메뉴 건너뛰기




Volumn 16, Issue 15, 2010, Pages 1718-1741

Natural products in structure-assisted design of molecular cancer therapeutics

Author keywords

Cancer; Docking; Drug discovery; In silico techniques; Molecular modeling; Natural product; Phytochemicals; Virtual screening

Indexed keywords

2 MORPHOLINO 8 PHENYLCHROMONE; ANACARDIC ACID; ANTINEOPLASTIC AGENT; BUTYROLACTONE; COMBRETASTATIN A1 PHOSPHATE; DEHYDRODIDEMNIN B; DOCETAXEL; EPIDERMAL GROWTH FACTOR RECEPTOR; ERLOTINIB; FLAVOPIRIDOL; GEFITINIB; GELDANAMYCIN; GEMCITABINE; GENISTEIN; HEAT SHOCK PROTEIN 90; IDN 5390; IXABEPILONE; LIGAND; MAMMALIAN TARGET OF RAPAMYCIN; MOTESANIB; MYRICETIN; NATURAL PRODUCT; OMBRABULIN; PACLITAXEL; PICEATANNOL; PROTEIN KINASE B; PROTEIN KINASE INHIBITOR; QUERCETIN; RESVERATROL; SORAFENIB; STAUROSPORINE; STEROID RECEPTOR COACTIVATOR 1; STEROID RECEPTOR COACTIVATOR 3; TEMSIROLIMUS; TIPIFARNIB; TOZASERTIB; UNCLASSIFIED DRUG; UNINDEXED DRUG; VINBLASTINE SULFATE; VINFLUNINE; BIOLOGICAL PRODUCT; DRUG DERIVATIVE; PLANT MEDICINAL PRODUCT; RAPAMYCIN;

EID: 78049511546     PISSN: 13816128     EISSN: 18734286     Source Type: Journal    
DOI: 10.2174/138161210791164027     Document Type: Review
Times cited : (23)

References (243)
  • 1
    • 52049109838 scopus 로고    scopus 로고
    • Natural products in drug discovery
    • Harvey AL. Natural products in drug discovery. Drug Discov Today 2008; 13: 894-901.
    • (2008) Drug Discov Today , vol.13 , pp. 894-901
    • Harvey, A.L.1
  • 2
    • 34247109045 scopus 로고    scopus 로고
    • Natural products as sources of new drugs over the last 25 years
    • Newman DJ, Cragg GM. Natural products as sources of new drugs over the last 25 years. J Nat Prod 2007; 70: 461-477.
    • (2007) J Nat Prod , vol.70 , pp. 461-477
    • Newman, D.J.1    Cragg, G.M.2
  • 3
    • 44249098800 scopus 로고    scopus 로고
    • Natural products to drugs: Natural product-derived compounds in clinical trials
    • Butler MS. Natural products to drugs: natural product-derived compounds in clinical trials. Nat Prod Rep 2008; 25: 475-516.
    • (2008) Nat Prod Rep , vol.25 , pp. 475-516
    • Butler, M.S.1
  • 5
    • 0037208308 scopus 로고    scopus 로고
    • Property distributions: Differences between drugs, natural products, and molecules from combinatorial chemistry
    • Feher M, Schmidt JM. Property distributions: differences between drugs, natural products, and molecules from combinatorial chemistry. J Chem Inf Comput Sci 2003; 43: 218-227.
    • (2003) J Chem Inf Comput Sci , vol.43 , pp. 218-227
    • Feher, M.1    Schmidt, J.M.2
  • 6
    • 0029854741 scopus 로고    scopus 로고
    • The combinatorial chemistry of nature
    • Verdine GL. The combinatorial chemistry of nature. Nature 1996; 384: 11-13.
    • (1996) Nature , vol.384 , pp. 11-13
    • Verdine, G.L.1
  • 7
    • 81255132014 scopus 로고    scopus 로고
    • Plants and cancer
    • In: Kintzios SE, Barberaki MG, Eds., Boca Raton: CRC Press LLC
    • Kintzios SE, Barberaki MG. Plants and cancer. In: Kintzios SE, Barberaki MG, Eds. Plants that fight cancer. Boca Raton: CRC Press LLC 2004; pp. 15-34.
    • (2004) Plants That Fight Cancer , pp. 15-34
    • Kintzios, S.E.1    Barberaki, M.G.2
  • 8
    • 44849093562 scopus 로고    scopus 로고
    • Oncogene addiction
    • Weinstein IB, Joe A. Oncogene addiction. Cancer Res 2008; 68: 3077-3080.
    • (2008) Cancer Res , vol.68 , pp. 3077-3080
    • Weinstein, I.B.1    Joe, A.2
  • 9
    • 64249135764 scopus 로고    scopus 로고
    • Novel agents on the horizon for cancer therapy
    • Ma WW, Adjei AA. Novel agents on the horizon for cancer therapy. CA Cancer J Clin 2009; 59: 111-37.
    • (2009) CA Cancer J Clin , vol.59 , pp. 111-137
    • Ma, W.W.1    Adjei, A.A.2
  • 11
    • 69249136243 scopus 로고    scopus 로고
    • Target profiling of small molecules by chemical proteomics
    • Rix U, Superti-Furga G. Target profiling of small molecules by chemical proteomics. Nat Chem Biol 2009; 5: 616-624.
    • (2009) Nat Chem Biol , vol.5 , pp. 616-624
    • Rix, U.1    Superti-Furga, G.2
  • 12
    • 33646406554 scopus 로고    scopus 로고
    • Celastrol, a triterpene extracted from the chinese Thunder of God Vine, is a potent proteasome inhibitor and suppresses human prostate cancer growth in nude mice
    • Yang H, Chen D, Cui QC, Yuan X, Dou QP. Celastrol, a triterpene extracted from the chinese Thunder of God Vine, is a potent proteasome inhibitor and suppresses human prostate cancer growth in nude mice. Cancer Res 2006; 66: 4758-4765.
    • (2006) Cancer Res , vol.66 , pp. 4758-4765
    • Yang, H.1    Chen, D.2    Cui, Q.C.3    Yuan, X.4    Dou, Q.P.5
  • 13
    • 15044349115 scopus 로고    scopus 로고
    • The efficiency of multi-target drugs: The network approach might help drug design
    • Csermely P, Agoston V, Pongor S. The efficiency of multi-target drugs: the network approach might help drug design. Trends Pharmacol Sci 2005; 26: 178-182.
    • (2005) Trends Pharmacol Sci , vol.26 , pp. 178-182
    • Csermely, P.1    Agoston, V.2    Pongor, S.3
  • 15
    • 42449161986 scopus 로고    scopus 로고
    • Dissection of mechanisms of Chinese medicinal formula Realgar-Indigo naturalis as an effective treatment for promyelocytic leukemia
    • Wang L, Zhou GB, Liu P, Song JH, Liang Y, Yan XJ, et al. Dissection of mechanisms of Chinese medicinal formula Realgar-Indigo naturalis as an effective treatment for promyelocytic leukemia. Proc Natl Acad Sci USA 2008; 105: 4826-4831.
    • (2008) Proc Natl Acad Sci USA , vol.105 , pp. 4826-4831
    • Wang, L.1    Zhou, G.B.2    Liu, P.3    Song, J.H.4    Liang, Y.5    Yan, X.J.6
  • 16
    • 38049028234 scopus 로고    scopus 로고
    • Western-medicine-validated anti-tumor agents and traditional Chinese medicine
    • Li XJ, Zhang HY. Western-medicine-validated anti-tumor agents and traditional Chinese medicine. Trends Mol Med 2008; 14: 1-2.
    • (2008) Trends Mol Med , vol.14 , pp. 1-2
    • Li, X.J.1    Zhang, H.Y.2
  • 17
    • 45849091861 scopus 로고    scopus 로고
    • Synergy in natural medicines: Implications for drug discovery
    • Li XJ, Zhang HY. Synergy in natural medicines: implications for drug discovery. Trends Pharmacol Sci 2008; 29: 331-332.
    • (2008) Trends Pharmacol Sci , vol.29 , pp. 331-332
    • Li, X.J.1    Zhang, H.Y.2
  • 18
    • 63049086100 scopus 로고    scopus 로고
    • Accessing target information by virtual parallel screening - the impact on natural product research
    • Rollinger JM. Accessing target information by virtual parallel screening - the impact on natural product research. Phytochem Lett 2009; 2: 53-58.
    • (2009) Phytochem Lett , vol.2 , pp. 53-58
    • Rollinger, J.M.1
  • 19
    • 37249035096 scopus 로고    scopus 로고
    • Phytochemical informatics of traditional chinese medicine and therapeutic relevance
    • Ehrmann TM, Barlow DJ, Hylands PJ. Phytochemical informatics of traditional chinese medicine and therapeutic relevance. J Chem Inf Model 2007; 47: 2316-2334.
    • (2007) J Chem Inf Model , vol.47 , pp. 2316-2334
    • Ehrmann, T.M.1    Barlow, D.J.2    Hylands, P.J.3
  • 20
    • 0036591874 scopus 로고    scopus 로고
    • Structural biology in drug design: Selective protein kinase inhibitors
    • Scapin G. Structural biology in drug design: selective protein kinase inhibitors. Drug Discov Today 2002; 7: 601-611.
    • (2002) Drug Discov Today , vol.7 , pp. 601-611
    • Scapin, G.1
  • 21
    • 64749110949 scopus 로고    scopus 로고
    • Structure-based design of molecular cancer therapeutics
    • van Montfort RL, Workman P. Structure-based design of molecular cancer therapeutics. Trends Biotechnol 2009; 27: 315-28.
    • (2009) Trends Biotechnol , vol.27 , pp. 315-328
    • van Montfort, R.L.1    Workman, P.2
  • 22
    • 0034677966 scopus 로고    scopus 로고
    • Drug discovery: A historical perspective
    • Drews J. Drug discovery: a historical perspective. Science 2000; 287: 1960-1964.
    • (2000) Science , vol.287 , pp. 1960-1964
    • Drews, J.1
  • 23
    • 33746042161 scopus 로고    scopus 로고
    • Integrated in silico tools for exploiting the natural products' bioactivity
    • Rollinger JM, Langer T, Stuppner H. Integrated in silico tools for exploiting the natural products' bioactivity. Planta Med 2006; 72: 671-678.
    • (2006) Planta Med , vol.72 , pp. 671-678
    • Rollinger, J.M.1    Langer, T.2    Stuppner, H.3
  • 24
    • 33744804321 scopus 로고    scopus 로고
    • Strategies for efficient lead structure discovery from natural products
    • Rollinger JM, Langer T, Stuppner H. Strategies for efficient lead structure discovery from natural products. Curr Med Chem 2006; 13: 1491-1507.
    • (2006) Curr Med Chem , vol.13 , pp. 1491-1507
    • Rollinger, J.M.1    Langer, T.2    Stuppner, H.3
  • 25
    • 37649009919 scopus 로고    scopus 로고
    • Molecule-pharmacophore superpositioning and pattern matching in computational drug design
    • Wolber G, Seidel T, Bendix F, Langer T. Molecule-pharmacophore superpositioning and pattern matching in computational drug design. Drug Discov Today 2008; 13: 23-29.
    • (2008) Drug Discov Today , vol.13 , pp. 23-29
    • Wolber, G.1    Seidel, T.2    Bendix, F.3    Langer, T.4
  • 26
    • 44349144497 scopus 로고    scopus 로고
    • Pharmacophore-based virtual screening
    • Sun HM. Pharmacophore-based virtual screening. Curr Med Chem 2008; 15: 1018-1024.
    • (2008) Curr Med Chem , vol.15 , pp. 1018-1024
    • Sun, H.M.1
  • 27
    • 64549138026 scopus 로고    scopus 로고
    • In silico target fishing for rationalized ligand discovery exemplified on constituents of Ruta graveolens
    • Rollinger JM, Schuster D, Danzl B, Schwaiger S, Markt P, Schmidtke M, et al. In silico target fishing for rationalized ligand discovery exemplified on constituents of Ruta graveolens. Planta Med 2009; 75: 195-204.
    • (2009) Planta Med , vol.75 , pp. 195-204
    • Rollinger, J.M.1    Schuster, D.2    Danzl, B.3    Schwaiger, S.4    Markt, P.5    Schmidtke, M.6
  • 29
    • 0030599010 scopus 로고    scopus 로고
    • A fast flexible docking method using an incremental construction algorithm
    • Rarey M, Kramer B, Lengauer T, Klebe G. A fast flexible docking method using an incremental construction algorithm. J Mol Biol 1996; 261: 470-489.
    • (1996) J Mol Biol , vol.261 , pp. 470-489
    • Rarey, M.1    Kramer, B.2    Lengauer, T.3    Klebe, G.4
  • 30
    • 0035025191 scopus 로고    scopus 로고
    • DOCK 4.0: Search strategies for automated molecular docking of flexible molecule databases
    • Ewing TJA, Makino S, Skillman AG, Kuntz ID. DOCK 4.0: search strategies for automated molecular docking of flexible molecule databases. J Comput-Aided Mol Des 2001; 15: 411-428.
    • (2001) J Comput-Aided Mol Des , vol.15 , pp. 411-428
    • Ewing, T.J.A.1    Makino, S.2    Skillman, A.G.3    Kuntz, I.D.4
  • 31
    • 0031552362 scopus 로고    scopus 로고
    • Development and validation of a genetic algorithm for flexible docking
    • Jones G, Willett P, Glen RC, Leach AR, Taylor R. Development and validation of a genetic algorithm for flexible docking. J Mol Biol 1997; 267: 727-748.
    • (1997) J Mol Biol , vol.267 , pp. 727-748
    • Jones, G.1    Willett, P.2    Glen, R.C.3    Leach, A.R.4    Taylor, R.5
  • 32
    • 11644261806 scopus 로고    scopus 로고
    • Automated docking using a Lamarckian genetic algorithm and an empirical binding free energy function
    • Morris GM, Goodsell DS, Halliday RS, Huey R, Hart WE, Belew RK, et al. Automated docking using a Lamarckian genetic algorithm and an empirical binding free energy function. J Comput Chem 1998; 19: 1639-1662.
    • (1998) J Comput Chem , vol.19 , pp. 1639-1662
    • Morris, G.M.1    Goodsell, D.S.2    Halliday, R.S.3    Huey, R.4    Hart, W.E.5    Belew, R.K.6
  • 33
    • 1642310340 scopus 로고    scopus 로고
    • Glide: A new approach for rapid, accurate docking and scoring. 2. Enrichment factors in database screening
    • Halgren TA, Murphy RB, Friesner RA, Beard HS, Frye LL, Pollard WT, et al. Glide: a new approach for rapid, accurate docking and scoring. 2. Enrichment factors in database screening. J Med Chem 2004; 47: 1750-1759.
    • (2004) J Med Chem , vol.47 , pp. 1750-1759
    • Halgren, T.A.1    Murphy, R.B.2    Friesner, R.A.3    Beard, H.S.4    Frye, L.L.5    Pollard, W.T.6
  • 34
    • 0037212102 scopus 로고    scopus 로고
    • LigandFit: A novel method for the shape-directed rapid docking of ligands to protein active sites
    • Venkatachalam CM, Jiang X, Oldfield T, Waldman M. LigandFit: a novel method for the shape-directed rapid docking of ligands to protein active sites. J Mol Graph Model 2003; 21: 289-307.
