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Volumn 4, Issue 6, 2008, Pages 974-984

pH dependence of a 3-helix versus a turn in the M-loop region of PDE4: Observations on PDB entries and an electronic structure study

Author keywords

[No Author keywords available]

Indexed keywords


EID: 58149114921     PISSN: 15499618     EISSN: None     Source Type: Journal    
DOI: 10.1021/ct700261b     Document Type: Article
Times cited : (4)

References (57)
  • 1
    • 33748686575 scopus 로고    scopus 로고
    • Cyclic Nucleotide Phosphodiesterases: Molecular Regulation to Clinical Use
    • (a) Bender, A. T.; Baevo, A. J. Cyclic Nucleotide Phosphodiesterases: Molecular Regulation to Clinical Use. Pharmacol Rev. 2006, 58, 488-520.
    • (2006) Pharmacol Rev , vol.58 , pp. 488-520
    • Bender, A.T.1    Baevo, A.J.2
  • 2
    • 0035224418 scopus 로고    scopus 로고
    • Houslay, M. D. PDE4-cAMP-specific Phosphodiesterases. Prog. Nucleic Acid Res. Mol. Biol. 2001, 69, 249-315.
    • (b) Houslay, M. D. PDE4-cAMP-specific Phosphodiesterases. Prog. Nucleic Acid Res. Mol. Biol. 2001, 69, 249-315.
  • 3
    • 33644811309 scopus 로고    scopus 로고
    • Phosphodiesterase Inhibitors in Airways Disease
    • (c) Chung, K. F. Phosphodiesterase Inhibitors in Airways Disease. Eur. J. Pharmacol. 2006, 533, 110-117.
    • (2006) Eur. J. Pharmacol , vol.533 , pp. 110-117
    • Chung, K.F.1
  • 5
    • 14544272401 scopus 로고    scopus 로고
    • Cyclic nucleotide Phosphodiesterases and their Role in Immunomodulatory Responses: Advances in the Development of Specific Phosphodiesterase Inhibitors
    • (a) Castro, A.; Jerez, M. J.; Martinez, A.; Gil, C. Cyclic nucleotide Phosphodiesterases and their Role in Immunomodulatory Responses: Advances in the Development of Specific Phosphodiesterase Inhibitors. Med. Res. Rev. 2005, 25, 229-244.
    • (2005) Med. Res. Rev , vol.25 , pp. 229-244
    • Castro, A.1    Jerez, M.J.2    Martinez, A.3    Gil, C.4
  • 8
    • 21144437565 scopus 로고    scopus 로고
    • Jeon, J. H.; Heo, Y.-S.; Kim, C. M.; Hyun, Y.-L.; Lee, T. G.; Ro, S.; Cho, J. M. Phosphodiestrase: Overview of Protein Structures, Potential Therapeutic Applications and Recent progress in Drug Development. Cell. Mol. Life Sci. 2005, 62, 1198-1220.
    • (a) Jeon, J. H.; Heo, Y.-S.; Kim, C. M.; Hyun, Y.-L.; Lee, T. G.; Ro, S.; Cho, J. M. Phosphodiestrase: Overview of Protein Structures, Potential Therapeutic Applications and Recent progress in Drug Development. Cell. Mol. Life Sci. 2005, 62, 1198-1220.
  • 9
    • 34347257750 scopus 로고    scopus 로고
    • Molecular Docking Studies of Pyridopurinone Derivatives - Potential Phosphodiesterases Inhibitor
    • (b) Srivani, P.; Srinivas, E.; Raghu, R.; Sastry, G. N. Molecular Docking Studies of Pyridopurinone Derivatives - Potential Phosphodiesterases Inhibitor. J. Mol. Graphics Modell. 2007, 26, 378-390.
    • (2007) J. Mol. Graphics Modell , vol.26 , pp. 378-390
    • Srivani, P.1    Srinivas, E.2    Raghu, R.3    Sastry, G.N.4
  • 11
    • 0037163858 scopus 로고    scopus 로고
    • Crystal structure of Phosphodiesterase 4D and Inhibitor complex
    • Lee, M. E.; Markowitz, J.; Lee, J.-O.; Lee, H. Crystal structure of Phosphodiesterase 4D and Inhibitor complex. FEBS Lett. 2002, 530, 53-58.
