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Volumn 393, Issue 5, 2009, Pages 1043-1055

Solution Structure of an Archaeal RNase P Binary Protein Complex: Formation of the 30-kDa Complex between Pyrococcus furiosus RPP21 and RPP29 Is Accompanied by Coupled Protein Folding and Highlights Critical Features for Protein-Protein and Protein-RNA Interactions

Author keywords

archaea; binding coupled protein folding; NMR of a protein protein complex; ribonuclease P, RNase P; RNA footprinting

Indexed keywords

BACTERIAL PROTEIN; BACTERIAL RNA; MAGNESIUM ION; RIBONUCLEASE P; RIBONUCLEOPROTEIN; TRANSFER RNA;

EID: 70350020742     PISSN: 00222836     EISSN: None     Source Type: Journal    
DOI: 10.1016/j.jmb.2009.08.068     Document Type: Article
Times cited : (36)

References (60)
  • 1
    • 34547892624 scopus 로고    scopus 로고
    • A view of RNase P
    • Altman S. A view of RNase P. Mol. Biosyst. 3 (2007) 604-607
    • (2007) Mol. Biosyst. , vol.3 , pp. 604-607
    • Altman, S.1
  • 2
    • 34848856061 scopus 로고    scopus 로고
    • Ribonuclease P: structure and catalysis
    • Gesteland R., Cech T., and Atkins J. (Eds), Cold Spring Harbor Laboratory Press, Cold Spring Harbor, NY (only online at http://rna.cshl.edu)
    • Gopalan V., and Altman S. Ribonuclease P: structure and catalysis. In: Gesteland R., Cech T., and Atkins J. (Eds). The RNA World (2006), Cold Spring Harbor Laboratory Press, Cold Spring Harbor, NY. http://rna.cshl.edu (only online at http://rna.cshl.edu)
    • (2006) The RNA World
    • Gopalan, V.1    Altman, S.2
  • 3
    • 33745166320 scopus 로고    scopus 로고
    • RNase P: interface of the RNA and protein worlds
    • Evans D., Marquez S.M., and Pace N.R. RNase P: interface of the RNA and protein worlds. Trends Biochem. Sci. 31 (2006) 333-341
    • (2006) Trends Biochem. Sci. , vol.31 , pp. 333-341
    • Evans, D.1    Marquez, S.M.2    Pace, N.R.3
  • 4
    • 0021013526 scopus 로고
    • The RNA moiety of ribonuclease P is the catalytic subunit of the enzyme
    • Guerrier-Takada C., Gardiner K., Marsh T., Pace N., and Altman S. The RNA moiety of ribonuclease P is the catalytic subunit of the enzyme. Cell 35 (1983) 849-857
    • (1983) Cell , vol.35 , pp. 849-857
    • Guerrier-Takada, C.1    Gardiner, K.2    Marsh, T.3    Pace, N.4    Altman, S.5
  • 6
    • 33847784925 scopus 로고    scopus 로고
    • Eukaryotic RNase P RNA mediates cleavage in the absence of protein
    • Kikovska E., Svard S.G., and Kirsebom L.A. Eukaryotic RNase P RNA mediates cleavage in the absence of protein. Proc. Natl Acad. Sci. USA 104 (2007) 2062-2067
    • (2007) Proc. Natl Acad. Sci. USA , vol.104 , pp. 2062-2067
    • Kikovska, E.1    Svard, S.G.2    Kirsebom, L.A.3
  • 7
    • 0347763706 scopus 로고    scopus 로고
    • Roles of protein subunits in RNA-protein complexes: lessons from ribonuclease P
    • Hsieh J., Andrews A.J., and Fierke C.A. Roles of protein subunits in RNA-protein complexes: lessons from ribonuclease P. Biopolymers 73 (2004) 79-89
    • (2004) Biopolymers , vol.73 , pp. 79-89
    • Hsieh, J.1    Andrews, A.J.2    Fierke, C.A.3
  • 8
    • 33748361597 scopus 로고    scopus 로고
    • Evidence that substrate-specific effects of C5 protein lead to uniformity in binding and catalysis by RNase P
    • Sun L., Campbell F.E., Zahler N.H., and Harris M.E. Evidence that substrate-specific effects of C5 protein lead to uniformity in binding and catalysis by RNase P. EMBO J. 25 (2006) 3998-4007
    • (2006) EMBO J. , vol.25 , pp. 3998-4007
