메뉴 건너뛰기




Volumn 9, Issue , 1996, Pages 1-79

Peptide mimetic design with the aid of computational chemistry

Author keywords

[No Author keywords available]

Indexed keywords

PEPTIDES;

EID: 0345664910     PISSN: 10693599     EISSN: None     Source Type: Book Series    
DOI: None     Document Type: Article
Times cited : (22)

References (219)
  • 1
    • 19944367529 scopus 로고
    • Introduction to Peptide Pharmaceuticals
    • D. J. Ward, Ed., Elsevier, New York
    • D. J. Ward, in Peptide Pharmaceuticals, D. J. Ward, Ed., Elsevier, New York, 1991, pp. 1-17. Introduction to Peptide Pharmaceuticals.
    • (1991) Peptide Pharmaceuticals , pp. 1-17
    • Ward, D.J.1
  • 2
    • 0001918583 scopus 로고
    • Synthetic Chemistry and the Design of Peptide-Based Drugs
    • D. J. Ward, Ed., Elsevier, New York
    • V. J. Hruby, W. Kazmierski, A. M. Kawasaki, and T. O. Matsunaga, in Peptide Pharmaceuticals, D. J. Ward, Ed., Elsevier, New York, 1991, pp. 135-184. Synthetic Chemistry and the Design of Peptide-Based Drugs.
    • (1991) Peptide Pharmaceuticals , pp. 135-184
    • Hruby, V.J.1    Kazmierski, W.2    Kawasaki, A.M.3    Matsunaga, T.O.4
  • 4
    • 33745502124 scopus 로고
    • Peptidomimetics for Receptor Ligands - Discovery, Development and Medicinal Perspectives
    • A. Giannis and T. Kolter, Angew. Chem. Int. Ed. Engl., 32, 1244 (1993). Peptidomimetics for Receptor Ligands - Discovery, Development and Medicinal Perspectives.
    • (1993) Angew. Chem. Int. Ed. Engl. , vol.32 , pp. 1244
    • Giannis, A.1    Kolter, T.2
  • 5
    • 0027478912 scopus 로고
    • Peptidomimetics Derived from Natural Products
    • R. A. Wiley and D. H. Rich, Med. Res. Rev. 13, 327 (1993). Peptidomimetics Derived from Natural Products.
    • (1993) Med. Res. Rev. , vol.13 , pp. 327
    • Wiley, R.A.1    Rich, D.H.2
  • 6
    • 77957079236 scopus 로고
    • Peptide Secondary Structure Mimetics: Recent Advances and Future Challenges
    • M. Kahn, Synlett, 11, 821 (1993). Peptide Secondary Structure Mimetics: Recent Advances and Future Challenges.
    • (1993) Synlett , vol.11 , pp. 821
    • Kahn, M.1
  • 8
    • 0013534646 scopus 로고
    • Conformationally Restricted Amino Acids and Dipeptides (Non)Peptidomimetics and Secondary Structure Mimetics
    • R. M. J. Liskamp, Recl. Trav. Chim. Pays-Bas, 113, 1 (1994). Conformationally Restricted Amino Acids and Dipeptides (Non)Peptidomimetics and Secondary Structure Mimetics.
    • (1994) Recl. Trav. Chim. Pays-Bas , vol.113 , pp. 1
    • Liskamp, R.M.J.1
  • 10
    • 0028038601 scopus 로고
    • Peptidomimetics - Tailored Enzyme Inhibitors
    • J. Gante, Angew. Chem. Int. Ed. Engl., 33, 1699 (1994). Peptidomimetics - Tailored Enzyme Inhibitors.
    • (1994) Angew. Chem. Int. Ed. Engl. , vol.33 , pp. 1699
    • Gante, J.1
  • 13
    • 0000219483 scopus 로고
    • Peptide Secondary Structure Mimetics
    • M. Kahn, Ed., Tetrahedron Symposiwn-in-Print 50, 49, pp. 3433 ff. (1993). Peptide Secondary Structure Mimetics.
    • (1993) Tetrahedron Symposiwn-in-Print 50 , vol.49
    • Kahn, M.1
  • 14
    • 85068946418 scopus 로고    scopus 로고
    • U.S. Patent 5,331,573 (1994). Method of Design of Compounds That Mimic Conformational Features of Selected Peptides
    • V. N. Balaji and U. C. Singh, U.S. Patent 5,331,573 (1994). Method of Design of Compounds That Mimic Conformational Features of Selected Peptides.
    • Balaji, V.N.1    Singh, U.C.2
  • 16
    • 0027193713 scopus 로고
    • GroupBuild: A Fragment-Based Method for de Novo Drug Design
    • S. H. Rotstein and M. A. Murcko, J. Med. Chem., 36, 1700 (1993). GroupBuild: A Fragment-Based Method for De Novo Drug Design.
    • (1993) J. Med. Chem. , vol.36 , pp. 1700
    • Rotstein, S.H.1    Murcko, M.A.2
  • 17
    • 0024380931 scopus 로고
    • Cholecystokinin Antagonists. Synthesis and Biological Evaluation of 3-Substituted Benzolactams
    • See, for example, W. H. Parsons, A. A. Patchett, M. K. Holloway, G. M. Smith, J. L. Davison, V. J. Lotti, and R. S. L. Chang, J. Med. Chem., 32, 1681 (1989). Cholecystokinin Antagonists. Synthesis and Biological Evaluation of 3-Substituted Benzolactams. See also references therein.
    • (1989) J. Med. Chem. , vol.32 , pp. 1681
    • Parsons, W.H.1    Patchett, A.A.2    Holloway, M.K.3    Smith, G.M.4    Davison, J.L.5    Lotti, V.J.6    Chang, R.S.L.7
  • 19
    • 0002649780 scopus 로고
    • Design and Discovery in the Development of Peptide Analogs
    • J. A. Smith and J. E. Rivier, Eds., ESCOM, Leiden
    • D. F. Veber, in Peptides: Proceedings of the Twelfth American Peptide Symposium, J. A. Smith and J. E. Rivier, Eds., ESCOM, Leiden, 1992, pp. 3-14. Design and Discovery in the Development of Peptide Analogs.
    • (1992) Peptides: Proceedings of the Twelfth American Peptide Symposium , pp. 3-14
    • Veber, D.F.1
  • 22
  • 23
  • 25
    • 0027996496 scopus 로고
    • Non-Peptidic Inhibitors of Human Leukocyte Elastase. 1. The Design and Synthesis of Pyridone-Containing Inhibitors
    • P. Warner, R. C. Green, B. Gomes, and A. M. Strimpler, J. Med. Chem., 37, 3090 (1994). Non-Peptidic Inhibitors of Human Leukocyte Elastase. 1. The Design and Synthesis of Pyridone-Containing Inhibitors.
    • (1994) J. Med. Chem. , vol.37 , pp. 3090
    • Warner, P.1    Green, R.C.2    Gomes, B.3    Strimpler, A.M.4
  • 29
    • 0022801412 scopus 로고
    • Crystal Structure of the Complex of Human Leukocyte Elastase (PMN Elastase) and the Third Domain of the Turkey Ovomucoid Inhibitor
    • W. Bode, A.-Z. Wie, R. Huber, E. Meyer, J. Travis, and S. Neumann, EMBO J., 5, 2453 (1986). Crystal Structure of the Complex of Human Leukocyte Elastase (PMN Elastase) and the Third Domain of the Turkey Ovomucoid Inhibitor.