    • (2002) FEBS Lett , vol.530 , pp. 53-58
    • Lee, M.E.1    Markowitz, J.2    Lee, J.-O.3    Lee, H.4
  • 12
    • 0038154006 scopus 로고    scopus 로고
    • Three-dimensional Structures of PDE4D in Complex with Roliprams and Implication on Inhibitor selectivity
    • (a) Huai, Q.; Wang, H.; Sun, Y.; Kim, H.-Y.; Liu, Y.; Ke, H. Three-dimensional Structures of PDE4D in Complex with Roliprams and Implication on Inhibitor selectivity. Structure 2003, 11, 865-873.
    • (2003) Structure , vol.11 , pp. 865-873
    • Huai, Q.1    Wang, H.2    Sun, Y.3    Kim, H.-Y.4    Liu, Y.5    Ke, H.6
  • 13
    • 1842581748 scopus 로고    scopus 로고
    • Crystal structures of Phosphodiesterases 4 and 5 in Complex with Inhibitor 3-isobutyl-l-Methyl Xanthine suggest a Conformation Determinant of Inhibitor Selectivity
    • (b) Huai, Q.; Liu, Y.; Francis, S. H.; Corbin, J. D.; Ke, H. Crystal structures of Phosphodiesterases 4 and 5 in Complex with Inhibitor 3-isobutyl-l-Methyl Xanthine suggest a Conformation Determinant of Inhibitor Selectivity. J. Biol. Chem. 2004, 279, 13095-13101.
    • (2004) J. Biol. Chem , vol.279 , pp. 13095-13101
    • Huai, Q.1    Liu, Y.2    Francis, S.H.3    Corbin, J.D.4    Ke, H.5
  • 14
    • 0242401840 scopus 로고    scopus 로고
    • The crystal structure of AMP-bound PDE4 Suggests a Mechanism for Phosphodiesterase Catalysis
    • (a) Huai, Q.; Colicelli, J.; Ke, H. The crystal structure of AMP-bound PDE4 Suggests a Mechanism for Phosphodiesterase Catalysis. Biochemistry 2003, 42, 13220-13226.
    • (2003) Biochemistry , vol.42 , pp. 13220-13226
    • Huai, Q.1    Colicelli, J.2    Ke, H.3
  • 15
    • 1442323778 scopus 로고    scopus 로고
    • Crystal structures of the Catalytic Domain of Phosphodiesterase 4B complexed with AMP, 8-Br-AMP, and Rolipram
    • (b) Xu, R. X.; Rocque, W. J.; Lambert, M. H.; Vanderwall, D. E.; Luther, M. A.; Nolte, R. T. Crystal structures of the Catalytic Domain of Phosphodiesterase 4B complexed with AMP, 8-Br-AMP, and Rolipram. J. Mol. Biol. 2004, 337, 355-365.
    • (2004) J. Mol. Biol , vol.337 , pp. 355-365
    • Xu, R.X.1    Rocque, W.J.2    Lambert, M.H.3    Vanderwall, D.E.4    Luther, M.A.5    Nolte, R.T.6
  • 19
    • 33645382172 scopus 로고    scopus 로고
    • Enantiomer discrimination Illustrated by the High Resolution Crystal Structures of Type 4 Phosphodiesterase
    • Huai, Q.; Sun, Y.; Wang, H.; Macdonald, D.; Aspiotis, R.; Robinson, H.; Huang, Z.; Ke, H. Enantiomer discrimination Illustrated by the High Resolution Crystal Structures of Type 4 Phosphodiesterase. J. Med. Chem. 2006, 49, 1867-1873.
    • (2006) J. Med. Chem , vol.49 , pp. 1867-1873
    • Huai, Q.1    Sun, Y.2    Wang, H.3    Macdonald, D.4    Aspiotis, R.5    Robinson, H.6    Huang, Z.7    Ke, H.8
  • 20
    • 36749000152 scopus 로고    scopus 로고
    • Structures of the Four subfamilies of Phosphodiesterase-4 provide Insight into the Selectivity of their Inhibitors
    • Wang, H.; Peng, M.; Chen, Y.; Geng, J.; Robinson, H.; Houslay, M. D.; Cai, J.; Ke, H. Structures of the Four subfamilies of Phosphodiesterase-4 provide Insight into the Selectivity of their Inhibitors. Biochem. J. 2007, 408, 193-201.
