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Volumn 59, Issue 5, 2016, Pages 1655-1670

Computational Tools to Model Halogen Bonds in Medicinal Chemistry

Author keywords

[No Author keywords available]

Indexed keywords

HALOGEN;

EID: 84960866293     PISSN: 00222623     EISSN: 15204804     Source Type: Journal    
DOI: 10.1021/acs.jmedchem.5b00997     Document Type: Article
Times cited : (123)

References (116)
  • 1
  • 2
    • 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 (18) 4543-4551 10.1039/b926326h
    • (2010) Phys. Chem. Chem. Phys. , vol.12 , Issue.18 , pp. 4543-4551
    • Lu, Y.1    Wang, Y.2    Zhu, W.3
  • 3
    • 84893415560 scopus 로고    scopus 로고
    • Halogen Bond: Its Role beyond Drug-Target Binding Affinity for Drug Discovery and Development
    • Xu, Z.; Yang, Z.; Liu, Y.; Lu, Y.; Chen, K.; Zhu, W. Halogen Bond: Its Role beyond Drug-Target Binding Affinity for Drug Discovery and Development J. Chem. Inf. Model. 2014, 54, 69-78 10.1021/ci400539q
    • (2014) J. Chem. Inf. Model. , vol.54 , pp. 69-78
    • Xu, Z.1    Yang, Z.2    Liu, Y.3    Lu, Y.4    Chen, K.5    Zhu, W.6
  • 5
  • 6
    • 84906542695 scopus 로고    scopus 로고
    • The Enhancing Effects of Group V Sigma-Hole Interactions on the F-O Halogen Bond
    • Li, W.; Zeng, Y.; Zhang, X.; Zheng, S.; Meng, L. The Enhancing Effects of Group V Sigma-Hole Interactions on the F-O Halogen Bond Phys. Chem. Chem. Phys. 2014, 16 (1) 19282-19289 10.1039/C4CP02430C
    • (2014) Phys. Chem. Chem. Phys. , vol.16 , Issue.1 , pp. 19282-19289
    • Li, W.1    Zeng, Y.2    Zhang, X.3    Zheng, S.4    Meng, L.5
  • 8
    • 0000148479 scopus 로고
    • Structural Aspects of Interatomic Charge-Transfer Bonding
    • Hassel, O. Structural Aspects of Interatomic Charge-Transfer Bonding Science (Washington, DC, U. S.) 1970, 170 (3957) 497-502 10.1126/science.170.3957.497
    • (1970) Science (Washington, DC, U. S.) , vol.170 , Issue.3957 , pp. 497-502
    • Hassel, O.1
  • 9
    • 0000199579 scopus 로고
    • Overlap Integrals and Chemical Binding
    • Mulliken, R. S. Overlap Integrals and Chemical Binding J. Am. Chem. Soc. 1950, 72 (10) 4493-4503 10.1021/ja01166a045
    • (1950) J. Am. Chem. Soc. , vol.72 , Issue.10 , pp. 4493-4503
    • Mulliken, R.S.1
  • 10
    • 0001172670 scopus 로고
    • Molecular Compounds and Their Spectra. XXI. Some General Considerations
    • Mulliken, R. S.; Person, W. B. Molecular Compounds and Their Spectra. XXI. Some General Considerations J. Am. Chem. Soc. 1969, 91 (13) 3409-3413 10.1021/ja01041a001
    • (1969) J. Am. Chem. Soc. , vol.91 , Issue.13 , pp. 3409-3413
    • Mulliken, R.S.1    Person, W.B.2
  • 11
    • 33746190548 scopus 로고
    • A Spectrophotometric Investigation of the Interaction of Iodine with Aromatic Hydrocarbons
    • Benesi, H. a; Hildebrand, J. H. A Spectrophotometric Investigation of the Interaction of Iodine with Aromatic Hydrocarbons J. Am. Chem. Soc. 1949, 71 (8) 2703-2707 10.1021/ja01176a030
    • (1949) J. Am. Chem. Soc. , vol.71 , Issue.8 , pp. 2703-2707
    • Benesi, H.A.1    Hildebrand, J.H.2
  • 12
    • 33746451365 scopus 로고    scopus 로고
    • Charge-Transfer Character of Halogen Bonding: Molecular Structures and Electronic Spectroscopy of Carbon Tetrabromide and Bromoform Complexes with Organic Σ- And Π-Donors
    • Rosokha, S.; Neretin, I.; Rosokha, T.; Hecht, J.; Kochi, J. Charge-Transfer Character of Halogen Bonding: Molecular Structures and Electronic Spectroscopy of Carbon Tetrabromide and Bromoform Complexes with Organic Σ- and Π-Donors Heteroat. Chem. 2006, 17 (5) 449-459 10.1002/hc.20264
    • (2006) Heteroat. Chem. , vol.17 , Issue.5 , pp. 449-459
    • Rosokha, S.1    Neretin, I.2    Rosokha, T.3    Hecht, J.4    Kochi, J.5
  • 13
    • 67349235534 scopus 로고    scopus 로고
    • Expansion of the Sigma-Hole Concept
    • Murray, J. S.; Lane, P.; Politzer, P. Expansion of the Sigma-Hole Concept J. Mol. Model. 2009, 15, 723-729 10.1007/s00894-008-0386-9
    • (2009) J. Mol. Model. , vol.15 , pp. 723-729
    • Murray, J.S.1    Lane, P.2    Politzer, P.3
  • 14
    • 84856764814 scopus 로고    scopus 로고
    • Further Studies of Fluoride Ion Entrapment in Octasilsesquioxane Cages; X-Ray Crystal Structure Studies and Factors That Affect Their Formation
    • Taylor, P. G.; Bassindale, A. R.; El Aziz, Y.; Pourny, M.; Hursthouse, M. B.; Coles, S. J. Further Studies of Fluoride Ion Entrapment in Octasilsesquioxane Cages; X-Ray Crystal Structure Studies and Factors That Affect Their Formation Dalt. Trans. 2012, 41 (7) 2048-2059 10.1039/C1DT11340B
    • (2012) Dalt. Trans. , vol.41 , Issue.7 , pp. 2048-2059
    • Taylor, P.G.1    Bassindale, A.R.2    El Aziz, Y.3    Pourny, M.4    Hursthouse, M.B.5    Coles, S.J.6
  • 15
    • 84887519675 scopus 로고    scopus 로고
    • Tetrel-Bonding Interaction: Rediscovered Supramolecular Force?
