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Volumn 584, Issue 13, 2010, Pages 2759-2766

Examining the case for the effect of barrier compression on tunneling, vibrationally enhanced catalysis, catalytic entropy and related issues

Author keywords

Barrier compression; Catalytic entropy; Enzyme catalysis; Kinetic isotope effect; Promoting mode; Tunneling

Indexed keywords

ALCOHOL DEHYDROGENASE; ENZYME; OXIDOREDUCTASE;

EID: 77953692230     PISSN: 00145793     EISSN: None     Source Type: Journal    
DOI: 10.1016/j.febslet.2010.04.062     Document Type: Review
Times cited : (76)

References (60)
  • 3
    • 0001214684 scopus 로고
    • Enzyme catalysis and transition structures in vacuo. Transition structures for the enolization, carboxylation and oxygenation reactions in ribulose-1,5-bisphosphate carboxylase/oxygenase enzyme (Rubisco)
    • Tapia O., Andrés J., Safront V.S. Enzyme catalysis and transition structures in vacuo. Transition structures for the enolization, carboxylation and oxygenation reactions in ribulose-1,5-bisphosphate carboxylase/oxygenase enzyme (Rubisco). J. Chem. Soc., Faraday Trans. 1 1994, 90:2365-2374.
    • (1994) J. Chem. Soc., Faraday Trans. 1 , vol.90 , pp. 2365-2374
    • Tapia, O.1    Andrés, J.2    Safront, V.S.3
  • 4
    • 0013971370 scopus 로고
    • The 3-dimensional structure of an enzyme molecule
    • Phillips D.C. The 3-dimensional structure of an enzyme molecule. Sci. Am. 1966, 215:78-90.
    • (1966) Sci. Am. , vol.215 , pp. 78-90
    • Phillips, D.C.1
  • 6
    • 0033470016 scopus 로고    scopus 로고
    • Transition state structure invariance to model system size and calculation levels: a QM/MM study of the carboxylation step catalyzed by Rubisco
    • Moliner V., Andrés J., Oliva M., Safont V.S., Tapia O. Transition state structure invariance to model system size and calculation levels: a QM/MM study of the carboxylation step catalyzed by Rubisco. Theor. Chem. Acc. 1999, 101:228-233.
    • (1999) Theor. Chem. Acc. , vol.101 , pp. 228-233
    • Moliner, V.1    Andrés, J.2    Oliva, M.3    Safont, V.S.4    Tapia, O.5
  • 7
    • 0037022251 scopus 로고    scopus 로고
    • The mechanism of catalysis of the chorismate to prephenate reaction by the Escherichia coli mutase enzyme
    • Hur S., Bruice T.C. The mechanism of catalysis of the chorismate to prephenate reaction by the Escherichia coli mutase enzyme. Proc. Natl. Acad. Sci. USA 2002, 99:1176-1181.
    • (2002) Proc. Natl. Acad. Sci. USA , vol.99 , pp. 1176-1181
    • Hur, S.1    Bruice, T.C.2
  • 8
    • 0037433232 scopus 로고    scopus 로고
    • Enzymes do what is expected (Chalcone Isomerase versus Chorismate Mutase)
    • Hur S., Bruice T.C. Enzymes do what is expected (Chalcone Isomerase versus Chorismate Mutase). J. Am Chem. Soc. 2003, 125:1472-1473.
    • (2003) J. Am Chem. Soc. , vol.125 , pp. 1472-1473
    • Hur, S.1    Bruice, T.C.2
  • 9
    • 0041429611 scopus 로고    scopus 로고
    • Apparent NAC effect in chorismate mutase reflects electrostatic transition state stabilization
    • Štrajbl M., Shurki A., Kato M., Warshel A. Apparent NAC effect in chorismate mutase reflects electrostatic transition state stabilization. J. Am. Chem. Soc. 2003, 125:10228-10237.
    • (2003) J. Am. Chem. Soc. , vol.125 , pp. 10228-10237
    • Štrajbl, M.1    Shurki, A.2    Kato, M.3    Warshel, A.4
  • 11
    • 2942739060 scopus 로고    scopus 로고
    • Conformational effects in enzyme catalysis: QM/MM free energy calculation of the 'NAC' contribution in chorismate mutase
    • Ranaghan K.E., Mulholland A.J. Conformational effects in enzyme catalysis: QM/MM free energy calculation of the 'NAC' contribution in chorismate mutase. Chem. Commun. 2004, 1238-1239.