    • (2007) Biochem. J , vol.408 , pp. 193-201
    • Wang, H.1    Peng, M.2    Chen, Y.3    Geng, J.4    Robinson, H.5    Houslay, M.D.6    Cai, J.7    Ke, H.8
  • 21
    • 58149122775 scopus 로고    scopus 로고
    • Nelson, D. L.; Cox, M. M. Amino acids, peptides and proteins. Lehninger Principles of Biochemistry, 4th ed.; W. H. Freman and Company: 41 Madison Avenue, New York, 2006.
    • Nelson, D. L.; Cox, M. M. Amino acids, peptides and proteins. Lehninger Principles of Biochemistry, 4th ed.; W. H. Freman and Company: 41 Madison Avenue, New York, 2006.
  • 22
    • 0028921182 scopus 로고
    • 10-Helix along the Thermodynamic Folding Pathway
    • 10-Helix along the Thermodynamic Folding Pathway. Biochemistry 1995, 34, 3873-77.
    • (1995) Biochemistry , vol.34 , pp. 3873-3877
    • Millhauser, G.L.1
  • 24
    • 24144469823 scopus 로고    scopus 로고
    • 10-Helix in a Three-Residue Peptide Chain: Role of Side Chain-Backbone Interactions as Evidenced by IR-UV Double Resonance Experiments
    • 10-Helix in a Three-Residue Peptide Chain: Role of Side Chain-Backbone Interactions as Evidenced by IR-UV Double Resonance Experiments. J. Am. Chem. Soc. 2005, 127, 11900-01.
    • (2005) J. Am. Chem. Soc , vol.127 , pp. 11900-11901
    • Chin, W.1    Piuzzi, F.2    Dognon, J.-P.3    Dimicoli, I.4    Tardivel, B.5    Mons, M.6
  • 25
    • 2642531012 scopus 로고    scopus 로고
    • Structural and Conformational Changes Concomitant with the E1-E2 Transition in H+K+-ATPase: A Comparative Protein Modeling Study
    • Bindu, P. H.; Sastry, G. M.; Murty, U. S. N.; Sastry, G. N. Structural and Conformational Changes Concomitant with the E1-E2 Transition in H+K+-ATPase: A Comparative Protein Modeling Study. Biochem. Biophys. Res. Commun. 2004, 319, 312-320.
    • (2004) Biochem. Biophys. Res. Commun , vol.319 , pp. 312-320
    • Bindu, P.H.1    Sastry, G.M.2    Murty, U.S.N.3    Sastry, G.N.4
  • 26
    • 58149127263 scopus 로고    scopus 로고
    • MOE version 2006; Chemical Computing Group, 954, First Floor, 16th Main, BTM Layout 2nd Stage, Bangalore, India 560 076
    • MOE version 2006; Chemical Computing Group, 954, First Floor, 16th Main, BTM Layout 2nd Stage, Bangalore, India 560 076.
  • 27
    • 0000189651 scopus 로고
    • Density-functional Thermochemistry. III. The role of exact exchange
    • (a) Becke, A. D. Density-functional Thermochemistry. III. The role of exact exchange. J. Chem. Phys. 1993, 98, 5648-5652.
    • (1993) J. Chem. Phys , vol.98 , pp. 5648-5652
    • Becke, A.D.1
  • 28
    • 4243553426 scopus 로고
    • Density-Functional Exchange-Energy Approximation with Correct Asymptotic Behavior
    • (b) Becke, A. D. Density-Functional Exchange-Energy Approximation with Correct Asymptotic Behavior. Phys. Rev. A 1988, 38, 3098-3100.
    • (1988) Phys. Rev. A , vol.38 , pp. 3098-3100
    • Becke, A.D.1
  • 29
    • 58149107237 scopus 로고    scopus 로고
    • Insight II Version 2000; Molecular Modelling System 2000 Molecular Simulations: 9685 Scrantan Road, San Deigo, CA
    • Insight II Version 2000; Molecular Modelling System 2000 Molecular Simulations: 9685 Scrantan Road, San Deigo, CA.
  • 30
    • 0033515394 scopus 로고    scopus 로고
    • A new ONIOM implementation in Gaussian98. Part I. The Calculation of Energies, Gradients, Vibrational Frequencies and Electric Field Derivatives
    • Dapprich, S.; Komáromi, I.; Suzie Byun, K.; Morokuma, K.; Frisch, M. J. A new ONIOM implementation in Gaussian98. Part I. The Calculation of Energies, Gradients, Vibrational Frequencies and Electric Field Derivatives. J. Mol. Struct. (Theochem) 1999, 462, 1-21.
