메뉴 건너뛰기




Volumn 46, Issue 24, 2003, Pages 5208-5221

Synthesis, Activity, and Molecular Modeling Studies of Novel Human Aldose Reductase Inhibitors Based on a Marine Natural Product

Author keywords

[No Author keywords available]

Indexed keywords

3,3',4,4'5,5' HEXACHLORO 2,2' DIHYDROXYDIPHENYL ETHER; ALDEHYDE REDUCTASE; ALDOSE REDUCTASE INHIBITOR; BROMINE; BROMOBENZENE; CHLOROBENZENE; DIPHENYL ETHER DERIVATIVE; FLUOROBENZENE; IDITOL DEHYDROGENASE; NATURAL PRODUCT; POLYBROMINATED DIPHENYL ETHER; POLYOL; SORBINIL; SORBITOL; TOLRESTAT; UNCLASSIFIED DRUG; ZENARESTAT; ZOPOLRESTAT;

EID: 0242607620     PISSN: 00222623     EISSN: None     Source Type: Journal    
DOI: 10.1021/jm030957n     Document Type: Article
Times cited : (61)

References (61)
  • 1
    • 0035856980 scopus 로고    scopus 로고
    • Biochemistry and Molecular Cell Biology of Diabetic Complications
    • Brownlee, M. Biochemistry and Molecular Cell Biology of Diabetic Complications. Nature 2001, 414, 813-820.
    • (2001) Nature , vol.414 , pp. 813-820
    • Brownlee, M.1
  • 2
    • 0015929739 scopus 로고
    • The Sorbitol Pathway and the Complications of Diabetes
    • Gabbay, K. H. The Sorbitol Pathway and the Complications of Diabetes. N. Engl. J. Med. 1973, 288, 831-836.
    • (1973) N. Engl. J. Med. , vol.288 , pp. 831-836
    • Gabbay, K.H.1
  • 3
    • 0023899991 scopus 로고
    • The Role of Aldose Reductase in the Development of Diabetic Complications
    • Kador, P. F. The Role of Aldose Reductase in the Development of Diabetic Complications. Med. Res. Rev. 1988, 8, 325-352.
    • (1988) Med. Res. Rev. , vol.8 , pp. 325-352
    • Kador, P.F.1
  • 4
    • 0027934146 scopus 로고
    • Aldose Reductase Inhibitors and Their Potential for the Treatment of Diabetic Complications
    • Tomlinson, D. R.; Stevens, E. J.; Diemel, L. Aldose Reductase Inhibitors and Their Potential for the Treatment of Diabetic Complications. Trends Pharmcol. Sci. 1994, 15, 293-297.
    • (1994) Trends Pharmcol. Sci. , vol.15 , pp. 293-297
    • Tomlinson, D.R.1    Stevens, E.J.2    Diemel, L.3
  • 5
    • 0031875592 scopus 로고    scopus 로고
    • Aldose Reductase: A Window to the Treatment of Diabetic Complications?
    • Crabbe, M. J. C.; Goode, D. Aldose Reductase: a Window to the Treatment of Diabetic Complications? Prog. Retin. Eye Res. 1998, 17, 313-383.
    • (1998) Prog. Retin. Eye Res. , vol.17 , pp. 313-383
    • Crabbe, M.J.C.1    Goode, D.2
  • 6
    • 0031920049 scopus 로고    scopus 로고
    • Aldose Reductase in Glucose Toxicity: A Potential Target for the Prevention of Diabetic Complications
    • Yabe-Nishimura, C. Aldose Reductase in Glucose Toxicity: a Potential Target for the Prevention of Diabetic Complications. Pharmacol. Rev. 1998, 50, 21-33.
    • (1998) Pharmacol. Rev. , vol.50 , pp. 21-33
    • Yabe-Nishimura, C.1
  • 8
    • 0032959371 scopus 로고    scopus 로고
    • Diabetes Complications and Their Potential Prevention: Aldose Reductase Inhibition and Other Approaches
    • Costantino, L.; Rastelli, G.; Vianello, P.; Cignarella, G.; Barlocco, D. Diabetes Complications and Their Potential Prevention: Aldose Reductase Inhibition and Other Approaches. Med. Res. Rev. 1999, 19, 3-23.