    • (2003) J Mol Graph Model , vol.21 , pp. 289-307
    • Venkatachalam, C.M.1    Jiang, X.2    Oldfield, T.3    Waldman, M.4
  • 35
    • 0037434582 scopus 로고    scopus 로고
    • Surflex: Fully automatic flexible molecular docking using a molecular similarity-based search engine
    • Jain AN. Surflex: fully automatic flexible molecular docking using a molecular similarity-based search engine. J Med Chem 2003; 46: 499-511.
    • (2003) J Med Chem , vol.46 , pp. 499-511
    • Jain, A.N.1
  • 37
    • 0027027467 scopus 로고
    • LUDI - Rule-based automatic design of new substituents for enzyme-inhibitor leads
    • Böhm HJ. LUDI - Rule-based automatic design of new substituents for enzyme-inhibitor leads. J Comput-Aided Mol Des 1992; 6: 593-606.
    • (1992) J Comput-Aided Mol Des , vol.6 , pp. 593-606
    • Böhm, H.J.1
  • 38
    • 47349110113 scopus 로고    scopus 로고
    • A template-finding algorithm and a comprehensive benchmark for homology modeling of proteins
    • Vallat BK, Pillardy J, Elber R. A template-finding algorithm and a comprehensive benchmark for homology modeling of proteins. Proteins 2008; 72: 910-928.
    • (2008) Proteins , vol.72 , pp. 910-928
    • Vallat, B.K.1    Pillardy, J.2    Elber, R.3
  • 39
    • 13844320566 scopus 로고    scopus 로고
    • LigandScout: 3-d pharmacophores derived from protein-bound ligands and their use as virtual screening filters
    • Wolber G, Langer T. LigandScout: 3-d pharmacophores derived from protein-bound ligands and their use as virtual screening filters. J Chem Inf Model 2005; 45: 160-169.
    • (2005) J Chem Inf Model , vol.45 , pp. 160-169
    • Wolber, G.1    Langer, T.2
  • 40
    • 0008951090 scopus 로고    scopus 로고
    • CombiGen: A novel software package for the rapid generation of virtual combinatorial libraries
    • Wolber G, Langer T. CombiGen: a novel software package for the rapid generation of virtual combinatorial libraries. Rat Approach Drug Design 2001: 390-399.
    • (2001) Rat Approach Drug Design , pp. 390-399
    • Wolber, G.1    Langer, T.2
  • 42
    • 67650720900 scopus 로고    scopus 로고
    • Generation of ligand-based pharmacophore model and virtual screening for identification of novel tubulin inhibitors with potent anticancer activity
    • Chiang YK, Kuo CC, Wu YS, Chen CT, Coumar MS, Wu JS, et al. Generation of ligand-based pharmacophore model and virtual screening for identification of novel tubulin inhibitors with potent anticancer activity. J Med Chem 2009; 52: 4221-4233.
    • (2009) J Med Chem , vol.52 , pp. 4221-4233
    • Chiang, Y.K.1    Kuo, C.C.2    Wu, Y.S.3    Chen, C.T.4    Coumar, M.S.5    Wu, J.S.6
  • 43
    • 0027548454 scopus 로고
    • A fast new approach to pharmacophore mapping and its application to dopaminergic and benzodiazepine agonists
    • Martin YC, Bures MG, Danaher EA, DeLazzer J, Lico I, Pavlik PA. A fast new approach to pharmacophore mapping and its application to dopaminergic and benzodiazepine agonists. J Comput-Aided Mol Des 1993; 7: 83-102.
    • (1993) J Comput-Aided Mol Des , vol.7 , pp. 83-102
    • Martin, Y.C.1    Bures, M.G.2    Danaher, E.A.3    Delazzer, J.4    Lico, I.5    Pavlik, P.A.6
  • 44
    • 84864522264 scopus 로고    scopus 로고
    • Accelrys. San Diego, CA, USA
    • Discovery Studio 2.1/Catalyst; available from Accelrys. San Diego, CA, USA. (www.accelrys.com).
    • Discovery Studio 2.1/Catalyst
  • 45
    • 84864508005 scopus 로고    scopus 로고
    • Schrodinger Inc, New York, NY, USA
    • PHASE; available from Schrodinger Inc, New York, NY, USA. (www.schrodinger.com).
    • PHASE
  • 46
    • 33947575766 scopus 로고    scopus 로고
    • Incorporating partial matches within multiobjective pharmacophore identification
    • Cottrell SJ, Gillet VJ, Taylor R. Incorporating partial matches within multiobjective pharmacophore identification. J Comput-Aided Mol Des 2006; 20: 735-749.
    • (2006) J Comput-Aided Mol Des , vol.20 , pp. 735-749
    • Cottrell, S.J.1    Gillet, V.J.2    Taylor, R.3
  • 47
    • 33947599081 scopus 로고    scopus 로고
    • Efficient overlay of small organic molecules using 3D pharmacophores
    • Wolber G, Dornhofer AA, Langer T. Efficient overlay of small organic molecules using 3D pharmacophores. J Comput-Aided Mol Des 2006; 20: 773-788.
    • (2006) J Comput-Aided Mol Des , vol.20 , pp. 773-788
    • Wolber, G.1    Dornhofer, A.A.2    Langer, T.3
  • 49
    • 65249089058 scopus 로고    scopus 로고
    • How to optimize shape-based virtual screening: Choosing the right query and including chemical information
    • Kirchmair J, Distinto S, Markt P, Schuster D, Spitzer GM, Liedl KR, et al. How to optimize shape-based virtual screening: choosing the right query and including chemical information. J Chem Inf Model 2009; 49: 678-692.
    • (2009) J Chem Inf Model , vol.49 , pp. 678-692
    • Kirchmair, J.1    Distinto, S.2    Markt, P.3    Schuster, D.4    Spitzer, G.M.5    Liedl, K.R.6
  • 50
    • 0038336897 scopus 로고    scopus 로고
    • Application and limitations of X-ray crystallographic data in structure-based ligand and drug design
    • Davis AM, Teague SJ, Kleywegt GJ. Application and limitations of X-ray crystallographic data in structure-based ligand and drug design. Angew Chem Int Ed Engl 2003; 42: 2718-2736.
    • (2003) Angew Chem Int Ed Engl , vol.42 , pp. 2718-2736
    • Davis, A.M.1    Teague, S.J.2    Kleywegt, G.J.3
  • 51
    • 0028838971 scopus 로고
    • Protein kinases and phosphatases: The yin and yang of protein phosphorylation and signaling
    • Hunter T. Protein kinases and phosphatases: the yin and yang of protein phosphorylation and signaling. Cell 1995; 80: 225-236.
    • (1995) Cell , vol.80 , pp. 225-236
    • Hunter, T.1
  • 52
    • 0036527429 scopus 로고    scopus 로고
    • Protein kinases--the major drug targets of the twenty-first century?
    • Cohen P. Protein kinases--the major drug targets of the twenty-first century? Nat Rev Drug Discov 2002; 1: 309-315.
    • (2002) Nat Rev Drug Discov , vol.1 , pp. 309-315
    • Cohen, P.1
  • 53
    • 0033786922 scopus 로고    scopus 로고
    • Protein tyrosine kinase structure and function
    • Hubbard SR, Till JH. Protein tyrosine kinase structure and function. Annu Rev Biochem 2000; 69: 373-698.
    • (2000) Annu Rev Biochem , vol.69 , pp. 373-698
    • Hubbard, S.R.1    Till, J.H.2
  • 54
    • 40949151046 scopus 로고    scopus 로고
    • Doing more than just the structure-structural genomics in kinase drug discovery
    • Marsden BD, Knapp S. Doing more than just the structure-structural genomics in kinase drug discovery. Curr Opin Chem Biol 2008; 12: 40-45.
    • (2008) Curr Opin Chem Biol , vol.12 , pp. 40-45
    • Marsden, B.D.1    Knapp, S.2
  • 55
    • 65249170904 scopus 로고    scopus 로고
    • Binding site similarity analysis for the functional classification of the protein kinase family
    • Kinnings SL, Jackson RM. Binding site similarity analysis for the functional classification of the protein kinase family. J Chem Inf Model 2009; 49: 318-329.
    • (2009) J Chem Inf Model , vol.49 , pp. 318-329
    • Kinnings, S.L.1    Jackson, R.M.2
  • 56
    • 33646833091 scopus 로고    scopus 로고
    • Structure selection for protein kinase docking and virtual screening: Homology models or crystal structures?
    • Rockey WM, Elcock AH. Structure selection for protein kinase docking and virtual screening: homology models or crystal structures? Curr Protein Pept Sci 2006; 7: 437-457.
    • (2006) Curr Protein Pept Sci , vol.7 , pp. 437-457
    • Rockey, W.M.1    Elcock, A.H.2
  • 57
    • 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. Nat Chem Biol 2006; 2: 358-364.
    • (2006) Nat Chem Biol , vol.2 , pp. 358-364
    • Liu, Y.1    Gray, N.S.2
  • 59
    • 0141599428 scopus 로고    scopus 로고
    • Structure of the epidermal growth factor receptor kinase domain alone and in complex with a 4-anilinoquinazoline inhibitor
    • Stamos J, Sliwkowski MX, Eigenbrot C. Structure of the epidermal growth factor receptor kinase domain alone and in complex with a 4-anilinoquinazoline inhibitor. J Biol Chem 2002; 277: 46265-46272.
    • (2002) J Biol Chem , vol.277 , pp. 46265-46272
    • Stamos, J.1    Sliwkowski, M.X.2    Eigenbrot, C.3
  • 60
    • 4644289313 scopus 로고    scopus 로고
    • A unique structure for epidermal growth factor receptor bound to GW572016 (Lapatinib): Relationships among protein conformation, inhibitor off-rate, and receptor activity in tumor cells
    • Wood ER, Truesdale AT, McDonald OB, Yuan D, Hassell A, Dickerson SH, et al. A unique structure for 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: 6652-6659.
    • (2004) Cancer Res , vol.64 , 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
  • 63
    • 0037418759 scopus 로고    scopus 로고
    • Selective separation of active inhibitors of epidermal growth factor receptor from Caragana jubata by molecularly imprinted solid-phase extraction
    • Zhu L, Xu X. Selective separation of active inhibitors of epidermal growth factor receptor from Caragana jubata by molecularly imprinted solid-phase extraction. J Chromatogr A 2003; 991: 151-158.
    • (2003) J Chromatogr A , vol.991 , pp. 151-158
    • Zhu, L.1    Xu, X.2
  • 65
    • 0031034930 scopus 로고    scopus 로고
    • Crystal structure of the Src family tyrosine kinase Hck
    • Sicheri F, Moarefi I, Kuriyan J. Crystal structure of the Src family tyrosine kinase Hck. Nature 1997; 385: 602-609.
    • (1997) Nature , vol.385 , pp. 602-609
    • Sicheri, F.1    Moarefi, I.2    Kuriyan, J.3
  • 67
    • 0033602541 scopus 로고    scopus 로고
    • Use of a pharmacophore model for the design of EGFR tyrosine kinase inhibitors: Isoflavones and 3-phenyl-4(1H)-quinolones
    • Traxler P, Green J, Mett H, Sequin U, Furet P. Use of a pharmacophore model for the design of EGFR tyrosine kinase inhibitors: isoflavones and 3-phenyl-4(1H)-quinolones. J Med Chem 1999; 42: 1018-1026.
    • (1999) J Med Chem , vol.42 , pp. 1018-1026
    • Traxler, P.1    Green, J.2    Mett, H.3    Sequin, U.4    Furet, P.5
  • 68
    • 0031025991 scopus 로고    scopus 로고
    • Three-dimensional structure of the tyrosine kinase c-Src
    • Xu W, Harrison SC, Eck MJ. Three-dimensional structure of the tyrosine kinase c-Src. Nature 1997; 385: 595-602.
    • (1997) Nature , vol.385 , pp. 595-602
    • Xu, W.1    Harrison, S.C.2    Eck, M.J.3
  • 70
    • 0034693877 scopus 로고    scopus 로고
    • Role of Src expression and activation in human cancer
    • Irby RB, Yeatman TJ. Role of Src expression and activation in human cancer. Oncogene 2000; 19: 5636-5642.
    • (2000) Oncogene , vol.19 , pp. 5636-5642
    • Irby, R.B.1    Yeatman, T.J.2
  • 71
    • 49449108208 scopus 로고    scopus 로고
    • Naturally occurring homoisoflavonoids function as potent protein tyrosine kinase inhibitors by c-Src-based high-throughput screening
    • Lin LG, Xie H, Li HL, Tong LJ, Tang CP, Ke CQ, et al. Naturally occurring homoisoflavonoids function as potent protein tyrosine kinase inhibitors by c-Src-based high-throughput screening. J Med Chem 2008; 51: 4419-4429.
    • (2008) J Med Chem , vol.51 , pp. 4419-4429
    • Lin, L.G.1    Xie, H.2    Li, H.L.3    Tong, L.J.4    Tang, C.P.5    Ke, C.Q.6
  • 72
    • 32944465388 scopus 로고    scopus 로고
    • Handicapping the race to develop inhibitors of the phosphoinositide 3-kinase/Akt/mammalian target of rapamycin pathway
    • Granville CA, Memmott RM, Gills JJ, Dennis PA. Handicapping the race to develop inhibitors of the phosphoinositide 3-kinase/Akt/mammalian target of rapamycin pathway. Clin Cancer Res 2006; 12: 679-689.
    • (2006) Clin Cancer Res , vol.12 , pp. 679-689
    • Granville, C.A.1    Memmott, R.M.2    Gills, J.J.3    Dennis, P.A.4
  • 73
    • 48649107474 scopus 로고    scopus 로고
    • Efficacy of everolimus in advanced renal cell carcinoma: A double-blind, randomised, placebo-controlled phase III trial
    • Motzer RJ, Escudier B, Oudard S, Hutson TE, Porta C, Bracarda S, et al. Efficacy of everolimus in advanced renal cell carcinoma: a double-blind, randomised, placebo-controlled phase III trial. Lancet 2008; 372: 449-456.
    • (2008) Lancet , vol.372 , pp. 449-456
    • Motzer, R.J.1    Escudier, B.2    Oudard, S.3    Hutson, T.E.4    Porta, C.5    Bracarda, S.6
  • 74
    • 38649140450 scopus 로고    scopus 로고
    • Phase I trial of the novel mammalian target of rapamycin inhibitor deforolimus (AP23573; MK-8669) administered intravenously daily for 5 days every 2 weeks to patients with advanced malignancies
    • Mita MM, Mita AC, Chu QS, Rowinsky EK, Fetterly GJ, Goldston M, et al. Phase I trial of the novel mammalian target of rapamycin inhibitor deforolimus (AP23573; MK-8669) administered intravenously daily for 5 days every 2 weeks to patients with advanced malignancies. J Clin Oncol 2008; 26: 361-367.