    • (1986) EMBO J. , vol.5 , pp. 2453
    • Bode, W.1    Wie, A.-Z.2    Huber, R.3    Meyer, E.4    Travis, J.5    Neumann, S.6
  • 31
    • 0014211618 scopus 로고
    • On the Size of the Active Site in Proteases. I. Papain
    • The nomenclature system of Schechter and Berger for residues on either side of the scissile bond is used throughout this chapter. I. Schechter and A. Berger, Biochem. Biophys. Res. Commun., 27, 157 (1967). On the Size of the Active Site in Proteases. I. Papain.
    • (1967) Biochem. Biophys. Res. Commun. , vol.27 , pp. 157
    • Schechter, I.1    Berger, A.2
  • 32
    • 0343405849 scopus 로고
    • AESOP is an in-house molecular mechanics program at Zeneca, Inc., Wilmington, DE 19897, derived in part from BIGSTRN-3 (QCPE 514): R. B. Nachbar, Jr., and K. Mislow, QCPE Bull., 6, 96 (1986).
    • (1986) QCPE Bull. , vol.6 , pp. 96
    • Nachbar Jr., R.B.1    Mislow, K.2
  • 36
    • 84862582328 scopus 로고
    • Computer Simulation of Biomolecular Systems using Molecular Dynamics and Free Energy Perturbation Methods
    • K. B. Lipkowitz and D. B. Boyd, Eds., VCH Publishers, New York
    • T. P. Lybrand, in Reviews in Computational Chemistry, K. B. Lipkowitz and D. B. Boyd, Eds., VCH Publishers, New York, 1990, Vol. 1, pp. 295-320. Computer Simulation of Biomolecular Systems using Molecular Dynamics and Free Energy Perturbation Methods.
    • (1990) Reviews in Computational Chemistry , vol.1 , pp. 295-320
    • Lybrand, T.P.1
  • 37
    • 85068951603 scopus 로고    scopus 로고
    • U. C. Singh, P. Weiner, J. C. Caldwell, and P. A. Kollman, AMBER, University of California, San Francisco, 1989
    • U. C. Singh, P. Weiner, J. C. Caldwell, and P. A. Kollman, AMBER, University of California, San Francisco, 1989.
  • 38
    • 0029040711 scopus 로고
    • Non-Peptidic Inhibitors of Human Leukocyte Elastase. 4. Design, Synthesis, and in Vitro and in Vivo Activity of a Series of β-Carbolinone-Containing Trifluoromethyl Ketones
    • C. A. Veale, J. R. Damewood, Jr., G. B. Steelman, C. Bryant, B. Gomes, and J. Williams, J. Med. Chem., 38, 86 (1995). Non-Peptidic Inhibitors of Human Leukocyte Elastase. 4. Design, Synthesis, and In Vitro and In Vivo Activity of a Series of β-Carbolinone-Containing Trifluoromethyl Ketones.
    • (1995) J. Med. Chem. , vol.38 , pp. 86
    • Veale, C.A.1    Damewood Jr., J.R.2    Steelman, G.B.3    Bryant, C.4    Gomes, B.5    Williams, J.6
  • 39
    • 0030009748 scopus 로고    scopus 로고
    • Nonpeptidic Inhibitors of Human Neutrophil Elastase. 7. Design, Synthesis, and in Vitro Activity of a Series of Pyridopyrimidine-Containing Trifluoromethyl Ketones
    • P. D. Edwards, D. W. Andisik, A. M. Strimpler, B. Gomes, and P. A. Tuthill, J. Med. Chem., 39, 1112 (1996). Nonpeptidic Inhibitors of Human Neutrophil Elastase. 7. Design, Synthesis, and in Vitro Activity of a Series of Pyridopyrimidine-Containing Trifluoromethyl Ketones.
    • (1996) J. Med. Chem. , vol.39 , pp. 1112
    • Edwards, P.D.1    Andisik, D.W.2    Strimpler, A.M.3    Gomes, B.4    Tuthill, P.A.5
  • 40
    • 7044239742 scopus 로고
    • Free Energy Calculations: Applications to Chemical and Biochemical Phenomena
    • P. Kollman, Cheat. Rev., 93, 2395 (1993). Free Energy Calculations: Applications to Chemical and Biochemical Phenomena.
    • (1993) Cheat. Rev. , vol.93 , pp. 2395
    • Kollman, P.1
  • 44
    • 0026354245 scopus 로고
    • Comparative Modeling of Proteins in the Design of Novel Renin Inhibitors
    • C. Hutchins and J. Greer, Crit. Rev. Biochem. Mol. Biol., 26, 77 (1991). Comparative Modeling of Proteins in the Design of Novel Renin Inhibitors.
    • (1991) Crit. Rev. Biochem. Mol. Biol. , vol.26 , pp. 77
    • Hutchins, C.1    Greer, J.2
  • 45
    • 0343140960 scopus 로고
    • Renin-Inhibitoren-von 'Transition-State' Analogen und Peptidmimetika zu blutdrucksenkenden Wirkstoffen
    • B. Weidmann, Chimia, 45, 367 (1991). Renin-Inhibitoren-von 'Transition-State' Analogen und Peptidmimetika zu blutdrucksenkenden Wirkstoffen.
    • (1991) Chimia , vol.45 , pp. 367
    • Weidmann, B.1
  • 47
    • 19944405022 scopus 로고
    • Renin Inhibitor Design Through Molecular Modeling
    • Pharmaco Chemistry Library, P. B. M. W. M. Timmermans and R. R. Wexler, Eds., Elsevier, New York
    • E. A. Lunney and C. Humblet, in Medicinal Chemistry of the Renin-Angiotensin System, Pharmaco Chemistry Library, 21, P. B. M. W. M. Timmermans and R. R. Wexler, Eds., Elsevier, New York, 1994, pp. 73-101. Renin Inhibitor Design Through Molecular Modeling.
    • (1994) Medicinal Chemistry of the Renin-Angiotensin System , vol.21 , pp. 73-101
    • Lunney, E.A.1    Humblet, C.2
  • 48
    • 0027081659 scopus 로고
    • Design, Synthesis, and Crystal Structure of a Pyrrolinone-Based Peptidomimetic Possessing the Conformation of a β-Strand: Potential Application to the Design of Novel Inhibitors of Proteolytic Enzymes
    • A. B. Smith III, T. P. Keenan, R. C. Holcomb, P. A. Sprengeler, M. C. Guzman, J. L. Wood, P. J. Carroll, and R. Hirschmann, J. Am. Chem. Soc., 114, 10672 (1992). Design, Synthesis, and Crystal Structure of a Pyrrolinone-Based Peptidomimetic Possessing the Conformation of a β-Strand: Potential Application to the Design of Novel Inhibitors of Proteolytic Enzymes.
    • (1992) J. Am. Chem. Soc. , vol.114 , pp. 10672
    • Smith III, A.B.1    Keenan, T.P.2    Holcomb, R.C.3    Sprengeler, P.A.4    Guzman, M.C.5    Wood, J.L.6    Carroll, P.J.7    Hirschmann, R.8
  • 53
    • 0023910548 scopus 로고
    • New Human Renin Inhibitors Containing an Unnatural Amino Acid, Norstatine
    • K. Izuka, T. Kamijo, T. Kubota, K. Akahane, H. Umeyama, and Y. Kiso. J. Med. Chem., 31, 701 (1988). New Human Renin Inhibitors Containing an Unnatural Amino Acid, Norstatine.
