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Volumn 3, Issue 7, 2008, Pages 819-831

Alternative assay formats to identify diverse inhibitors of protein kinases

Author keywords

Allosteric; Assay technology; ATP competitive; Binding; High throughput screening; Hit identificafion; Inhibitor; Kinase assay; Protein kinase

Indexed keywords

ADENOSINE DIPHOSPHATE; ADENOSINE TRIPHOSPHATE; DASATINIB; ERLOTINIB; GEFITINIB; IMATINIB; LAPATINIB; PHOSPHOTRANSFERASE INHIBITOR; PROTEIN KINASE; PROTEIN KINASE INHIBITOR; PURINE; SORAFENIB; SUNITINIB;

EID: 48049114377     PISSN: 17460441     EISSN: None     Source Type: Journal    
DOI: 10.1517/17460441.3.7.819     Document Type: Review
Times cited : (4)

References (51)
  • 1
    • 0037032835 scopus 로고    scopus 로고
    • The protein kinase complement of the human genome
    • Manning G, Whyte DB, Martinez R, et al. The protein kinase complement of the human genome. Science 2002;298:1912-34
    • (2002) Science , vol.298 , pp. 1912-1934
    • Manning, G.1    Whyte, D.B.2    Martinez, R.3
  • 2
    • 48049106017 scopus 로고    scopus 로고
    • editor, Drug discovery and development Technology in transition, Churchill Livingstone Elsevier Publishers;
    • Stoeckli K, Haag H. High-throughput screening. Chapter 8. In: Rang HP, editor, Drug discovery and development (Technology in transition). Churchill Livingstone Elsevier Publishers; 2006. p. 99-119
    • (2006) High-throughput screening , pp. 99-119
    • Stoeckli, K.1    Haag, H.2
  • 3
    • 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(4):309-15
    • (2002) Nat Rev Drug Discov , vol.1 , Issue.4 , pp. 309-315
    • Cohen, P.1
  • 4
    • 0029993727 scopus 로고    scopus 로고
    • Active and inactive protein kinases: Structural basis for regulation
    • Johnson LN, Noble ME, Owen DJ. Active and inactive protein kinases: structural basis for regulation. Cell 1996;85(2):149-58
    • (1996) Cell , vol.85 , Issue.2 , pp. 149-158
    • Johnson, L.N.1    Noble, M.E.2    Owen, D.J.3
  • 5
    • 0036161020 scopus 로고    scopus 로고
    • A new model for random screening inhibitors of vascular endothelial growth factor receptor 1 kinase
    • Zhuang SF, Zhou CH, Qian J, et al. A new model for random screening inhibitors of vascular endothelial growth factor receptor 1 kinase. Acta Pharmacol Sin 2002;23(2):117-23
    • (2002) Acta Pharmacol Sin , vol.23 , Issue.2 , pp. 117-123
    • Zhuang, S.F.1    Zhou, C.H.2    Qian, J.3
  • 6
    • 0036808565 scopus 로고    scopus 로고
    • Developments of a time-resolved fluorescent assay for measuring tyrosine-phosphorylated proteins in cells
    • Waddleton D, Ramachandran C, Wang QP. Developments of a time-resolved fluorescent assay for measuring tyrosine-phosphorylated proteins in cells. Anal Biochem 2002;309(1):150-7
    • (2002) Anal Biochem , vol.309 , Issue.1 , pp. 150-157
    • Waddleton, D.1    Ramachandran, C.2    Wang, Q.P.3
  • 7
    • 0037016352 scopus 로고    scopus 로고
    • A scintillation proximity assay for studying inhibitors of tau protein kinase II/cdk5 using a 96-well format
    • Evans DB, Rank KB, Sharma SK. A scintillation proximity assay for studying inhibitors of tau protein kinase II/cdk5 using a 96-well format. J Biochem Biophys Methods 2002;50(2-3):151-61
    • (2002) J Biochem Biophys Methods , vol.50 , Issue.2-3 , pp. 151-161
    • Evans, D.B.1    Rank, K.B.2    Sharma, S.K.3
