메뉴 건너뛰기




Volumn 6, Issue 6, 2014, Pages 617-639

Halogen-enriched fragment libraries as chemical probes for harnessing halogen bonding in fragment-based lead discovery

Author keywords

[No Author keywords available]

Indexed keywords

HALOGEN; PROTEIN P53; MOLECULAR LIBRARY; PROTEIN; PROTEIN BINDING;

EID: 84902117987     PISSN: 17568919     EISSN: 17568927     Source Type: Journal    
DOI: 10.4155/fmc.14.20     Document Type: Review
Times cited : (38)

References (169)
  • 1
    • 0004688750 scopus 로고
    • XXVIII. on the iodide of iodammonium
    • Guthrie F. XXVIII. On the iodide of iodammonium. J. Chem. Soc. 16, 239-244 (1863).
    • (1863) J. Chem. Soc. , vol.16 , pp. 239-244
    • Guthrie, F.1
  • 2
    • 0000728179 scopus 로고
    • The structure of bromine 1,4-dioxanate
    • Hassel O, Hvoslef J. The structure of bromine 1,4-dioxanate. Acta Chem. Scand. 8, 873-873 (1954).
    • (1954) Acta Chem. Scand. , vol.8 , pp. 873-873
    • Hassel, O.1    Hvoslef, J.2
  • 3
    • 33746190548 scopus 로고
    • A spectrophotometric investigation of the interaction of iodine with aromatic hydrocarbons
    • Benesi HA, Hildebrand JH. A spectrophotometric investigation of the interaction of iodine with aromatic hydrocarbons. J. Am. Chem. Soc. 71(8), 2703-2707 (1949).
    • (1949) J. Am. Chem. Soc. , vol.71 , Issue.8 , pp. 2703-2707
    • Benesi, H.A.1    Hildebrand, J.H.2
  • 5
    • 0030567353 scopus 로고    scopus 로고
    • The nature and geometry of intermolecular interactions between halogens and oxygen or nitrogen
    • Lommerse JPM, Stone AJ, Taylor R, Allen FH. The nature and geometry of intermolecular interactions between halogens and oxygen or nitrogen. J. Am. Chem. Soc. 118(13), 3108-3116 (1996).
    • (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
  • 6
    • 0000516245 scopus 로고
    • Angular preferences of intermolecular forces around halogen centers: Preferred directions of approach of electrophiles and nucleophiles around carbon-halogen bond
    • Ramasubbu N, Parthasarathy R, Murray-Rust P. Angular preferences of intermolecular forces around halogen centers: Preferred directions of approach of electrophiles and nucleophiles around carbon-halogen bond. J. Am. Chem. Soc. 108(15), 4308-4314 (1986).
    • (1986) J. Am. Chem. Soc. , vol.108 , Issue.15 , pp. 4308-4314
    • Ramasubbu, N.1    Parthasarathy, R.2    Murray-Rust, P.3
  • 8
    • 47149109408 scopus 로고    scopus 로고
    • Investigations into the nature of halogen bonding including symmetry adapted perturbation theory analyses
    • Riley KE, Hobza P. Investigations into the nature of halogen bonding including symmetry adapted perturbation theory analyses. J. Chem. Theory Comput. 4(2), 232-242 (2008).
    • (2008) J. Chem. Theory Comput. , vol.4 , Issue.2 , pp. 232-242
    • Riley, K.E.1    Hobza, P.2
  • 9
    • 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. 12(28), 7748-7757 (2010).
    • (2010) Phys. Chem. Chem. Phys. , vol.12 , Issue.28 , pp. 7748-7757
    • Politzer, P.1    Murray, J.S.2    Clark, T.3
  • 10
    • 84877734097 scopus 로고    scopus 로고
    • Halogen bonding and other sigma-hole interactions: A perspective
    • Politzer P, Murray JS, Clark T. Halogen bonding and other sigma-hole interactions: A perspective. Phys. Chem. Chem. Phys. 15(27), 11178-11189 (2013).
    • (2013) Phys. Chem. Chem. Phys. , vol.15 , Issue.27 , pp. 11178-11189
    • Politzer, P.1    Murray, J.S.2    Clark, T.3
  • 11
    • 20444479110 scopus 로고    scopus 로고
    • Halogen bonding based recognition processes: A world parallel to hydrogen bonding
    • Metrangolo P, Neukirch H, Pilati T, Resnati G. Halogen bonding based recognition processes: A world parallel to hydrogen bonding. Acc. Chem. Res. 38(5), 386-395 (2005).
    • (2005) Acc. Chem. Res. , vol.38 , Issue.5 , pp. 386-395
    • Metrangolo, P.1    Neukirch, H.2    Pilati, T.3    Resnati, G.4
  • 13
    • 0035907730 scopus 로고    scopus 로고
    • Halogen bonding: A paradigm in supramolecular chemistry
    • Metrangolo P, Resnati G. Halogen Bonding: A paradigm in supramolecular chemistry. Chemistry 7(12), 2511-2519 (2001).
    • (2001) Chemistry , vol.7 , Issue.12 , pp. 2511-2519
    • Metrangolo, P.1    Resnati, G.2
  • 14
    • 0043028476 scopus 로고    scopus 로고
    • Effect of sequence on the conformation of DNA holliday junctions
    • Hays FA, Vargason JM, Ho PS. Effect of sequence on the conformation of DNA holliday junctions. Biochemistry 42(32), 9586-9597 (2003).
    • (2003) Biochemistry , vol.42 , Issue.32 , pp. 9586-9597
    • Hays, F.A.1    Vargason, J.M.2    Ho, P.S.3
  • 16
    • 34547508202 scopus 로고    scopus 로고
    • Directing macromolecular conformation through halogen bonds
    • Voth AR, Hays FA, Ho PS. Directing macromolecular conformation through halogen bonds. Proc. Natl Acad. Sci. USA 104(15), 6188-6193 (2007).
    • (2007) Proc. Natl Acad. Sci. USA , vol.104 , Issue.15 , pp. 6188-6193
    • Voth, A.R.1    Hays, F.A.2    Ho, P.S.3
  • 17
    • 67849128457 scopus 로고    scopus 로고
    • Halogen bonds as orthogonal molecular interactions to hydrogen bonds
    • Voth AR, Khuu P, Oishi K, Ho PS. Halogen bonds as orthogonal molecular interactions to hydrogen bonds. Nat. Chem. 1(1), 74-79 (2009).
    • (2009) Nat. Chem. , vol.1 , Issue.1 , pp. 74-79
    • Voth, A.R.1    Khuu, P.2    Oishi, K.3    Ho, P.S.4
  • 18
    • 84874632186 scopus 로고    scopus 로고
    • Principles and applications of halogen bonding in medicinal chemistry and chemical biology
    • Wilcken R, Zimmermann MO, Lange A, Joerger AC, Boeckler FM. Principles and applications of halogen bonding in medicinal chemistry and chemical biology. J. Med. Chem. 56(4), 1363-1388 (2013).
    • (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
  • 19
    • 65649095907 scopus 로고    scopus 로고
    • Halogen bonding, a novel interaction for rational drug design J
    • Lu Y, Shi T, Wang Y et al. Halogen bonding, a novel interaction for rational drug design J. Med. Chem. 52(9), 2854-2862 (2009).
    • (2009) Med. Chem. , vol.52 , Issue.9 , pp. 2854-2862
    • Lu, Y.1    Shi, T.2    Wang, Y.3
  • 20
    • 79954586104 scopus 로고    scopus 로고
    • Halogen bonding in halocarbon-protein complexes: A structural survey
    • Parisini E, Metrangolo P, Pilati T, Resnati G, Terraneo G. Halogen bonding in halocarbon-protein complexes: A structural survey. Chem. Soc. Rev. 40(5), 2267-2278 (2011).
    • (2011) Chem. Soc. Rev. , vol.40 , Issue.5 , pp. 2267-2278
    • Parisini, E.1    Metrangolo, P.2    Pilati, T.3    Resnati, G.4    Terraneo, G.5
  • 21
    • 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. 50(1), 314-318 (2011).
    • (2011) Angew. Chem. Int. Ed. , vol.50 , Issue.1 , pp. 314-318
    • Hardegger, L.A.1    Kuhn, B.2    Spinnler, B.3
  • 22
    • 79961216539 scopus 로고    scopus 로고
    • Utilization of halogen bond in lead optimization: A case study of rational design of potent phosphodiesterase type 5 (PDE5) 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 (PDE5) inhibitors. J. Med. Chem. 54(15), 5607-5611 (2011).
    • (2011) J. Med. Chem. , vol.54 , Issue.15 , pp. 5607-5611
    • Xu, Z.1    Liu, Z.2    Chen, T.3
  • 24
    • 84881059458 scopus 로고    scopus 로고
    • Definition of the halogen bond (IUPAC Recommendations 2013)
    • Desiraju GR, Ho PS, Kloo L et al. Definition of the halogen bond (IUPAC Recommendations 2013). Pure Appl. Chem. 85(8), 1711-1713 (2013).
    • (2013) Pure Appl. Chem. , vol.85 , Issue.8 , pp. 1711-1713
    • Desiraju, G.R.1    Ho, P.S.2    Kloo, L.3
  • 25
    • 34548168122 scopus 로고    scopus 로고
    • Sigma;-hole bonding: Molecules containing group VI atoms
    • Murray J, Lane P, Clark T, Politzer P. σ-hole bonding: Molecules containing group VI atoms. J. Mol. Model. 13(10), 1033-1038 (2007).
