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Volumn 85, Issue , 2011, Pages 1-26

Application of computational methods to the design of fatty acid amide hydrolase (FAAH) inhibitors based on a carbamic template structure

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EID: 80052788690     PISSN: 18761623     EISSN: None     Source Type: Book Series    
DOI: 10.1016/B978-0-12-386485-7.00001-6     Document Type: Chapter
Times cited : (12)

References (60)
  • 2
    • 27744466783 scopus 로고    scopus 로고
    • Mechanism of carbamate inactivation of FAAH: Implications for the design of covalent inhibitors and in vivo functional probes for enzymes
    • DOI 10.1016/j.chembiol.2005.08.011, PII S107455210500267X
    • J.P. Alexander, and B.F. Cravatt Mechanism of carbamate inactivation of FAAH: implications for the design of covalent inhibitors and in vivo functional probes for enzymes Chem. Biol. 12 2005 1179 1187 (Pubitemid 41628253)
    • (2005) Chemistry and Biology , vol.12 , Issue.11 , pp. 1179-1187
    • Alexander, J.P.1    Cravatt, B.F.2
  • 3
    • 73449121150 scopus 로고    scopus 로고
    • Structure-based drug design strategies in medicinal chemistry
    • A.D. Andricopulo, L.B. Salum, and D.J. Abraham Structure-based drug design strategies in medicinal chemistry Curr. Top. Med. Chem. 9 2009 771 790
    • (2009) Curr. Top. Med. Chem. , vol.9 , pp. 771-790
    • Andricopulo, A.D.1    Salum, L.B.2    Abraham, D.J.3
  • 4
    • 0035665229 scopus 로고    scopus 로고
    • The linear interaction energy method for predicting ligand binding free energies
    • J. Aqvist, and J. Marelius The linear interaction energy method for predicting ligand binding free energies Comb. Chem. High. Throughput Screen. 4 2001 613 626 (Pubitemid 34003156)
    • (2001) Combinatorial Chemistry and High Throughput Screening , vol.4 , Issue.8 , pp. 613-626
    • Aqvist, J.1    Marelius, J.2
  • 5
    • 67650635375 scopus 로고    scopus 로고
    • Endocannabinoids in the treatment of mood disorders: Evidence from animal models
    • F.R. Bambico, A. Duranti, A. Tontini, G. Tarzia, and G. Gobbi Endocannabinoids in the treatment of mood disorders: evidence from animal models Curr. Pharm. Des. 15 2009 1623 1646
    • (2009) Curr. Pharm. Des. , vol.15 , pp. 1623-1646
    • Bambico, F.R.1    Duranti, A.2    Tontini, A.3    Tarzia, G.4    Gobbi, G.5
  • 6
    • 10844248401 scopus 로고    scopus 로고
    • Tandem mass spectrometric data-FAAH inhibitory activity relationships of some carbamic acid O-aryl esters
    • DOI 10.1002/jms.729
    • E. Basso, A. Duranti, M. Mor, D. Piomelli, A. Tontini, and G. Tarzia Tandem mass spectrometric data-FAAH inhibitory activity relationships of some carbamic acid O-aryl esters J. Mass Spectrom. 39 2004 1450 1455 (Pubitemid 39664930)
    • (2004) Journal of Mass Spectrometry , vol.39 , Issue.12 , pp. 1450-1455
    • Basso, E.1    Duranti, A.2    Mor, M.3    Piomelli, D.4    Tontini, A.5    Tarzia, G.6    Traldi, P.7
  • 7
    • 2242490907 scopus 로고    scopus 로고
    • Structural adaptations in a membrane enzyme that terminates endocannabinoid signaling
    • DOI 10.1126/science.1076535