    • Sun, L.1    Campbell, F.E.2    Zahler, N.H.3    Harris, M.E.4
  • 9
    • 34548371821 scopus 로고    scopus 로고
    • Evidence that binding of C5 protein to P RNA enhances ribozyme catalysis by influencing active site metal ion affinity
    • Sun L., and Harris M.E. Evidence that binding of C5 protein to P RNA enhances ribozyme catalysis by influencing active site metal ion affinity. RNA 13 (2007) 1505-1515
    • (2007) RNA , vol.13 , pp. 1505-1515
    • Sun, L.1    Harris, M.E.2
  • 10
    • 37549069403 scopus 로고    scopus 로고
    • Importance of RNA-protein interactions in bacterial ribonuclease P structure and catalysis
    • Smith J.K., Hsieh J., and Fierke C.A. Importance of RNA-protein interactions in bacterial ribonuclease P structure and catalysis. Biopolymers 87 (2007) 329-338
    • (2007) Biopolymers , vol.87 , pp. 329-338
    • Smith, J.K.1    Hsieh, J.2    Fierke, C.A.3
  • 11
    • 0141450351 scopus 로고    scopus 로고
    • The enigma of ribonuclease P evolution
    • Hartmann E., and Hartmann R.K. The enigma of ribonuclease P evolution. Trends Genet. 19 (2003) 561-569
    • (2003) Trends Genet. , vol.19 , pp. 561-569
    • Hartmann, E.1    Hartmann, R.K.2
  • 12
    • 33847775629 scopus 로고    scopus 로고
    • Uniformity amid diversity in RNase P
    • Gopalan V. Uniformity amid diversity in RNase P. Proc. Natl Acad. Sci. USA 104 (2007) 2031-2032
    • (2007) Proc. Natl Acad. Sci. USA , vol.104 , pp. 2031-2032
    • Gopalan, V.1
  • 13
    • 33750831489 scopus 로고    scopus 로고
    • Functional reconstitution and characterization of Pyrococcus furiosus RNase P
    • Tsai H.Y., Pulukkunat D.K., Woznick W.K., and Gopalan V. Functional reconstitution and characterization of Pyrococcus furiosus RNase P. Proc. Natl Acad. Sci. USA 103 (2006) 16147-16152
    • (2006) Proc. Natl Acad. Sci. USA , vol.103 , pp. 16147-16152
    • Tsai, H.Y.1    Pulukkunat, D.K.2    Woznick, W.K.3    Gopalan, V.4
  • 14
    • 0036231352 scopus 로고    scopus 로고
    • Archaeal RNase P has multiple protein subunits homologous to eukaryotic nuclear RNase P proteins
    • Hall T.A., and Brown J.W. Archaeal RNase P has multiple protein subunits homologous to eukaryotic nuclear RNase P proteins. RNA 8 (2002) 296-306
    • (2002) RNA , vol.8 , pp. 296-306
    • Hall, T.A.1    Brown, J.W.2
  • 15
    • 33748863131 scopus 로고    scopus 로고
    • Bacterial RNase P: a new view of an ancient enzyme
    • Kazantsev A.V., and Pace N.R. Bacterial RNase P: a new view of an ancient enzyme. Nat. Rev., Microbiol. 4 (2006) 729-740
    • (2006) Nat. Rev., Microbiol. , vol.4 , pp. 729-740
    • Kazantsev, A.V.1    Pace, N.R.2
  • 16
    • 0344298926 scopus 로고    scopus 로고
    • The Ribonuclease P Database
    • Brown J.W. The Ribonuclease P Database. Nucleic Acids Res. 27 (1999) 314
    • (1999) Nucleic Acids Res. , vol.27 , pp. 314
    • Brown, J.W.1
  • 17
    • 0029949699 scopus 로고    scopus 로고
    • Domain structure of the ribozyme from eubacterial ribonuclease P
    • Loria A., and Pan T. Domain structure of the ribozyme from eubacterial ribonuclease P. RNA 2 (1996) 551-563
    • (1996) RNA , vol.2 , pp. 551-563
    • Loria, A.1    Pan, T.2
  • 18
    • 6044275739 scopus 로고    scopus 로고
    • Basis for structural diversity in homologous RNAs
    • Krasilnikov A.S., Xiao Y., Pan T., and Mondragon A. Basis for structural diversity in homologous RNAs. Science 306 (2004) 104-107
    • (2004) Science , vol.306 , pp. 104-107
    • Krasilnikov, A.S.1    Xiao, Y.2    Pan, T.3    Mondragon, A.4
  • 19
    • 0037434709 scopus 로고    scopus 로고
