메뉴 건너뛰기




Volumn 7, Issue 5, 2012, Pages 375-383

Halogen bonding for rational drug design and new drug discovery

Author keywords

Binding affinity; Drug design; Halogen bonding; Inhibitors

Indexed keywords

BENZIMIDAZOLE DERIVATIVE; BLOOD CLOTTING FACTOR 10A; CYCLIN DEPENDENT KINASE 2; CYCLIN DEPENDENT KINASE 9; HALOGEN; HYDROGEN; LEWIS BASE; LIGAND; PHOSPHODIESTERASE V; PROTEIN KINASE; RNA DIRECTED DNA POLYMERASE; SILDENAFIL;

EID: 84860380236     PISSN: 17460441     EISSN: 1746045X     Source Type: Journal    
DOI: 10.1517/17460441.2012.678829     Document Type: Review
Times cited : (262)

References (76)
  • 3
    • 79955766939 scopus 로고    scopus 로고
    • Aromatic rings in chemical and biological recognition: Energetics and structures
    • Salonen LM, Ellermann M, Diederich F. Aromatic rings in chemical and biological recognition: Energetics and structures. Angew Chem Int Ed 2011;50:4808-42
    • (2011) Angew. Chem. Int. Ed. , vol.50 , pp. 4808-4842
    • Salonen, L.M.1    Ellermann, M.2    Diederich, F.3
  • 5
    • 77953631827 scopus 로고    scopus 로고
    • A medicinal chemist's guide to molecular interactions
    • Bissantz C, Kuhn B, Stahl M. A medicinal chemist's guide to molecular interactions. J Med Chem 2010;53:5061-84
    • (2010) J. Med. Chem. , vol.53 , pp. 5061-5084
    • Bissantz, C.1    Kuhn, B.2    Stahl, M.3
  • 6
    • 80053464530 scopus 로고    scopus 로고
    • Putting anion-pi interactions into perspective
    • Frontera A, Gamez P, Mascal M, et al. Putting anion-pi interactions into perspective. Angew Chem Int Ed 2011;50:9564-83
    • (2011) Angew. Chem. Int. Ed. , vol.50 , pp. 9564-9583
    • Frontera, A.1    Gamez, P.2    Mascal, M.3
  • 7
    • 34147213661 scopus 로고    scopus 로고
    • Lone pair-Aromatic interactions: To stabilize or not to stabilize
    • Egli M, Sarkhel S. Lone pair-Aromatic interactions: To stabilize or not to stabilize. Acc Chem Res 2007;40:197-205
    • (2007) Acc. Chem. Res. , vol.40 , pp. 197-205
    • Egli, M.1    Sarkhel, S.2
  • 8
    • 33947666527 scopus 로고    scopus 로고
    • Propensities of polar and aromatic amino acids in noncanonical interactions: Nonbonded contacts analysis of protein-ligand complexes in crystal structures
    • DOI 10.1021/jm061038a
    • Imai YN, Inoue Y, Yamamoto Y. Propensities of polar and aromatic amino acid in noncanonical interactions: Nonbonded contacts analysis of protein-ligand complexes in crystal structures. J Med Chem 2007;50:1189-96 (Pubitemid 46496319)
    • (2007) Journal of Medicinal Chemistry , vol.50 , Issue.6 , pp. 1189-1196
    • Imai, Y.N.1    Inoue, Y.2    Yamamoto, Y.3
  • 10
    • 20444479110 scopus 로고    scopus 로고
    • Halogen bonding based recognition processes: A world parallel to hydrogen bonding
    • DOI 10.1021/ar0400995
    • Metrangolo P, Neukirch H, Pilati T, et al. Halogen bonding based recognition process: A world parallel to hydrogen bonding. Acc Chem Res 2005;38:386-95 (Pubitemid 40816650)
    • (2005) Accounts of Chemical Research , vol.38 , Issue.5 , pp. 386-395
    • Metrangolo, P.1    Neukirch, H.2    Pilati, T.3    Resnati, G.4
  • 13
    • 77955809684 scopus 로고    scopus 로고
    • Halogen bonding: A general route in anion recognition and coordination