    • M.H. Bracey, M.A. Hanson, K.R. Masuda, R.C. Stevens, and B.F. Cravatt Structural adaptation in a membrane enzyme that terminates endocannabinoid signaling Science 298 2002 1793 1796 (Pubitemid 35404124)
    • (2002) Science , vol.298 , Issue.5599 , pp. 1793-1796
    • Bracey, M.H.1    Hanson, M.A.2    Masuda, K.R.3    Stevens, R.C.4    Cravatt, B.F.5
  • 9
    • 0001389474 scopus 로고
    • An extended linear response method for determining free energies of hydration
    • H.A. Carlson, and W.L. Jorgensen An extended linear response method for determining free energies of hydration J. Phys. Chem. 99 1995 10667 10673
    • (1995) J. Phys. Chem. , vol.99 , pp. 10667-10673
    • Carlson, H.A.1    Jorgensen, W.L.2
  • 10
    • 77949363118 scopus 로고    scopus 로고
    • Novel irreversible epidermal growth factor receptor inhibitors by chemical modulation of the cysteine-trap portion
    • C. Carmi, A. Cavazzoni, S. Vezzosi, F. Bordi, F. Vacondio, and C. Silva Novel irreversible epidermal growth factor receptor inhibitors by chemical modulation of the cysteine-trap portion J. Med. Chem. 53 2010 2038 2050
    • (2010) J. Med. Chem. , vol.53 , pp. 2038-2050
    • Carmi, C.1    Cavazzoni, A.2    Vezzosi, S.3    Bordi, F.4    Vacondio, F.5    Silva, C.6
  • 11
    • 69749121642 scopus 로고    scopus 로고
    • A second generation of carbamate-based fatty acid amide hydrolase inhibitors with improved activity in vivo
    • J.R. Clapper, F. Vacondio, A.R. King, A. Duranti, A. Tontini, and C. Silva A second generation of carbamate-based fatty acid amide hydrolase inhibitors with improved activity in vivo ChemMedChem 4 2009 1505 1513
    • (2009) ChemMedChem , vol.4 , pp. 1505-1513
    • Clapper, J.R.1    Vacondio, F.2    King, A.R.3    Duranti, A.4    Tontini, A.5    Silva, C.6
  • 13
    • 77952844866 scopus 로고    scopus 로고
    • Single-molecule pulling simulations can discern active from inactive enzyme inhibitors
    • F. Colizzi, R. Perozzo, L. Scapozza, M. Recanatini, and A. Cavalli Single-molecule pulling simulations can discern active from inactive enzyme inhibitors J. Am. Chem. Soc. 132 2010 7361 7371
    • (2010) J. Am. Chem. Soc. , vol.132 , pp. 7361-7371
    • Colizzi, F.1    Perozzo, R.2    Scapozza, L.3    Recanatini, M.4    Cavalli, A.5
  • 14
    • 79955045990 scopus 로고    scopus 로고
    • Bridging quantum mechanics and structure-based drug design
    • M. De Vivo Bridging quantum mechanics and structure-based drug design Front. Biosci. 16 2011 1619 1633
    • (2011) Front. Biosci. , vol.16 , pp. 1619-1633
    • De Vivo, M.1
  • 15
    • 65249124122 scopus 로고    scopus 로고
    • Computations of standard binding free energies with molecular dynamics simulations
    • Y. Deng, and B. Roux Computations of standard binding free energies with molecular dynamics simulations J. Phys. Chem. B 113 2009 2234 2346
    • (2009) J. Phys. Chem. B , vol.113 , pp. 2234-2346
    • Deng, Y.1    Roux, B.2
  • 16
    • 79954989328 scopus 로고    scopus 로고
    • Theoretical and computational approaches to ligand-based drug discovery
    • A.D. Favia Theoretical and computational approaches to ligand-based drug discovery Front. Biosci. 16 2011 1276 1290