    • (1999) J. Mol. Struct. (Theochem) , vol.462 , pp. 1-21
    • Dapprich, S.1    Komáromi, I.2    Suzie Byun, K.3    Morokuma, K.4    Frisch, M.J.5
  • 31
    • 0037473497 scopus 로고    scopus 로고
    • Vreven, T.; Morokuma, K.; Farkas, Ö.; Schlegel, H. B.; Frisch, M. J. Geometry Optimization with QM/MM, ONIOM, and Other Combined Methods. I. Microiterations and Constraints. J. Comput. Chem. 2003, 24, 760-769.
    • Vreven, T.; Morokuma, K.; Farkas, Ö.; Schlegel, H. B.; Frisch, M. J. Geometry Optimization with QM/MM, ONIOM, and Other Combined Methods. I. Microiterations and Constraints. J. Comput. Chem. 2003, 24, 760-769.
  • 32
    • 0042041206 scopus 로고
    • Full Periodic Table Force Field for Molecular Mechanics and Molecular Dynamics Simulations
    • Rappé, A. K.; Casewit, C. J.; Colwell, K. S.; Goddard, W. A., III; Skiff, W. M. UFF, A Full Periodic Table Force Field for Molecular Mechanics and Molecular Dynamics Simulations. J. Am. Chem. Soc. 1992, 114, 10024-35.
    • (1992) J. Am. Chem. Soc , vol.114 , pp. 10024-10035
    • Rappé, A.K.1    Casewit, C.J.2    Colwell, K.S.3    Goddard III, W.A.4    Skiff, W.M.5    UFF, A.6
  • 33
    • 58149133616 scopus 로고    scopus 로고
    • Gaussian 03, Revision B.03, Frisch, M. J, Trucks, G. W, Schlegel, H. B, Scuseria, G. E, Robb, M. A, Cheeseman, J. R, Montgomery, J. A, Jr, Vreven, T, Kudin, K. N, Burant, J. C, Millam, J. M, Iyengar, S. S, Tomasi, J, Barone, V, Mennucci, B, Cossi, M, Scalmani, G, Rega, N, Petersson, G. A, Nakatsuji, H, Hada, M, Ehara, M, Toyota, K, Fukuda, R, Hasegawa, J, Ishida, M, Nakajima, T, Honda, Y, Kitao,O, Nakai, H, Klene, M, Li, X, Knox, J. E, Hratchian, H. P, Cross, J. B, Bakken, V, Adamo, C, Jaramillo, J, Gomperts, R, Stratmann, R. E, Yazyev, O, Austin, A. J, Cammi, R, Pomelli, C, Ochterski, J. W, Ayala, P. Y, Morokuma, K, Voth, G. A, Salvador, P, Dannenberg, J. J, Zakrzewski, V. G, Dapprich, S, Daniels, A. D, Strain, M. C, Farkas, O, Malick, D. K, Rabuck, A. D, Raghavachari, K, Foresman, J. B, Ortiz, J. V, Cui, Q, Baboul, A. G, Clifford, S, Cioslowski, J, Stefanov, B. B, Liu, G, Liashenko, A, Piskorz, P, Komaromi, I
    • Gaussian 03, Revision B.03, Frisch, M. J.; Trucks, G. W.; Schlegel, H. B.; Scuseria, G. E.; Robb, M. A.; Cheeseman, J. R.; Montgomery, J. A., Jr.; Vreven, T.; Kudin, K. N.; Burant, J. C.; Millam, J. M.; Iyengar, S. S.; Tomasi, J.; Barone, V.; Mennucci, B.; Cossi, M.; Scalmani, G.; Rega, N.; Petersson, G. A.; Nakatsuji, H.; Hada, M.; Ehara, M.; Toyota, K.; Fukuda, R.; Hasegawa, J.; Ishida, M.; Nakajima, T.; Honda, Y.; Kitao,O.; Nakai, H.; Klene, M.; Li, X.; Knox, J. E.; Hratchian, H. P.; Cross, J. B.; Bakken, V.; Adamo, C.; Jaramillo, J.; Gomperts, R.; Stratmann, R. E.; Yazyev, O.; Austin, A. J.; Cammi, R.; Pomelli, C.; Ochterski, J. W.; Ayala, P. Y.; Morokuma, K.; Voth, G. A.; Salvador, P.; Dannenberg, J. J.; Zakrzewski, V. G.; Dapprich, S.; Daniels, A. D.; Strain, M. C.; Farkas, O.; Malick, D. K.; Rabuck, A. D.; Raghavachari, K.; Foresman, J. B.; Ortiz, J. V.; Cui, Q.; Baboul, A. G.; Clifford, S.; Cioslowski, J.; Stefanov, B. B.; Liu, G.; Liashenko, A.; Piskorz, P.; Komaromi, I.; Martin, R. L.; Fox, D. J.; Keith, T.; Al-Laham, M. A.; Peng, C. Y.; Nanayakkara, A.; Challacombe, M.; Gill, P. M. W. B.; Chen, W.; Wong, M. W.; Gonzalez, C.; Pople, J. A. Gaussian, Inc.: Wallingford, CT, 2003.