    • Cavallo G, Metrangolo P, Pilati T, et al. Halogen bonding: A general route in anion recognition and coordination. Chem Soc Rev 2010;39:3772-84
    • (2010) Chem. Soc. Rev. , vol.39 , pp. 3772-3784
    • Cavallo, G.1    Metrangolo, P.2    Pilati, T.3
  • 14
    • 49649098999 scopus 로고    scopus 로고
    • Halogen versus hydrogen
    • Metrangolo P, Resnati G. Halogen versus hydrogen. Science 2008;321:918-19
    • (2008) Science , vol.321 , pp. 918-919
    • Metrangolo, P.1    Resnati, G.2
  • 15
    • 72149112462 scopus 로고    scopus 로고
    • Halogen bonding in metal-organic-supramolecular networks
    • Bertani R, Sgarbossa P, Venzo A, et al. Halogen bonding in metal-organic-supramolecular networks. Coord Chem Rev 2010;254:677-95
    • (2010) Coord Chem. Rev. , vol.254 , pp. 677-695
    • Bertani, R.1    Sgarbossa, P.2    Venzo, A.3
  • 16
    • 62449180950 scopus 로고    scopus 로고
    • Nonporous organic solids capable of dynamically resolving mixtures of diiodoperfluoroalkanes
    • Metrangolo P, Carcenac Y, Lahtinen M, et al. Nonporous organic solids capable of dynamically resolving mixtures of diiodoperfluoroalkanes. Science 2009;323:1461-4
    • (2009) Science , vol.323 , pp. 1461-1464
    • Metrangolo, P.1    Carcenac, Y.2    Lahtinen, M.3
  • 17
    • 77954598483 scopus 로고    scopus 로고
    • The halogen bond: An interim perspective
    • Legon AC. The halogen bond: An interim perspective. Phys Chem Chem Phys 2010;12:7736-47
    • (2010) Phys. Chem. Chem. Phys. , vol.12 , pp. 7736-7747
    • Legon, A.C.1
  • 19
    • 50249112252 scopus 로고    scopus 로고
    • Halogen bonded supramolecular complexes and networks
    • Rissanen K. Halogen bonded supramolecular complexes and networks. CrystEngComm 2008;10:1107-13
    • (2008) Cryst. Eng. Comm. , vol.10 , pp. 1107-1113
    • Rissanen, K.1
  • 22
    • 82955171705 scopus 로고    scopus 로고
    • Assaying the energies of biological halogen bonds
    • Carter M, Ho PS. Assaying the energies of biological halogen bonds. Cryst Growth Des 2011;11:5087-95
    • (2011) Cryst. Growth Des. , vol.11 , pp. 5087-5095
    • Carter, M.1    Ho, P.S.2
  • 23
    • 77950789591 scopus 로고    scopus 로고
    • Halogen atoms in the modern medicinal chemistry: Hints for the drug design
    • Hernandes MZ, Cavalcanti SMT, Moreira DRM, et al. Halogen atoms in the modern medicinal chemistry: Hints for the drug design. Curr Drug Targets 2010;11:303-14
    • (2010) Curr. Drug Targets , vol.11 , pp. 303-314
    • Hernandes, M.Z.1    Cavalcanti, S.M.T.2    Moreira, D.R.M.3
  • 24
    • 65649131517 scopus 로고    scopus 로고
    • Evaluating the potential for halogen bonding in the oxyanion hole of ketosteroid isomerase using unnatural amino acid mutagenesis
    • Kraut DA, Churchill MJ, Dawson PE, et al. Evaluating the potential for halogen bonding in the oxyanion hole of ketosteroid isomerase using unnatural amino acid mutagenesis. ACS Chem Biol 2009;4:269-73
    • (2009) ACS Chem. Biol. , vol.4 , pp. 269-273
    • Kraut, D.A.1    Churchill, M.J.2    Dawson, P.E.3
  • 25
    • 67849128457 scopus 로고    scopus 로고
    • Halogen bonds as orthogonal molecular interactions to hydrogen bonds
    • Voth AR, Khuu P, Oishi K, et al. Halogen bonds as orthogonal molecular interactions to hydrogen bonds. Nat Chem 2009;1:74-9