    • (1988) J. Med. Chem. , vol.31 , pp. 701
    • Izuka, K.1    Kamijo, T.2    Kubota, T.3    Akahane, K.4    Umeyama, H.5    Kiso, Y.6
  • 57
    • 33845283120 scopus 로고
    • An Acyl-Iminium Ion Cyclization Route to a Novel Conformationally Restricted Dipeptide Mimic: Applications to Angiotensin-Converting Enzyme Inhibition
    • G. A. Flynn, E. L. Giroux, and R. C. Dage, J. Am. Chem. Soc., 109, 7914 (1987). An Acyl-Iminium Ion Cyclization Route to a Novel Conformationally Restricted Dipeptide Mimic: Applications to Angiotensin-Converting Enzyme Inhibition.
    • (1987) J. Am. Chem. Soc. , vol.109 , pp. 7914
    • Flynn, G.A.1    Giroux, E.L.2    Dage, R.C.3
  • 60
    • 19944421330 scopus 로고
    • Angiotensin II Receptor Antagonists: Molecular Modeling
    • Pharmaco Chemistry Library, P. B. M. W. M. Timmermans and R. R. Wexler, Eds., Elsevier, New York
    • R. H. Bradbury, B. B. Masek, and D. A. Roberts, in Medicinal Chemistry of the Renin-Angiotensin System, Pharmaco Chemistry Library, 21, P. B. M. W. M. Timmermans and R. R. Wexler, Eds., Elsevier, New York, 1994, pp. 157-174. Angiotensin II Receptor Antagonists: Molecular Modeling.
    • (1994) Medicinal Chemistry of the Renin-Angiotensin System , vol.21 , pp. 157-174
    • Bradbury, R.H.1    Masek, B.B.2    Roberts, D.A.3
  • 69
    • 0027241303 scopus 로고
    • Refinement of a Molecular Model of Angiotensin II (AII) Employed in the Discovery of Potent Nonpeptide Antagonists
    • J. M. Samanen, C. E. Peishoff, R. M. Keenan, and J. Weinstock, Bioorg. Med. Chem. Lett., 3, 909 (1993). Refinement of a Molecular Model of Angiotensin II (AII) Employed in the Discovery of Potent Nonpeptide Antagonists.
    • (1993) Bioorg. Med. Chem. Lett. , vol.3 , pp. 909
    • Samanen, J.M.1    Peishoff, C.E.2    Keenan, R.M.3    Weinstock, J.4
  • 71
    • 85068946630 scopus 로고    scopus 로고
    • Tripos, Inc., St. Louis, MO 63144
    • Tripos, Inc., St. Louis, MO 63144.
  • 72
    • 0028293066 scopus 로고
    • Designing Peptide Mimetics
    • G. J. Moore, Trends Pharmacol. Sci., 15, 124 (1994). Designing Peptide Mimetics.
    • (1994) Trends Pharmacol. Sci. , vol.15 , pp. 124
    • Moore, G.J.1
  • 76
    • 85068948085 scopus 로고
    • (IUPUI), personal communication
    • D. B. Boyd (IUPUI), personal communication, 1995.
    • (1995)
    • Boyd, D.B.1
  • 78
    • 0024538318 scopus 로고
    • Neutral Endopeptidase 24.11 (Enkephalinase) and Related Regulators of Peptide Hormones
    • E. G. Erdös and R. A. Skidgel, FASEB J., 3, 145 (1989). Neutral Endopeptidase 24.11 (Enkephalinase) and Related Regulators of Peptide Hormones.
    • (1989) FASEB J. , vol.3 , pp. 145
    • Erdös, E.G.1    Skidgel, R.A.2
  • 79
    • 0027180453 scopus 로고
    • Application of a Conformationally Restricted Phe-Leu Dipeptide Mimetic to the Design of a Combined Inhibitor of Angiotensin-I Converting Enzyme and Neutral Endopeptidase 24.11
    • G. A. Flynn, D. W. Beight, S. Mehdi, J. R. Koehl, E. L. Giroux, J. F. French, P. W. Hake, and R. C. Dage,J. Med. Chem., 36, 2420 (1993). Application of a Conformationally Restricted Phe-Leu Dipeptide Mimetic to the Design of a Combined Inhibitor of Angiotensin-I Converting Enzyme and Neutral Endopeptidase 24.11.
    • (1993) J. Med. Chem. , vol.36 , pp. 2420
    • Flynn, G.A.1    Beight, D.W.2    Mehdi, S.3    Koehl, J.R.4    Giroux, E.L.5    French, J.F.6    Hake, P.W.7    Dage, R.C.8
  • 80
    • 85068954755 scopus 로고    scopus 로고
    • BIOSYM Technologies, San Diego, CA 92121
    • BIOSYM Technologies, San Diego, CA 92121.
  • 81
    • 0028299371 scopus 로고
    • New Dual Inhibitors of Neutral Endopeptidase and Angiotensin-Converting Enzyme: Rational Design, Bioavailability, and Pharmacological Responses in Experimental Hypertension
    • M.-C. Fournié-Zaluski, P. Coric, S. Turcaud, N. Rousselet, W. Gonzalez, B. Barbe, I. Pham, N. Jullian, J.-B. Michel, and B. P. Roques, J. Med. Chem., 37, 1070 (1994). New Dual Inhibitors of Neutral Endopeptidase and Angiotensin-Converting Enzyme: Rational Design, Bioavailability, and Pharmacological Responses in Experimental Hypertension. See also references therein.
    • (1994) J. Med. Chem. , vol.37 , pp. 1070
    • Fournié-Zaluski, M.-C.1    Coric, P.2    Turcaud, S.3    Rousselet, N.4    Gonzalez, W.5    Barbe, B.6    Pham, I.7    Jullian, N.8    Michel, J.-B.9    Roques, B.P.10
  • 82
    • 0024334170 scopus 로고
    • Role of Human Immunodeficiency Virus Type 1-Specific Protease in Core Protein Maturation and Viral Infectivity
    • See, for example, C. Peng, B. K. Ho, T. W. Chang, and N. T. Chang, J. Virol., 63, 2550 (1989). Role of Human Immunodeficiency Virus Type 1-Specific Protease in Core Protein Maturation and Viral Infectivity.
    • (1989) J. Virol. , vol.63 , pp. 2550
    • Peng, C.1    Ho, B.K.2    Chang, T.W.3    Chang, N.T.4
  • 84
    • 0025225682 scopus 로고
    • X-Ray Cristallographic Structure of a Complex between a Synthetic Protease of Human Immunodeficiency Virus 1 and a Substrate-Based Hydroxyethylamine Inhibitor
    • A. L. Swain, M. M. Miller, J. Green, D. H. Rich, J. Schneider, S. B. H. Kent, and A. Wlodawer, Proc. Natl. Acad. Sci., U.S.A., 87, 8805 (1990). X-Ray Cristallographic Structure of a Complex Between a Synthetic Protease of Human Immunodeficiency Virus 1 and a Substrate-Based Hydroxyethylamine Inhibitor.
