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Volumn 413, Issue 4, 2011, Pages 773-789

Analysis of binding site hot spots on the surface of Ras GTPase

Author keywords

allosteric switch; binding site hot spots; drug target; Ras dynamics; Ras isoforms

Indexed keywords

ISOENZYME; K RAS PROTEIN; RAS PROTEIN;

EID: 80054860512     PISSN: 00222836     EISSN: 10898638     Source Type: Journal    
DOI: 10.1016/j.jmb.2011.09.011     Document Type: Article
Times cited : (124)

References (56)
  • 1
    • 0025010979 scopus 로고
    • The GTPase superfamily: Conserved switch for diverse cell functions
    • Bourne, H. R., Sanders, D. A. & McCormick, F. (1990). The GTPase superfamily: conserved switch for diverse cell functions. Nature, 348, 125-132.
    • (1990) Nature , vol.348 , pp. 125-132
    • Bourne, H.R.1    Sanders, D.A.2    McCormick, F.3
  • 2
    • 0032560850 scopus 로고    scopus 로고
    • The structural basis of the activation of Ras by Sos
    • DOI 10.1038/28548
    • Boriack-Sjodin, P. A., Margarit, S. M., Bar-Sagi, D. & Kuriyan, J. (1998). The structural basis of the activation of Ras by Sos. Nature, 394, 337-343. (Pubitemid 28373822)
    • (1998) Nature , vol.394 , Issue.6691 , pp. 337-343
    • Boriack-Sjodin, P.A.1    Margarit, S.M.2    Bar-Sagi, D.3    Kuriyan, J.4
  • 3
    • 0030772378 scopus 로고    scopus 로고
    • The Ras-RasGAP complex: Structural basis for GTPase activation and its loss in oncogenic ras mutants
    • DOI 10.1126/science.277.5324.333
    • Scheffzek, K., Ahmadian, M. R., Kabsch, W., Wiesmüller, L., Lautwein, A., Schmitz, F. & Wittinghofer, A. (1997). The Ras-RasGAP complex: structural basis for GTPase activation and its loss in oncogenic Ras mutants. Science, 277, 333-338. (Pubitemid 27450699)
    • (1997) Science , vol.277 , Issue.5324 , pp. 333-338
    • Scheffzek, K.1    Ahmadian, M.R.2    Kabsch, W.3    Wiesmuller, L.4    Lautwein, A.5    Schmitz, F.6    Wittinghofer, A.7
  • 4
    • 0037308836 scopus 로고    scopus 로고
    • Ras-effector interactions: After one decade
    • Herrmann, C. (2003). Ras-effector interactions: after one decade. Curr. Opin. Struct. Biol. 13, 122-129.
    • (2003) Curr. Opin. Struct. Biol. , vol.13 , pp. 122-129
    • Herrmann, C.1
  • 5
    • 1642553461 scopus 로고    scopus 로고
    • The dark side of Ras: Regulation of apoptosis
    • DOI 10.1038/sj.onc.1207111, Apoptosis - Part 2
    • Cox, A. D. & Der, C. J. (2003). The dark side of Ras: regulation of apoptosis. Oncogene, 22, 8999-9006. (Pubitemid 38121700)
    • (2003) Oncogene , vol.22 , Issue.56 REV. ISS. 8 , pp. 8999-9006
    • Cox, A.D.1    Der, C.J.2
  • 7
  • 8
    • 61449104961 scopus 로고    scopus 로고
    • Fragment-based identification of druggable "hot spots" of proteins using Fourier domain correlation techniques
    • Brenke, R., Kozakov, D., Chuang, G. Y., Beglov, D., Hall, D., Landon, M. R. et al. (2009). Fragment-based identification of druggable "hot spots" of proteins using Fourier domain correlation techniques. Bioinformatics, 25, 621-627.
    • (2009) Bioinformatics , vol.25 , pp. 621-627
    • Brenke, R.1    Kozakov, D.2    Chuang, G.Y.3    Beglov, D.4    Hall, D.5    Landon, M.R.6
  • 9
    • 0028916599 scopus 로고
    • A hot spot of binding energy in a hormone-receptor interface
    • Clackson, T. & Wells, J. A. (1995). A hot spot of binding energy in a hormone-receptor interface. Science, 267, 383-386.