  • 8
    • 0041828800 scopus 로고    scopus 로고
    • A generic time-resolved fluorescence assay for serine/threonine kinase activity: Application to Cdc7/Dbf4
    • Xu K, Stern AS, Levin W, et al. A generic time-resolved fluorescence assay for serine/threonine kinase activity: application to Cdc7/Dbf4. J Biochem Mol Biol 2003;36(4):421-5
    • (2003) J Biochem Mol Biol , vol.36 , Issue.4 , pp. 421-425
    • Xu, K.1    Stern, A.S.2    Levin, W.3
  • 9
    • 33751558665 scopus 로고    scopus 로고
    • Homogeneous and nonradioactive high-throughput screening platform for the characterization of kinase inhibitors in cell lysates
    • Guenat S, Rouleau N, Bielmann C, et al. Homogeneous and nonradioactive high-throughput screening platform for the characterization of kinase inhibitors in cell lysates. J Biomol Screen 2006;11(8):1015-26
    • (2006) J Biomol Screen , vol.11 , Issue.8 , pp. 1015-1026
    • Guenat, S.1    Rouleau, N.2    Bielmann, C.3
  • 10
    • 1642270826 scopus 로고    scopus 로고
    • Recent kinase and kinase inhibitor X-ray structures: Mechanisms of inhibition and selectivity insights
    • Cherry M, Williams DH. Recent kinase and kinase inhibitor X-ray structures: mechanisms of inhibition and selectivity insights. Curr Med Chem 2004;11(6):663-73
    • (2004) Curr Med Chem , vol.11 , Issue.6 , pp. 663-673
    • Cherry, M.1    Williams, D.H.2
  • 11
    • 0344626926 scopus 로고    scopus 로고
    • Structural basis for the autoinhibition of c-Abl tyrosine kinase
    • Nagar B, Hantschel O, Young MA, et al. Structural basis for the autoinhibition of c-Abl tyrosine kinase. Cell 2003;112(6):859-71
    • (2003) Cell , vol.112 , Issue.6 , pp. 859-871
    • Nagar, B.1    Hantschel, O.2    Young, M.A.3
  • 12
    • 0036635291 scopus 로고    scopus 로고
    • Glivec (STI571, imatinib), a rationally developed, targeted anticancer drug
    • Capdeville R, Buchdunger E, Zimmermann J, et al. Glivec (STI571, imatinib), a rationally developed, targeted anticancer drug. Nat Rev Drug Discov 2002;1(7):493-502
    • (2002) Nat Rev Drug Discov , vol.1 , Issue.7 , pp. 493-502
    • Capdeville, R.1    Buchdunger, E.2    Zimmermann, J.3
  • 13
    • 0034665713 scopus 로고    scopus 로고
    • Structural mechanism for STI-571 inhibition of abelson tyrosine kinase
    • Schindler T, Bornmann W, Pellicena P, et al. Structural mechanism for STI-571 inhibition of abelson tyrosine kinase. Science 2000;289(5486):1938-42
    • (2000) Science , vol.289 , Issue.5486 , pp. 1938-1942
    • Schindler, T.1    Bornmann, W.2    Pellicena, P.3
  • 14
    • 18344395134 scopus 로고    scopus 로고
    • Inhibition of p38 MAP kinase by utilizing a novel allosteric binding site
    • Pargellis C, Tong L, Churchill L, et al. Inhibition of p38 MAP kinase by utilizing a novel allosteric binding site. Nat Struct Biol 2002;9(4):268-72
    • (2002) Nat Struct Biol , vol.9 , Issue.4 , pp. 268-272
    • Pargellis, C.1    Tong, L.2    Churchill, L.3
  • 15
    • 12144289677 scopus 로고    scopus 로고
    • Mechanism of activation of the RAF-ERK signaling pathway by oncogenic mutations of B-RAF
    • Wan PTC, Garnett MJ, Roe SM, et al. Mechanism of activation of the RAF-ERK signaling pathway by oncogenic mutations of B-RAF. Cell 2004;116(6):855-67
    • (2004) Cell , vol.116 , Issue.6 , pp. 855-867
    • Wan, P.T.C.1    Garnett, M.J.2    Roe, S.M.3
  • 16