    • (2004) Chem. Commun. , pp. 1238-1239
    • Ranaghan, K.E.1    Mulholland, A.J.2
  • 12
    • 2342565009 scopus 로고    scopus 로고
    • Transition state stabilization and substrate strain in enzyme catalysis: ab initio QM/MM modelling of the chorismate mutase reaction
    • Ranaghan K.E., Ridder L., Szefczyk B., Sokalski W.A., Hermann J.C., Mulholland A.J. Transition state stabilization and substrate strain in enzyme catalysis: ab initio QM/MM modelling of the chorismate mutase reaction. Org. Biomol. Chem. 2004, 2:968-980.
    • (2004) Org. Biomol. Chem. , vol.2 , pp. 968-980
    • Ranaghan, K.E.1    Ridder, L.2    Szefczyk, B.3    Sokalski, W.A.4    Hermann, J.C.5    Mulholland, A.J.6
  • 13
    • 4944242943 scopus 로고    scopus 로고
    • Enzymes: by chance, or by design?
    • Ball P. Enzymes: by chance, or by design?. Nature 2004, 431:396.
    • (2004) Nature , vol.431 , pp. 396
    • Ball, P.1
  • 14
    • 0032817216 scopus 로고    scopus 로고
    • 2OH on the distance between reactants when catalyzed by horse liver alcohol dehydrogenase and 203 single point mutants
    • 2OH on the distance between reactants when catalyzed by horse liver alcohol dehydrogenase and 203 single point mutants. Bioorg. Chem. 1999, 27:289-296.
    • (1999) Bioorg. Chem. , vol.27 , pp. 289-296
    • Luo, J.1    Kahn, K.2    Bruice, T.C.3
  • 16
    • 0024723235 scopus 로고
    • Quantum-mechanical effects in enzyme-catalyzed hydrogen transfer-reactions
    • Klinman J.P. Quantum-mechanical effects in enzyme-catalyzed hydrogen transfer-reactions. Trends Biochem. Sci. 1989, 14:368-377.
    • (1989) Trends Biochem. Sci. , vol.14 , pp. 368-377
    • Klinman, J.P.1
  • 17
    • 0037426823 scopus 로고    scopus 로고
    • A computational method to identify residues important in creating a protein promoting vibration in enzymes
    • Mincer J.S., Schwartz S.D. A computational method to identify residues important in creating a protein promoting vibration in enzymes. J. Phys. Chem. B 2003, 107:366-371.
    • (2003) J. Phys. Chem. B , vol.107 , pp. 366-371
    • Mincer, J.S.1    Schwartz, S.D.2
  • 18
    • 85056405071 scopus 로고    scopus 로고
    • Vibrationally enhanced tunneling and kinetic isotope effects in enzymatic reactions
    • CRC, Boca Raton, FL, A. Kohen, H.H. Limbach (Eds.)
    • Schwartz S.D. Vibrationally enhanced tunneling and kinetic isotope effects in enzymatic reactions. Isotope Effects in Chemistry and Biology 2004, 475-498. CRC, Boca Raton, FL. A. Kohen, H.H. Limbach (Eds.).
    • (2004) Isotope Effects in Chemistry and Biology , pp. 475-498
    • Schwartz, S.D.1
  • 19
    • 68049085675 scopus 로고    scopus 로고
    • A 21st century revisionist's view at a turning point in enzymology
    • Nagel Z.D., Klinman J.P. A 21st century revisionist's view at a turning point in enzymology. Nat. Chem. Biol. 2009, 5:543-550.
    • (2009) Nat. Chem. Biol. , vol.5 , pp. 543-550
    • Nagel, Z.D.1    Klinman, J.P.2
  • 20
    • 0037123216 scopus 로고    scopus 로고
    • Temperature-dependent isotope effects in soybean lipoxygenase-1: correlating hydrogen tunneling with protein dynamics
    • Knapp M.J., Rickert K., Klinman J.P. Temperature-dependent isotope effects in soybean lipoxygenase-1: correlating hydrogen tunneling with protein dynamics. J. Am. Chem. Soc. 2002, 124:3865-3874.