    • (2007) J. Mol. Model. , vol.13 , Issue.10 , pp. 1033-1038
    • Murray, J.1    Lane, P.2    Clark, T.3    Politzer, P.4
  • 26
    • 67349235534 scopus 로고    scopus 로고
    • Expansion of the σ-hole concept
    • Murray J, Lane P, Politzer P. Expansion of the σ-hole concept. J. Mol. Model. 15(6), 723-729 (2009).
    • (2009) J. Mol. Model. , vol.15 , Issue.6 , pp. 723-729
    • Murray, J.1    Lane, P.2    Politzer, P.3
  • 27
    • 84857801456 scopus 로고    scopus 로고
    • Sigmaholes, pi-holes and electrostatically-driven interactions
    • Murray JS, Lane P, Clark T, Riley KE, Politzer P. Sigmaholes, pi-holes and electrostatically-driven interactions. J. Mol. Model. 18(2), 541-548 (2012).
    • (2012) J. Mol. Model. , vol.18 , Issue.2 , pp. 541-548
    • Murray, J.S.1    Lane, P.2    Clark, T.3    Riley, K.E.4    Politzer, P.5
  • 28
    • 0026590397 scopus 로고
    • A graphics program for the analysis and display of molecular dynamics trajectories
    • 24
    • Laaksonen L. A graphics program for the analysis and display of molecular dynamics trajectories. J. Mol. Graph 10(1), 33-34, 24 (1992).
    • (1992) J. Mol. Graph , vol.10 , Issue.1 , pp. 33-34
    • Laaksonen, L.1
  • 29
    • 84902100723 scopus 로고    scopus 로고
    • V1.4, MOLCAD GmbH: Darmstadt, Germany
    • V1.4, MOLCAD GmbH: Darmstadt, Germany. www. molcad.de
  • 30
    • 84869055505 scopus 로고    scopus 로고
    • Benchmark calculations of noncovalent interactions of halogenated molecules
    • Rezac J, Riley KE, Hobza P. Benchmark calculations of noncovalent interactions of halogenated molecules. J. Chem. Theory Comput. 8(11), 4285-4292 (2012).
    • (2012) J. Chem. Theory Comput. , vol.8 , Issue.11 , pp. 4285-4292
    • Rezac, J.1    Riley, K.E.2    Hobza, P.3
  • 31
    • 84875979464 scopus 로고    scopus 로고
    • Halogen bonds: Benchmarks and theoretical analysis
    • Kozuch S, Martin JML. Halogen bonds: benchmarks and theoretical analysis. J. Chem. Theory Comput. 9(4), 1918-1931 (2013).
    • (2013) J. Chem. Theory Comput. , vol.9 , Issue.4 , pp. 1918-1931
    • Kozuch, S.1    Martin, J.M.L.2
  • 32
    • 84885137961 scopus 로고    scopus 로고
    • The relative roles of electrostatics and dispersion in the stabilization of halogen bonds
    • Riley KE, Hobza P. The relative roles of electrostatics and dispersion in the stabilization of halogen bonds. Phys. Chem. Chem. Phys. 15(41), 17742-17751 (2013).
    • (2013) Phys. Chem. Chem. Phys. , vol.15 , Issue.41 , pp. 17742-17751
    • Riley, K.E.1    Hobza, P.2
  • 33
    • 6944251055 scopus 로고
    • Note on an approximation treatment for many-electron systems
    • Møller C, Plesset MS. Note on an approximation treatment for many-electron systems. Phys. Rev. 46(7), 618-622 (1934).
    • (1934) Phys. Rev. , vol.46 , Issue.7 , pp. 618-622
    • Møller, C.1    Plesset, M.S.2
  • 35
    • 0038617502 scopus 로고    scopus 로고
    • Improved second-order Moller-Plesset perturbation theory by separate scaling of parallel-and antiparallel-spin pair correlation energies
    • Grimme S. Improved second-order Moller-Plesset perturbation theory by separate scaling of parallel-and antiparallel-spin pair correlation energies. J. Chem. Phys. 118(20), 9095-9102 (2003).
    • (2003) J. Chem. Phys. , vol.118 , Issue.20 , pp. 9095-9102
    • Grimme, S.1
  • 36
    • 26244461462 scopus 로고    scopus 로고
    • Balanced basis sets of split valence, triple zeta valence and quadruple zeta valence quality for H to Rn: Design and assessment of accuracy
    • Weigend F, Ahlrichs R. Balanced basis sets of split valence, triple zeta valence and quadruple zeta valence quality for H to Rn: design and assessment of accuracy. Phys. Chem. Chem. Phys. 7(18), 3297-3305 (2005).
    • (2005) Phys. Chem. Chem. Phys. , vol.7 , Issue.18 , pp. 3297-3305
    • Weigend, F.1    Ahlrichs, R.2
  • 37
    • 0346521279 scopus 로고    scopus 로고
    • Systematically convergent basis sets with relativistic pseudopotentials. II. Small-core pseudopotentials and correlation consistent basis sets for the post-d group 16-18 elements
    • Peterson KA, Figgen D, Goll E, Stoll H, Dolg M. Systematically convergent basis sets with relativistic pseudopotentials. II. Small-core pseudopotentials and correlation consistent basis sets for the post-d group 16-18 elements. J. Chem. Phys. 119(21), 11113-11123 (2003).
    • (2003) J. Chem. Phys. , vol.119 , Issue.21 , pp. 11113-11123
    • Peterson, K.A.1    Figgen, D.2    Goll, E.3    Stoll, H.4    Dolg, M.5
  • 38
    • 77951680464 scopus 로고    scopus 로고
    • A consistent and accurate ab initio parametrization of density functional dispersion correction (DFT-D) for the 94 elements H-Pu
    • Grimme S, Antony J, Ehrlich S, Krieg H. A consistent and accurate ab initio parametrization of density functional dispersion correction (DFT-D) for the 94 elements H-Pu. J. Chem. Phys. 132(15), 154104 (2010).
    • (2010) J. Chem. Phys. , vol.132 , Issue.15 , pp. 154104
    • Grimme, S.1    Antony, J.2    Ehrlich, S.3    Krieg, H.4
  • 40
    • 84896508445 scopus 로고    scopus 로고
    • Targeting histidine sidechains in molecular design through nitrogen-halogen bonds
    • Lange A, Zimmermann MO, Wilcken R, Zahn S, Boeckler FM. Targeting histidine sidechains in molecular design through nitrogen-halogen bonds. J. Chem. Inf. Model. 53(12), 3178-3189 (2013).
    • (2013) J. Chem. Inf. Model. , vol.53 , Issue.12 , pp. 3178-3189
    • Lange, A.1    Zimmermann, M.O.2    Wilcken, R.3    Zahn, S.4    Boeckler, F.M.5
  • 42
    • 70350515927 scopus 로고    scopus 로고
    • Fluorine bonding-how does it work in protein-ligand interactions J
    • Zhou P, Zou JW, Tian FF, Shang ZC. Fluorine bonding-how does it work in protein-ligand interactions J. Chem. Inf. Model. 49(10), 2344-2355 (2009).
    • (2009) Chem. Inf. Model. , vol.49 , Issue.10 , pp. 2344-2355
    • Zhou, P.1    Zou, J.W.2    Tian, F.F.3    Shang, Z.C.4
  • 43
    • 84890021933 scopus 로고
    • The calculation of small molecular interactions by the differences of separate total energies. Some procedures with reduced errors
    • Boys SF, Bernardi F. The calculation of small molecular interactions by the differences of separate total energies. Some procedures with reduced errors. Mol. Phys. 19, 553-566 (1970).
    • (1970) Mol. Phys. , vol.19 , pp. 553-566
    • Boys, S.F.1    Bernardi, F.2
  • 44
    • 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. 11(11), 5087-5095 (2011).
    • (2011) Cryst. Growth Des. , vol.11 , Issue.11 , pp. 5087-5095
    • Carter, M.1    Ho, P.S.2
  • 45
    • 61449098598 scopus 로고    scopus 로고
    • Br-O complexes as probes of factors affecting halogen bonding: Interactions of bromobenzenes and bromopyrimidines with acetone
    • Riley KE, Murray JS, Politzer P, Concha MC, Hobza P. Br-O complexes as probes of factors affecting halogen bonding: interactions of bromobenzenes and bromopyrimidines with acetone. J. Chem. Theory Comput. 5(1), 155-163 (2009).
    • (2009) J. Chem. Theory Comput. , vol.5 , Issue.1 , pp. 155-163
    • Riley, K.E.1    Murray, J.S.2    Politzer, P.3    Concha, M.C.4    Hobza, P.5
  • 47
    • 84855661131 scopus 로고    scopus 로고
    • Halogen bond tunability I: The effects of aromatic fluorine substitution on the strengths of halogen-bonding interactions involving chlorine, bromine, and iodine
    • Riley KE, Murray JS, Fanfrlik J et al. Halogen bond tunability I: the effects of aromatic fluorine substitution on the strengths of halogen-bonding interactions involving chlorine, bromine, and iodine. J. Mol. Model. 17(12), 3309-3318 (2011).
    • (2011) J. Mol. Model. , vol.17 , Issue.12 , pp. 3309-3318
    • Riley, K.E.1    Murray, J.S.2    Fanfrlik, J.3
  • 48
    • 84888294131 scopus 로고    scopus 로고
    • Halogen bond tunability II: The varying roles of electrostatic and dispersion contributions to attraction in halogen bonds
    • Riley K, Murray J, Fanfrlík J et al. Halogen bond tunability II: the varying roles of electrostatic and dispersion contributions to attraction in halogen bonds. J. Mol. Model. 19, 4651-4659 (2013).
