메뉴 건너뛰기




Volumn 12, Issue , 2011, Pages

A theoretical entropy score as a single value to express inhibitor selectivity

Author keywords

[No Author keywords available]

Indexed keywords

COMPOUND SELECTIVITY; DRUG DISCOVERY PROCESS; HIGH-THROUGHPUT SCREENING; INHIBITOR SELECTIVITY; KINASE INHIBITORS; MOLECULAR MECHANISM; QUANTITATIVE MEASURES; SELECTIVE LIGANDS;

EID: 79953837902     PISSN: None     EISSN: 14712105     Source Type: Journal    
DOI: 10.1186/1471-2105-12-94     Document Type: Article
Times cited : (35)

References (53)
  • 1
    • 0034306450 scopus 로고    scopus 로고
    • Specificity and mechanism of some commonly used protein kinase inhibitors
    • 10.1042/0264-6021:3510095, 1221339, 10998351
    • Davies SP, Reddy H, Caivano M, Cohen P. Specificity and mechanism of some commonly used protein kinase inhibitors. Biochem J 2000, 351(Pt1):95-105. 10.1042/0264-6021:3510095, 1221339, 10998351.
    • (2000) Biochem J , vol.351 , Issue.PART 1 , pp. 95-105
    • Davies, S.P.1    Reddy, H.2    Caivano, M.3    Cohen, P.4
  • 6
    • 58149102549 scopus 로고    scopus 로고
    • Assessment of chemical coverage of kinome space and its implications for kinase drug discovery
    • 10.1021/jm8011036, 19035792
    • Bamborough P, Drewry D, Harper G, Smith GK, Schneider K. Assessment of chemical coverage of kinome space and its implications for kinase drug discovery. J Med Chem 2008, 51(24):7898-7914. 10.1021/jm8011036, 19035792.
    • (2008) J Med Chem , vol.51 , Issue.24 , pp. 7898-7914
    • Bamborough, P.1    Drewry, D.2    Harper, G.3    Smith, G.K.4    Schneider, K.5
  • 7
    • 68949147006 scopus 로고    scopus 로고
    • Measuring and interpreting the selectivity of protein kinase inhibitors
    • 10.1007/s12154-009-0023-9, 2725273, 19568781
    • Smyth LA, Collins I. Measuring and interpreting the selectivity of protein kinase inhibitors. J Chem Biol 2009, 2(3):131-151. 10.1007/s12154-009-0023-9, 2725273, 19568781.
    • (2009) J Chem Biol , vol.2 , Issue.3 , pp. 131-151
    • Smyth, L.A.1    Collins, I.2
  • 8
    • 61649096359 scopus 로고    scopus 로고
    • G-protein-coupled receptor focused drug discovery using a target class platform approach
    • 10.1016/j.drudis.2008.11.011, 19121411
    • Heilker R, Wolff M, Tautermann CS, Bieler M. G-protein-coupled receptor focused drug discovery using a target class platform approach. Drug Discov Today 2009, 14(5-6):231-240. 10.1016/j.drudis.2008.11.011, 19121411.
    • (2009) Drug Discov Today , vol.14 , Issue.5-6 , pp. 231-240
    • Heilker, R.1    Wolff, M.2    Tautermann, C.S.3    Bieler, M.4
  • 9
    • 51249106641 scopus 로고    scopus 로고
    • Compound profiling using a panel of steroid hormone receptor cell-based assays
    • 10.1177/1087057108322155, 18753690
    • Wilkinson JM, Hayes S, Thompson D, Whitney P, Bi K. Compound profiling using a panel of steroid hormone receptor cell-based assays. J Biomol Screen 2008, 13(8):755-765. 10.1177/1087057108322155, 18753690.
