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Volumn 3, Issue 5, 2004, Pages 490-500

Proteome-wide identification of cellular targets affected by bisindolylmaleimide-type protein kinase C inhibitors

Author keywords

[No Author keywords available]

Indexed keywords

2 [1 (3 AMINOPROPYL) 1H INDOL 3 YL] 3 (1H INDOL 3 YL)MALEIMIDE; 2 [1 (3 AMINOPROPYL) 6,7,8,9 TETRAHYDROPYRIDOL[1,2 A]INDOL 3 YL] 3 (1 METHYLINDOL 3 YL)MALEIMIDE; 2 [1 (3 AMINOPROPYL)INDOL 3 YL] 3 (1 METHYLINDOL 3 YL)MALEIMIDE; 2 [1 (3 DIMETHYLAMINOPROPYL) 3 INDOLYL] 3 (3 INDOLYL)MALEIMIDE; ADENOSINE KINASE; BISINDOLYLMALEIMIDE; CYCLIN DEPENDENT KINASE 2; LIGAND; MALEIMIDE DERIVATIVE; OXIDOREDUCTASE; PROTEIN KINASE; PROTEIN KINASE C ALPHA; PROTEIN KINASE C INHIBITOR; PROTEOME; REDUCED NICOTINAMIDE ADENINE DINUCLEOTIDE (PHOSPHATE) DEHYDROGENASE (QUINONE); RIBOSOME PROTEIN; S6 KINASE; STAUROSPORINE; UNCLASSIFIED DRUG;

EID: 2442455834     PISSN: 15359476     EISSN: None     Source Type: Journal    
DOI: 10.1074/mcp.M300139-MCP200     Document Type: Article
Times cited : (102)