    • Bauzá, A.; Mooibroek, T. J.; Frontera, A. Tetrel-Bonding Interaction: Rediscovered Supramolecular Force? Angew. Chem., Int. Ed. 2013, 52 (47) 12317-12321 10.1002/anie.201306501
    • (2013) Angew. Chem., Int. Ed. , vol.52 , Issue.47 , pp. 12317-12321
    • Bauzá, A.1    Mooibroek, T.J.2    Frontera, A.3
  • 17
    • 34547957478 scopus 로고    scopus 로고
    • A Predicted New Type of Directional Noncovalent Interaction
    • Murray, J. S.; Lane, P.; Politzer, P. A Predicted New Type of Directional Noncovalent Interaction Int. J. Quantum Chem. 2007, 107 (12) 2286-2292 10.1002/qua.21352
    • (2007) Int. J. Quantum Chem. , vol.107 , Issue.12 , pp. 2286-2292
    • Murray, J.S.1    Lane, P.2    Politzer, P.3
  • 19
    • 84890035472 scopus 로고    scopus 로고
    • Pnicogen Bonds: A Theoretical Study Based on the Laplacian of Electron Density
    • Eskandari, K.; Mahmoodabadi, N. Pnicogen Bonds: A Theoretical Study Based on the Laplacian of Electron Density J. Phys. Chem. A 2013, 117 (48) 13018-13024 10.1021/jp4098974
    • (2013) J. Phys. Chem. A , vol.117 , Issue.48 , pp. 13018-13024
    • Eskandari, K.1    Mahmoodabadi, N.2
  • 20
    • 77953293767 scopus 로고    scopus 로고
    • Halogen Bonding: A Lump-Hole Interaction
    • Eskandari, K.; Zariny, H. Halogen Bonding: A Lump-Hole Interaction Chem. Phys. Lett. 2010, 492 (1) 9-13 10.1016/j.cplett.2010.04.021
    • (2010) Chem. Phys. Lett. , vol.492 , Issue.1 , pp. 9-13
    • Eskandari, K.1    Zariny, H.2
  • 21
    • 70349782332 scopus 로고    scopus 로고
    • The Nature of Halogen-Halogen Interactions: A Model Derived from Experimental Charge-Density Analysis
    • Bui, T. T. T.; Dahaoui, S.; Lecomte, C.; Desiraju, G. R.; Espinosa, E. The Nature of Halogen-Halogen Interactions: A Model Derived from Experimental Charge-Density Analysis Angew. Chem., Int. Ed. 2009, 48 (21) 3838-3841 10.1002/anie.200805739
    • (2009) Angew. Chem., Int. Ed. , vol.48 , Issue.21 , pp. 3838-3841
    • Bui, T.T.T.1    Dahaoui, S.2    Lecomte, C.3    Desiraju, G.R.4    Espinosa, E.5
  • 22
    • 0041806640 scopus 로고    scopus 로고
    • Electrostatic Complementarity in an Aldose Reductase Complex from Ultra-High-Resolution Crystallography and First-Principles Calculations
    • Muzet, N.; Guillot, B.; Jelsch, C.; Howard, E.; Lecomte, C. Electrostatic Complementarity in an Aldose Reductase Complex from Ultra-High-Resolution Crystallography and First-Principles Calculations Proc. Natl. Acad. Sci. U. S. A. 2003, 100 (15) 8742-8747 10.1073/pnas.1432955100
    • (2003) Proc. Natl. Acad. Sci. U. S. A. , vol.100 , Issue.15 , pp. 8742-8747
    • Muzet, N.1    Guillot, B.2    Jelsch, C.3    Howard, E.4    Lecomte, C.5
  • 23
    • 84874046410 scopus 로고    scopus 로고
    • Halogen Bonding (X-Bonding): A Biological Perspective
    • Scholfield, M. R.; Zanden, C. M. V.; Carter, M.; Ho, P. S. Halogen Bonding (X-Bonding): A Biological Perspective Protein Sci. 2013, 22 (2) 139-152 10.1002/pro.2201
    • (2013) Protein Sci. , vol.22 , Issue.2 , pp. 139-152
    • Scholfield, M.R.1    Zanden, C.M.V.2    Carter, M.3    Ho, P.S.4
  • 24
    • 33846025811 scopus 로고    scopus 로고
    • Single-Electron Halogen Bond: Ab Initio Study
    • Wang, Y.-H.; Zou, J.; Lu, Y.; Yu, Q.; Xu, H.-Y. Single-Electron Halogen Bond: Ab Initio Study Int. J. Quantum Chem. 2007, 107 (2) 501-506 10.1002/qua.21097
    • (2007) Int. J. Quantum Chem. , vol.107 , Issue.2 , pp. 501-506
    • Wang, Y.-H.1    Zou, J.2    Lu, Y.3    Yu, Q.4    Xu, H.-Y.5
  • 25
    • 67849128457 scopus 로고    scopus 로고
    • Halogen Bonds as Orthogonal Molecular Interactions to Hydrogen Bonds
    • Voth, A. R.; Khuu, P.; Oishi, K.; Ho, P. S. Halogen Bonds as Orthogonal Molecular Interactions to Hydrogen Bonds Nat. Chem. 2009, 1 (1) 74-79 10.1038/nchem.112
    • (2009) Nat. Chem. , vol.1 , Issue.1 , pp. 74-79
    • Voth, A.R.1    Khuu, P.2    Oishi, K.3    Ho, P.S.4
  • 26
    • 77954743940 scopus 로고    scopus 로고
    • Unexpected "amphoteric" Character of the Halogen Bond: The Charge Density Study of the Co-Crystal of N-Methylpyrazine Iodide with I2
    • Nelyubina, Y. V.; Antipin, M. Y.; Dunin, D. S.; Kotov, V. Y.; Lyssenko, K. a. Unexpected "Amphoteric" Character of the Halogen Bond: The Charge Density Study of the Co-Crystal of N-Methylpyrazine Iodide with I2 Chem. Commun. 2010, 46 (29) 5325-5327 10.1039/c0cc01094d
    • (2010) Chem. Commun. , vol.46 , Issue.29 , pp. 5325-5327
    • Nelyubina, Y.V.1    Antipin, M.Y.2    Dunin, D.S.3    Kotov, V.Y.4    Lyssenko, K.A.5
  • 27
    • 74449088877 scopus 로고    scopus 로고
    • Halogen-Water-Hydrogen Bridges in Biomolecules
    • Zhou, P.; Lv, J.; Zou, J.; Tian, F.; Shang, Z. Halogen-Water-Hydrogen Bridges in Biomolecules J. Struct. Biol. 2010, 169 (2) 172-182 10.1016/j.jsb.2009.10.006
    • (2010) J. Struct. Biol. , vol.169 , Issue.2 , pp. 172-182
    • Zhou, P.1    Lv, J.2    Zou, J.3    Tian, F.4    Shang, Z.5
  • 29
    • 55949118406 scopus 로고    scopus 로고
    • Competition of Hydrogen Bonds and Halogen Bonds in Complexes of Hypohalous Acids with Nitrogenated Bases
    • Alkorta, I.; Blanco, F.; Solimannejad, M.; Elguero, J. Competition of Hydrogen Bonds and Halogen Bonds in Complexes of Hypohalous Acids with Nitrogenated Bases J. Phys. Chem. A 2008, 112 (43) 10856-10863 10.1021/jp806101t
    • (2008) J. Phys. Chem. A , vol.112 , Issue.43 , pp. 10856-10863
    • Alkorta, I.1    Blanco, F.2    Solimannejad, M.3    Elguero, J.4
  • 30
    • 77953860607 scopus 로고    scopus 로고
