메뉴 건너뛰기




Volumn 370, Issue 2, 2007, Pages 256-268

Mechanism for De Novo RNA Synthesis and Initiating Nucleotide Specificity by T7 RNA Polymerase

Author keywords

de novo RVA synthesis; GTP specificity; T7 RNA polymerase

Indexed keywords

ADENOSINE TRIPHOSPHATE; CYTIDINE TRIPHOSPHATE; DNA DIRECTED RNA POLYMERASE; GUANOSINE TRIPHOSPHATE; NUCLEOTIDE BINDING PROTEIN; RNA; RNA POLYMERASE; SINGLE STRANDED DNA; URIDINE TRIPHOSPHATE;

EID: 34249652496     PISSN: 00222836     EISSN: None     Source Type: Journal    
DOI: 10.1016/j.jmb.2007.03.041     Document Type: Article
Times cited : (52)

References (55)
  • 1
    • 0037133504 scopus 로고    scopus 로고
    • Kinetic and thermodynamic basis of promoter strength: multiple steps of transcription initiation by T7 RNA polymerase are modulated by the promoter sequence
    • Bandwar R.P., Jia Y., Stano N.M., and Patel S.S. Kinetic and thermodynamic basis of promoter strength: multiple steps of transcription initiation by T7 RNA polymerase are modulated by the promoter sequence. Biochemistry 41 (2002) 3586-3595
    • (2002) Biochemistry , vol.41 , pp. 3586-3595
    • Bandwar, R.P.1    Jia, Y.2    Stano, N.M.3    Patel, S.S.4
  • 2
    • 0032483305 scopus 로고    scopus 로고
    • NTP concentration effects on initial transcription by T7 RNAP indicate that translocation occurs through passive sliding and reveal that divergent promoters have distinct NTP concentration requirements for productive initiation
    • Guajardo R., Lopez P., Dreyfus M., and Sousa R. NTP concentration effects on initial transcription by T7 RNAP indicate that translocation occurs through passive sliding and reveal that divergent promoters have distinct NTP concentration requirements for productive initiation. J. Mol. Biol. 281 (1998) 777-792
    • (1998) J. Mol. Biol. , vol.281 , pp. 777-792
    • Guajardo, R.1    Lopez, P.2    Dreyfus, M.3    Sousa, R.4
  • 3
    • 33845967859 scopus 로고    scopus 로고
    • Transient state kinetics of transcription elongation by T7 RNA polymerase
    • Anand V.S., and Patel S.S. Transient state kinetics of transcription elongation by T7 RNA polymerase. J. Biol. Chem. 281 (2006) 35677-35685
    • (2006) J. Biol. Chem. , vol.281 , pp. 35677-35685
    • Anand, V.S.1    Patel, S.S.2
  • 4
    • 0015935359 scopus 로고
    • Characterization of T7-specific ribonucleic acid polymerase. 1. General properties of the enzymatic reaction and the template specificity of the enzyme
    • Chamberlin M., and Ring J. Characterization of T7-specific ribonucleic acid polymerase. 1. General properties of the enzymatic reaction and the template specificity of the enzyme. J. Biol. Chem. 248 (1973) 2235-2244
    • (1973) J. Biol. Chem. , vol.248 , pp. 2235-2244
    • Chamberlin, M.1    Ring, J.2
  • 5
    • 33745962422 scopus 로고    scopus 로고
    • Comparative mechanistic studies of de novo RNA synthesis by flavivirus RNA-dependent RNA polymerases
    • Selisko B., Dutartre H., Guillemot J.C., Debarnot C., Benarroch D., Khromykh A., et al. Comparative mechanistic studies of de novo RNA synthesis by flavivirus RNA-dependent RNA polymerases. Virology 351 (2006) 145-158
    • (2006) Virology , vol.351 , pp. 145-158
    • Selisko, B.1    Dutartre, H.2    Guillemot, J.C.3    Debarnot, C.4    Benarroch, D.5    Khromykh, A.6
  • 6
    • 0033529089 scopus 로고    scopus 로고
    • Structural basis for initiation of transcription from an RNA polymerase-promoter complex
    • Cheetham G.M., Jeruzalmi D., and Steitz T.A. Structural basis for initiation of transcription from an RNA polymerase-promoter complex. Nature 399 (1999) 80-83