    • (1990) Proc. Natl. Acad. Sci., U.S.A. , vol.87 , pp. 8805
    • Swain, A.L.1    Miller, M.M.2    Green, J.3    Rich, D.H.4    Schneider, J.5    Kent, S.B.H.6    Wlodawer, A.7
  • 85
    • 0002039443 scopus 로고
    • HIV Protease: Structure-Based Design
    • M. Clare, Perspect. Drug Discovery Design, 1, 49 (1993). HIV Protease: Structure-Based Design.
    • (1993) Perspect. Drug Discovery Design , vol.1 , pp. 49
    • Clare, M.1
  • 86
    • 0028452628 scopus 로고
    • A Shape- and Chemistry-Based Docking Method and its Use in the Design of HIV-1 Protease Inhibitors
    • See, for example, R. L. Desjarlais, and J. S. Dixon, J. Comput.-Aided Mol. Design, 8, 231 (1994). A Shape- and Chemistry-Based Docking Method and its Use in the Design of HIV-1 Protease Inhibitors.
    • (1994) J. Comput.-Aided Mol. Design , vol.8 , pp. 231
    • Desjarlais, R.L.1    Dixon, J.S.2
  • 87
    • 0029028338 scopus 로고
    • Use of Molecular Dynamics and Free Energy Perturbation Calculations in Anti-Human Immunodeficiency Virus Drug Design
    • M. A. McCarrick and P. Kollman, Methods Enzymol, 241, 370 (1994). Use of Molecular Dynamics and Free Energy Perturbation Calculations in Anti-Human Immunodeficiency Virus Drug Design.
    • (1994) Methods Enzymol , vol.241 , pp. 370
    • McCarrick, M.A.1    Kollman, P.2
  • 89
    • 0028349919 scopus 로고
    • Calculation of Relative Differences in the Binding Free Energies of HIV-1 Protease Inhibitors: A Thermodynamic Cycle Perturbation Approach
    • M. R. Reddy, M. D. Varney, V. Kalish, V. N. Viswanadhan, and K. Appelt, J. Med. Chem., 37, 1145 (1994). Calculation of Relative Differences in the Binding Free Energies of HIV-1 Protease Inhibitors: A Thermodynamic Cycle Perturbation Approach.
    • (1994) J. Med. Chem. , vol.37 , pp. 1145
    • Reddy, M.R.1    Varney, M.D.2    Kalish, V.3    Viswanadhan, V.N.4    Appelt, K.5
  • 93
    • 45149145779 scopus 로고
    • The Dielectric Constant of SPCJE Water
    • See, for example, M. R. Reddy and M. Berkowitz, Chem. Phys. Lett., 155, 173 (1989). The Dielectric Constant of SPCJE Water. See also references therein.
    • (1989) Chem. Phys. Lett. , vol.155 , pp. 173
    • Reddy, M.R.1    Berkowitz, M.2
  • 95
    • 0001835759 scopus 로고
    • 3D Search and Research Using the Cambridge Structural Database
    • F. H. Allen and O. Kennard, Chem. Design Autant. News, 8, 31 (1993). 3D Search and Research Using the Cambridge Structural Database.
    • (1993) Chem. Design Autant. News , vol.8 , pp. 31
    • Allen, F.H.1    Kennard, O.2
  • 96
    • 85068946505 scopus 로고    scopus 로고
    • MDL Information Systems, Inc., San Leandro, CA 94577
    • MDL Information Systems, Inc., San Leandro, CA 94577.
  • 98
    • 0028287967 scopus 로고
    • De Novo Design of Nonpeptidic HIV-1 Protease Inhibitors: Incorporation of Structural Water
    • R. S. Randad, W. Pan, S. V. Gulnik, S. Burt, and J. W. Erickson, Bioorg. Med. Chem. Lett., 4, 1247 (1994). De Novo Design of Nonpeptidic HIV-1 Protease Inhibitors: Incorporation of Structural Water.
    • (1994) Bioorg. Med. Chem. Lett. , vol.4 , pp. 1247
    • Randad, R.S.1    Pan, W.2    Gulnik, S.V.3    Burt, S.4    Erickson, J.W.5
  • 106
    • 0039837427 scopus 로고
    • Structure-Based Design of Human Immunodeficiency Virus-1 Protease Inhibitors: Correlating Calculated Energy with Activity
    • Computer-Aided Molecular Design: Applications in Agrochemicals, Materials, and Pharmaceutical. March 13-17, 1994, San Diego, CA, C. H. Reynolds, M. K. Holloway, and H. K. Cox, Eds., American Chemical Society, Washington, DC
    • See also, M. K. Holloway and J. M. Wai, in Computer-Aided Molecular Design: Applications in Agrochemicals, Materials, and Pharmaceutical. (A symposium at the 207th American Chemical Society National Meeting, March 13-17, 1994, San Diego, CA), C. H. Reynolds, M. K. Holloway, and H. K. Cox, Eds., American Chemical Society, Washington, DC, 1995, pp. 36-50. Structure-Based Design of Human Immunodeficiency Virus-1 Protease Inhibitors: Correlating Calculated Energy with Activity.
    • (1995) A Symposium at the 207th American Chemical Society National Meeting , pp. 36-50
    • Holloway, M.K.1    Wai, J.M.2
  • 107
    • 85068946951 scopus 로고    scopus 로고
    • Merck Research Laboratories, unpublished results
    • P. M. D. Fitzgerald, Merck Research Laboratories, unpublished results.
    • Fitzgerald, P.M.D.1
  • 111
    • 0027742264 scopus 로고
    • Peptidomimetics of the Immunoglobulin Supergene Family - A Review
    • H. Nakanishi, S. Ramurthy, A. Raktabutr, R. Shen, and M. Kahn, Gene, 137, 51 (1993). Peptidomimetics of the Immunoglobulin Supergene Family - A Review.
    • (1993) Gene , vol.137 , pp. 51
    • Nakanishi, H.1    Ramurthy, S.2    Raktabutr, A.3    Shen, R.4    Kahn, M.5
  • 112
    • 0023840802 scopus 로고
    • The CD4 Antigen: Physiological Ligand and HIV Receptor
    • Q. J. Sattentau and R. A. Weiss, Cell, 52, 631 (1988). The CD4 Antigen: Physiological Ligand and HIV Receptor.
    • (1988) Cell , vol.52 , pp. 631
    • Sattentau, Q.J.1    Weiss, R.A.2
  • 116
    • 0344778061 scopus 로고
    • Semianalytical Treatment of Solvation for Molecular Mechanics and Dynamics
    • W. C. Still, A. Tempczyk, R. C. Hawley, and T. Hendrickson, J. Am. Chem. Soc., 112, 6127 (1990). Semianalytical Treatment of Solvation for Molecular Mechanics and Dynamics.
    • (1990) J. Am. Chem. Soc. , vol.112 , pp. 6127
    • Still, W.C.1    Tempczyk, A.2    Hawley, R.C.3    Hendrickson, T.4
  • 117
    • 0028340743 scopus 로고
    • Structure-Based Design of an Inhibitor of the Zinc Peptidase Thermolysin
    • B. P. Morgan, D. R. Holland, B. W. Matthews, and P. A. Bartlett, J. Am. Chem. Soc., 116, 3251 (1994). Structure-Based Design of an Inhibitor of the Zinc Peptidase Thermolysin.