    • Crystal structure of the specificity domain of ribonuclease P
    • Krasilnikov A.S., Yang X., Pan T., and Mondragon A. Crystal structure of the specificity domain of ribonuclease P. Nature 421 (2003) 760-764
    • (2003) Nature , vol.421 , pp. 760-764
    • Krasilnikov, A.S.1    Yang, X.2    Pan, T.3    Mondragon, A.4
  • 23
    • 0032076249 scopus 로고    scopus 로고
    • Ribonuclease P protein structure: evolutionary origins in the translational apparatus
    • Stams T., Niranjanakumari S., Fierke C.A., and Christianson D.W. Ribonuclease P protein structure: evolutionary origins in the translational apparatus. Science 280 (1998) 752-755
    • (1998) Science , vol.280 , pp. 752-755
    • Stams, T.1    Niranjanakumari, S.2    Fierke, C.A.3    Christianson, D.W.4
  • 24
    • 0034614360 scopus 로고    scopus 로고
    • The structure of ribonuclease P protein from Staphylococcus aureus reveals a unique binding site for single-stranded RNA
    • Spitzfaden C., Nicholson N., Jones J.J., Guth S., Lehr R., Prescott C.D., et al. The structure of ribonuclease P protein from Staphylococcus aureus reveals a unique binding site for single-stranded RNA. J. Mol. Biol. 295 (2000) 105-115
    • (2000) J. Mol. Biol. , vol.295 , pp. 105-115
    • Spitzfaden, C.1    Nicholson, N.2    Jones, J.J.3    Guth, S.4    Lehr, R.5    Prescott, C.D.6
  • 25
    • 0037462929 scopus 로고    scopus 로고
    • Molecular modeling of the three-dimensional structure of the bacterial RNase P holoenzyme
    • Tsai H.Y., Masquida B., Biswas R., Westhof E., and Gopalan V. Molecular modeling of the three-dimensional structure of the bacterial RNase P holoenzyme. J. Mol. Biol. 325 (2003) 661-675
    • (2003) J. Mol. Biol. , vol.325 , pp. 661-675
    • Tsai, H.Y.1    Masquida, B.2    Biswas, R.3    Westhof, E.4    Gopalan, V.5
  • 26
  • 27
    • 33947716757 scopus 로고    scopus 로고
    • Probing the architecture of the B. subtilis RNase P holoenzyme active site by cross-linking and affinity cleavage
    • Niranjanakumari S., Day-Storms J.J., Ahmed M., Hsieh J., Zahler N.H., Venters R.A., and Fierke C.A. Probing the architecture of the B. subtilis RNase P holoenzyme active site by cross-linking and affinity cleavage. RNA 13 (2007) 521-535
    • (2007) RNA , vol.13 , pp. 521-535
    • Niranjanakumari, S.1    Day-Storms, J.J.2    Ahmed, M.3    Hsieh, J.4    Zahler, N.H.5    Venters, R.A.6    Fierke, C.A.7
  • 28
    • 0035259427 scopus 로고    scopus 로고
    • New insight into RNase P RNA structure from comparative analysis of the archaeal RNA
    • Harris J.K., Haas E.S., Williams D., Frank D.N., and Brown J.W. New insight into RNase P RNA structure from comparative analysis of the archaeal RNA. RNA 7 (2001) 220-232
    • (2001) RNA , vol.7 , pp. 220-232
    • Harris, J.K.1    Haas, E.S.2    Williams, D.3    Frank, D.N.4    Brown, J.W.5
  • 29
    • 47249122660 scopus 로고    scopus 로고
    • Studies on Methanocaldococcus jannaschii RNase P reveal insights into the roles of RNA and protein cofactors in RNase P catalysis
    • Pulukkunat D.K., and Gopalan V. Studies on Methanocaldococcus jannaschii RNase P reveal insights into the roles of RNA and protein cofactors in RNase P catalysis. Nucleic Acids Res. 36 (2008) 4172-4180
    • (2008) Nucleic Acids Res. , vol.36 , pp. 4172-4180
    • Pulukkunat, D.K.1    Gopalan, V.2
  • 31
    • 0344823672 scopus 로고    scopus 로고
    • NMR structure of an archaeal homologue of ribonuclease P protein Rpp29