References (34)
  • 1
    • 0035413601 scopus 로고    scopus 로고
    • Protein kinase C: Structural and spatial regulation by phosphorylation, cofactors, and macromolecular interactions
    • Newton, A. C. (2001) Protein kinase C: Structural and spatial regulation by phosphorylation, cofactors, and macromolecular interactions. Chem. Rev. 101, 2353-2364
    • (2001) Chem. Rev. , vol.101 , pp. 2353-2364
    • Newton, A.C.1
  • 3
    • 0032847677 scopus 로고    scopus 로고
    • Protein kinase C in the treatment of disease: Signal transcluction pathways, inhibitors, and agents in development
    • Goekjian, P. G., and Jirousek, M. R. (1999) Protein kinase C in the treatment of disease: signal transcluction pathways, inhibitors, and agents in development. Curr. Med. Chem. 6, 877-903
    • (1999) Curr. Med. Chem. , vol.6 , pp. 877-903
    • Goekjian, P.G.1    Jirousek, M.R.2
  • 4
    • 0034776809 scopus 로고    scopus 로고
    • Protein kinase C isozymes, novel phorbol ester receptors and cancer chemotherapy
    • Barry, O. P., and Kazanietz, M. G. (2001) Protein kinase C isozymes, novel phorbol ester receptors and cancer chemotherapy. Curr. Pharm. Des. 7, 1725-1744
    • (2001) Curr. Pharm. Des. , vol.7 , pp. 1725-1744
    • Barry, O.P.1    Kazanietz, M.G.2
  • 7
    • 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
  • 8
    • 0032966912 scopus 로고    scopus 로고
    • Competitive antagonism of the mouse 5-hydroxytryptamine3 receptor by bisindolylmaleimide I, a "selective" protein kinase C inhibitor
    • Coultrap, S. J., Sun, H., Tanner, T. E., Jr., and Machu, T. K. (1999) Competitive antagonism of the mouse 5-hydroxytryptamine3 receptor by bisindolylmaleimide I, a "selective" protein kinase C inhibitor. J. Pharmacol. Exp. Ther. 290, 76-82
    • (1999) J. Pharmacol. Exp. Ther. , vol.290 , pp. 76-82
    • Coultrap, S.J.1    Sun, H.2    Tanner Jr., T.E.3    Machu, T.K.4
  • 9
    • 0034640214 scopus 로고    scopus 로고
    • Inhibition of voltage-dependent sodium channels by Ro 31-8220, a "specific" protein kinase C inhibitor
    • Lingameneni, R., Vysotskaya, T. N., Duch, D. S., and Hemmings, H. C., Jr. (2000) Inhibition of voltage-dependent sodium channels by Ro 31-8220, a "specific" protein kinase C inhibitor. FEBS Lett. 473, 265-268
    • (2000) FEBS Lett. , vol.473 , pp. 265-268
    • Lingameneni, R.1    Vysotskaya, T.N.2    Duch, D.S.3    Hemmings Jr., H.C.4
  • 13
    • 0842274205 scopus 로고    scopus 로고
    • Rediscovering the sweet spot in drug discovery
    • Brown, D., and Superti-Furga, G. (2003) Rediscovering the sweet spot in drug discovery. Drug Discov. Today 8, 1067-1077
    • (2003) Drug Discov. Today , vol.8 , pp. 1067-1077
    • Brown, D.1    Superti-Furga, G.2
  • 15
    • 0036318795 scopus 로고    scopus 로고
    • Identification of SRPK1 and SRPK2 as the major cellular protein kinases phosphorylating hepatitis B virus core protein
    • Daub, H., Blencke, S., Habenberger, P., Kurtenbach, A., Dennenmoser, J., Wissing, J., Ullrich, A., and Cotten, M. (2002) Identification of SRPK1 and SRPK2 as the major cellular protein kinases phosphorylating hepatitis B virus core protein. J. Virol. 76, 8124-8137
    • (2002) J. Virol. , vol.76 , pp. 8124-8137
    • Daub, H.1    Blencke, S.2    Habenberger, P.3    Kurtenbach, A.4    Dennenmoser, J.5    Wissing, J.6    Ullrich, A.7    Cotten, M.8
  • 18
    • 0037674323 scopus 로고    scopus 로고
    • Mutation of threonine 766 in the epidermal growth factor receptor reveals a hotspot for resistance formation against selective tyrosine kinase inhibitors
    • Blencke, S., Ullrich, A., and Daub, H. (2003) Mutation of threonine 766 in the epidermal growth factor receptor reveals a hotspot for resistance formation against selective tyrosine kinase inhibitors. J. Biol. Chem. 278, 15435-15440
    • (2003) J. Biol. Chem. , vol.278 , pp. 15435-15440
    • Blencke, S.1    Ullrich, A.2    Daub, H.3
  • 19
    • 0031253655 scopus 로고    scopus 로고
    • Protein kinase inhibition by staurosporine revealed in details of the molecular interaction with CDK2
    • Lawrie, A. M., Noble, M. E., Tunnah, P., Brown, N. R., Johnson, L. N., and Endicott, J. A. (1997) Protein kinase inhibition by staurosporine revealed in details of the molecular interaction with CDK2. Nat. Struct. Biol. 4, 796-801
    • (1997) Nat. Struct. Biol. , vol.4 , pp. 796-801
    • Lawrie, A.M.1    Noble, M.E.2    Tunnah, P.3    Brown, N.R.4    Johnson, L.N.5    Endicott, J.A.6
  • 21
    • 0033152210 scopus 로고    scopus 로고
    • Structural analysis of the lymphocyte-specific kinase Lck in complex with non-selective and Src family selective kinase inhibitors
    • Zhu, X., Kim, J. L., Newcomb, J. R., Rose, P. E., Stover, D. R., Toledo, L. M., Zhao, H., and Morgenstern, K. A. (1999) Structural analysis of the lymphocyte-specific kinase Lck in complex with non-selective and Src family selective kinase inhibitors. Structure. Fold. Des. 7, 651-661
    • (1999) Structure Fold. Des. , vol.7 , pp. 651-661
    • Zhu, X.1    Kim, J.L.2    Newcomb, J.R.3    Rose, P.E.4    Stover, D.R.5    Toledo, L.M.6    Zhao, H.7    Morgenstern, K.A.8
  • 22
    • 0141426663 scopus 로고    scopus 로고