    • (1994) J. Am. Chem. Soc. , vol.116 , pp. 3251
    • Morgan, B.P.1    Holland, D.R.2    Matthews, B.W.3    Bartlett, P.A.4
  • 118
    • 9144240095 scopus 로고
    • A Generic Force Field for Molecular Simulations
    • S. L. Mayo, B. D. Olafson, and W. A. Goddard III, J. Phys. Chem., 94, 8897 (1990). A Generic Force Field for Molecular Simulations.
    • (1990) J. Phys. Chem. , vol.94 , pp. 8897
    • Mayo, S.L.1    Olafson, B.D.2    Goddard III, W.A.3
  • 119
    • 0027207873 scopus 로고
    • Cyclopropanes as Conformationally Restricted Peptide Isosteres. Design and Synthesis of Novel Collagenase Inhibitors
    • S. F. Martin, C. J. Oalmann, and S. Liras, Tetrahedron, 49, 3521 (1993). Cyclopropanes as Conformationally Restricted Peptide Isosteres. Design and Synthesis of Novel Collagenase Inhibitors.
    • (1993) Tetrahedron , vol.49 , pp. 3521
    • Martin, S.F.1    Oalmann, C.J.2    Liras, S.3
  • 120
    • 0022486526 scopus 로고
    • Crystal Structure Determination, Refinement, and the Molecular Model of the α-Amylase Inhibitor HOE-467A
    • J. W. Pflugrath, G. Wiegand, R. Huber, and L. Vértesy, J. Mol. Biol. 189, 383 (1986). Crystal Structure Determination, Refinement, and the Molecular Model of the α-Amylase Inhibitor HOE-467A.
    • (1986) J. Mol. Biol. , vol.189 , pp. 383
    • Pflugrath, J.W.1    Wiegand, G.2    Huber, R.3    Vértesy, L.4
  • 121
    • 0024239356 scopus 로고
    • Determination of the Complete Three-Dimensional Structure of the á-Amylase Inhibitor Tendamistat in Aqueous Solution by Nuclear Magnetic Resonance and Distance Geometry
    • A. D. Kline, W. Braun, and K. Wüthrich, J. Mol. Biol., 204, 675 (1988). Determination of the Complete Three-Dimensional Structure of the á-Amylase Inhibitor Tendamistat in Aqueous Solution by Nuclear Magnetic Resonance and Distance Geometry.
    • (1988) J. Mol. Biol. , vol.204 , pp. 675
    • Kline, A.D.1    Braun, W.2    Wüthrich, K.3
  • 123
    • 0003495713 scopus 로고
    • CAVEAT: A Program to Facilitate the Structure-Derived Design of Biologically Active Molecules
    • S. M. Roberts, Ed., Royal Society of Chemistry, London
    • P. A. Bartlett, G. T. Shea, S. J. Telfer, and S. Waterman, in Molecular Recognition: Chemical and Biological Problems, S. M. Roberts, Ed., Royal Society of Chemistry, London, 1989, pp. 182-196. CAVEAT: A Program to Facilitate the Structure-Derived Design of Biologically Active Molecules.
    • (1989) Molecular Recognition: Chemical and Biological Problems , pp. 182-196
    • Bartlett, P.A.1    Shea, G.T.2    Telfer, S.J.3    Waterman, S.4
  • 124
    • 0028380643 scopus 로고
    • CAVEAT: A Program to Facilitate the Design of Organic Molecules
    • G. Lauri and P. A. Bartlett, J. Compitt.-Aided Mol. Design, 8, 51 (1994). CAVEAT: A Program to Facilitate the Design of Organic Molecules.
    • (1994) J. Compitt.-Aided Mol. Design , vol.8 , pp. 51
    • Lauri, G.1    Bartlett, P.A.2
  • 125
    • 0028136087 scopus 로고
    • Nonpeptidic Fibrinogen Receptor Antagonists
    • V. Austel, F. Himmelsbach, and T. Müller, Drags Future, 19, 757 (1994). Nonpeptidic Fibrinogen Receptor Antagonists.
    • (1994) Drags Future , vol.19 , pp. 757
    • Austel, V.1    Himmelsbach, F.2    Müller, T.3
  • 132
    • 85068953320 scopus 로고    scopus 로고
    • See Reference 124 for a discussion of this methodology in detail
    • See Reference 124 for a discussion of this methodology in detail.
  • 133
    • 85050562346 scopus 로고
    • Distance Geometry in Molecular Modeling
    • J. M. Blaney, G. M. Crippen, A. Dearing, and J. S. Dixon, QCPE, Indiana University, Bloomington IN 47405. DGEOM, Program 590 K. B. Lipkowitz and D. B. Boyd, Eds., VCH Publishers, New York
    • J. M. Blaney, G. M. Crippen, A. Dearing, and J. S. Dixon, QCPE, Indiana University, Bloomington IN 47405. DGEOM, Program 590. See also J. M. Blaney and J. S. Dixon, in Reviews in Computational Chemistry, K. B. Lipkowitz and D. B. Boyd, Eds., VCH Publishers, New York, 1994, Vol. 5, pp. 299-335. Distance Geometry in Molecular Modeling.
    • (1994) Reviews in Computational Chemistry , vol.5 , pp. 299-335
    • Blaney, J.M.1    Dixon, J.S.2
  • 135
    • 0027053751 scopus 로고
    • Potent Inhibitors of Platelet Aggregation Based Upon the Arg-Gly-Asp-Phe Sequence of Fibrinogen. A Proposal on the Nature of the Binding Interactions between the Asp-Carboxylate of RGDX Mimetics and the Platelet GP IIb/IIIa Receptor
    • J. A. Zablocki, M. Miyano, S. N. Rao, S. Panzer-Knodle, N. Nicholson, and L. Feigen, J. Med. Chem., 35, 4914 (1992). Potent Inhibitors of Platelet Aggregation Based Upon the Arg-Gly-Asp-Phe Sequence of Fibrinogen. A Proposal on the Nature of the Binding Interactions Between the Asp-Carboxylate of RGDX Mimetics and the Platelet GP IIb/IIIa Receptor.
    • (1992) J. Med. Chem. , vol.35 , pp. 4914
    • Zablocki, J.A.1    Miyano, M.2    Rao, S.N.3    Panzer-Knodle, S.4    Nicholson, N.5    Feigen, L.6
  • 138
    • 85068947792 scopus 로고    scopus 로고
    • Gaussian, Inc., Pittsburgh, PA 15106
    • Gaussian, Inc., Pittsburgh, PA 15106.
  • 140
    • 0028263876 scopus 로고
    • Inhibition of CD4+ T Lymphocyte Binding to Fibronectin and Immune-Cell Accumulation in Inflammatory Sites by Nonpeptide Mimics of Arg-Gly-Asp
    • R. Hershkoviz, N. Greenspoon, Y. A. Mekori, R. Hadari, R. Alon, G. Kapustina, and O. Lider, Clin. Exp. Immunol., 95, 270 (1994). Inhibition of CD4+ T Lymphocyte Binding to Fibronectin and Immune-Cell Accumulation in Inflammatory Sites by Nonpeptide Mimics of Arg-Gly-Asp.