    • Competition between Hydrogen Bond and Halogen Bond in Complexes of Formaldehyde with Hypohalous Acids
    • Li, Q.; Xu, X.; Liu, T.; Jing, B.; Li, W.; Cheng, J.; Gong, B.; Sun, J. Competition between Hydrogen Bond and Halogen Bond in Complexes of Formaldehyde with Hypohalous Acids Phys. Chem. Chem. Phys. 2010, 12 (25) 6837-6843 10.1039/b926355a
    • (2010) Phys. Chem. Chem. Phys. , vol.12 , Issue.25 , pp. 6837-6843
    • Li, Q.1    Xu, X.2    Liu, T.3    Jing, B.4    Li, W.5    Cheng, J.6    Gong, B.7    Sun, J.8
  • 31
    • 36148936708 scopus 로고    scopus 로고
    • Structural Competition between Hydrogen Bonds and Halogen Bonds
    • Aakeröy, C. B.; Fasulo, M.; Schultheiss, N.; Desper, J.; Moore, C. Structural Competition between Hydrogen Bonds and Halogen Bonds J. Am. Chem. Soc. 2007, 129 (45) 13772-13773 10.1021/ja073201c
    • (2007) J. Am. Chem. Soc. , vol.129 , Issue.45 , pp. 13772-13773
    • Aakeröy, C.B.1    Fasulo, M.2    Schultheiss, N.3    Desper, J.4    Moore, C.5
  • 32
    • 84901322273 scopus 로고    scopus 로고
    • Halogen- and Hydrogen-Bonded Salts and Co-Crystals Formed from 4-Halo-2,3,5,6-Tetrafluorophenol and Cyclic Secondary and Tertiary Amines: Orthogonal and Non-Orthogonal Halogen and Hydrogen Bonding, and Synthetic Analogues of Halogen-Bonded Biological Syst
    • Takemura, A.; McAllister, L. J.; Hart, S.; Pridmore, N. E.; Karadakov, P. B.; Whitwood, A. C.; Bruce, D. W. Halogen- and Hydrogen-Bonded Salts and Co-Crystals Formed from 4-Halo-2,3,5,6-Tetrafluorophenol and Cyclic Secondary and Tertiary Amines: Orthogonal and Non-Orthogonal Halogen and Hydrogen Bonding, and Synthetic Analogues of Halogen-Bonded Biological Syst Chem.-Eur. J. 2014, 20 (22) 6721-6732 10.1002/chem.201402128
    • (2014) Chem. - Eur. J. , vol.20 , Issue.22 , pp. 6721-6732
    • Takemura, A.1    McAllister, L.J.2    Hart, S.3    Pridmore, N.E.4    Karadakov, P.B.5    Whitwood, A.C.6    Bruce, D.W.7
  • 33
    • 84906085823 scopus 로고    scopus 로고
    • Orthogonal Halogen and Hydrogen Bonds Involving a Peptide Bond Model
    • Vasylyeva, V.; Nayak, S. K.; Terraneo, G.; Cavallo, G.; Metrangolo, P.; Resnati, G. Orthogonal Halogen and Hydrogen Bonds Involving a Peptide Bond Model CrystEngComm 2014, 16 (35) 8102-8105 10.1039/C4CE01514B
    • (2014) CrystEngComm , vol.16 , Issue.35 , pp. 8102-8105
    • Vasylyeva, V.1    Nayak, S.K.2    Terraneo, G.3    Cavallo, G.4    Metrangolo, P.5    Resnati, G.6
  • 34
    • 84896744306 scopus 로고    scopus 로고
    • Halogen Interactions in Biomolecular Crystal Structures
    • Vallejos, M.; Auffinger, P.; Ho, P. S. Halogen Interactions in Biomolecular Crystal Structures Int. Tables Crystallogr. 2012, F (2) 821-826 10.1107/97809553602060000895
    • (2012) Int. Tables Crystallogr. , vol.F , Issue.2 , pp. 821-826
    • Vallejos, M.1    Auffinger, P.2    Ho, P.S.3
  • 35
    • 0030567353 scopus 로고    scopus 로고
    • The Nature and Geometry of Intermolecular Interactions between Halogens and Oxygen or Nitrogen
    • Lommerse, J. P. M.; Stone, A. J.; Taylor, R.; Allen, F. H. The Nature and Geometry of Intermolecular Interactions between Halogens and Oxygen or Nitrogen J. Am. Chem. Soc. 1996, 118 (13) 3108-3116 10.1021/ja953281x
    • (1996) J. Am. Chem. Soc. , vol.118 , Issue.13 , pp. 3108-3116
    • Lommerse, J.P.M.1    Stone, A.J.2    Taylor, R.3    Allen, F.H.4
  • 36
    • 82955171705 scopus 로고    scopus 로고
    • Assaying the Energies of Biological Halogen Bonds
    • Carter, M.; Ho, P. S. Assaying the Energies of Biological Halogen Bonds Cryst. Growth Des. 2011, 11 (11) 5087-5095 10.1021/cg200991v
    • (2011) Cryst. Growth Des. , vol.11 , Issue.11 , pp. 5087-5095
    • Carter, M.1    Ho, P.S.2
  • 37
    • 84863710158 scopus 로고    scopus 로고
    • Scalable Anisotropic Shape and Electrostatic Models for Biological Bromine Halogen Bonds
    • Carter, M.; Rappe, A. K.; Ho, P. S. Scalable Anisotropic Shape and Electrostatic Models for Biological Bromine Halogen Bonds J. Chem. Theory Comput. 2012, 8, 2461-2473 10.1021/ct3001969
    • (2012) J. Chem. Theory Comput. , vol.8 , pp. 2461-2473
    • Carter, M.1    Rappe, A.K.2    Ho, P.S.3
  • 41
    • 0029066380 scopus 로고
    • Structure-Activity Relationship for the Binding of Nucleoside Ligands to Adenosine Kinase from Toxoplasma Gondii
    • Iltzsch, M.; Uber, S. S.; Tankersley, K.; Kouni, M. H. Structure-Activity Relationship for the Binding of Nucleoside Ligands to Adenosine Kinase from Toxoplasma Gondii Biochem. Pharmacol. 1995, 49 (10) 1501-1512 10.1016/0006-2952(95)00029-Y
    • (1995) Biochem. Pharmacol. , vol.49 , Issue.10 , pp. 1501-1512
    • Iltzsch, M.1    Uber, S.S.2    Tankersley, K.3    Kouni, M.H.4
  • 42
    • 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
    • Benjahad, A.; Guillemont, J.; Andries, K.; Nguyen, C. H.; Grierson, D. S. 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 (24) 4309-4312 10.1016/j.bmcl.2003.09.045
    • (2003) Bioorg. Med. Chem. Lett. , vol.13 , Issue.24 , pp. 4309-4312
    • Benjahad, A.1    Guillemont, J.2    Andries, K.3    Nguyen, C.H.4    Grierson, D.S.5
  • 46
    • 84949018565 scopus 로고    scopus 로고
    • Halogen Bonding I: Impact on Materials Chemistry and Life Sciences
    • In; Metrangolo, P. Resnati, G. Springer International Publishing: Switzerland
    • Ho, P. S. Halogen Bonding I: Impact on Materials Chemistry and Life Sciences. In Topics in current chemistry; Metrangolo, P.; Resnati, G., Eds.; Springer International Publishing: Switzerland, 2014; pp 241-276.
