메뉴 건너뛰기




Volumn 451, Issue 2, 2013, Pages 313-328

A broad activity screen in support of a chemogenomic map for kinase signalling research and drug discovery

Author keywords

DFG motif; Functional genomics; Inhibitor; Kinase; Polypharmacology; Profile

Indexed keywords

4 (1 AMINOETHYL) N (4 PYRIDYL)CYCLOHEXANECARBOXAMIDE; 4 (3 BROMOANILINO) 6 (METHYLAMINO)PYRIDO[3,4 D]PYRIMIDINE; 4 (4 FLUOROPHENYL) 2 (4 METHYLSULFINYLPHENYL) 5 (4 PYRIDYL)IMIDAZOLE; 4 (4 FLUOROPHENYL) 2 (4 NITROPHENYL) 5 (4 PYRIDYL)IMIDAZOLE; 5 (2 AMINO 4 PYRIMIDINYL) 4 (4 FLUOROPHENYL) 1 (4 PIPERIDINYL)IMIDAZOLE; ANTHRA[1,9 CD]PYRAZOL 6(2H) ONE; FASUDIL; PHOSPHOTRANSFERASE INHIBITOR; PROTEIN KINASE SYK INHIBITOR; PROTEIN TYROSINE KINASE INHIBITOR;

EID: 84875619719     PISSN: 02646021     EISSN: 14708728     Source Type: Journal    
DOI: 10.1042/BJ20121418     Document Type: Article
Times cited : (112)

