메뉴 건너뛰기




Volumn 59, Issue 18, 2016, Pages 8189-8206

Design Principles for Fragment Libraries: Maximizing the Value of Learnings from Pharma Fragment-Based Drug Discovery (FBDD) Programs for Use in Academia

Author keywords

[No Author keywords available]

Indexed keywords

CHECKPOINT KINASE 2; DRUG; ENDOTHIAPEPSIN; HEAT SHOCK PROTEIN 90; INTEGRASE; LIGAND; MACROPHAGE ELASTASE; MITOGEN ACTIVATED PROTEIN KINASE 14; TRYPSIN; INTEGRASE INHIBITOR; MATRIX METALLOPROTEINASE INHIBITOR; PROTEIN KINASE INHIBITOR; TRYPSIN INHIBITOR;

EID: 84984690427     PISSN: 00222623     EISSN: 15204804     Source Type: Journal    
DOI: 10.1021/acs.jmedchem.6b00197     Document Type: Review
Times cited : (186)

References (145)
  • 1
    • 2942564021 scopus 로고    scopus 로고
    • Pursuing the leadlikeness concept in pharmaceutical research
    • Hann, M. M.; Oprea, T. L. Pursuing the leadlikeness concept in pharmaceutical research Curr. Opin. Chem. Biol. 2004, 8, 255-263 10.1016/j.cbpa.2004.04.003
    • (2004) Curr. Opin. Chem. Biol. , vol.8 , pp. 255-263
    • Hann, M.M.1    Oprea, T.L.2
  • 2
    • 84924038029 scopus 로고    scopus 로고
    • Efficient exploration of chemical space by fragment-based screening
    • Hall, R. J.; Mortenson, P. N.; Murray, C. W. Efficient exploration of chemical space by fragment-based screening Prog. Biophys. Mol. Biol. 2014, 116, 82-91 10.1016/j.pbiomolbio.2014.09.007
    • (2014) Prog. Biophys. Mol. Biol. , vol.116 , pp. 82-91
    • Hall, R.J.1    Mortenson, P.N.2    Murray, C.W.3
  • 3
    • 67849113794 scopus 로고    scopus 로고
    • The rise of fragment-based drug discovery
    • Murray, C. W.; Rees, D. C. The rise of fragment-based drug discovery Nat. Chem. 2009, 1, 187-192 10.1038/nchem.217
    • (2009) Nat. Chem. , vol.1 , pp. 187-192
    • Murray, C.W.1    Rees, D.C.2
  • 4
    • 84958958841 scopus 로고    scopus 로고
    • On the enthalpic preference of fragment binding
    • Ferenczy, G. G.; Keseru, G. M. On the enthalpic preference of fragment binding MedChemComm 2016, 7, 332-337 10.1039/C5MD00542F
    • (2016) MedChemComm , vol.7 , pp. 332-337
    • Ferenczy, G.G.1    Keseru, G.M.2
  • 5
    • 84875727654 scopus 로고    scopus 로고
    • How are fragments optimized? A retrospective analysis of 145 fragment optimizations
    • Ferenczy, G. G.; Keseru, G. M. How are fragments optimized? A retrospective analysis of 145 fragment optimizations J. Med. Chem. 2013, 56, 2478-2486 10.1021/jm301851v
    • (2013) J. Med. Chem. , vol.56 , pp. 2478-2486
    • Ferenczy, G.G.1    Keseru, G.M.2
  • 6
    • 84860359784 scopus 로고    scopus 로고
    • Finding the sweet spot: The role of nature and nurture in medicinal chemistry
    • Hann, M. M.; Keseru, G. M. Finding the sweet spot: the role of nature and nurture in medicinal chemistry Nat. Rev. Drug Discovery 2012, 11, 355-365 10.1038/nrd3701
    • (2012) Nat. Rev. Drug Discovery , vol.11 , pp. 355-365
    • Hann, M.M.1    Keseru, G.M.2
  • 8
    • 79953703975 scopus 로고    scopus 로고
    • Fragment screening to predict druggability (ligandability) and lead discovery success
    • Edfeldt, F. N.; Folmer, R. H.; Breeze, A. L. Fragment screening to predict druggability (ligandability) and lead discovery success Drug Discovery Today 2011, 16, 284-287 10.1016/j.drudis.2011.02.002
    • (2011) Drug Discovery Today , vol.16 , pp. 284-287
    • Edfeldt, F.N.1    Folmer, R.H.2    Breeze, A.L.3
  • 9
    • 0141726877 scopus 로고    scopus 로고
    • A"Rule of Three" for fragment-based lead discovery?
    • Congreve, M.; Carr, R.; Murray, C.; Jhoti, H. A"Rule of Three" for fragment-based lead discovery? Drug Discovery Today 2003, 8, 876-877 10.1016/S1359-6446(03)02831-9
    • (2003) Drug Discovery Today , vol.8 , pp. 876-877
    • Congreve, M.1    Carr, R.2    Murray, C.3    Jhoti, H.4
  • 10
    • 84881315859 scopus 로고    scopus 로고
    • The 'rule of three' for fragment-based drug discovery: Where are we now?