    • (2014) Topics in Current Chemistry , pp. 241-276
    • Ho, P.S.1
  • 48
    • 0034597646 scopus 로고    scopus 로고
    • Sildenafil in Primary Pulmonary Hypertension
    • Prasad, S.; Wilkinson, J.; Gatzoulis, M. A. Sildenafil in Primary Pulmonary Hypertension N. Engl. J. Med. 2000, 343, 1342 10.1056/NEJM200011023431814
    • (2000) N. Engl. J. Med. , vol.343 , pp. 1342
    • Prasad, S.1    Wilkinson, J.2    Gatzoulis, M.A.3
  • 50
    • 33750124980 scopus 로고    scopus 로고
    • Extra Precision Glide: Docking and Scoring Incorporating a Model of Hydrophobic Enclosure for Protein-Ligand Complexes
    • Friesner, R. a.; Murphy, R. B.; Repasky, M. P.; Frye, L. L.; Greenwood, J. R.; Halgren, T. a.; Sanschagrin, P. C.; Mainz, D. T. Extra Precision Glide: Docking and Scoring Incorporating a Model of Hydrophobic Enclosure for Protein-Ligand Complexes J. Med. Chem. 2006, 49 (21) 6177-6196 10.1021/jm051256o
    • (2006) J. Med. Chem. , vol.49 , Issue.21 , pp. 6177-6196
    • Friesner, R.A.1    Murphy, R.B.2    Repasky, M.P.3    Frye, L.L.4    Greenwood, J.R.5    Halgren, T.A.6    Sanschagrin, P.C.7    Mainz, D.T.8
  • 52
    • 24444468650 scopus 로고
    • Ground States of Molecules. 38. the MNDO Method. Approximations and Parameters
    • Dewar, M.; Thiel, W. Ground States of Molecules. 38. The MNDO Method. Approximations and Parameters J. Am. Chem. Soc. 1977, 99, 4899-4907 10.1021/ja00457a004
    • (1977) J. Am. Chem. Soc. , vol.99 , pp. 4899-4907
    • Dewar, M.1    Thiel, W.2
  • 53
    • 0842341771 scopus 로고
    • Development and Use of Quantum Mechanical Molecular Models. 76. AM1: A New General Purpose Quantum Mechanical Molecular Model
    • Dewar, M. J. S.; Zoebisch, E. G.; Healy, E. F.; Stewart, J. J. P. Development and Use of Quantum Mechanical Molecular Models. 76. AM1: A New General Purpose Quantum Mechanical Molecular Model J. Am. Chem. Soc. 1985, 107 (13) 3902-3909 10.1021/ja00299a024
    • (1985) J. Am. Chem. Soc. , vol.107 , Issue.13 , pp. 3902-3909
    • Dewar, M.J.S.1    Zoebisch, E.G.2    Healy, E.F.3    Stewart, J.J.P.4
  • 54
    • 2542462121 scopus 로고    scopus 로고
    • Optimization of Parameters for Semiempirical Methods IV: Extension of MNDO, AM1 and PM3 to More Main Group Elements
    • Stewart, J. J. P. Optimization of Parameters for Semiempirical Methods IV: Extension of MNDO, AM1 and PM3 to More Main Group Elements J. Mol. Model. 2004, 10 (2) 155-164 10.1007/s00894-004-0183-z
    • (2004) J. Mol. Model. , vol.10 , Issue.2 , pp. 155-164
    • Stewart, J.J.P.1
  • 55
    • 35448937584 scopus 로고    scopus 로고
    • Optimization of Parameters for Semiempirical Methods V: Modification of NDDO Approximations and Application to 70 Elements
    • Stewart, J. J. P. Optimization of Parameters for Semiempirical Methods V: Modification of NDDO Approximations and Application to 70 Elements J. Mol. Model. 2007, 13 (12) 1173-1213 10.1007/s00894-007-0233-4
    • (2007) J. Mol. Model. , vol.13 , Issue.12 , pp. 1173-1213
    • Stewart, J.J.P.1
  • 56
    • 67349218843 scopus 로고    scopus 로고
    • Application of the PM6Method to Modeling Proteins
    • Stewart, J. J. P. Application of the PM6Method to Modeling Proteins J. Mol. Model. 2009, 15, 765-805 10.1007/s00894-008-0420-y
    • (2009) J. Mol. Model. , vol.15 , pp. 765-805
    • Stewart, J.J.P.1
  • 57
    • 77955003137 scopus 로고    scopus 로고
    • Hobza. Stabilization and Structure Calculations for Noncovalent Interactions in Extended Molecular Systems Based on Wave Function and Density Functional Theories
    • Riley, K. E.; Pitonak, M.; Jurecka, P. Hobza. Stabilization and Structure Calculations for Noncovalent Interactions in Extended Molecular Systems Based on Wave Function and Density Functional Theories Chem. Rev. 2010, 110, 5023-5063 10.1021/cr1000173
    • (2010) Chem. Rev. , vol.110 , pp. 5023-5063
    • Riley, K.E.1    Pitonak, M.2    Jurecka, P.3
  • 58
    • 67849101722 scopus 로고    scopus 로고
    • Semiempirical Quantum Chemical PM6Method Augmented by Dispersion and H-Bonding Correction Terms Reliably Describes Various Types of Noncovalent Complexes
    • Řezáč, J.; Fanfrlík, J.; Salahub, D.; Hobza, P. Semiempirical Quantum Chemical PM6Method Augmented by Dispersion and H-Bonding Correction Terms Reliably Describes Various Types of Noncovalent Complexes J. Chem. Theory Comput. 2009, 5 (7) 1749-1760 10.1021/ct9000922
    • (2009) J. Chem. Theory Comput. , vol.5 , Issue.7 , pp. 1749-1760
    • Řezáč, J.1    Fanfrlík, J.2    Salahub, D.3    Hobza, P.4
  • 59
    • 33744470857 scopus 로고    scopus 로고
    • Benchmark Database of Accurate (MP2 and CCSD(T) Complete Basis Set Limit) Interaction Energies of Small Model Complexes, DNA Base Pairs, and Amino Acid Pairs
    • Jurecka, P.; Sponer, J.; Cerný, J.; Hobza, P. Benchmark Database of Accurate (MP2 and CCSD(T) Complete Basis Set Limit) Interaction Energies of Small Model Complexes, DNA Base Pairs, and Amino Acid Pairs Phys. Chem. Chem. Phys. 2006, 8 (17) 1985-1993 10.1039/b600027d
    • (2006) Phys. Chem. Chem. Phys. , vol.8 , Issue.17 , pp. 1985-1993
    • Jurecka, P.1    Sponer, J.2    Cerný, J.3    Hobza, P.4
  • 60
    • 79955395664 scopus 로고    scopus 로고