    • (1999) Med. Res. Rev. , vol.19 , pp. 3-23
    • Costantino, L.1    Rastelli, G.2    Vianello, P.3    Cignarella, G.4    Barlocco, D.5
  • 9
    • 0030751728 scopus 로고    scopus 로고
    • New Aldose Reductase Inhibitors as Potential Agents for the Prevention of Long-term Diabetic Complications
    • Costantino, L.; Rastelli, G.; Cignarella, G.; Vianello, P.; Barlocco, D. New Aldose Reductase Inhibitors as Potential Agents for the Prevention of Long-term Diabetic Complications. Exp. Opin. Ther. Pat. 1997, 7, 843-858.
    • (1997) Exp. Opin. Ther. Pat. , vol.7 , pp. 843-858
    • Costantino, L.1    Rastelli, G.2    Cignarella, G.3    Vianello, P.4    Barlocco, D.5
  • 10
    • 0027326529 scopus 로고
    • Aldose Reductase Inhibitors: Recent Developments
    • Sarges, R.; Oates, P. J. Aldose Reductase Inhibitors: Recent Developments. Prog. Drug Res. 1993, 40, 99-161.
    • (1993) Prog. Drug Res. , vol.40 , pp. 99-161
    • Sarges, R.1    Oates, P.J.2
  • 11
    • 0037392916 scopus 로고    scopus 로고
    • Aldose Reductase Inhibitors from Natural Sources
    • De la Fuente, J. A.; Manzanaro, S. Aldose Reductase Inhibitors from Natural Sources. Nat. Prod. Rep. 2003, 20, 243-251.
    • (2003) Nat. Prod. Rep. , vol.20 , pp. 243-251
    • De La Fuente, J.A.1    Manzanaro, S.2
  • 13
    • 0031570301 scopus 로고    scopus 로고
    • A 'Specificity' Pocket Inferred from the Crystal Structures of the Complexes of Aldose Reductase with Pharmaceutically Important Inhibitors Tolrestat and Sorbinil
    • Urzhumtsev, A.; Tete-Favier, F.; Mitschler, A.; Barbanton, J.; Parth, P. ; Urzhumtseva, L.; Biellmann, J.-F.; Podjarny, A. D.; Moras, D. A 'Specificity' Pocket Inferred from the Crystal Structures of the Complexes of Aldose Reductase with Pharmaceutically Important Inhibitors Tolrestat and Sorbinil. Structure 1997, 5, 601-612.
    • (1997) Structure , vol.5 , pp. 601-612
    • Urzhumtsev, A.1    Tete-Favier, F.2    Mitschler, A.3    Barbanton, J.4    Parth, P.5    Urzhumtseva, L.6    Biellmann, J.-F.7    Podjarny, A.D.8    Moras, D.9
  • 14
    • 0026719692 scopus 로고
    • An Unlikely Sugar Substrate in the 1.65 A Structure of the Human Aldose Reductase Holoenzyme Implicated in Diabetic Complications
    • Wilson, D. K.; Bohren, K. M.; Gabbay, K. H.; Quiocho, F. A. An Unlikely Sugar Substrate in the 1.65 A Structure of the Human Aldose Reductase Holoenzyme Implicated in Diabetic Complications. Science 1992, 257, 81-84.
    • (1992) Science , vol.257 , pp. 81-84
    • Wilson, D.K.1    Bohren, K.M.2    Gabbay, K.H.3    Quiocho, F.A.4
  • 15
    • 0027378377 scopus 로고
    • Refined 1.8 Å Structure of Human Aldose Reductase Complexed with the Potent Inhibitor Zopolrestat
    • Wilson, D. K.; Tarle, I.; Petrash, J. M.; Quiocho, F. A. Refined 1.8 Å Structure of Human Aldose Reductase Complexed with the Potent Inhibitor Zopolrestat. Proc. Natl. Acad. Sci. U.S.A. 1993, 90, 9847-9851.
    • (1993) Proc. Natl. Acad. Sci. U.S.A. , vol.90 , pp. 9847-9851
    • Wilson, D.K.1    Tarle, I.2    Petrash, J.M.3    Quiocho, F.A.4
  • 16
    • 0027461303 scopus 로고
    • Molecular Cloning of Testicular 20 Alpha-Hydroxysteroid Dehydrogenase: Identity with Aldose Reductase
    • Warren, J. C.; Murdock, G. L.; Ma, Y.; Goodman, S. R.; Zimmer, W. E. Molecular Cloning of Testicular 20 Alpha-Hydroxysteroid Dehydrogenase: Identity with Aldose Reductase. Biochemistry 1993, 32, 1401-1406.