    • Sidote D.J., and Hoffman D.W. NMR structure of an archaeal homologue of ribonuclease P protein Rpp29. Biochemistry 42 (2003) 13541-13550
    • (2003) Biochemistry , vol.42 , pp. 13541-13550
    • Sidote, D.J.1    Hoffman, D.W.2
  • 32
    • 8344266164 scopus 로고    scopus 로고
    • Crystal structure of archaeal ribonuclease P protein aRpp29 from Archaeoglobus fulgidus
    • Sidote D.J., Heideker J., and Hoffman D.W. Crystal structure of archaeal ribonuclease P protein aRpp29 from Archaeoglobus fulgidus. Biochemistry 43 (2004) 14128-14138
    • (2004) Biochemistry , vol.43 , pp. 14128-14138
    • Sidote, D.J.1    Heideker, J.2    Hoffman, D.W.3
  • 33
    • 4344638194 scopus 로고    scopus 로고
    • Crystal structure of archaeal ribonuclease P protein Ph1771p from Pyrococcus horikoshii OT3: an archaeal homolog of eukaryotic ribonuclease P protein Rpp29
    • Numata T., Ishimatsu I., Kakuta Y., Tanaka I., and Kimura M. Crystal structure of archaeal ribonuclease P protein Ph1771p from Pyrococcus horikoshii OT3: an archaeal homolog of eukaryotic ribonuclease P protein Rpp29. RNA 10 (2004) 1423-1432
    • (2004) RNA , vol.10 , pp. 1423-1432
    • Numata, T.1    Ishimatsu, I.2    Kakuta, Y.3    Tanaka, I.4    Kimura, M.5
  • 34
    • 24644469952 scopus 로고    scopus 로고
    • Crystal structure of a ribonuclease P protein Ph1601p from Pyrococcus horikoshii OT3: an archaeal homologue of human nuclear ribonuclease P protein Rpp21
    • Kakuta Y., Ishimatsu I., Numata T., Kimura K., Yao M., Tanaka I., and Kimura M. Crystal structure of a ribonuclease P protein Ph1601p from Pyrococcus horikoshii OT3: an archaeal homologue of human nuclear ribonuclease P protein Rpp21. Biochemistry 44 (2005) 12086-12093
    • (2005) Biochemistry , vol.44 , pp. 12086-12093
    • Kakuta, Y.1    Ishimatsu, I.2    Numata, T.3    Kimura, K.4    Yao, M.5    Tanaka, I.6    Kimura, M.7
  • 35
    • 55849120858 scopus 로고    scopus 로고
    • Solution structure of Pyrococcus furiosus RPP21, a component of the archaeal RNase P holoenzyme, and interactions with its RPP29 protein partner
    • Amero C.D., Boomershine W.P., Xu Y., and Foster M. Solution structure of Pyrococcus furiosus RPP21, a component of the archaeal RNase P holoenzyme, and interactions with its RPP29 protein partner. Biochemistry 47 (2008) 11704-11710
    • (2008) Biochemistry , vol.47 , pp. 11704-11710
    • Amero, C.D.1    Boomershine, W.P.2    Xu, Y.3    Foster, M.4
  • 37
  • 38
    • 22444431914 scopus 로고    scopus 로고
    • Protein-protein interactions in the subunits of ribonuclease P in the hyperthermophilic archaeon Pyrococcus horikoshii OT3
    • Kifusa M., Fukuhara H., Hayashi T., and Kimura M. Protein-protein interactions in the subunits of ribonuclease P in the hyperthermophilic archaeon Pyrococcus horikoshii OT3. Biosci. Biotechnol. Biochem. 69 (2005) 1209-1212
    • (2005) Biosci. Biotechnol. Biochem. , vol.69 , pp. 1209-1212
    • Kifusa, M.1    Fukuhara, H.2    Hayashi, T.3    Kimura, M.4
  • 39
    • 4344684743 scopus 로고    scopus 로고
    • Interactions between RNase P protein subunits in archaea
    • Hall T.A., and Brown J.W. Interactions between RNase P protein subunits in archaea. Archaea 1 (2004) 247-254
    • (2004) Archaea , vol.1 , pp. 247-254
    • Hall, T.A.1    Brown, J.W.2
  • 41
    • 33344479270 scopus 로고    scopus 로고
    • Crystal structure of protein Ph1481p in complex with protein Ph1877p of archaeal RNase P from Pyrococcus horikoshii OT3: implication of dimer formation of the holoenzyme