    • (1995) Science , vol.267 , pp. 383-386
    • Clackson, T.1    Wells, J.A.2
  • 10
    • 0025117674 scopus 로고
    • Molecular switch for signal transduction: Structural differences between active and inactive forms of protooncogenic Ras proteins
    • Milburn, M., Tong, L., deVos, A. M., Brünger, A., Yamaizumi, Z., Nishimura, S. & Kim, S. H. (1990). Molecular switch for signal transduction: structural differences between active and inactive forms of protooncogenic Ras proteins. Science, 247, 939-945.
    • (1990) Science , vol.247 , pp. 939-945
    • Milburn, M.1    Tong, L.2    DeVos, A.M.3    Brünger, A.4    Yamaizumi, Z.5    Nishimura, S.6    Kim, S.H.7
  • 11
    • 0026026818 scopus 로고
    • The GTPase superfamily: Conserved structure and molecular mechanism
    • Bourne, H. R., Sanders, D. A. & McCormick, F. (1991). The GTPase superfamily: conserved structure and molecular mechanism. Nature, 349, 117-127. (Pubitemid 21912023)
    • (1991) Nature , vol.349 , Issue.6305 , pp. 117-127
    • Bourne, H.R.1    Sanders, D.A.2    McCormick, F.3
  • 12
    • 77950397231 scopus 로고    scopus 로고
    • Allosteric modulation of Ras positions Q61 for a direct role in catalysis
    • Buhrman, G., Holzapfel, G., Fetics, S. & Mattos, C. (2010). Allosteric modulation of Ras positions Q61 for a direct role in catalysis. Proc. Natl Acad. Sci. USA, 107, 4931-4936.
    • (2010) Proc. Natl Acad. Sci. USA , vol.107 , pp. 4931-4936
    • Buhrman, G.1    Holzapfel, G.2    Fetics, S.3    Mattos, C.4
  • 13
    • 79952811451 scopus 로고    scopus 로고
    • Allosteric modulation of Ras-GTP is linked to signal transduction through RAF kinase
    • Buhrman, G., Kumar, V. S., Cirit, M., Haugh, J. M. & Mattos, C. (2011). Allosteric modulation of Ras-GTP is linked to signal transduction through RAF kinase. J. Biol. Chem. 286, 3323-3331.
    • (2011) J. Biol. Chem. , vol.286 , pp. 3323-3331
    • Buhrman, G.1    Kumar, V.S.2    Cirit, M.3    Haugh, J.M.4    Mattos, C.5
  • 14
    • 52949089338 scopus 로고    scopus 로고
    • Global conformational dynamics in Ras
    • O'Connor, C. & Kovrigin, E. L. (2008). Global conformational dynamics in Ras. Biochemistry, 47, 10244-10246.
    • (2008) Biochemistry , vol.47 , pp. 10244-10246
    • O'Connor, C.1    Kovrigin, E.L.2
  • 15
    • 77249157335 scopus 로고    scopus 로고
    • Mechanisms of allostery and membrane attachment in Ras GTPases: Implications for anti-cancer drug discovery
    • Gorfe, A. A. (2010). Mechanisms of allostery and membrane attachment in Ras GTPases: implications for anti-cancer drug discovery. Curr. Med. Chem. 17, 1-9.
    • (2010) Curr. Med. Chem. , vol.17 , pp. 1-9
    • Gorfe, A.A.1
  • 16
    • 0037542854 scopus 로고    scopus 로고
    • Ras proteins: Different signals from different locations
    • Hancock, J. F. (2003). Ras proteins: different signals from different locations. Nat. Rev., Mol. Cell Biol. 4, 373-384.