    • (1994) Clin. Exp. Immunol. , vol.95 , pp. 270
    • Hershkoviz, R.1    Greenspoon, N.2    Mekori, Y.A.3    Hadari, R.4    Alon, R.5    Kapustina, G.6    Lider, O.7
  • 142
    • 84982506235 scopus 로고
    • The First Design and Synthesis of a Steroidal Peptidomimetic. The Potential Value of Peptidomimetics in Elucidating the Bioactive Conformation of Peptide Ligands
    • R. Hirschmann, P. A. Sprengeler, T. Kawasaki, J. W. Leahy, W. C. Shakespeare, and A. B. Smith III,J. Am. Chem. Soc. 114, 9699 (1992). The First Design and Synthesis of a Steroidal Peptidomimetic. The Potential Value of Peptidomimetics in Elucidating the Bioactive Conformation of Peptide Ligands.
    • (1992) J. Am. Chem. Soc. , vol.114 , pp. 9699
    • Hirschmann, R.1    Sprengeler, P.A.2    Kawasaki, T.3    Leahy, J.W.4    Shakespeare, W.C.5    Smith III, A.B.6
  • 145
    • 33947092515 scopus 로고
    • Structural Basis of Activation and Action of Trypsin
    • R. Huber, and W. Bode, Acc. Chem. Res., 111 (1978). Structural Basis of Activation and Action of Trypsin. See also references therein.
    • (1978) Acc. Chem. Res. , pp. 111
    • Huber, R.1    Bode, W.2
  • 149
    • 85068954402 scopus 로고    scopus 로고
    • Details are to be published
    • Details are to be published.
  • 151
    • 0028064679 scopus 로고
    • Conformations of Cyclic Pentapeptide Endothelin Receptor Antagonists
    • J. W. Bean, C. E. Peishoff, and K. D. Kopple, Int. J. Peptide Protein Res., 44, 223 (1994). Conformations of Cyclic Pentapeptide Endothelin Receptor Antagonists.
    • (1994) Int. J. Peptide Protein Res. , vol.44 , pp. 223
    • Bean, J.W.1    Peishoff, C.E.2    Kopple, K.D.3
  • 152
    • 0037541976 scopus 로고
    • Side Chain Conformation of Somatostatin Analogs when Bound to Receptors
    • S. Reichlin, Ed., Plenum Press, New York
    • R. F. Nutt, C. D. Colton, R. Saperstein, and D. F. Veber, in Somatostatin, S. Reichlin, Ed., Plenum Press, New York, 1987, pp. 83-88. Side Chain Conformation of Somatostatin Analogs when Bound to Receptors.
    • (1987) Somatostatin , pp. 83-88
    • Nutt, R.F.1    Colton, C.D.2    Saperstein, R.3    Veber, D.F.4
  • 155
  • 156
    • 5944250450 scopus 로고
    • Energy Parameters in Polypeptides. VII. Geometric Parameters, Partial Atomic Charges, Nonbonded Interactions, Hydrogen Bond Interactions, and Intrinsic Torsional Potentials for the Naturally Occurring Amino Acids
    • F. Momany, R. F. McGuire, A. W. Burgess, and H. A. Scheraga,J. Phys. Chem., 79, 2361 (1975). Energy Parameters in Polypeptides. VII. Geometric Parameters, Partial Atomic Charges, Nonbonded Interactions, Hydrogen Bond Interactions, and Intrinsic Torsional Potentials for the Naturally Occurring Amino Acids.
    • (1975) J. Phys. Chem. , vol.79 , pp. 2361
    • Momany, F.1    McGuire, R.F.2    Burgess, A.W.3    Scheraga, H.A.4
  • 160
    • 85068953720 scopus 로고    scopus 로고
    • Molecular Simulations, Inc., San Diego, CA
    • Molecular Simulations, Inc., San Diego, CA.
  • 162
    • 44949267284 scopus 로고
    • An Alternative Method for the Alignment of Molecular Structures: Maximizing Electrostatic and Steric Overlap
    • S. Kearsley and G. Smith, Tetrahedron Compttt. Methodol., 3, 615 (1992). An Alternative Method for the Alignment of Molecular Structures: Maximizing Electrostatic and Steric Overlap.
    • (1992) Tetrahedron Compttt. Methodol. , vol.3 , pp. 615
    • Kearsley, S.1    Smith, G.2
  • 165
    • 0037571112 scopus 로고    scopus 로고
    • Merck Molecular Force Field. I. Basis, Form, Scope, Parameterization, and Performance of MMFF94
    • T. A. Halgren, J. Comput. Chem., 17, 490 (1996). Merck Molecular Force Field. I. Basis, Form, Scope, Parameterization, and Performance of MMFF94. See also following papers of series.
    • (1996) J. Comput. Chem. , vol.17 , pp. 490
    • Halgren, T.A.1
  • 166
    • 85068948278 scopus 로고    scopus 로고
    • SQUEAL (Structural and Qualitative Electrostatic ALignment) is an unpublished variation of SEAL. M. D. Miller, Merck Research Laboratories, West Point, PA
    • SQUEAL (Structural and Qualitative Electrostatic ALignment) is an unpublished variation of SEAL. M. D. Miller, Merck Research Laboratories, West Point, PA.
  • 167
    • 0021326036 scopus 로고
    • Neurotensin Stimulates Formation of Cyclic-GMP in Murine Neuro-Balstoma Clone N1E-115
    • J. A. Gilbert and E. Richelson, Eur. J. Pharmacol., 99, 245 (1984). Neurotensin Stimulates Formation of Cyclic-GMP in Murine Neuro-Balstoma Clone N1E-115.
    • (1984) Eur. J. Pharmacol. , vol.99 , pp. 245
    • Gilbert, J.A.1    Richelson, E.2
  • 168
    • 0028493021 scopus 로고
    • Rational Design of Novel Neurotensin Mimetics: Discovery of a Pharmacologically Unprecedented Agent Exhibiting Concentration-Dependent Dual Effects as Antagonist and Full Agonist
    • Y.-P. Pang, J. Zaidi, A. P. Kozikowski. B. Cusack, and E. Richelson, J. Comput. Aided Mol. Design, 8, 433 (1994). Rational Design of Novel Neurotensin Mimetics: Discovery of a Pharmacologically Unprecedented Agent Exhibiting Concentration-Dependent Dual Effects as Antagonist and Full Agonist.
    • (1994) J. Comput. Aided Mol. Design , vol.8 , pp. 433
    • Pang, Y.-P.1    Zaidi, J.2    Kozikowski, A.P.3    Cusack, B.4    Richelson, E.5
  • 171
    • 0025974617 scopus 로고
    • Simulation of the Structure and Dynamics of the Bis(penicillamine) Enkephalin Zwitterion
    • P. E. Smith, L. X. Dang, and B. M. Pettitt, J. Am. Chem. Soc., 113, 67 (1991). Simulation of the Structure and Dynamics of the Bis(penicillamine) Enkephalin Zwitterion.
    • (1991) J. Am. Chem. Soc. , vol.113 , pp. 67
    • Smith, P.E.1    Dang, L.X.2    Pettitt, B.M.3
  • 172
    • 0027158693 scopus 로고
    • Conformationally Constrained Nonpeptide β-Turn Mimetics of Enkephalin
    • B. Gardner, H. Nakanishi, and M. Kahn, Tetrahedron, 49, 3433 (1993). Conformationally Constrained Nonpeptide β-Turn Mimetics of Enkephalin.
    • (1993) Tetrahedron , vol.49 , pp. 3433
    • Gardner, B.1    Nakanishi, H.2    Kahn, M.3
  • 176
    • 0000782536 scopus 로고
    • A New Approach to Probing Conformational Space with Molecular Mechanics: Random Incremental Pulse Search
    • D. M. Ferguson and D. J. Raber,J. Am. Chem. Soc., 111,4371 (1989). A New Approach to Probing Conformational Space with Molecular Mechanics: Random Incremental Pulse Search.