    • Jhoti, H.; Williams, G.; Rees, D. C.; Murray, C. W. The 'rule of three' for fragment-based drug discovery: where are we now? Nat. Rev. Drug Discovery 2013, 12, 644-645 10.1038/nrd3926-c1
    • (2013) Nat. Rev. Drug Discovery , vol.12 , pp. 644-645
    • Jhoti, H.1    Williams, G.2    Rees, D.C.3    Murray, C.W.4
  • 11
    • 0035324944 scopus 로고    scopus 로고
    • Molecular complexity and its impact on the probability of finding leads for drug discovery
    • Hann, M. M.; Leach, A. R.; Harper, G. Molecular complexity and its impact on the probability of finding leads for drug discovery J. Chem. Inf. Comput. Sci. 2001, 41, 856-864 10.1021/ci000403i
    • (2001) J. Chem. Inf. Comput. Sci. , vol.41 , pp. 856-864
    • Hann, M.M.1    Leach, A.R.2    Harper, G.3
  • 12
    • 84956997912 scopus 로고    scopus 로고
    • Design and synthesis of dihydroisoquinolones for fragment-based drug discovery (FBDD)
    • Palmer, N.; Peakman, T. M; Norton, D.; Rees, D. C. Design and synthesis of dihydroisoquinolones for fragment-based drug discovery (FBDD) Org. Biomol. Chem. 2016, 14, 1599-1610 10.1039/C5OB02461G
    • (2016) Org. Biomol. Chem. , vol.14 , pp. 1599-1610
    • Palmer, N.1    Peakman, T.M.2    Norton, D.3    Rees, D.C.4
  • 13
    • 84929533115 scopus 로고    scopus 로고
    • Learning from our mistakes: The 'unknown knowns' in fragment screening
    • Davis, B. J.; Erlanson, D. A. Learning from our mistakes: the 'unknown knowns' in fragment screening Bioorg. Med. Chem. Lett. 2013, 23, 2844-2852 10.1016/j.bmcl.2013.03.028
    • (2013) Bioorg. Med. Chem. Lett. , vol.23 , pp. 2844-2852
    • Davis, B.J.1    Erlanson, D.A.2
  • 14
    • 84988718406 scopus 로고    scopus 로고
    • (accessed Jan 20, 2016)
    • Practical Fragments Blog; http://practicalfragments.blogspot.hu/2014/01/poll-results-affiliation-fragment.html (accessed Jan 20, 2016).
    • Practical Fragments Blog
  • 15
    • 84988686834 scopus 로고    scopus 로고
    • (accessed Jan 20, 2016)
    • Optibrium Home Page; http://www.optibrium.com/downloads/Swain-Fragments.pdf (accessed Jan 20, 2016).
    • Optibrium Home Page
  • 16
    • 36549033318 scopus 로고    scopus 로고
    • Integration of fragment screening and library design
    • Siegal, G.; Eiso, A. B.; Schultz, J. Integration of fragment screening and library design Drug Discovery Today 2007, 12, 1032-1039 10.1016/j.drudis.2007.08.005
    • (2007) Drug Discovery Today , vol.12 , pp. 1032-1039
    • Siegal, G.1    Eiso, A.B.2    Schultz, J.3
  • 18
    • 84953884907 scopus 로고    scopus 로고
    • Rapid experimental SAD phasing and hot-spot identification with halogenated fragments
    • Bauman, J. D.; Harrison, J. J. E. K.; Arnold, E. Rapid experimental SAD phasing and hot-spot identification with halogenated fragments IUCrJ 2016, 3, 51-60 10.1107/S2052252515021259
    • (2016) IUCrJ , vol.3 , pp. 51-60
    • Bauman, J.D.1    Harrison, J.J.E.K.2    Arnold, E.3
  • 20
    • 84943743884 scopus 로고    scopus 로고
    • Discovery and optimization of a series of pyrimidine-based phosphodiesterase 10A (PDE10A) inhibitors through fragment screening, structure-based design, and parallel synthesis
    • Shipe, W. D.; Sharik, S. S.; Barrow, J. C.; McGaughey, G. B.; Theberge, C. R.; Uslaner, J. M.; Yan, Y.; Renger, J. J.; Smith, S. M.; Coleman, P. J.; Cox, C. D. Discovery and optimization of a series of pyrimidine-based phosphodiesterase 10A (PDE10A) inhibitors through fragment screening, structure-based design, and parallel synthesis J. Med. Chem. 2015, 58, 7888-7894 10.1021/acs.jmedchem.5b00983
    • (2015) J. Med. Chem. , vol.58 , pp. 7888-7894
    • Shipe, W.D.1    Sharik, S.S.2    Barrow, J.C.3    McGaughey, G.B.4    Theberge, C.R.5    Uslaner, J.M.6    Yan, Y.7    Renger, J.J.8    Smith, S.M.9    Coleman, P.J.10    Cox, C.D.11
  • 21
    • 77950571108 scopus 로고    scopus 로고
    • New substructure filters for removal of pan assay interference compounds (PAINS) from screening libraries and for their exclusion in bioassays
    • Baell, J. B.; Holloway, G. A. New substructure filters for removal of pan assay interference compounds (PAINS) from screening libraries and for their exclusion in bioassays J. Med. Chem. 2010, 53, 2719-2740 10.1021/jm901137j
    • (2010) J. Med. Chem. , vol.53 , pp. 2719-2740
    • Baell, J.B.1    Holloway, G.A.2
  • 22
    • 84908530414 scopus 로고    scopus 로고
    • Chemistry: Chemical con artists foil drug discovery
    • Baell, J. B.; Walters, M. A. Chemistry: Chemical con artists foil drug discovery Nature. 2014, 513, 481-483 10.1038/513481a
    • (2014) Nature. , vol.513 , pp. 481-483
    • Baell, J.B.1    Walters, M.A.2
  • 25
    • 79952383501 scopus 로고    scopus 로고
    • From experimental design to validated hits: A comprehensive walk-through of fragment lead identification using surface plasmon resonance
    • Lawrence, C. K. Ed. Academic Press: New York
    • Giannetti, A. M. From experimental design to validated hits: a comprehensive walk-through of fragment lead identification using surface plasmon resonance. In Methods in Enzymology, Lawrence, C. K., Ed. Academic Press: New York, 2011; Vol. 493, pp 169-218.
    • (2011) Methods in Enzymology , vol.493 , pp. 169-218
    • Giannetti, A.M.1
  • 29
    • 67650999672 scopus 로고    scopus 로고
    • Lessons for fragment library design: Analysis of output from multiple screening campaigns
    • Chen, I. J.; Hubbard, R. E. Lessons for fragment library design: analysis of output from multiple screening campaigns J. Comput.-Aided Mol. Des. 2009, 23, 603-620 10.1007/s10822-009-9280-5
    • (2009) J. Comput.-Aided Mol. Des. , vol.23 , pp. 603-620
    • Chen, I.J.1    Hubbard, R.E.2
  • 37
    • 84934285658 scopus 로고    scopus 로고
    • Current status and future direction of fragment-based drug discovery: A computational chemistry perspective
    • Howard, S. Abell, C. RSC: London
    • Wall, I. D.; Hann, M. M.; Leach, A. R.; Pickett, S. D. Current status and future direction of fragment-based drug discovery: a computational chemistry perspective. In Fragment-Based Drug Discovery; Howard, S.; Abell, C., Eds.; RSC: London, 2015; pp 73-100.