    • (2002) J. Am. Chem. Soc. , vol.124 , pp. 3865-3874
    • Knapp, M.J.1    Rickert, K.2    Klinman, J.P.3
  • 21
    • 33846307373 scopus 로고    scopus 로고
    • Promoting motions in enzyme catalysis probed by pressure studies of kinetic isotope effects
    • Hay S., Sutcliffe M.J., Scrutton N.S. Promoting motions in enzyme catalysis probed by pressure studies of kinetic isotope effects. Proc. Natl. Acad. Sci. USA 2007, 104:507-512.
    • (2007) Proc. Natl. Acad. Sci. USA , vol.104 , pp. 507-512
    • Hay, S.1    Sutcliffe, M.J.2    Scrutton, N.S.3
  • 22
    • 74049100280 scopus 로고    scopus 로고
    • Barrier compression and its contribution to both classical and quantum mechanical aspects of enzyme catalysis
    • Hay S., Johannissen L.O., Sutcliffe M.J., Scrutton N.S. Barrier compression and its contribution to both classical and quantum mechanical aspects of enzyme catalysis. Biophys. J. 2010, 98:121-128.
    • (2010) Biophys. J. , vol.98 , pp. 121-128
    • Hay, S.1    Johannissen, L.O.2    Sutcliffe, M.J.3    Scrutton, N.S.4
  • 23
    • 34547456661 scopus 로고    scopus 로고
    • Origin of the temperature dependence of isotope effects in enzymatic reactions: the case of dihydrofolate reductase
    • Liu H., Warshel A. Origin of the temperature dependence of isotope effects in enzymatic reactions: the case of dihydrofolate reductase. J. Phys. Chem. B 2007, 111:7852-7861.
    • (2007) J. Phys. Chem. B , vol.111 , pp. 7852-7861
    • Liu, H.1    Warshel, A.2
  • 24
    • 0036301901 scopus 로고    scopus 로고
    • Environmentally coupled hydrogen tunneling - linking catalysis to dynamics
    • Knapp M.J., Klinman J.P. Environmentally coupled hydrogen tunneling - linking catalysis to dynamics. Eur. J. Biochem. 2002, 269:3113-3121.
    • (2002) Eur. J. Biochem. , vol.269 , pp. 3113-3121
    • Knapp, M.J.1    Klinman, J.P.2
  • 26
    • 33748365234 scopus 로고    scopus 로고
    • Transition state theory can be used in studies of enzyme catalysis: lessons from simulations of tunneling and dynamical effects in lipoxygenase and other systems
    • Olsson M.H.M., Mavri J., Warshel A. Transition state theory can be used in studies of enzyme catalysis: lessons from simulations of tunneling and dynamical effects in lipoxygenase and other systems. Philos. Trans. R. Soc. B 2006, 361:1417-1432.
    • (2006) Philos. Trans. R. Soc. B , vol.361 , pp. 1417-1432
    • Olsson, M.H.M.1    Mavri, J.2    Warshel, A.3
  • 28
    • 72249089538 scopus 로고    scopus 로고
    • Evidence to support the hypothesis that promoting vibrations enhance the rate of an enzyme catalyzed H-tunneling reaction
    • Pudney C.R., Hay S., Levy C., Pang J., Sutcliffe M.J., Leys D., Scrutton N.S. Evidence to support the hypothesis that promoting vibrations enhance the rate of an enzyme catalyzed H-tunneling reaction. J. Am. Chem. Soc. 2009, 131:17072-17073.
    • (2009) J. Am. Chem. Soc. , vol.131 , pp. 17072-17073
    • Pudney, C.R.1    Hay, S.2    Levy, C.3    Pang, J.4    Sutcliffe, M.J.5    Leys, D.6    Scrutton, N.S.7
  • 29
    • 0023396209 scopus 로고
    • The uncoupled O-H or O-D stretch in water as an internal pressure gauge for high-pressure infrared spectroscopy of aqueous systems
    • Wong P.T.T., Moffat D.J. The uncoupled O-H or O-D stretch in water as an internal pressure gauge for high-pressure infrared spectroscopy of aqueous systems. Appl. Spectr. 1987, 41:1070-1072.