    • (2011) Front. Biosci. , vol.16 , pp. 1276-1290
    • Favia, A.D.1
  • 17
    • 84986513644 scopus 로고
    • A combined quantum-mechanical and molecular mechanical potential for molecular-dynamics simulations
    • M.J. Field, P.A. Bash, and M. Karplus A combined quantum-mechanical and molecular mechanical potential for molecular-dynamics simulations J. Comput. Chem. 11 1990 700 733
    • (1990) J. Comput. Chem. , vol.11 , pp. 700-733
    • Field, M.J.1    Bash, P.A.2    Karplus, M.3
  • 18
    • 0036283048 scopus 로고    scopus 로고
    • Evolution and physics in comparative protein structure modeling
    • A. Fiser, M. Feig, C.L. Brooks 3rd, and A. Sali Evolution and physics in comparative protein structure modeling Acc. Chem. Res. 35 2002 413 421
    • (2002) Acc. Chem. Res. , vol.35 , pp. 413-421
    • Fiser, A.1    Feig, M.2    Brooks III, C.L.3    Sali, A.4
  • 19
    • 77249093143 scopus 로고    scopus 로고
    • Enol carbamates as inhibitors of fatty acid amide hydrolase (FAAH) endowed with high selectivity for FAAH over the other targets of the endocannabinoid system
    • S. Gattinoni, C. De Simone, S. Dallavalle, F. Fezza, R. Nannei, and D. Amadio Enol carbamates as inhibitors of fatty acid amide hydrolase (FAAH) endowed with high selectivity for FAAH over the other targets of the endocannabinoid system ChemMedChem 5 2010 357 360
    • (2010) ChemMedChem , vol.5 , pp. 357-360
    • Gattinoni, S.1    De Simone, C.2    Dallavalle, S.3    Fezza, F.4    Nannei, R.5    Amadio, D.6
  • 20
    • 0001246294 scopus 로고    scopus 로고
    • Generalized born model based on a surface integral formulation
    • A. Ghosh, C. Sendrovic Rapp, and R.A. Friesner Generalized Born model based on a surface integral formulation J. Phys. Chem. B 102 1998 10983 10990 (Pubitemid 128716615)
    • (1998) Journal of Physical Chemistry B , vol.102 , Issue.52 , pp. 10983-10990
    • Ghosh, A.1    Rapp, C.S.2    Friesner, R.A.3
  • 23
    • 67649225348 scopus 로고    scopus 로고
    • Efficient drug lead discovery and optimization
    • W.L. Jorgensen Efficient drug lead discovery and optimization Acc. Chem. Res. 42 2009 724 733
    • (2009) Acc. Chem. Res. , vol.42 , pp. 724-733
    • Jorgensen, W.L.1
  • 25
    • 8844263008 scopus 로고    scopus 로고
    • Docking and scoring in virtual screening for drug discovery: Methods and applications
    • DOI 10.1038/nrd1549
    • D.B. Kitchen, H. Decornez, J.R. Furr, and J. Bajorath Docking and scoring in virtual screening for drug discovery: methods and applications Nat. Rev. Drug Discov. 3 2004 935 949 (Pubitemid 39529931)
    • (2004) Nature Reviews Drug Discovery , vol.3 , Issue.11 , pp. 935-949
    • Kitchen, D.B.1    Decornez, H.2    Furr, J.R.3    Bajorath, J.4
  • 26
    • 33745199815 scopus 로고    scopus 로고
    • Virtual ligand screening: Strategies, perspectives and limitations
    • G. Klebe Virtual ligand screening: strategies, perspectives and limitations Drug Discov. Today 11 2006 580 594
    • (2006) Drug Discov. Today , vol.11 , pp. 580-594
    • Klebe, G.1
  • 27
    • 34548200847 scopus 로고    scopus 로고
    • Structure-based drug design: Docking and scoring
    • DOI 10.2174/138920307781369382