    • (2015) Fragment-Based Drug Discovery , pp. 73-100
    • Wall, I.D.1    Hann, M.M.2    Leach, A.R.3    Pickett, S.D.4
  • 39
    • 84880564425 scopus 로고    scopus 로고
    • Water network perturbation in ligand binding: Adenosine A2A antagonists as a case study
    • Bortolato, A.; Tehan, B. G.; Bodnarchuk, M. S.; Essex, J. W.; Mason, J. S. Water network perturbation in ligand binding: adenosine A2A antagonists as a case study J. Chem. Inf. Model. 2013, 53, 1700-1713 10.1021/ci4001458
    • (2013) J. Chem. Inf. Model. , vol.53 , pp. 1700-1713
    • Bortolato, A.1    Tehan, B.G.2    Bodnarchuk, M.S.3    Essex, J.W.4    Mason, J.S.5
  • 40
    • 84887072730 scopus 로고    scopus 로고
    • The importance of molecular complexity in the design of screening libraries
    • Nilar, S. H.; Ma, N. L.; Keller, T. H. The importance of molecular complexity in the design of screening libraries J. Comput.-Aided Mol. Des. 2013, 27, 783-792 10.1007/s10822-013-9683-1
    • (2013) J. Comput.-Aided Mol. Des. , vol.27 , pp. 783-792
    • Nilar, S.H.1    Ma, N.L.2    Keller, T.H.3
  • 41
    • 79960997906 scopus 로고    scopus 로고
    • Molecular complexity and fragment-based drug discovery: Ten years on
    • Leach, A. R.; Hann, M. M. Molecular complexity and fragment-based drug discovery: ten years on Curr. Opin. Chem. Biol. 2011, 15, 489-496 10.1016/j.cbpa.2011.05.008
    • (2011) Curr. Opin. Chem. Biol. , vol.15 , pp. 489-496
    • Leach, A.R.1    Hann, M.M.2
  • 42
    • 84996572063 scopus 로고    scopus 로고
    • Coping with complexity in molecular design
    • Schneider, G. Wiley-VCH Verlag GmbH & Co: Weinheim, Germany
    • Hann, M. M.; Leach, A. R. Coping with complexity in molecular design. In De Novo Molecular Design; Schneider, G., Ed.; Wiley-VCH Verlag GmbH & Co: Weinheim, Germany, 2014; pp 57-77.
    • (2014) De Novo Molecular Design , pp. 57-77
    • Hann, M.M.1    Leach, A.R.2
  • 43
    • 84862013042 scopus 로고    scopus 로고
    • Thermodynamics of fragment binding
    • Ferenczy, G. G.; Keseru, G. M. Thermodynamics of fragment binding J. Chem. Inf. Model. 2012, 52, 1039-1045 10.1021/ci200608b
    • (2012) J. Chem. Inf. Model. , vol.52 , pp. 1039-1045
    • Ferenczy, G.G.1    Keseru, G.M.2
  • 44
    • 80051799265 scopus 로고    scopus 로고
    • Assessing the lipophilicity of fragments and early hits
    • Mortenson, P. N.; Murray, C. W. Assessing the lipophilicity of fragments and early hits J. Comput.-Aided Mol. Des. 2011, 25, 663-667 10.1007/s10822-011-9435-z
    • (2011) J. Comput.-Aided Mol. Des. , vol.25 , pp. 663-667
    • Mortenson, P.N.1    Murray, C.W.2
  • 45
    • 54449102045 scopus 로고    scopus 로고
    • Group efficiency: A guideline for hits-to-leads chemistry
    • Verdonk, M. L.; Rees, D. C. Group efficiency: a guideline for hits-to-leads chemistry ChemMedChem 2008, 3, 1179-1180 10.1002/cmdc.200800132
    • (2008) ChemMedChem , vol.3 , pp. 1179-1180
    • Verdonk, M.L.1    Rees, D.C.2
  • 46
    • 84954028329 scopus 로고    scopus 로고
    • Optimization of inhibitors of Mycobacterium tuberculosis pantothenate synthetase based on group efficiency analysis
    • Hung, A. W.; Silvestre, H. L.; Wen, S.; George, G. P.; Boland, J.; Blundell, T. L.; Ciulli, A.; Abell, C. Optimization of inhibitors of Mycobacterium tuberculosis pantothenate synthetase based on group efficiency analysis ChemMedChem 2016, 11, 38-42 10.1002/cmdc.201500414
    • (2016) ChemMedChem , vol.11 , pp. 38-42
    • Hung, A.W.1    Silvestre, H.L.2    Wen, S.3    George, G.P.4    Boland, J.5    Blundell, T.L.6    Ciulli, A.7    Abell, C.8
  • 47
    • 84916230872 scopus 로고    scopus 로고
    • Physical properties in drug design
    • Meanwell, N. A. Springer: Berlin, Gemany
    • Young, R. J. Physical properties in drug design. In Tactics in Contemporary Drug Design; Meanwell, N. A., Ed.; Springer: Berlin, Gemany, 2015; pp 1-68.
    • (2015) Tactics in Contemporary Drug Design , pp. 1-68
    • Young, R.J.1
  • 48
    • 33645067372 scopus 로고    scopus 로고
    • Multiple solvent crystal structures: Probing binding sites, plasticity and hydration
    • Mattos, C.; Bellamacina, C. R.; Peisach, E.; Pereira, A.; Vitkup, D.; Petsko, G. A.; Ringe, D. Multiple solvent crystal structures: probing binding sites, plasticity and hydration J. Mol. Biol. 2006, 357, 1471-1482 10.1016/j.jmb.2006.01.039
    • (2006) J. Mol. Biol. , vol.357 , pp. 1471-1482
    • Mattos, C.1    Bellamacina, C.R.2    Peisach, E.3    Pereira, A.4    Vitkup, D.5    Petsko, G.A.6    Ringe, D.7
  • 49
    • 84855915978 scopus 로고    scopus 로고
    • Analysis of protein binding sites by computational solvent mapping
    • Hall, D. R.; Kozakov, D.; Vajda, S. Analysis of protein binding sites by computational solvent mapping Methods Mol. Biol. 2012, 819, 13-27 10.1007/978-1-61779-465-0-2
    • (2012) Methods Mol. Biol. , vol.819 , pp. 13-27
    • Hall, D.R.1    Kozakov, D.2    Vajda, S.3
  • 51
    • 84988718406 scopus 로고    scopus 로고
    • (accessed Jan 20, 2016)
    • Practical Fragments Blog; http://practicalfragments.blogspot.hu/2013/06/poll-results-how-small-are-your.html (accessed Jan 20, 2016).