    • (2013) J. Mol. Model. , vol.19 , pp. 4651-4659
    • Riley, K.M.1
  • 49
    • 84887901729 scopus 로고    scopus 로고
    • Modulation of aldose reductase inhibition by halogen bond tuning
    • Fanfrlik J, Kolar M, Kamlar M et al. Modulation of aldose reductase inhibition by halogen bond tuning. ACS Chem. Biol. 8(11), 2484-2492 (2013).
    • (2013) ACS Chem. Biol. , vol.8 , Issue.11 , pp. 2484-2492
    • Fanfrlik, J.1    Kolar, M.2    Kamlar, M.3
  • 50
    • 77956968392 scopus 로고    scopus 로고
    • Halogen bonds form the basis for selective P-TEFb inhibition by DRB
    • Baumli S, Endicott JA, Johnson LN. Halogen bonds form the basis for selective P-TEFb inhibition by DRB. Chem. Biol. 17(9), 931-936 (2010).
    • (2010) Chem. Biol. , vol.17 , Issue.9 , pp. 931-936
    • Baumli, S.1    Endicott, J.A.2    Johnson, L.N.3
  • 51
    • 79953783228 scopus 로고    scopus 로고
    • Small-molecule ligands of methyl-lysine binding proteins
    • Herold JM, Wigle TJ, Norris JL et al. Small-molecule ligands of methyl-lysine binding proteins. J. Med. Chem. 54(7), 2504-2511 (2011).
    • (2011) J. Med. Chem. , vol.54 , Issue.7 , pp. 2504-2511
    • Herold, J.M.1    Wigle, T.J.2    Norris, J.L.3
  • 54
    • 30344455620 scopus 로고    scopus 로고
    • Enhanced FTase activity achieved via piperazine interaction with catalytic zinc
    • Njoroge FG, Vibulbhan B, Pinto P et al. Enhanced FTase activity achieved via piperazine interaction with catalytic zinc. Bioorg. Med. Chem. Lett. 16(4), 984-988 (2006).
    • (2006) Bioorg. Med. Chem. Lett. , vol.16 , Issue.4 , pp. 984-988
    • Njoroge, F.G.1    Vibulbhan, B.2    Pinto, P.3
  • 55
    • 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, Baase 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. 385(2), 595-605 (2009).
    • (2009) J. Mol. Biol. , vol.385 , Issue.2 , pp. 595-605
    • Liu, L.1    Baase, W.A.2    Matthews, B.W.3
  • 56
    • 79955118487 scopus 로고    scopus 로고
    • Crystallographic analysis reveals the structural basis of the high-affinity binding of iophenoxic acid to human serum albumin
    • Ryan A, Chung C-W, Curry S. Crystallographic analysis reveals the structural basis of the high-affinity binding of iophenoxic acid to human serum albumin. BMC Struct. Biol. 11(1), 18 (2011).
    • (2011) BMC Struct. Biol. , vol.11 , Issue.1
    • Ryan, A.1    Chung, C.-W.2    Curry, S.3
  • 57
    • 67349271141 scopus 로고    scopus 로고
    • Design of novel aminopyrrolidine factor Xa inhibitors from a screening hit
    • Zbinden KG, Anselm L, Banner DW et al. Design of novel aminopyrrolidine factor Xa inhibitors from a screening hit. Eur. J. Med. Chem. 44(7), 2787-2795 (2009).
    • (2009) Eur. J. Med. Chem. , vol.44 , Issue.7 , pp. 2787-2795
    • Zbinden, K.G.1    Anselm, L.2    Banner, D.W.3
  • 58
    • 77956345169 scopus 로고    scopus 로고
    • Identification and mechanism of ABA receptor antagonism
    • Melcher K, Xu Y, Ng L-M et al. Identification and mechanism of ABA receptor antagonism. Nat. Struct. Mol. Biol. 17(99), 1102-1108 (2010).
    • (2010) Nat. Struct. Mol. Biol. , vol.17 , Issue.99 , pp. 1102-1108
    • Melcher, K.1    Xu, Y.2    Ng, L.-M.3
  • 59
    • 47749128054 scopus 로고    scopus 로고
    • Conformationally constrained farnesoid X receptor (FXR) agonists: Naphthoic acid-based analogs of GW 4064
    • Akwabi-Ameyaw A, Bass JY, Caldwell RD et al. Conformationally constrained farnesoid X receptor (FXR) agonists: Naphthoic acid-based analogs of GW 4064. Bioorg. Med. Chem. Lett. 18(15), 4339-4343 (2008).
    • (2008) Bioorg. Med. Chem. Lett. , vol.18 , Issue.15 , pp. 4339-4343
    • Akwabi-Ameyaw, A.1    Bass, J.Y.2    Caldwell, R.D.3
  • 60
    • 68349160571 scopus 로고    scopus 로고
    • Substituted tetrahydroquinolines as potent allosteric inhibitors of reverse transcriptase and its key mutants
    • Su D-S, Lim JJ, Tinney E et al. Substituted tetrahydroquinolines as potent allosteric inhibitors of reverse transcriptase and its key mutants. Bioorg. Med. Chem. Lett. 19(17), 5119-5123 (2009).
    • (2009) Bioorg. Med. Chem. Lett. , vol.19 , Issue.17 , pp. 5119-5123
    • Su, D.-S.1    Lim, J.J.2    Tinney, E.3
  • 61
    • 1542358099 scopus 로고    scopus 로고
    • Axial ligand complexes of the Rhodnius nitrophorins: Reduction potentials, binding constants, EPR spectra, and structures of the 4-iodopyrazole and imidazole complexes of NP4
    • Berry R, Ding X, Shokhireva T, Weichsel A, Montfort W, Walker FA. Axial ligand complexes of the Rhodnius nitrophorins: reduction potentials, binding constants, EPR spectra, and structures of the 4-iodopyrazole and imidazole complexes of NP4. J. Biol. Inorg. Chem. 9(2), 135-144 (2004).
    • (2004) J. Biol. Inorg. Chem. , vol.9 , Issue.2 , pp. 135-144
    • Berry, R.1    Ding, X.2    Shokhireva, T.3    Weichsel, A.4    Montfort, W.5    Walker, F.A.6
  • 62
    • 0036968894 scopus 로고    scopus 로고
    • Structural basis for AMPA receptor activation and ligand selectivity: Crystal structures of five agonist complexes with the GluR2 ligand-binding core
    • Hogner A, Kastrup JS, Jin R et al. Structural basis for AMPA receptor activation and ligand selectivity: crystal structures of five agonist complexes with the GluR2 ligand-binding core. J. Mol. Biol. 322(1), 93-109 (2002).
    • (2002) J. Mol. Biol. , vol.322 , Issue.1 , pp. 93-109
    • Hogner, A.1    Kastrup, J.S.2    Jin, R.3
  • 63
    • 80052806086 scopus 로고    scopus 로고
    • Structure based drug design of crizotinib (PF-02341066), a potent and selective dual inhibitor of mesenchymal-epithelial transition factor (c-MET) kinase and anaplastic lymphoma kinase (ALK)
    • Cui JJ, Tran-Dubé M, Shen H et al. Structure based drug design of crizotinib (PF-02341066), a potent and selective dual inhibitor of mesenchymal-epithelial transition factor (c-MET) kinase and anaplastic lymphoma kinase (ALK). J. Med. Chem. 54(18), 6342-6363 (2011).
    • (2011) J. Med. Chem. , vol.54 , Issue.18 , pp. 6342-6363
    • Cui, J.J.1    Tran-Dubé, M.2    Shen, H.3
  • 65
    • 24944536065 scopus 로고    scopus 로고
    • Discovery of the novel antithrombotic agent 5-chloro-N-({(5S)-2-oxo-3-[4- (3-oxomorpholin-4-yl)phenyl]-1,3-oxazolidin-5-yl} methyl)thiophene-2-carboxamide (BAY 59-7939): An oral, direct factor Xa inhibitor
    • Roehrig S, Straub A, Pohlmann J et al. Discovery of the novel antithrombotic agent 5-chloro-N-({(5S)-2-oxo-3-[4-(3-oxomorpholin-4-yl)phenyl]- 1,3-oxazolidin-5-yl} methyl)thiophene-2-carboxamide (BAY 59-7939): an oral, direct factor Xa inhibitor. J. Med. Chem. 48(19), 5900-5908 (2005).
    • (2005) J. Med. Chem. , vol.48 , Issue.19 , pp. 5900-5908
    • Roehrig, S.1    Straub, A.2    Pohlmann, J.3
  • 66
    • 67349109896 scopus 로고    scopus 로고
    • More than a simple lipophilic contact: A detailed thermodynamic analysis of nonbasic residues in the s1 pocket of thrombin
    • Baum B, Mohamed M, Zayed M et al. More than a simple lipophilic contact: a detailed thermodynamic analysis of nonbasic residues in the s1 pocket of thrombin. J. Mol. Biol. 390(1), 56-69 (2009).