References (63)
  • 2
    • 57749188299 scopus 로고    scopus 로고
    • Targeting cancer with small molecule kinase inhibitors
    • Zhang, J., Yang, P. L. and Gray, N. S. (2009) Targeting cancer with small molecule kinase inhibitors. Nat. Rev. Cancer 9, 28-39
    • (2009) Nat. Rev. Cancer , vol.9 , pp. 28-39
    • Zhang, J.1    Yang, P.L.2    Gray, N.S.3
  • 4
    • 77954315861 scopus 로고    scopus 로고
    • Spleen tyrosine kinases: Biology, therapeutic targets and drugs
    • Riccaboni, M., Bianchi, I. and Petrillo, P. (2010) Spleen tyrosine kinases: biology, therapeutic targets and drugs. Drug Discov. Today 15, 517-530
    • (2010) Drug Discov. Today , vol.15 , pp. 517-530
    • Riccaboni, M.1    Bianchi, I.2    Petrillo, P.3
  • 5
    • 84860851057 scopus 로고    scopus 로고
    • A guide to picking the most selective kinase inhibitor tool compounds for pharmacological validation of drug targets
    • Uitdehaag, J. C., Verkaar, F., Alwan, H., de Man, J., Buijsman, R. C. and Zaman, G. J. (2012) A guide to picking the most selective kinase inhibitor tool compounds for pharmacological validation of drug targets. Br. J. Pharmacol. 166, 858-876
    • (2012) Br. J. Pharmacol. , Issue.166 , pp. 858-876
    • Uitdehaag, J.C.1    Verkaar, F.2    Alwan, H.3    De Man, J.4    Buijsman, R.C.5    Zaman, G.J.6
  • 7
    • 80155142474 scopus 로고    scopus 로고
    • Rapamycin passes the torch: A new generation of mtor inhibitors
    • Benjamin, D., Colombi, M., Moroni, C. and Hall, M. N. (2011) Rapamycin passes the torch: a new generation of mTOR inhibitors. Nat. Rev. Drug Discov. 10, 868-880
    • (2011) Nat. Rev. Drug Discov. , vol.10 , pp. 868-880
    • Benjamin, D.1    Colombi, M.2    Moroni, C.3    Hall, M.N.4
  • 8
    • 80053305462 scopus 로고    scopus 로고
    • Identifying compound-target associations by combining bioactivity profile similarity search and public databases mining
    • Cheng, T., Li, Q., Wang, Y. and Bryant, S. H. (2011) Identifying compound-target associations by combining bioactivity profile similarity search and public databases mining. J. Chem. Inf. Model. 51, 2440-2448
    • (2011) J. Chem. Inf. Model. , vol.51 , pp. 2440-2448
    • Cheng, T.1    Li, Q.2    Wang, Y.3    Bryant, S.H.4
  • 10
  • 11
    • 33746716196 scopus 로고    scopus 로고
    • Aromatic interactions with phenylalanine 691 and cysteine 828: A concept for fms-like tyrosine kinase-3 inhibition. Application to the discovery of a new class of potential antileukemia agents
    • Furet, P., Bold, G., Meyer, T., Roesel, J. and Guagnano, V. (2006) Aromatic interactions with phenylalanine 691 and cysteine 828: a concept for FMS-like tyrosine kinase-3 inhibition. Application to the discovery of a new class of potential antileukemia agents. J. Med. Chem. 49, 4451-4454
    • (2006) J. Med. Chem. , vol.49 , pp. 4451-4454
    • Furet, P.1    Bold, G.2    Meyer, T.3    Roesel, J.4    Guagnano, V.5
  • 12
    • 0032802397 scopus 로고    scopus 로고
    • Structure-activity relationship homology (sarah): A conceptual framework for drug discovery in the genomic era
    • Frye, S. V. (1999) Structure-activity relationship homology (SARAH): a conceptual framework for drug discovery in the genomic era. Chem. Biol. 6, R3-R7
    • (1999) Chem. Biol. , vol.6
    • Frye, S.V.1
  • 13
    • 84861943484 scopus 로고    scopus 로고
    • Chemical genetic discovery of targets and anti-targets for cancer polypharmacology
    • Dar, A. C., Das, T. K., Shokat, K. M. and Cagan, R. L. (2012) Chemical genetic discovery of targets and anti-targets for cancer polypharmacology. Nature 486, 80-84
    • (2012) Nature , vol.486 , pp. 80-84
    • Dar, A.C.1    Das, T.K.2    Shokat, K.M.3    Cagan, R.L.4
  • 14
    • 75149130051 scopus 로고    scopus 로고
    • Targeting the cancer kinome through polypharmacology
    • Knight, Z. A., Lin, H. and Shokat, K. M. (2010) Targeting the cancer kinome through polypharmacology. Nat. Rev. Cancer 10, 130-137
    • (2010) Nat Rev Cancer , vol.10 , pp. 130-137
    • Knight, Z.A.1    Lin, H.2    Shokat, K.M.3
  • 15
    • 77249142404 scopus 로고    scopus 로고