    • (2003) Nat. Rev., Mol. Cell Biol. , vol.4 , pp. 373-384
    • Hancock, J.F.1
  • 18
    • 33847413103 scopus 로고    scopus 로고
    • Structure and dynamics of the full-length lipid-modified H-Ras protein in a 1,2-dimyristoylglycero-3-phosphocholine bilayer
    • DOI 10.1021/jm061053f
    • Gorfe, A. A., Hanzal-Bayer, M., Abankwa, D., Hancock, J. F. & McCammon, J. A. (2007). Structure and dynamics of the full-length lipid-modified H-Ras protein in a 1,2-dimyristoylglycero-3-phosphocholine bilayer. J. Med. Chem. 50, 674-684. (Pubitemid 46332980)
    • (2007) Journal of Medicinal Chemistry , vol.50 , Issue.4 , pp. 674-684
    • Gorfe, A.A.1    Hanzal-Bayer, M.2    Abankwa, D.3    Hancock, J.F.4    McCammon, J.A.5
  • 19
    • 44649199260 scopus 로고    scopus 로고
    • Mapping the Nucleotide and Isoform-Dependent Structural and Dynamical Features of Ras Proteins
    • DOI 10.1016/j.str.2008.03.009, PII S0969212608001494
    • Gorfe, A. A., Grant, B. J. & McCammon, J. A. (2008). Mapping the nucleotide and isoform-dependent structural and dynamical features of Ras proteins. Structure, 16, 885-896. (Pubitemid 351778381)
    • (2008) Structure , vol.16 , Issue.6 , pp. 885-896
    • Gorfe, A.A.1    Grant, B.J.2    McCammon, J.A.3
  • 20
    • 75749150934 scopus 로고    scopus 로고
    • Ras membrane orientation and nanodomain localization generate isoform diversity
    • Abankwa, D., Gorfe, A. A., Inder, K. & Hancock, J. F. (2010). Ras membrane orientation and nanodomain localization generate isoform diversity. Proc. Natl Acad. Sci. USA, 107, 1130-1135.
    • (2010) Proc. Natl Acad. Sci. USA , vol.107 , pp. 1130-1135
    • Abankwa, D.1    Gorfe, A.A.2    Inder, K.3    Hancock, J.F.4
  • 21
    • 33846696047 scopus 로고    scopus 로고
    • Empirical rules facilitate the search for binding sites on protein surfaces
    • DOI 10.1016/j.jmgm.2006.05.005, PII S1093326306000921
    • Heesen, H., Schlitter, A. M. & Schlitter, J. (2007). Empirical rules facilitate the search for binding sites on protein surfaces. J. Mol. Graphics Modell. 25, 671-679. (Pubitemid 46188546)
    • (2007) Journal of Molecular Graphics and Modelling , vol.25 , Issue.5 , pp. 671-679
    • Te, H.H.1    Schlitter, A.M.2    Schlitter, J.3
  • 23
    • 67650168962 scopus 로고    scopus 로고
    • First experimental identification of Ras-inhibitor binding interface using a water-soluble Ras ligand
    • Palmioli, A., Sacco, E., Abraham, S., Thomas, C. J., Di Domizio, A., De Gioia, L. et al. (2009). First experimental identification of Ras-inhibitor binding interface using a water-soluble Ras ligand. Bioorg. Med. Chem. Lett. 19, 4217-4222.
    • (2009) Bioorg. Med. Chem. Lett. , vol.19 , pp. 4217-4222
    • Palmioli, A.1    Sacco, E.2    Abraham, S.3    Thomas, C.J.4    Di Domizio, A.5    De Gioia, L.6
  • 24
    • 68149159752 scopus 로고    scopus 로고
    • Multiple solvent crystal structures of ribonuclease A: An assessment of the method
    • Dechene, M., Wink, G., Smith, M., Swartz, P. & Mattos, C. (2009). Multiple solvent crystal structures of ribonuclease A: an assessment of the method. Proteins, 76, 861-881.