    • R.T. Kroemer Structure-based drug design: docking and scoring Curr. Protein Pept. Sci. 8 2007 312 328 (Pubitemid 47317039)
    • (2007) Current Protein and Peptide Science , vol.8 , Issue.4 , pp. 312-328
    • Kroemer, R.T.1
  • 28
    • 33749245117 scopus 로고    scopus 로고
    • Prediction of protein-ligand interactions. Docking and scoring: Successes and gaps
    • DOI 10.1021/jm060999m
    • A.R. Leach, B.K. Shoichet, and C.E. Peishoff Prediction of protein-ligand interactions. Docking and scoring: successes and gaps J. Med. Chem. 49 2006 5851 5855 (Pubitemid 44484931)
    • (2006) Journal of Medicinal Chemistry , vol.49 , Issue.20 , pp. 5851-5855
    • Leach, A.R.1    Shoichet, B.K.2    Peishoff, C.E.3
  • 29
    • 25444523794 scopus 로고    scopus 로고
    • QM/MM modelling of oleamide hydrolysis in fatty acid amide hydrolase (FAAH) reveals a new mechanism of nucleophile activation
    • DOI 10.1039/b503887a
    • A. Lodola, M. Mor, J.C. Hermann, G. Tarzia, D. Piomelli, and A.J. Mulholland QM/MM modelling of oleamide hydrolysis in fatty acid amide hydrolase (FAAH) reveals a new mechanism of nucleophile activation Chem. Commun. 2005 4399 4401 (Pubitemid 41375016)
    • (2005) Chemical Communications , Issue.35 , pp. 4399-4401
    • Lodola, A.1    Mor, M.2    Hermann, J.C.3    Tarzia, G.4    Piomelli, D.5    Mulholland, A.J.6
  • 30
    • 37349122437 scopus 로고    scopus 로고
    • Identification of productive inhibitor binding orientation in fatty acid amide hydrolase (FAAH) by QM/MM mechanistic modelling
    • DOI 10.1039/b714136j
    • A. Lodola, M. Mor, S. Rivara, C. Christov, G. Tarzia, and D. Piomelli Identification of productive inhibitor binding orientation in fatty acid amide hydrolase (FAAH) by QM/MM mechanistic modelling Chem. Commun. 2008 214 216 (Pubitemid 350294105)
    • (2008) Chemical Communications , Issue.2 , pp. 214-216
    • Lodola, A.1    Mor, M.2    Rivara, S.3    Christov, C.4    Tarzia, G.5    Piomelli, D.6    Mulholland, A.J.7
  • 31
    • 65549124465 scopus 로고    scopus 로고
    • Insights into the mechanism and inhibition of fatty acid amide hydrolase from quantum mechanics/molecular mechanics (QM/MM) modeling
    • A. Lodola, M. Mor, J. Sirirak, and A.J. Mulholland Insights into the mechanism and inhibition of fatty acid amide hydrolase from quantum mechanics/molecular mechanics (QM/MM) modeling Biochem. Soc. Trans. 37 2009 363 367
    • (2009) Biochem. Soc. Trans. , vol.37 , pp. 363-367
    • Lodola, A.1    Mor, M.2    Sirirak, J.3    Mulholland, A.J.4
  • 32
    • 79952258863 scopus 로고    scopus 로고
    • Understanding the role of carbamate reactivity in fatty acid amide hydrolase inhibition by QM/MM mechanistic modelling
    • A. Lodola, L. Capoferri, S. Rivara, E. Chudyk, J. Sirirak, and E. Dyguda-Kazimierowicz Understanding the role of carbamate reactivity in fatty acid amide hydrolase inhibition by QM/MM mechanistic modelling Chem. Commun. 47 2011 2517 2519
    • (2011) Chem. Commun. , vol.47 , pp. 2517-2519
    • Lodola, A.1    Capoferri, L.2    Rivara, S.3    Chudyk, E.4    Sirirak, J.5    Dyguda-Kazimierowicz, E.6
  • 36
    • 22244484464 scopus 로고    scopus 로고
    • Structure and function of fatty acid amide hydrolase