    • The art of the chemical probe
    • Frye, S. V. (2010) The art of the chemical probe. Nat. Chem. Biol. 6, 159-161
    • (2010) Nat. Chem. Biol. , vol.6 , pp. 159-161
    • Frye, S.V.1
  • 16
    • 72449192809 scopus 로고    scopus 로고
    • Guidelines for the effective use of chemical inhibitors of protein function to understand their roles in cell regulation
    • Cohen, P. (2010) Guidelines for the effective use of chemical inhibitors of protein function to understand their roles in cell regulation. Biochem. J. 425, 53-54
    • (2010) Biochem. J. , Issue.425 , pp. 53-54
    • Cohen, P.1
  • 19
    • 80755125565 scopus 로고    scopus 로고
    • Comprehensive assay of kinase catalytic activity reveals features of kinase inhibitor selectivity
    • Anastassiadis, T., Deacon, S. W., Devarajan, K., Ma, H. and Peterson, J. R. (2011) Comprehensive assay of kinase catalytic activity reveals features of kinase inhibitor selectivity. Nat. Biotechnol. 29, 1039-1045
    • (2011) Nat. Biotechnol. , vol.29 , pp. 1039-1045
    • Anastassiadis, T.1    Deacon, S.W.2    Devarajan, K.3    Ma, H.4    Peterson, J.R.5
  • 22
  • 24
    • 0037392942 scopus 로고    scopus 로고
    • The specificities of protein kinase inhibitors: An update
    • Bain, J., McLauchlan, H., Elliott, M. and Cohen, P. (2003) The specificities of protein kinase inhibitors: an update. Biochem. J. 371, 199-204
    • (2003) Biochem. J. , vol.371 , pp. 199-204
    • Bain, J.1    McLauchlan, H.2    Elliott, M.3    Cohen, P.4
  • 26
    • 0034306450 scopus 로고    scopus 로고
    • Specificity and mechanism of action of some commonly used protein kinase inhibitors
    • Davies, S. P., Reddy, H., Caivano, M. and Cohen, P. (2000) Specificity and mechanism of action of some commonly used protein kinase inhibitors. Biochem. J. 351, 95-105
    • (2000) Biochem. J. , vol.351 , pp. 95-105
    • Davies, S.P.1    Reddy, H.2    Caivano, M.3    Cohen, P.4
  • 27
    • 79959476700 scopus 로고    scopus 로고
    • The evolution of protein kinase inhibitors from antagonists to agonists of cellular signaling
    • Dar, A. C. and Shokat, K. M. (2011) The evolution of protein kinase inhibitors from antagonists to agonists of cellular signaling. Annu. Rev. Biochem. 80, 769-795
    • (2011) Annu. Rev. Biochem. , vol.80 , pp. 769-795
    • Dar, A.C.1    Shokat, K.M.2
  • 28
    • 24944497371 scopus 로고    scopus 로고
    • Features of selective kinase inhibitors
    • Knight, Z. A. and Shokat, K. M. (2005) Features of selective kinase inhibitors. Chem. Biol. 12, 621-637
    • (2005) Chem. Biol. , vol.12 , pp. 621-637
    • Knight, Z.A.1    Shokat, K.M.2
  • 30
    • 79952768718 scopus 로고    scopus 로고
    • β2 integrin induces TCRζ -Syk-phospholipase C-γ phosphorylation and paxillin-dependent granule polarization in human NK cells
    • March, M. E. and Long, E. O. (2011) β2 integrin induces TCRζ -Syk-phospholipase C-γ phosphorylation and paxillin-dependent granule polarization in human NK cells. J. Immunol. 186, 2998-3005
    • (2011) J. Immunol. , vol.186 , pp. 2998-3005
    • March, M.E.1    Long, E.O.2
  • 32
    • 0031755916 scopus 로고    scopus 로고
    • Inhibition of human glioblastoma cell adhesion and invasion by 4-(4-hydroxylphenyl)-amino-6,7-dimethoxyquinazoline (whi-p131) and 4-(3-bromo-4-hydroxylphenyl)-amino-6,7-dimethoxyquinazoline (whi-p154)
    • Narla, R. K., Liu, X. P., Klis, D. and Uckun, F. M. (1998) Inhibition of human glioblastoma cell adhesion and invasion by 4-(4-hydroxylphenyl)-amino-6,7- dimethoxyquinazoline (WHI-P131) and 4-(3-bromo-4-hydroxylphenyl)-amino-6,7- dimethoxyquinazoline (WHI-P154). Clin. Cancer Res. 4, 2463-2471
    • (1998) Clin. Cancer Res. , Issue.4 , pp. 2463-2471
    • Narla, R.K.1    Liu, X.P.2    Klis, D.3    Uckun, F.M.4
  • 33
    • 0028884033 scopus 로고
    • Pd 098059 is a specific inhibitor of the activation of mitogen-activated protein kinase kinase in vitro and in vivo
    • Alessi, D. R., Cuenda, A., Cohen, P., Dudley, D. T. and Saltiel, A. R. (1995) PD 098059 is a specific inhibitor of the activation of mitogen-activated protein kinase kinase in vitro and in vivo. J. Biol. Chem. 270, 27489-27494