    • (2009) Proteins , vol.76 , pp. 861-881
    • Dechene, M.1    Wink, G.2    Smith, M.3    Swartz, P.4    Mattos, C.5
  • 27
    • 36749036721 scopus 로고    scopus 로고
    • Transformation Efficiency of RasQ61 Mutants Linked to Structural Features of the Switch Regions in the Presence of Raf
    • DOI 10.1016/j.str.2007.10.011, PII S096921260700408X
    • Buhrman, G., Wink, G. & Mattos, C. (2007). Transformation efficiency of RasQ61 mutants linked to structural features of the switch regions in the presence of Raf. Structure, 15, 1618-1629. (Pubitemid 350213406)
    • (2007) Structure , vol.15 , Issue.12 , pp. 1618-1629
    • Buhrman, G.1    Wink, G.2    Mattos, C.3
  • 28
    • 0037666814 scopus 로고    scopus 로고
    • Organic solvents order the dynamic switch II in Ras crystals
    • DOI 10.1016/S0969-2126(03)00128-X
    • Buhrman, G., de Serrano, V. & Mattos, C. (2003). Organic solvents order the dynamic switch II in Ras crystals. Structure, 11, 747-751. (Pubitemid 36830842)
    • (2003) Structure , vol.11 , Issue.7 , pp. 747-751
    • Buhrman, G.1    De Serrano, V.2    Mattos, C.3
  • 29
    • 0033612390 scopus 로고    scopus 로고
    • Structural view of the Ran-importin β interaction at 2.3 Å resolution
    • DOI 10.1016/S0092-8674(00)80774-6
    • Vetter, I. R., Arndt, A., Kutay, U., Gorlich, D. &Wittinghofer, A. (1999). Structural view of the Ran-importin β interaction at 2.3 Å resolution. Cell, 97, 635-646. (Pubitemid 29256966)
    • (1999) Cell , vol.97 , Issue.5 , pp. 635-646
    • Vetter, I.R.1    Arndt, A.2    Kutay, U.3    Gorlich, D.4    Wittinghofer, A.5
  • 30
    • 79952551201 scopus 로고    scopus 로고
    • Ubiquitination of K-Ras enhances activation and facilitates binding to select downstream effectors
    • Sasaki, A. T., Carracedo, A., Locasale, J. W., Anastasiou, D., Takeuchi, K., Kahoud, E. R. et al. (2011). Ubiquitination of K-Ras enhances activation and facilitates binding to select downstream effectors. Sci. Signal. 4, ra13.
    • (2011) Sci. Signal. , vol.4
    • Sasaki, A.T.1    Carracedo, A.2    Locasale, J.W.3    Anastasiou, D.4    Takeuchi, K.5    Kahoud, E.R.6
  • 32
    • 0029587739 scopus 로고
    • Cysteine-rich region of Raf-1 interacts with activator domain of post-translationally modified Ha-Ras
    • Hu, C. D., Kariya, K., Tamada, M., Akasaka, K., Shirouzu, M., Yokoyama, S. & Kataoka, T. (1995). Cysteine-rich region of Raf-1 interacts with activator domain of post-translationally modified Ha-Ras. J. Biol. Chem. 270, 30274-30277.
    • (1995) J. Biol. Chem. , vol.270 , pp. 30274-30277
    • Hu, C.D.1    Kariya, K.2    Tamada, M.3    Akasaka, K.4    Shirouzu, M.5    Yokoyama, S.6    Kataoka, T.7
  • 33
    • 33947658802 scopus 로고    scopus 로고
    • Identification of hot spots within druggable binding regions by computational solvent mapping of proteins
    • DOI 10.1021/jm061134b
    • Landon, M. R., Lancia, D. R., Jr., Yu, J., Thiel, S. C. & Vajda, S. (2007). Identification of hot spots within druggable binding regions by computational solvent mapping of proteins. J. Med. Chem. 50, 1231-1240. (Pubitemid 46496323)
    • (2007) Journal of Medicinal Chemistry , vol.50 , Issue.6 , pp. 1231-1240
    • Landon, M.R.1    Lancia Jr., D.R.2    Yu, J.3    Thiel, S.C.4    Vajda, S.5
  • 34
    • 80051966197 scopus 로고    scopus 로고
    • Structural conservation of druggable hot spots in protein-protein interfaces
    • doi: 1101835108, [pii]10.1073/pnas.1101835108
    • Kozakov, D., Hall, D. R., Chuang, G. Y., Cencic, R., Brenke, R., Grove, L. E. et al. (2011). Structural conservation of druggable hot spots in protein-protein interfaces.Proc. Natl Acad. Sci. USA, doi: 1101835108, [pii]10.1073/pnas.1101835108.
    • (2011) Proc. Natl. Acad. Sci. USA
    • Kozakov, D.1    Hall, D.R.2    Chuang, G.Y.3    Cencic, R.4    Brenke, R.5    Grove, L.E.6
  • 36
    • 78650054960 scopus 로고    scopus 로고
    • Conformational states of human rat sarcoma (Ras) protein complexed with its natural ligand GTP and their role for effector interaction and GTP hydrolysis
    • Spoerner, M., Hozsa, C., Poetzl, J. A., Reiss, K., Ganser, P., Geyer, M. & Kalbitzer, H. R. (2010). Conformational states of human rat sarcoma (Ras) protein complexed with its natural ligand GTP and their role for effector interaction and GTP hydrolysis. J. Biol. Chem. 285, 39768-39778.