    • DOI 10.1146/annurev.biochem.74.082803.133450
    • M.K. McKinney, and B.F. Cravatt Structure and function of fatty acid amide hydrolase Annu. Rev. Biochem. 74 2005 411 432 (Pubitemid 40995513)
    • (2005) Annual Review of Biochemistry , vol.74 , pp. 411-432
    • McKinney, M.K.1    Cravatt, B.E.2
  • 37
    • 77955663115 scopus 로고    scopus 로고
    • Prediction of protein-ligand binding affinity by free energy simulations: Assumptions, pitfalls and expectations
    • J. Michel, and J.W. Essex Prediction of protein-ligand binding affinity by free energy simulations: assumptions, pitfalls and expectations J. Comput. Aided. Mol. Des. 24 2010 639 658
    • (2010) J. Comput. Aided. Mol. Des. , vol.24 , pp. 639-658
    • Michel, J.1    Essex, J.W.2
  • 38
    • 77954385220 scopus 로고    scopus 로고
    • Crystal structure of fatty acid amide hydrolase bound to the carbamate inhibitor URB597: Discovery of a deacylating water molecule and insight into enzyme inactivation
    • M. Mileni, S. Kamtekar, D.C. Wood, T.E. Benson, B.F. Cravatt, and R.C. Stevens Crystal structure of fatty acid amide hydrolase bound to the carbamate inhibitor URB597: discovery of a deacylating water molecule and insight into enzyme inactivation J. Mol. Biol. 400 2010 743 754
    • (2010) J. Mol. Biol. , vol.400 , pp. 743-754
    • Mileni, M.1    Kamtekar, S.2    Wood, D.C.3    Benson, T.E.4    Cravatt, B.F.5    Stevens, R.C.6
  • 39
    • 77954379126 scopus 로고    scopus 로고
    • Discovery and development of endocannabinoid-hydrolyzing enzyme inhibitors
    • A. Minkkilä, S. Saario, and T. Nevalainen Discovery and development of endocannabinoid-hydrolyzing enzyme inhibitors Curr. Top. Med. Chem. 10 2010 828 858
    • (2010) Curr. Top. Med. Chem. , vol.10 , pp. 828-858
    • Minkkilä, A.1    Saario, S.2    Nevalainen, T.3
  • 40
    • 79952115220 scopus 로고    scopus 로고
    • Pharmacological tools in endocannabinoid neurobiology
    • M. Mor, and A. Lodola Pharmacological tools in endocannabinoid neurobiology Curr. Top. Behav. Neurosci. 1 2009 87 110
    • (2009) Curr. Top. Behav. Neurosci. , vol.1 , pp. 87-110
    • Mor, M.1    Lodola, A.2
  • 41
    • 4744354729 scopus 로고    scopus 로고
    • Cyclohexylcarbamic acid 3′- or 4′-substituted biphenyl-3-yl esters as fatty acid amide hydrolase inhibitors: Synthesis, quantitative structure-activity relationships, and molecular modeling studies
    • DOI 10.1021/jm031140x
    • M. Mor, S. Rivara, A. Lodola, P.V. Plazzi, G. Tarzia, and A. Duranti Cyclohexylcarbamic acid 3′- or 4′-substituted biphenyl-3-yl esters as fatty acid amide hydrolase inhibitors: synthesis, quantitative structure-activity relationships, and molecular modelling studies J. Med. Chem. 47 2004 4998 5008 (Pubitemid 39314898)
    • (2004) Journal of Medicinal Chemistry , vol.47 , Issue.21 , pp. 4998-5008
    • Mor, M.1    Rivara, S.2    Lodola, A.3    Plazzi, P.V.4    Tarzia, G.5    Duranti, A.6    Tontini, A.7    Piersanti, G.8    Kathuria, S.9    Piomelli, D.10
  • 43
    • 45749124873 scopus 로고    scopus 로고
    • Synthesis and structure-reactivity relationship of fatty acid amide hydrolase inhibitors: Modulation at the N-portion of biphenyl-3-yl alkylcarbamates