    • (1999) Nature , vol.399 , pp. 80-83
    • Cheetham, G.M.1    Jeruzalmi, D.2    Steitz, T.A.3
  • 7
    • 0033579380 scopus 로고    scopus 로고
    • Structure of a transcribing T7 RNA polymerase initiation complex
    • Cheetham G.M., and Steitz T.A. Structure of a transcribing T7 RNA polymerase initiation complex. Science 286 (1999) 2305-2309
    • (1999) Science , vol.286 , pp. 2305-2309
    • Cheetham, G.M.1    Steitz, T.A.2
  • 8
    • 0037112082 scopus 로고    scopus 로고
    • Structural basis for the transition from initiation to elongation transcription in T7 RNA polymerase
    • Yin Y.W., and Steitz T.A. Structural basis for the transition from initiation to elongation transcription in T7 RNA polymerase. Science 298 (2002) 1387-1395
    • (2002) Science , vol.298 , pp. 1387-1395
    • Yin, Y.W.1    Steitz, T.A.2
  • 10
    • 1342313235 scopus 로고    scopus 로고
    • The structural mechanism of translocation and helicase activity in T7 RNA polymerase
    • Yin Y.W., and Steitz T.A. The structural mechanism of translocation and helicase activity in T7 RNA polymerase. Cell 116 (2004) 393-404
    • (2004) Cell , vol.116 , pp. 393-404
    • Yin, Y.W.1    Steitz, T.A.2
  • 12
    • 0037474202 scopus 로고    scopus 로고
    • Binding of the priming nucleotide in the initiation of transcription by T7 RNA polymerase
    • Kuzmine I., Gottlieb P.A., and Martin C.T. Binding of the priming nucleotide in the initiation of transcription by T7 RNA polymerase. J. Biol. Chem. 278 (2003) 2819-2823
    • (2003) J. Biol. Chem. , vol.278 , pp. 2819-2823
    • Kuzmine, I.1    Gottlieb, P.A.2    Martin, C.T.3
  • 13
    • 0027184481 scopus 로고
    • A general two-metal-ion mechanism for catalytic RNA
    • Steitz T.A., and Steitz J.A. A general two-metal-ion mechanism for catalytic RNA. Proc. Natl Acad. Sci. USA 90 (1993) 6498-6502
    • (1993) Proc. Natl Acad. Sci. USA , vol.90 , pp. 6498-6502
    • Steitz, T.A.1    Steitz, J.A.2
  • 14
    • 0016219032 scopus 로고
    • Characterization of T7-specific ribonucleic acid polymerase. IV. Resolution of the major in vitro transcripts by gel electrophoresis
    • Golomb M., and Chamberlin M. Characterization of T7-specific ribonucleic acid polymerase. IV. Resolution of the major in vitro transcripts by gel electrophoresis. J. Biol. Chem. 249 (1974) 2858-2863
    • (1974) J. Biol. Chem. , vol.249 , pp. 2858-2863
    • Golomb, M.1    Chamberlin, M.2
  • 15
    • 0016723692 scopus 로고
    • Translational mapping of bacteriophage T7 RNAs synthesized in vitro by purified T7 RNA polymerase
    • Niles E.G., and Condit R.C. Translational mapping of bacteriophage T7 RNAs synthesized in vitro by purified T7 RNA polymerase. J. Mol. Biol. 98 (1975) 57-67
    • (1975) J. Mol. Biol. , vol.98 , pp. 57-67
    • Niles, E.G.1    Condit, R.C.2
  • 16
    • 0019191653 scopus 로고
    • Regulation of promoter selection by the bacteriophage T7 RNA polymerase in vitro
    • McAllister W.T., and Carter A.D. Regulation of promoter selection by the bacteriophage T7 RNA polymerase in vitro. Nucl. Acids Res. 8 (1980) 4821-4837
    • (1980) Nucl. Acids Res. , vol.8 , pp. 4821-4837
    • McAllister, W.T.1    Carter, A.D.2
  • 17
    • 0014669561 scopus 로고
    • Fluorescence studies of nucleotides and polynucleotides. I. Formycin, 2-aminopurine riboside, 2,6-diaminopurine riboside, and their derivatives
    • Ward D.C., Reich E., and Stryer L. Fluorescence studies of nucleotides and polynucleotides. I. Formycin, 2-aminopurine riboside, 2,6-diaminopurine riboside, and their derivatives. J. Biol. Chem. 244 (1969) 1228-1237