    • (1993) Biochemistry , vol.32 , pp. 1401-1406
    • Warren, J.C.1    Murdock, G.L.2    Ma, Y.3    Goodman, S.R.4    Zimmer, W.E.5
  • 17
    • 0038167343 scopus 로고    scopus 로고
    • Computer Simulation Studies of the Catalytic Mechanism of Human Aldose Reductase
    • Várnai, P.; Warshel, A. Computer Simulation Studies of the Catalytic Mechanism of Human Aldose Reductase. J. Am. Chem. Soc. 2000, 122, 3849-3860.
    • (2000) J. Am. Chem. Soc. , vol.122 , pp. 3849-3860
    • Várnai, P.1    Warshel, A.2
  • 18
    • 0033975861 scopus 로고    scopus 로고
    • Isolation of a Non-Covalent Aldose Reductase-Nucleotide-Inhibitor Complex
    • Sugiyama, K.; Chen, Z.; Lee, Y. S.; Kador, P. F. Isolation of a Non-Covalent Aldose Reductase-Nucleotide-Inhibitor Complex. Biochem. Pharmacol. 2000, 59, 329-336.
    • (2000) Biochem. Pharmacol. , vol.59 , pp. 329-336
    • Sugiyama, K.1    Chen, Z.2    Lee, Y.S.3    Kador, P.F.4
  • 19
    • 0034664071 scopus 로고    scopus 로고
    • The Sorbinil Trap: A Predicted Dead-end Complex Confirms the Mechanism of Aldose Reductase Inhibition
    • Bohren, K. M.; Grimshaw, C. E. The Sorbinil Trap: a Predicted Dead-end Complex Confirms the Mechanism of Aldose Reductase Inhibition. Biochemistry 2000, 39, 9967-9974.
    • (2000) Biochemistry , vol.39 , pp. 9967-9974
    • Bohren, K.M.1    Grimshaw, C.E.2
  • 20
    • 0034128735 scopus 로고    scopus 로고
    • Structural Bases for the Inhibition of Aldose Reductase by Phenolic Compounds
    • Rastelli, G.; Antolini, L.; Benvenuti, S.; Costantino, L. Structural Bases for the Inhibition of Aldose Reductase by Phenolic Compounds. Bioorg. Med. Chem. 2000, 8, 1151-1158.
    • (2000) Bioorg. Med. Chem. , vol.8 , pp. 1151-1158
    • Rastelli, G.1    Antolini, L.2    Benvenuti, S.3    Costantino, L.4
  • 22
    • 0030931810 scopus 로고    scopus 로고
    • Aldose Reductase Inhibitors: The End of an Era or the Need for Different Trial Designs?
    • Pfeifer, M. A.; Schumer, M. P.; Gelber, D. A. Aldose Reductase Inhibitors: the End of an Era or the Need for Different Trial Designs? Diabetes 1997, 46 Suppl. 2, S82-89.
    • (1997) Diabetes , vol.46 , Issue.SUPPL.
    • Pfeifer, M.A.1    Schumer, M.P.2    Gelber, D.A.3
  • 26
    • 1342328481 scopus 로고
    • Polybrominated Diphenyl Ethers from Dysidea herbacea, Dysidea chlorea and Phyllospongia foliascens
    • Carté, B.; Faulkner, J. Polybrominated Diphenyl Ethers from Dysidea herbacea, Dysidea chlorea and Phyllospongia foliascens. Tetrahedron 1981, 37, 2335-2339.
    • (1981) Tetrahedron , vol.37 , pp. 2335-2339
    • Carté, B.1    Faulkner, J.2
  • 29
    • 0021837112 scopus 로고
    • Aldose Reductase Inhibitors: Flavonoids, Alkaloids, Acetophenones, Benzophenones, and Spirohydantoins of Chroman
    • Nakai, N.; Fujii, Y.; Kobashi, K.; Nomura, K. Aldose Reductase Inhibitors: Flavonoids, Alkaloids, Acetophenones, Benzophenones, and Spirohydantoins of Chroman. Arch. Biochem. Biophys. 1985, 239, 491-496.