    • (1995) J. Biol. Chem. , vol.270 , pp. 27489-27494
    • Alessi, D.R.1    Cuenda, A.2    Cohen, P.3    Dudley, D.T.4    Saltiel, A.R.5
  • 34
    • 84859442323 scopus 로고    scopus 로고
    • Discovery and development of spleen tyrosine kinase (syk) inhibitors
    • Singh, R., Masuda, E. S. and Payan, D. G. (2012) Discovery and development of spleen tyrosine kinase (SYK) inhibitors. J. Med. Chem. 55, 3614-3643
    • (2012) J. Med. Chem. , vol.55 , pp. 3614-3643
    • Singh, R.1    Masuda, E.S.2    Payan, D.G.3
  • 37
  • 38
    • 79955506828 scopus 로고    scopus 로고
    • Casein kinase 1 δ functions at the centrosome to mediate wnt-3a-dependent neurite outgrowth
    • Greer, Y. E. and Rubin, J. S. (2011) Casein kinase 1 δ functions at the centrosome to mediate Wnt-3a-dependent neurite outgrowth. J. Cell Biol. 192, 993-1004
    • (2011) J. Cell Biol. , Issue.192 , pp. 993-1004
    • Greer, Y.E.1    Rubin, J.S.2
  • 39
    • 84860851412 scopus 로고    scopus 로고
    • Sequential application of anticancer drugs enhances cell death by rewiring apoptotic signaling networks
    • Lee, M. J., Ye, A. S., Gardino, A. K., Heijink, A. M., Sorger, P. K., MacBeath, G. and Yaffe, M. B. (2012) Sequential application of anticancer drugs enhances cell death by rewiring apoptotic signaling networks. Cell 149, 780-794
    • (2012) Cell , vol.149 , pp. 780-794
    • Lee, M.J.1    Ye, A.S.2    Gardino, A.K.3    Heijink, A.M.4    Sorger, P.K.5    MacBeath, G.6    Yaffe, M.B.7
  • 41
    • 80054694121 scopus 로고    scopus 로고
    • Inhibition of c-jun-n-terminal kinase increases cardiac peroxisome proliferator-activated receptor α expression and fatty acid oxidation and prevents lipopolysaccharide-induced heart dysfunction
    • Drosatos, K., Drosatos-Tampakaki, Z., Khan, R., Homma, S., Schulze, P. C., Zannis, V. I. and Goldberg, I. J. (2011) Inhibition of c-Jun-N-terminal kinase increases cardiac peroxisome proliferator-activated receptor α expression and fatty acid oxidation and prevents lipopolysaccharide-induced heart dysfunction. J. Biol. Chem. 286, 36331-36339
    • (2011) J. Biol. Chem. , Issue.286 , pp. 36331-36339
    • Drosatos, K.1    Drosatos-Tampakaki, Z.2    Khan, R.3    Homma, S.4    Schulze, P.C.5    Zannis, V.6    Goldberg, I.7
  • 42
    • 38649085620 scopus 로고    scopus 로고
    • The c-jun n-terminal kinase pathway is critical for cell transformation by the latent membrane protein 1 of epstein-barr virus
    • Kutz, H., Reisbach, G., Schultheiss, U. and Kieser, A. (2008) The c-Jun N-terminal kinase pathway is critical for cell transformation by the latent membrane protein 1 of Epstein-Barr virus. Virology 371, 246-256
    • (2008) Virology , vol.371 , pp. 246-256
    • Kutz, H.1    Reisbach, G.2    Schultheiss, U.3    Kieser, A.4
  • 44
    • 0034715885 scopus 로고    scopus 로고
    • Regulation and functions of rho-associated kinase
    • Amano, M., Fukata, Y. and Kaibuchi, K. (2000) Regulation and functions of Rho-associated kinase. Exp. Cell Res. 261, 44-51
    • (2000) Exp. Cell Res. , vol.261 , pp. 44-51
    • Amano, M.1    Fukata, Y.2    Kaibuchi, K.3
  • 46
    • 60349103901 scopus 로고    scopus 로고
    • Mitogen-activated protein kinase phosphatase-1 modulated jnk activation is critical for apoptosis induced by inhibitor of epidermal growth factor receptor-tyrosine kinase
    • Takeuchi, K., Shin-ya, T., Nishio, K. and Ito, F. (2009) Mitogen-activated protein kinase phosphatase-1 modulated JNK activation is critical for apoptosis induced by inhibitor of epidermal growth factor receptor-tyrosine kinase. FEBS J. 276, 1255-1265
    • (2009) FEBS J. , vol.276 , pp. 1255-1265
    • Takeuchi, K.1    Shin-ya, T.2    Nishio, K.3    Ito, F.4
  • 47
    • 69949120824 scopus 로고    scopus 로고
    • Critical role of nuclear calcium/calmodulin-dependent protein kinase iiδb in cardiomyocyte survival in cardiomyopathy