    • Kawano S., Nakashima T., Kakuta Y., Tanaka I., and Kimura M. Crystal structure of protein Ph1481p in complex with protein Ph1877p of archaeal RNase P from Pyrococcus horikoshii OT3: implication of dimer formation of the holoenzyme. J. Mol. Biol. 357 (2006) 583-591
    • (2006) J. Mol. Biol. , vol.357 , pp. 583-591
    • Kawano, S.1    Nakashima, T.2    Kakuta, Y.3    Tanaka, I.4    Kimura, M.5
  • 42
    • 55349099821 scopus 로고    scopus 로고
    • Structure of an archaeal homolog of the human protein complex Rpp21-Rpp29 that is a key core component for the assembly of active ribonuclease P
    • Honda T., Kakuta Y., Kimura K., Saho J., and Kimura M. Structure of an archaeal homolog of the human protein complex Rpp21-Rpp29 that is a key core component for the assembly of active ribonuclease P. J. Mol. Biol. 384 (2008) 652-662
    • (2008) J. Mol. Biol. , vol.384 , pp. 652-662
    • Honda, T.1    Kakuta, Y.2    Kimura, K.3    Saho, J.4    Kimura, M.5
  • 43
    • 0000112965 scopus 로고    scopus 로고
    • Isotope-filtered NMR methods for the study of biomolecular structure and interactions
    • Breeze A. Isotope-filtered NMR methods for the study of biomolecular structure and interactions. Prog. Nucl. Magn. Reson. Spectrosc. 36 (2000) 323-372
    • (2000) Prog. Nucl. Magn. Reson. Spectrosc. , vol.36 , pp. 323-372
    • Breeze, A.1
  • 44
    • 0030808350 scopus 로고    scopus 로고
    • Methods for measurement of intermolecular NOEs by multinuclear NMR spectroscopy: application to a bacteriophage λ N-peptide/boxB RNA complex
    • Zwahlen C., Legault P., Vincent S.J.F., Greenblatt J., Konrat R., and Kay L.E. Methods for measurement of intermolecular NOEs by multinuclear NMR spectroscopy: application to a bacteriophage λ N-peptide/boxB RNA complex. J. Am. Chem. Soc. 119 (1997) 6711-6721
    • (1997) J. Am. Chem. Soc. , vol.119 , pp. 6711-6721
    • Zwahlen, C.1    Legault, P.2    Vincent, S.J.F.3    Greenblatt, J.4    Konrat, R.5    Kay, L.E.6
  • 45
    • 0030339738 scopus 로고    scopus 로고
    • AQUA and PROCHECK-NMR: programs for checking the quality of protein structures solved by NMR
    • Laskowski R.A., Rullmannn J.A., MacArthur M.W., Kaptein R., and Thornton J.M. AQUA and PROCHECK-NMR: programs for checking the quality of protein structures solved by NMR. J. Biomol. NMR 8 (1996) 477-486
    • (1996) J. Biomol. NMR , vol.8 , pp. 477-486
    • Laskowski, R.A.1    Rullmannn, J.A.2    MacArthur, M.W.3    Kaptein, R.4    Thornton, J.M.5
  • 46
    • 0034960193 scopus 로고    scopus 로고
    • Protein-RNA interactions in the subunits of human nuclear RNase P
    • Jiang T., Guerrier-Takada C., and Altman S. Protein-RNA interactions in the subunits of human nuclear RNase P. Proc. Natl Acad. Sci. USA 7 (2001) 937-941
    • (2001) Proc. Natl Acad. Sci. USA , vol.7 , pp. 937-941
    • Jiang, T.1    Guerrier-Takada, C.2    Altman, S.3
  • 47
    • 33847775629 scopus 로고    scopus 로고
    • Uniformity amid diversity in RNase P
    • Gopalan V. Uniformity amid diversity in RNase P. Proc. Natl Acad. Sci. USA 104 (2007) 2031-2032
    • (2007) Proc. Natl Acad. Sci. USA , vol.104 , pp. 2031-2032
    • Gopalan, V.1
  • 48
    • 0034896788 scopus 로고    scopus 로고
    • Function and subnuclear distribution of Rpp21, a protein subunit of the human ribonucleoprotein ribonuclease P
    • Jarrous N., Reiner R., Wesolowski D., Mann H., Guerrier-Takada C., and Altman S. Function and subnuclear distribution of Rpp21, a protein subunit of the human ribonucleoprotein ribonuclease P. RNA 7 (2001) 1153-1164
    • (2001) RNA , vol.7 , pp. 1153-1164