    • (2009) Nat. Chem. , vol.1 , pp. 74-9
    • Voth, A.R.1    Khuu, P.2    Oishi, K.3
  • 29
    • 77954593406 scopus 로고    scopus 로고
    • Halogen bonding: An electrostatically-driven highly directional noncovalent interaction
    • Politzer P, Murray JS, Clark T. Halogen bonding: An electrostatically- driven highly directional noncovalent interaction. Phys Chem Chem Phys 2010;12:7748-57
    • (2010) Phys. Chem. Chem. Phys. , vol.12 , pp. 7748-7757
    • Politzer, P.1    Murray, J.S.2    Clark, T.3
  • 30
    • 78650168509 scopus 로고    scopus 로고
    • Directional weak intermolecular interactions: Tau-hole bonding
    • Murray JS, Riley KE, Politer P, et al. Directional weak intermolecular interactions: Tau-hole bonding. Aust J Chem 2010;63:1598-607
    • (2010) Aust. J. Chem. , vol.63 , pp. 1598-1607
    • Murray, J.S.1    Riley, K.E.2    Politer, P.3
  • 31
    • 77649091129 scopus 로고    scopus 로고
    • A tridentate halogen-bonding receptor for tight binding of halide anions
    • Sarwar MG, Dragisic B, Sagoo S, et al. A tridentate halogen-bonding receptor for tight binding of halide anions. Angew Chem Int Ed 2010;49:1674-7
    • (2010) Angew. Chem. Int. Ed. , vol.49 , pp. 1674-1677
    • Sarwar, M.G.1    Dragisic, B.2    Sagoo, S.3
  • 32
    • 79960031261 scopus 로고    scopus 로고
    • Anion receptors composed of hydrogen- and halogen-bond donor groups: Modulating selectivity with combinations of district noncovalent interactions
    • Chudzinski MG, McClary CA, Taylor MS. Anion receptors composed of hydrogen- and halogen-bond donor groups: Modulating selectivity with combinations of district noncovalent interactions. J Am Chem Soc 2010;133:10559-68
    • (2010) J. Am. Chem. Soc. , vol.133 , pp. 10559-68
    • Chudzinski, M.G.1    McClary, C.A.2    Taylor, M.S.3
  • 33
    • 82455205707 scopus 로고    scopus 로고
    • Ditopic ion transport systems: Anion-pi interactions and halogen bonds at work
    • Jentzsch AV, Emery D, Mareda J, et al. Ditopic ion transport systems: Anion-pi interactions and halogen bonds at work. Angew Chem Int Ed 2011;50:11675-8
    • (2011) Angew. Chem. Int. Ed. , vol.50 , pp. 11675-8
    • Jentzsch, A.V.1    Emery, D.2    Mareda, J.3
  • 34
    • 34347385022 scopus 로고    scopus 로고
    • Halogen bonding and the design of new materials: Organic bromides, chlorides and perhaps even fluorides as donors
    • DOI 10.1007/s00894-007-0176-9, International conference and workshop: Modeling and Design of Molecular Materials, 10-15 September 2006, Wrocklaw, Poland
    • Politzer P, Murray JS, Concha MC. Halogen bonding and the design of new materials: Organic bromines, chlorides and perhaps even fluorides as donors. J Mol Model 2007;13:643-50 (Pubitemid 47023388)
    • (2007) Journal of Molecular Modeling , vol.13 , Issue.6-7 , pp. 643-650
    • Politzer, P.1    Murray, J.S.2    Concha, M.C.3
  • 35
    • 36048948031 scopus 로고    scopus 로고
    • Ab initio investigation of halogen bonding interactions involving fluorine as an electron acceptor
    • Lu YX, Zou JW, Yu QS, et al. Ab initio investigation of halogen bonding interactions involving fluorine as an electron acceptor. Chem Phys Lett 2007;449:6-10
    • (2007) Chem. Phys. Lett. , vol.449 , pp. 6-10