    • (2009) J. Mol. Biol. , vol.390 , Issue.1 , pp. 56-69
    • Baum, B.1    Mohamed, M.2    Zayed, M.3
  • 67
    • 84866693984 scopus 로고    scopus 로고
    • 3D-QSAR based on quantum-chemical molecular fields: Toward an improved description of halogen interactions
    • Gussregen S, Matter H, Hessler G, Muller M, Schmidt F, Clark T. 3D-QSAR based on quantum-chemical molecular fields: toward an improved description of halogen interactions. J. Chem. Inf. Model. 52(9), 2441-2453 (2012).
    • (2012) J. Chem. Inf. Model. , vol.52 , Issue.9 , pp. 2441-2453
    • Gussregen, S.1    Matter, H.2    Hessler, G.3    Muller, M.4    Schmidt, F.5    Clark, T.6
  • 68
    • 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. Engl. 48(16), 2911-2916 (2009).
    • (2009) Angew. Chem. Int. Ed. Engl. , vol.48 , Issue.16 , pp. 2911-2916
    • Matter, H.1    Nazare, M.2    Gussregen, S.3
  • 69
    • 84856083088 scopus 로고    scopus 로고
    • Skepinone-L is a selective p38 mitogen-activated protein kinase inhibitor
    • Koeberle SC, Romir J, Fischer S et al. Skepinone-L is a selective p38 mitogen-activated protein kinase inhibitor. Nat. Chem. Biol. 8(2), 141-143 (2012).
    • (2012) Nat. Chem. Biol. , vol.8 , Issue.2 , pp. 141-143
    • Koeberle, S.C.1    Romir, J.2    Fischer, S.3
  • 70
    • 84872337099 scopus 로고    scopus 로고
    • Dibenzosuberones as p38 mitogen-activated protein kinase inhibitors with low ATP competitiveness and outstanding whole blood activity
    • Fischer S, Wentsch HK, Mayer-Wrangowski SC et al. Dibenzosuberones as p38 mitogen-activated protein kinase inhibitors with low ATP competitiveness and outstanding whole blood activity. J. Med. Chem. 56(1), 241-253 (2013).
    • (2013) J. Med. Chem. , vol.56 , Issue.1 , pp. 241-253
    • Fischer, S.1    Wentsch, H.K.2    Mayer-Wrangowski, S.C.3
  • 71
    • 84856380089 scopus 로고    scopus 로고
    • Tri-and tetrasubstituted pyrazole derivates: Regioisomerism switches activity from p38MAP kinase to important cancer kinases
    • Abu Thaher B, Arnsmann M, Totzke F et al. Tri-and tetrasubstituted pyrazole derivates: regioisomerism switches activity from p38MAP kinase to important cancer kinases. J. Med. Chem. 55(2), 961-965 (2012).
    • (2012) J. Med. Chem. , vol.55 , Issue.2 , pp. 961-965
    • Abu Thaher, B.1    Arnsmann, M.2    Totzke, F.3
  • 72
    • 84878879186 scopus 로고    scopus 로고
    • Halogen bonding at the ATP binding site of protein kinases: Preferred geometry and topology of ligand binding
    • Poznanski J, Shugar D. Halogen bonding at the ATP binding site of protein kinases: preferred geometry and topology of ligand binding. Biochim. Biophys. Acta 1834(7), 1381-1386 (2013).
    • (2013) Biochim. Biophys. Acta , vol.1834 , Issue.7 , pp. 1381-1386
    • Poznanski, J.1    Shugar, D.2
  • 73
    • 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. 18(1), 67-76 (2011).
    • (2011) Chem. Biol. , vol.18 , Issue.1 , pp. 67-76
    • Fedorov, O.1    Huber, K.2    Eisenreich, A.3
  • 74
    • 79251562528 scopus 로고    scopus 로고
    • Kinase inhibition that hinges on halogen bonds
    • Grant SK, Lunney EA. Kinase inhibition that hinges on halogen bonds. Chem. Biol. 18(1), 3-4 (2011).
    • (2011) Chem. Biol. , vol.18 , Issue.1 , pp. 3-4
    • Grant, S.K.1    Lunney, E.A.2
  • 75
    • 84855824393 scopus 로고    scopus 로고
    • 7,8-dichloro-1-oxo-β-carbolines as a versatile scaffold for the development of potent and selective kinase inhibitors with unusual binding modes
    • Huber K, Brault L, Fedorov O et al. 7,8-dichloro-1-oxo-β-carbolines as a versatile scaffold for the development of potent and selective kinase inhibitors with unusual binding modes. J. Med. Chem. 55(1), 403-413 (2011).
    • (2011) J. Med. Chem. , vol.55 , Issue.1 , pp. 403-413
    • Huber, K.1    Brault, L.2    Fedorov, O.3
  • 76
    • 84866682261 scopus 로고    scopus 로고
    • Treatment of halogen bonding in the OPLS-AA force field: Application to potent anti-HIV agents
    • Jorgensen WL, Schyman P. Treatment of halogen bonding in the OPLS-AA force field: application to potent anti-HIV agents. J. Chem. Theory Comput. 8(10), 3895-3901 (2012).
    • (2012) J. Chem. Theory Comput. , vol.8 , Issue.10 , pp. 3895-3901
    • Jorgensen, W.L.1    Schyman, P.2
  • 77
    • 84055211792 scopus 로고    scopus 로고
    • Computationally-guided optimization of a docking hit to yield catechol diethers as potent anti-HIV agents
    • Bollini M, Domaoal RA, Thakur VV et al. Computationally-guided optimization of a docking hit to yield catechol diethers as potent anti-HIV agents. J. Med. Chem. 54(24), 8582-8591 (2011).
    • (2011) J. Med. Chem. , vol.54 , Issue.24 , pp. 8582-8591
    • Bollini, M.1    Domaoal, R.A.2    Thakur, V.V.3
  • 78
    • 84899489984 scopus 로고    scopus 로고
    • Structure-based evaluation of C5 derivatives in the catechol diether series targeting HIV-1 reverse transcriptase
    • doi:10.1111/cbdd.12266 (Epub ahead of print
    • Frey KM, Gray WT, Spasov KA et al. Structure-based evaluation of C5 derivatives in the catechol diether series targeting HIV-1 reverse transcriptase. Chem. Biol. Drug Design (2013) doi:10.1111/cbdd.12266 (Epub ahead of print).
    • (2013) Chem. Biol. Drug Design
    • Frey, K.M.1    Gray, W.T.2    Spasov, K.A.3
  • 79
    • 84863290357 scopus 로고    scopus 로고
    • Design synthesis, and biological evaluation of 1-[(2-benzyloxyl/alkoxyl) methyl]-5-halo-6-aryluracils as potent HIV-1 non-nucleoside reverse transcriptase inhibitors with an improved drug resistance profile
    • Wang XW, Zhang JF, Huang Y et al. Design, synthesis, and biological evaluation of 1-[(2-benzyloxyl/alkoxyl)methyl]-5-halo-6-aryluracils as potent HIV-1 non-nucleoside reverse transcriptase inhibitors with an improved drug resistance profile. J. Med. Chem. 55(5), 2242-2250 (2012).
    • (2012) J. Med. Chem. , vol.55 , Issue.5 , pp. 2242-2250
    • Wang, X.W.1    Zhang, J.F.2    Huang, Y.3
  • 80
    • 84870654424 scopus 로고    scopus 로고
    • Crystal structures of HIV-1 reverse transcriptase with picomolar inhibitors reveal key interactions for drug design
    • Frey KM, Bollini M, Mislak AC et al. Crystal structures of HIV-1 reverse transcriptase with picomolar inhibitors reveal key interactions for drug design. J. Am. Chem. Soc. 134(48), 19501-19503 (2012).
    • (2012) J. Am. Chem. Soc. , vol.134 , Issue.48 , pp. 19501-19503
    • Frey, K.M.1    Bollini, M.2    Mislak, A.C.3
  • 81
    • 84856756647 scopus 로고    scopus 로고
    • Intersubunit bridge formation governs agonist efficacy at nicotinic acetylcholine alpha4beta2 receptors: Unique role of halogen bonding revealed
    • Rohde LA, Ahring PK, Jensen ML et al. Intersubunit bridge formation governs agonist efficacy at nicotinic acetylcholine alpha4beta2 receptors: unique role of halogen bonding revealed. J. Biol. Chem. 287(6), 4248-4259 (2012).
    • (2012) J. Biol. Chem. , vol.287 , Issue.6 , pp. 4248-4259
    • Rohde, L.A.1    Ahring, P.K.2    Jensen, M.L.3
  • 82
    • 84860157680 scopus 로고    scopus 로고
    • New mutations in the mycobacterial ATP synthase: New insights into the binding of the diarylquinoline TMC207 to the ATP synthase C-ring structure
    • Segala E, Sougakoff W, Nevejans-Chauffour A, Jarlier V, Petrella S. New mutations in the mycobacterial ATP synthase: new insights into the binding of the diarylquinoline TMC207 to the ATP synthase C-ring structure. Antimicrob Agents Chemother. 56(5), 2326-2334 (2012).
    • (2012) Antimicrob Agents Chemother. , vol.56 , Issue.5 , pp. 2326-2334
    • Segala, E.1    Sougakoff, W.2    Nevejans-Chauffour, A.3    Jarlier, V.4    Petrella, S.5
  • 83
    • 84874602301 scopus 로고    scopus 로고
    • Identification of bacteria-selective threonyl-tRNA synthetase substrate inhibitors by structure-based design
    • Teng M, Hilgers MT, Cunningham ML et al. Identification of bacteria-selective threonyl-tRNA synthetase substrate inhibitors by structure-based design. J. Med. Chem. 56(4), 1748-1760 (2013).
