메뉴 건너뛰기




Volumn 56, Issue 20, 2013, Pages 8073-8088

Discovery of novel small-molecule inhibitors of BRD4 using structure-based virtual screening

Author keywords

[No Author keywords available]

Indexed keywords

BROMODOMAIN 4; BROMODOMAIN 4 INHIBITOR; LYSINE; PEPTIDES AND PROTEINS; PROTEIN INHIBITOR; UNCLASSIFIED DRUG;

EID: 84886504602     PISSN: 00222623     EISSN: 15204804     Source Type: Journal    
DOI: 10.1021/jm4011302     Document Type: Article
Times cited : (115)

References (63)
  • 3
    • 84866338076 scopus 로고    scopus 로고
    • Druggability analysis and structural classification of bromodomain acetyl-lysine binding sites
    • Vidler, L. R.; Brown, N.; Knapp, S.; Hoelder, S. Druggability analysis and structural classification of bromodomain acetyl-lysine binding sites J. Med. Chem. 2012, 55, 7346-7359
    • (2012) J. Med. Chem. , vol.55 , pp. 7346-7359
    • Vidler, L.R.1    Brown, N.2    Knapp, S.3    Hoelder, S.4
  • 4
    • 0037138363 scopus 로고    scopus 로고
    • Bromodomain: An acetyl-lysine binding domain
    • Zeng, L.; Zhou, M.-M. Bromodomain: An acetyl-lysine binding domain FEBS Lett. 2002, 513, 124-128
    • (2002) FEBS Lett. , vol.513 , pp. 124-128
    • Zeng, L.1    Zhou, M.-M.2
  • 5
    • 34547858913 scopus 로고    scopus 로고
    • Structure and acetyl-lysine recognition of the bromodomain
    • Mujtaba, S.; Zeng, L.; Zhou, M.-M. Structure and acetyl-lysine recognition of the bromodomain Oncogene 2007, 26, 5521-5527
    • (2007) Oncogene , vol.26 , pp. 5521-5527
    • Mujtaba, S.1    Zeng, L.2    Zhou, M.-M.3
  • 6
    • 84864578590 scopus 로고    scopus 로고
    • The bromodomain interaction module
    • Filippakopoulos, P.; Knapp, S. The bromodomain interaction module FEBS Lett. 2012, 586, 2692-2704
    • (2012) FEBS Lett. , vol.586 , pp. 2692-2704
    • Filippakopoulos, P.1    Knapp, S.2
  • 13
    • 84862738480 scopus 로고    scopus 로고
    • BET domain co-regulators in obesity, inflammation and cancer
    • Belkina, A. C.; Denis, G. V. BET domain co-regulators in obesity, inflammation and cancer Nat. Rev. Cancer 2012, 12, 465-477
    • (2012) Nat. Rev. Cancer , vol.12 , pp. 465-477
    • Belkina, A.C.1    Denis, G.V.2
  • 15
    • 80052595172 scopus 로고    scopus 로고
    • Short hairpin RNA screen reveals bromodomain proteins as novel targets in acute myeloid leukemia
    • Blobel, G. A.; Kalota, A.; Sanchez, P. V.; Carroll, M. Short hairpin RNA screen reveals bromodomain proteins as novel targets in acute myeloid leukemia Cancer Cell 2011, 20, 287-288
    • (2011) Cancer Cell , vol.20 , pp. 287-288
    • Blobel, G.A.1    Kalota, A.2    Sanchez, P.V.3    Carroll, M.4
  • 16
    • 84869753078 scopus 로고    scopus 로고
    • Sensitivity of human lung adenocarcinoma cell lines to targeted inhibition of BET epigenetic signaling proteins
    • Lockwood, W. W.; Zejnullahu, K.; Bradner, J. E.; Varmus, H. Sensitivity of human lung adenocarcinoma cell lines to targeted inhibition of BET epigenetic signaling proteins Proc. Natl. Acad. Sci. U.S.A. 2012, 109, 19408-19413
    • (2012) Proc. Natl. Acad. Sci. U.S.A. , vol.109 , pp. 19408-19413
    • Lockwood, W.W.1    Zejnullahu, K.2    Bradner, J.E.3    Varmus, H.4
  • 19
    • 84857331171 scopus 로고    scopus 로고