    • (1987) Appl. Spectr. , vol.41 , pp. 1070-1072
    • Wong, P.T.T.1    Moffat, D.J.2
  • 32
    • 0346500562 scopus 로고    scopus 로고
    • Molecular dynamics simulations of water and biomolecules with a Monte Carlo constant pressure algorithm
    • Åqvist J., Wennerström P., Nervall M., Bjelic S., Brandsdal B.O. Molecular dynamics simulations of water and biomolecules with a Monte Carlo constant pressure algorithm. Chem. Phys. Lett. 2004, 384:288-294.
    • (2004) Chem. Phys. Lett. , vol.384 , pp. 288-294
    • Åqvist, J.1    Wennerström, P.2    Nervall, M.3    Bjelic, S.4    Brandsdal, B.O.5
  • 33
    • 0017100947 scopus 로고
    • Theoretical studies of enzymic reactions: dielectric, electrostatic and steric stabilization of the carbonium ion in the reaction of lysozyme
    • Warshel A., Levitt M. Theoretical studies of enzymic reactions: dielectric, electrostatic and steric stabilization of the carbonium ion in the reaction of lysozyme. J. Mol. Biol. 1976, 103:227-249.
    • (1976) J. Mol. Biol. , vol.103 , pp. 227-249
    • Warshel, A.1    Levitt, M.2
  • 34
    • 44449093622 scopus 로고    scopus 로고
    • Deep tunneling dominates the biologically important hydride transfer reaction from NADH to FMN in Morphinone reductase
    • Pang J., Hay S., Scrutton N.S., Sutcliffe M.J. Deep tunneling dominates the biologically important hydride transfer reaction from NADH to FMN in Morphinone reductase. J. Am. Chem. Soc. 2008, 130:7092-7097.
    • (2008) J. Am. Chem. Soc. , vol.130 , pp. 7092-7097
    • Pang, J.1    Hay, S.2    Scrutton, N.S.3    Sutcliffe, M.J.4
  • 35
    • 77955127388 scopus 로고    scopus 로고
    • (in press) An analysis of all the relevant facts and arguments indicates that enzyme catalysis does not involve large contributions from nuclear tunneling
    • Kamerlin, S.C.L. and Warshel, A. (in press) An analysis of all the relevant facts and arguments indicates that enzyme catalysis does not involve large contributions from nuclear tunneling. J. Phys. Org. Chem.
    • J. Phys. Org. Chem.
    • Kamerlin, S.C.L.1    Warshel, A.2
  • 36
    • 0034097153 scopus 로고    scopus 로고
    • Effect of pressure on deuterium isotope effects of yeast alcohol dehydrogenase: evidence for mechanical models of catalysis
    • Northrop D.B., Cho Y.K. Effect of pressure on deuterium isotope effects of yeast alcohol dehydrogenase: evidence for mechanical models of catalysis. Biochemistry 2000, 39:2406-2412.
    • (2000) Biochemistry , vol.39 , pp. 2406-2412
    • Northrop, D.B.1    Cho, Y.K.2
  • 37
    • 1042282260 scopus 로고    scopus 로고
    • Donor-acceptor distance and protein promoting vibration coupling to hydride transfer: a possible mechanism for kinetic control in isozymes of human lactate dehydrogenase
    • Basner J.E., Schwartz S.D. Donor-acceptor distance and protein promoting vibration coupling to hydride transfer: a possible mechanism for kinetic control in isozymes of human lactate dehydrogenase. J. Phys. Chem. B 2004, 108:444-451.
    • (2004) J. Phys. Chem. B , vol.108 , pp. 444-451
    • Basner, J.E.1    Schwartz, S.D.2
  • 38
    • 0037104752 scopus 로고    scopus 로고
    • Promoting modes and demoting modes in enzyme-catalyzed proton transfer reactions: a study of models and realistic systems
    • Cui Q.A., Karplus M. Promoting modes and demoting modes in enzyme-catalyzed proton transfer reactions: a study of models and realistic systems. J. Phys. Chem. B 2002, 106:7927-7947.
    • (2002) J. Phys. Chem. B , vol.106 , pp. 7927-7947
    • Cui, Q.A.1    Karplus, M.2
  • 39
    • 0347866726 scopus 로고    scopus 로고
    • Activated chemistry in the presence of a strongly symmetrically coupled vibration
    • Antoniou D., Schwartz S.D. Activated chemistry in the presence of a strongly symmetrically coupled vibration. J. Chem. Phys. 1998, 108:3620-3625.