    • Transferable Scoring Function Based on Semiempirical Quantum Mechanical PM6-DH2Method: CDK2 with 15 Structurally Diverse Inhibitors
    • Dobeš, P.; Fanfrlík, J.; Rezáč, J.; Otyepka, M.; Hobza, P. Transferable Scoring Function Based on Semiempirical Quantum Mechanical PM6-DH2Method: CDK2 with 15 Structurally Diverse Inhibitors J. Comput.-Aided Mol. Des. 2011, 25 (3) 223-235 10.1007/s10822-011-9413-5
    • (2011) J. Comput.-Aided Mol. Des. , vol.25 , Issue.3 , pp. 223-235
    • Dobeš, P.1    Fanfrlík, J.2    Rezáč, J.3    Otyepka, M.4    Hobza, P.5
  • 61
    • 84986432941 scopus 로고
    • Automated Docking with Grid-Based Energy Evaluation
    • Meng, E. C.; Shoichet, B. K.; Kuntz, I. D. Automated Docking with Grid-Based Energy Evaluation J. Comput. Chem. 1992, 13 (4) 505-524 10.1002/jcc.540130412
    • (1992) J. Comput. Chem. , vol.13 , Issue.4 , pp. 505-524
    • Meng, E.C.1    Shoichet, B.K.2    Kuntz, I.D.3
  • 62
    • 77957291978 scopus 로고    scopus 로고
    • A Reliable Docking/scoring Scheme Based on the Semiempirical Quantum Mechanical PM6-DH2Method Accurately Covering Dispersion and H-Bonding: HIV-1 Protease with 22 Ligands
    • Fanfrlík, J.; Bronowska, A. K.; Rezác, J.; Prenosil, O.; Konvalinka, J.; Hobza, P. A Reliable Docking/scoring Scheme Based on the Semiempirical Quantum Mechanical PM6-DH2Method Accurately Covering Dispersion and H-Bonding: HIV-1 Protease with 22 Ligands J. Phys. Chem. B 2010, 114 (39) 12666-12678 10.1021/jp1032965
    • (2010) J. Phys. Chem. B , vol.114 , Issue.39 , pp. 12666-12678
    • Fanfrlík, J.1    Bronowska, A.K.2    Rezác, J.3    Prenosil, O.4    Konvalinka, J.5    Hobza, P.6
  • 63
    • 0346993724 scopus 로고    scopus 로고
    • Cell Cycle Inhibitors for the Treatment of Cancer
    • Kong, N.; Fotouhi, N.; Wovkulich, P.; Roberts, J. Cell Cycle Inhibitors for the Treatment of Cancer Drugs Future 2003, 28 (9) 881 10.1358/dof.2003.028.09.761413
    • (2003) Drugs Future , vol.28 , Issue.9 , pp. 881
    • Kong, N.1    Fotouhi, N.2    Wovkulich, P.3    Roberts, J.4
  • 64
    • 79954583073 scopus 로고    scopus 로고
    • A Halogen-Bonding Correction for the Semiempirical PM6 Method
    • Řezáč, J.; Hobza, P. A Halogen-Bonding Correction for the Semiempirical PM6 Method Chem. Phys. Lett. 2011, 506 (4-6) 286-289 10.1016/j.cplett.2011.03.009
    • (2011) Chem. Phys. Lett. , vol.506 , Issue.4-6 , pp. 286-289
    • Řezáč, J.1    Hobza, P.2
  • 65
    • 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 Ez
    • Dobes, P.; Rezac, J.; Fanfrlik, J.; Otyepka, M.; Hobza, P. Semiempirical Quantum Mechanical Method PM6-DH2X Describes the Geometry and Energetics of CK2-Inhibitor Complexes Involving Halogen Bonds Well, While the Empirical Potential Fails Ez J. Phys. Chem. B 2011, 115, 8581-8589 10.1021/jp202149z
    • (2011) J. Phys. Chem. B , vol.115 , pp. 8581-8589
    • Dobes, P.1    Rezac, J.2    Fanfrlik, J.3    Otyepka, M.4    Hobza, P.5
  • 66
    • 34548821001 scopus 로고    scopus 로고
    • The Role of Halogen Bonding in Inhibitor Recognition and Binding by Protein Kinases
    • Voth, A. R.; Ho, P. S. The Role of Halogen Bonding in Inhibitor Recognition and Binding by Protein Kinases Curr. Top. Med. Chem. 2007, 7 (14) 1336-1348 10.2174/156802607781696846
    • (2007) Curr. Top. Med. Chem. , vol.7 , Issue.14 , pp. 1336-1348
    • Voth, A.R.1    Ho, P.S.2
  • 70
    • 27744504303 scopus 로고    scopus 로고
    • Inspecting the Structure-Activity Relationship of Protein Kinase CK2 Inhibitors Derived from Tetrabromo-Benzimidazole
    • Battistutta, R.; Mazzorana, M.; Sarno, S.; Kazimierczuk, Z.; Zanotti, G.; Pinna, L. a. Inspecting the Structure-Activity Relationship of Protein Kinase CK2 Inhibitors Derived from Tetrabromo-Benzimidazole Chem. Biol. 2005, 12 (11) 1211-1219 10.1016/j.chembiol.2005.08.015
    • (2005) Chem. Biol. , 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
  • 72
    • 0034775155 scopus 로고    scopus 로고
    • Structural Features Underlying Selective Inhibition of Protein Kinase CK2 by ATP Site-Directed Tetrabromo-2-Benzotriazole
    • Battistutta, R.; De Moliner, E.; Sarno, S.; Zanotti, G.; Pinna, L. a. Structural Features Underlying Selective Inhibition of Protein Kinase CK2 by ATP Site-Directed Tetrabromo-2-Benzotriazole Protein Sci. 2001, 10 (11) 2200-2206 10.1110/ps.19601
    • (2001) Protein Sci. , vol.10 , Issue.11 , pp. 2200-2206
    • Battistutta, R.1    De Moliner, E.2    Sarno, S.3    Zanotti, G.4    Pinna, L.A.5
  • 73
    • 84858957245 scopus 로고    scopus 로고
    • AMBER Empirical Potential Describes the Geometry and Energy of Noncovalent Halogen Interactions Better than Advanced Semiempirical Quantum Mechanical Method PM6-DH2X
    • Ibrahim, M. A. A. AMBER Empirical Potential Describes the Geometry and Energy of Noncovalent Halogen Interactions Better than Advanced Semiempirical Quantum Mechanical Method PM6-DH2X J. Phys. Chem. B 2012, 116 (11) 3659-3669 10.1021/jp3003905
    • (2012) J. Phys. Chem. B , vol.116 , Issue.11 , pp. 3659-3669
    • Ibrahim, M.A.A.1
  • 74
    • 65649095907 scopus 로고    scopus 로고
    • Halogen Bonding - A Novel Interaction for Rational Drug Design?