    • (2008) J Biomol Screen , vol.13 , Issue.8 , pp. 755-765
    • Wilkinson, J.M.1    Hayes, S.2    Thompson, D.3    Whitney, P.4    Bi, K.5
  • 10
    • 54249154267 scopus 로고    scopus 로고
    • Predicting kinase selectivity profiles using free-wilson QSAR analysis
    • 10.1021/ci800138n, 18717582
    • Sciabola S, Stanton RV, Wittkop S, Wildman S, Moshinsky D, Potluri S, Xi H. Predicting kinase selectivity profiles using free-wilson QSAR analysis. J Chem Inf Model 2008, 48(9):1851-1867. 10.1021/ci800138n, 18717582.
    • (2008) J Chem Inf Model , vol.48 , Issue.9 , pp. 1851-1867
    • Sciabola, S.1    Stanton, R.V.2    Wittkop, S.3    Wildman, S.4    Moshinsky, D.5    Potluri, S.6    Xi, H.7
  • 11
    • 69549121940 scopus 로고    scopus 로고
    • QSAR models for predicting the similarity in binding profiles for pairs of protein kinases and the variation of models between experimental data sets
    • 10.1021/ci900176y, 19639957
    • Sheridan RP, Nam K, Maiorov VN, McMasters DR, Cornell WD. QSAR models for predicting the similarity in binding profiles for pairs of protein kinases and the variation of models between experimental data sets. J Chem Inf Model 2009, 49(8):1974-1985. 10.1021/ci900176y, 19639957.
    • (2009) J Chem Inf Model , vol.49 , Issue.8 , pp. 1974-1985
    • Sheridan, R.P.1    Nam, K.2    Maiorov, V.N.3    McMasters, D.R.4    Cornell, W.D.5
  • 12
    • 70349216447 scopus 로고    scopus 로고
    • Small kinase assay panels can provide a measure of selectivity
    • Brandt P, Jensen AJ, Nilsson J. Small kinase assay panels can provide a measure of selectivity. BioOrg Med Chem Letters 2009, 19(20):5861-5863.
    • (2009) BioOrg Med Chem Letters , vol.19 , Issue.20 , pp. 5861-5863
    • Brandt, P.1    Jensen, A.J.2    Nilsson, J.3
  • 13
    • 0037032835 scopus 로고    scopus 로고
    • The protein kinase complement of the human genome
    • 10.1126/science.1075762, 12471243
    • Manning G, Whyte DB, Martinez R, Hunter T, Sudarsanam S. The protein kinase complement of the human genome. Science 2002, 298(5600):1912-1934. 10.1126/science.1075762, 12471243.
    • (2002) Science , vol.298 , Issue.5600 , pp. 1912-1934
    • Manning, G.1    Whyte, D.B.2    Martinez, R.3    Hunter, T.4    Sudarsanam, S.5
  • 15
    • 36148943501 scopus 로고    scopus 로고
    • Gini coefficient: a new way to express kinase selectivity against a family of kinases
    • 10.1021/jm070562u, 17948979
    • Graczyk P. Gini coefficient: a new way to express kinase selectivity against a family of kinases. J Med Chem 2007, 50(23):5773-5779. 10.1021/jm070562u, 17948979.
    • (2007) J Med Chem , vol.50 , Issue.23 , pp. 5773-5779
    • Graczyk, P.1
  • 16
    • 77953193637 scopus 로고    scopus 로고
    • Analysis of kinase inhibitor selectivity using a thermodynamics-based partition index
    • 10.1021/jm100301x, 20459125
    • Cheng AC, Eksterowicz J, Geuns-Meyer S, Sun Y. Analysis of kinase inhibitor selectivity using a thermodynamics-based partition index. J Med Chem 2010, 53(11):4502-4510. 10.1021/jm100301x, 20459125.
    • (2010) J Med Chem , vol.53 , Issue.11 , pp. 4502-4510
    • Cheng, A.C.1    Eksterowicz, J.2    Geuns-Meyer, S.3    Sun, Y.4
  • 17
    • 84856043672 scopus 로고
    • A mathematical theory of communication
    • Shannon CE. A mathematical theory of communication. The Bell Systems Technical J 1948, 27:379-423.