    • (2010) J. Biol. Chem. , vol.285 , pp. 39768-39778
    • Spoerner, M.1    Hozsa, C.2    Poetzl, J.A.3    Reiss, K.4    Ganser, P.5    Geyer, M.6    Kalbitzer, H.R.7
  • 37
    • 0036534542 scopus 로고    scopus 로고
    • Protein-water interactions in a dynamic world
    • Mattos, C. (2002). Protein-water interactions in a dynamic world. Trends Biochem. Sci. 27, 203-208.
    • (2002) Trends Biochem. Sci. , vol.27 , pp. 203-208
    • Mattos, C.1
  • 39
    • 0033577288 scopus 로고    scopus 로고
    • A relaxation-compensated Carr-Purcell-Meiboom-Gill sequence for characterizing chemical exchange by NMR spectroscopy [13]
    • DOI 10.1021/ja983961a
    • Loria, J. P., Rance, M. & Palmer, A. G. (1999). A relaxation-compensated Carr-Purcell-Meiboom-Gill sequence for characterizing chemical exchange by NMR spectroscopy. J. Am. Chem. Soc. 121, 2331-2332. (Pubitemid 29152458)
    • (1999) Journal of the American Chemical Society , vol.121 , Issue.10 , pp. 2331-2332
    • Loria, J.P.1    Rance, M.2    Palmer III, A.G.3
  • 40
    • 4243155782 scopus 로고    scopus 로고
    • NMR characterization of the dynamics of biomacromolecules
    • Palmer, A. G., III (2004). NMR characterization of the dynamics of biomacromolecules. Chem. Rev. 104, 3623-3640.
    • (2004) Chem. Rev. , vol.104 , pp. 3623-3640
    • Palmer III, A.G.1
  • 41
    • 0033635157 scopus 로고    scopus 로고
    • Crystal structure and functional analysis of Ras binding to its effector phosphoinositide 3-kinase γ
    • Pacold, M. E., Suire, S., Perisic, O., Lara-Gonzalez, S., Davis, C. T., Walker, E.H. et al. (2000). Crystal structure and functional analysis of Ras binding to its effector phosphoinositide 3-kinase γ. Cell, 103, 931-943.
    • (2000) Cell , vol.103 , pp. 931-943
    • Pacold, M.E.1    Suire, S.2    Perisic, O.3    Lara-Gonzalez, S.4    Davis, C.T.5    Walker, E.H.6
  • 42
    • 0031778630 scopus 로고    scopus 로고
    • Structural basis for the interaction of Ras with RalGDS
    • DOI 10.1038/nsb0698-422
    • Huang, L., Hofer, F., Martin, G. S. & Kim, S. H. (1998). Structural basis for the interaction of Ras with RalGDS. Nat. Struct. Biol. 5, 422-426. (Pubitemid 28265022)
    • (1998) Nature Structural Biology , vol.5 , Issue.6 , pp. 422-426
    • Huang, L.1    Hofer, F.2    Martin, G.S.3    Kim, S.-H.4
  • 43
    • 3543012707 scopus 로고    scopus 로고
    • Crystallography & NMR system: A new software suite for macromolecular structure determination. Acta Crystallogr
    • Brunger, A. T., Adams, P. D., Clore, G. M., DeLano, W. L., Gros, P., Grosse-Kunstleve, R. W. et al. (1998). Crystallography & NMR system: a new software suite for macromolecular structure determination. Acta Crystallogr., Sect. D: Biol. Crystallogr. 54, 905-921.
    • (1998) Sect. D: Biol. Crystallogr. , vol.54 , pp. 905-921
    • Brunger, A.T.1    Adams, P.D.2    Clore, G.M.3    DeLano, W.L.4    Gros, P.5    Grosse-Kunstleve, R.W.6
  • 46
    • 79251593544 scopus 로고    scopus 로고
    • Macromolecular structure determination by NMR spectroscopy
    • Markley, J. D. (2009). Macromolecular structure determination by NMR spectroscopy. Struct. Bioinformatics, 2, 93-142.
    • (2009) Struct. Bioinformatics , vol.2 , pp. 93-142
    • Markley, J.D.1
  • 47
    • 0029400480 scopus 로고
    • NMRPipe: A multidimensional spectral processing system based on UNIX pipes
    • Delaglio, F., Grzesiek, S., Vuister, G. W., Zhu, G., Pfeifer, J. & Bax, A. (1995). NMRPipe: a multidimensional spectral processing system based on UNIX pipes. J. Biol. NMR, 6, 277-293.