  • 37
    • 33846823909 scopus 로고
    • Particle mesh Ewald: An N·log(N) Method For Ewald Sums in Large Systems
    • Darden, T.; York, D.; Pedersen, L. Particle mesh Ewald: An N·log(N) Method For Ewald Sums in Large Systems. J. Chem. Phys. 1993, 98, 10089-92.
    • (1993) J. Chem. Phys , vol.98 , pp. 10089-10092
    • Darden, T.1    York, D.2    Pedersen, L.3
  • 39
    • 1642499126 scopus 로고    scopus 로고
    • Numerical Calculations of the pH of Maximal Protein Stability
    • (a) Alexov, E. Numerical Calculations of the pH of Maximal Protein Stability. Eur. J. Biochem. 2004, 271, 173-185.
    • (2004) Eur. J. Biochem , vol.271 , pp. 173-185
    • Alexov, E.1
  • 40
    • 0031076776 scopus 로고    scopus 로고
    • pH Dependence of Protein Stability: Absolute Electrostatic Free Energy Differences between Conformations
    • (b) Schaefer, M.; Sommer, M.; Karplus, M. pH Dependence of Protein Stability: Absolute Electrostatic Free Energy Differences between Conformations. J. Phys. Chem. 1997, 101, 1663-1683.
    • (1997) J. Phys. Chem , vol.101 , pp. 1663-1683
    • Schaefer, M.1    Sommer, M.2    Karplus, M.3
  • 41
    • 0028305457 scopus 로고
    • Prediciton of pH-Dependent Properties of Proteins
    • (c) Antosiewicz, J.; McCammon, J. A.; Gilson, M. K. Prediciton of pH-Dependent Properties of Proteins. J. MoL Biol. 1994, 238, 415-436.
    • (1994) J. MoL Biol , vol.238 , pp. 415-436
    • Antosiewicz, J.1    McCammon, J.A.2    Gilson, M.K.3
  • 42
    • 33746047069 scopus 로고    scopus 로고
    • The pH-dependence of Amide Chemical Shift of Asp/Glu Reflects its pka in Intrinsically Disordered Proteins with Local Interactions
    • (d) Pujato, M.; Navarro, A.; Versace, R.; Mancusso, R.; Ghose, R.; Tasayco, M. L. The pH-dependence of Amide Chemical Shift of Asp/Glu Reflects its pka in Intrinsically Disordered Proteins with Local Interactions. Biochim. Biophys. Acta 2006, 1764, 1227-1233.
    • (2006) Biochim. Biophys. Acta , vol.1764 , pp. 1227-1233
    • Pujato, M.1    Navarro, A.2    Versace, R.3    Mancusso, R.4    Ghose, R.5    Tasayco, M.L.6
  • 43
    • 0022386437 scopus 로고
    • Tailoring the pH Dependence of Enzyme Catalysis using Protein Engineering
    • (e) Thomas, P. G.; Russell, A. J.; Fersht, A. R. Tailoring the pH Dependence of Enzyme Catalysis using Protein Engineering. Nature 1985, 318, 375-376.