    • (1948) The Bell Systems Technical J , vol.27 , pp. 379-423
    • Shannon, C.E.1
  • 19
    • 0015861774 scopus 로고
    • Relationship between the inhibition constant (Ki) and the concentration of inhibitor which causes 50 per cent inhibition (I50) of an enzymatic reaction
    • 10.1016/0006-2952(73)90196-2, 4202581
    • Cheng Y, Prusoff WH. Relationship between the inhibition constant (Ki) and the concentration of inhibitor which causes 50 per cent inhibition (I50) of an enzymatic reaction. Biochem Pharmacol 1973, 22(23):3099-3108. 10.1016/0006-2952(73)90196-2, 4202581.
    • (1973) Biochem Pharmacol , vol.22 , Issue.23 , pp. 3099-3108
    • Cheng, Y.1    Prusoff, W.H.2
  • 20
    • 24944497371 scopus 로고    scopus 로고
    • Features of selective kinase inhibitors
    • 10.1016/j.chembiol.2005.04.011, 15975507
    • Knight ZA, Shokat KM. Features of selective kinase inhibitors. Chem Biol 2005, 12(6):621-637. 10.1016/j.chembiol.2005.04.011, 15975507.
    • (2005) Chem Biol , vol.12 , Issue.6 , pp. 621-637
    • Knight, Z.A.1    Shokat, K.M.2
  • 21
    • 33845301393 scopus 로고    scopus 로고
    • Identification of small-molecule inhibitors of RGS4 using a high-troughput flow cytometry protein interaction assay
    • 10.1124/mol.106.028670, 17012620
    • Roman DL, Talbot JN, Roof RA, Sunahara RK, Traynor JR, Neubig RR. Identification of small-molecule inhibitors of RGS4 using a high-troughput flow cytometry protein interaction assay. Mol Pharmacol 2006, 71(1):169-175. 10.1124/mol.106.028670, 17012620.
    • (2006) Mol Pharmacol , vol.71 , Issue.1 , pp. 169-175
    • Roman, D.L.1    Talbot, J.N.2    Roof, R.A.3    Sunahara, R.K.4    Traynor, J.R.5    Neubig, R.R.6
  • 22
    • 0036085920 scopus 로고    scopus 로고
    • SB-431542 is a potent and specific inhibitor of transforming growth factor-β superfamily type I activin receptor-like kinase (ALK) receptors ALK4, ALK5, and ALK7
    • 10.1124/mol.62.1.65, 12065756
    • Inman GJ, Nicolás FJ, Callahan JF, Harling JD, Gaster LM, Reith AD, Laping NJ, Hill CS. SB-431542 is a potent and specific inhibitor of transforming growth factor-β superfamily type I activin receptor-like kinase (ALK) receptors ALK4, ALK5, and ALK7. Mol Pharmacol 2002, 62(1):65-74. 10.1124/mol.62.1.65, 12065756.
    • (2002) Mol Pharmacol , vol.62 , Issue.1 , pp. 65-74
    • Inman, G.J.1    Nicolás, F.J.2    Callahan, J.F.3    Harling, J.D.4    Gaster, L.M.5    Reith, A.D.6    Laping, N.J.7    Hill, C.S.8
  • 24
    • 0037075812 scopus 로고    scopus 로고
    • Novel 4-anilinoquinazolines with C-7 basic side chains: design and structure activity relationship of a series of potent, orally active, VEGF receptor tyrosine kinase inhibitors
    • 10.1021/jm011022e, 11881999
    • Hennequin LF, Stokes ES, Thomas AP, Johnstone C, Plé PA, Ogilvie DJ, Dukes M, Wedge SR, Kendrew J, Curwen JO. Novel 4-anilinoquinazolines with C-7 basic side chains: design and structure activity relationship of a series of potent, orally active, VEGF receptor tyrosine kinase inhibitors. J Med Chem 2002, 45(6):1300-1312. 10.1021/jm011022e, 11881999.
    • (2002) J Med Chem , vol.45 , Issue.6 , pp. 1300-1312
    • Hennequin, L.F.1    Stokes, E.S.2    Thomas, A.P.3    Johnstone, C.4    Plé, P.A.5    Ogilvie, D.J.6    Dukes, M.7    Wedge, S.R.8    Kendrew, J.9    Curwen, J.O.10
  • 25
    • 33745298429 scopus 로고    scopus 로고
    • Rational design of inhibitors that bind to inactive kinase conformations
    • Liu Y, Gray NS. Rational design of inhibitors that bind to inactive kinase conformations. Nature Chem Biol 2006, 2(7):358-364.