    • (1985) Arch. Biochem. Biophys. , vol.239 , pp. 491-496
    • Nakai, N.1    Fujii, Y.2    Kobashi, K.3    Nomura, K.4
  • 31
    • 0035979364 scopus 로고    scopus 로고
    • Comparative Binding Energy (COMBINE) Analysis of the Substrate Specificity of Haloalkane Dehalogenase from Xanthobacter autotrophicus GJ10
    • Kmunicek, J.; Luengo, S.; Gago, F.; Ramirez Ortiz, A.; Wade, R.; Damborsky, J. Comparative Binding Energy (COMBINE) Analysis of the Substrate Specificity of Haloalkane Dehalogenase from Xanthobacter autotrophicus GJ10. Biochemistry 2001, 40, 8905-8917.
    • (2001) Biochemistry , vol.40 , pp. 8905-8917
    • Kmunicek, J.1    Luengo, S.2    Gago, F.3    Ramirez Ortiz, A.4    Wade, R.5    Damborsky, J.6
  • 32
    • 0036005614 scopus 로고    scopus 로고
    • The structure of human recombinant aldose reductase complexed with the potent inhibitor zenarestat
    • Kinoshita, T.; Miyake, H.; Fujii, T.; Takakura, S.; Goto, T. The structure of human recombinant aldose reductase complexed with the potent inhibitor zenarestat. Acta Crystallogr. D Biol. Crystallogr. 2002, 58, 622-626.
    • (2002) Acta Crystallogr. D Biol. Crystallogr. , vol.58 , pp. 622-626
    • Kinoshita, T.1    Miyake, H.2    Fujii, T.3    Takakura, S.4    Goto, T.5
  • 34
    • 0037194544 scopus 로고    scopus 로고
    • Synthesis of 3″-substituted TSAO derivatives with anti-HIV-1 and anti-HIV-2 activity through an efficient palladium-catalyzed cross-coupling approach
    • Lobatón, E.; Rodriguez-Barrios, F.; Gago, F.; Pé rez-Pérez, M. J.; De Clercq, E.; Balzarini, J.; Camarasa, M. J.; Velázquez, S. Synthesis of 3″-substituted TSAO derivatives with anti-HIV-1 and anti-HIV-2 activity through an efficient palladium-catalyzed cross-coupling approach. J. Med. Chem. 2002, 45, 3934-3945.
    • (2002) J. Med. Chem. , vol.45 , pp. 3934-3945
    • Lobatón, E.1    Rodriguez-Barrios, F.2    Gago, F.3    Pérez-Pérez, M.J.4    De Clercq, E.5    Balzarini, J.6    Camarasa, M.J.7    Velázquez, S.8
  • 36
    • 84954820170 scopus 로고
    • Allosteric Interactions of Metal Ions with Saccharides in a Crowned Diboronic Acid
    • Deng, G.; James, T. D.; Shinkai, S. Allosteric Interactions of Metal Ions with Saccharides in a Crowned Diboronic Acid. J. Am. Chem. Soc. 1994, 116, 4567-4572.
    • (1994) J. Am. Chem. Soc. , vol.116 , pp. 4567-4572
    • Deng, G.1    James, T.D.2    Shinkai, S.3
  • 38
    • 0027509591 scopus 로고
    • An Expedient Approach to the Diphenyl Ether Cross-linked Amino Acids of Glycopeptide Antibiotics
    • Rao, A. V. R.; Gurjar, M. K.; Kaiwar, V.; Khare, V. B. An Expedient Approach to the Diphenyl Ether Cross-linked Amino Acids of Glycopeptide Antibiotics. Tetrahedron Lett. 1993, 34, 1661-1664.
    • (1993) Tetrahedron Lett. , vol.34 , pp. 1661-1664
    • Rao, A.V.R.1    Gurjar, M.K.2    Kaiwar, V.3    Khare, V.B.4
  • 39
    • 0012865896 scopus 로고
    • Phenoxyquinones II. The Diphenoxyquinones
    • Ungnade, H. E.; Zilch, K. T. Phenoxyquinones II. The Diphenoxyquinones. J. Org. Chem. 1951, 16, 64-69.
    • (1951) J. Org. Chem. , vol.16 , pp. 64-69
    • Ungnade, H.E.1    Zilch, K.T.2
  • 41
    • 0242719086 scopus 로고
    • Substitution Products of 2′-Nitro- and 2′:4′ -Dinitro-2-methoxy-diphenyl Ethers
    • Scarborough, H. A.; Sweeten, J. L, Substitution Products of 2′-Nitro- and 2′:4′-Dinitro-2-methoxy-diphenyl Ethers. J. Chem. Soc. 1934, 867-869.