    • Practical Fragments Blog
  • 52
    • 84868026890 scopus 로고    scopus 로고
    • Dissecting fragment-based lead discovery at the von Hippel-Lindau Protein: Hypoxia inducible factor 1α protein-protein interface
    • Van Molle, I.; Thomann, A.; Buckley, D. L.; So, E. C.; Lang, S.; Crews, C. M.; Ciulli, A. Dissecting fragment-based lead discovery at the von Hippel-Lindau Protein: hypoxia inducible factor 1α protein-protein interface Chem. Biol. 2012, 19, 1300-1312 10.1016/j.chembiol.2012.08.015
    • (2012) Chem. Biol. , vol.19 , pp. 1300-1312
    • Van Molle, I.1    Thomann, A.2    Buckley, D.L.3    So, E.C.4    Lang, S.5    Crews, C.M.6    Ciulli, A.7
  • 54
    • 0242439332 scopus 로고    scopus 로고
    • Requirements for specific binding of low affinity inhibitor fragments to the SH2 domain of pp60Src are identical to those for high affinity binding of full length inhibitors
    • Lange, G.; Lesuisse, D.; Deprez, P.; Schoot, B.; Loenze, P.; Bénard, D.; Marquette, J.-P.; Broto, P.; Sarubbi, E.; Mandine, E. Requirements for specific binding of low affinity inhibitor fragments to the SH2 domain of pp60Src are identical to those for high affinity binding of full length inhibitors J. Med. Chem. 2003, 46, 5184-5195 10.1021/jm020970s
    • (2003) J. Med. Chem. , vol.46 , pp. 5184-5195
    • Lange, G.1    Lesuisse, D.2    Deprez, P.3    Schoot, B.4    Loenze, P.5    Bénard, D.6    Marquette, J.-P.7    Broto, P.8    Sarubbi, E.9    Mandine, E.10
  • 55
    • 40749152751 scopus 로고    scopus 로고
    • Structure-based dissection of the natural product cyclopentapeptide Chitinase inhibitor argifin
    • Andersen, O. A.; Nathubhai, A.; Dixon, M. J.; Eggleston, I. M.; van Aalten, D. M. Structure-based dissection of the natural product cyclopentapeptide Chitinase inhibitor argifin Chem. Biol. 2008, 15, 295-301 10.1016/j.chembiol.2008.02.015
    • (2008) Chem. Biol. , vol.15 , pp. 295-301
    • Andersen, O.A.1    Nathubhai, A.2    Dixon, M.J.3    Eggleston, I.M.4    Van Aalten, D.M.5
  • 57
    • 33751076241 scopus 로고    scopus 로고
    • Deconstructing fragment-based inhibitor discovery
    • Babaoglu, K.; Shoichet, B. K. Deconstructing fragment-based inhibitor discovery Nat. Chem. Biol. 2006, 2, 720-723 10.1038/nchembio831
    • (2006) Nat. Chem. Biol. , vol.2 , pp. 720-723
    • Babaoglu, K.1    Shoichet, B.K.2
  • 60
    • 79851482963 scopus 로고    scopus 로고
    • Deconstruction of non-nucleoside reverse transcriptase inhibitors of human immunodeficiency virus type 1 for exploration of the optimization landscape of fragments
    • Brandt, P.; Geitmann, M.; Danielson, U. H. Deconstruction of non-nucleoside reverse transcriptase inhibitors of human immunodeficiency virus type 1 for exploration of the optimization landscape of fragments J. Med. Chem. 2011, 54, 709-718 10.1021/jm101052g
    • (2011) J. Med. Chem. , vol.54 , pp. 709-718
    • Brandt, P.1    Geitmann, M.2    Danielson, U.H.3
  • 63
    • 65349195698 scopus 로고    scopus 로고
    • Molecular docking and ligand specificity in fragment-based inhibitor discovery
    • Chen, Y.; Shoichet, B. K. Molecular docking and ligand specificity in fragment-based inhibitor discovery Nat. Chem. Biol. 2009, 5, 358-364 10.1038/nchembio.155
    • (2009) Nat. Chem. Biol. , vol.5 , pp. 358-364
    • Chen, Y.1    Shoichet, B.K.2
  • 64
    • 79952390132 scopus 로고    scopus 로고
    • Lead generation and examples: Opinion regarding how to follow up hits
    • Orita, M.; Ohno, K.; Warizaya, M.; Amano, Y.; Niimi, T. Lead generation and examples: opinion regarding how to follow up hits Methods Enzymol. 2011, 493, 383-419 10.1016/B978-0-12-381274-2.00015-7
    • (2011) Methods Enzymol. , vol.493 , pp. 383-419
    • Orita, M.1    Ohno, K.2    Warizaya, M.3    Amano, Y.4    Niimi, T.5
  • 67
    • 84907510306 scopus 로고    scopus 로고
    • Multiple fragment docking and linking in primary and secondary pockets of dopamine receptors
    • Vass, M.; ágai-Csongor, é.; Horti, F.; Keseru, G. M. Multiple fragment docking and linking in primary and secondary pockets of dopamine receptors ACS Med. Chem. Lett. 2014, 5, 1010-1014 10.1021/ml500201u
    • (2014) ACS Med. Chem. Lett. , vol.5 , pp. 1010-1014
    • Vass, M.1    Ágai-Csongor, E.2    Horti, F.3    Keseru, G.M.4
  • 68
    • 84940544977 scopus 로고    scopus 로고
    • Fragment and structure-based drug discovery for a class C GPCR: Discovery of the mGlu5 negative allosteric modulator HTL14242 (3-Chloro-5-[6-(5-fluoropyridin-2-yl)pyrimidin-4-yl]benzonitrile)
    • Christopher, J. A.; Aves, S. J.; Bennett, K. A.; Doré, A. S.; Errey, J. C.; Jazayeri, A.; Marshall, F. H.; Okrasa, K.; Serrano-Vega, M. J.; Tehan, B. G.; Wiggin, G. R.; Congreve, M. Fragment and structure-based drug discovery for a class C GPCR: Discovery of the mGlu5 negative allosteric modulator HTL14242 (3-Chloro-5-[6-(5-fluoropyridin-2-yl)pyrimidin-4-yl]benzonitrile) J. Med. Chem. 2015, 58, 6653-6664 10.1021/acs.jmedchem.5b00892
    • (2015) J. Med. Chem. , vol.58 , pp. 6653-6664
    • Christopher, J.A.1    Aves, S.J.2    Bennett, K.A.3    Doré, A.S.4    Errey, J.C.5    Jazayeri, A.6    Marshall, F.H.7    Okrasa, K.8    Serrano-Vega, M.J.9    Tehan, B.G.10    Wiggin, G.R.11    Congreve, M.12
  • 69
    • 84870649266 scopus 로고    scopus 로고
    • (accesssed on 22 January, 2016)
    • Protein Data Bank; http://www.rcsb.org/pdb/home/home.do (accesssed on 22 January, 2016).