    • (2008) J Clin Oncol , vol.26 , pp. 361-367
    • Mita, M.M.1    Mita, A.C.2    Chu, Q.S.3    Rowinsky, E.K.4    Fetterly, G.J.5    Goldston, M.6
  • 75
    • 0033634827 scopus 로고    scopus 로고
    • Structural determinants of phosphoinositide 3-kinase inhibition by wortmannin, LY294002, quercetin, myricetin, and staurosporine
    • Walker EH, Pacold ME, Perisic O, Stephens L, Hawkins PT, Wymann MP, et al. Structural determinants of phosphoinositide 3-kinase inhibition by wortmannin, LY294002, quercetin, myricetin, and staurosporine. Mol Cell 2000; 6: 909-919.
    • (2000) Mol Cell , vol.6 , pp. 909-919
    • Walker, E.H.1    Pacold, M.E.2    Perisic, O.3    Stephens, L.4    Hawkins, P.T.5    Wymann, M.P.6
  • 76
    • 0028170210 scopus 로고
    • A specific inhibitor of phosphatidylinositol 3-kinase, 2-(4-morpholinyl)-8-phenyl-4H-1-benzopyran-4-one (LY294002)
    • Vlahos CJ, Matter WF, Hui KY, Brown RF. A specific inhibitor of phosphatidylinositol 3-kinase, 2-(4-morpholinyl)-8-phenyl-4H-1-benzopyran-4-one (LY294002). J Biol Chem 1994; 269: 5241-5218.
    • (1994) J Biol Chem , vol.269 , pp. 5241-5248
    • Vlahos, C.J.1    Matter, W.F.2    Hui, K.Y.3    Brown, R.F.4
  • 77
    • 33646147812 scopus 로고    scopus 로고
    • Action mechanisms and structure-activity relationships of PI3Kgamma inhibitors on the enzyme: A molecular modeling study
    • Kuang RR, Qian F, Li Z, Wei DZ, Tang Y. Action mechanisms and structure-activity relationships of PI3Kgamma inhibitors on the enzyme: a molecular modeling study. Eur J Med Chem 2006; 41: 558-565.
    • (2006) Eur J Med Chem , vol.41 , pp. 558-565
    • Kuang, R.R.1    Qian, F.2    Li, Z.3    Wei, D.Z.4    Tang, Y.5
  • 78
    • 33644787284 scopus 로고    scopus 로고
    • Study on improving the selectivity of compounds that inhibit two PI3Ks (gamma and delta)
    • Kuang RR, Qian F, Li Z, Wei DZ. Study on improving the selectivity of compounds that inhibit two PI3Ks (gamma and delta). J Mol Model 2006; 12: 445-452.
    • (2006) J Mol Model , vol.12 , pp. 445-452
    • Kuang, R.R.1    Qian, F.2    Li, Z.3    Wei, D.Z.4
  • 79
    • 50149115138 scopus 로고    scopus 로고
    • Structural analysis of PI3-kinase isoforms: Identification of residues enabling selective inhibition by small molecule ATP-competitive inhibitors
    • Zvelebil MJ, Waterfield MD, Shuttleworth SJ. Structural analysis of PI3-kinase isoforms: identification of residues enabling selective inhibition by small molecule ATP-competitive inhibitors. Arch Biochem Biophys 2008; 477: 404-410.
    • (2008) Arch Biochem Biophys , vol.477 , pp. 404-410
    • Zvelebil, M.J.1    Waterfield, M.D.2    Shuttleworth, S.J.3
  • 80
    • 42149156181 scopus 로고    scopus 로고
    • Phosphoinositide-3-kinases (PI3Ks): Combined comparative modeling and 3D-QSAR to rationalize the inhibition of p110alpha
    • Frederick R, Denny WA. Phosphoinositide-3-kinases (PI3Ks): combined comparative modeling and 3D-QSAR to rationalize the inhibition of p110alpha. J Chem Inf Model 2008; 48: 629-638.
    • (2008) J Chem Inf Model , vol.48 , pp. 629-638
    • Frederick, R.1    Denny, W.A.2
  • 81
    • 37249056471 scopus 로고    scopus 로고
    • The structure of a human p110alpha/p85alpha complex elucidates the effects of oncogenic PI3Kalpha mutations
    • Huang CH, Mandelker D, Schmidt-Kittler O, Samuels Y, Velculescu VE, Kinzler KW, et al. The structure of a human p110alpha/p85alpha complex elucidates the effects of oncogenic PI3Kalpha mutations. Science 2007; 318: 1744-1748.
    • (2007) Science , vol.318 , pp. 1744-1748
    • Huang, C.H.1    Mandelker, D.2    Schmidt-Kittler, O.3    Samuels, Y.4    Velculescu, V.E.5    Kinzler, K.W.6
  • 82
    • 10344258041 scopus 로고    scopus 로고
    • Targeting the mitogen-activated protein kinase cascade to treat cancer
    • Sebolt-Leopold JS, Herrera R. Targeting the mitogen-activated protein kinase cascade to treat cancer. Nat Rev Cancer 2004; 4: 937-947.
    • (2004) Nat Rev Cancer , vol.4 , pp. 937-947
    • Sebolt-Leopold, J.S.1    Herrera, R.2
  • 84
    • 0025193871 scopus 로고
    • Three-dimensional structures of H-ras p21 mutants: Molecular basis for their inability to function as signal switch molecules
    • Krengel U, Schlichting I, Scherer A, Schumann R, Frech M, John J, et al. Three-dimensional structures of H-ras p21 mutants: molecular basis for their inability to function as signal switch molecules. Cell 1990; 62: 539-548.
    • (1990) Cell , vol.62 , pp. 539-548
    • Krengel, U.1    Schlichting, I.2    Scherer, A.3    Schumann, R.4    Frech, M.5    John, J.6
  • 85
    • 0028097472 scopus 로고
    • Pharmaceutical research in molecular oncology
    • Gibbs JB, Oliff A. Pharmaceutical research in molecular oncology. Cell 1994; 79: 193-198.
    • (1994) Cell , vol.79 , pp. 193-198
    • Gibbs, J.B.1    Oliff, A.2
  • 86
    • 0030909826 scopus 로고    scopus 로고
    • Crystal structure of protein farnesyltransferase at 2.25 angstrom resolution
    • Park HW, Boduluri SR, Moomaw JF, Casey PJ, Beese LS. Crystal structure of protein farnesyltransferase at 2.25 angstrom resolution. Science 1997; 275: 1800-1804.
    • (1997) Science , vol.275 , pp. 1800-1804
    • Park, H.W.1    Boduluri, S.R.2    Moomaw, J.F.3    Casey, P.J.4    Beese, L.S.5
  • 87
    • 0025183869 scopus 로고
    • Evidence for an S-farnesylcysteine methyl ester at the carboxyl terminus of the Saccharomyces cerevisiae RAS2 protein
    • Stimmel JB, Deschenes RJ, Volker C, Stock J, Clarke S. Evidence for an S-farnesylcysteine methyl ester at the carboxyl terminus of the Saccharomyces cerevisiae RAS2 protein. Biochemistry 1990; 29: 9651-9659.
    • (1990) Biochemistry , vol.29 , pp. 9651-9659
    • Stimmel, J.B.1    Deschenes, R.J.2    Volker, C.3    Stock, J.4    Clarke, S.5
  • 88
    • 2342645506 scopus 로고    scopus 로고
    • Phase III trial of gemcitabine plus tipifarnib compared with gemcitabine plus placebo in advanced pancreatic cancer
    • Van Cutsem E, van de Velde H, Karasek P, Oettle H, Vervenne WL, Szawlowski A, et al. Phase III trial of gemcitabine plus tipifarnib compared with gemcitabine plus placebo in advanced pancreatic cancer. J Clin Oncol 2004; 22: 1430-1438.
    • (2004) J Clin Oncol , vol.22 , pp. 1430-1438
    • van Cutsem, E.1    van de Velde, H.2    Karasek, P.3    Oettle, H.4    Vervenne, W.L.5    Szawlowski, A.6
  • 89
    • 0037187388 scopus 로고    scopus 로고
    • Modeling of binding modes and inhibition mechanism of some natural ligands of farnesyl transferase using molecular docking
    • Pedretti A, Villa L, Vistoli G. Modeling of binding modes and inhibition mechanism of some natural ligands of farnesyl transferase using molecular docking. J Med Chem 2002; 45: 1460-1465.
    • (2002) J Med Chem , vol.45 , pp. 1460-1465
    • Pedretti, A.1    Villa, L.2    Vistoli, G.3
  • 90
    • 0346788642 scopus 로고    scopus 로고
    • Modeling of inhibition mechanism of natural ligands to farnesyl protein transferase using molecular docking
    • Sung ND, Cheun YG, Kwon BM, Park HY, Kim CK. Modeling of inhibition mechanism of natural ligands to farnesyl protein transferase using molecular docking. Bull Korean Chem Soc 2003; 24: 1509-1511.
    • (2003) Bull Korean Chem Soc , vol.24 , pp. 1509-1511
    • Sung, N.D.1    Cheun, Y.G.2    Kwon, B.M.3    Park, H.Y.4    Kim, C.K.5
  • 91
    • 15744380263 scopus 로고    scopus 로고
    • Structures of human MAP kinase kinase 1 (MEK1) and MEK2 describe novel noncompetitive kinase inhibition
    • Ohren JF, Chen H, Pavlovsky A, Whitehead C, Zhang E, Kuffa P, et al. Structures of human MAP kinase kinase 1 (MEK1) and MEK2 describe novel noncompetitive kinase inhibition. Nat Struct Mol Biol 2004; 11: 1192-1197.
    • (2004) Nat Struct Mol Biol , vol.11 , pp. 1192-1197
    • Ohren, J.F.1    Chen, H.2    Pavlovsky, A.3    Whitehead, C.4    Zhang, E.5    Kuffa, P.6
  • 92
    • 57349153022 scopus 로고    scopus 로고
    • The resveratrol analogue 3,5,3',4',5'-pentahydroxy-trans-stilbene inhibits cell transformation via MEK
    • Lee KW, Kang NJ, Rogozin EA, Oh SM, Heo YS, Pugliese A, et al. The resveratrol analogue 3,5,3',4',5'-pentahydroxy-trans-stilbene inhibits cell transformation via MEK. Int J Cancer 2008; 123: 2487-2496.
    • (2008) Int J Cancer , vol.123 , pp. 2487-2496
    • Lee, K.W.1    Kang, N.J.2    Rogozin, E.A.3    Oh, S.M.4    Heo, Y.S.5    Pugliese, A.6
  • 93
    • 34848916118 scopus 로고    scopus 로고
    • Myricetin is a novel natural inhibitor of neoplastic cell transformation and MEK1
    • Lee KW, Kang NJ, Rogozin EA, Kim HG, Cho YY, Bode AM, et al. Myricetin is a novel natural inhibitor of neoplastic cell transformation and MEK1. Carcinogenesis 2007; 28: 1918-1927.
    • (2007) Carcinogenesis , vol.28 , pp. 1918-1927
    • Lee, K.W.1    Kang, N.J.2    Rogozin, E.A.3    Kim, H.G.4    Cho, Y.Y.5    Bode, A.M.6
  • 94
    • 58249129942 scopus 로고    scopus 로고
    • MKK4 is a novel target for the inhibition of tumor necrosis factor-alpha-induced vascular endothelial growth factor expression by myricetin
    • Kim JE, Kwon JY, Lee DE, Kang NJ, Heo YS, Lee KW, et al. MKK4 is a novel target for the inhibition of tumor necrosis factor-alpha-induced vascular endothelial growth factor expression by myricetin. Biochem Pharmacol 2009; 77: 412-421.
    • (2009) Biochem Pharmacol , vol.77 , pp. 412-421
    • Kim, J.E.1    Kwon, J.Y.2    Lee, D.E.3    Kang, N.J.4    Heo, Y.S.5    Lee, K.W.6
  • 95
    • 0028234529 scopus 로고
    • Jak-STAT pathways and transcriptional activation in response to IFNs and other extracellular signaling proteins
    • Darnell JE, Jr., Kerr IM, Stark GR. Jak-STAT pathways and transcriptional activation in response to IFNs and other extracellular signaling proteins. Science 1994; 264: 1415-1421.
    • (1994) Science , vol.264 , pp. 1415-1421
    • Darnell Jr., J.E.1    Kerr, I.M.2    Stark, G.R.3
  • 97
    • 0029069540 scopus 로고
    • Enhanced DNA-binding activity of a Stat3-related protein in cells transformed by the Src oncoprotein
    • Yu CL, Meyer DJ, Campbell GS, Larner AC, Carter-Su C, Schwartz J, et al. Enhanced DNA-binding activity of a Stat3-related protein in cells transformed by the Src oncoprotein. Science 1995; 269: 81-83.
    • (1995) Science , vol.269 , pp. 81-83
    • Yu, C.L.1    Meyer, D.J.2    Campbell, G.S.3    Larner, A.C.4    Carter-Su, C.5    Schwartz, J.6
  • 98
    • 0028349904 scopus 로고
    • Interferon activation of the transcription factor Stat91 involves dimerization through SH2-phosphotyrosyl peptide interactions
    • Shuai K, Horvath CM, Huang LH, Qureshi SA, Cowburn D, Darnell JE, Jr. Interferon activation of the transcription factor Stat91 involves dimerization through SH2-phosphotyrosyl peptide interactions. Cell 1994; 76: 821-828.
    • (1994) Cell , vol.76 , pp. 821-828
    • Shuai, K.1    Horvath, C.M.2    Huang, L.H.3    Qureshi, S.A.4    Cowburn, D.5    Darnell Jr., J.E.6
  • 100
    • 0032499801 scopus 로고    scopus 로고
    • Three-dimensional structure of the Stat3beta homodimer bound to DNA
    • Becker S, Groner B, Muller CW. Three-dimensional structure of the Stat3beta homodimer bound to DNA. Nature 1998; 394: 145-151.
    • (1998) Nature , vol.394 , pp. 145-151
    • Becker, S.1    Groner, B.2    Muller, C.W.3
  • 101
    • 51349156533 scopus 로고    scopus 로고
    • Discovery of the catechol structural moiety as a Stat3 SH2 domain inhibitor by virtual screening
    • Hao W, Hu Y, Niu C, Huang X, Chang CP, Gibbons J, et al. Discovery of the catechol structural moiety as a Stat3 SH2 domain inhibitor by virtual screening. Bioorg Med Chem Lett 2008; 18: 4988-4992.
    • (2008) Bioorg Med Chem Lett , vol.18 , pp. 4988-4992
    • Hao, W.1    Hu, Y.2    Niu, C.3    Huang, X.4    Chang, C.P.5    Gibbons, J.6
  • 102
    • 0035415663 scopus 로고    scopus 로고
    • SH2 domain inhibition: A problem solved?
    • Shakespeare WC. SH2 domain inhibition: a problem solved? Curr Opin Chem Biol 2001; 5: 409-415.
    • (2001) Curr Opin Chem Biol , vol.5 , pp. 409-415
    • Shakespeare, W.C.1
  • 103
    • 0032726122 scopus 로고    scopus 로고
    • STAT proteins as novel targets for cancer therapy. Signal transducer an activator of transcription
    • Catlett-Falcone R, Dalton WS, Jove R. STAT proteins as novel targets for cancer therapy. Signal transducer an activator of transcription. Curr Opin Oncol 1999; 11: 490-496.