    • Little, G. H., Saw, A., Bai, Y., Dow, J., Marjoram, P., Simkhovich, B., Leeka, J., Kedes, L., Kloner, R. A. and Poizat, C. (2009) Critical role of nuclear calcium/calmodulin-dependent protein kinase IIδB in cardiomyocyte survival in cardiomyopathy. J. Biol. Chem. 284, 24857-24868
    • (2009) J. Biol. Chem. , vol.284 , pp. 24857-24868
    • Little, G.H.1    Saw, A.2    Bai, Y.3    Dow, J.4    Marjoram, P.5    Simkhovich, B.6    Leeka, J.7    Kedes, L.8    Kloner, R.A.9    Poizat, C.10
  • 53
    • 84857831583 scopus 로고    scopus 로고
    • Dyrk2 priming phosphorylation of c-jun and c-myc modulates cell cycle progression in human cancer cells
    • Taira, N., Mimoto, R., Kurata, M., Yamaguchi, T., Kitagawa, M., Miki, Y. and Yoshida, K. (2012) DYRK2 priming phosphorylation of c-Jun and c-Myc modulates cell cycle progression in human cancer cells. J. Clin. Invest. 122, 859-872
    • (2012) J. Clin. Invest. , Issue.122 , pp. 859-872
    • Taira, N.1    Mimoto, R.2    Kurata, M.3    Yamaguchi, T.4    Kitagawa, M.5    Miki, Y.6    Yoshida, K.7
  • 55
    • 0030768744 scopus 로고    scopus 로고
    • Csf-1 signal transduction
    • Hamilton, J. A. (1997) CSF-1 signal transduction. J. Leukoc. Biol. 62, 145-155
    • (1997) J. Leukoc. Biol. , vol.62 , pp. 145-155
    • Hamilton, J.A.1
  • 57
    • 0034928792 scopus 로고    scopus 로고
    • Negative regulation of protein translation by mitogen-activated protein kinase-interacting kinases 1 and 2
    • Knauf, U., Tschopp, C. and Gram, H. (2001) Negative regulation of protein translation by mitogen-activated protein kinase-interacting kinases 1 and 2. Mol. Cell. Biol. 21, 5500-5511
    • (2001) Mol. Cell. Biol. , vol.21 , pp. 5500-5511
    • Knauf, U.1    Tschopp, C.2    Gram, H.3
  • 58
    • 0347593987 scopus 로고    scopus 로고
    • Mimicry of pre-b cell receptor signaling by activation of the tyrosine kinase blk
    • Tretter, T., Ross, A. E., Dordai, D. I. and Desiderio, S. (2003) Mimicry of pre-B cell receptor signaling by activation of the tyrosine kinase Blk. J. Exp. Med. 198, 1863-1873
    • (2003) J. Exp. Med. , vol.198 , pp. 1863-1873
    • Tretter, T.1    Ross, A.E.2    Dordai, D.I.3    Desiderio, S.4
  • 60
    • 84865164084 scopus 로고    scopus 로고
    • Pas kinase: Integrating nutrient sensing with nutrient partitioning
    • Cardon, C. M. and Rutter, J. (2012) PAS kinase: integrating nutrient sensing with nutrient partitioning. Semin. Cell. Dev. Biol. 23, 626-630
    • (2012) Semin. Cell. Dev. Biol. , Issue.23 , pp. 626-630
    • Cardon, C.M.1    Rutter, J.2
  • 61
    • 84856582258 scopus 로고    scopus 로고
    • Pas kinase promotes cell survival and growth through activation of rho1
    • Cardon, C. M., Beck, T., Hall, M. N. and Rutter, J. (2012) PAS kinase promotes cell survival and growth through activation of Rho1. Sci. Signaling 5, ra9
    • (2012) Sci. Signaling , vol.5
    • Cardon, C.M.1    Beck, T.2    Hall, M.N.3    Rutter, J.4
  • 62
    • 79955611332 scopus 로고    scopus 로고
    • Substrate preference and phosphatidylinositol monophosphate inhibition of the catalytic domain of the per-arnt-sim domain kinase paskin
    • Schlafli, P., Troger, J., Eckhardt, K., Borter, E., Spielmann, P. and Wenger, R. H. (2011) Substrate preference and phosphatidylinositol monophosphate inhibition of the catalytic domain of the Per-Arnt-Sim domain kinase PASKIN. FEBS J. 278, 1757-1768
    • (2011) FEBS J. , vol.278 , pp. 1757-1768
    • Schlafli, P.1    Troger, J.2    Eckhardt, K.3    Borter, E.4    Spielmann, P.5    Wenger, R.H.6
  • 63
    • 78049231804 scopus 로고    scopus 로고
    • A small-molecule scaffold induces autophagy in primary neurons and protects against toxicity in a huntington disease model
    • Tsvetkov, A. S., Miller, J., Arrasate, M., Wong, J. S., Pleiss, M. A. and Finkbeiner, S. (2010) A small-molecule scaffold induces autophagy in primary neurons and protects against toxicity in a Huntington disease model. Proc. Natl. Acad. Sci. U.S.A. 107, 16982-16987
    • (2010) Proc. Natl. Acad. Sci. U.S.A. , vol.107 , pp. 16982-16987
    • Tsvetkov, A.S.1    Miller, J.2    Arrasate, M.3    Wong, J.S.4    Pleiss, M.A.5    Finkbeiner, S.6


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.