    • Inhibition of bromodomain-mediated protein-protein interactions as a novel therapeutic strategy
    • Furdas, S. D.; Carlino, L.; Sippl, W.; Jung, M. Inhibition of bromodomain-mediated protein-protein interactions as a novel therapeutic strategy MedChemComm 2012, 3, 123-134
    • (2012) MedChemComm , vol.3 , pp. 123-134
    • Furdas, S.D.1    Carlino, L.2    Sippl, W.3    Jung, M.4
  • 26
    • 84856397832 scopus 로고    scopus 로고
    • Fragment-based discovery of bromodomain inhibitors part 1: Inhibitor binding modes and implications for lead discovery
    • Chung, C.; Dean, A. W.; Woolven, J. M.; Bamborough, P. Fragment-based discovery of bromodomain inhibitors part 1: Inhibitor binding modes and implications for lead discovery J. Med. Chem. 2011, 55, 576-586
    • (2011) J. Med. Chem. , vol.55 , pp. 576-586
    • Chung, C.1    Dean, A.W.2    Woolven, J.M.3    Bamborough, P.4
  • 30
    • 84886476656 scopus 로고    scopus 로고
    • eMolecules Home Page.
    • eMolecules Home Page. http://www.emolecules.com/.
  • 31
    • 0034649618 scopus 로고    scopus 로고
    • Protein-based virtual screening of chemical databases. 1. Evaluation of different docking/scoring combinations
    • Bissantz, C.; Folkers, G.; Rognan, D. Protein-based virtual screening of chemical databases. 1. Evaluation of different docking/scoring combinations J. Med. Chem. 2000, 43, 4759-4767
    • (2000) J. Med. Chem. , vol.43 , pp. 4759-4767
    • Bissantz, C.1    Folkers, G.2    Rognan, D.3
  • 33
    • 33749245117 scopus 로고    scopus 로고
    • Prediction of protein-ligand interactions. Docking and scoring: Successes and gaps
    • Leach, A. R.; Shoichet, B. K.; Peishoff, C. E. Prediction of protein-ligand interactions. Docking and scoring: Successes and gaps J. Med. Chem. 2006, 49, 5851-5855
    • (2006) J. Med. Chem. , vol.49 , pp. 5851-5855
    • Leach, A.R.1    Shoichet, B.K.2    Peishoff, C.E.3
  • 34
    • 84865212063 scopus 로고    scopus 로고
    • Docking performance of the glide program as evaluated on the Astex and DUD datasets: A complete set of glide SP results and selected results for a new scoring function integrating WaterMap and glide
    • Repasky, M.; Murphy, R.; Banks, J.; Greenwood, J.; Tubert-Brohman, I.; Bhat, S.; Friesner, R. Docking performance of the glide program as evaluated on the Astex and DUD datasets: A complete set of glide SP results and selected results for a new scoring function integrating WaterMap and glide J. Comput.-Aided Mol. Des. 2012, 26, 787-799
    • (2012) J. Comput.-Aided Mol. Des. , vol.26 , pp. 787-799
    • Repasky, M.1    Murphy, R.2    Banks, J.3    Greenwood, J.4    Tubert-Brohman, I.5    Bhat, S.6    Friesner, R.7
  • 36
    • 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
    • (2010) J. Med. Chem. , vol.53 , pp. 2719-2740
    • Baell, J.B.1    Holloway, G.A.2
  • 38
    • 23944454816 scopus 로고    scopus 로고
    • Virtual screening of biogenic amine-binding g-protein coupled receptors: Comparative evaluation of protein- and ligand-based virtual screening protocols
    • Evers, A.; Hessler, G.; Matter, H.; Klabunde, T. Virtual screening of biogenic amine-binding g-protein coupled receptors: Comparative evaluation of protein- and ligand-based virtual screening protocols J. Med. Chem. 2005, 48, 5448-5465
    • (2005) J. Med. Chem. , vol.48 , pp. 5448-5465