    • (1999) Curr Opin Oncol , vol.11 , pp. 490-496
    • Catlett-Falcone, R.1    Dalton, W.S.2    Jove, R.3
  • 104
    • 16344380754 scopus 로고    scopus 로고
    • A low-molecular-weight compound discovered through virtual database screening inhibits Stat3 function in breast cancer cells
    • Song H, Wang R, Wang S, Lin J. A low-molecular-weight compound discovered through virtual database screening inhibits Stat3 function in breast cancer cells. Proc Natl Acad Sci USA 2005; 102: 4700-4705.
    • (2005) Proc Natl Acad Sci USA , vol.102 , pp. 4700-4705
    • Song, H.1    Wang, R.2    Wang, S.3    Lin, J.4
  • 105
    • 33746508429 scopus 로고    scopus 로고
    • Mitotic kinases: The key to duplication, segregation, and cytokinesis errors, chromosomal instability, and oncogenesis
    • Li JJ, Li SA. Mitotic kinases: the key to duplication, segregation, and cytokinesis errors, chromosomal instability, and oncogenesis. Pharmacol Ther 2006; 111: 974-984.
    • (2006) Pharmacol Ther , vol.111 , pp. 974-984
    • Li, J.J.1    Li, S.A.2
  • 106
    • 67650073265 scopus 로고    scopus 로고
    • Cell cycle kinases as therapeutic targets for cancer
    • Lapenna S, Giordano A. Cell cycle kinases as therapeutic targets for cancer. Nat Rev Drug Discov 2009; 8: 547-566.
    • (2009) Nat Rev Drug Discov , vol.8 , pp. 547-566
    • Lapenna, S.1    Giordano, A.2
  • 107
    • 0035015532 scopus 로고    scopus 로고
    • Identification of cylin-dependent kinase 1 inhibitors of a new chemical type by structure-based design and database searching
    • Furet P, Meyer T, Mittl P, Fretz H. Identification of cylin-dependent kinase 1 inhibitors of a new chemical type by structure-based design and database searching. J Comput Aided Mol Des 2001; 15: 489-495.
    • (2001) J Comput Aided Mol Des , vol.15 , pp. 489-495
    • Furet, P.1    Meyer, T.2    Mittl, P.3    Fretz, H.4
  • 108
    • 0030271304 scopus 로고    scopus 로고
    • Chemical inhibitors of cyclin-dependent kinases
    • Meijer L. Chemical inhibitors of cyclin-dependent kinases. Trends Cell Biol 1996; 6: 393-397.
    • (1996) Trends Cell Biol , vol.6 , pp. 393-397
    • Meijer, L.1
  • 109
    • 3142694085 scopus 로고    scopus 로고
    • Synthesis and biological evaluation of analogues of butyrolactone I and molecular model of its interaction with CDK2
    • Brana MF, Garcia ML, Lopez B, de Pascual-Teresa B, Ramos A, Pozuelo JM, et al. Synthesis and biological evaluation of analogues of butyrolactone I and molecular model of its interaction with CDK2. Org Biomol Chem 2004; 2: 1864-1871.
    • (2004) Org Biomol Chem , vol.2 , pp. 1864-1871
    • Brana, M.F.1    Garcia, M.L.2    Lopez, B.3    de Pascual-Teresa, B.4    Ramos, A.5    Pozuelo, J.M.6
  • 110
    • 33947577413 scopus 로고    scopus 로고
    • Peripheral white blood cell toxicity induced by broad spectrum cyclin-dependent kinase inhibitors
    • Jessen BA, Lee L, Koudriakova T, Haines M, Lundgren K, Price S, et al. Peripheral white blood cell toxicity induced by broad spectrum cyclin-dependent kinase inhibitors. J Appl Toxicol 2007; 27: 133-142.
    • (2007) J Appl Toxicol , vol.27 , pp. 133-142
    • Jessen, B.A.1    Lee, L.2    Koudriakova, T.3    Haines, M.4    Lundgren, K.5    Price, S.6
  • 111
    • 37549000240 scopus 로고    scopus 로고
    • Expression of serine/threonine protein-kinases and related factors in normal monkey and human retinas: The mechanistic understanding of a CDK2 inhibitor induced retinal toxicity
    • Saturno G, Pesenti M, Cavazzoli C, Rossi A, Giusti AM, Gierke B, et al. Expression of serine/threonine protein-kinases and related factors in normal monkey and human retinas: the mechanistic understanding of a CDK2 inhibitor induced retinal toxicity. Toxicol Pathol 2007; 35: 972-983.
    • (2007) Toxicol Pathol , vol.35 , pp. 972-983
    • Saturno, G.1    Pesenti, M.2    Cavazzoli, C.3    Rossi, A.4    Giusti, A.M.5    Gierke, B.6
  • 113
    • 33845395240 scopus 로고    scopus 로고
    • REPLACE: A strategy for iterative design of cyclin- binding groove inhibitors
    • Andrews MJ, Kontopidis G, McInnes C, Plater A, Innes L, Cowan A, et al. REPLACE: a strategy for iterative design of cyclin- binding groove inhibitors. ChemBioChem 2006; 7: 1909-1915.
    • (2006) ChemBioChem , vol.7 , pp. 1909-1915
    • Andrews, M.J.1    Kontopidis, G.2    McInnes, C.3    Plater, A.4    Innes, L.5    Cowan, A.6
  • 114
    • 65649152925 scopus 로고    scopus 로고
    • Discovery and development of aurora kinase inhibitors as anticancer agents
    • Pollard JR, Mortimore M. Discovery and development of aurora kinase inhibitors as anticancer agents. J Med Chem 2009; 52: 2629-2651.
    • (2009) J Med Chem , vol.52 , pp. 2629-2651
    • Pollard, J.R.1    Mortimore, M.2
  • 115
    • 16844366286 scopus 로고    scopus 로고
    • RNA interference targeting aurora kinase a suppresses tumor growth and enhances the taxane chemosensitivity in human pancreatic cancer cells
    • Hata T, Furukawa T, Sunamura M, Egawa S, Motoi F, Ohmura N, et al. RNA interference targeting aurora kinase a suppresses tumor growth and enhances the taxane chemosensitivity in human pancreatic cancer cells. Cancer Res 2005; 65: 2899-2905.
    • (2005) Cancer Res , vol.65 , pp. 2899-2905
    • Hata, T.1    Furukawa, T.2    Sunamura, M.3    Egawa, S.4    Motoi, F.5    Ohmura, N.6
  • 116
    • 37049000352 scopus 로고    scopus 로고
    • Enhancement of radiation response by inhibition of Aurora-A kinase using siRNA or a selective Aurora kinase inhibitor PHA680632 in p53-deficient cancer cells
    • Tao Y, Zhang P, Frascogna V, Lecluse Y, Auperin A, Bourhis J, et al. Enhancement of radiation response by inhibition of Aurora-A kinase using siRNA or a selective Aurora kinase inhibitor PHA680632 in p53-deficient cancer cells. Br J Cancer 2007; 97: 1664-1672.
    • (2007) Br J Cancer , vol.97 , pp. 1664-1672
    • Tao, Y.1    Zhang, P.2    Frascogna, V.3    Lecluse, Y.4    Auperin, A.5    Bourhis, J.6
  • 118
    • 34250773487 scopus 로고    scopus 로고
    • Inhibition of Aurora-B function increases formation of multinucleated cells in p53 gene deficient cells and enhances anti-tumor effect of temozolomide in human glioma cells
    • Tsuno T, Natsume A, Katsumata S, Mizuno M, Fujita M, Osawa H, et al. Inhibition of Aurora-B function increases formation of multinucleated cells in p53 gene deficient cells and enhances anti-tumor effect of temozolomide in human glioma cells. J Neurooncol 2007; 83: 249-258.
    • (2007) J Neurooncol , vol.83 , pp. 249-258
    • Tsuno, T.1    Natsume, A.2    Katsumata, S.3    Mizuno, M.4    Fujita, M.5    Osawa, H.6
  • 119
    • 39749138724 scopus 로고    scopus 로고
    • Specific small-molecule activator of Aurora kinase A induces autophosphorylation in a cell-free system
    • Kishore AH, Vedamurthy BM, Mantelingu K, Agrawal S, Reddy BA, Roy S, et al. Specific small-molecule activator of Aurora kinase A induces autophosphorylation in a cell-free system. J Med Chem 2008; 51: 792-797.
    • (2008) J Med Chem , vol.51 , pp. 792-797
    • Kishore, A.H.1    Vedamurthy, B.M.2    Mantelingu, K.3    Agrawal, S.4    Reddy, B.A.5    Roy, S.6
  • 120
    • 53349143838 scopus 로고    scopus 로고
    • Jadomycin B, an Aurora-B kinase inhibitor discovered through virtual screening
    • Fu DH, Jiang W, Zheng JT, Zhao GY, Li Y, Yi H, et al. Jadomycin B, an Aurora-B kinase inhibitor discovered through virtual screening. Mol Cancer Ther 2008; 7: 2386-2393.
    • (2008) Mol Cancer Ther , vol.7 , pp. 2386-2393
    • Fu, D.H.1    Jiang, W.2    Zheng, J.T.3    Zhao, G.Y.4    Li, Y.5    Yi, H.6
  • 121
    • 34247615972 scopus 로고    scopus 로고
    • Structural basis for potent inhibition of the Aurora kinases and a T315I multi-drug resistant mutant form of Abl kinase by VX-680
    • Cheetham GM, Charlton PA, Golec JM, Pollard JR. Structural basis for potent inhibition of the Aurora kinases and a T315I multi-drug resistant mutant form of Abl kinase by VX-680. Cancer Lett 2007; 251: 323-329.
    • (2007) Cancer Lett , vol.251 , pp. 323-329
    • Cheetham, G.M.1    Charlton, P.A.2    Golec, J.M.3    Pollard, J.R.4
  • 123
    • 85013312416 scopus 로고
    • Tumor angiogenesis: Therapeutic implications
    • Folkman J. Tumor angiogenesis: therapeutic implications. N Engl J Med 1971; 285: 1182-1186.
    • (1971) N Engl J Med , vol.285 , pp. 1182-1186
    • Folkman, J.1
  • 124
    • 14644440555 scopus 로고    scopus 로고
    • Role of the vascular endothelial growth factor pathway in tumor growth and angiogenesis
    • Hicklin DJ, Ellis LM. Role of the vascular endothelial growth factor pathway in tumor growth and angiogenesis. J Clin Oncol 2005; 23: 1011-1027.
    • (2005) J Clin Oncol , vol.23 , pp. 1011-1027
    • Hicklin, D.J.1    Ellis, L.M.2
  • 125
    • 0037265805 scopus 로고    scopus 로고
    • Aplidine, a new anticancer agent of marine origin, inhibits vascular endothelial growth factor (VEGF) secretion and blocks VEGF-VEGFR-1 (flt-1) autocrine loop in human leukemia cells MOLT-4
    • Broggini M, Marchini SV, Galliera E, Borsotti P, Taraboletti G, Erba E, et al. Aplidine, a new anticancer agent of marine origin, inhibits vascular endothelial growth factor (VEGF) secretion and blocks VEGF-VEGFR-1 (flt-1) autocrine loop in human leukemia cells MOLT-4. Leukemia 2003; 17: 52-59.
    • (2003) Leukemia , vol.17 , pp. 52-59
    • Broggini, M.1    Marchini, S.V.2    Galliera, E.3    Borsotti, P.4    Taraboletti, G.5    Erba, E.6
  • 126
    • 27144487474 scopus 로고    scopus 로고
    • VEGF inhibition and cytotoxic effect of aplidin in leukemia cell lines and cells from acute myeloid leukemia
    • Biscardi M, Caporale R, Balestri F, Gavazzi S, Jimeno J, Grossi A. VEGF inhibition and cytotoxic effect of aplidin in leukemia cell lines and cells from acute myeloid leukemia. Ann Oncol 2005; 16: 1667-1674.
    • (2005) Ann Oncol , vol.16 , pp. 1667-1674
    • Biscardi, M.1    Caporale, R.2    Balestri, F.3    Gavazzi, S.4    Jimeno, J.5    Grossi, A.6
  • 127
    • 0344666682 scopus 로고    scopus 로고
    • Analysis of conformational equilibria in aplidine using selective excitation 2D NMR spectroscopy and molecular mechanics/ dynamics calculations
    • Cardenas F, Caba JM, Feliz M, Lloyd-Williams P, Giralt E. Analysis of conformational equilibria in aplidine using selective excitation 2D NMR spectroscopy and molecular mechanics/ dynamics calculations. J Org Chem 2003; 68: 9554-9562.
    • (2003) J Org Chem , vol.68 , pp. 9554-9562
    • Cardenas, F.1    Caba, J.M.2    Feliz, M.3    Lloyd-Williams, P.4    Giralt, E.5
  • 128
    • 0035967788 scopus 로고    scopus 로고
    • Conformational analysis of dehydrodidemnin B (aplidine) by NMR spectroscopy and molecular mechanics/dynamics calculations
    • Cardenas F, Thormann M, Feliz M, Caba JM, Lloyd-Williams P, Giralt E. Conformational analysis of dehydrodidemnin B (aplidine) by NMR spectroscopy and molecular mechanics/dynamics calculations. J Org Chem 2001; 66: 4580-4584.
    • (2001) J Org Chem , vol.66 , pp. 4580-4584
    • Cardenas, F.1    Thormann, M.2    Feliz, M.3    Caba, J.M.4    Lloyd-Williams, P.5    Giralt, E.6
  • 129
    • 0037006785 scopus 로고    scopus 로고
    • Natural product derived receptor tyrosine kinase inhibitors: Identification of IGF1R, Tie-2, and VEGFR-3 inhibitors
    • Stahl P, Kissau L, Mazitschek R, Giannis A, Waldmann H. Natural product derived receptor tyrosine kinase inhibitors: identification of IGF1R, Tie-2, and VEGFR-3 inhibitors. Angew Chem Int Ed 2002; 41: 1174-1178.
    • (2002) Angew Chem Int Ed , vol.41 , pp. 1174-1178
    • Stahl, P.1    Kissau, L.2    Mazitschek, R.3    Giannis, A.4    Waldmann, H.5
  • 130
    • 0026452135 scopus 로고
    • Enhanced expression of the tie receptor tyrosine kinase in endothelial cells during neovascularization
    • Korhonen J, Partanen J, Armstrong E, Vaahtokari A, Elenius K, Jalkanen M, et al. Enhanced expression of the tie receptor tyrosine kinase in endothelial cells during neovascularization. Blood 1992; 80: 2548-2555.
    • (1992) Blood , vol.80 , pp. 2548-2555
    • Korhonen, J.1    Partanen, J.2    Armstrong, E.3    Vaahtokari, A.4    Elenius, K.5    Jalkanen, M.6
  • 131
    • 0034435424 scopus 로고    scopus 로고
    • Structure of the Tie2 RTK domain: Self-inhibition by the nucleotide binding loop, activation loop, and C-terminal tail
    • Shewchuk LM, Hassell AM, Ellis B, Holmes WD, Davis R, Horne EL, et al. Structure of the Tie2 RTK domain: self-inhibition by the nucleotide binding loop, activation loop, and C-terminal tail. Structure 2000; 8: 1105-1113.