    • (1934) J. Chem. Soc. , pp. 867-869
    • Scarborough, H.A.1    Sweeten, J.L.2
  • 42
    • 37049146847 scopus 로고
    • Investigations in the Diphenylene Oxide Series. Part IV
    • Cullinane, N. M.; Davey, H. G.; Padfield, H. J. H. Investigations in the Diphenylene Oxide Series. Part IV. J. Chem. Soc. 1934, 716-719.
    • (1934) J. Chem. Soc. , pp. 716-719
    • Cullinane, N.M.1    Davey, H.G.2    Padfield, H.J.H.3
  • 43
    • 0008508704 scopus 로고
    • Analogues of Phenothiazines. II. Phenoxazine and Phenoselenazine Analogues of Phenothiazine Drugs
    • Olmsted, M. P.; Craig, P, N.; Lafferty, J. J.; Pavloff, A. M.; Zirkle, C. L. Analogues of Phenothiazines. II. Phenoxazine and Phenoselenazine Analogues of Phenothiazine Drugs. J. Org. Chem. 1961, 26, 1901-1907.
    • (1961) J. Org. Chem. , vol.26 , pp. 1901-1907
    • Olmsted, M.P.1    Craig, P.N.2    Lafferty, J.J.3    Pavloff, A.M.4    Zirkle, C.L.5
  • 44
    • 84985274643 scopus 로고
    • Antibiotics from Algae. 38. Base-catalyzed Reactions of Multiple Hydroxylated Diphenyl Ethers
    • Glombitza, K. W.; Woelwer-Rieck, U. Antibiotics from Algae. 38. Base-catalyzed Reactions of Multiple Hydroxylated Diphenyl Ethers. Liebigs Annalen der Chemie 1988, 3, 261-265.
    • (1988) Liebigs Annalen der Chemie , vol.3 , pp. 261-265
    • Glombitza, K.W.1    Woelwer-Rieck, U.2
  • 45
    • 0025829982 scopus 로고
    • Purification and Characterization of the Recombinant Human Aldose Reductase Expressed in Baculovirus System
    • Nishimura, C.; Yamaoka, T.; Mizutani, M.; Yamashita, K.; Akera, T.; Tanimoto, T. Purification and Characterization of the Recombinant Human Aldose Reductase Expressed in Baculovirus System. Biochim. Biophys. Acta. 1991, 1078, 171-178.
    • (1991) Biochim. Biophys. Acta , vol.1078 , pp. 171-178
    • Nishimura, C.1    Yamaoka, T.2    Mizutani, M.3    Yamashita, K.4    Akera, T.5    Tanimoto, T.6
  • 47
    • 0242466496 scopus 로고
    • Cell Culture Methods
    • Hockwin, O., Green, K., Rubin, L. F., Eds.; Gustav Fischer Verlag: Stuttgart, Germany
    • Rink, H.; Baumstark-Khan, C. Cell Culture Methods. In Manual of Oculotoxicity; Hockwin, O., Green, K., Rubin, L. F., Eds.; Gustav Fischer Verlag: Stuttgart, Germany, 1992; pp 389-401.
    • (1992) Manual of Oculotoxicity , pp. 389-401
    • Rink, H.1    Baumstark-Khan, C.2
  • 48
    • 0242549981 scopus 로고
    • Aldostatin, a New Aldose Reductase Inhibitor
    • Demain, A. L., Somkuti, G. A., Hunter-Cevera, J. C., Rossmore, H. W., Eds.; Society for Industrial Microbiology; Elsevier Science Ltd: New York
    • Yaginuma, S.; Asahi, A.; Takada, M.; Hayashi, M.; Tsujino, M.; Mizuno, K. Aldostatin, a New Aldose Reductase Inhibitor. In Novel Microbial Products for Medicine and Agriculture; Demain, A. L., Somkuti, G. A., Hunter-Cevera, J. C., Rossmore, H. W., Eds.; Society for Industrial Microbiology; Elsevier Science Ltd: New York, 1989; pp 127-133.
    • (1989) Novel Microbial Products for Medicine and Agriculture , pp. 127-133
    • Yaginuma, S.1    Asahi, A.2    Takada, M.3    Hayashi, M.4    Tsujino, M.5    Mizuno, K.6
  • 50
    • 3042524904 scopus 로고
    • A Well-Behaved Electrostatic Potential Based Method Using Charge Restraints for Deriving Atomic Charges the RESP Model
    • Bayly, C. I.; Cieplak, P.; Cornell, W. D.; Kollman, P. A. A Well-Behaved Electrostatic Potential Based Method Using Charge Restraints for Deriving Atomic Charges: the RESP Model. J. Phys. Chem. 1993, 97, 10269-10280.