    • M. Mor, A. Lodola, S. Rivara, F. Vacondio, A. Duranti, and A. Tontini Synthesis and structure-reactivity relationship of fatty acid amide hydrolase inhibitors: modulation at the N-portion of biphenyl-3-yl alkylcarbamates J. Med. Chem. 51 2008 3484 3498
    • (2008) J. Med. Chem. , vol.51 , pp. 3484-3498
    • Mor, M.1    Lodola, A.2    Rivara, S.3    Vacondio, F.4    Duranti, A.5    Tontini, A.6
  • 44
    • 77954819357 scopus 로고    scopus 로고
    • Endocannabinoid biosynthesis and inactivation, from simple to complex
    • G.G. Muccioli Endocannabinoid biosynthesis and inactivation, from simple to complex Drug Discov. Today 15 2010 474 483
    • (2010) Drug Discov. Today , vol.15 , pp. 474-483
    • Muccioli, G.G.1
  • 45
    • 27144494583 scopus 로고    scopus 로고
    • Modelling enzyme reaction mechanisms, specificity and catalysis
    • DOI 10.1016/S1359-6446(05)03611-1, PII S1359644605036111
    • A.J. Mulholland Modelling enzyme reaction mechanisms, specificity and catalysis Drug Discov. Today 10 2005 1393 1402 (Pubitemid 41501794)
    • (2005) Drug Discovery Today , vol.10 , Issue.20 , pp. 1393-1402
    • Mulholland, A.J.1
  • 46
    • 74549185125 scopus 로고    scopus 로고
    • FAAH and MAGL inhibitors: Therapeutic opportunities from regulating endocannabinoid levels
    • S. Petrosino, and V. Di Marzo FAAH and MAGL inhibitors: therapeutic opportunities from regulating endocannabinoid levels Curr. Opin. Invest. Drugs 11 2010 51 62
    • (2010) Curr. Opin. Invest. Drugs , vol.11 , pp. 51-62
    • Petrosino, S.1    Di Marzo, V.2
  • 47
    • 0242268553 scopus 로고    scopus 로고
    • The molecular logic of endocannabinoid signalling
    • DOI 10.1038/nrn1247
    • D. Piomelli The molecular logic of endocannabinoid signalling Nat. Rev. Neurosci. 4 2003 873 884 (Pubitemid 37351427)
    • (2003) Nature Reviews Neuroscience , vol.4 , Issue.11 , pp. 873-884
    • Piomelli, D.1
  • 48
    • 21344432777 scopus 로고    scopus 로고
    • The endocannabinoid system: A drug discovery perspective
    • D. Piomelli The endocannabinoid system: a drug discovery perspective Curr. Opin. Invest. Drugs 6 2005 672 679 (Pubitemid 40904037)
    • (2005) Current Opinion in Investigational Drugs , vol.6 , Issue.7 , pp. 672-679
    • Piomelli, D.1
  • 50
    • 57349170752 scopus 로고    scopus 로고
    • Discovery and development of fatty acid amide hydrolase (FAAH) inhibitors
    • M. Seierstad, and J.G. Breitenbucher Discovery and development of fatty acid amide hydrolase (FAAH) inhibitors J. Med. Chem. 51 2008 7327 7343
    • (2008) J. Med. Chem. , vol.51 , pp. 7327-7343
    • Seierstad, M.1    Breitenbucher, J.G.2
  • 51
    • 1842653539 scopus 로고    scopus 로고
    • History of quantitative structure-activity relationship
    • D.J. Abraham, John Wiley & Sons Hoboken
    • C.D. Selassie History of quantitative structure-activity relationship D.J. Abraham, Burger's Medicinal Chemistry and Drug Discovery vol. 1 2003 John Wiley & Sons Hoboken 1 48
    • (2003) Burger's Medicinal Chemistry and Drug Discovery , vol.1 , pp. 1-48
    • Selassie, C.D.1
  • 52
    • 60349127442 scopus 로고    scopus 로고