    • (1995) J. Biol. NMR , vol.6 , pp. 277-293
    • Delaglio, F.1    Grzesiek, S.2    Vuister, G.W.3    Zhu, G.4    Pfeifer, J.5    Bax, A.6
  • 48
    • 63549111769 scopus 로고    scopus 로고
    • Probabilistic interaction network of evidence algorithm and its application to complete labeling of peak lists from protein NMR spectroscopy
    • doi:10.1371/journal.pcbi.1000307
    • Bahrami, A., Assadi, A. H., Markley, J. L. & Eghbalnia, H. R. (2009). Probabilistic interaction network of evidence algorithm and its application to complete labeling of peak lists from protein NMR spectroscopy. PLoS Comput. Biol. 5, e1000307, doi:10.1371/journal.pcbi.1000307.
    • (2009) PLoS Comput. Biol. , vol.5
    • Bahrami, A.1    Assadi, A.H.2    Markley, J.L.3    Eghbalnia, H.R.4
  • 49
    • 68549111266 scopus 로고    scopus 로고
    • PINE-SPARKY: Graphical interface for evaluating automated probabilistic peak assignments in protein NMR spectroscopy
    • Lee, W., Westler, W. M., Bahrami, A., Eghbalnia, H. R. & Markley, J. L. (2009). PINE-SPARKY: graphical interface for evaluating automated probabilistic peak assignments in protein NMR spectroscopy. Bioinformatics, 25, 2085-2087.
    • (2009) Bioinformatics , vol.25 , pp. 2085-2087
    • Lee, W.1    Westler, W.M.2    Bahrami, A.3    Eghbalnia, H.R.4    Markley, J.L.5
  • 52
    • 25144515100 scopus 로고    scopus 로고
    • Improvement of duty-cycle heating compensation in NMR spin relaxation experiments
    • DOI 10.1016/j.jmr.2005.06.003, PII S109078070500193X
    • Yip, G. N. & Zuiderweg, E. R. (2005). Improvement of duty-cycle heating compensation in NMR spin relaxation experiments. J. Magn. Reson. 176, 171-178. (Pubitemid 41336684)
    • (2005) Journal of Magnetic Resonance , vol.176 , Issue.2 , pp. 171-178
    • Yip, G.N.B.1    Zuiderweg, E.R.P.2
  • 54
    • 0032871220 scopus 로고    scopus 로고
    • Estimating the time scale of chemical exchange of proteins from measurements of transverse relaxation rates in solution
    • DOI 10.1023/A:1008324025406
    • Ishima, R. & Torchia, D. A. (1999). Estimating the time scale of chemical exchange of proteins from measurements of transverse relaxation rates in solution. J. Biomol. NMR, 14, 369-372. (Pubitemid 29469059)
    • (1999) Journal of Biomolecular NMR , vol.14 , Issue.4 , pp. 369-372
    • Ishima, R.1    Torchia, D.A.2
  • 55
    • 36849127400 scopus 로고
    • Nuclear magnetic resonance study of the protolysis of trimethylammonium ion in aqueous solution - Order of the reaction with respect to solvent
    • Luz, Z. & Meiboom, S. (1963). Nuclear magnetic resonance study of the protolysis of trimethylammonium ion in aqueous solution - order of the reaction with respect to solvent. J. Chem. Phys. 39, 366-370.
    • (1963) J. Chem. Phys. , vol.39 , pp. 366-370
    • Luz, Z.1    Meiboom, S.2
  • 56
    • 0034728579 scopus 로고    scopus 로고
    • The static magnetic field dependence of chemical exchange linebroadening defines the NMR chemical shift time scale
    • DOI 10.1021/ja993511y
    • Millet, O., Loria, J. P., Kroenke, C. D., Pons, M. &Palmer, A. G. (2000). The static magnetic field dependence of chemical exchange linebroadening defines the NMR chemical shift time scale. J. Am. Chem. Soc. 122, 2867-2877. (Pubitemid 30191047)
    • (2000) Journal of the American Chemical Society , vol.122 , Issue.12 , pp. 2867-2877
    • Millet, O.1    Loria, J.P.2    Kroenke, C.D.3    Pons, M.4    Palmer III, A.G.5


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