    • (1969) J. Biol. Chem. , vol.244 , pp. 1228-1237
    • Ward, D.C.1    Reich, E.2    Stryer, L.3
  • 19
    • 0028128641 scopus 로고
    • Melting and premelting transitions of an oligomer measured by DNA base fluorescence and absorption
    • Xu D., Evans K.O., and Nordlund T.M. Melting and premelting transitions of an oligomer measured by DNA base fluorescence and absorption. Biochemistry 33 (1994) 9592-9599
    • (1994) Biochemistry , vol.33 , pp. 9592-9599
    • Xu, D.1    Evans, K.O.2    Nordlund, T.M.3
  • 20
    • 0020964297 scopus 로고
    • Complete nucleotide sequence of bacteriophage T7 DNA and the locations of T7 genetic elements
    • Dunn J.J., and Studier F.W. Complete nucleotide sequence of bacteriophage T7 DNA and the locations of T7 genetic elements. J. Mol. Biol. 166 (1983) 477-535
    • (1983) J. Mol. Biol. , vol.166 , pp. 477-535
    • Dunn, J.J.1    Studier, F.W.2
  • 21
    • 4944260681 scopus 로고    scopus 로고
    • Topological and conformational analysis of the initiation and elongation complex of T7 RNA polymerase suggests a new twist
    • Theis K., Gong P., and Martin C.T. Topological and conformational analysis of the initiation and elongation complex of T7 RNA polymerase suggests a new twist. Biochemistry 43 (2004) 12709-12715
    • (2004) Biochemistry , vol.43 , pp. 12709-12715
    • Theis, K.1    Gong, P.2    Martin, C.T.3
  • 22
    • 33751218319 scopus 로고    scopus 로고
    • Abortive initiation and productive initiation by RNA polymerase involve DNA scrunching
    • Revyakin A., Liu C., Ebright R.H., and Strick T.R. Abortive initiation and productive initiation by RNA polymerase involve DNA scrunching. Science 314 (2006) 1139-1143
    • (2006) Science , vol.314 , pp. 1139-1143
    • Revyakin, A.1    Liu, C.2    Ebright, R.H.3    Strick, T.R.4
  • 23
    • 2342419732 scopus 로고    scopus 로고
    • DNA replication fidelity
    • Kunkel T.A. DNA replication fidelity. J. Biol. Chem. 279 (2004) 16895-16898
    • (2004) J. Biol. Chem. , vol.279 , pp. 16895-16898
    • Kunkel, T.A.1
  • 24
    • 0032518398 scopus 로고    scopus 로고
    • Crystal structure of a bacteriophage T7 DNA replication complex at 2.2 Å resolution
    • Doublie S., Tabor S., Long A.M., Richardson C.C., and Ellenberger T. Crystal structure of a bacteriophage T7 DNA replication complex at 2.2 Å resolution. Nature 391 (1998) 251-258
    • (1998) Nature , vol.391 , pp. 251-258
    • Doublie, S.1    Tabor, S.2    Long, A.M.3    Richardson, C.C.4    Ellenberger, T.5
  • 25
    • 0035369086 scopus 로고    scopus 로고
    • Structure of the replicating complex of a pol alpha family DNA polymerase
    • Franklin M.C., Wang J., and Steitz T.A. Structure of the replicating complex of a pol alpha family DNA polymerase. Cell 105 (2001) 657-667
    • (2001) Cell , vol.105 , pp. 657-667
    • Franklin, M.C.1    Wang, J.2    Steitz, T.A.3
  • 26
    • 0032535528 scopus 로고    scopus 로고
    • Crystal structures of open and closed forms of binary and ternary complexes of the large fragment of Thermus aquaticus DNA polymerase I: structural basis for nucleotide incorporation
    • Li Y., Korolev S., and Waksman G. Crystal structures of open and closed forms of binary and ternary complexes of the large fragment of Thermus aquaticus DNA polymerase I: structural basis for nucleotide incorporation. EMBO J. 17 (1998) 7514-7525
    • (1998) EMBO J. , vol.17 , pp. 7514-7525
    • Li, Y.1    Korolev, S.2    Waksman, G.3
  • 27