    • (1989) J. Am. Chem. Soc. , vol.111 , pp. 4371
    • Ferguson, D.M.1    Raber, D.J.2
  • 177
    • 84988120944 scopus 로고
    • Molecular Mechanics Conformational Analysis of Cyclononane using the RIPS Method and Comparison with Quantum-Mechanical Calculations
    • D. M. Ferguson, W. A. Glauser, and D. J. Raber, J. Comput. Chem., 10, 903 (1989). Molecular Mechanics Conformational Analysis of Cyclononane using the RIPS Method and Comparison with Quantum-Mechanical Calculations.
    • (1989) J. Comput. Chem. , vol.10 , pp. 903
    • Ferguson, D.M.1    Glauser, W.A.2    Raber, D.J.3
  • 180
    • 0024418444 scopus 로고
    • Thyrotropin Releasing Hormone: Biomedical Significance, G. Metcalf, and I. M. D. Jackson, Eds., New York
    • See, for example, M. Miyamoto, N. Yamazaki, A. Nagaoka, and Y. Nigawa, in Thyrotropin Releasing Hormone: Biomedical Significance, G. Metcalf, and I. M. D. Jackson, Eds., Annals of the New York Academy of Science, New York, pp. 508 ff., 1989.
    • (1989) Annals of the New York Academy of Science
    • Miyamoto, M.1    Yamazaki, N.2    Nagaoka, A.3    Nigawa, Y.4
  • 181
    • 37049107472 scopus 로고
    • Molecular Conformation of Thyrotropin Releasing Hormone from the X-Ray Analysis of its Tartrate
    • K. Kamiya, M. Takamoto, Y. Wada, M. Fujino, and M. Nishikawa, J. Chem. Soc. Chem. Commun., 438 (1980). Molecular Conformation of Thyrotropin Releasing Hormone from the X-Ray Analysis of its Tartrate.
    • (1980) J. Chem. Soc. Chem. Commun. , pp. 438
    • Kamiya, K.1    Takamoto, M.2    Wada, Y.3    Fujino, M.4    Nishikawa, M.5
  • 183
    • 0003118187 scopus 로고
    • Ph.D. Thesis, Washington University, St. Louis, MO
    • M. L. Moore, Ph.D. Thesis, Washington University, St. Louis, MO, 1978, p. 23. Probing the Thyroliberin Receptor.
    • (1978) Probing the Thyroliberin Receptor , pp. 23
    • Moore, M.L.1
  • 185
    • 0029102387 scopus 로고
    • Peptide Mimetics of Thyrotropin-Releasing Hormone Based on a Cyclohexane Framework: Design, Synthesis, and Cognition-Enhancing Properties
    • G. L. Oison, H.-C. Cheung, E. Chiang, V. S. Madison, J. Sepinwall, G. P. Vincent, A. Winokur, and K. A. Gary, J. Med. Chem., 38, 2866 (1995). Peptide Mimetics of Thyrotropin-Releasing Hormone Based on a Cyclohexane Framework: Design, Synthesis, and Cognition-Enhancing Properties.
    • (1995) J. Med. Chem. , vol.38 , pp. 2866
    • Oison, G.L.1    Cheung, H.-C.2    Chiang, E.3    Madison, V.S.4    Sepinwall, J.5    Vincent, G.P.6    Winokur, A.7    Gary, K.A.8
  • 188
    • 0024318318 scopus 로고
    • Neuropeptides and Inflammation: The Role of Substance P
    • D. G. Payan, Annu. Rev. Med. Chem., 40, 341 (1989). Neuropeptides and Inflammation: The Role of Substance P.
    • (1989) Annu. Rev. Med. Chem. , vol.40 , pp. 341
    • Payan, D.G.1
  • 189
    • 0026153696 scopus 로고
    • Toward Nonpeptidal Substance P Mimetic Analogues: Design, Synthesis, and Biological Activity
    • M. Chorev, E. Roubini, C. Gilon, and Z. Selinger, Biopolymers, 31, 725 (1991). Toward Nonpeptidal Substance P Mimetic Analogues: Design, Synthesis, and Biological Activity.
    • (1991) Biopolymers , vol.31 , pp. 725
    • Chorev, M.1    Roubini, E.2    Gilon, C.3    Selinger, Z.4
  • 191
    • 0027300608 scopus 로고
    • Design, Synthesis and Three-Dimensional Structural Characterization of a Constrained Ω-Loop Excised from Interleukin 1α
    • R. Sarabu, K. Lovey, V. S. Madison, D. C. Fry, D. N. Greeley, C. M. Cook, and G. L. Olson, Tetrahedron, 49, 3629 (1993). Design, Synthesis and Three-Dimensional Structural Characterization of a Constrained Ω-Loop Excised from Interleukin 1α.
    • (1993) Tetrahedron , vol.49 , pp. 3629
    • Sarabu, R.1    Lovey, K.2    Madison, V.S.3    Fry, D.C.4    Greeley, D.N.5    Cook, C.M.6    Olson, G.L.7
  • 195
    • 0000762297 scopus 로고
    • Crystal Structure and Conformation of cyclo-(Glycylprolylglycyl-D-alanylprolyl) Containing 4 → 1 and 3 → 1 Intramolecular Hydrogen Bonds
    • I. L. Karle, J. Am. Chem. Soc., 100, 1286 (1978). Crystal Structure and Conformation of cyclo-(Glycylprolylglycyl-D-alanylprolyl) Containing 4 → 1 and 3 → 1 Intramolecular Hydrogen Bonds.
    • (1978) J. Am. Chem. Soc. , vol.100 , pp. 1286
    • Karle, I.L.1
  • 198
    • 0000603111 scopus 로고
    • Conformational Analysis of Bradykinin by Annealed Molecular Dynamics and Comparison to NMR Derived Conformations
    • J. M. Salvino, P. R. Seoane, and R. E. Dolle,J. Comput. Chem., 14, 438 (1993). Conformational Analysis of Bradykinin by Annealed Molecular Dynamics and Comparison to NMR Derived Conformations.
    • (1993) J. Comput. Chem. , vol.14 , pp. 438
    • Salvino, J.M.1    Seoane, P.R.2    Dolle, R.E.3
  • 200
    • 0025845088 scopus 로고
    • Design and Conformational Analysis of Several Highly Potent Bradykinin Receptor Antagonists
    • D. J. Kyle, J. A. Martin, S. G. Farmer, and R. M. Burch, J. Med. Chein., 34, 1230 (1991). Design and Conformational Analysis of Several Highly Potent Bradykinin Receptor Antagonists.
    • (1991) J. Med. Chein. , vol.34 , pp. 1230
    • Kyle, D.J.1    Martin, J.A.2    Farmer, S.G.3    Burch, R.M.4
  • 201
    • 0026897295 scopus 로고
    • A Novel β-Turn Mimic Useful for Mapping the Unknown Topology of Peptide Receptors
    • D. J. Kyle, L. M. Green, P. R. Blake, D. Smithwick, and M. F. Summers, Peptide Res., 5, 206 (1992). A Novel β-Turn Mimic Useful for Mapping the Unknown Topology of Peptide Receptors.