    • (2013) J. Med. Chem. , vol.56 , Issue.4 , pp. 1748-1760
    • Teng, M.1    Hilgers, M.T.2    Cunningham, M.L.3
  • 84
    • 84888862217 scopus 로고    scopus 로고
    • Pyrido[2,3-d] pyrimidines: Discovery and preliminary SAR of a novel series of DYRK1B and DYRK1A inhibitors
    • Anderson K, Chen Y, Chen Z et al. Pyrido[2,3-d] pyrimidines: discovery and preliminary SAR of a novel series of DYRK1B and DYRK1A inhibitors. Bioorg. Med. Chem. Lett. 23(24), 6610-6615 (2013).
    • (2013) Bioorg. Med. Chem. Lett. , vol.23 , Issue.24 , pp. 6610-6615
    • Anderson, K.1    Chen, Y.2    Chen, Z.3
  • 86
    • 0019407381 scopus 로고
    • On the attribution and additivity of binding energies
    • Jencks WP. On the attribution and additivity of binding energies. Proc. Natl Acad. Sci. USA 78(7), 4046-4050 (1981).
    • (1981) Proc. Natl Acad. Sci. USA , vol.78 , Issue.7 , pp. 4046-4050
    • Jencks, W.P.1
  • 87
    • 0021871375 scopus 로고
    • A computational procedure for determining energetically favorable binding sites on biologically important macromolecules
    • Goodford PJ. A computational procedure for determining energetically favorable binding sites on biologically important macromolecules. J. Med. Chem. 28(7), 849-857 (1985).
    • (1985) J. Med. Chem. , vol.28 , Issue.7 , pp. 849-857
    • Goodford, P.J.1
  • 88
    • 0025916872 scopus 로고
    • Functionality maps of binding sites: A multiple copy simultaneous search method
    • Miranker A, Karplus M. Functionality maps of binding sites: a multiple copy simultaneous search method. Proteins 11(1), 29-34 (1991).
    • (1991) Proteins , vol.11 , Issue.1 , pp. 29-34
    • Miranker, A.1    Karplus, M.2
  • 90
    • 0029868304 scopus 로고    scopus 로고
    • Locating and characterizing binding sites on proteins
    • Mattos C, Ringe D. Locating and characterizing binding sites on proteins. Nat. Biotechnol. 14(5), 595-599 (1996).
    • (1996) Nat. Biotechnol. , vol.14 , Issue.5 , pp. 595-599
    • Mattos, C.1    Ringe, D.2
  • 91
    • 0035044857 scopus 로고    scopus 로고
    • Experimental and computational mapping of the binding surface of a crystalline protein
    • English AC, Groom CR, Hubbard RE. Experimental and computational mapping of the binding surface of a crystalline protein. Protein Eng. 14(1), 47-59 (2001).
    • (2001) Protein Eng. , vol.14 , Issue.1 , pp. 47-59
    • English, A.C.1    Groom, C.R.2    Hubbard, R.E.3
  • 92
    • 0028282687 scopus 로고
    • HOOK: A program for finding novel molecular architectures that satisfy the chemical and steric requirements of a macromolecule binding site
    • Eisen MB, Wiley DC, Karplus M, Hubbard RE. HOOK: a program for finding novel molecular architectures that satisfy the chemical and steric requirements of a macromolecule binding site. Proteins 19(3), 199-221 (1994).
    • (1994) Proteins , vol.19 , Issue.3 , pp. 199-221
    • Eisen, M.B.1    Wiley, D.C.2    Karplus, M.3    Hubbard, R.E.4
  • 93
    • 0028380643 scopus 로고
    • CAVEAT: A program to facilitate the design of organic molecules
    • Lauri G, Bartlett PA. CAVEAT: a program to facilitate the design of organic molecules. J. Comput. Aided Mol. Des. 8(1), 51-66 (1994).
    • (1994) J. Comput. Aided Mol. Des. , vol.8 , Issue.1 , pp. 51-66
    • Lauri, G.1    Bartlett, P.A.2
  • 94
    • 0029836953 scopus 로고    scopus 로고
    • Discovering high-affinity ligands for proteins: SAR by NMR
    • Shuker SB, Hajduk PJ, Meadows RP, Fesik SW. Discovering high-affinity ligands for proteins: SAR by NMR. Science 274(5292), 1531-1534 (1996).
    • (1996) Science , vol.274 , Issue.5292 , pp. 1531-1534
    • Shuker, S.B.1    Hajduk, P.J.2    Meadows, R.P.3    Fesik, S.W.4
  • 96
    • 70349425790 scopus 로고    scopus 로고
    • Recent progress in fragmentbased lead discovery
    • Schulz MN, Hubbard RE. Recent progress in fragmentbased lead discovery. Curr. Opin. Pharmacol. 9(5), 615-621 (2009).
    • (2009) Curr. Opin. Pharmacol. , vol.9 , Issue.5 , pp. 615-621
    • Schulz, M.N.1    Hubbard, R.E.2
  • 97
    • 84874414338 scopus 로고    scopus 로고
    • Fragment-based lead discovery grows up
    • Baker M. Fragment-based lead discovery grows up. Nat. Rev. Drug Discov. 12(1), 5-7 (2013).
    • (2013) Nat. Rev. Drug Discov. , vol.12 , Issue.1 , pp. 5-7
    • Baker, M.1
  • 98
    • 79960997906 scopus 로고    scopus 로고
    • Molecular complexity and fragmentbased drug discovery: Ten years on
    • Leach AR, Hann MM. Molecular complexity and fragmentbased drug discovery: ten years on. Curr. Opin. Chem. Biol. 15(4), 489-496 (2011).
    • (2011) Curr. Opin. Chem. Biol. , vol.15 , Issue.4 , pp. 489-496
    • Leach, A.R.1    Hann, M.M.2
  • 99
    • 79952131874 scopus 로고    scopus 로고
    • Impact of highthroughput screening in biomedical research
    • Macarron R, Banks MN, Bojanic D et al. Impact of highthroughput screening in biomedical research. Nat. Rev. Drug Discov. 10(3), 188-195 (2011).
    • (2011) Nat. Rev. Drug Discov. , vol.10 , Issue.3 , pp. 188-195
    • MacArron, R.1    Banks, M.N.2    Bojanic, D.3
  • 100
    • 69249218864 scopus 로고    scopus 로고
    • Design, synthesis and selection of DNA-encoded small-molecule libraries
    • Clark MA, Acharya RA, Arico-Muendel CC et al. Design, synthesis and selection of DNA-encoded small-molecule libraries. Nat. Chem. Biol. 5(9), 647-654 (2009).
    • (2009) Nat. Chem. Biol. , vol.5 , Issue.9 , pp. 647-654
    • Clark, M.A.1    Acharya, R.A.2    Arico-Muendel, C.C.3
  • 101
    • 77956513286 scopus 로고    scopus 로고
    • Clinical efficacy of a RAF inhibitor needs broad target blockade in BRAF-mutant melanoma
    • Bollag G, Hirth P, Tsai J et al. Clinical efficacy of a RAF inhibitor needs broad target blockade in BRAF-mutant melanoma. Nature 467(7315), 596-599 (2010).
    • (2010) Nature , vol.467 , Issue.7315 , pp. 596-599
    • Bollag, G.1    Hirth, P.2    Tsai, J.3
  • 102
    • 67649341990 scopus 로고    scopus 로고
    • From fragment to clinical candidate-A historical perspective
    • Chessari G, Woodhead AJ. From fragment to clinical candidate-a historical perspective. Drug Discov. Today 14(13-14), 668-675 (2009).
    • (2009) Drug Discov. Today , vol.14 , Issue.13-14 , pp. 668-675
    • Chessari, G.1    Woodhead, A.J.2
  • 104
    • 33845903833 scopus 로고    scopus 로고
    • Drugs for bad bugs: Confronting the challenges of antibacterial discovery
    • Payne DJ, Gwynn MN, Holmes DJ, Pompliano DL. Drugs for bad bugs: confronting the challenges of antibacterial discovery. Nat. Rev. Drug Discov. 6(1), 29-40 (2007).
    • (2007) Nat. Rev. Drug Discov. , vol.6 , Issue.1 , pp. 29-40
    • Payne, D.J.1    Gwynn, M.N.2    Holmes, D.J.3    Pompliano, D.L.4
  • 105
    • 0141726877 scopus 로고    scopus 로고
    • A 'rule of three' for fragment-based lead discovery Drug Discov
    • Congreve M, Carr R, Murray C, Jhoti H. A 'rule of three' for fragment-based lead discovery Drug Discov. Today 8(19), 876-877 (2003).
    • (2003) Today , vol.8 , Issue.19 , pp. 876-877
    • Congreve, M.1    Carr, R.2    Murray, C.3    Jhoti, H.4
  • 107
    • 0035324944 scopus 로고    scopus 로고
    • Molecular complexity and its impact on the probability of finding leads for drug discovery
    • Hann MM, Leach AR, Harper G. Molecular complexity and its impact on the probability of finding leads for drug discovery. J. Chem. Inf. Comput. Sci. 41(3), 856-864 (2001).
    • (2001) J. Chem. Inf. Comput. Sci. , vol.41 , Issue.3 , pp. 856-864
    • Hann, M.M.1    Leach, A.R.2    Harper, G.3
  • 109
    • 84860359784 scopus 로고    scopus 로고
    • Finding the sweet spot: The role of nature and nurture in medicinal chemistry
    • Hann MM, Keseru GM. Finding the sweet spot: the role of nature and nurture in medicinal chemistry. Nat. Rev. Drug Discov. 11(5), 355-365 (2012).