    • (2000) Structure , vol.8 , pp. 1105-1113
    • Shewchuk, L.M.1    Hassell, A.M.2    Ellis, B.3    Holmes, W.D.4    Davis, R.5    Horne, E.L.6
  • 133
    • 65249123159 scopus 로고    scopus 로고
    • Antivascular actions of microtubule-binding drugs
    • Schwartz EL. Antivascular actions of microtubule-binding drugs. Clin Cancer Res 2009; 15: 2594-2601.
    • (2009) Clin Cancer Res , vol.15 , pp. 2594-2601
    • Schwartz, E.L.1
  • 134
    • 34249308550 scopus 로고    scopus 로고
    • In vitro and in vivo anticancer activities of synthetic (-)-laulimalide, a marine natural product microtubule stabilizing agent
    • Liu J, Towle MJ, Cheng H, Saxton P, Reardon C, Wu J, et al. In vitro and in vivo anticancer activities of synthetic (-)-laulimalide, a marine natural product microtubule stabilizing agent. Anticancer Res 2007; 27: 1509-1518.
    • (2007) Anticancer Res , vol.27 , pp. 1509-1518
    • Liu, J.1    Towle, M.J.2    Cheng, H.3    Saxton, P.4    Reardon, C.5    Wu, J.6
  • 136
    • 2342455797 scopus 로고    scopus 로고
    • Antitumour and antiangiogenic effects of IDN 5390, a novel C-seco taxane, in a paclitaxel-resistant human ovarian tumour xenograft
    • Petrangolini G, Cassinelli G, Pratesi G, Tortoreto M, Favini E, Supino R, et al. Antitumour and antiangiogenic effects of IDN 5390, a novel C-seco taxane, in a paclitaxel-resistant human ovarian tumour xenograft. Br J Cancer 2004; 90: 1464-1468.
    • (2004) Br J Cancer , vol.90 , pp. 1464-1468
    • Petrangolini, G.1    Cassinelli, G.2    Pratesi, G.3    Tortoreto, M.4    Favini, E.5    Supino, R.6
  • 137
    • 0035834521 scopus 로고    scopus 로고
    • Refined structure of alpha beta-tubulin at 3.5 A resolution
    • Löwe J, Li H, Downing KH, Nogales E. Refined structure of alpha beta-tubulin at 3.5 A resolution. J Mol Biol 2001; 313: 1045-1057.
    • (2001) J Mol Biol , vol.313 , pp. 1045-1057
    • Löwe, J.1    Li, H.2    Downing, K.H.3    Nogales, E.4
  • 138
    • 3843053396 scopus 로고    scopus 로고
    • The binding mode of epothilone A on alpha,beta-tubulin by electron crystallography
    • Nettles JH, Li H, Cornett B, Krahn JM, Snyder JP, Downing KH. The binding mode of epothilone A on alpha,beta-tubulin by electron crystallography. Science 2004; 305: 866-869.
    • (2004) Science , vol.305 , pp. 866-869
    • Nettles, J.H.1    Li, H.2    Cornett, B.3    Krahn, J.M.4    Snyder, J.P.5    Downing, K.H.6
  • 139
    • 53849091740 scopus 로고    scopus 로고
    • The bound conformation of microtubule-stabilizing agents: NMR insights into the bioactive 3D structure of discodermolide and dictyostatin
    • Canales A, Matesanz R, Gardner NM, Andreu JM, Paterson I, Diaz JF, et al. The bound conformation of microtubule-stabilizing agents: NMR insights into the bioactive 3D structure of discodermolide and dictyostatin. Chem Eur J 2008; 14: 7557-7569.
    • (2008) Chem Eur J , vol.14 , pp. 7557-7569
    • Canales, A.1    Matesanz, R.2    Gardner, N.M.3    Andreu, J.M.4    Paterson, I.5    Diaz, J.F.6
  • 140
    • 33645405334 scopus 로고    scopus 로고
    • Diastereomers of dibromo-7-epi-10-deacetylcephalomannine: Crowded and cytotoxic taxanes exhibit halogen bonds
    • Jiang Y, Alcaraz AA, Chen JM, Kobayashi H, Lu YJ, Snyder JP. Diastereomers of dibromo-7-epi-10-deacetylcephalomannine: crowded and cytotoxic taxanes exhibit halogen bonds. J Med Chem 2006; 49: 1891-1899.
    • (2006) J Med Chem , vol.49 , pp. 1891-1899
    • Jiang, Y.1    Alcaraz, A.A.2    Chen, J.M.3    Kobayashi, H.4    Lu, Y.J.5    Snyder, J.P.6
  • 141
    • 49849105959 scopus 로고    scopus 로고
    • Total synthesis and evaluation of C25-benzyloxyepothilone C for tubulin assembly and cytotoxicity against MCF-7 breast cancer cells
    • Hutt OE, Reddy BS, Nair SK, Reiff EA, Henri JT, Greiner JF, et al. Total synthesis and evaluation of C25-benzyloxyepothilone C for tubulin assembly and cytotoxicity against MCF-7 breast cancer cells. Bioorg Med Chem Lett 2008; 18: 4904-4906.
    • (2008) Bioorg Med Chem Lett , vol.18 , pp. 4904-4906
    • Hutt, O.E.1    Reddy, B.S.2    Nair, S.K.3    Reiff, E.A.4    Henri, J.T.5    Greiner, J.F.6
  • 143
    • 34247125590 scopus 로고    scopus 로고
    • CoMFA 3D-QSAR analysis of epothilones based on docking conformation and alignment
    • Yuan W, Luan LB, Li YN. CoMFA 3D-QSAR analysis of epothilones based on docking conformation and alignment. Chin J Chem 2007; 25: 453-460.
    • (2007) Chin J Chem , vol.25 , pp. 453-460
    • Yuan, W.1    Luan, L.B.2    Li, Y.N.3
  • 144
    • 4444315009 scopus 로고    scopus 로고
    • Computational comparison of microtubule-stabilising agents laulimalide and peloruside with taxol and colchicine
    • Pineda O, Farras J, Maccari L, Manetti F, Botta M, Vilarrasa J. Computational comparison of microtubule-stabilising agents laulimalide and peloruside with taxol and colchicine. Bioorg Med Chem Lett 2004; 14: 4825-4829.
    • (2004) Bioorg Med Chem Lett , vol.14 , pp. 4825-4829
    • Pineda, O.1    Farras, J.2    Maccari, L.3    Manetti, F.4    Botta, M.5    Vilarrasa, J.6
  • 145
    • 17944377638 scopus 로고    scopus 로고
    • Conformational studies and solution structure of laulimalide and simplified analogues using NMR spectroscopy and molecular modeling
    • Paterson I, Menche D, Britton R, Hakansson AE, Silva-Martinez MA. Conformational studies and solution structure of laulimalide and simplified analogues using NMR spectroscopy and molecular modeling. Tetrahedron Lett 2005; 46: 3677-3682.
    • (2005) Tetrahedron Lett , vol.46 , pp. 3677-3682
    • Paterson, I.1    Menche, D.2    Britton, R.3    Hakansson, A.E.4    Silva-Martinez, M.A.5
  • 146
    • 33745593252 scopus 로고    scopus 로고
    • The betaI/betaIII-tubulin isoforms and their complexes with antimitotic agents. Docking and molecular dynamics studies
    • Magnani M, Ortuso F, Soro S, Alcaro S, Tramontano A, Botta M. The betaI/betaIII-tubulin isoforms and their complexes with antimitotic agents. Docking and molecular dynamics studies. FEBS J 2006; 273: 3301-3310.
    • (2006) FEBS J , vol.273 , pp. 3301-3310
    • Magnani, M.1    Ortuso, F.2    Soro, S.3    Alcaro, S.4    Tramontano, A.5    Botta, M.6
  • 147
    • 8344289232 scopus 로고    scopus 로고
    • Localization of the antimitotic peptide and depsipeptide binding site on beta-tubulin
    • Mitra A, Sept D. Localization of the antimitotic peptide and depsipeptide binding site on beta-tubulin. Biochemistry 2004; 43: 13955-13962.
    • (2004) Biochemistry , vol.43 , pp. 13955-13962
    • Mitra, A.1    Sept, D.2
  • 148
    • 1642401199 scopus 로고    scopus 로고
    • Insight into tubulin regulation from a complex with colchicine and a stathmin-like domain
    • Ravelli RB, Gigant B, Curmi PA, Jourdain I, Lachkar S, Sobel A, et al. Insight into tubulin regulation from a complex with colchicine and a stathmin-like domain. Nature 2004; 428: 198-202.
    • (2004) Nature , vol.428 , pp. 198-202
    • Ravelli, R.B.1    Gigant, B.2    Curmi, P.A.3    Jourdain, I.4    Lachkar, S.5    Sobel, A.6
  • 150
    • 33745659825 scopus 로고    scopus 로고
    • Synthesis and biological evaluation of 2-amino-3-(3',4',5'-trimethoxybenzoyl)-5-aryl thiophenes as a new class of potent antitubulin agents
    • Romagnoli R, Baraldi PG, Pavani MG, Tabrizi MA, Preti D, Fruttarolo F, et al. Synthesis and biological evaluation of 2-amino-3-(3',4',5'-trimethoxybenzoyl)-5-aryl thiophenes as a new class of potent antitubulin agents. J Med Chem 2006; 49: 3906-3915.
    • (2006) J Med Chem , vol.49 , pp. 3906-3915
    • Romagnoli, R.1    Baraldi, P.G.2    Pavani, M.G.3    Tabrizi, M.A.4    Preti, D.5    Fruttarolo, F.6
  • 152
    • 33749258555 scopus 로고    scopus 로고
    • Novel imidazole-based combretastatin A-4 analogues: Evaluation of their in vitro antitumor activity and molecular modeling study of their binding to the colchicine site of tubulin
    • Bellina F, Cauteruccio S, Monti S, Rossi R. Novel imidazole-based combretastatin A-4 analogues: evaluation of their in vitro antitumor activity and molecular modeling study of their binding to the colchicine site of tubulin. Bioorg Med Chem Lett 2006; 16: 5757-5762.
    • (2006) Bioorg Med Chem Lett , vol.16 , pp. 5757-5762
    • Bellina, F.1    Cauteruccio, S.2    Monti, S.3    Rossi, R.4
  • 154
    • 24944515311 scopus 로고    scopus 로고
    • A common pharmacophore for a diverse set of colchicine site inhibitors using a structure-based approach
    • Nguyen TL, McGrath C, Hermone AR, Burnett JC, Zaharevitz DW, Day BW, et al. A common pharmacophore for a diverse set of colchicine site inhibitors using a structure-based approach. J Med Chem 2005; 48: 6107-6116.
    • (2005) J Med Chem , vol.48 , pp. 6107-6116
    • Nguyen, T.L.1    McGrath, C.2    Hermone, A.R.3    Burnett, J.C.4    Zaharevitz, D.W.5    Day, B.W.6
  • 155
    • 33846261713 scopus 로고    scopus 로고
    • Histone deacetylase inhibitors for cancer therapy
    • Kim TY, Bang YJ, Robertson KD. Histone deacetylase inhibitors for cancer therapy. Epigenetics 2006; 1: 14-23.
    • (2006) Epigenetics , vol.1 , pp. 14-23
    • Kim, T.Y.1    Bang, Y.J.2    Robertson, K.D.3
  • 156
    • 0032948005 scopus 로고    scopus 로고
    • Synergy of demethylation and histone deacetylase inhibition in the re-expression of genes silenced in cancer
    • Cameron EE, Bachman KE, Myöhänen S, Herman JG, Baylin SB. Synergy of demethylation and histone deacetylase inhibition in the re-expression of genes silenced in cancer. Nat Genet 1999; 21: 103-107.
    • (1999) Nat Genet , vol.21 , pp. 103-107
    • Cameron, E.E.1    Bachman, K.E.2    Myöhänen, S.3    Herman, J.G.4    Baylin, S.B.5
  • 157
    • 0035866353 scopus 로고    scopus 로고
    • DNA methyltransferase inhibition enhances apoptosis induced by histone deacetylase inhibitors
    • Zhu WG, Lakshmanan RR, Beal MD, Otterson GA. DNA methyltransferase inhibition enhances apoptosis induced by histone deacetylase inhibitors. Cancer Res 2001; 61: 1327-1333.
    • (2001) Cancer Res , vol.61 , pp. 1327-1333
    • Zhu, W.G.1    Lakshmanan, R.R.2    Beal, M.D.3    Otterson, G.A.4
  • 158
    • 0242610850 scopus 로고    scopus 로고
    • Inhibition of histone deacetylase increases cytotoxicity to anticancer drugs targeting DNA
    • Kim MS, Blake M, Baek JH, Kohlhagen G, Pommier Y, Carrier F. Inhibition of histone deacetylase increases cytotoxicity to anticancer drugs targeting DNA. Cancer Res 2003; 63: 7291-7300.
    • (2003) Cancer Res , vol.63 , pp. 7291-7300
    • Kim, M.S.1    Blake, M.2    Baek, J.H.3    Kohlhagen, G.4    Pommier, Y.5    Carrier, F.6
  • 159
    • 0035477320 scopus 로고    scopus 로고
    • Synergistic activation of functional estrogen receptor (ER)-alpha by DNA methyltransferase and histone deacetylase inhibition in human ER-alpha-negative breast cancer cells
    • Yang X, Phillips DL, Ferguson AT, Nelson WG, Herman JG, Davidson NE. Synergistic activation of functional estrogen receptor (ER)-alpha by DNA methyltransferase and histone deacetylase inhibition in human ER-alpha-negative breast cancer cells. Cancer Res 2001; 61: 7025-7029.
    • (2001) Cancer Res , vol.61 , pp. 7025-7029
    • Yang, X.1    Phillips, D.L.2    Ferguson, A.T.3    Nelson, W.G.4    Herman, J.G.5    Davidson, N.E.6
  • 160
    • 0035962631 scopus 로고    scopus 로고
    • DNA methylation, methyltransferases, and cancer
    • Robertson KD. DNA methylation, methyltransferases, and cancer. Oncogene 2001; 20: 3139-3155.
    • (2001) Oncogene , vol.20 , pp. 3139-3155
    • Robertson, K.D.1
  • 161
    • 0345275879 scopus 로고    scopus 로고
    • Tea polyphenol (-)-epigallocatechin-3-gallate inhibits DNA methyl-transferase and reactivates methylation-silenced genes in cancer cell lines
    • Fang MZ, Wang Y, Ai N, Hou Z, Sun Y, Lu H, et al. Tea polyphenol (-)-epigallocatechin-3-gallate inhibits DNA methyl-transferase and reactivates methylation-silenced genes in cancer cell lines. Cancer Res 2003; 63: 7563-7570.