    • (1998) J. Chem. Phys. , vol.108 , pp. 3620-3625
    • Antoniou, D.1    Schwartz, S.D.2
  • 40
    • 10044273966 scopus 로고    scopus 로고
    • Promoting vibrations in human purine nucleoside phosphorylase. A molecular dynamics and hybrid quantum mechanical/molecular mechanical study
    • Nunez S., Antoniou D., Schramm V.L., Schwartz S.D. Promoting vibrations in human purine nucleoside phosphorylase. A molecular dynamics and hybrid quantum mechanical/molecular mechanical study. J. Am. Chem. Soc. 2004, 126:15720-15729.
    • (2004) J. Am. Chem. Soc. , vol.126 , pp. 15720-15729
    • Nunez, S.1    Antoniou, D.2    Schramm, V.L.3    Schwartz, S.D.4
  • 41
    • 33646935697 scopus 로고    scopus 로고
    • Dynamical contributions to enzyme catalysis: critical tests of a popular hypothesis
    • Olsson M.H.M., Parson W.W., Warshel A. Dynamical contributions to enzyme catalysis: critical tests of a popular hypothesis. Chem. Rev. 2006, 106:1737-1756.
    • (2006) Chem. Rev. , vol.106 , pp. 1737-1756
    • Olsson, M.H.M.1    Parson, W.W.2    Warshel, A.3
  • 42
    • 77951226274 scopus 로고    scopus 로고
    • At the dawn of the 21st century: is dynamics the missing link for understanding enzyme catalysis?
    • Kamerlin S.C.L., Warshel A. At the dawn of the 21st century: is dynamics the missing link for understanding enzyme catalysis?. Proteins: Struct. Funct. Bioinformat. 2010, 78:1339-1375.
    • (2010) Proteins: Struct. Funct. Bioinformat. , vol.78 , pp. 1339-1375
    • Kamerlin, S.C.L.1    Warshel, A.2
  • 44
    • 0035707451 scopus 로고    scopus 로고
    • Dynamics of biochemical and biophysical reactions: insight from computer simulations
    • Warshel A., Parson W.W. Dynamics of biochemical and biophysical reactions: insight from computer simulations. Q. Rev. Biophys. 2001, 34:563-670.
    • (2001) Q. Rev. Biophys. , vol.34 , pp. 563-670
    • Warshel, A.1    Parson, W.W.2
  • 45
    • 9344245168 scopus 로고    scopus 로고
    • N2 reaction of dehalogenase as a general benchmark
    • N2 reaction of dehalogenase as a general benchmark. J. Am. Chem. Soc. 2004, 126:15167-15179.
    • (2004) J. Am. Chem. Soc. , vol.126 , pp. 15167-15179
    • Olsson, M.H.M.1    Warshel, A.2
  • 46
    • 0033519723 scopus 로고    scopus 로고
    • Enzyme dynamics and hydrogen tunnelling in a thermophilic alcohol dehydrogenase
    • Kohen A., Cannio R., Bartolucci S., Klinman J.P. Enzyme dynamics and hydrogen tunnelling in a thermophilic alcohol dehydrogenase. Nature 1999, 399:496-499.
    • (1999) Nature , vol.399 , pp. 496-499
    • Kohen, A.1    Cannio, R.2    Bartolucci, S.3    Klinman, J.P.4
  • 47
    • 33750441144 scopus 로고    scopus 로고
    • Coordinated effects of distal mutations on environmentally coupled tunneling in dihydrofolate reductase
    • Wang L., Goodey N.M., Benkovic S.J., Kohen A. Coordinated effects of distal mutations on environmentally coupled tunneling in dihydrofolate reductase. Proc. Natl. Acad. Sci. USA 2006, 103:15753-15758.
    • (2006) Proc. Natl. Acad. Sci. USA , vol.103 , pp. 15753-15758
    • Wang, L.1    Goodey, N.M.2    Benkovic, S.J.3    Kohen, A.4
  • 48
    • 0035940264 scopus 로고    scopus 로고
    • Energetics and dynamics of enzymatic reactions
    • Villà J., Warshel A. Energetics and dynamics of enzymatic reactions. J. Phys. Chem. B 2001, 105:7887-7907.