    • QM/MM methods for biomolecular systems
    • H.M. Senn, and W. Thiel QM/MM methods for biomolecular systems Angew. Chem. Int. Ed. 48 2009 1198 1229
    • (2009) Angew. Chem. Int. Ed. , vol.48 , pp. 1198-1229
    • Senn, H.M.1    Thiel, W.2
  • 54
    • 77955405511 scopus 로고    scopus 로고
    • Synthesis and structure-activity relationships of N-(2-oxo-3-oxetanyl) amides as N-acylethanolamine-hydrolyzing acid amidase inhibitors
    • C. Solorzano, F. Antonietti, A. Duranti, A. Tontini, S. Rivara, and A. Lodola Synthesis and structure-activity relationships of N-(2-oxo-3-oxetanyl) amides as N-acylethanolamine-hydrolyzing acid amidase inhibitors J. Med. Chem. 53 2010 5770 5781
    • (2010) J. Med. Chem. , vol.53 , pp. 5770-5781
    • Solorzano, C.1    Antonietti, F.2    Duranti, A.3    Tontini, A.4    Rivara, S.5    Lodola, A.6
  • 56
    • 33746301093 scopus 로고    scopus 로고
    • Synthesis and structure-activity relationships of FAAH inhibitors: Cyclohexylcarbamic acid biphenyl esters with chemical modulation at the proximal phenyl ring
    • DOI 10.1002/cmdc.200500017
    • G. Tarzia, A. Duranti, G. Gatti, G. Piersanti, A. Tontini, and S. Rivara Synthesis and structure-activity relationships of FAAH inhibitors: cyclohexylcarbamic acid biphenyl esters with chemical modulation at the proximal phenyl ring ChemMedChem 1 2006 130 139 (Pubitemid 44104985)
    • (2006) ChemMedChem , vol.1 , Issue.1 , pp. 130-139
    • Tarzia, G.1    Duranti, A.2    Gatti, G.3    Piersanti, G.4    Tontini, A.5    Rivara, S.6    Lodola, A.7    Plazzi, P.V.8    Mor, M.9    Kathuria, S.10    Piomelli, D.11
  • 57
    • 20444411998 scopus 로고    scopus 로고
    • Recent trends in quantitative structure-activity relationship
    • D.J. Abraham, John Wiley & Sons Hoboken
    • A. Tropsha Recent trends in quantitative structure-activity relationship D.J. Abraham, Burger's Medicinal Chemistry and Drug Discovery vol. 1 2003 John Wiley & Sons Hoboken 49 76
    • (2003) Burger's Medicinal Chemistry and Drug Discovery , vol.1 , pp. 49-76
    • Tropsha, A.1
  • 58
    • 69849098851 scopus 로고    scopus 로고
    • Structure-property relationships of a class of carbamate-based fatty acid amide hydrolase (FAAH) inhibitors: Chemical and biological stability
    • F. Vacondio, C. Silva, A. Lodola, A. Fioni, S. Rivara, and A. Duranti Structure-property relationships of a class of carbamate-based fatty acid amide hydrolase (FAAH) inhibitors: chemical and biological stability ChemMedChem 4 2009 1495 1504
    • (2009) ChemMedChem , vol.4 , pp. 1495-1504
    • Vacondio, F.1    Silva, C.2    Fioni, A.3    Rivara, S.4    Duranti, A.5
  • 60
    • 79951543355 scopus 로고    scopus 로고
    • A water-swap reaction coordinate for the calculation of absolute protein-ligand binding free energies
    • C.J. Woods, M. Malaisree, S. Hannongbua, and A.J. Mulholland A water-swap reaction coordinate for the calculation of absolute protein-ligand binding free energies J. Chem. Phys. 134 2011 054114
    • (2011) J. Chem. Phys. , vol.134 , pp. 054114
    • Woods, C.J.1    Malaisree, M.2    Hannongbua, S.3    Mulholland, A.J.4


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