    • (1993) J. Phys. Chem. , vol.97 , pp. 10269-10280
    • Bayly, C.I.1    Cieplak, P.2    Cornell, W.D.3    Kollman, P.A.4
  • 53
    • 0000730887 scopus 로고    scopus 로고
    • A Application of the RESP Methodology in the Parametrization of Organic Solvents
    • Fox, T.; Kollman, P. A, Application of the RESP Methodology in the Parametrization of Organic Solvents. J. Phys. Chem. B. 1998, 102, 8070-8079.
    • (1998) J. Phys. Chem. B , vol.102 , pp. 8070-8079
    • Fox, T.1    Kollman, P.2
  • 54
    • 0003834096 scopus 로고    scopus 로고
    • Molecular Simulations Inc. 9685 Scranton Road, San Diego, CA 92121-2777
    • Insight II, version 98.0, 1998. Molecular Simulations Inc. 9685 Scranton Road, San Diego, CA 92121-2777.
    • (1998) Insight II, Version 98.0
  • 55
    • 11644261806 scopus 로고    scopus 로고
    • Automated Docking Using a Lamarekian Genetic Algorithm and an Empirical Binding Free Energy Function
    • Morris, G. M.; Goodsell, D. S.; Halliday, R. S.; Huey, R.; Hart, W. E.; Belew, R. K.; Olson, A. J. Automated Docking Using a Lamarekian Genetic Algorithm and an Empirical Binding Free Energy Function. J. Comput. Chem. 1998, 19, 1639-1662.
    • (1998) J. Comput. Chem. , vol.19 , pp. 1639-1662
    • Morris, G.M.1    Goodsell, D.S.2    Halliday, R.S.3    Huey, R.4    Hart, W.E.5    Belew, R.K.6    Olson, A.J.7
  • 58
    • 84988087911 scopus 로고
    • Calculating the Electrostatic Potential of Molecules in Solution: Method and Error Assessment
    • Gilson, M. K.; Sharp, K. A.; Honig, B. H. Calculating the Electrostatic Potential of Molecules in Solution: Method and Error Assessment. J. Comput. Chem. 1987, 9, 327-335.
    • (1987) J. Comput. Chem. , vol.9 , pp. 327-335
    • Gilson, M.K.1    Sharp, K.A.2    Honig, B.H.3
  • 59
    • 0032510317 scopus 로고    scopus 로고
    • Comparative Binding Energy Analysis of HIV-1 Protease Inhibitors: Incorporation of Solvent Effects and Validation as a Powerful Tool in Receptor-Based Drug Design
    • Pérez, C.; Ortiz, A. R.; Pastor, M.; Gago, F. Comparative Binding Energy Analysis of HIV-1 Protease Inhibitors: Incorporation of Solvent Effects and Validation as a Powerful Tool in Receptor-Based Drug Design. J. Med. Chem. 1998, 41, 836-852.
    • (1998) J. Med. Chem. , vol.41 , pp. 836-852
    • Pérez, C.1    Ortiz, A.R.2    Pastor, M.3    Gago, F.4
  • 60
    • 0035658221 scopus 로고    scopus 로고
    • Comparative Binding Energy (COMBINE) Analysis of Human Neutrophil Elastase Inhibition by Pyridone-containing Trifluoromethylketones
    • Cuevas, C.; Pastor, M.; Pérez, C.; Gago, F. Comparative Binding Energy (COMBINE) Analysis of Human Neutrophil Elastase Inhibition by Pyridone-containing Trifluoromethylketones. Comb. Chem. High Throughput Screen, 2001, 4, 627-642.
    • (2001) Comb. Chem. High Throughput Screen , vol.4 , pp. 627-642
    • Cuevas, C.1    Pastor, M.2    Pérez, C.3    Gago, F.4
  • 61
    • 36449004340 scopus 로고
    • Determining the Contributions of Constraints in Free Energy Calculations: Development, Characterization, and Recommendations
    • Pearlmann, D. A. Determining the Contributions of Constraints in Free Energy Calculations: Development, Characterization, and Recommendations. J. Chem. Phys. 1993, 98, 8946-8957.
    • (1993) J. Chem. Phys. , vol.98 , pp. 8946-8957
    • Pearlmann, D.A.1


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.