    • (2003) Cancer Res , vol.63 , pp. 7563-7570
    • Fang, M.Z.1    Wang, Y.2    Ai, N.3    Hou, Z.4    Sun, Y.5    Lu, H.6
  • 162
    • 0030575782 scopus 로고    scopus 로고
    • A structural basis for the preferential binding of hemimethylated DNA by HhaI DNA methyltransferase
    • O'Gara M, Roberts RJ, Cheng X. A structural basis for the preferential binding of hemimethylated DNA by HhaI DNA methyltransferase. J Mol Biol 1996; 263: 597-5606.
    • (1996) J Mol Biol , vol.263 , pp. 597-5606
    • O'Gara, M.1    Roberts, R.J.2    Cheng, X.3
  • 163
    • 41949125723 scopus 로고    scopus 로고
    • Suppressive effect of epigallocatechin gallate (EGCG) on DNA methylation in mice: Detection by methylation sensitive restriction endonuclease digestion and PCR
    • Yamada H, Sugimura H, Tsuneyoshi T. Suppressive effect of epigallocatechin gallate (EGCG) on DNA methylation in mice: detection by methylation sensitive restriction endonuclease digestion and PCR. J Food Agric Environ 2005; 3: 73-76.
    • (2005) J Food Agric Environ , vol.3 , pp. 73-76
    • Yamada, H.1    Sugimura, H.2    Tsuneyoshi, T.3
  • 164
    • 25144507259 scopus 로고    scopus 로고
    • Mechanisms for the inhibition of DNA methyltransferases by tea catechins and bioflavonoids
    • Lee WJ, Shim JY, Zhu BT. Mechanisms for the inhibition of DNA methyltransferases by tea catechins and bioflavonoids. Mol Pharmacol 2005; 68: 1018-1030.
    • (2005) Mol Pharmacol , vol.68 , pp. 1018-1030
    • Lee, W.J.1    Shim, J.Y.2    Zhu, B.T.3
  • 165
    • 3142562372 scopus 로고    scopus 로고
    • Structural snapshots of human HDAC8 provide insights into the class I histone deacetylases
    • Somoza JR, Skene RJ, Katz BA, Mol C, Ho JD, Jennings AJ, et al. Structural snapshots of human HDAC8 provide insights into the class I histone deacetylases. Structure 2004; 12: 1325-1334.
    • (2004) Structure , vol.12 , pp. 1325-1334
    • Somoza, J.R.1    Skene, R.J.2    Katz, B.A.3    Mol, C.4    Ho, J.D.5    Jennings, A.J.6
  • 166
    • 0033539092 scopus 로고    scopus 로고
    • Structures of a histone deacetylase homologue bound to the TSA and SAHA inhibitors
    • Finnin MS, Donigian JR, Cohen A, Richon VM, Rifkind RA, Marks PA, et al. Structures of a histone deacetylase homologue bound to the TSA and SAHA inhibitors. Nature 1999; 401: 188-193.
    • (1999) Nature , vol.401 , pp. 188-193
    • Finnin, M.S.1    Donigian, J.R.2    Cohen, A.3    Richon, V.M.4    Rifkind, R.A.5    Marks, P.A.6
  • 167
    • 0035927427 scopus 로고    scopus 로고
    • 3-(4-aroyl-1H-pyrrol-2-yl)-N-hydroxy-2-propenamides, a new class of synthetic histone deacetylase inhibitors
    • Massa S, Mai A, Sbardella G, Esposito M, Ragno R, Loidl P, et al. 3-(4-aroyl-1H-pyrrol-2-yl)-N-hydroxy-2-propenamides, a new class of synthetic histone deacetylase inhibitors. J Med Chem 2001; 44: 2069-2072.
    • (2001) J Med Chem , vol.44 , pp. 2069-2072
    • Massa, S.1    Mai, A.2    Sbardella, G.3    Esposito, M.4    Ragno, R.5    Loidl, P.6
  • 168
    • 0037171823 scopus 로고    scopus 로고
    • Binding mode analysis of 3-(4-benzoyl-1-methyl-1H-2-pyrrolyl)-N-hydroxy-2-propenamide: A new synthetic histone deacetylase inhibitor inducing histone hyperacetylation, growth inhibition, and terminal cell differentiation
    • Mai A, Massa S, Ragno R, Esposito M, Sbardella G, Nocca G, et al. Binding mode analysis of 3-(4-benzoyl-1-methyl-1H-2-pyrrolyl)-N-hydroxy-2-propenamide: a new synthetic histone deacetylase inhibitor inducing histone hyperacetylation, growth inhibition, and terminal cell differentiation. J Med Chem 2002; 45: 1778-1784.
    • (2002) J Med Chem , vol.45 , pp. 1778-1784
    • Mai, A.1    Massa, S.2    Ragno, R.3    Esposito, M.4    Sbardella, G.5    Nocca, G.6
  • 169
    • 0037434511 scopus 로고    scopus 로고
    • 3-(4-Aroyl-1-methyl-1H-2-pyrrolyl)-N-hydroxy-2-alkylamides as a new class of synthetic histone deacetylase inhibitors. 1. Design, synthesis, biological evaluation, and binding mode studies performed through three different docking procedures
    • Mai A, Massa S, Ragno R, Cerbara I, Jesacher F, Loidl P, et al. 3-(4-Aroyl-1-methyl-1H-2-pyrrolyl)-N-hydroxy-2-alkylamides as a new class of synthetic histone deacetylase inhibitors. 1. Design, synthesis, biological evaluation, and binding mode studies performed through three different docking procedures. J Med Chem 2003; 46: 512-524.
    • (2003) J Med Chem , vol.46 , pp. 512-524
    • Mai, A.1    Massa, S.2    Ragno, R.3    Cerbara, I.4    Jesacher, F.5    Loidl, P.6
  • 170
    • 12144291023 scopus 로고    scopus 로고
    • 3-(4-Aroyl-1-methyl-1H-pyrrol-2-yl)-N-hydroxy-2-propenamides as a new class of synthetic histone deacetylase inhibitors. 3. Discovery of novel lead compounds through structure-based drug design and docking studies
    • Ragno R, Mai A, Massa S, Cerbara I, Valente S, Bottoni P, et al. 3-(4-Aroyl-1-methyl-1H-pyrrol-2-yl)-N-hydroxy-2-propenamides as a new class of synthetic histone deacetylase inhibitors. 3. Discovery of novel lead compounds through structure-based drug design and docking studies. J Med Chem 2004; 47: 1351-1359.
    • (2004) J Med Chem , vol.47 , pp. 1351-1359
    • Ragno, R.1    Mai, A.2    Massa, S.3    Cerbara, I.4    Valente, S.5    Bottoni, P.6
  • 171
    • 27444435580 scopus 로고    scopus 로고
    • Toward selective histone deacetylase inhibitor design: Homology modeling, docking studies, and molecular dynamics simulations of human class I histone deacetylases
    • Wang DF, Helquist P, Wiech NL, Wiest O. Toward selective histone deacetylase inhibitor design: homology modeling, docking studies, and molecular dynamics simulations of human class I histone deacetylases. J Med Chem 2005; 48: 6936-6947.
    • (2005) J Med Chem , vol.48 , pp. 6936-6947
    • Wang, D.F.1    Helquist, P.2    Wiech, N.L.3    Wiest, O.4
  • 172
    • 38949141196 scopus 로고    scopus 로고
    • Phenylalanine-containing hydroxamic acids as selective inhibitors of class IIb histone deacetylases (HDACs)
    • Schäfer S, Saunders L, Eliseeva E, Velena A, Jung M, Schwienhorst A, et al. Phenylalanine-containing hydroxamic acids as selective inhibitors of class IIb histone deacetylases (HDACs). Bioorg Med Chem 2008; 16: 2011-2033.
    • (2008) Bioorg Med Chem , vol.16 , pp. 2011-2033
    • Schäfer, S.1    Saunders, L.2    Eliseeva, E.3    Velena, A.4    Jung, M.5    Schwienhorst, A.6
  • 174
    • 33947239221 scopus 로고    scopus 로고
    • Molecular insights into azumamide E histone deacetylases inhibitory activity
    • Maulucci N, Chini MG, Di Micco S, Izzo I, Cafaro E, Russo A, et al. Molecular insights into azumamide E histone deacetylases inhibitory activity. J Am Chem Soc 2007; 129: 3007-3112.
    • (2007) J Am Chem Soc , vol.129 , pp. 3007-3112
    • Maulucci, N.1    Chini, M.G.2    Di Micco, S.3    Izzo, I.4    Cafaro, E.5    Russo, A.6
  • 175
    • 33947586979 scopus 로고    scopus 로고
    • Total synthesis of azumamide A and azumamide E, evaluation as histone deacetylase inhibitors, and design of a more potent analogue
    • Wen S, Carey KL, Nakao Y, Fusetani N, Packham G, Ganesan A. Total synthesis of azumamide A and azumamide E, evaluation as histone deacetylase inhibitors, and design of a more potent analogue. Org Lett 2007; 9: 1105-1108.
    • (2007) Org Lett , vol.9 , pp. 1105-1108
    • Wen, S.1    Carey, K.L.2    Nakao, Y.3    Fusetani, N.4    Packham, G.5    Ganesan, A.6
  • 176
    • 41149111451 scopus 로고    scopus 로고
    • The Hsp90 molecular chaperone: An open and shut case for treatment
    • Pearl LH, Prodromou C, Workman P. The Hsp90 molecular chaperone: an open and shut case for treatment. Biochem J 2008; 410: 439-453.
    • (2008) Biochem J , vol.410 , pp. 439-453
    • Pearl, L.H.1    Prodromou, C.2    Workman, P.3
  • 177
    • 0141484615 scopus 로고    scopus 로고
    • A high-affinity conformation of Hsp90 confers tumour selectivity on Hsp90 inhibitors
    • Kamal A, Thao L, Sensintaffar J, Zhang L, Boehm MF, Fritz LC, et al. A high-affinity conformation of Hsp90 confers tumour selectivity on Hsp90 inhibitors. Nature 2003; 425: 407-410.
    • (2003) Nature , vol.425 , pp. 407-410
    • Kamal, A.1    Thao, L.2    Sensintaffar, J.3    Zhang, L.4    Boehm, M.F.5    Fritz, L.C.6
  • 178
    • 0031444238 scopus 로고    scopus 로고
    • Identification and structural characterization of the ATP/ADP-binding site in the Hsp90 molecular chaperone
    • Prodromou C, Roe SM, O'Brien R, Ladbury JE, Piper PW, Pearl LH. Identification and structural characterization of the ATP/ADP-binding site in the Hsp90 molecular chaperone. Cell 1997; 90: 65-75.
    • (1997) Cell , vol.90 , pp. 65-75
    • Prodromou, C.1    Roe, S.M.2    O'Brien, R.3    Ladbury, J.E.4    Piper, P.W.5    Pearl, L.H.6
  • 179
    • 0036718795 scopus 로고    scopus 로고
    • ATPases as drug targets: Learning from their structure
    • Chene P. ATPases as drug targets: learning from their structure. Nat Rev Drug Discov 2002; 1: 665-673.
    • (2002) Nat Rev Drug Discov , vol.1 , pp. 665-673
    • Chene, P.1
  • 180
    • 0031005361 scopus 로고    scopus 로고
    • Crystal structure of an Hsp90-geldanamycin complex: Targeting of a protein chaperone by an antitumor agent
    • Stebbins CE, Russo AA, Schneider C, Rosen N, Hartl FU, Pavletich NP. Crystal structure of an Hsp90-geldanamycin complex: targeting of a protein chaperone by an antitumor agent. Cell 1997; 89: 239-250.
    • (1997) Cell , vol.89 , pp. 239-250
    • Stebbins, C.E.1    Russo, A.A.2    Schneider, C.3    Rosen, N.4    Hartl, F.U.5    Pavletich, N.P.6
  • 181
    • 0032959590 scopus 로고    scopus 로고
    • Structural basis for inhibition of the Hsp90 molecular chaperone by the antitumor antibiotics radicicol and geldanamycin
    • Roe SM, Prodromou C, O'Brien R, Ladbury JE, Piper PW, Pearl LH. Structural basis for inhibition of the Hsp90 molecular chaperone by the antitumor antibiotics radicicol and geldanamycin. J Med Chem 1999; 42: 260-266.
    • (1999) J Med Chem , vol.42 , pp. 260-266
    • Roe, S.M.1    Prodromou, C.2    O'Brien, R.3    Ladbury, J.E.4    Piper, P.W.5    Pearl, L.H.6
  • 182
    • 0035071607 scopus 로고    scopus 로고
    • A small molecule designed to bind to the adenine nucleotide pocket of Hsp90 causes Her2 degradation and the growth arrest and differentiation of breast cancer cells
    • Chiosis G, Timaul MN, Lucas B, Munster PN, Zheng FF, Sepp-Lorenzino L, et al. A small molecule designed to bind to the adenine nucleotide pocket of Hsp90 causes Her2 degradation and the growth arrest and differentiation of breast cancer cells. Chem Biol 2001; 8: 289-299.
    • (2001) Chem Biol , vol.8 , pp. 289-299
    • Chiosis, G.1    Timaul, M.N.2    Lucas, B.3    Munster, P.N.4    Zheng, F.F.5    Sepp-Lorenzino, L.6
  • 183
    • 62149135294 scopus 로고    scopus 로고
    • Discovery and development of heat shock protein 90 inhibitors
    • Taldone T, Sun W, Chiosis G. Discovery and development of heat shock protein 90 inhibitors. Bioorg Med Chem 2009; 17: 2225-2235.
    • (2009) Bioorg Med Chem , vol.17 , pp. 2225-2235
    • Taldone, T.1    Sun, W.2    Chiosis, G.3
  • 184
    • 3042637928 scopus 로고    scopus 로고
    • Structure-activity relationships in purine-based inhibitor binding to HSP90 isoforms
    • Wright L, Barril X, Dymock B, Sheridan L, Surgenor A, Beswick M, et al. Structure-activity relationships in purine-based inhibitor binding to HSP90 isoforms. Chem Biol 2004; 11: 775-785.
    • (2004) Chem Biol , vol.11 , pp. 775-785
    • Wright, L.1    Barril, X.2    Dymock, B.3    Sheridan, L.4    Surgenor, A.5    Beswick, M.6
  • 186
    • 20644448390 scopus 로고    scopus 로고
    • The identification, synthesis, protein crystal structure and in vitro biochemical evaluation of a new 3,4-diarylpyrazole class of Hsp90 inhibitors
    • Cheung KM, Matthews TP, James K, Rowlands MG, Boxall KJ, Sharp SY, et al. The identification, synthesis, protein crystal structure and in vitro biochemical evaluation of a new 3,4-diarylpyrazole class of Hsp90 inhibitors. Bioorg Med Chem Lett 2005; 15: 3338-3343.
    • (2005) Bioorg Med Chem Lett , vol.15 , pp. 3338-3343
    • Cheung, K.M.1    Matthews, T.P.2    James, K.3    Rowlands, M.G.4    Boxall, K.J.5    Sharp, S.Y.6
  • 187
    • 42349084306 scopus 로고    scopus 로고
    • NVP-AUY922: A novel heat shock protein 90 inhibitor active against xenograft tumor growth, angiogenesis, and metastasis
    • Eccles SA, Massey A, Raynaud FI, Sharp SY, Box G, Valenti M, et al. NVP-AUY922: a novel heat shock protein 90 inhibitor active against xenograft tumor growth, angiogenesis, and metastasis. Cancer Res 2008; 68: 2850-2860.