    • (2001) J. Phys. Chem. B , vol.105 , pp. 7887-7907
    • Villà, J.1    Warshel, A.2
  • 49
    • 62249181529 scopus 로고    scopus 로고
    • An integrated model for enzyme catalysis emerges from studies of hydrogen tunneling
    • Klinman J.P. An integrated model for enzyme catalysis emerges from studies of hydrogen tunneling. Chem. Phys. Lett. 2009, 471:179-193.
    • (2009) Chem. Phys. Lett. , vol.471 , pp. 179-193
    • Klinman, J.P.1
  • 50
    • 0034663824 scopus 로고    scopus 로고
    • Temperature effects on the catalytic efficiency, rate enhancement, and transition state affinity of cytidine deaminase, and the thermodynamic consequences for catalysis of removing a substrate " anchor"
    • Snider M.J., Gaunitz S., Ridgway C., Short S.A., Wolfenden R. Temperature effects on the catalytic efficiency, rate enhancement, and transition state affinity of cytidine deaminase, and the thermodynamic consequences for catalysis of removing a substrate " anchor" Biochemistry 2000, 39:9746-9753.
    • (2000) Biochemistry , vol.39 , pp. 9746-9753
    • Snider, M.J.1    Gaunitz, S.2    Ridgway, C.3    Short, S.A.4    Wolfenden, R.5
  • 52
    • 52249116531 scopus 로고    scopus 로고
    • Cold adaptation of enzyme reaction rates
    • Sinisa B., Brandsdal B., Aqvist J. Cold adaptation of enzyme reaction rates. Biochemistry 2008, 47:10049-10057.
    • (2008) Biochemistry , vol.47 , pp. 10049-10057
    • Sinisa, B.1    Brandsdal, B.2    Aqvist, J.3
  • 53
    • 52949128744 scopus 로고    scopus 로고
    • On the relationship between folding and chemical landscapes in enzyme catalysis
    • Roca M., Messer B., Hilvert D., Warshel A. On the relationship between folding and chemical landscapes in enzyme catalysis. Proc. Natl. Acad. Sci. USA 2008, 105:13877-13882.
    • (2008) Proc. Natl. Acad. Sci. USA , vol.105 , pp. 13877-13882
    • Roca, M.1    Messer, B.2    Hilvert, D.3    Warshel, A.4
  • 56
    • 0000997465 scopus 로고    scopus 로고
    • Calculations of activation entropies of chemical reactions in solution
    • Štrajbl M., Sham Y.Y., Villà J., Chu Z.T., Warshel A. Calculations of activation entropies of chemical reactions in solution. J. Phys. Chem. B 2000, 104:4578-4584.
    • (2000) J. Phys. Chem. B , vol.104 , pp. 4578-4584
    • Štrajbl, M.1    Sham, Y.Y.2    Villà, J.3    Chu, Z.T.4    Warshel, A.5
  • 57
    • 67650079411 scopus 로고    scopus 로고
    • Toward accurate microscopic calculation of solvation entropies: extending the restraint release approach to studies of solvation effects
    • Singh N., Warshel A. Toward accurate microscopic calculation of solvation entropies: extending the restraint release approach to studies of solvation effects. J. Phys. Chem. B 2009, 113:7372-7382.
    • (2009) J. Phys. Chem. B , vol.113 , pp. 7372-7382
    • Singh, N.1    Warshel, A.2
  • 58
    • 77951247516 scopus 로고    scopus 로고
    • A comprehensive examination of the contributions to binding entropy of protein-ligand complexes
    • Singh N., Warshel A. A comprehensive examination of the contributions to binding entropy of protein-ligand complexes. Proteins: Struct. Funct. Bioinformat. 2010, 8:1724-1735.
    • (2010) Proteins: Struct. Funct. Bioinformat. , vol.8 , pp. 1724-1735
    • Singh, N.1    Warshel, A.2
  • 60
    • 34250827316 scopus 로고    scopus 로고
    • Infrared spectrum of 4-methoxypicolinic acid N-oxide: computation of asymmetric O-H stretching band
    • Balazic K., Stare J., Mavri J. Infrared spectrum of 4-methoxypicolinic acid N-oxide: computation of asymmetric O-H stretching band. J. Chem. Inf. Model. 2007, 47:832-839.
    • (2007) J. Chem. Inf. Model. , vol.47 , pp. 832-839
    • Balazic, K.1    Stare, J.2    Mavri, J.3


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