    • 0035019856 scopus 로고    scopus 로고
    • Crystal structures of a ddATP-, ddTTP-, ddCTP, and ddGTP-trapped ternary complex of Klentaq1: insights into nucleotide incorporation and selectivity
    • Li Y., and Waksman G. Crystal structures of a ddATP-, ddTTP-, ddCTP, and ddGTP-trapped ternary complex of Klentaq1: insights into nucleotide incorporation and selectivity. Protein Sci. 10 (2001) 1225-1233
    • (2001) Protein Sci. , vol.10 , pp. 1225-1233
    • Li, Y.1    Waksman, G.2
  • 28
    • 0024961074 scopus 로고
    • T7 RNA polymerase does not interact with the 5′-phosphate of the initiating nucleotide
    • Martin C.T., and Coleman J.E. T7 RNA polymerase does not interact with the 5′-phosphate of the initiating nucleotide. Biochemistry 28 (1989) 2760-2762
    • (1989) Biochemistry , vol.28 , pp. 2760-2762
    • Martin, C.T.1    Coleman, J.E.2
  • 29
    • 0029118487 scopus 로고
    • A free energy analysis of nucleic acid base stacking in aqueous solution
    • Friedman R.A., and Honig B. A free energy analysis of nucleic acid base stacking in aqueous solution. Biophys. J. 69 (1995) 1528-1535
    • (1995) Biophys. J. , vol.69 , pp. 1528-1535
    • Friedman, R.A.1    Honig, B.2
  • 31
    • 0034730077 scopus 로고    scopus 로고
    • Studies of promoter recognition and start site selection by T7 RNA polymerase using a comprehensive collection of promoter variants
    • Imburgio D., Rong M., Ma K., and McAllister W.T. Studies of promoter recognition and start site selection by T7 RNA polymerase using a comprehensive collection of promoter variants. Biochemistry 39 (2000) 10419-10430
    • (2000) Biochemistry , vol.39 , pp. 10419-10430
    • Imburgio, D.1    Rong, M.2    Ma, K.3    McAllister, W.T.4
  • 32
    • 0037020232 scopus 로고    scopus 로고
    • The + 2 NTP binding drives open complex formation in T7 RNA polymerase
    • Stano N.M., Levin M.K., and Patel S.S. The + 2 NTP binding drives open complex formation in T7 RNA polymerase. J. Biol. Chem. 277 (2002) 37292-37300
    • (2002) J. Biol. Chem. , vol.277 , pp. 37292-37300
    • Stano, N.M.1    Levin, M.K.2    Patel, S.S.3
  • 33
    • 0036303923 scopus 로고    scopus 로고
    • Effects of substitutions in a conserved DX(2)GR sequence motif, found in many DNA-dependent nucleotide polymerases, on transcription by T7 RNA polymerase
    • Imburgio D., Anikin M., and McAllister W.T. Effects of substitutions in a conserved DX(2)GR sequence motif, found in many DNA-dependent nucleotide polymerases, on transcription by T7 RNA polymerase. J. Mol. Biol. 319 (2002) 37-51
    • (2002) J. Mol. Biol. , vol.319 , pp. 37-51
    • Imburgio, D.1    Anikin, M.2    McAllister, W.T.3
  • 35
    • 0030899746 scopus 로고    scopus 로고
    • Probing the mechanisms of T7 RNA polymerase transcription initiation using photochemical conjugation of psoralen to a promoter
    • Sastry S.S., and Ross B.M. Probing the mechanisms of T7 RNA polymerase transcription initiation using photochemical conjugation of psoralen to a promoter. Biochemistry 36 (1997) 3133-3144
    • (1997) Biochemistry , vol.36 , pp. 3133-3144
    • Sastry, S.S.1    Ross, B.M.2
  • 36
    • 0031567783 scopus 로고    scopus 로고
    • Role of open complex instability in kinetic promoter selection by bacteriophage T7 RNA polymerase
    • Villemain J., Guajardo R., and Sousa R. Role of open complex instability in kinetic promoter selection by bacteriophage T7 RNA polymerase. J. Mol. Biol. 273 (1997) 958-977
    • (1997) J. Mol. Biol. , vol.273 , pp. 958-977
    • Villemain, J.1    Guajardo, R.2    Sousa, R.3