    • Jarrous, N.1    Reiner, R.2    Wesolowski, D.3    Mann, H.4    Guerrier-Takada, C.5    Altman, S.6
  • 49
    • 34548501510 scopus 로고    scopus 로고
    • Evidence for induced fit in bacterial RNase P RNA-mediated cleavage
    • Brannvall M., Kikovska E., Wu S., and Kirsebom L.A. Evidence for induced fit in bacterial RNase P RNA-mediated cleavage. J. Mol. Biol. 372 (2007) 1149-1164
    • (2007) J. Mol. Biol. , vol.372 , pp. 1149-1164
    • Brannvall, M.1    Kikovska, E.2    Wu, S.3    Kirsebom, L.A.4
  • 50
    • 0029556990 scopus 로고
    • Probing of tertiary interactions in RNA: 2′-hydroxyl-base contacts between the RNase P RNA and pre-tRNA
    • Pan T., Loria A., and Zhong K. Probing of tertiary interactions in RNA: 2′-hydroxyl-base contacts between the RNase P RNA and pre-tRNA. Proc. Natl Acad. Sci. USA 92 (1995) 12510-12514
    • (1995) Proc. Natl Acad. Sci. USA , vol.92 , pp. 12510-12514
    • Pan, T.1    Loria, A.2    Zhong, K.3
  • 52
    • 4644259437 scopus 로고    scopus 로고
    • Using NMRView to visualize and analyze the NMR spectra of macromolecules
    • Johnson B.A. Using NMRView to visualize and analyze the NMR spectra of macromolecules. Methods Mol. Biol. 278 (2004) 313-352
    • (2004) Methods Mol. Biol. , vol.278 , pp. 313-352
    • Johnson, B.A.1
  • 55
    • 0024449503 scopus 로고
    • Backbone dynamics of proteins as studied by nitrogen-15 inverse detected heteronuclear NMR spectroscopy: application to staphylococcal nuclease
    • Kay L.E., Torchia D.A., and Bax A. Backbone dynamics of proteins as studied by nitrogen-15 inverse detected heteronuclear NMR spectroscopy: application to staphylococcal nuclease. Biochemistry 28 (1989) 8972-8979
    • (1989) Biochemistry , vol.28 , pp. 8972-8979
    • Kay, L.E.1    Torchia, D.A.2    Bax, A.3
  • 56
    • 0033003335 scopus 로고    scopus 로고
    • Protein backbone angle restraints from searching a database for chemical shift and sequence homology
    • Cornilescu G., Delaglio F., and Bax A. Protein backbone angle restraints from searching a database for chemical shift and sequence homology. J. Biomol. NMR 13 (1999) 289-302
    • (1999) J. Biomol. NMR , vol.13 , pp. 289-302
    • Cornilescu, G.1    Delaglio, F.2    Bax, A.3
  • 58
    • 0035029325 scopus 로고    scopus 로고
    • SANE (Structure Assisted NOE Evaluation): an automated model-based approach for NOE assignment
    • Duggan B.M., Legge G.B., Dyson H.J., and Wright P.E. SANE (Structure Assisted NOE Evaluation): an automated model-based approach for NOE assignment. J. Biomol. NMR 19 (2001) 321-329
    • (2001) J. Biomol. NMR , vol.19 , pp. 321-329
    • Duggan, B.M.1    Legge, G.B.2    Dyson, H.J.3    Wright, P.E.4
  • 59
    • 0033997037 scopus 로고    scopus 로고
    • Structure-based thermodynamic analysis of the dissociation of protein phosphatase-1 catalytic subunit and microcystin-LR docked complexes
    • Lavigne P., Bagu J.R., Boyko R., Willard L., Holmes C.F., and Sykes B.D. Structure-based thermodynamic analysis of the dissociation of protein phosphatase-1 catalytic subunit and microcystin-LR docked complexes. Protein Sci. 9 (2000) 252-264
    • (2000) Protein Sci. , vol.9 , pp. 252-264
    • Lavigne, P.1    Bagu, J.R.2    Boyko, R.3    Willard, L.4    Holmes, C.F.5    Sykes, B.D.6
  • 60
    • 70350025892 scopus 로고    scopus 로고
    • Ph. D. Thesis, The Ohio State University, Columbus, OH
    • Pulukkunat, D. K. (2008). Ph. D. Thesis, The Ohio State University, Columbus, OH.
    • (2008)
    • Pulukkunat, D.K.1


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