    • (2008) Cancer Res , vol.68 , pp. 2850-2860
    • Eccles, S.A.1    Massey, A.2    Raynaud, F.I.3    Sharp, S.Y.4    Box, G.5    Valenti, M.6
  • 188
    • 34347256360 scopus 로고    scopus 로고
    • Structural basis for depletion of heat shock protein 90 client proteins by deguelin
    • Oh SH, Woo JK, Yazici YD, Myers JN, Kim WY, Jin Q, et al. Structural basis for depletion of heat shock protein 90 client proteins by deguelin. J Natl Cancer Inst 2007; 99: 949-9461.
    • (2007) J Natl Cancer Inst , vol.99 , pp. 949-9461
    • Oh, S.H.1    Woo, J.K.2    Yazici, Y.D.3    Myers, J.N.4    Kim, W.Y.5    Jin, Q.6
  • 189
    • 58849127710 scopus 로고    scopus 로고
    • Inside the Hsp90 inhibitors binding mode through induced fit docking
    • Lauria A, Ippolito M, Almerico AM. Inside the Hsp90 inhibitors binding mode through induced fit docking. J Mol Graph 2009; 27: 712-722.
    • (2009) J Mol Graph , vol.27 , pp. 712-722
    • Lauria, A.1    Ippolito, M.2    Almerico, A.M.3
  • 190
    • 21244479779 scopus 로고    scopus 로고
    • Unveiling the full potential of flexible receptor docking using multiple crystallographic structures
    • Barril X, Morley SD. Unveiling the full potential of flexible receptor docking using multiple crystallographic structures. J Med Chem 2005; 48: 4432-4443.
    • (2005) J Med Chem , vol.48 , pp. 4432-4443
    • Barril, X.1    Morley, S.D.2
  • 191
    • 0034646511 scopus 로고    scopus 로고
    • Structure of TPR domain-peptide complexes: Critical elements in the assembly of the Hsp70-Hsp90 multicha-perone machine
    • Scheufler C, Brinker A, Bourenkov G, Pegoraro S, Moroder L, Bartunik H, et al. Structure of TPR domain-peptide complexes: critical elements in the assembly of the Hsp70-Hsp90 multicha-perone machine. Cell 2000; 101: 199-210.
    • (2000) Cell , vol.101 , pp. 199-210
    • Scheufler, C.1    Brinker, A.2    Bourenkov, G.3    Pegoraro, S.4    Moroder, L.5    Bartunik, H.6
  • 192
    • 27944495299 scopus 로고    scopus 로고
    • Chaperoned ubiquitylation--crystal structures of the CHIP U box E3 ubiquitin ligase and a CHIP-Ubc13-Uev1a complex
    • Zhang M, Windheim M, Roe SM, Peggie M, Cohen P, Prodromou C, et al. Chaperoned ubiquitylation--crystal structures of the CHIP U box E3 ubiquitin ligase and a CHIP-Ubc13-Uev1a complex. Mol Cell 2005; 20: 525-538.
    • (2005) Mol Cell , vol.20 , pp. 525-538
    • Zhang, M.1    Windheim, M.2    Roe, S.M.3    Peggie, M.4    Cohen, P.5    Prodromou, C.6
  • 193
    • 10744221887 scopus 로고    scopus 로고
    • Structural basis for recruitment of the ATPase activator Aha1 to the Hsp90 chaperone machinery
    • Meyer P, Prodromou C, Liao C, Hu B, Roe SM, Vaughan CK, et al. Structural basis for recruitment of the ATPase activator Aha1 to the Hsp90 chaperone machinery. EMBO J 2004; 23: 511-519.
    • (2004) EMBO J , vol.23 , pp. 511-519
    • Meyer, P.1    Prodromou, C.2    Liao, C.3    Hu, B.4    Roe, S.M.5    Vaughan, C.K.6
  • 194
    • 0742269688 scopus 로고    scopus 로고
    • The Mechanism of Hsp90 regulation by the protein kinase-specific cochaperone p50(cdc37)
    • Roe SM, Ali MM, Meyer P, Vaughan CK, Panaretou B, Piper PW, et al. The Mechanism of Hsp90 regulation by the protein kinase-specific cochaperone p50(cdc37). Cell 2004; 116: 87-98.
    • (2004) Cell , vol.116 , pp. 87-98
    • Roe, S.M.1    Ali, M.M.2    Meyer, P.3    Vaughan, C.K.4    Panaretou, B.5    Piper, P.W.6
  • 196
    • 33749433916 scopus 로고    scopus 로고
    • Gene expression signature-based chemical genomic prediction identifies a novel class of HSP90 pathway modulators
    • Hieronymus H, Lamb J, Ross KN, Peng XP, Clement C, Rodina A, et al. Gene expression signature-based chemical genomic prediction identifies a novel class of HSP90 pathway modulators. Cancer Cell 2006; 10: 321-330.
    • (2006) Cancer Cell , vol.10 , pp. 321-330
    • Hieronymus, H.1    Lamb, J.2    Ross, K.N.3    Peng, X.P.4    Clement, C.5    Rodina, A.6
  • 197
    • 38349153572 scopus 로고    scopus 로고
    • A novel Hsp90 inhibitor to disrupt Hsp90/Cdc37 complex against pancreatic cancer cells
    • Zhang T, Hamza A, Cao X, Wang B, Yu S, Zhan CG, et al. A novel Hsp90 inhibitor to disrupt Hsp90/Cdc37 complex against pancreatic cancer cells. Mol Cancer Ther 2008; 7: 162-170.
    • (2008) Mol Cancer Ther , vol.7 , pp. 162-170
    • Zhang, T.1    Hamza, A.2    Cao, X.3    Wang, B.4    Yu, S.5    Zhan, C.G.6
  • 198
    • 0034614637 scopus 로고    scopus 로고
    • The hallmarks of cancer
    • Hanahan D, Weinberg RA. The hallmarks of cancer. Cell 2000; 100: 57-70.
    • (2000) Cell , vol.100 , pp. 57-70
    • Hanahan, D.1    Weinberg, R.A.2
  • 199
    • 0034641918 scopus 로고    scopus 로고
    • The biochemistry of apoptosis
    • Hengartner MO. The biochemistry of apoptosis. Nature 2000; 407: 770-776.
    • (2000) Nature , vol.407 , pp. 770-776
    • Hengartner, M.O.1
  • 201
    • 0028982183 scopus 로고
    • Expression of Bcl-xL can confer a multidrug resistance phenotype
    • Minn AJ, Rudin CM, Boise LH, Thompson CB. Expression of Bcl-xL can confer a multidrug resistance phenotype. Blood 1995; 86: 1903-1910.
    • (1995) Blood , vol.86 , pp. 1903-1910
    • Minn, A.J.1    Rudin, C.M.2    Boise, L.H.3    Thompson, C.B.4
  • 202
    • 0031032294 scopus 로고    scopus 로고
    • Bcl-2 and Bcl-XL antagonize the mitochondrial dysfunction preceding nuclear apoptosis induced by chemotherapeutic agents
    • Decaudin D, Geley S, Hirsch T, Castedo M, Marchetti P, Macho A, et al. Bcl-2 and Bcl-XL antagonize the mitochondrial dysfunction preceding nuclear apoptosis induced by chemotherapeutic agents. Cancer Res 1997; 57: 62-67.
    • (1997) Cancer Res , vol.57 , pp. 62-67
    • Decaudin, D.1    Geley, S.2    Hirsch, T.3    Castedo, M.4    Marchetti, P.5    Macho, A.6
  • 203
    • 5244224827 scopus 로고    scopus 로고
    • X-ray and NMR structure of human Bcl-xL, an inhibitor of programmed cell death
    • Muchmore SW, Sattler M, Liang H, Meadows RP, Harlan JE, Yoon HS, et al. X-ray and NMR structure of human Bcl-xL, an inhibitor of programmed cell death. Nature 1996; 381: 335-341.
    • (1996) Nature , vol.381 , pp. 335-341
    • Muchmore, S.W.1    Sattler, M.2    Liang, H.3    Meadows, R.P.4    Harlan, J.E.5    Yoon, H.S.6
  • 205
    • 0030614915 scopus 로고    scopus 로고
    • Structure of Bcl-xL-Bak peptide complex: Recognition between regulators of apoptosis
    • Sattler M, Liang H, Nettesheim D, Meadows RP, Harlan JE, Eberstadt M, et al. Structure of Bcl-xL-Bak peptide complex: recognition between regulators of apoptosis. Science 1997; 275: 983-986.
    • (1997) Science , vol.275 , pp. 983-986
    • Sattler, M.1    Liang, H.2    Nettesheim, D.3    Meadows, R.P.4    Harlan, J.E.5    Eberstadt, M.6
  • 206
    • 0035818885 scopus 로고    scopus 로고
    • Discovery of small-molecule inhibitors of Bcl-2 through structure-based computer screening
    • Enyedy IJ, Ling Y, Nacro K, Tomita Y, Wu X, Cao Y, et al. Discovery of small-molecule inhibitors of Bcl-2 through structure-based computer screening. J Med Chem 2001; 44: 4313-4324.
    • (2001) J Med Chem , vol.44 , pp. 4313-4324
    • Enyedy, I.J.1    Ling, Y.2    Nacro, K.3    Tomita, Y.4    Wu, X.5    Cao, Y.6
  • 207
    • 0034691130 scopus 로고    scopus 로고
    • Structure-based discovery of an organic compound that binds Bcl-2 protein and induces apoptosis of tumor cells
    • Wang JL, Liu D, Zhang ZJ, Shan S, Han X, Srinivasula SM, et al. Structure-based discovery of an organic compound that binds Bcl-2 protein and induces apoptosis of tumor cells. Proc Natl Acad Sci USA 2000; 97: 7124-7129.
    • (2000) Proc Natl Acad Sci USA , vol.97 , pp. 7124-7129
    • Wang, J.L.1    Liu, D.2    Zhang, Z.J.3    Shan, S.4    Han, X.5    Srinivasula, S.M.6
  • 208
    • 1442335327 scopus 로고    scopus 로고
    • Shooting at survivors: Bcl-2 family members as drug targets for cancer
    • Juin P, Geneste O, Raimbaud E, Hickman JA. Shooting at survivors: Bcl-2 family members as drug targets for cancer. Biochim Biophys Acta 2004; 1644: 251-260.
    • (2004) Biochim Biophys Acta , vol.1644 , pp. 251-260
    • Juin, P.1    Geneste, O.2    Raimbaud, E.3    Hickman, J.A.4
  • 211
    • 33750112776 scopus 로고    scopus 로고
    • Structure-based design of potent small-molecule inhibitors of anti-apoptotic Bcl-2 proteins
    • Wang G, Nikolovska-Coleska Z, Yang CY, Wang R, Tang G, Guo J, et al. Structure-based design of potent small-molecule inhibitors of anti-apoptotic Bcl-2 proteins. J Med Chem 2006; 49: 6139-6142.
    • (2006) J Med Chem , vol.49 , pp. 6139-6142
    • Wang, G.1    Nikolovska-Coleska, Z.2    Yang, C.Y.3    Wang, R.4    Tang, G.5    Guo, J.6
  • 212
    • 47049099431 scopus 로고    scopus 로고
    • TW-37, a small-molecule inhibitor of Bcl-2, inhibits cell growth and invasion in pancreatic cancer
    • Wang Z, Song W, Aboukameel A, Mohammad M, Wang G, Banerjee S, et al. TW-37, a small-molecule inhibitor of Bcl-2, inhibits cell growth and invasion in pancreatic cancer. Int J Cancer 2008; 123: 958-966.
    • (2008) Int J Cancer , vol.123 , pp. 958-966
    • Wang, Z.1    Song, W.2    Aboukameel, A.3    Mohammad, M.4    Wang, G.5    Banerjee, S.6
  • 213
    • 66149090396 scopus 로고    scopus 로고
    • TW-37, a small-molecule inhibitor of Bcl-2, inhibits cell growth and induces apoptosis in pancreatic cancer: Involvement of Notch-1 signaling pathway
    • Wang Z, Azmi AS, Ahmad A, Banerjee S, Wang S, Sarkar FH, et al. TW-37, a small-molecule inhibitor of Bcl-2, inhibits cell growth and induces apoptosis in pancreatic cancer: involvement of Notch-1 signaling pathway. Cancer Res 2009; 69: 2757-2765.
    • (2009) Cancer Res , vol.69 , pp. 2757-2765
    • Wang, Z.1    Azmi, A.S.2    Ahmad, A.3    Banerjee, S.4    Wang, S.5    Sarkar, F.H.6
  • 214
    • 66449133268 scopus 로고    scopus 로고
    • TW-37, a small-molecule inhibitor of Bcl-2, mediates S-phase cell cycle arrest and suppresses head and neck tumor angiogenesis
    • Ashimori N, Zeitlin BD, Zhang Z, Warner K, Turkienicz IM, Spalding AC, et al. TW-37, a small-molecule inhibitor of Bcl-2, mediates S-phase cell cycle arrest and suppresses head and neck tumor angiogenesis. Mol Cancer Ther 2009; 8: 893-903.
    • (2009) Mol Cancer Ther , vol.8 , pp. 893-903
    • Ashimori, N.1    Zeitlin, B.D.2    Zhang, Z.3    Warner, K.4    Turkienicz, I.M.5    Spalding, A.C.6
  • 215
    • 34447548988 scopus 로고    scopus 로고
    • Structure-based design of flavonoid compounds as a new class of small-molecule inhibitors of the anti-apoptotic Bcl-2 proteins
    • Tang G, Ding K, Nikolovska-Coleska Z, Yang CY, Qiu S, Shangary S, et al. Structure-based design of flavonoid compounds as a new class of small-molecule inhibitors of the anti-apoptotic Bcl-2 proteins. J Med Chem 2007; 50: 3163-3166.
    • (2007) J Med Chem , vol.50 , pp. 3163-3166
    • Tang, G.1    Ding, K.2    Nikolovska-Coleska, Z.3    Yang, C.Y.4    Qiu, S.5    Shangary, S.6
  • 217
    • 0141569444 scopus 로고    scopus 로고
    • Discovery, characterization, and structure-activity relationships studies of proapoptotic polyphenols targeting B-cell lymphocyte/leukemia-2 proteins
    • Kitada S, Leone M, Sareth S, Zhai D, Reed JC, Pellecchia M. Discovery, characterization, and structure-activity relationships studies of proapoptotic polyphenols targeting B-cell lymphocyte/leukemia-2 proteins. J Med Chem 2003; 46: 4259-4264.
    • (2003) J Med Chem , vol.46 , pp. 4259-4264
    • Kitada, S.1    Leone, M.2    Sareth, S.3    Zhai, D.4    Reed, J.C.5    Pellecchia, M.6
  • 218
    • 0036619804 scopus 로고    scopus 로고
    • Different pathways of cell killing by gossypol enantiomers
    • Qiu J, Levin LR, Buck J, Reidenberg MM. Different pathways of cell killing by gossypol enantiomers. Exp Biol Med 2002; 227: 398-401.