    • Protein Data Bank
  • 70
    • 84958747186 scopus 로고    scopus 로고
    • Opportunity knocks: Organic chemistry for fragment-based drug discovery (FBDD)
    • Murray, C. W.; Rees, D. C. Opportunity knocks: organic chemistry for fragment-based drug discovery (FBDD) Angew. Chem., Int. Ed. 2016, 55, 488-492 10.1002/anie.201506783
    • (2016) Angew. Chem., Int. Ed. , vol.55 , pp. 488-492
    • Murray, C.W.1    Rees, D.C.2
  • 71
    • 0032479179 scopus 로고    scopus 로고
    • Anatomy of hot spots in protein interfaces
    • Bogan, A. A.; Thorn, K. S. Anatomy of hot spots in protein interfaces J. Mol. Biol. 1998, 280, 1-9 10.1006/jmbi.1998.1843
    • (1998) J. Mol. Biol. , vol.280 , pp. 1-9
    • Bogan, A.A.1    Thorn, K.S.2
  • 72
    • 79952199844 scopus 로고    scopus 로고
    • Dehydron analysis: Quantifying the effect of hydrophobic groups on the strength and stability of hydrogen bonds
    • Fraser, C. M.; Fernández, A.; Scott, L. R. Dehydron analysis: quantifying the effect of hydrophobic groups on the strength and stability of hydrogen bonds Adv. Exp. Med. Biol. 2010, 680, 473-479 10.1007/978-1-4419-5913-3-53
    • (2010) Adv. Exp. Med. Biol. , vol.680 , pp. 473-479
    • Fraser, C.M.1    Fernández, A.2    Scott, L.R.3
  • 73
    • 33846524439 scopus 로고    scopus 로고
    • Motifs for molecular recognition exploiting hydrophobic enclosure in protein-ligand binding
    • Young, T.; Abel, R.; Kim, B.; Berne, B. J.; Friesner, R. A. Motifs for molecular recognition exploiting hydrophobic enclosure in protein-ligand binding Proc. Natl. Acad. Sci. U. S. A. 2007, 104, 808-813 10.1073/pnas.0610202104
    • (2007) Proc. Natl. Acad. Sci. U. S. A. , vol.104 , pp. 808-813
    • Young, T.1    Abel, R.2    Kim, B.3    Berne, B.J.4    Friesner, R.A.5
  • 74
    • 77949359890 scopus 로고    scopus 로고
    • Enhancement of hydrophobic interactions and hydrogen bond strength by cooperativity: Synthesis, modeling, and molecular dynamics simulations of a congeneric series of thrombin inhibitors
    • Muley, L.; Baum, B.; Smolinski, M.; Freindorf, M.; Heine, A.; Klebe, G.; Hangauer, D. G. Enhancement of hydrophobic interactions and hydrogen bond strength by cooperativity: synthesis, modeling, and molecular dynamics simulations of a congeneric series of thrombin inhibitors J. Med. Chem. 2010, 53, 2126-2135 10.1021/jm9016416
    • (2010) J. Med. Chem. , vol.53 , pp. 2126-2135
    • Muley, L.1    Baum, B.2    Smolinski, M.3    Freindorf, M.4    Heine, A.5    Klebe, G.6    Hangauer, D.G.7
  • 75
    • 79961000327 scopus 로고    scopus 로고
    • Ligand specificity, privileged substructures and protein druggability from fragment-based screening
    • Barelier, S.; Krimm, I. Ligand specificity, privileged substructures and protein druggability from fragment-based screening Curr. Opin. Chem. Biol. 2011, 15, 469-474 10.1016/j.cbpa.2011.02.020
    • (2011) Curr. Opin. Chem. Biol. , vol.15 , pp. 469-474
    • Barelier, S.1    Krimm, I.2
  • 76
    • 79955613841 scopus 로고    scopus 로고
    • Molecular obesity, potency and other addictions in drug discovery
    • Hann, M. M. Molecular obesity, potency and other addictions in drug discovery MedChemComm 2011, 2, 349-355 10.1039/c1md00017a
    • (2011) MedChemComm , vol.2 , pp. 349-355
    • Hann, M.M.1
  • 78
    • 84859782888 scopus 로고    scopus 로고
    • Missing fragments: Detecting cooperative binding in fragment-based drug design
    • Nair, P. C.; Malde, A. K.; Drinkwater, N.; Mark, A. E. Missing fragments: detecting cooperative binding in fragment-based drug design ACS Med. Chem. Lett. 2012, 3, 322-326 10.1021/ml300015u
    • (2012) ACS Med. Chem. Lett. , vol.3 , pp. 322-326
    • Nair, P.C.1    Malde, A.K.2    Drinkwater, N.3    Mark, A.E.4
  • 80
    • 77952713014 scopus 로고    scopus 로고
    • Entropic contribution to the linking coefficient in fragment based drug design: A case study
    • Borsi, V.; Calderone, V.; Fragai, M.; Luchinat, C.; Sarti, N. Entropic contribution to the linking coefficient in fragment based drug design: a case study J. Med. Chem. 2010, 53, 4285-4289 10.1021/jm901723z
    • (2010) J. Med. Chem. , vol.53 , pp. 4285-4289
    • Borsi, V.1    Calderone, V.2    Fragai, M.3    Luchinat, C.4    Sarti, N.5
  • 81
    • 84856010975 scopus 로고    scopus 로고
    • Fragment deconstruction of small, potent factor Xa inhibitors: Exploring the superadditivity energetic of fragment linking in protein-ligand complexes
    • Nazaré, M.; Matter, H.; Will, D. W.; Wagner, M.; Urmann, M.; Czech, J.; Schreuder, H.; Bauer, A.; Ritter, K.; Wehner, V. Fragment deconstruction of small, potent factor Xa inhibitors: exploring the superadditivity energetic of fragment linking in protein-ligand complexes Angew. Chem., Int. Ed. 2012, 51, 905-911 10.1002/anie.201107091
    • (2012) Angew. Chem., Int. Ed. , vol.51 , pp. 905-911
    • Nazaré, M.1    Matter, H.2    Will, D.W.3    Wagner, M.4    Urmann, M.5    Czech, J.6    Schreuder, H.7    Bauer, A.8    Ritter, K.9    Wehner, V.10
  • 82
    • 0036821028 scopus 로고    scopus 로고
    • The consequences of translational and rotational entropy lost by small molecules on binding to proteins
    • Murray, C. W.; Verdonk, M. L. The consequences of translational and rotational entropy lost by small molecules on binding to proteins J. Comput.-Aided Mol. Des. 2002, 16, 741-753 10.1023/A:1022446720849
    • (2002) J. Comput.-Aided Mol. Des. , vol.16 , pp. 741-753
    • Murray, C.W.1    Verdonk, M.L.2