    • (2012) Nat. Rev. Drug Discov. , vol.11 , Issue.5 , pp. 355-365
    • Hann, M.M.1    Keseru, G.M.2
  • 110
    • 1942453243 scopus 로고    scopus 로고
    • Ligand efficiency: A useful metric for lead selection
    • Hopkins AL, Groom CR, Alex A. Ligand efficiency: a useful metric for lead selection. Drug Discov. Today 9(10), 430-431 (2004).
    • (2004) Drug Discov. Today , vol.9 , Issue.10 , pp. 430-431
    • Hopkins, A.L.1    Groom, C.R.2    Alex, A.3
  • 112
    • 0036051992 scopus 로고    scopus 로고
    • High-throughput crystallography for lead discovery in drug design
    • Blundell TL, Jhoti H, Abell C. High-throughput crystallography for lead discovery in drug design. Nat. Rev. Drug Discov. 1(1), 45-54 (2002).
    • (2002) Nat. Rev. Drug Discov. , vol.1 , Issue.1 , pp. 45-54
    • Blundell, T.L.1    Jhoti, H.2    Abell, C.3
  • 113
    • 0036804362 scopus 로고    scopus 로고
    • The genesis of high-throughput structure-based drug discovery using protein crystallography
    • Kuhn P, Wilson K, Patch MG, Stevens RC. The genesis of high-throughput structure-based drug discovery using protein crystallography. Curr. Opin. Chem. Biol. 6(5), 704-710 (2002).
    • (2002) Curr. Opin. Chem. Biol. , vol.6 , Issue.5 , pp. 704-710
    • Kuhn, P.1    Wilson, K.2    Patch, M.G.3    Stevens, R.C.4
  • 114
    • 84859993146 scopus 로고    scopus 로고
    • Halogenenriched fragment libraries as leads for drug rescue of mutant p53
    • Wilcken R, Liu X, Zimmermann MO et al. Halogenenriched fragment libraries as leads for drug rescue of mutant p53. J. Am. Chem. Soc. 134(15), 6810-6818 (2012).
    • (2012) J. Am. Chem. Soc. , vol.134 , Issue.15 , pp. 6810-6818
    • Wilcken, R.1    Liu, X.2    Zimmermann, M.O.3
  • 115
    • 84880234835 scopus 로고    scopus 로고
    • Small molecule induced reactivation of mutant p53 in cancer cells
    • Liu X, Wilcken R, Joerger AC et al. Small molecule induced reactivation of mutant p53 in cancer cells. Nucleic Acids Res. 41(12), 6034-6044 (2013).
    • (2013) Nucleic Acids Res. , vol.41 , Issue.12 , pp. 6034-6044
    • Liu, X.1    Wilcken, R.2    Joerger, A.C.3
  • 117
    • 79952428086 scopus 로고    scopus 로고
    • Practical aspects of NMR-based fragment screening
    • Lepre CA. Practical aspects of NMR-based fragment screening. Methods Enzymol. 493, 219-239 (2011).
    • (2011) Methods Enzymol. , vol.493 , pp. 219-239
    • Lepre, C.A.1
  • 118
    • 84879844246 scopus 로고    scopus 로고
    • Fragment-based drug discovery using NMR spectroscopy
    • Harner MJ, Frank AO, Fesik SW. Fragment-based drug discovery using NMR spectroscopy. J. Biomol. NMR 56(2), 65-75 (2013).
    • (2013) J. Biomol. NMR 56 , vol.2 , pp. 65-75
    • Harner, M.J.1    Frank, A.O.2    Fesik, S.W.3
  • 120
    • 36249028775 scopus 로고    scopus 로고
    • SPR-based fragment screening: Advantages and applications
    • Neumann T, Junker HD, Schmidt K, Sekul R. SPR-based fragment screening: advantages and applications. Curr. Top. Med. Chem. 7(16), 1630-1642 (2007).
    • (2007) Curr. Top. Med. Chem. , vol.7 , Issue.16 , pp. 1630-1642
    • Neumann, T.1    Junker, H.D.2    Schmidt, K.3    Sekul, R.4
  • 121
    • 74249116139 scopus 로고    scopus 로고
    • Fragment library screening and lead characterization using SPR biosensors
    • Danielson UH. Fragment library screening and lead characterization using SPR biosensors. Curr. Top. Med. Chem. 9(18), 1725-1735 (2009).
    • (2009) Curr. Top. Med. Chem. , vol.9 , Issue.18 , pp. 1725-1735
    • Danielson, U.H.1
  • 122
    • 77956622674 scopus 로고    scopus 로고
    • Fragment screening by surface plasmon resonance
    • Navratilova I, Hopkins AL. Fragment screening by surface plasmon resonance. ACS Med. Chem. Lett. 1(1), 44-48 (2010).
    • (2010) ACS Med. Chem. Lett. , vol.1 , Issue.1 , pp. 44-48
    • Navratilova, I.1    Hopkins, A.L.2
  • 123
    • 33750470057 scopus 로고    scopus 로고
    • Chemical screening methods to identify ligands that promote protein stability, protein crystallization, and structure determination
    • Vedadi M, Niesen FH, Allali-Hassani A et al. Chemical screening methods to identify ligands that promote protein stability, protein crystallization, and structure determination. Proc. Natl Acad. Sci. USA 103(43), 15835-15840 (2006).
    • (2006) Proc. Natl Acad. Sci. USA , vol.103 , Issue.43 , pp. 15835-15840
    • Vedadi, M.1    Niesen, F.H.2    Allali-Hassani, A.3
  • 124
    • 37249005205 scopus 로고    scopus 로고
    • The use of differential scanning fluorimetry to detect ligand interactions that promote protein stability
    • Niesen FH, Berglund H, Vedadi M. The use of differential scanning fluorimetry to detect ligand interactions that promote protein stability. Nat. Protoc. 2(9), 2212-2221 (2007).
    • (2007) Nat. Protoc. , vol.2 , Issue.9 , pp. 2212-2221
    • Niesen, F.H.1    Berglund, H.2    Vedadi, M.3
  • 125
    • 75149134332 scopus 로고    scopus 로고
    • Toward the rational design of p53-stabilizing drugs: Probing the surface of the oncogenic Y220C mutant
    • Basse N, Kaar JL, Settanni G, Joerger AC, Rutherford TJ, Fersht AR. Toward the rational design of p53-stabilizing drugs: probing the surface of the oncogenic Y220C mutant. Chem. Biol. 17(1), 46-56 (2010).
    • (2010) Chem. Biol. , vol.17 , Issue.1 , pp. 46-56
    • Basse, N.1    Kaar, J.L.2    Settanni, G.3    Joerger, A.C.4    Rutherford, T.J.5    Fersht, A.R.6
  • 126
    • 79955613841 scopus 로고    scopus 로고
    • Molecular obesity, potency and other addictions in drug discovery
    • Hann MM. Molecular obesity, potency and other addictions in drug discovery. MedChemComm 2(5), 349-355 (2011).
    • (2011) MedChemComm , vol.2 , Issue.5 , pp. 349-355
    • Hann, M.M.1
  • 127
    • 67849113794 scopus 로고    scopus 로고
    • The rise of fragment-based drug discovery
    • Murray CW, Rees DC. The rise of fragment-based drug discovery. Nat. Chem. 1(3), 187-192 (2009).
    • (2009) Nat. Chem. , vol.1 , Issue.3 , pp. 187-192
    • Murray, C.W.1    Rees, D.C.2
  • 129
    • 84863242691 scopus 로고    scopus 로고
    • Combining NMR and X-ray crystallography in fragment-based drug discovery: Discovery of highly potent and selective BACE-1 inhibitors
    • Wyss DF, Wang YS, Eaton HL et al. Combining NMR and X-ray crystallography in fragment-based drug discovery: discovery of highly potent and selective BACE-1 inhibitors. Top. Curr. Chem. 317, 83-114 (2012).
    • (2012) Top. Curr. Chem. , vol.317 , pp. 83-114
    • Wyss, D.F.1    Wang, Y.S.2    Eaton, H.L.3
  • 130
    • 84858141881 scopus 로고    scopus 로고
    • Combining biophysical screening and X-ray crystallography for fragment-based drug discovery
    • Hennig M, Ruf A, Huber W. Combining biophysical screening and X-ray crystallography for fragment-based drug discovery. Top. Curr. Chem. 317, 115-143 (2012).
    • (2012) Top. Curr. Chem. , vol.317 , pp. 115-143
    • Hennig, M.1    Ruf, A.2    Huber, W.3
  • 131
    • 84872508886 scopus 로고    scopus 로고
    • Parallel screening of low molecular weight fragment libraries: Do differences in methodology affect hit identification J
    • Wielens J, Headey SJ, Rhodes DI et al. Parallel screening of low molecular weight fragment libraries: do differences in methodology affect hit identification J. Biomol. Screen. 18(2), 147-159 (2013).
    • (2013) Biomol. Screen. , vol.18 , Issue.2 , pp. 147-159
    • Wielens, J.1    Headey, S.J.2    Rhodes, D.I.3
  • 132
    • 84869987352 scopus 로고    scopus 로고
    • Enumeration of 166 billion organic small molecules in the chemical universe database GDB-17
    • Ruddigkeit L, Van Deursen R, Blum LC, Reymond JL. Enumeration of 166 billion organic small molecules in the chemical universe database GDB-17. J. Chem. Inf. Model. 52(11), 2864-2875 (2012).