    • Lu, Y.X.1    Zou, J.W.2    Yu, Q.S.3
  • 36
    • 80054984935 scopus 로고    scopus 로고
    • The fluorine atom as a halogen bond donor, viz a positive site
    • Metrangolo P, Murray JS, Pilati T, et al. The fluorine atom as a halogen bond donor, viz. a positive site. CrystEngComm 2011;13:6593-6
    • (2011) Cryst. Eng. Comm. , vol.13 , pp. 6593-6596
    • Metrangolo, P.1    Murray, J.S.2    Pilati, T.3
  • 37
    • 80052540036 scopus 로고    scopus 로고
    • Fluorine-centered halogen bonding: A factor in recognition phenomena and reactivity
    • Metrangolo P, Murray JS, Pilati T, et al. Fluorine-centered halogen bonding: A factor in recognition phenomena and reactivity. Cryst Growth Des 2011;11:4238-46
    • (2011) Cryst. Growth Des. , vol.11 , pp. 4238-4246
    • Metrangolo, P.1    Murray, J.S.2    Pilati, T.3
  • 38
    • 70349155924 scopus 로고    scopus 로고
    • C-X H contacts in biomolecular systems: How they contribute to protein-ligand binding affinity
    • Lu Y, Wang Y, Xu Z, et al. C-X.H contacts in biomolecular systems: How they contribute to protein-ligand binding affinity. J Phys Chem B 2009;113:12615-21
    • (2009) J. Phys. Chem. B. , vol.113 , pp. 12615-21
    • Lu, Y.1    Wang, Y.2    Xu, Z.3
  • 39
    • 17044421336 scopus 로고    scopus 로고
    • Orthogonal multipolar interactions in structural chemistry and biology
    • Paulini R, Muller K, Dieherich F. Orthogonal multipolar interactions in structural chemistry and biology. Angew Chem Int Ed 2005;44:1788-805
    • (2005) Angew Chem. Int. Ed. , vol.44 , pp. 1788-1805
    • Paulini, R.1    Muller, K.2    Dieherich, F.3
  • 40
    • 0000243556 scopus 로고    scopus 로고
    • Understanding the Behavior of Halogens as Hydrogen Bond Acceptors
    • DOI 10.1021/cg015522k
    • Brammer L, Bruton EA, Sherwood P. Understanding the behavior of halogens as hydrogen bond acceptors. Cryst Growth Des 2001;1:277-90 (Pubitemid 33680419)
    • (2001) Crystal Growth and Design , vol.1 , Issue.4 , pp. 277-290
    • Brammer, L.1    Bruton, E.A.2    Sherwood, P.3
  • 42
    • 34548821001 scopus 로고    scopus 로고
    • The role of halogen bonding in inhibitor recognition and binding by protein kinases
    • DOI 10.2174/156802607781696846
    • Voth AR, Ho PS. The role of halogen bonding in inhibitor recognition and binding by protein kinases. Curr Top Med Chem 2007;7:1336-48 (Pubitemid 47484763)
    • (2007) Current Topics in Medicinal Chemistry , vol.7 , Issue.14 , pp. 1336-1348
    • Voth, A.R.1    Ho, P.S.2
  • 43
    • 77951793408 scopus 로고    scopus 로고
    • Nonbonding interactions of organic halogens in biological systems: Implications for drug discovery and biomolecular design
    • Lu Y, Wang Y, Zhu W. Nonbonding interactions of organic halogens in biological systems: Implications for drug discovery and biomolecular design. Phys Chem Chem Phys 2010;12:4543-51
    • (2010) Phys. Chem. Chem. Phys. , vol.12 , pp. 4543-4551
    • Lu, Y.1    Wang, Y.2    Zhu, W.3
  • 44
    • 79954586104 scopus 로고    scopus 로고
    • Halogen bonding in halocarbon-protein complexes: A structural survey
    • Parisini E, Metrangolo P, Pilati T. Halogen bonding in halocarbon-protein complexes: A structural survey. Chem Soc Rev 2011;40:2267-78