  • 37
    • 0035910269 scopus 로고    scopus 로고
    • Pre-steady-state kinetics of initiation of transcription by T7 RNA polymerase: a new kinetic model
    • Kuzmine I., and Martin C.T. Pre-steady-state kinetics of initiation of transcription by T7 RNA polymerase: a new kinetic model. J. Mol. Biol. 305 (2001) 559-566
    • (2001) J. Mol. Biol. , vol.305 , pp. 559-566
    • Kuzmine, I.1    Martin, C.T.2
  • 38
    • 0001210090 scopus 로고
    • Interactions of the RNA polymerase of bacteriophage T7 with its promoter during binding and initiation of transcription
    • Ikeda R.A., and Richardson C.C. Interactions of the RNA polymerase of bacteriophage T7 with its promoter during binding and initiation of transcription. Proc. Natl Acad. Sci. USA 83 (1986) 3614-3618
    • (1986) Proc. Natl Acad. Sci. USA , vol.83 , pp. 3614-3618
    • Ikeda, R.A.1    Richardson, C.C.2
  • 39
    • 0022247421 scopus 로고
    • Interaction of RNA polymerase with lacUV5 promoter DNA during mRNA initiation and elongation. Footprinting, methylation, and rifampicin-sensitivity changes accompanying transcription initiation
    • Carpousis A.J., and Gralla J.D. Interaction of RNA polymerase with lacUV5 promoter DNA during mRNA initiation and elongation. Footprinting, methylation, and rifampicin-sensitivity changes accompanying transcription initiation. J. Mol. Biol. 183 (1985) 165-177
    • (1985) J. Mol. Biol. , vol.183 , pp. 165-177
    • Carpousis, A.J.1    Gralla, J.D.2
  • 40
    • 0023118838 scopus 로고
    • Comparison of the open complexes formed by RNA polymerase at the Escherichia coli lac UV5 promoter
    • Straney D.C., and Crothers D.M. Comparison of the open complexes formed by RNA polymerase at the Escherichia coli lac UV5 promoter. J. Mol. Biol. 193 (1987) 279-292
    • (1987) J. Mol. Biol. , vol.193 , pp. 279-292
    • Straney, D.C.1    Crothers, D.M.2
  • 41
    • 33751212468 scopus 로고    scopus 로고
    • Initial transcription by RNA polymerase proceeds through a DNA-scrunching mechanism
    • Kapanidis A.N., Margeat E., Ho S.O., Kortkhonjia E., Weiss S., and Ebright R.H. Initial transcription by RNA polymerase proceeds through a DNA-scrunching mechanism. Science 314 (2006) 1144-1147
    • (2006) Science , vol.314 , pp. 1144-1147
    • Kapanidis, A.N.1    Margeat, E.2    Ho, S.O.3    Kortkhonjia, E.4    Weiss, S.5    Ebright, R.H.6
  • 42
    • 0029330856 scopus 로고
    • The large genome segment of dsRNA bacteriophage phi6 is the key regulator in the in vitro minus and plus strand synthesis
    • Frilander M., Poranen M., and Bamford D.H. The large genome segment of dsRNA bacteriophage phi6 is the key regulator in the in vitro minus and plus strand synthesis. Rna 1 (1995) 510-518
    • (1995) Rna , vol.1 , pp. 510-518
    • Frilander, M.1    Poranen, M.2    Bamford, D.H.3
  • 43
    • 0034602836 scopus 로고    scopus 로고
    • Replicase activity of purified recombinant protein P2 of double-stranded RNA bacteriophage phi6
    • Makeyev E.V., and Bamford D.H. Replicase activity of purified recombinant protein P2 of double-stranded RNA bacteriophage phi6. EMBO J. 19 (2000) 124-133
    • (2000) EMBO J. , vol.19 , pp. 124-133
    • Makeyev, E.V.1    Bamford, D.H.2
  • 45
    • 0032876683 scopus 로고    scopus 로고
    • Crystal structure of the RNA-dependent RNA polymerase from hepatitis C virus reveals a fully encircled active site
    • Lesburg C.A., Cable M.B., Ferrari E., Hong Z., Mannarino A.F., and Weber P.C. Crystal structure of the RNA-dependent RNA polymerase from hepatitis C virus reveals a fully encircled active site. Nature Struct. Biol. 6 (1999) 937-943