    • (2012) J. Chem. Inf. Model. , vol.52 , Issue.11 , pp. 2864-2875
    • Ruddigkeit, L.1    Van Deursen, R.2    Blum, L.C.3    Reymond, J.L.4
  • 133
    • 35748934487 scopus 로고    scopus 로고
    • The influence of drug-like concepts on decision-making in medicinal chemistry
    • Leeson PD, Springthorpe B. The influence of drug-like concepts on decision-making in medicinal chemistry. Nat. Rev. Drug Discov. 6(11), 881-890 (2007).
    • (2007) Nat. Rev. Drug Discov. , vol.6 , Issue.11 , pp. 881-890
    • Leeson, P.D.1    Springthorpe, B.2
  • 134
    • 61649109015 scopus 로고    scopus 로고
    • The influence of lead discovery strategies on the properties of drug candidates
    • Keseru GM, Makara GM. The influence of lead discovery strategies on the properties of drug candidates. Nat. Rev. Drug Discov. 8(3), 203-212 (2009).
    • (2009) Nat. Rev. Drug Discov. , vol.8 , Issue.3 , pp. 203-212
    • Keseru, G.M.1    Makara, G.M.2
  • 135
    • 0035289779 scopus 로고    scopus 로고
    • Experimental and computational approaches to estimate solubility and permeability in drug discovery and development settings
    • Lipinski CA, Lombardo F, Dominy BW, Feeney PJ. Experimental and computational approaches to estimate solubility and permeability in drug discovery and development settings. Adv. Drug Deliv. Rev. 46(1-3), 3-26 (2001).
    • (2001) Adv. Drug Deliv. Rev. , vol.46 , Issue.1-3 , pp. 3-26
    • Lipinski, C.A.1    Lombardo, F.2    Dominy, B.W.3    Feeney, P.J.4
  • 136
    • 84902100715 scopus 로고    scopus 로고
    • Practical fragments: the-rule-of-three-at-ten
    • Practical fragments: the-rule-of-three-at-ten. http://practicalfragments. blogspot.com/2013/07/the-rule-ofthree-at-ten.html
  • 137
    • 84881315859 scopus 로고    scopus 로고
    • The 'rule of three' for fragment-based drug discovery: Where are we now
    • Jhoti H, Williams G, Rees DC, Murray CW. The 'rule of three' for fragment-based drug discovery: where are we now Nat. Rev. Drug Discov. 12(8), 644-645 (2013).
    • (2013) Nat. Rev. Drug Discov. , vol.12 , Issue.8 , pp. 644-645
    • Jhoti, H.1    Williams, G.2    Rees, D.C.3    Murray, C.W.4
  • 139
    • 84871599677 scopus 로고    scopus 로고
    • Natural-product-derived fragments for fragment-based ligand discovery
    • Over B, Wetzel S, Grutter C et al. Natural-product-derived fragments for fragment-based ligand discovery. Nat. Chem. 5(1), 21-28 (2013).
    • (2013) Nat. Chem. , vol.5 , Issue.1 , pp. 21-28
    • Over, B.1    Wetzel, S.2    Grutter, C.3
  • 140
    • 79955566051 scopus 로고    scopus 로고
    • Route to threedimensional fragments using diversity-oriented synthesis
    • Hung AW, Ramek A, Wang YK et al. Route to threedimensional fragments using diversity-oriented synthesis. Proc. Natl Acad. Sci. USA 108(17), 6799-6804 (2011).
    • (2011) Proc. Natl Acad. Sci. USA , vol.108 , Issue.17 , pp. 6799-6804
    • Hung, A.W.1    Ramek, A.2    Wang, Y.K.3
  • 141
    • 70349124638 scopus 로고    scopus 로고
    • Design and NMR-based screening of LEF, a library of chemical fragments with different local environment of fluorine
    • Vulpetti A, Hommel U, Landrum G, Lewis R, Dalvit C. Design and NMR-based screening of LEF, a library of chemical fragments with different local environment of fluorine. J. Am. Chem. Soc. 131(36), 12949-12959 (2009).
    • (2009) J. Am. Chem. Soc. , vol.131 , Issue.36 , pp. 12949-12959
    • Vulpetti, A.1    Hommel, U.2    Landrum, G.3    Lewis, R.4    Dalvit, C.5
  • 142
    • 84863052839 scopus 로고    scopus 로고
    • Fragment based drug discovery: Practical implementation based on (1)(9)F NMR spectroscopy
    • Jordan JB, Poppe L, Xia X et al. Fragment based drug discovery: practical implementation based on (1)(9)F NMR spectroscopy. J. Med. Chem. 55(2), 678-687 (2012).
    • (2012) J. Med. Chem. , vol.55 , Issue.2 , pp. 678-687
    • Jordan, J.B.1    Poppe, L.2    Xia, X.3
  • 143
    • 0034142070 scopus 로고    scopus 로고
    • Novel approach to phasing proteins: Derivatization by short cryo-soaking with halides
    • Dauter Z, Dauter M, Rajashankar KR. Novel approach to phasing proteins: derivatization by short cryo-soaking with halides. Acta Crystallogr. D Biol. Crystallogr. 56(Pt 2), 232-237 (2000).
    • (2000) Acta Crystallogr. D Biol. Crystallogr. , vol.56 , Issue.PART 2 , pp. 232-237
    • Dauter, Z.1    Dauter, M.2    Rajashankar, K.R.3
  • 144
    • 77950807078 scopus 로고    scopus 로고
    • The magic triangle goes MAD: Experimental phasing with a bromine derivative
    • Beck T, Gruene T, Sheldrick GM. The magic triangle goes MAD: experimental phasing with a bromine derivative. Acta Crystallogr. D Biol. Crystallogr. 66(Part 4), 374-380 (2010).
    • (2010) Acta Crystallogr. D Biol. Crystallogr. , vol.66 , Issue.PART 4 , pp. 374-380
    • Beck, T.1    Gruene, T.2    Sheldrick, G.M.3
  • 146
    • 84864878309 scopus 로고    scopus 로고
    • Fragment-based lead discovery and optimization using X-ray crystallography, computational chemistry, and high-throughput organic synthesis
    • Jahnke W, Erlanson DA (Eds). Wiley-VCH Verlag GmbH and Co. KGaA, Weinheim, Germany
    • Blaney J, Nienaber V, Burley SK. Fragment-based lead discovery and optimization using X-ray crystallography, computational chemistry, and high-throughput organic synthesis. In: Fragment-based Approaches in Drug Discovery. Jahnke W, Erlanson DA (Eds). Wiley-VCH Verlag GmbH and Co. KGaA, Weinheim, Germany, 215-248 (2006).
    • (2006) Fragment-based Approaches in Drug Discovery , pp. 215-248
    • Blaney, J.1    Nienaber, V.2    Burley, S.K.3
  • 147
    • 84858133314 scopus 로고    scopus 로고
    • Fragment screening and HIV therapeutics
    • Bauman JD, Patel D, Arnold E. Fragment screening and HIV therapeutics. Top. Curr. Chem. 317, 181-200 (2012).
    • (2012) Top. Curr. Chem. , vol.317 , pp. 181-200
    • Bauman, J.D.1    Patel, D.2    Arnold, E.3
  • 148
    • 84892534600 scopus 로고    scopus 로고
    • Crystallographic fragment based drug discovery: Use of a brominated fragment library targeting hiv protease
    • Tiefenbrunn T, Forli S, Happer M et al. Crystallographic fragment based drug discovery: use of a brominated fragment library targeting hiv protease. Chemical Biol. Drug Design 83(2), 141-148 (2013).
    • (2013) Chemical Biol. Drug Design , vol.83 , Issue.2 , pp. 141-148
    • Tiefenbrunn, T.1    Forli, S.2    Happer, M.3
  • 150
    • 0346786657 scopus 로고    scopus 로고
    • Recent advances in the cross-coupling reactions of organoboron derivatives with organic electrophiles1995-1998
    • Suzuki A. Recent advances in the cross-coupling reactions of organoboron derivatives with organic electrophiles, 1995-1998. J. Organomet. Chem. 576(1-2), 147-168 (1999).
    • (1999) J. Organomet. Chem. , vol.576 , Issue.1-2 , pp. 147-168
    • Suzuki, A.1
  • 151
    • 2042507954 scopus 로고
    • Palladium-catalyzed cross-coupling reactions of organoboron compounds
    • Miyaura N, Suzuki A. Palladium-catalyzed cross-coupling reactions of organoboron compounds. Chem. Rev. 95(7), 2457-2483 (1995).
    • (1995) Chem. Rev. , vol.95 , Issue.7 , pp. 2457-2483
    • Miyaura, N.1    Suzuki, A.2
  • 152
    • 33750026643 scopus 로고
    • Palladium-catalyzed or nickel-catalyzed cross coupling-A new selective method for carbon carbon bond formation
    • Negishi EI. Palladium-catalyzed or nickel-catalyzed cross coupling-a new selective method for carbon carbon bond formation. Acc. Chem. Res. 15(11), 340-348 (1982).