    • (2011) Chem. Soc. Rev. , vol.40 , pp. 2267-2278
    • Parisini, E.1    Metrangolo, P.2    Pilati, T.3
  • 45
    • 65649095907 scopus 로고    scopus 로고
    • Halogen bonding - A novel interaction for rational drug design
    • Lu Y, Shi T, Wang Y, et al. Halogen bonding - A novel interaction for rational drug design. J Med Chem 2009;52:2854-62
    • (2009) J. Med. Chem. , vol.52 , pp. 2854-2862
    • Lu, Y.1    Shi, T.2    Wang, Y.3
  • 46
    • 79955526259 scopus 로고    scopus 로고
    • How does halogen bonding behave in solution? A theoretical study using implicit solvation model
    • Lu Y, Li H, Zhu X, et al. How does halogen bonding behave in solution? A theoretical study using implicit solvation model. J Phys Chem A 2011;115:4467-75
    • (2011) J. Phys. Chem. A. , vol.115 , pp. 4467-4475
    • Lu, Y.1    Li, H.2    Zhu, X.3
  • 47
    • 84859580690 scopus 로고    scopus 로고
    • Effects of solvent on weak halogen bonds: Density functional theory calculations
    • Lu Y, Li H, Zhu X, et al. Effects of solvent on weak halogen bonds: Density functional theory calculations. Int J Quantum Chem 2012;112:1421-30
    • (2012) Int. J. Quantum. Chem. , Issue.112 , pp. 1421-1430
    • Lu, Y.1    Li, H.2    Zhu, X.3
  • 48
    • 79959921557 scopus 로고    scopus 로고
    • Semiempirical quantum mechanical method PM6-DH2X describes the geometry and energetics of CK2-inhibitor complexes involving halogen bonds well, while the empirical potential fails
    • Dobes P, Rezac J, Fanfrlik J, et al. Semiempirical quantum mechanical method PM6-DH2X describes the geometry and energetics of CK2-inhibitor complexes involving halogen bonds well, while the empirical potential fails. J Phys Chem B 2011;115:8581-9
    • (2011) J. Phys. Chem. B. , vol.115 , pp. 8581-8589
    • Dobes, P.1    Rezac, J.2    Fanfrlik, J.3
  • 49
    • 80053555768 scopus 로고    scopus 로고
    • Strength and character of halogen bonds in protein-ligand complexes
    • Riley KE, Hobza P. Strength and character of halogen bonds in protein-ligand complexes. Cryst Growth Des 2011;11:4272-8
    • (2011) Cryst. Growth Des. , vol.11 , pp. 4272-4278
    • Riley, K.E.1    Hobza, P.2
  • 50
    • 79959739959 scopus 로고    scopus 로고
    • Molecular mechanical study of halogen bonding in drug design
    • Ibrahim MAA. Molecular mechanical study of halogen bonding in drug design. J Comput Chem 2011;32:2564-74
    • (2011) J. Comput. Chem. , vol.32 , pp. 2564-2574
    • Ibrahim, M.A.A.1
  • 51
    • 80054898012 scopus 로고    scopus 로고
    • Performance assessment of semiempirical molecular orbital methods in describing halogen bonding: Quantum mechanical and quantum mechanical/molecular mechanical-molecular dynamics study
    • Ibrahim MAA. Performance assessment of semiempirical molecular orbital methods in describing halogen bonding: quantum mechanical and quantum mechanical/molecular mechanical-molecular dynamics study. J Chem Inf Model 2011;51:2549-59
    • (2011) J. Chem. Inf. Model , vol.51 , pp. 2549-2559
    • Ibrahim, M.A.A.1
  • 52
    • 80055038428 scopus 로고    scopus 로고
    • Halogen bonding in ligand-receptor systems in the framework of classical force fields