    • (1999) Nature Struct. Biol. , vol.6 , pp. 937-943
    • Lesburg, C.A.1    Cable, M.B.2    Ferrari, E.3    Hong, Z.4    Mannarino, A.F.5    Weber, P.C.6
  • 46
    • 1842481188 scopus 로고    scopus 로고
    • The structure of the RNA-dependent RNA polymerase from bovine viral diarrhea virus establishes the role of GTP in de novo initiation
    • Choi K.H., Groarke J.M., Young D.C., Kuhn R.J., Smith J.L., Pevear D.C., and Rossmann M.G. The structure of the RNA-dependent RNA polymerase from bovine viral diarrhea virus establishes the role of GTP in de novo initiation. Proc. Natl Acad. Sci. USA 101 (2004) 4425-4430
    • (2004) Proc. Natl Acad. Sci. USA , vol.101 , pp. 4425-4430
    • Choi, K.H.1    Groarke, J.M.2    Young, D.C.3    Kuhn, R.J.4    Smith, J.L.5    Pevear, D.C.6    Rossmann, M.G.7
  • 47
    • 0037053339 scopus 로고    scopus 로고
    • Bacteriophage phi 6 RNA-dependent RNA polymerase: molecular details of initiating nucleic acid synthesis without primer
    • Laurila M.R., Makeyev E.V., and Bamford D.H. Bacteriophage phi 6 RNA-dependent RNA polymerase: molecular details of initiating nucleic acid synthesis without primer. J. Biol. Chem. 277 (2002) 17117-17124
    • (2002) J. Biol. Chem. , vol.277 , pp. 17117-17124
    • Laurila, M.R.1    Makeyev, E.V.2    Bamford, D.H.3
  • 48
    • 0026749487 scopus 로고
    • Functional transcription elongation complexes from synthetic RNA-DNA bubble duplexes
    • Daube S.S., and von Hippel P.H. Functional transcription elongation complexes from synthetic RNA-DNA bubble duplexes. Science 258 (1992) 1320-1324
    • (1992) Science , vol.258 , pp. 1320-1324
    • Daube, S.S.1    von Hippel, P.H.2
  • 49
    • 0032527832 scopus 로고    scopus 로고
    • Structure of T7 RNA polymerase complexed to the transcriptional inhibitor T7 lysozyme
    • Jeruzalmi D., and Steitz T.A. Structure of T7 RNA polymerase complexed to the transcriptional inhibitor T7 lysozyme. EMBO J. 17 (1998) 4101-4113
    • (1998) EMBO J. , vol.17 , pp. 4101-4113
    • Jeruzalmi, D.1    Steitz, T.A.2
  • 51
    • 0031059866 scopus 로고    scopus 로고
    • Processing of X-ray diffraction data collected in oscillation mode
    • Otwinowski Z., and Minor M. Processing of X-ray diffraction data collected in oscillation mode. Methods Enzymol 276 (1997) 307-326
    • (1997) Methods Enzymol , vol.276 , pp. 307-326
    • Otwinowski, Z.1    Minor, M.2
  • 52
    • 0035788101 scopus 로고    scopus 로고
    • Implementation of molecular replacement in AMoRe
    • Navaza J. Implementation of molecular replacement in AMoRe. Acta Crystallog. sect. D 57 (2001) 1367-1372
    • (2001) Acta Crystallog. sect. D , vol.57 , pp. 1367-1372
    • Navaza, J.1
  • 54
    • 0035182073 scopus 로고    scopus 로고
    • Use of TLS parameters to model anisotropic displacements in macromolecular refinement
    • Winn M.D., Isupov M.N., and Murshudov G.N. 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
  • 55
    • 84889120137 scopus 로고
    • Improved methods for building protein models in electron density maps and the location of errors in these models
    • Jones T.A., Zou J.Y., Cowan S.W., and Kjeldgaard. Improved methods for building protein models in electron density maps and the location of errors in these models. Acta Crystallog. sect. A 47 (1991) 110-119
    • (1991) Acta Crystallog. sect. A , vol.47 , pp. 110-119
    • Jones, T.A.1    Zou, J.Y.2    Cowan, S.W.3    Kjeldgaard4


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.