    • (1992) Peptide Res. , vol.5 , pp. 206
    • Kyle, D.J.1    Green, L.M.2    Blake, P.R.3    Smithwick, D.4    Summers, M.F.5
  • 202
    • 0025850422 scopus 로고
    • Design and Synthesis of a Mimetic from an Antibody Complementarity-Determining Region
    • H. U. Saragovi, D. Fitzpatrick, A. Raktabutr, H. Nakanishi, M. Kahn, and M. I. Greene, Science, 253, 792 (1991). Design and Synthesis of a Mimetic from an Antibody Complementarity-Determining Region.
    • (1991) Science , vol.253 , pp. 792
    • Saragovi, H.U.1    Fitzpatrick, D.2    Raktabutr, A.3    Nakanishi, H.4    Kahn, M.5    Greene, M.I.6
  • 203
    • 0026781840 scopus 로고
    • Refined Crystal Structure of the Influenza Virus N9 Neuraminidase-NC41 Fab Complex
    • W. R. Tulip, J. N. Varghese, W. G. Laver, R. G. Webster, and P. M. Colman, J. Mol. Biol., 227, 122 (1992). Refined Crystal Structure of the Influenza Virus N9 Neuraminidase-NC41 Fab Complex.
    • (1992) J. Mol. Biol. , vol.227 , pp. 122
    • Tulip, W.R.1    Varghese, J.N.2    Laver, W.G.3    Webster, R.G.4    Colman, P.M.5
  • 204
    • 0028236239 scopus 로고
    • Design and Synthesis of a Biologically Active Antibody Mimic Based on an Antibody-Antigen Crystal Structure
    • M. L. Smythe and M. von Itzstein, J. Am. Chein. Soc., 116, 2725 (1994). Design and Synthesis of a Biologically Active Antibody Mimic Based on an Antibody-Antigen Crystal Structure.
    • (1994) J. Am. Chein. Soc. , vol.116 , pp. 2725
    • Smythe, M.L.1    Von Itzstein, M.2
  • 205
    • 0027324832 scopus 로고
    • Protein β-Turn Mimetics II: Design, Synthesis, and Evaluation in the Cyclic Peptide Gramicidin S
    • W. C. Ripka, G. V. De Lucca, A. C. Bach II, R. S. Pottorf, and J. M. Blaney, Tetrahedron, 49, 3609 (1993). Protein β-Turn Mimetics II: Design, Synthesis, and Evaluation in the Cyclic Peptide Gramicidin S.
    • (1993) Tetrahedron , vol.49 , pp. 3609
    • Ripka, W.C.1    De Lucca, G.V.2    Bach II, A.C.3    Pottorf, R.S.4    Blaney, J.M.5
  • 206
    • 0023059915 scopus 로고
    • Insect Hypertrehalosemic Hormone: Isolation and Primary Structure from Blaberus discoidalis Cockroaches
    • T. K. Hayes, L. L. Keeley, and D. K. Knight, Biochem. Biophys. Res. Commun., 140, 674 (1986). Insect Hypertrehalosemic Hormone: Isolation and Primary Structure from Blaberus discoidalis Cockroaches.
    • (1986) Biochem. Biophys. Res. Commun. , vol.140 , pp. 674
    • Hayes, T.K.1    Keeley, L.L.2    Knight, D.K.3
  • 208
    • 0017183201 scopus 로고
    • The Crystal Structure of a Post-Synaptic Neurotoxin from Sea Snake at 2.2 a Resolution
    • G. A. Petsko and D. Tsernoglou, FEBS Lett., 68, 1 (1976). The Crystal Structure of a Post-Synaptic Neurotoxin from Sea Snake at 2.2 A Resolution.
    • (1976) FEBS Lett. , vol.68 , pp. 1
    • Petsko, G.A.1    Tsernoglou, D.2
  • 210
    • 0343674306 scopus 로고
    • The Design and Synthesis of a Nonpeptide Mimic of Erabutoxin
    • M. Kahn, B. Chen, and P. Zieske, Heterocycles, 25, 29 (1987). The Design and Synthesis of a Nonpeptide Mimic of Erabutoxin.
    • (1987) Heterocycles , vol.25 , pp. 29
    • Kahn, M.1    Chen, B.2    Zieske, P.3
  • 213
    • 0001586425 scopus 로고
    • Probing a Molecular Model of Taste Utilizing Peptidomimetic Stereoisomers of 2-Aminocyclopentanecarboxylic Acid Methyl Ester
    • T. Yamazaki, Y.-F. Zhu, A. Probstl, R. K. Chadha, and M. Goodman, J. Org. Chem., 56, 6644 (1991). Probing a Molecular Model of Taste Utilizing Peptidomimetic Stereoisomers of 2-Aminocyclopentanecarboxylic Acid Methyl Ester.
    • (1991) J. Org. Chem. , vol.56 , pp. 6644
    • Yamazaki, T.1    Zhu, Y.-F.2    Probstl, A.3    Chadha, R.K.4    Goodman, M.5
  • 214
    • 33748247569 scopus 로고
    • Conformational Requirements for Sweet-Tasting Peptides and Peptidomimetics
    • T. Yamazaki, E. Benedetti, D. Kent, and M. Goodman, Angew. Chem. Int. Ed. Engl., 33, 1437 (1994). Conformational Requirements for Sweet-Tasting Peptides and Peptidomimetics.
    • (1994) Angew. Chem. Int. Ed. Engl. , vol.33 , pp. 1437
    • Yamazaki, T.1    Benedetti, E.2    Kent, D.3    Goodman, M.4
  • 216
    • 0000603109 scopus 로고
    • Design, Synthesis and Conformational Analysis of a Novel Spiro-Bicyclic System as a Type II β-Turn Peptidomimetic
    • M. J. Genin and R. L. Johnson, J. Am. Chem. Soc., 114, 8778 (1992). Design, Synthesis and Conformational Analysis of a Novel Spiro-Bicyclic System as a Type II β-Turn Peptidomimetic.
    • (1992) J. Am. Chem. Soc. , vol.114 , pp. 8778
    • Genin, M.J.1    Johnson, R.L.2
  • 218
    • 0030503687 scopus 로고    scopus 로고
    • Free Energy by Molecular Simulation
    • K. B. Lipkowitz and D. B. Boyd, Eds., VCH Publishers, New York
    • T. P. Straatsma, in Reviews in Computational Chemistry, K. B. Lipkowitz and D. B. Boyd, Eds., VCH Publishers, New York, 1996, Vol. 9, pp. 81-127. Free Energy by Molecular Simulation.
    • (1996) Reviews in Computational Chemistry , vol.9 , pp. 81-127
    • Straatsma, T.P.1
  • 219
    • 0000956129 scopus 로고    scopus 로고
    • A Perspective of Modern Methods in Computer-Aided Drug Design
    • K. B. Lipkowitz and D. B. Boyd, Eds., VCH Publishers, New York
    • See also, L. M. Balbes, S. W. Mascarella, and D. B. Boyd, in Reviews in Computational Chemistry, K. B. Lipkowitz and D. B. Boyd, Eds., VCH Publishers, New York, Vol. 5, pp. 357-379. A Perspective of Modern Methods in Computer-Aided Drug Design.
    • Reviews in Computational Chemistry , vol.5 , pp. 357-379
    • Balbes, L.M.1    Mascarella, S.W.2    Boyd, D.B.3


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.