    • Evers, A.1    Hessler, G.2    Matter, H.3    Klabunde, T.4
  • 39
    • 0029894013 scopus 로고    scopus 로고
    • The properties of known drugs. 1. Molecular frameworks
    • Bemis, G. W.; Murcko, M. A. The properties of known drugs. 1. Molecular frameworks J. Med. Chem. 1996, 39, 2887-2893
    • (1996) J. Med. Chem. , vol.39 , pp. 2887-2893
    • Bemis, G.W.1    Murcko, M.A.2
  • 41
    • 84878172023 scopus 로고    scopus 로고
    • Scaffold-focused virtual screening: Prospective application to the discovery of TTK inhibitors
    • Langdon, S. R.; Westwood, I. M.; Van Montfort, R. L. M.; Brown, N.; Blagg, J. Scaffold-focused virtual screening: Prospective application to the discovery of TTK inhibitors J. Chem. Inf. Model. 2013, 53, 1100-1112
    • (2013) J. Chem. Inf. Model. , vol.53 , pp. 1100-1112
    • Langdon, S.R.1    Westwood, I.M.2    Van Montfort, R.L.M.3    Brown, N.4    Blagg, J.5
  • 42
    • 77951986384 scopus 로고    scopus 로고
    • Conformer generation with OMEGA: Algorithm and validation using high quality structures from the Protein Databank and Cambridge Structural Database
    • Hawkins, P. C. D.; Skillman, A. G.; Warren, G. L.; Ellingson, B. A.; Stahl, M. T. Conformer generation with OMEGA: Algorithm and validation using high quality structures from the Protein Databank and Cambridge Structural Database J. Chem. Inf. Model. 2010, 50, 572-284
    • (2010) J. Chem. Inf. Model. , vol.50 , pp. 572-284
    • Hawkins, P.C.D.1    Skillman, A.G.2    Warren, G.L.3    Ellingson, B.A.4    Stahl, M.T.5
  • 43
    • 84886464668 scopus 로고    scopus 로고
    • OpenEye Scientific Software: Santa Fe, NM.
    • OMEGA; OpenEye Scientific Software: Santa Fe, NM; http://www.eyesopen. com/.
    • OMEGA
  • 44
    • 84886473799 scopus 로고    scopus 로고
    • OpenEye Scientific Software: Santa Fe, NM.
    • FILTER; OpenEye Scientific Software: Santa Fe, NM; http://www.eyesopen. com/.
    • FILTER
  • 45
    • 84886578396 scopus 로고    scopus 로고
    • Chemical Computing Group: Montreal, Quebec, Canada.
    • MOE; Chemical Computing Group: Montreal, Quebec, Canada; http://www.chemcomp.com/.
    • MOE
  • 46
    • 0001109246 scopus 로고    scopus 로고
    • A fast method of molecular shape comparison: A simple application of a Gaussian description of molecular shape
    • Grant, J. A.; Gallardo, M. A.; Pickup, B. T. A fast method of molecular shape comparison: A simple application of a Gaussian description of molecular shape J. Comput. Chem. 1996, 17, 1653-1666
    • (1996) J. Comput. Chem. , vol.17 , pp. 1653-1666
    • Grant, J.A.1    Gallardo, M.A.2    Pickup, B.T.3
  • 47
    • 84886576194 scopus 로고    scopus 로고
    • OpenEye Scientific Software: Santa Fe, NM.
    • vROCS; OpenEye Scientific Software: Santa Fe, NM; http://www.eyesopen. com/.
    • VROCS
  • 48
    • 61949166066 scopus 로고    scopus 로고
    • How similar are similarity searching methods? A principal component analysis of molecular descriptor space
    • Bender, A.; Jenkins, J. L.; Scheiber, J.; Sukuru, S. C. K.; Glick, M.; Davies, J. W. How similar are similarity searching methods? A principal component analysis of molecular descriptor space J. Chem. Inf. Model. 2009, 49, 108-119
    • (2009) J. Chem. Inf. Model. , vol.49 , pp. 108-119