  • 83
    • 71049126548 scopus 로고    scopus 로고
    • Escape from flatland: Increasing saturation as an approach to improving clinical success
    • Lovering, F.; Bikker, J.; Humblet, C. Escape from flatland: Increasing saturation as an approach to improving clinical success J. Med. Chem. 2009, 52, 6752-6756 10.1021/jm901241e
    • (2009) J. Med. Chem. , vol.52 , pp. 6752-6756
    • Lovering, F.1    Bikker, J.2    Humblet, C.3
  • 84
    • 70350409235 scopus 로고    scopus 로고
    • The impact of aromatic ring count on compound developability - Are too many aromatic rings a liability in drug design?
    • Ritchie, T. J.; Macdonald, S. J. F. The impact of aromatic ring count on compound developability-are too many aromatic rings a liability in drug design? Drug Discovery Today 2009, 14, 1011-1020 10.1016/j.drudis.2009.07.014
    • (2009) Drug Discovery Today , vol.14 , pp. 1011-1020
    • Ritchie, T.J.1    Macdonald, S.J.F.2
  • 85
    • 84872038006 scopus 로고    scopus 로고
    • Inflation of correlation in the pursuit of drug-likeness
    • Kenny, P. W.; Montanari, C. A. Inflation of correlation in the pursuit of drug-likeness J. Comput.-Aided Mol. Des. 2013, 27, 1-13 10.1007/s10822-012-9631-5
    • (2013) J. Comput.-Aided Mol. Des. , vol.27 , pp. 1-13
    • Kenny, P.W.1    Montanari, C.A.2
  • 88
    • 33646715920 scopus 로고    scopus 로고
    • The influence of target family and functional activity on the physicochemical properties of pre-clinical compounds
    • Morphy, R. The influence of target family and functional activity on the physicochemical properties of pre-clinical compounds J. Med. Chem. 2006, 49, 2969-2978 10.1021/jm0512185
    • (2006) J. Med. Chem. , vol.49 , pp. 2969-2978
    • Morphy, R.1
  • 89
    • 56549131177 scopus 로고    scopus 로고
    • The thermodynamics of protein-ligand interaction and solvation: Insights for ligand design
    • Olsson, T. S.; Williams, M. A.; Pitt, W. R.; Ladbury, J. E. The thermodynamics of protein-ligand interaction and solvation: insights for ligand design J. Mol. Biol. 2008, 384, 1002-1017 10.1016/j.jmb.2008.09.073
    • (2008) J. Mol. Biol. , vol.384 , pp. 1002-1017
    • Olsson, T.S.1    Williams, M.A.2    Pitt, W.R.3    Ladbury, J.E.4
  • 90
    • 84929452807 scopus 로고    scopus 로고
    • The FTMap family of web servers for determining and characterizing ligand-binding hot spots of proteins
    • Kozakov, D.; Grove, L. E.; Hall, D. R.; Bohnuud, T.; Mottarella, S. E.; Luo, L.; Xia, B.; Beglov, D.; Vajda, S. The FTMap family of web servers for determining and characterizing ligand-binding hot spots of proteins Nat. Protoc. 2015, 10, 733-755 10.1038/nprot.2015.043
    • (2015) Nat. Protoc. , vol.10 , pp. 733-755
    • Kozakov, D.1    Grove, L.E.2    Hall, D.R.3    Bohnuud, T.4    Mottarella, S.E.5    Luo, L.6    Xia, B.7    Beglov, D.8    Vajda, S.9
  • 91
    • 17144373303 scopus 로고    scopus 로고
    • Druggability indices for protein targets derived from NMR-based screening data
    • Hajduk, P. J.; Huth, J. R.; Fesik, S. W. Druggability indices for protein targets derived from NMR-based screening data J. Med. Chem. 2005, 48, 2518-2525 10.1021/jm049131r
    • (2005) J. Med. Chem. , vol.48 , pp. 2518-2525
    • Hajduk, P.J.1    Huth, J.R.2    Fesik, S.W.3
  • 92
    • 37249004920 scopus 로고    scopus 로고
    • Reaching for high-hanging fruit in drug discovery at protein-protein interfaces
    • Wells, J. A.; McClendon, C. L. Reaching for high-hanging fruit in drug discovery at protein-protein interfaces Nature 2007, 450, 1001-1009 10.1038/nature06526
    • (2007) Nature , vol.450 , pp. 1001-1009
    • Wells, J.A.1    McClendon, C.L.2
  • 93
    • 84897026211 scopus 로고    scopus 로고
    • Structure-based and fragment-based GPCR drug discovery
    • Andrews, S. P.; Brown, G. A.; Christopher, J. A. Structure-based and fragment-based GPCR drug discovery ChemMedChem 2014, 9, 256-275 10.1002/cmdc.201300382
    • (2014) ChemMedChem , vol.9 , pp. 256-275
    • Andrews, S.P.1    Brown, G.A.2    Christopher, J.A.3
  • 94
    • 61649114657 scopus 로고    scopus 로고
    • Kinase-targeted libraries: The design and synthesis of novel, potent, and selective kinase inhibitors
    • Akritopoulou-Zanze, I.; Hajduk, P. J. Kinase-targeted libraries: the design and synthesis of novel, potent, and selective kinase inhibitors Drug Discovery Today 2009, 14, 291-297 10.1016/j.drudis.2008.12.002
    • (2009) Drug Discovery Today , vol.14 , pp. 291-297
    • Akritopoulou-Zanze, I.1    Hajduk, P.J.2
  • 97
    • 84919756006 scopus 로고    scopus 로고
    • The azaindole framework in the design of kinase inhibitors
    • Mérour, J. Y.; Buron, F.; Plé, K.; Bonnet, P.; Routier, S. The azaindole framework in the design of kinase inhibitors Molecules 2014, 19, 19935-19979 10.3390/molecules191219935
    • (2014) Molecules , vol.19 , pp. 19935-19979
    • Mérour, J.Y.1    Buron, F.2    Plé, K.3    Bonnet, P.4    Routier, S.5
  • 99
    • 84893306189 scopus 로고    scopus 로고
    • Fragment growing to retain or alter the selectivity of anchored kinase hinge-binding fragments
    • Allen, C. E.; Welford, A. J.; Matthews, T. P.; Caldwell, J. J.; Collins, I. Fragment growing to retain or alter the selectivity of anchored kinase hinge-binding fragments MedChemComm 2014, 5, 180-185 10.1039/C3MD00308F
    • (2014) MedChemComm , vol.5 , pp. 180-185
    • Allen, C.E.1    Welford, A.J.2    Matthews, T.P.3    Caldwell, J.J.4    Collins, I.5