    • Rendine S, Pieraccini S, Forni A, et al. Halogen bonding in ligand-receptor systems in the framework of classical force fields. Phys Chem Chem Phys 2011;13:19508-16
    • (2011) Phys. Chem. Chem. Phys. , vol.13 , pp. 19508-16
    • Rendine, S.1    Pieraccini, S.2    Forni, A.3
  • 53
    • 0344927100 scopus 로고    scopus 로고
    • 3-Iodo-4-phenoxypyridinones (IOPY's), a new family of highly potent non-nucleoside inhibitors of HIV-1 reverse transcriptase
    • DOI 10.1016/j.bmcl.2003.09.045
    • Benjahad A, Guillemont J, Andries K. 3-Iodo-4-phenoxypyridinones (IOPY's), a new family of highly potent non-nucleoside inhibitors of HIV-1 reverse transcriptase. Bioorg Med Chem Lett 2003;13:4309-12 (Pubitemid 37490809)
    • (2003) Bioorganic and Medicinal Chemistry Letters , vol.13 , Issue.24 , pp. 4309-4312
    • Benjahad, A.1    Guillemont, J.2    Andries, K.3    Nguyen, C.H.4    Grierson, D.S.5
  • 55
    • 0037032835 scopus 로고    scopus 로고
    • The protein kinase complement of the human genome
    • DOI 10.1126/science.1075762
    • Manning G, Whyte DB, Martinez R, et al. The protein kinase complement of the human genome. Science 2002;298:1912-34 (Pubitemid 35425239)
    • (2002) Science , vol.298 , Issue.5600 , pp. 1912-1934
    • Manning, G.1    Whyte, D.B.2    Martinez, R.3    Hunter, T.4    Sudarsanam, S.5
  • 56
    • 0036527429 scopus 로고    scopus 로고
    • Protein kinases-The major drug targets of the twenty-first century
    • Cohen P. Protein kinases-The major drug targets of the twenty-first century? Nat Rev Drug Discov 2001;1:309-15
    • (2001) Nat. Rev. Drug Discov. , vol.1 , pp. 309-315
    • Cohen, P.1
  • 57
    • 33748942862 scopus 로고    scopus 로고
    • The isoform-specific functions of the c-Jun N-terminal kinases (JNKs): Differences revealed by gene targeting
    • DOI 10.1002/bies.20458
    • Bogoyevitch MA. The isoform-specific functions of the c-Jun N-Terminal Kinases (JNKs): Differences revealed by gene targeting. Bioessays 2006;28:923-34 (Pubitemid 44433755)
    • (2006) BioEssays , vol.28 , Issue.9 , pp. 923-934
    • Bogoyevitch, M.A.1
  • 58
    • 0036710767 scopus 로고    scopus 로고
    • Pharmacological inhibitors of cyclin-dependent kinases
    • DOI 10.1016/S0165-6147(02)02071-0, PII S0165614702020710
    • Knockaert M, Greengard P, Meijer L. Pharmacological inhibitors of cyclin-dependent kinases. Trends Pharmacol Sci 2002;23:417-25 (Pubitemid 35247771)
    • (2002) Trends in Pharmacological Sciences , vol.23 , Issue.9 , pp. 417-425
    • Knockaert, M.1    Greengard, P.2    Meijer, L.3
  • 59
    • 27744504303 scopus 로고    scopus 로고
    • Inspecting the structure-activity relationship of protein kinase CK2 inhibitors derived from tetrabromo-benzimidazole
    • DOI 10.1016/j.chembiol.2005.08.015, PII S1074552105002711
    • Battistutta R, Mazzorana M, Sarno S, et al. Inspecting the structure-Activity relationship of protein kinase CK2 inhibitors derived from tetrabromo-benzimidazole. Chem Biol 2005;12:1211-19 (Pubitemid 41628256)
    • (2005) Chemistry and Biology , vol.12 , Issue.11 , pp. 1211-1219
    • Battistutta, R.1    Mazzorana, M.2    Sarno, S.3    Kazimierczuk, Z.4    Zanotti, G.5    Pinna, L.A.6
  • 60
    • 70349321218 scopus 로고    scopus 로고
    • Structural bases of protein kinase CK2 inhibitor