    • (1982) Acc. Chem. Res. , vol.15 , Issue.11 , pp. 340-348
    • Negishi, E.I.1
  • 153
    • 33847088408 scopus 로고
    • Selective carboncarbon bond formation via transition-metal catalysis .3. Highly selective synthesis of unsymmetrical biaryls and diarylmethanes by nickel-catalyzed or palladium-catalyzed reaction of aryl derivatives and benzylzinc derivatives with aryl halides
    • Negishi E, King AO, Okukado N. Selective carboncarbon bond formation via transition-metal catalysis .3. Highly selective synthesis of unsymmetrical biaryls and diarylmethanes by nickel-catalyzed or palladium-catalyzed reaction of aryl derivatives and benzylzinc derivatives with aryl halides. J. Org. Chem. 42(10), 1821-1823 (1977).
    • (1977) J. Org. Chem. , vol.42 , Issue.10 , pp. 1821-1823
    • Negishi, E.1    King, A.O.2    Okukado, N.3
  • 154
    • 37049091909 scopus 로고
    • Highly general stereoselective, regio-selective, and chemo-selective synthesis of terminal and internal conjugated enynes by Pd-catalysed reaction of alkynylzinc reagents with alkenyl halides
    • King AO, Okukado N, Negishi EI. Highly general stereoselective, regio-selective, and chemo-selective synthesis of terminal and internal conjugated enynes by Pd-catalysed reaction of alkynylzinc reagents with alkenyl halides. J. Chem. Soc. Chem. Commun. (19), 683-684 (1977).
    • (1977) J. Chem. Soc. Chem. Commun. , vol.19 , pp. 683-684
    • King, A.O.1    Okukado, N.2    Negishi, E.I.3
  • 155
    • 84985570392 scopus 로고
    • The palladium-catalyzed cross-coupling reactions of organotin reagents with organic electrophiles
    • Stille JK. The palladium-catalyzed cross-coupling reactions of organotin reagents with organic electrophiles. Angew. Chem. Int. Ed. 25(6), 508-523 (1986).
    • (1986) Angew. Chem. Int. Ed. , vol.25 , Issue.6 , pp. 508-523
    • Stille, J.K.1
  • 156
    • 84943950090 scopus 로고
    • Synthetic studies via the cross-coupling reaction of organoboron derivatives with organic halides
    • Suzuki A. Synthetic studies via the cross-coupling reaction of organoboron derivatives with organic halides. Pure Appl. Chem. 63(3), 419-422 (1991).
    • (1991) Pure Appl. Chem. , vol.63 , Issue.3 , pp. 419-422
    • Suzuki, A.1
  • 157
    • 33947727055 scopus 로고    scopus 로고
    • The Sonogashira reaction: A booming methodology in synthetic organic chemistry
    • Chinchilla R, Najera C. The Sonogashira reaction: a booming methodology in synthetic organic chemistry. Chem. Rev. 107(3), 874-922 (2007).
    • (2007) Chem. Rev. , vol.107 , Issue.3 , pp. 874-922
    • Chinchilla, R.1    Najera, C.2
  • 158
    • 17044430638 scopus 로고    scopus 로고
    • Efficient Stille cross-coupling reaction catalyzed by the Pd(OAc)2/Dabco catalytic system
    • Li JH, Liang Y, Wang DP, Liu WJ, Xie YX, Yin DL. Efficient Stille cross-coupling reaction catalyzed by the Pd(OAc)2/Dabco catalytic system. J. Org. Chem. 70(7), 2832-2834 (2005).
    • (2005) J. Org. Chem. , vol.70 , Issue.7 , pp. 2832-2834
    • Li, J.H.1    Liang, Y.2    Wang, D.P.3    Liu, W.J.4    Xie, Y.X.5    Yin, D.L.6
  • 159
    • 0001038733 scopus 로고    scopus 로고
    • Rational development of practical catalysts for aromatic carbon nitrogen bond formation
    • Wolfe JP, Wagaw S, Marcoux J-F, Buchwald SL. Rational development of practical catalysts for aromatic carbon nitrogen bond formation. Acc. Chem. Res. 31(12), 805-818 (1998).
    • (1998) Acc. Chem. Res. , vol.31 , Issue.12 , pp. 805-818
    • Wolfe, J.P.1    Wagaw, S.2    Marcoux, J.-F.3    Buchwald, S.L.4
  • 160
    • 33746283734 scopus 로고    scopus 로고
    • Significantly improved method for the Pd-catalyzed coupling of phenols with aryl halides: Understanding ligand effects
    • Burgos CH, Barder TE, Huang X, Buchwald SL. Significantly improved method for the Pd-catalyzed coupling of phenols with aryl halides: understanding ligand effects. Angew. Chem. Int. Ed. 45(26), 4321-4326 (2006).
    • (2006) Angew. Chem. Int. Ed. , vol.45 , Issue.26 , pp. 4321-4326
    • Burgos, C.H.1    Barder, T.E.2    Huang, X.3    Buchwald, S.L.4
  • 161
    • 0142227985 scopus 로고    scopus 로고
    • Application of a new bicyclic triaminophosphine ligand in Pd-catalyzed Buchwald-Hartwig amination reactions of aryl chlorides, bromides, and iodides
    • Urgaonkar S, Xu JH, Verkade JG. Application of a new bicyclic triaminophosphine ligand in Pd-catalyzed Buchwald-Hartwig amination reactions of aryl chlorides, bromides, and iodides. J. Org. Chem. 68(22), 8416-8423 (2003).
    • (2003) J. Org. Chem. , vol.68 , Issue.22 , pp. 8416-8423
    • Urgaonkar, S.1    Xu, J.H.2    Verkade, J.G.3
  • 162
    • 0037112673 scopus 로고    scopus 로고
    • Palladium-catalyzed coupling reactions of aryl chlorides
    • Littke AF, Fu GC. Palladium-catalyzed coupling reactions of aryl chlorides. Angew. Chem. Int. Ed. Engl. 41(22), 4176-4211 (2002).
    • (2002) Angew. Chem. Int. Ed. Engl. , vol.41 , Issue.22 , pp. 4176-4211
    • Littke, A.F.1    Fu, G.C.2
  • 163
    • 0029060527 scopus 로고
    • Synthesis of phenolic natural products using palladium catalyzed coupling reactions
    • Bates RW, Gabel CJ, Ji J, Rama-Devi T. Synthesis of phenolic natural products using palladium catalyzed coupling reactions. Tetrahedron 51(30), 8199-8212 (1995).
    • (1995) Tetrahedron , vol.51 , Issue.30 , pp. 8199-8212
    • Bates, R.W.1    Gabel, C.J.2    Ji, J.3    Rama-Devi, T.4
  • 164
    • 47649096991 scopus 로고    scopus 로고
    • Structural biology of the tumor suppressor p53
    • Joerger AC, Fersht AR. Structural biology of the tumor suppressor p53. Annu. Rev. Biochem. 77, 557-582 (2008).
    • (2008) Annu. Rev. Biochem. , vol.77 , pp. 557-582
    • Joerger, A.C.1    Fersht, A.R.2
  • 165
    • 34047224955 scopus 로고    scopus 로고
    • Structure-function-rescue: The diverse nature of common p53 cancer mutants
    • Joerger AC, Fersht AR. Structure-function-rescue: the diverse nature of common p53 cancer mutants. Oncogene 26(15), 2226-2242 (2007).
    • (2007) Oncogene , vol.26 , Issue.15 , pp. 2226-2242
    • Joerger, A.C.1    Fersht, A.R.2
  • 166
    • 0034594995 scopus 로고    scopus 로고
    • Quantitative analysis of residual folding and DNA binding in mutant p53 core domain: Definition of mutant states for rescue in cancer therapy
    • Bullock AN, Henckel J, Fersht AR. Quantitative analysis of residual folding and DNA binding in mutant p53 core domain: definition of mutant states for rescue in cancer therapy. Oncogene 19(10), 1245-1256 (2000).
    • (2000) Oncogene , vol.19 , Issue.10 , pp. 1245-1256
    • Bullock, A.N.1    Henckel, J.2    Fersht, A.R.3
  • 167
    • 0032516219 scopus 로고    scopus 로고
    • Human tumor-derived p53 proteins exhibit binding site selectivity and temperature sensitivity for transactivation in a yeast-based assay
    • Di Como CJ, Prives C. Human tumor-derived p53 proteins exhibit binding site selectivity and temperature sensitivity for transactivation in a yeast-based assay. Oncogene 16(19), 2527-2539 (1998).
    • (1998) Oncogene , vol.16 , Issue.19 , pp. 2527-2539
    • Di Como, C.J.1    Prives, C.2
  • 168
    • 33750036093 scopus 로고    scopus 로고
    • Structural basis for understanding oncogenic p53 mutations and designing rescue drugs
    • Joerger AC, Ang HC, Fersht AR. Structural basis for understanding oncogenic p53 mutations and designing rescue drugs. Proc. Natl Acad. Sci. USA 103(41), 15056-15061 (2006).
    • (2006) Proc. Natl Acad. Sci. USA , vol.103 , Issue.41 , pp. 15056-15061
    • Joerger, A.C.1    Ang, H.C.2    Fersht, A.R.3
  • 169
    • 84865281347 scopus 로고    scopus 로고
    • Kinetic mechanism of p53 oncogenic mutant aggregation and its inhibition
    • Wilcken R, Wang G, Boeckler FM, Fersht AR. Kinetic mechanism of p53 oncogenic mutant aggregation and its inhibition. Proc. Natl Acad. Sci. USA 109(34), 13584-13589 (2012).
    • (2012) Proc. Natl Acad. Sci. USA , vol.109 , Issue.34 , pp. 13584-13589
    • Wilcken, R.1    Wang, G.2    Boeckler, F.M.3    Fersht, A.R.4


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.