    • 12144290647 scopus 로고    scopus 로고
    • Advances in the structural biology, design and clinical development of VEGF-R kinase inhibitors for the treatment of angiogenesis
    • Manley PW, Bold G, Brüggen J, et al. Advances in the structural biology, design and clinical development of VEGF-R kinase inhibitors for the treatment of angiogenesis. Biochim Biophys Acta 2004;1697(1-2):17-27
    • (2004) Biochim Biophys Acta , vol.1697 , Issue.1-2 , pp. 17-27
    • Manley, P.W.1    Bold, G.2    Brüggen, J.3
  • 17
    • 34548489855 scopus 로고    scopus 로고
    • Discovery of novel benzimidazoles as potent inhibitors of TIE-2 and VEGFR-2 tyrosine kinase receptors
    • Hasegawa M, Nishigakin N, Washio Y, et al. Discovery of novel benzimidazoles as potent inhibitors of TIE-2 and VEGFR-2 tyrosine kinase receptors. J Med Chem 2007;50(18):4453-70
    • (2007) J Med Chem , vol.50 , Issue.18 , pp. 4453-4470
    • Hasegawa, M.1    Nishigakin, N.2    Washio, Y.3
  • 18
    • 29244448317 scopus 로고    scopus 로고
    • Prevention of MKK6-dependent activation by binding to p38alpha MAP kinase
    • Sullivan JE, Holdgate GA, Campbell D, et al. Prevention of MKK6-dependent activation by binding to p38alpha MAP kinase. Biochemistry 2005;44(50):16475-90
    • (2005) Biochemistry , vol.44 , Issue.50 , pp. 16475-16490
    • Sullivan, J.E.1    Holdgate, G.A.2    Campbell, D.3
  • 19
    • 19744365702 scopus 로고    scopus 로고
    • A small molecule-kinase interaction map for clinical kinase inhibitors
    • Fabian MA, Biggs WH 3rd, Treiber DK, et al. A small molecule-kinase interaction map for clinical kinase inhibitors. Nat Biotechnol 2005;23(3):329-36
    • (2005) Nat Biotechnol , vol.23 , Issue.3 , pp. 329-336
    • Fabian, M.A.1    Biggs 3rd, W.H.2    Treiber, D.K.3
  • 20
    • 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(12):937-47
    • (2004) Nat Rev Cancer , vol.4 , Issue.12 , pp. 937-947
    • Sebolt-Leopold, J.S.1    Herrera, R.2
  • 21
    • 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, et al. Structures of human MAP kinase kinase 1 (MEK1) and MEK2 describe novel noncompetitive kinase inhibition. Nat Struct Mol Biol 2004;11(12):1192-7
    • (2004) Nat Struct Mol Biol , vol.11 , Issue.12 , pp. 1192-1197
    • Ohren, J.F.1    Chen, H.2    Pavlovsky, A.3
  • 22
    • 0034306450 scopus 로고    scopus 로고
    • Specificity and mechanism of action of some commonly used protein kinase inhibitors
    • Davies SP, Reddy H, Caivano M, et al. Specificity and mechanism of action of some commonly used protein kinase inhibitors. Biochem J 2000;351(1):95-105
    • (2000) Biochem J , vol.351 , Issue.1 , pp. 95-105
    • Davies, S.P.1    Reddy, H.2    Caivano, M.3
  • 23
    • 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, 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(18):6652-9
    • (2004) Cancer Res , vol.64 , Issue.18 , pp. 6652-6659
    • Wood, E.R.1    Truesdale, A.T.2    McDonald, O.B.3
  • 24
    • 0037013143 scopus 로고    scopus 로고
    • The conformational plasticity of protein kinases
    • Huse M, Kuriyan J. The conformational plasticity of protein kinases. Cell 2002;109:275-82
    • (2002) Cell , vol.109 , pp. 275-282
    • Huse, M.1    Kuriyan, J.2
  • 25
    • 0348133551 scopus 로고    scopus 로고
    • IQ technology: Development of a universal, homogeneous method for high throughput screening and phosphatase activity