    • Battistutta R. Structural bases of protein kinase CK2 inhibitor. Cell Mol Life Sci 2009;66:1868-89
    • (2009) Cell Mol. Life Sci. , vol.66 , pp. 1868-1889
    • Battistutta, R.1
  • 61
    • 77956968392 scopus 로고    scopus 로고
    • Halogen bonds from the basis for selective P-TEFb inhibitor by DRB
    • Baumli S, Endicott JA, Johnson LN. Halogen bonds from the basis for selective P-TEFb inhibitor by DRB. Chem Biol 2010;17:931-6
    • (2010) Chem. Biol. , vol.17 , pp. 931-936
    • Baumli, S.1    Endicott, J.A.2    Johnson, L.N.3
  • 62
    • 79251579303 scopus 로고    scopus 로고
    • Specific CLK inhibitors from a novel chemotype for regulation of alternative splicing
    • Fedorov O, Huber K, Eisenreich A, et al. Specific CLK inhibitors from a novel chemotype for regulation of alternative splicing. Chem Biol 2011;18:67-76
    • (2011) Chem. Biol. , vol.18 , pp. 67-76
    • Fedorov, O.1    Huber, K.2    Eisenreich, A.3
  • 63
    • 79251562528 scopus 로고    scopus 로고
    • Kinase inhibitor that hinges on halogen bonds
    • Grant SK, Lunney EA. Kinase inhibitor that hinges on halogen bonds. Chem Biol 2011;18:3-4
    • (2011) Chem. Biol. , vol.18 , pp. 3-4
    • Grant, S.K.1    Lunney, E.A.2
  • 64
  • 65
    • 72949118944 scopus 로고    scopus 로고
    • Role of halogen bonds in thyroid hormone receptor selectivity: Pharmacophore-based 3D-QSSR studies
    • Valadares NF, Salum LB, Polikarpov I, et al. Role of halogen bonds in thyroid hormone receptor selectivity: Pharmacophore-based 3D-QSSR studies. J Chem Inf Model 2009;49:2606-16
    • (2009) J. Chem. Inf. Model. , vol.49 , pp. 2606-2616
    • Valadares, N.F.1    Salum, L.B.2    Polikarpov, I.3
  • 66
    • 0026567907 scopus 로고
    • Response of a protein structure to cavity-creating mutations and its relation to the hydrophobic effect
    • Eriksson AE, Baase WA, Zhang XJ, et al. Response of a protein structure to cavity-creating mutations and its relation to the hydrophobic effect. Science 1992;255:178-83
    • (1992) Science , vol.255 , pp. 178-183
    • Eriksson, A.E.1    Baase, W.A.2    Zhang, X.J.3
  • 67
    • 0026509036 scopus 로고
    • A cavity-containing mutant of T4 lysozyme is stabilized by buried benzene
    • Eriksson AE, Baase WA, Wozniak JA, et al. A cavity-containing mutant of T4 lysozyme is stabilized by buried benzene. Nature 1992;355:371-3
    • (1992) Nature , vol.355 , pp. 371-373
    • Eriksson, A.E.1    Baase, W.A.2    Wozniak, J.A.3
  • 68
    • 58149091254 scopus 로고    scopus 로고
    • Halogenated benzenes bound within a non-polar cavity in T4 lysozyme provide examples of i S and i Se halogen-bonding
    • Liu L, Basse WA, Matthews BW. Halogenated benzenes bound within a non-polar cavity in T4 lysozyme provide examples of I S and I Se halogen-bonding. J Mol Biol 2009;385:595-605
    • (2009) J. Mol. Biol. , vol.385 , pp. 595-605
    • Liu, L.1    Basse, W.A.2    Matthews, B.W.3
  • 70
    • 18344364519 scopus 로고    scopus 로고
    • Structural requirements for factor Xa inhibition by 3-oxybenzamides with neutral P1 substituents: Combining X-ray crystallography, 3D-QSAR, and tailored scoring functions
    • DOI 10.1021/jm049187l