    • CB 1954: From the Walker tumor to NQO2 and VDEPT
    • Knox, R. J., Burke, P. J., Chen, S., and Kerr, D. J. (2003) CB 1954: From the Walker tumor to NQO2 and VDEPT. Curr. Pharm. Des. 9. 2091-2104
    • (2003) Curr. Pharm. Des. , vol.9 , pp. 2091-2104
    • Knox, R.J.1    Burke, P.J.2    Chen, S.3    Kerr, D.J.4
  • 23
    • 0037195924 scopus 로고    scopus 로고
    • Disruption of dihydronicotinamide riboside: Quinone oxidoreductase 2 (NQO2) leads to myeloid hyperplasia of bone marrow and decreased sensitivity to menadione toxicity
    • Long, D. J., Iskander, K., Gaikwad, A., Arin, M., Roop, D. R., Knox, R., Barrios, R., and Jaiswal, A. K. (2002) Disruption of dihydronicotinamide riboside:quinone oxidoreductase 2 (NQO2) leads to myeloid hyperplasia of bone marrow and decreased sensitivity to menadione toxicity. J. Biol. Chem. 277, 46131-46139
    • (2002) J. Biol. Chem. , vol.277 , pp. 46131-46139
    • Long, D.J.1    Iskander, K.2    Gaikwad, A.3    Arin, M.4    Roop, D.R.5    Knox, R.6    Barrios, R.7    Jaiswal, A.K.8
  • 24
    • 0031573462 scopus 로고    scopus 로고
    • Catalytic properties of NAD(P)H: Quinone oxidoreductase-2 (NQO2), a dihydronicotinamide riboside dependent oxidoreductase
    • Wu, K., Knox, R., Sun, X. Z., Joseph, P., Jaiswal, A. K., Zhang, D., Deng, P. S., and Chen, S. (1997) Catalytic properties of NAD(P)H:quinone oxidoreductase-2 (NQO2), a dihydronicotinamide riboside dependent oxidoreductase. Arch. Biochem. Biophys. 347, 221-228
    • (1997) Arch. Biochem. Biophys. , vol.347 , pp. 221-228
    • Wu, K.1    Knox, R.2    Sun, X.Z.3    Joseph, P.4    Jaiswal, A.K.5    Zhang, D.6    Deng, P.S.7    Chen, S.8
  • 26
    • 0034721142 scopus 로고    scopus 로고
    • Adenosine kinase inhibitors. 2. Synthesis, enzyme inhibition, and antiseizure activity of diaryltubercidin analogues
    • Ugarkar, B. G., Castellino, A. J., Dare, J. M., Kopcho, J. J., Wiesner, J. B., Schanzer, J. M., and Erion, M. D. (2000) Adenosine kinase inhibitors. 2. Synthesis, enzyme inhibition, and antiseizure activity of diaryltubercidin analogues. J. Med. Chem. 43, 2894-2905
    • (2000) J. Med. Chem. , vol.43 , pp. 2894-2905
    • Ugarkar, B.G.1    Castellino, A.J.2    Dare, J.M.3    Kopcho, J.J.4    Wiesner, J.B.5    Schanzer, J.M.6    Erion, M.D.7
  • 27
    • 0034721186 scopus 로고    scopus 로고
    • Adenosine kinase inhibitors. 1. Synthesis, enzyme inhibition, and antiseizure activity of 5-iodotubercidin analogues
    • Ugarkar, B. G., DaRe, J. M., Kopcho, J. J., Browne, C. E., III, Schanzer, J. M., Wiesner, J. B., and Erion, M. D. (2000) Adenosine kinase inhibitors. 1. Synthesis, enzyme inhibition, and antiseizure activity of 5-iodotubercidin analogues. J. Med. Chem. 43, 2883-2893
    • (2000) J. Med. Chem. , vol.43 , pp. 2883-2893
    • Ugarkar, B.G.1    DaRe, J.M.2    Kopcho, J.J.3    Browne III, C.E.4    Schanzer, J.M.5    Wiesner, J.B.6    Erion, M.D.7
  • 28
    • 0033539894 scopus 로고    scopus 로고
    • Induction of apoptosis by SLK, a Ste20-related kinase
    • Sabourin, L. A., and Rudnicki, M. A. (1999) Induction of apoptosis by SLK, a Ste20-related kinase. Oncogene 18, 7566-7575
    • (1999) Oncogene , vol.18 , pp. 7566-7575
    • Sabourin, L.A.1    Rudnicki, M.A.2
  • 29
    • 0033961249 scopus 로고    scopus 로고
    • Caspase 3 cleavage of the Ste20-related kinase SLK releases and activates an apoptosis-inducing kinase domain and an actin-disassembling region
    • Sabourin, L. A., Tamai, K., Seale, P., Wagner, J., and Rudnicki, M. A. (2000) Caspase 3 cleavage of the Ste20-related kinase SLK releases and activates an apoptosis-inducing kinase domain and an actin-disassembling region. Mol. Cell. Biol. 20, 684-696
    • (2000) Mol. Cell. Biol. , vol.20 , pp. 684-696
    • Sabourin, L.A.1    Tamai, K.2    Seale, P.3    Wagner, J.4    Rudnicki, M.A.5
  • 30
    • 0038112035 scopus 로고    scopus 로고
    • Phosphorylation of p90 ribosomal S6 kinase (RSK) regulates extracellular signal-regulated kinase docking and RSK activity
    • Roux, P. P., Richards, S. A., and Blenis, J. (2003) Phosphorylation of p90 ribosomal S6 kinase (RSK) regulates extracellular signal-regulated kinase docking and RSK activity. Mol. Cell. Biol. 23, 4796-4804
    • (2003) Mol. Cell. Biol. , vol.23 , pp. 4796-4804
    • Roux, P.P.1    Richards, S.A.2    Blenis, J.3
  • 31
    • 0037392444 scopus 로고    scopus 로고
    • Issues and progress with protein kinase inhibitors for cancer treatment
    • Dancey, J., and Sausville, E. A. (2003) Issues and progress with protein kinase inhibitors for cancer treatment. Nat. Rev. Drug Discov. 2, 296-313
    • (2003) Nat. Rev. Drug Discov. , vol.2 , pp. 296-313
    • Dancey, J.1    Sausville, E.A.2
  • 34
    • 0038561131 scopus 로고    scopus 로고
    • A method for the comprehensive proteomic analysis of membrane proteins
    • Wu, C. C., MacCoss, M. J., Howell, K. E., and Yates, J. R., III (2003) A method for the comprehensive proteomic analysis of membrane proteins. Nat. Biotechnol. 21, 532-538
    • (2003) Nat. Biotechnol. , vol.21 , pp. 532-538
    • Wu, C.C.1    MacCoss, M.J.2    Howell, K.E.3    Yates III, J.R.4


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