    • McCaulry TJ, Stanaitis ML, Dean SM, et al. IQ technology: development of a universal, homogeneous method for high throughput screening and phosphatase activity. J Assoc Lab Automation 2003;8(2):36-40
    • (2003) J Assoc Lab Automation , vol.8 , Issue.2 , pp. 36-40
    • McCaulry, T.J.1    Stanaitis, M.L.2    Dean, S.M.3
  • 26
    • 18844404436 scopus 로고    scopus 로고
    • Using IMAP technology to identify kinase inhibitors: Comparison with a substrate depletion approach and analysis of the nature of false positives
    • Singh P, Lillywhite B, Bannaghan C, et al. Using IMAP technology to identify kinase inhibitors: comparison with a substrate depletion approach and analysis of the nature of false positives. Comb Chem High Throughput Screen 2005;8:319-25
    • (2005) Comb Chem High Throughput Screen , vol.8 , pp. 319-325
    • Singh, P.1    Lillywhite, B.2    Bannaghan, C.3
  • 27
    • 0025845205 scopus 로고
    • The pyruvate-coupled assay for ATPases: A critical analysis
    • Jenkins WT. The pyruvate-coupled assay for ATPases: a critical analysis. Anal Biochem 1991;194(1):136-9
    • (1991) Anal Biochem , vol.194 , Issue.1 , pp. 136-139
    • Jenkins, W.T.1
  • 28
    • 17344367525 scopus 로고    scopus 로고
    • Development of a non-radioactive, 384-well format assay to detect inhibitors of the mitogen-activated protein kinase kinase 4
    • Togame H, Fuchikami K, Sagara A, et al. Development of a non-radioactive, 384-well format assay to detect inhibitors of the mitogen-activated protein kinase kinase 4. Assay Drug Dev Technol 2005;31:65-76
    • (2005) Assay Drug Dev Technol , vol.31 , pp. 65-76
    • Togame, H.1    Fuchikami, K.2    Sagara, A.3
  • 29
    • 2442436388 scopus 로고    scopus 로고
    • Identification of kinase inhibitors by an ATP depletion method
    • Singh P, Harden BJ, Lillywhite BJ, et al. Identification of kinase inhibitors by an ATP depletion method. Assay Drug Dev Tech 2004;2(2):161-9
    • (2004) Assay Drug Dev Tech , vol.2 , Issue.2 , pp. 161-169
    • Singh, P.1    Harden, B.J.2    Lillywhite, B.J.3
  • 30
    • 48049090717 scopus 로고    scopus 로고
    • Available from: http://www.berthold-ds.com (PKLight assay, developed by Cambrex)
    • Available from: http://www.berthold-ds.com (PKLight assay, developed by Cambrex)
  • 31
    • 48049116682 scopus 로고    scopus 로고
    • Available from: http://www.promega.com (Kinase-Glo™, from Promega)
    • Available from: http://www.promega.com (Kinase-Glo™, from Promega)
  • 32
    • 48049083577 scopus 로고    scopus 로고
    • Available from: http://www.biothema.com (Kinase reaction rate kit, from BioThema)
    • Available from: http://www.biothema.com (Kinase reaction rate kit, from BioThema)
  • 33
    • 19944433628 scopus 로고    scopus 로고
    • Identification and characterization of pleckstrin-homology-domain-dependent and isoenzyme-specific Akt inhibitors
    • Barnett SF, Defeo-Jones D, Fu S, et al. Identification and characterization of pleckstrin-homology-domain-dependent and isoenzyme-specific Akt inhibitors. Biochem J 2005;385(2):399-408
    • (2005) Biochem J , vol.385 , Issue.2 , pp. 399-408
    • Barnett, S.F.1    Defeo-Jones, D.2    Fu, S.3
  • 34
    • 4644223114 scopus 로고    scopus 로고
    • Discovery and characterization of a substrate selective p38alpha inhibitor
    • Davidson W, Frego L, Peet GW, et al. Discovery and characterization of a substrate selective p38alpha inhibitor. Biochemistry 2004;43(37):11658-71