    • Matter H, Will DW, Nazare M, et al. Structural requirements for factor Xa inhibitor by 3-Oxybenzamides with neutral P1 substituents: Combining X-ray Crystallography, 3D-QSAR, and tailored scoring functions. J Med Chem 2005;48:3290-312 (Pubitemid 40637203)
    • (2005) Journal of Medicinal Chemistry , vol.48 , Issue.9 , pp. 3290-3312
    • Matter, H.1    Will, D.W.2    Nazare, M.3    Schreuder, H.4    Laux, V.5    Wehner, V.6
  • 71
    • 57349194524 scopus 로고    scopus 로고
    • Design, structural-Activity relationship, X-ray crystal structure, and energetic contributions of a critical P1 phamacophore: 3-chloroindole-7-ylbased factor Xa inhibitors
    • Shi Y, Sitkoff D, Zhang J, et al. Design, structural-Activity relationship, X-ray crystal structure, and energetic contributions of a critical P1 phamacophore: 3-chloroindole-7-ylbased factor Xa inhibitors. J Med Chem 2008;51:7541-51
    • (2008) J. Med. Chem. , vol.51 , pp. 7541-7551
    • Shi, Y.1    Sitkoff, D.2    Zhang, J.3
  • 72
    • 70349786321 scopus 로고    scopus 로고
    • Evidence for C-Cl/C-Br pi interactions as an important contribution to protein-ligand binding affinity
    • Matter H, Nazare M, Gussregen S, et al. Evidence for C-Cl/C-Br pi interactions as an important contribution to protein-ligand binding affinity. Angew Chem Int Ed 2009;48:2911-16
    • (2009) Angew Chem. Int. Ed , vol.48 , pp. 2911-2916
    • Matter, H.1    Nazare, M.2    Gussregen, S.3
  • 73
    • 78650706711 scopus 로고    scopus 로고
    • Systematic investigation of halogen bonding in protein-ligand interactions
    • Hardegger LA, Kuhn B, Spinnler B, et al. Systematic investigation of halogen bonding in protein-ligand interactions. Angew Chem Int Ed 2011;50:314-18
    • (2011) Angew Chem. Int. Ed. , vol.50 , pp. 314-318
    • Hardegger, L.A.1    Kuhn, B.2    Spinnler, B.3
  • 74
    • 80055006729 scopus 로고    scopus 로고
    • Halogen bonding at the active sites of human cathepsin L and MEK1 kinase: Efficient interactions in different environments
    • Hardegger LA, Kuhn B, Spinnler B, et al. Halogen bonding at the active sites of human cathepsin L and MEK1 kinase: Efficient interactions in different environments. ChemMedChem 2011;6:2048-54
    • (2011) Chem. Med. Chem. , vol.6 , pp. 2048-2054
    • Hardegger, L.A.1    Kuhn, B.2    Spinnler, B.3
  • 75
    • 79961216539 scopus 로고    scopus 로고
    • Utilization of halogen bond in lead optimization: A case study of rational design of potent phosphodiesterase type 5 (PDE 5) inhibitors
    • Xu Z, Liu Z, Chen T, et al. Utilization of halogen bond in lead optimization: A case study of rational design of potent phosphodiesterase type 5 (PDE 5) inhibitors. J Med Chem 2011;54:5607-11
    • (2011) J. Med. Chem. , vol.54 , pp. 5607-5611
    • Xu, Z.1    Liu, Z.2    Chen, T.3
  • 76
    • 65649131517 scopus 로고    scopus 로고
    • Evaluating the potential for halogen bonding in the oxyanion hole of ketosteroid isomerase using unnatural amino acid mutagenesis
    • Kraut DA, Churchill MJ, Dawson PE, et al. Evaluating the potential for halogen bonding in the oxyanion hole of ketosteroid isomerase using unnatural amino acid mutagenesis. ACS Chem Biol 2009;4:269-73
    • (2009) ACS Chem. Biol. , vol.4 , pp. 269-273
    • Kraut, D.A.1    Churchill, M.J.2    Dawson, P.E.3


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.