    • (2006) Nature Chem Biol , vol.2 , Issue.7 , pp. 358-364
    • Liu, Y.1    Gray, N.S.2
  • 27
    • 12144289677 scopus 로고    scopus 로고
    • Mechanism of activation of the RAF-ERK signaling pathway by oncogenic mutations of B-RAF
    • 10.1016/S0092-8674(04)00215-6, 15035987, Cancer Genome Project
    • Wan PTC, Garnett MJ, Roe SM, Lee S, Niculescu-Duvaz D, Good VM, Jones CM, Marshall CJ, Springer CJ, Barford D, Marais R. Cancer Genome Project Mechanism of activation of the RAF-ERK signaling pathway by oncogenic mutations of B-RAF. Cell 2004, 116(6):855-867. 10.1016/S0092-8674(04)00215-6, 15035987, Cancer Genome Project.
    • (2004) Cell , vol.116 , Issue.6 , pp. 855-867
    • Wan, P.T.C.1    Garnett, M.J.2    Roe, S.M.3    Lee, S.4    Niculescu-Duvaz, D.5    Good, V.M.6    Jones, C.M.7    Marshall, C.J.8    Springer, C.J.9    Barford, D.10    Marais, R.11
  • 28
    • 49649108911 scopus 로고    scopus 로고
    • Solution conformations and dynamics of ABL kinase-inhibitor complexes determined by NMR substantiate the different binding modes of imatinib/nilotinib and dasatinib
    • 10.1074/jbc.M801337200, 18434310
    • Vajpai N, Strauss A, Fendrich G, Cowan-Jacob SW, Manley PW, Grzesiek S, Jahnke W. Solution conformations and dynamics of ABL kinase-inhibitor complexes determined by NMR substantiate the different binding modes of imatinib/nilotinib and dasatinib. J Biol Chem 2008, 283(26):18292-18302. 10.1074/jbc.M801337200, 18434310.
    • (2008) J Biol Chem , vol.283 , Issue.26 , pp. 18292-18302
    • Vajpai, N.1    Strauss, A.2    Fendrich, G.3    Cowan-Jacob, S.W.4    Manley, P.W.5    Grzesiek, S.6    Jahnke, W.7
  • 31
    • 4644289313 scopus 로고    scopus 로고
    • A unique structure of epidermal growth factor receptor bound to GW572016 (lapatinib): relationships among protein conformation, inhibitor off-rate, and receptor activity in tumor cells
    • 10.1158/0008-5472.CAN-04-1168, 15374980
    • Wood ER, Truesdale AT, McDonald OB, Yuan D, Hassell A, Dickerson SH, Ellis B, Pennisi C, Horne E, Lackey K, Alligood KJ, Rusnak DW, Gilmer TM, Shewchuk L. A unique structure of epidermal growth factor receptor bound to GW572016 (lapatinib): relationships among protein conformation, inhibitor off-rate, and receptor activity in tumor cells. Cancer Res 2004, 64(18):6652-6659. 10.1158/0008-5472.CAN-04-1168, 15374980.
    • (2004) Cancer Res , vol.64 , Issue.18 , pp. 6652-6659
    • Wood, E.R.1    Truesdale, A.T.2    McDonald, O.B.3    Yuan, D.4    Hassell, A.5    Dickerson, S.H.6    Ellis, B.7    Pennisi, C.8    Horne, E.9    Lackey, K.10    Alligood, K.J.11    Rusnak, D.W.12    Gilmer, T.M.13    Shewchuk, L.14
  • 34
    • 67649726156 scopus 로고    scopus 로고
    • Protein kinase inhibitors: contributions from structure to clinical compounds
    • Johnson LN. Protein kinase inhibitors: contributions from structure to clinical compounds. Q Rev Biophysics 2009, 42(1):1-40.