    • Lu, Y.; Shi, T.; Wang, Y.; Yang, H.; Yan, X.; Luo, X.; Jiang, H.; Zhu, W. Halogen Bonding - a Novel Interaction for Rational Drug Design? J. Med. Chem. 2009, 52 (9) 2854-2862 10.1021/jm9000133
    • (2009) J. Med. Chem. , vol.52 , Issue.9 , pp. 2854-2862
    • Lu, Y.1    Shi, T.2    Wang, Y.3    Yang, H.4    Yan, X.5    Luo, X.6    Jiang, H.7    Zhu, W.8
  • 75
    • 79959739959 scopus 로고    scopus 로고
    • Molecular Mechanical Study of Halogen Bonding in Drug Discovery
    • Ibrahim, M. A. A. Molecular Mechanical Study of Halogen Bonding in Drug Discovery J. Comput. Chem. 2011, 32 (12) 2564-2574 10.1002/jcc.21836
    • (2011) J. Comput. Chem. , vol.32 , Issue.12 , pp. 2564-2574
    • Ibrahim, M.A.A.1
  • 76
    • 0001253772 scopus 로고    scopus 로고
    • Advancing beyond the Atom-Centered Model in Additive and Nonadditive Molecular Mechanics
    • Dixon, R. W.; Kollman, P. A. Advancing beyond the Atom-Centered Model in Additive and Nonadditive Molecular Mechanics J. Comput. Chem. 1997, 18 (13) 1632-1646 10.1002/(SICI)1096-987X(199710)18:13<1632::AID-JCC5>3.0.CO;2-S
    • (1997) J. Comput. Chem. , vol.18 , Issue.13 , pp. 1632-1646
    • Dixon, R.W.1    Kollman, P.A.2
  • 77
    • 0035974484 scopus 로고    scopus 로고
    • Organic and Biological Systems Going beyond the Atom Centered Two Body Additive Approximation: Aqueous Solution Free Energies of Methanol and Amide Hydrogen Bonding and Chloroform/Water Partition Coefficients of the Nucleic Acid Bases
    • Cieplak, P.; Caldwell, J.; Kollman, P. Organic and Biological Systems Going Beyond the Atom Centered Two Body Additive Approximation: Aqueous Solution Free Energies of Methanol and Amide Hydrogen Bonding and Chloroform/Water Partition Coefficients of the Nucleic Acid Bases J. Comput. Chem. 2001, 22 (10) 1048-1057 10.1002/jcc.1065
    • (2001) J. Comput. Chem. , vol.22 , Issue.10 , pp. 1048-1057
    • Cieplak, P.1    Caldwell, J.2    Kollman, P.3
  • 78
    • 0035312821 scopus 로고    scopus 로고
    • Polarizable Force Fields
    • Halgren, T. A.; Damm, W. Polarizable Force Fields Curr. Opin. Struct. Biol. 2001, 11 (2) 236-242 10.1016/S0959-440X(00)00196-2
    • (2001) Curr. Opin. Struct. Biol. , vol.11 , Issue.2 , pp. 236-242
    • Halgren, T.A.1    Damm, W.2
  • 79
    • 10644250257 scopus 로고
    • Inhomogeneous Electron Gas
    • Hohenberg, P.; Kohn, W. Inhomogeneous Electron Gas Phys. Rev. 1964, 136 (3B) 864-871 10.1103/PhysRev.136.B864
    • (1964) Phys. Rev. , vol.136 , Issue.3 , pp. 864-871
    • Hohenberg, P.1    Kohn, W.2
  • 80
    • 0042113153 scopus 로고
    • Self-Consistent Equations Including Exchange and Correlation Effects
    • Kohn, W.; Sham, L. Self-Consistent Equations Including Exchange and Correlation Effects Phys. Rev. 1965, 140 (4A) 1133-1138 10.1103/PhysRev.140.A1133
    • (1965) Phys. Rev. , vol.140 , Issue.4 , pp. 1133-1138
    • Kohn, W.1    Sham, L.2
  • 81
    • 2942532422 scopus 로고    scopus 로고
    • Development and Testing of a General Amber Force Field
    • Wang, J.; Wolf, R. M.; Caldwell, J. W.; Kollman, P. A.; Case, D. A. Development and Testing of a General Amber Force Field J. Comput. Chem. 2004, 25 (9) 1157-1174 10.1002/jcc.20035
    • (2004) J. Comput. Chem. , vol.25 , Issue.9 , pp. 1157-1174
    • Wang, J.1    Wolf, R.M.2    Caldwell, J.W.3    Kollman, P.A.4    Case, D.A.5
  • 82
    • 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, M. A. A. 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 (10) 2549-2559 10.1021/ci2002582
    • (2011) J. Chem. Inf. Model. , vol.51 , Issue.10 , pp. 2549-2559
    • Ibrahim, M.A.A.1
  • 83
    • 84859583695 scopus 로고    scopus 로고
    • On Extension of the Current Biomolecular Empirical Force Field for the Description of Halogen Bonds
    • Kolar, M.; Hobza, P. On Extension of the Current Biomolecular Empirical Force Field for the Description of Halogen Bonds J. Chem. Theory Comput. 2012, 8, 1325-1333 10.1021/ct2008389
    • (2012) J. Chem. Theory Comput. , vol.8 , pp. 1325-1333
    • Kolar, M.1    Hobza, P.2
  • 84
    • 0029912748 scopus 로고    scopus 로고
    • Development and Testing of the OLPS All-Atom Force Field on Conformational Energetics and Properties of Organic Liquids
    • Jorgensen, W. L.; Maxwell, D. S.; Tirado-Rives, J. Development and Testing of the OLPS All-Atom Force Field on Conformational Energetics and Properties of Organic Liquids J. Am. Chem. Soc. 1996, 118 (15) 11225-11236 10.1021/ja9621760
    • (1996) J. Am. Chem. Soc. , vol.118 , Issue.15 , pp. 11225-11236
    • Jorgensen, W.L.1    Maxwell, D.S.2    Tirado-Rives, J.3
  • 85
    • 33645941402 scopus 로고
    • The OPLS Potential Functions for Proteins. Energy Minimizations for Crystals of Cyclic Peptides and Crambin
    • Jorgensen, W.; Tirado-Rives, J. The OPLS Potential Functions for Proteins. Energy Minimizations for Crystals of Cyclic Peptides and Crambin J. Am. Chem. Soc. 1988, 110 (6) 1657-1666 10.1021/ja00214a001
    • (1988) J. Am. Chem. Soc. , vol.110 , Issue.6 , pp. 1657-1666
    • Jorgensen, W.1    Tirado-Rives, J.2
  • 86
    • 18744387415 scopus 로고    scopus 로고
    • Potential Energy Functions for Atomic-Level Simulations of Water and Organic and Biomolecular Systems
    • Jorgensen, W. L.; Tirado-Rives, J. Potential Energy Functions for Atomic-Level Simulations of Water and Organic and Biomolecular Systems Proc. Natl. Acad. Sci. U. S. A. 2005, 102 (19) 6665-6670 10.1073/pnas.0408037102