    • (2004) Biochemistry , vol.43 , Issue.37 , pp. 11658-11671
    • Davidson, W.1    Frego, L.2    Peet, G.W.3
  • 35
    • 2442449561 scopus 로고    scopus 로고
    • Development of a fluorescence polarization bead-based coupled assay to target different activity/conformation states of a protein kinase
    • Lu Z, Yin Z, James L, et al. Development of a fluorescence polarization bead-based coupled assay to target different activity/conformation states of a protein kinase. J Biomol Screen 2004;9:309-21
    • (2004) J Biomol Screen , vol.9 , pp. 309-321
    • Lu, Z.1    Yin, Z.2    James, L.3
  • 36
    • 48049097544 scopus 로고    scopus 로고
    • Available from: http://www.discoverx.com (HitHunter™ EFC Kutase Assays, DiscoveRx)
    • Available from: http://www.discoverx.com (HitHunter™ EFC Kutase Assays, DiscoveRx)
  • 37
    • 0141768651 scopus 로고    scopus 로고
    • A high-throughput, nonisotopic, competitive binding assay for kinases using nonselective inhibitor probes (ED-NSIP™)
    • Vainshtein I, Silveria S, Kaul P, et al. A high-throughput, nonisotopic, competitive binding assay for kinases using nonselective inhibitor probes (ED-NSIP™). J Biomol Screen 2002;7(6):507-14
    • (2002) J Biomol Screen , vol.7 , Issue.6 , pp. 507-514
    • Vainshtein, I.1    Silveria, S.2    Kaul, P.3
  • 38
    • 48049088805 scopus 로고    scopus 로고
    • Available from: http://www.corning.com_tm (Epic™ System, Corning™)
    • Available from: http://www.corning.com_tm (Epic™ System, Corning™)
  • 39
    • 48049097096 scopus 로고    scopus 로고
    • Available from: http://www.srubiosystems.com (BIND Reader™, SRU Biosystems)
    • Available from: http://www.srubiosystems.com (BIND Reader™, SRU Biosystems)
  • 40
    • 33751231711 scopus 로고    scopus 로고
    • Optical biosensors: Where next and how soon?
    • Cooper MA. Optical biosensors: where next and how soon? Drug Discov Today 2006;11(23/24):1061-7
    • (2006) Drug Discov Today , vol.11 , Issue.23-24 , pp. 1061-1067
    • Cooper, M.A.1
  • 41
    • 33751218906 scopus 로고    scopus 로고
    • Non-optical screening platforms: The next wave in label-free screening?
    • Cooper MA. Non-optical screening platforms: the next wave in label-free screening? Drug Discov Today 2006;11(23/24):1068-74
    • (2006) Drug Discov Today , vol.11 , Issue.23-24 , pp. 1068-1074
    • Cooper, M.A.1
  • 42
    • 20444451242 scopus 로고    scopus 로고
    • The discovery of novel protein kinase inhibitors by using fragment-based high-throughput x-ray crystallography
    • Gill A, Cleasby A, Jhoti H. The discovery of novel protein kinase inhibitors by using fragment-based high-throughput x-ray crystallography. Chembiochem 2005;6(3):506-12
    • (2005) Chembiochem , vol.6 , Issue.3 , pp. 506-512
    • Gill, A.1    Cleasby, A.2    Jhoti, H.3
  • 43
    • 33644889108 scopus 로고    scopus 로고
    • Allosteric inhibitors of Bcr-abl-dependent cell proliferation
    • Adrián FJ, Ding Q, Sim T, et al. Allosteric inhibitors of Bcr-abl-dependent cell proliferation. Nat Chem Biol 2006;2(2):95-102
    • (2006) Nat Chem Biol , vol.2 , Issue.2 , pp. 95-102
    • Adrián, F.J.1    Ding, Q.2    Sim, T.3
  • 44
    • 48049117349 scopus 로고    scopus 로고
    • Potent and selective in vitro and in vivo inhibition of tumor proliferation by KX01, a novel non-ATP competitive Src inhibitor