    • (1985) Nature , vol.318 , pp. 375-376
    • Thomas, P.G.1    Russell, A.J.2    Fersht, A.R.3
  • 44
    • 0026620720 scopus 로고
    • Conformational Changes in Cubic Insulin Crystals in the pH Range 7-11
    • Gursky, O.; Badger, J.; Li, Y.; Caspar, D. L. Conformational Changes in Cubic Insulin Crystals in the pH Range 7-11. Biophys. J. 1992, 63, 1210-1220.
    • (1992) Biophys. J , vol.63 , pp. 1210-1220
    • Gursky, O.1    Badger, J.2    Li, Y.3    Caspar, D.L.4
  • 47
    • 33845587527 scopus 로고    scopus 로고
    • Proton-Shuffle Mechanism of O-O Activation for Formation of a High-Valent Oxo-Iron Species of Bleomycin
    • (c) Kumar, D.; Hirao, H.; Shaik, S.; Kozlowski, P. M. Proton-Shuffle Mechanism of O-O Activation for Formation of a High-Valent Oxo-Iron Species of Bleomycin. J. Am. Chem. Soc. 2006, 128, 16148-16158.
    • (2006) J. Am. Chem. Soc , vol.128 , pp. 16148-16158
    • Kumar, D.1    Hirao, H.2    Shaik, S.3    Kozlowski, P.M.4
  • 52
    • 0037067059 scopus 로고    scopus 로고
    • Factors Governing The Protonation State of Cysteine In Proteins: An Ab initio/CDM study
    • (e) Dudev, T.; Lim, C. Factors Governing The Protonation State of Cysteine In Proteins: An Ab initio/CDM study. J. Am. Chem. Soc. 2002, 124, 6759-66.
    • (2002) J. Am. Chem. Soc , vol.124 , pp. 6759-6766
    • Dudev, T.1    Lim, C.2
  • 53
    • 10344226653 scopus 로고    scopus 로고
    • Determinants of Cysteine pKa Values in Creatine Kinase and a-Antitrypsin
    • Noar, M. M.; Jenson, J. H. Determinants of Cysteine pKa Values in Creatine Kinase and a-Antitrypsin. Proteins: Struct., Funct., Bioinfor. 2004, 57, 799-803.
    • (2004) Proteins: Struct., Funct., Bioinfor , vol.57 , pp. 799-803
    • Noar, M.M.1    Jenson, J.H.2
  • 54
    • 0035057633 scopus 로고    scopus 로고
    • Density Functional Computations of Proton Affinity and Gas-Phase Basicity of Proline
    • (a) Marino, T.; Russo, N.; Tocci, E.; Toscano, M. Density Functional Computations of Proton Affinity and Gas-Phase Basicity of Proline. J. Mass. Spectrom. 2001, 36, 301-305.
    • (2001) J. Mass. Spectrom , vol.36 , pp. 301-305
    • Marino, T.1    Russo, N.2    Tocci, E.3    Toscano, M.4
  • 56
    • 34247533707 scopus 로고    scopus 로고
    • Joseph, J.; Jemmis, E. D. Red-, Blue-, or No-Shift in Hydrogen Bonds: A Unified Explanation. J. Am. Chem. Soc. 2007, 129, 4620-4632.
    • Joseph, J.; Jemmis, E. D. Red-, Blue-, or No-Shift in Hydrogen Bonds: A Unified Explanation. J. Am. Chem. Soc. 2007, 129, 4620-4632.
  • 57
    • 20144385151 scopus 로고    scopus 로고
    • Design of Small-Sized Libraries by Combinatorial Assembly of Linkers and Functional Groups to a Given Scaffold: Application to the Structure-Based Optimization of a Phosphodiesterase 4 Inhibitor
    • Krier, M.; de Araújo-J-nior, J. X.; Schmitt, M.; Duranton, J.; Justiano-Basaran, H.; Lugnier, C.; Bourguignon, J.-J.; Rognan, D. Design of Small-Sized Libraries by Combinatorial Assembly of Linkers and Functional Groups to a Given Scaffold: Application to the Structure-Based Optimization of a Phosphodiesterase 4 Inhibitor. J. Med. Chem. 2005, 48, 3816-3822.
    • (2005) J. Med. Chem , vol.48 , pp. 3816-3822
    • Krier, M.1    de Araújo-J-nior, J.X.2    Schmitt, M.3    Duranton, J.4    Justiano-Basaran, H.5    Lugnier, C.6    Bourguignon, J.-J.7    Rognan, D.8


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