  • 101
    • 84875747743 scopus 로고    scopus 로고
    • αc helix displacement as a general approach for allosteric modulation of protein kinases
    • Palmieri, L.; Rastelli, G. αC helix displacement as a general approach for allosteric modulation of protein kinases Drug Discovery Today 2013, 18, 407-414 10.1016/j.drudis.2012.11.009
    • (2013) Drug Discovery Today , vol.18 , pp. 407-414
    • Palmieri, L.1    Rastelli, G.2
  • 102
    • 84874906779 scopus 로고    scopus 로고
    • (accessed Jan 20, 2016)
    • American Society of Hematology; https://ash.confex.com/ash/2014/webprogram/Paper76344.html (accessed Jan 20, 2016).
    • American Society of Hematology
  • 105
    • 84929703042 scopus 로고    scopus 로고
    • Progress in discovery of small-molecule modulators of protein-protein interactions via fragment screening
    • Magee, T. V. Progress in discovery of small-molecule modulators of protein-protein interactions via fragment screening Bioorg. Med. Chem. Lett. 2015, 25, 2461-2468 10.1016/j.bmcl.2015.04.089
    • (2015) Bioorg. Med. Chem. Lett. , vol.25 , pp. 2461-2468
    • Magee, T.V.1
  • 110
    • 84921731523 scopus 로고    scopus 로고
    • Small-molecule inhibitors that target protein-protein interactions in the RAD51 family of recombinases
    • Scott, D. E.; Coyne, A. G.; Venkitaraman, A.; Blundell, T. L.; Abell, C.; Hyvönen, M. Small-molecule inhibitors that target protein-protein interactions in the RAD51 family of recombinases ChemMedChem 2015, 10, 296-303 10.1002/cmdc.201402428
    • (2015) ChemMedChem , vol.10 , pp. 296-303
    • Scott, D.E.1    Coyne, A.G.2    Venkitaraman, A.3    Blundell, T.L.4    Abell, C.5    Hyvönen, M.6
  • 115
    • 84888639050 scopus 로고    scopus 로고
    • K-Ras(G12C) inhibitors allosterically control GTP affinity and effector interactions
    • Ostrem, J. M.; Peters, U.; Sos, M. L.; Wells, J. A.; Shokat, K. M. K-Ras(G12C) inhibitors allosterically control GTP affinity and effector interactions Nature 2013, 503, 548-551 10.1038/nature12796
    • (2013) Nature , vol.503 , pp. 548-551
    • Ostrem, J.M.1    Peters, U.2    Sos, M.L.3    Wells, J.A.4    Shokat, K.M.5
  • 116
    • 84902438455 scopus 로고    scopus 로고
    • A fragment-based method to discover irreversible covalent inhibitors of cysteine proteases
    • Kathman, S. G.; Xu, Z.; Statsyuk, A. V. A fragment-based method to discover irreversible covalent inhibitors of cysteine proteases J. Med. Chem. 2014, 57, 4969-4974 10.1021/jm500345q
    • (2014) J. Med. Chem. , vol.57 , pp. 4969-4974
    • Kathman, S.G.1    Xu, Z.2    Statsyuk, A.V.3
  • 117
  • 120
    • 0032058905 scopus 로고    scopus 로고
    • RECAP retrosynthetic combinatorial analysis procedure: A powerful new technique for identifying privileged molecular fragments with useful applications in combinatorial chemistry
    • Lewell, X. Q.; Judd, D. B.; Watson, S. P.; Hann, M. M. RECAP retrosynthetic combinatorial analysis procedure: A powerful new technique for identifying privileged molecular fragments with useful applications in combinatorial chemistry J. Chem. Inf. Comput. Sci. 1998, 38, 511-522 10.1021/ci970429i
    • (1998) J. Chem. Inf. Comput. Sci. , vol.38 , pp. 511-522
    • Lewell, X.Q.1    Judd, D.B.2    Watson, S.P.3    Hann, M.M.4
  • 122
    • 0033213957 scopus 로고    scopus 로고
    • The SHAPES strategy: An NMR-based approach for lead generation in drug discovery
    • Fejzo, J.; Lepre, C. A.; Peng, J. W.; Bemis, G. W.; Ajay; Murcko, M. A.; Moore, J. M. The SHAPES strategy: an NMR-based approach for lead generation in drug discovery Chem. Biol. 1999, 6, 755-769 10.1016/S1074-5521(00)80022-8
    • (1999) Chem. Biol. , vol.6 , pp. 755-769
    • Fejzo, J.1    Lepre, C.A.2    Peng, J.W.3    Bemis, G.W.4    Ajay5    Murcko, M.A.6    Moore, J.M.7
  • 123
    • 84861729758 scopus 로고    scopus 로고
    • E-Drugs3D: 3D structure collections dedicated to drug repurposing and fragment-based drug design
    • Pihan, E.; Colliandre, L.; Guichou, J. F.; Douguet, D. E-Drugs3D: 3D structure collections dedicated to drug repurposing and fragment-based drug design Bioinformatics 2012, 28, 1540-1541 10.1093/bioinformatics/bts186
    • (2012) Bioinformatics , vol.28 , pp. 1540-1541
    • Pihan, E.1    Colliandre, L.2    Guichou, J.F.3    Douguet, D.4
  • 125
    • 0037208308 scopus 로고    scopus 로고
    • Property distributions: Differences between drugs, natural products, and molecules from combinatorial chemistry
    • Feher, M.; Schmidt, J. M. Property distributions: differences between drugs, natural products, and molecules from combinatorial chemistry J. Chem. Inf. Comput. Sci. 2003, 43, 218-227 10.1021/ci0200467
    • (2003) J. Chem. Inf. Comput. Sci. , vol.43 , pp. 218-227
    • Feher, M.1    Schmidt, J.M.2
  • 126
    • 39449121965 scopus 로고    scopus 로고
    • Natural product-likeness score and its application for prioritization of compound libraries
    • Ertl, P.; Roggo, S.; Schuffenhauer, A. Natural product-likeness score and its application for prioritization of compound libraries J. Chem. Inf. Model. 2008, 48, 68-74 10.1021/ci700286x
    • (2008) J. Chem. Inf. Model. , vol.48 , pp. 68-74
    • Ertl, P.1    Roggo, S.2    Schuffenhauer, A.3
  • 127
  • 129
    • 84988697596 scopus 로고    scopus 로고
    • (accessed 22 January, 2016)
    • Cambridge Medchem Consulting; http://www.cambridgemedchemconsulting.com/resources/hit-identification/fragment-collections.html (accessed 22 January, 2016).