    • (2009) Q Rev Biophysics , vol.42 , Issue.1 , pp. 1-40
    • Johnson, L.N.1
  • 35
    • 33745775709 scopus 로고    scopus 로고
    • Non-steroidal steroid receptor modulators
    • Hermkens PH, Kamp S, Lusher S, Veeneman GH. Non-steroidal steroid receptor modulators. IDrugs 2006, 9(7):488-494.
    • (2006) IDrugs , vol.9 , Issue.7 , pp. 488-494
    • Hermkens, P.H.1    Kamp, S.2    Lusher, S.3    Veeneman, G.H.4
  • 36
    • 0034733912 scopus 로고    scopus 로고
    • Ligand-protein interaction in nuclear receptors of hormones
    • 10.1016/S0014-5793(00)01672-0, 10878252
    • Egea PF, Klaholz BP, Moras D. Ligand-protein interaction in nuclear receptors of hormones. FEBS Letters 2000, 476(1-2):62-67. 10.1016/S0014-5793(00)01672-0, 10878252.
    • (2000) FEBS Letters , vol.476 , Issue.1-2 , pp. 62-67
    • Egea, P.F.1    Klaholz, B.P.2    Moras, D.3
  • 38
    • 67749148919 scopus 로고    scopus 로고
    • The X-ray structure of RU486 bound to the progesterone receptor in a destabilized agonistic conformation
    • 10.1074/jbc.M109.007872, 2740583, 19372222
    • Raaijmakers HC, Versteegh JE, Uitdehaag JCM. The X-ray structure of RU486 bound to the progesterone receptor in a destabilized agonistic conformation. J Biol Chem 2009, 284(9):19572-19579. 10.1074/jbc.M109.007872, 2740583, 19372222.
    • (2009) J Biol Chem , vol.284 , Issue.9 , pp. 19572-19579
    • Raaijmakers, H.C.1    Versteegh, J.E.2    Uitdehaag, J.C.M.3
  • 40
    • 18044365802 scopus 로고    scopus 로고
    • Conformational adaptation of nuclear receptor ligand binding domains to agonists: potential for novel approaches to ligand design
    • 10.1016/j.jsbmb.2005.01.004, 15860255
    • Togashi M, Borngraeber S, Sandler B, Fletterick RJ, Webb P, Baxter JD. Conformational adaptation of nuclear receptor ligand binding domains to agonists: potential for novel approaches to ligand design. J Steroid Biochem Mol Biol 2005, 93(2-5):127-137. 10.1016/j.jsbmb.2005.01.004, 15860255.
    • (2005) J Steroid Biochem Mol Biol , vol.93 , Issue.2-5 , pp. 127-137
    • Togashi, M.1    Borngraeber, S.2    Sandler, B.3    Fletterick, R.J.4    Webb, P.5    Baxter, J.D.6
  • 41
    • 0033868825 scopus 로고    scopus 로고
    • Crystal structure of a heterodimeric complex of RAR and RXR ligand-binding domains
    • 10.1016/S1097-2765(00)80424-4, 10882070
    • Bourguet W, Vivat V, Wurtz JM, Chambon P, Gronemeyer H, Moras D. Crystal structure of a heterodimeric complex of RAR and RXR ligand-binding domains. Mol Cell 2000, 5(2):289-298. 10.1016/S1097-2765(00)80424-4, 10882070.
    • (2000) Mol Cell , vol.5 , Issue.2 , pp. 289-298
    • Bourguet, W.1    Vivat, V.2    Wurtz, J.M.3    Chambon, P.4    Gronemeyer, H.5    Moras, D.6
  • 43
    • 73449149087 scopus 로고    scopus 로고
    • Steroid hormone binding receptors: application of homology modeling, induced fit docking, and molecular dynamics to study structure function relationships
    • 10.2174/156802609789207109, 19754398
    • Cornell W, Nam K. Steroid hormone binding receptors: application of homology modeling, induced fit docking, and molecular dynamics to study structure function relationships. Curr Top Med Chem 2009, 9(9):844-853. 10.2174/156802609789207109, 19754398.