    • (2005) Proc. Natl. Acad. Sci. U. S. A. , vol.102 , Issue.19 , pp. 6665-6670
    • Jorgensen, W.L.1    Tirado-Rives, J.2
  • 87
    • 84055211792 scopus 로고    scopus 로고
    • Computationally-Guided Optimization of a Docking Hit to Yield Catechol Diethers as Potent Anti-HIV Agents
    • Bollini, M.; Domaoal, R. a; Thakur, V. V.; Gallardo-Macias, R.; Spasov, K. a; Anderson, K. S.; Jorgensen, W. L. Computationally-Guided Optimization of a Docking Hit to Yield Catechol Diethers as Potent Anti-HIV Agents J. Med. Chem. 2011, 54 (24) 8582-8591 10.1021/jm201134m
    • (2011) J. Med. Chem. , vol.54 , Issue.24 , pp. 8582-8591
    • Bollini, M.1    Domaoal, R.A.2    Thakur, V.V.3    Gallardo-Macias, R.4    Spasov, K.A.5    Anderson, K.S.6    Jorgensen, W.L.7
  • 88
    • 84866682261 scopus 로고    scopus 로고
    • Treatment of Halogen Bonding in the OPLS-AA Force Field: Application to Potent Anti-HIV Agents
    • Jorgensen, W. L.; Schyman, P. Treatment of Halogen Bonding in the OPLS-AA Force Field: Application to Potent Anti-HIV Agents J. Chem. Theory Comput. 2012, 8 (10) 3895-3901 10.1021/ct300180w
    • (2012) J. Chem. Theory Comput. , vol.8 , Issue.10 , pp. 3895-3901
    • Jorgensen, W.L.1    Schyman, P.2
  • 89
    • 84880638626 scopus 로고    scopus 로고
    • Enthalpy-Entropy Compensation in Biomolecular Halogen Bonds Measured in DNA Junctions
    • Carter, M.; Voth, A. R.; Scholfield, M. R.; Rummel, B.; Sowers, L. C.; Ho, P. S. Enthalpy-Entropy Compensation in Biomolecular Halogen Bonds Measured in DNA Junctions Biochemistry 2013, 52 (29) 4891-4903 10.1021/bi400590h
    • (2013) Biochemistry , vol.52 , Issue.29 , pp. 4891-4903
    • Carter, M.1    Voth, A.R.2    Scholfield, M.R.3    Rummel, B.4    Sowers, L.C.5    Ho, P.S.6
  • 91
    • 65349103899 scopus 로고    scopus 로고
    • Blinded by the Light: The Growing Complexity of p53
    • Vousden, K. H.; Prives, C. Blinded by the Light: The Growing Complexity of p53 Cell 2009, 137 (3) 413-431 10.1016/j.cell.2009.04.037
    • (2009) Cell , vol.137 , Issue.3 , pp. 413-431
    • Vousden, K.H.1    Prives, C.2
  • 94
    • 0029909384 scopus 로고    scopus 로고
    • An Iterative Method for Extracting Energy-like Quantities from Protein Structures
    • Thomas, P. D.; Dill, K. a. An Iterative Method for Extracting Energy-like Quantities from Protein Structures Proc. Natl. Acad. Sci. U. S. A. 1996, 93, 11628-11633 10.1073/pnas.93.21.11628
    • (1996) Proc. Natl. Acad. Sci. U. S. A. , vol.93 , pp. 11628-11633
    • Thomas, P.D.1    Dill, K.A.2
  • 95
    • 84888224178 scopus 로고    scopus 로고
    • A Knowledge-Based Halogen Bonding Scoring Function for Predicting Protein-Ligand Interactions
    • Liu, Y.; Xu, Z.; Yang, Z.; Chen, K.; Zhu, W. A Knowledge-Based Halogen Bonding Scoring Function for Predicting Protein-Ligand Interactions J. Mol. Model. 2013, 19 (11) 5015-5030 10.1007/s00894-013-2005-7
    • (2013) J. Mol. Model. , vol.19 , Issue.11 , pp. 5015-5030
    • Liu, Y.1    Xu, Z.2    Yang, Z.3    Chen, K.4    Zhu, W.5
  • 98
    • 0034645763 scopus 로고    scopus 로고
    • Knowledge-Based Scoring Function to Predict Protein-Ligand Interactions
    • Gohlke, H.; Hendlich, M.; Klebe, G. Knowledge-Based Scoring Function to Predict Protein-Ligand Interactions J. Mol. Biol. 2000, 295 (2) 337-356 10.1006/jmbi.1999.3371
    • (2000) J. Mol. Biol. , vol.295 , Issue.2 , pp. 337-356
    • Gohlke, H.1    Hendlich, M.2    Klebe, G.3
  • 99
    • 0030255303 scopus 로고    scopus 로고
    • Scoring Noncovalent Protein-Ligand Interactions: A Continuous Differentiable Function Tuned to Compute Binding Affinities
    • Jain, A. Scoring Noncovalent Protein-Ligand Interactions: A Continuous Differentiable Function Tuned to Compute Binding Affinities J. Comput.-Aided Mol. Des. 1996, 10 (5) 427-440 10.1007/BF00124474
    • (1996) J. Comput.-Aided Mol. Des. , vol.10 , Issue.5 , pp. 427-440
    • Jain, A.1
  • 100
    • 77956034718 scopus 로고    scopus 로고
    • Knowledge-Based Scoring Functions in Drug Design. 1. Developing a Target-Specific Method for Kinase-Ligand Interactions
    • Xue, M.; Zheng, M.; Xiong, B.; Li, Y.; Jiang, H.; Shen, J. Knowledge-Based Scoring Functions in Drug Design. 1. Developing a Target-Specific Method for Kinase-Ligand Interactions J. Chem. Inf. Model. 2010, 50 (8) 1378-1386 10.1021/ci100182c
    • (2010) J. Chem. Inf. Model. , vol.50 , Issue.8 , pp. 1378-1386
    • Xue, M.1    Zheng, M.2    Xiong, B.3    Li, Y.4    Jiang, H.5    Shen, J.6
  • 101
    • 33749242403 scopus 로고    scopus 로고
    • PMF Scoring Revisited
    • Muegge, I. PMF Scoring Revisited J. Med. Chem. 2006, 49 (20) 5895-5902 10.1021/jm050038s
    • (2006) J. Med. Chem. , vol.49 , Issue.20 , pp. 5895-5902
    • Muegge, I.1
  • 102
    • 0027185516 scopus 로고
    • Automated Docking in Crystallography: Analysis of the Substrates of Aconitase
    • Goodsell, D. S.; Lauble, H.; Stout, C.; Olson, A. J. Automated Docking in Crystallography: Analysis of the Substrates of Aconitase Proteins: Struct., Funct., Genet. 1993, 17 (1) 1-10 10.1002/prot.340170104
    • (1993) Proteins: Struct., Funct., Genet. , vol.17 , Issue.1 , pp. 1-10
    • Goodsell, D.S.1    Lauble, H.2    Stout, C.3    Olson, A.J.4
  • 103
    • 8844263008 scopus 로고    scopus 로고
    • Docking and Scoring in Virtual Screening for Drug Discovery: Methods and Applications