    • Cambridge Medchem Consulting
  • 130
    • 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, 1363-1388 10.1021/jm3012068
    • (2013) J. Med. Chem. , vol.56 , pp. 1363-1388
    • Wilcken, R.1    Zimmermann, M.O.2    Lange, A.3    Joerger, A.C.4    Boeckler, F.M.5
  • 131
    • 84988697596 scopus 로고    scopus 로고
    • (accessed Apr 4, 2016)
    • Cambridge MedChem Consulting; http://www.cambridgemedchemconsulting.com/resources/hit-identification/fragment-collection-profiles.html (accessed Apr 4, 2016).
    • Cambridge MedChem Consulting
  • 132
    • 84856134589 scopus 로고    scopus 로고
    • Lead-oriented synthesis: A new opportunity for synthetic chemistry
    • Nadin, A.; Hattotuwagama, C.; Churcher, I. Lead-oriented synthesis: A new opportunity for synthetic chemistry Angew. Chem., Int. Ed. 2012, 51, 1114-1122 10.1002/anie.201105840
    • (2012) Angew. Chem., Int. Ed. , vol.51 , pp. 1114-1122
    • Nadin, A.1    Hattotuwagama, C.2    Churcher, I.3
  • 133
    • 84956959993 scopus 로고    scopus 로고
    • The medicinal chemist's toolbox for late stage functionalization of drug-like molecules
    • Cernak, T.; Dykstra, K. D.; Tyagarajan, S.; Vachal, P.; Krska, S. W. The medicinal chemist's toolbox for late stage functionalization of drug-like molecules Chem. Soc. Rev. 2016, 45, 546-576 10.1039/C5CS00628G
    • (2016) Chem. Soc. Rev. , vol.45 , pp. 546-576
    • Cernak, T.1    Dykstra, K.D.2    Tyagarajan, S.3    Vachal, P.4    Krska, S.W.5
  • 134
  • 135
    • 84988730317 scopus 로고    scopus 로고
    • Personal communication from Justin Bower, 4 April 2016
    • Personal communication from Justin Bower, 4 April 2016.
  • 136
    • 84988718406 scopus 로고    scopus 로고
    • (accessed Jan 20, 2016)
    • Practical Fragments Blog; http://practicalfragments.blogspot.com/2014/10/caveat-emptor.html (accessed Jan 20, 2016).
    • Practical Fragments Blog
  • 137
    • 84891897444 scopus 로고    scopus 로고
    • Design and evaluation of the performance of an NMR screening fragment library
    • Doak, B. C.; Morton, C. J.; Simpson, J. S.; Scanlon, M. J. Design and evaluation of the performance of an NMR screening fragment library Aust. J. Chem. 2013, 66, 1465-1472 10.1071/CH13280
    • (2013) Aust. J. Chem. , vol.66 , pp. 1465-1472
    • Doak, B.C.1    Morton, C.J.2    Simpson, J.S.3    Scanlon, M.J.4
  • 139
  • 140
    • 84867577162 scopus 로고    scopus 로고
    • Hydrolytic instability of the important orexin 1 receptor antagonist SB-334867: Possible confounding effects on in vivo and in vitro studies
    • McElhinny, C. J., Jr.; Lewin, A. H.; Mascarella, S. W.; Runyon, S.; Brieaddy, L.; Carroll, F. I. Hydrolytic instability of the important orexin 1 receptor antagonist SB-334867: possible confounding effects on in vivo and in vitro studies Bioorg. Med. Chem. Lett. 2012, 22, 6661-6664 10.1016/j.bmcl.2012.08.109
    • (2012) Bioorg. Med. Chem. Lett. , vol.22 , pp. 6661-6664
    • McElhinny, C.J.1    Lewin, A.H.2    Mascarella, S.W.3    Runyon, S.4    Brieaddy, L.5    Carroll, F.I.6
  • 144
    • 84988718406 scopus 로고    scopus 로고
    • (accessed Jan 20, 2016)
    • Practical Fragments Blog; http://practicalfragments.blogspot.com/2014/02/poll-results-how-do-you-store-your.html (accessed Jan 20, 2016).
    • Practical Fragments Blog
  • 145
    • 84988718406 scopus 로고    scopus 로고
    • (accessed Jan 20, 2016)
    • Practical Fragments Blog; http://practicalfragments.blogspot.com/2015/01/fragments-in-clinic-2015-edition.html (accessed Jan 20, 2016).
    • Practical Fragments Blog


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.