    • (2009) Curr Top Med Chem , vol.9 , Issue.9 , pp. 844-853
    • Cornell, W.1    Nam, K.2
  • 44
    • 37349085453 scopus 로고    scopus 로고
    • A flexible approach to induced fit docking
    • 10.1021/jm070593p, 18031000
    • Nabuurs SB, Wagener M, de Vlieg J. A flexible approach to induced fit docking. J Med Chem 2007, 50(26):6507-6518. 10.1021/jm070593p, 18031000.
    • (2007) J Med Chem , vol.50 , Issue.26 , pp. 6507-6518
    • Nabuurs, S.B.1    Wagener, M.2    de Vlieg, J.3
  • 45
    • 75149130051 scopus 로고    scopus 로고
    • Targeting the cancer kinome through polypharmacology
    • Knight ZA, Lin H, Shokat KM. Targeting the cancer kinome through polypharmacology. Nature Rev Cancer 2010, 10(2):130-137.
    • (2010) Nature Rev Cancer , vol.10 , Issue.2 , pp. 130-137
    • Knight, Z.A.1    Lin, H.2    Shokat, K.M.3
  • 46
    • 65549171659 scopus 로고    scopus 로고
    • Designing multiple ligands - medicinal chemistry strategies and challenges
    • Morphy R, Rankovic Z. Designing multiple ligands - medicinal chemistry strategies and challenges. Curr Pharm Design 2009, 15(6):587-600.
    • (2009) Curr Pharm Design , vol.15 , Issue.6 , pp. 587-600
    • Morphy, R.1    Rankovic, Z.2
  • 47
    • 54249155522 scopus 로고    scopus 로고
    • Network pharmacology: the next paradigm in drug discovery
    • Hopkins A. Network pharmacology: the next paradigm in drug discovery. Nature Chem Biol 2008, 4(11):682-690.
    • (2008) Nature Chem Biol , vol.4 , Issue.11 , pp. 682-690
    • Hopkins, A.1
  • 48
    • 77950678935 scopus 로고    scopus 로고
    • Understanding kinase selectivity through energetic analysis of binding site waters
    • Robinson D, Sherman W, Farid R. Understanding kinase selectivity through energetic analysis of binding site waters. Chem Med Chem 2010, 5(4):618-627.
    • (2010) Chem Med Chem , vol.5 , Issue.4 , pp. 618-627
    • Robinson, D.1    Sherman, W.2    Farid, R.3
  • 49
    • 33750892907 scopus 로고    scopus 로고
    • Protein kinase inhibition: different approaches to selective inhibitor design
    • Scapin G. Protein kinase inhibition: different approaches to selective inhibitor design. Curr Drug Targets 2006, 7(11):1443-1454.
    • (2006) Curr Drug Targets , vol.7 , Issue.11 , pp. 1443-1454
    • Scapin, G.1
  • 51
    • 78149236457 scopus 로고    scopus 로고
    • Investigation of the relationship between topology and selectivity for druglike molecules
    • 10.1021/jm1008456, 20942392
    • Yang Y, Chen H, Nilsson I, Muresan S, Engkvist O. Investigation of the relationship between topology and selectivity for druglike molecules. J Med Chem 2010, 53(21):7709-7714. 10.1021/jm1008456, 20942392.
    • (2010) J Med Chem , vol.53 , Issue.21 , pp. 7709-7714
    • Yang, Y.1    Chen, H.2    Nilsson, I.3    Muresan, S.4    Engkvist, O.5
  • 52
    • 65549132575 scopus 로고    scopus 로고
    • Pharmacological promiscuity: dependence on compound properties and target specificity in a set of recent Roche compounds
    • Peters JU, Schnider P, Mattei P, Kansy M. Pharmacological promiscuity: dependence on compound properties and target specificity in a set of recent Roche compounds. Chem Med Chem 2009, 4(4):680-686.
    • (2009) Chem Med Chem , vol.4 , Issue.4 , pp. 680-686
    • Peters, J.U.1    Schnider, P.2    Mattei, P.3    Kansy, M.4


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.