    • Kitchen, D. B.; Decornez, H.; Furr, J. R.; Bajorath, J. Docking and Scoring in Virtual Screening for Drug Discovery: Methods and Applications Nat. Rev. Drug Discovery 2004, 3 (11) 935-949 10.1038/nrd1549
    • (2004) Nat. Rev. Drug Discovery , vol.3 , Issue.11 , pp. 935-949
    • Kitchen, D.B.1    Decornez, H.2    Furr, J.R.3    Bajorath, J.4
  • 104
    • 84555169381 scopus 로고    scopus 로고
    • Rationalizing Tight Ligand Binding Through Cooperative Interaction Networks
    • Kuhn, B.; Fuchs, J. E.; Reutlinger, M.; Stahl, M.; Taylor, N. R. Rationalizing Tight Ligand Binding Through Cooperative Interaction Networks J. Chem. Inf. Model. 2011, 51, 3180-3198 10.1021/ci200319e
    • (2011) J. Chem. Inf. Model. , vol.51 , pp. 3180-3198
    • Kuhn, B.1    Fuchs, J.E.2    Reutlinger, M.3    Stahl, M.4    Taylor, N.R.5
  • 105
    • 0032482432 scopus 로고    scopus 로고
    • Collective Dynamics of "small-World" Networks
    • Watts, D. J.; Strogatz, S. H. Collective Dynamics of "Small-World" Networks Nature 1998, 393, 440-442 10.1038/30918
    • (1998) Nature , vol.393 , pp. 440-442
    • Watts, D.J.1    Strogatz, S.H.2
  • 106
    • 23744436747 scopus 로고    scopus 로고
    • Crystal Structures of the RNA-Dependent RNA Polymerase Genotype 2a of Hepatitis C Virus Reveal Two Conformations and Suggest Mechanisms of Inhibition by Non-Nucleoside Inhibitors
    • Biswal, B. K.; Cherney, M. M.; Wang, M.; Chan, L.; Yannopoulos, C. G.; Bilimoria, D.; Nicolas, O.; Bedard, J.; James, M. N. G. Crystal Structures of the RNA-Dependent RNA Polymerase Genotype 2a of Hepatitis C Virus Reveal Two Conformations and Suggest Mechanisms of Inhibition by Non-Nucleoside Inhibitors J. Biol. Chem. 2005, 280 (18) 18202-18210 10.1074/jbc.M413410200
    • (2005) J. Biol. Chem. , vol.280 , Issue.18 , pp. 18202-18210
    • Biswal, B.K.1    Cherney, M.M.2    Wang, M.3    Chan, L.4    Yannopoulos, C.G.5    Bilimoria, D.6    Nicolas, O.7    Bedard, J.8    James, M.N.G.9
  • 107
    • 84925434864 scopus 로고    scopus 로고
    • Evaluating the Potential of Halogen Bonding in Molecular Design: Automated Scaffold Decoration Using an XB-Scoring Function
    • Zimmermann, M. O.; Lange, A.; Boeckler, F. M. Evaluating the Potential of Halogen Bonding in Molecular Design: Automated Scaffold Decoration Using an XB-Scoring Function J. Chem. Inf. Model. 2015, 55 (3) 687-699 10.1021/ci5007118
    • (2015) J. Chem. Inf. Model. , vol.55 , Issue.3 , pp. 687-699
    • Zimmermann, M.O.1    Lange, A.2    Boeckler, F.M.3
  • 108
    • 78651027245 scopus 로고
    • Susceptibility of Micro-Organisms to Chloramphenicol
    • McLean, I.; Schwab, J.; Hillegas, A.; Schlingman, A. Susceptibility of Micro-Organisms to Chloramphenicol J. Clin. Invest. 1949, 22, 953-963 10.1172/JCI102185
    • (1949) J. Clin. Invest. , vol.22 , pp. 953-963
    • McLean, I.1    Schwab, J.2    Hillegas, A.3    Schlingman, A.4
  • 109
    • 77956637674 scopus 로고    scopus 로고
    • Flavopiridol: The First Cyclin-Dependent Kinase Inhibitor in Human Clinical Trials
    • Wang, L.; Ren, D. Flavopiridol: The First Cyclin-Dependent Kinase Inhibitor in Human Clinical Trials Mini-Rev. Med. Chem. 2010, 10 (11) 1058-1070 10.2174/1389557511009011058
    • (2010) Mini-Rev. Med. Chem. , vol.10 , Issue.11 , pp. 1058-1070
    • Wang, L.1    Ren, D.2
  • 110
    • 4544240958 scopus 로고    scopus 로고
    • Halogenation of Drugs Enhances Membrane Binding and Permeation
    • Gerebtzoff, G.; Li-Blatter, X.; Fischer, H.; Frentzel, A.; Seelig, A. Halogenation of Drugs Enhances Membrane Binding and Permeation ChemBioChem 2004, 5 (5) 676-684 10.1002/cbic.200400017
    • (2004) ChemBioChem , vol.5 , Issue.5 , pp. 676-684
    • Gerebtzoff, G.1    Li-Blatter, X.2    Fischer, H.3    Frentzel, A.4    Seelig, A.5
  • 114
    • 84874632186 scopus 로고    scopus 로고
    • Principles and Applications of Halogen Bonding in Medicinal Chemistry and Chemical Biology
    • Wilcken, R.; Zimmermann, M. O.; Lange, A.; Joerger, A. C.; Boeckler, F. M. Principles and Applications of Halogen Bonding in Medicinal Chemistry and Chemical Biology J. Med. Chem. 2013, 56 (4) 1363-1388 10.1021/jm3012068
    • (2013) J. Med. Chem. , vol.56 , Issue.4 , pp. 1363-1388
    • Wilcken, R.1    Zimmermann, M.O.2    Lange, A.3    Joerger, A.C.4    Boeckler, F.M.5
  • 115
    • 0035154524 scopus 로고    scopus 로고
    • Structure-Activity Relationships for Aquatic Toxicity to Tetrahymena: Halogen-Substituted Aliphatic Esters
    • DeWeese, A. D.; Schultz, T. W. Structure-Activity Relationships for Aquatic Toxicity to Tetrahymena: Halogen-Substituted Aliphatic Esters Environ. Toxicol. 2001, 16 (1) 54-60 10.1002/1522-7278(2001)16:1<54::AID-TOX60>3.0.CO;2-M
    • (2001) Environ. Toxicol. , vol.16 , Issue.1 , pp. 54-60
    • DeWeese, A.D.1    Schultz, T.W.2
  • 116
    • 52049106111 scopus 로고    scopus 로고
    • Halogenated Ligands and Their Interactions with Amino Acids: Implications for Structure-Activity and Structure-Toxicity Relationships
    • Kortagere, S.; Ekins, S.; Welsh, W. J. Halogenated Ligands and Their Interactions with Amino Acids: Implications for Structure-Activity and Structure-Toxicity Relationships J. Mol. Graphics Modell. 2008, 27 (2) 170-177 10.1016/j.jmgm.2008.04.001
    • (2008) J. Mol. Graphics Modell. , vol.27 , Issue.2 , pp. 170-177
    • Kortagere, S.1    Ekins, S.2    Welsh, W.J.3


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