    • Bender, A.1    Jenkins, J.L.2    Scheiber, J.3    Sukuru, S.C.K.4    Glick, M.5    Davies, J.W.6
  • 49
    • 33646855259 scopus 로고    scopus 로고
    • Accelrys, Inc. San Diego, CA.
    • Pipeline Pilot; Accelrys, Inc.: San Diego, CA; http://www.accelrys.com/.
    • Pipeline Pilot
  • 50
    • 77956064328 scopus 로고    scopus 로고
    • Schrödinger, LLC: Portland, OR.
    • Protein Preparation Wizard; Schrödinger, LLC: Portland, OR; http://www.schrodinger.com/.
    • Protein Preparation Wizard
  • 51
    • 84886529736 scopus 로고    scopus 로고
    • Schrödinger, LLC: Portland, OR.
    • Maestro; Schrödinger, LLC: Portland, OR; http://www.schrodinger.com/ .
    • Maestro
  • 52
    • 84886502127 scopus 로고    scopus 로고
    • Schrödinger, LLC: Portland, OR.
    • LigPrep; Schrödinger, LLC: Portland, OR; http://www.schrodinger.com/ .
    • LigPrep
  • 53
    • 84886461894 scopus 로고    scopus 로고
    • Schrödinger, LLC: Portland, OR.
    • Epik; Schrödinger, LLC: Portland, OR; http://www.schrodinger.com/.
    • Epik
  • 54
    • 84886577204 scopus 로고    scopus 로고
    • Schrödinger, LLC: Portland, OR.
    • Glide; Schrödinger, LLC: Portland, OR; http://www.schrodinger.com/.
    • Glide
  • 56
    • 84886452205 scopus 로고    scopus 로고
    • CCDC: Cambridge, United Kingdom.
    • CSD System; CCDC: Cambridge, United Kingdom; http://www.ccdc.cam.ac.uk/.
    • CSD System
  • 57
    • 0004261782 scopus 로고    scopus 로고
    • MRC Laboratory of Molecular Biology: Cambridge, United Kingdom.
    • Leslie, A. G. W.; Powell, H. MOSFLM 7.01; MRC Laboratory of Molecular Biology: Cambridge, United Kingdom.
    • MOSFLM 7.01
    • Leslie, A.G.W.1    Powell, H.2
  • 60
    • 0032964481 scopus 로고    scopus 로고
    • Automated protein model building combined with iterative structure refinement
    • Perrakis, A.; Morris, R.; Lamzin, V. S. Automated protein model building combined with iterative structure refinement Nat. Struct. Mol. Biol. 1999, 6, 458-463
    • (1999) Nat. Struct. Mol. Biol. , vol.6 , pp. 458-463
    • Perrakis, A.1    Morris, R.2    Lamzin, V.S.3
  • 61
    • 13244281317 scopus 로고    scopus 로고
    • Coot: Model-building tools for molecular graphics
    • Emsley, P.; Cowtan, K. Coot: Model-building tools for molecular graphics Acta Crystallogr., Sect. D 2004, 60, 2126-2132
    • (2004) Acta Crystallogr., Sect. D , vol.60 , pp. 2126-2132
    • Emsley, P.1    Cowtan, K.2
  • 62
    • 0030924992 scopus 로고    scopus 로고
    • Refinement of macromolecular structures by the maximum-likelihood method
    • Murshudov, G. N.; Vagin, A. A.; Dodson, E. J. Refinement of macromolecular structures by the maximum-likelihood method Acta Crystallogr., Sect. D 1997, 53, 240-255
    • (1997) Acta Crystallogr., Sect. D , vol.53 , pp. 240-255
    • Murshudov, G.N.1    Vagin, A.A.2    Dodson, E.J.3
  • 63
    • 33646260450 scopus 로고    scopus 로고
    • Optimal description of a protein structure in terms of multiple groups undergoing TLS motion
    • Painter, J.; Merritt, E. A. Optimal description of a protein structure in terms of multiple groups undergoing TLS motion Acta Crystallogr., Sect. D 2006, 62, 439-450
    • (2006) Acta Crystallogr., Sect. D , vol.62 , pp. 439
    • Painter, J.1    Merritt, E.A.2


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.