    • (2002) Exp Biol Med , vol.227 , pp. 398-401
    • Qiu, J.1    Levin, L.R.2    Buck, J.3    Reidenberg, M.M.4
  • 219
    • 0032986405 scopus 로고    scopus 로고
    • Inhibition of oncogene product enzyme activity as an approach to cancer chemoprevention. Tyrosine-specific protein kinase inhibition by purpurogallin from Quercus sp. nutgall
    • Abou-Karam M, Shier WT. Inhibition of oncogene product enzyme activity as an approach to cancer chemoprevention. Tyrosine-specific protein kinase inhibition by purpurogallin from Quercus sp. nutgall. Phytother Res 1999; 13: 337-340.
    • (1999) Phytother Res , vol.13 , pp. 337-340
    • Abou-Karam, M.1    Shier, W.T.2
  • 220
    • 0347626109 scopus 로고    scopus 로고
    • Cancer prevention by tea polyphenols is linked to their direct inhibition of antiapoptotic Bcl-2-family proteins
    • Leone M, Zhai D, Sareth S, Kitada S, Reed JC, Pellecchia M. Cancer prevention by tea polyphenols is linked to their direct inhibition of antiapoptotic Bcl-2-family proteins. Cancer Res 2003; 63: 8118-81121.
    • (2003) Cancer Res , vol.63 , pp. 8118-81121
    • Leone, M.1    Zhai, D.2    Sareth, S.3    Kitada, S.4    Reed, J.C.5    Pellecchia, M.6
  • 221
    • 64749098018 scopus 로고    scopus 로고
    • Epigallocatechin-gallate modulates chemotherapy-induced apoptosis in human cholangio-carcinoma cells
    • Lang M, Henson R, Braconi C, Patel T. Epigallocatechin-gallate modulates chemotherapy-induced apoptosis in human cholangio-carcinoma cells. Liver Int 2009; 29: 670-677.
    • (2009) Liver Int , vol.29 , pp. 670-677
    • Lang, M.1    Henson, R.2    Braconi, C.3    Patel, T.4
  • 222
    • 17144438370 scopus 로고    scopus 로고
    • Expression and prognostic significance of IAP-family genes in human cancers and myeloid leukemias
    • Tamm I, Kornblau SM, Segall H, Krajewski S, Welsh K, Kitada S, et al. Expression and prognostic significance of IAP-family genes in human cancers and myeloid leukemias. Clin Cancer Res 2000; 6: 1796-1803.
    • (2000) Clin Cancer Res , vol.6 , pp. 1796-1803
    • Tamm, I.1    Kornblau, S.M.2    Segall, H.3    Krajewski, S.4    Welsh, K.5    Kitada, S.6
  • 223
    • 0037568185 scopus 로고    scopus 로고
    • The X-linked inhibitor of apoptosis protein inhibits taxol-induced apoptosis in LNCaP cells
    • Nomura T, Mimata H, Takeuchi Y, Yamamoto H, Miyamoto E, Nomura Y. The X-linked inhibitor of apoptosis protein inhibits taxol-induced apoptosis in LNCaP cells. Urol Res 2003; 31: 37-44.
    • (2003) Urol Res , vol.31 , pp. 37-44
    • Nomura, T.1    Mimata, H.2    Takeuchi, Y.3    Yamamoto, H.4    Miyamoto, E.5    Nomura, Y.6
  • 224
    • 0034710543 scopus 로고    scopus 로고
    • Translational upregulation of X-linked inhibitor of apoptosis (XIAP) increases resistance to radiation induced cell death
    • Holcik M, Yeh C, Korneluk RG, Chow T. Translational upregulation of X-linked inhibitor of apoptosis (XIAP) increases resistance to radiation induced cell death. Oncogene 2000; 19: 4174-4177.
    • (2000) Oncogene , vol.19 , pp. 4174-4177
    • Holcik, M.1    Yeh, C.2    Korneluk, R.G.3    Chow, T.4
  • 225
    • 0034616945 scopus 로고    scopus 로고
    • Smac, a mitochondrial protein that promotes cytochrome c-dependent caspase activation by eliminating IAP inhibition
    • Du C, Fang M, Li Y, Li L, Wang X. Smac, a mitochondrial protein that promotes cytochrome c-dependent caspase activation by eliminating IAP inhibition. Cell 2000; 102: 33-42.
    • (2000) Cell , vol.102 , pp. 33-42
    • Du, C.1    Fang, M.2    Li, Y.3    Li, L.4    Wang, X.5
  • 226
    • 0034616942 scopus 로고    scopus 로고
    • Identification of DIABLO, a mammalian protein that promotes apoptosis by binding to and antagonizing IAP proteins
    • Verhagen AM, Ekert PG, Pakusch M, Silke J, Connolly LM, Reid GE, et al. Identification of DIABLO, a mammalian protein that promotes apoptosis by binding to and antagonizing IAP proteins. Cell 2000; 102: 43-53.
    • (2000) Cell , vol.102 , pp. 43-53
    • Verhagen, A.M.1    Ekert, P.G.2    Pakusch, M.3    Silke, J.4    Connolly, L.M.5    Reid, G.E.6
  • 227
    • 0034700491 scopus 로고    scopus 로고
    • Structural basis of IAP recognition by Smac/DIABLO
    • Wu G, Chai J, Suber TL, Wu JW, Du C, Wang X, et al. Structural basis of IAP recognition by Smac/DIABLO. Nature 2000; 408: 1008-1012.
    • (2000) Nature , vol.408 , pp. 1008-1012
    • Wu, G.1    Chai, J.2    Suber, T.L.3    Wu, J.W.4    Du, C.5    Wang, X.6
  • 228
    • 0034700495 scopus 로고    scopus 로고
    • Structural basis for binding of Smac/DIABLO to the XIAP BIR3 domain
    • Liu Z, Sun C, Olejniczak ET, Meadows RP, Betz SF, Oost T, et al. Structural basis for binding of Smac/DIABLO to the XIAP BIR3 domain. Nature 2000; 408: 1004-1008.
    • (2000) Nature , vol.408 , pp. 1004-1008
    • Liu, Z.1    Sun, C.2    Olejniczak, E.T.3    Meadows, R.P.4    Betz, S.F.5    Oost, T.6
  • 229
    • 2342448582 scopus 로고    scopus 로고
    • Discovery of embelin as a cell-permeable, small-molecular weight inhibitor of XIAP through structure-based computational screening of a traditional herbal medicine three-dimensional structure database
    • Nikolovska-Coleska Z, Xu L, Hu Z, Tomita Y, Li P, Roller PP, et al. Discovery of embelin as a cell-permeable, small-molecular weight inhibitor of XIAP through structure-based computational screening of a traditional herbal medicine three-dimensional structure database. J Med Chem 2004; 47: 2430-2440.
    • (2004) J Med Chem , vol.47 , pp. 2430-2440
    • Nikolovska-Coleska, Z.1    Xu, L.2    Hu, Z.3    Tomita, Y.4    Li, P.5    Roller, P.P.6
  • 230
    • 68149132860 scopus 로고    scopus 로고
    • Micellar delivery of bicalutamide and embelin for treating prostate cancer
    • Danquah M, Li F, Duke CB, 3rd, Miller DD, Mahato RI. Micellar delivery of bicalutamide and embelin for treating prostate cancer. Pharm Res 2009; 26: 2081-2092.
    • (2009) Pharm Res , vol.26 , pp. 2081-2092
    • Danquah, M.1    Li, F.2    Duke 3rd, C.B.3    Miller, D.D.4    Mahato, R.I.5
  • 231
    • 66349089835 scopus 로고    scopus 로고
    • Peroxisome proliferator-activated receptor-gamma contributes to the inhibitory effects of Embelin on colon carcinogenesis
    • Dai Y, Qiao L, Chan KW, Yang M, Ye J, Ma J, et al. Peroxisome proliferator-activated receptor-gamma contributes to the inhibitory effects of Embelin on colon carcinogenesis. Cancer Res 2009; 69: 4776-4783.
    • (2009) Cancer Res , vol.69 , pp. 4776-4783
    • Dai, Y.1    Qiao, L.2    Chan, K.W.3    Yang, M.4    Ye, J.5    Ma, J.6
  • 232
    • 33749259614 scopus 로고    scopus 로고
    • Design, synthesis, and characterization of new embelin derivatives as potent inhibitors of X-linked inhibitor of apoptosis protein
    • Chen J, Nikolovska-Coleska Z, Wang G, Qiu S, Wang S. Design, synthesis, and characterization of new embelin derivatives as potent inhibitors of X-linked inhibitor of apoptosis protein. Bioorg Med Chem Lett 2006; 16: 5805-5808.
    • (2006) Bioorg Med Chem Lett , vol.16 , pp. 5805-5808
    • Chen, J.1    Nikolovska-Coleska, Z.2    Wang, G.3    Qiu, S.4    Wang, S.5
  • 233
    • 19944426570 scopus 로고    scopus 로고
    • Structure-based design of potent, conformationally constrained Smac mimetics
    • Sun H, Nikolovska-Coleska Z, Yang CY, Xu L, Liu M, Tomita Y, et al. Structure-based design of potent, conformationally constrained Smac mimetics. J Am Chem Soc 2004; 126: 16686-16687.
    • (2004) J Am Chem Soc , vol.126 , pp. 16686-16687
    • Sun, H.1    Nikolovska-Coleska, Z.2    Yang, C.Y.3    Xu, L.4    Liu, M.5    Tomita, Y.6
  • 234
    • 19944434282 scopus 로고    scopus 로고
    • Structure-based design, synthesis and biochemical testing of novel and potent Smac peptido-mimetics
    • Sun H, Nikolovska-Coleska Z, Chen J, Yang CY, Tomita Y, Pan H, et al. Structure-based design, synthesis and biochemical testing of novel and potent Smac peptido-mimetics. Bioorg Med Chem Lett 2005; 15: 793-797.
    • (2005) Bioorg Med Chem Lett , vol.15 , pp. 793-797
    • Sun, H.1    Nikolovska-Coleska, Z.2    Chen, J.3    Yang, C.Y.4    Tomita, Y.5    Pan, H.6
  • 235
    • 56749182336 scopus 로고    scopus 로고
    • Fragment-based design of small molecule X-linked inhibitor of apoptosis protein inhibitors
    • Huang JW, Zhang Z, Wu B, Cellitti JF, Zhang X, Dahl R, et al. Fragment-based design of small molecule X-linked inhibitor of apoptosis protein inhibitors. J Med Chem 2008; 51: 7111-7118.
    • (2008) J Med Chem , vol.51 , pp. 7111-7118
    • Huang, J.W.1    Zhang, Z.2    Wu, B.3    Cellitti, J.F.4    Zhang, X.5    Dahl, R.6
  • 236
    • 4143099131 scopus 로고    scopus 로고
    • Discovery of potent antagonists of the antiapoptotic protein XIAP for the treatment of cancer
    • Oost TK, Sun C, Armstrong RC, Al-Assaad AS, Betz SF, Deckwerth TL, et al. Discovery of potent antagonists of the antiapoptotic protein XIAP for the treatment of cancer. J Med Chem 2004; 47: 4417-4426.
    • (2004) J Med Chem , vol.47 , pp. 4417-4426
    • Oost, T.K.1    Sun, C.2    Armstrong, R.C.3    Al-Assaad, A.S.4    Betz, S.F.5    Deckwerth, T.L.6
  • 237
    • 56749160346 scopus 로고    scopus 로고
    • Structure-based design, synthesis, evaluation, and crystallographic studies of conformationally constrained Smac mimetics as inhibitors of the X-linked inhibitor of apoptosis protein (XIAP)
    • Sun H, Stuckey JA, Nikolovska-Coleska Z, Qin D, Meagher JL, Qiu S, et al. Structure-based design, synthesis, evaluation, and crystallographic studies of conformationally constrained Smac mimetics as inhibitors of the X-linked inhibitor of apoptosis protein (XIAP). J Med Chem 2008; 51: 7169-7180.
    • (2008) J Med Chem , vol.51 , pp. 7169-7180
    • Sun, H.1    Stuckey, J.A.2    Nikolovska-Coleska, Z.3    Qin, D.4    Meagher, J.L.5    Qiu, S.6
  • 240
    • 0035831022 scopus 로고    scopus 로고
    • Structural basis of caspase inhibition by XIAP: Differential roles of the linker versus the BIR domain
    • Huang Y, Park YC, Rich RL, Segal D, Myszka DG, Wu H. Structural basis of caspase inhibition by XIAP: differential roles of the linker versus the BIR domain. Cell 2001; 104: 781-790.
    • (2001) Cell , vol.104 , pp. 781-790
    • Huang, Y.1    Park, Y.C.2    Rich, R.L.3    Segal, D.4    Myszka, D.G.5    Wu, H.6
  • 241
    • 35648961848 scopus 로고    scopus 로고
    • A dimeric Smac/diablo peptide directly relieves caspase-3 inhibition by XIAP. Dynamic and cooperative regulation of XIAP by Smac/Diablo
    • Gao Z, Tian Y, Wang J, Yin Q, Wu H, Li YM, et al. A dimeric Smac/diablo peptide directly relieves caspase-3 inhibition by XIAP. Dynamic and cooperative regulation of XIAP by Smac/Diablo. J Biol Chem 2007; 282: 3018-3027.
    • (2007) J Biol Chem , vol.282 , pp. 3018-3027
    • Gao, Z.1    Tian, Y.2    Wang, J.3    Yin, Q.4    Wu, H.5    Li, Y.M.6
  • 242
    • 37049019494 scopus 로고    scopus 로고
    • Design, synthesis, and characterization of a potent, nonpep-tide, cell-permeable, bivalent Smac mimetic that concurrently targets both the BIR2 and BIR3 domains in XIAP
    • Sun H, Nikolovska-Coleska Z, Lu J, Meagher JL, Yang CY, Qiu S, et al. Design, synthesis, and characterization of a potent, nonpep-tide, cell-permeable, bivalent Smac mimetic that concurrently targets both the BIR2 and BIR3 domains in XIAP. J Am Chem Soc 2007; 129: 15279-15294.
    • (2007) J Am Chem Soc , vol.129 , pp. 15279-15294
    • Sun, H.1    Nikolovska-Coleska, Z.2    Lu, J.3    Meagher, J.L.4    Yang, C.Y.5    Qiu, S.6
  • 243
    • 72949124730 scopus 로고    scopus 로고
    • Virtual screening for the discovery of bioactive natural products
    • In: Peterson F, Amstutz R, Eds., Basel, Switzerland: Birkhäuser Verlag
    • Rollinger JM, Stuppner H, Langer T. Virtual screening for the discovery of bioactive natural products. In: Peterson F, Amstutz R, Eds. Natural Compounds as Drugs. Basel, Switzerland: Birkhäuser Verlag 2008; Vol. 1: pp. 212-249.
    • (2008) Natural Compounds As Drugs , vol.1 , pp. 212-249
    • Rollinger, J.M.1    Stuppner, H.2    Langer, T.3


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.