA , vol.16 , pp. 638-646
    • Rambo, R.P.1    Tainer, J.A.2
  • 44
    • 84886772732 scopus 로고    scopus 로고
    • An unusual topological structure of the HIV-1 Rev response element
    • X. Fang, and J. Wang Y.X. Wang An unusual topological structure of the HIV-1 Rev response element Cell 155 2013 594 605
    • (2013) Cell , vol.155 , pp. 594-605
    • Fang, X.1    Wang, J.2    Wang, Y.X.3
  • 45
    • 34248393495 scopus 로고    scopus 로고
    • Low-resolution models for nucleic acids from small-angle x-ray scattering with applications to electrostatic modeling
    • J. Lipfert, and V.B. Chu S. Doniach Low-resolution models for nucleic acids from small-angle x-ray scattering with applications to electrostatic modeling J. Appl. Crystallogr. 40 2007 s229 s234
    • (2007) J. Appl. Crystallogr. , vol.40 , pp. s229-s234
    • Lipfert, J.1    Chu, V.B.2    Doniach, S.3
  • 47
    • 33646116314 scopus 로고    scopus 로고
    • Uncoupling of RNA binding and PKR kinase activation by viral inhibitor RNAs
    • S.A. McKenna, and I. Kim J.D. Puglisi Uncoupling of RNA binding and PKR kinase activation by viral inhibitor RNAs J. Mol. Biol. 358 2006 1270 1285
    • (2006) J. Mol. Biol. , vol.358 , pp. 1270-1285
    • McKenna, S.A.1    Kim, I.2    Puglisi, J.D.3
  • 48
    • 33846077126 scopus 로고    scopus 로고
    • Mechanism of interaction of the double-stranded RNA (dsRNA) binding domain of protein kinase R with short dsRNA sequences
    • J.W. Ucci, and Y. Kobayashi J.L. Cole Mechanism of interaction of the double-stranded RNA (dsRNA) binding domain of protein kinase R with short dsRNA sequences Biochemistry 46 2007 55 65
    • (2007) Biochemistry , vol.46 , pp. 55-65
    • Ucci, J.W.1    Kobayashi, Y.2    Cole, J.L.3
  • 49
    • 84868561244 scopus 로고    scopus 로고
    • Analysis of high-affinity binding of protein kinase R to double-stranded RNA
    • B. Husain, I. Mukerji, and J.L. Cole Analysis of high-affinity binding of protein kinase R to double-stranded RNA Biochemistry 51 2012 8764 8770
    • (2012) Biochemistry , vol.51 , pp. 8764-8770
    • Husain, B.1    Mukerji, I.2    Cole, J.L.3
  • 50
    • 0029078852 scopus 로고
    • Functional characterization of the RNA-binding domain and motif of the double-stranded RNA-dependent protein kinase DAI (PKR)
    • C. Schmedt, and S.R. Green M.B. Mathews Functional characterization of the RNA-binding domain and motif of the double-stranded RNA-dependent protein kinase DAI (PKR) J. Mol. Biol. 249 1995 29 44
    • (1995) J. Mol. Biol. , vol.249 , pp. 29-44
    • Schmedt, C.1    Green, S.R.2    Mathews, M.B.3
  • 51
    • 22544463666 scopus 로고    scopus 로고
    • Suppression of RNA interference by adenovirus virus-associated RNA
    • M.G. Andersson, and P.C.J. Haasnoot G. Akusjärvi Suppression of RNA interference by adenovirus virus-associated RNA J. Virol. 79 2005 9556 9565
    • (2005) J. Virol. , vol.79 , pp. 9556-9565
    • Andersson, M.G.1    Haasnoot, P.C.J.2    Akusjärvi, G.3
  • 52
    • 8644247492 scopus 로고    scopus 로고
    • Adenovirus VA1 noncoding RNA can inhibit small interfering RNA and MicroRNA biogenesis
    • S. Lu, and B.R. Cullen Adenovirus VA1 noncoding RNA can inhibit small interfering RNA and MicroRNA biogenesis J. Virol. 78 2004 12868 12876
    • (2004) J. Virol. , vol.78 , pp. 12868-12876
    • Lu, S.1    Cullen, B.R.2
  • 53
    • 0028857491 scopus 로고
    • Activation of interferon-inducible 2′-5′ oligoadenylate synthetase by adenoviral VAI RNA
    • S.Y. Desai, and R.C. Patel B. Thimmapaya Activation of interferon-inducible 2′-5′ oligoadenylate synthetase by adenoviral VAI RNA J. Biol. Chem. 270 1995 3454 3461
    • (1995) J. Biol. Chem. , vol.270 , pp. 3454-3461
    • Desai, S.Y.1    Patel, R.C.2    Thimmapaya, B.3
  • 54
    • 84865675957 scopus 로고    scopus 로고
    • Regulation of the interferon-inducible 2′-5′-oligoadenylate synthetases by adenovirus VA(I) RNA
    • H. Meng, and S. Deo S.A. McKenna Regulation of the interferon-inducible 2′-5′-oligoadenylate synthetases by adenovirus VA(I) RNA J. Mol. Biol. 422 2012 635 649
    • (2012) J. Mol. Biol. , vol.422 , pp. 635-649
    • Meng, H.1    Deo, S.2    McKenna, S.A.3
  • 55
    • 0034009520 scopus 로고    scopus 로고
    • Size-distribution analysis of macromolecules by sedimentation velocity ultracentrifugation and lamm equation modeling
    • P. Schuck Size-distribution analysis of macromolecules by sedimentation velocity ultracentrifugation and lamm equation modeling Biophys. J. 78 2000 1606 1619
    • (2000) Biophys. J. , vol.78 , pp. 1606-1619
    • Schuck, P.1
  • 56
    • 0029185933 scopus 로고
    • CRYSOL - A program to evaluate x-ray solution scattering of biological macromolecules from atomic coordinates
    • D. Svergun, C. Barberato, and M.H.J. Koch CRYSOL - a program to evaluate x-ray solution scattering of biological macromolecules from atomic coordinates J. Appl. Crystallogr. 28 1995 768 773
    • (1995) J. Appl. Crystallogr. , vol.28 , pp. 768-773
    • Svergun, D.1    Barberato, C.2    Koch, M.H.J.3
  • 57
    • 42949089487 scopus 로고    scopus 로고
    • Flexible fitting of atomic structures into electron microscopy maps using molecular dynamics
    • L.G. Trabuco, and E. Villa K. Schulten Flexible fitting of atomic structures into electron microscopy maps using molecular dynamics Structure 16 2008 673 683
    • (2008) Structure , vol.16 , pp. 673-683
    • Trabuco, L.G.1    Villa, E.2    Schulten, K.3
  • 58
    • 84859782518 scopus 로고    scopus 로고
    • New developments in the ATSAS program package for small-angle scattering data analysis
    • M.V. Petoukhov, and D. Franke D.I. Svergun New developments in the ATSAS program package for small-angle scattering data analysis J. Appl. Cryst. 45 2012 342 350
    • (2012) J. Appl. Cryst. , vol.45 , pp. 342-350
    • Petoukhov, M.V.1    Franke, D.2    Svergun, D.I.3


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