    • abstract 3245
    • Hangauer D, Gelman D, Dyster L, et al. Potent and selective in vitro and in vivo inhibition of tumor proliferation by KX01, a novel non-ATP competitive Src inhibitor [abstract 3245]. Proc Am Cancer Res 2007;48
    • (2007) Proc Am Cancer Res , pp. 48
    • Hangauer, D.1    Gelman, D.2    Dyster, L.3
  • 45
    • 4344576752 scopus 로고    scopus 로고
    • The critical features and the mechanism of inhibition of a kinase interaction motif-based peptide inhibitor of JNK
    • Barr RK, Boehm I, Attwood PV, et al. The critical features and the mechanism of inhibition of a kinase interaction motif-based peptide inhibitor of JNK. J Biol Chem 2004;279(35):36327-38
    • (2004) J Biol Chem , vol.279 , Issue.35 , pp. 36327-36338
    • Barr, R.K.1    Boehm, I.2    Attwood, P.V.3
  • 46
    • 34247517344 scopus 로고    scopus 로고
    • Kinetic characterization of human JNK2alpha2 reaction mechanism using substrate competitive inhibitors
    • Niu L, Chang KC, Wilson S, et al. Kinetic characterization of human JNK2alpha2 reaction mechanism using substrate competitive inhibitors. Biochemistry 2007;46(16):4775-84
    • (2007) Biochemistry , vol.46 , Issue.16 , pp. 4775-4784
    • Niu, L.1    Chang, K.C.2    Wilson, S.3
  • 47
    • 34547817154 scopus 로고    scopus 로고
    • A new paradigm for protein kinase inhibition: Blocking phosphorylation without directly targeting ATP binding
    • Bogoyevitch MA, Fairlie DP. A new paradigm for protein kinase inhibition: blocking phosphorylation without directly targeting ATP binding. Drug Discov Today 2007;12(15-16):622-33
    • (2007) Drug Discov Today , vol.12 , Issue.15-16 , pp. 622-633
    • Bogoyevitch, M.A.1    Fairlie, D.P.2
  • 48
    • 33750906582 scopus 로고    scopus 로고
    • Maximising discovery using kinase assays
    • Kamath L. Maximising discovery using kinase assays. Genetic Engineering News 2006;26(18):1
    • (2006) Genetic Engineering News , vol.26 , Issue.18 , pp. 1
    • Kamath, L.1
  • 49
    • 0033003760 scopus 로고    scopus 로고
    • A simple statistical parameter for use in evaluating and validation of high-throughput screening assays
    • Zhang JH, Chung TD, Oldenburg KR. A simple statistical parameter for use in evaluating and validation of high-throughput screening assays. J Biomol Screen 1999;4:67-73
    • (1999) J Biomol Screen , vol.4 , pp. 67-73
    • Zhang, J.H.1    Chung, T.D.2    Oldenburg, K.R.3
  • 50
    • 33947101019 scopus 로고    scopus 로고
    • Patterns of somatic mutation in human cancer genomes
    • Greenman C, Stephens P, Smith R, et al. Patterns of somatic mutation in human cancer genomes. Nature 2007;446(7132):153-8
    • (2007) Nature , vol.446 , Issue.7132 , pp. 153-158
    • Greenman, C.1    Stephens, P.2    Smith, R.3
  • 51
    • 14744274624 scopus 로고    scopus 로고
    • Comparative analysis of two clinically active BCR-ABL kinase inhibitors reveals the role of conformation-specific binding in resistance
    • Burgess MR, Skaggs BJ, Shah NP, et al. Comparative analysis of two clinically active BCR-ABL kinase inhibitors reveals the role of conformation-specific binding in resistance. Proc Natl Acad Sci USA 2005;102(9):3395-400
    • (2005) Proc Natl Acad Sci USA , vol.102 , Issue.9 , pp. 3395-3400
    • Burgess, M.R.1    Skaggs, B.J.2    Shah, N.P.3


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.