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Volumn 5, Issue , 2015, Pages

Multiplex imaging and cellular target identification of kinase inhibitors via an affinity-based proteome profiling approach

Author keywords

[No Author keywords available]

Indexed keywords

MOLECULAR PROBE; PROTEIN KINASE INHIBITOR; PROTEOME;

EID: 84923106733     PISSN: None     EISSN: 20452322     Source Type: Journal    
DOI: 10.1038/srep07724     Document Type: Article
Times cited : (34)

References (56)
  • 1
    • 70549105789 scopus 로고    scopus 로고
    • Making the Auroras glow: Regulation of Aurora A and B kinase function by interacting proteins
    • Carmena, M., Ruchaud, S. & Earnshaw, W. C. Making the Auroras glow: regulation of Aurora A and B kinase function by interacting proteins. Curr. Opin. Cell Biol. 21, 796-805 (2009).
    • (2009) Curr. Opin. Cell Biol. , vol.21 , pp. 796-805
    • Carmena, M.1    Ruchaud, S.2    Earnshaw, W.C.3
  • 2
    • 10344236486 scopus 로고    scopus 로고
    • Aurora-kinase inhibitors as anticancer agents
    • Keen, N. & Taylor, S. Aurora-kinase inhibitors as anticancer agents. Nat. Rev. Cancer 4, 927-936 (2004).
    • (2004) Nat. Rev. Cancer , vol.4 , pp. 927-936
    • Keen, N.1    Taylor, S.2
  • 3
    • 34948901399 scopus 로고    scopus 로고
    • Aurora-A: The maker and breaker of spindle poles
    • Barr, A. R. & Gergely, F. Aurora-A: the maker and breaker of spindle poles. J. Cell Sci. 120, 2987-2996 (2007).
    • (2007) J. Cell Sci. , vol.120 , pp. 2987-2996
    • Barr, A.R.1    Gergely, F.2
  • 5
    • 2342639645 scopus 로고    scopus 로고
    • VX-680, a potent and selective small-molecule inhibitor of the Aurora kinases, suppresses tumor growth in vivo
    • Harrington, E. A. et al. VX-680, a potent and selective small-molecule inhibitor of the Aurora kinases, suppresses tumor growth in vivo. Nat. Med. 10, 262-267 (2004).
    • (2004) Nat. Med. , vol.10 , pp. 262-267
    • Harrington, E.A.1
  • 6
    • 23344440655 scopus 로고    scopus 로고
    • Inhibition of drug-resistant mutants of ABL, KIT, and EGF receptor kinases
    • Carter, T. A. et al. Inhibition of drug-resistant mutants of ABL, KIT, and EGF receptor kinases. Proc. Natl. Acad. Sci. 102, 11011-11016 (2005).
    • (2005) Proc. Natl. Acad. Sci. , vol.102 , pp. 11011-11016
    • Carter, T.A.1
  • 7
    • 34247259822 scopus 로고    scopus 로고
    • Antitumor activity of MLN8054, an orally active smallmolecule inhibitor of Aurora A kinase
    • Manfredi, M. G. et al. Antitumor activity of MLN8054, an orally active smallmolecule inhibitor of Aurora A kinase. Proc. Natl. Acad. Sci. 104, 4106-4111 (2007).
    • (2007) Proc. Natl. Acad. Sci. , vol.104 , pp. 4106-4111
    • Manfredi, M.G.1
  • 9
    • 84055217855 scopus 로고    scopus 로고
    • Characterization of Alisertib (MLN8237), an investigational small-molecule inhibitor of Aurora A kinase using novel in vivo pharmacodynamic assays
    • Manfredi, M. G. et al. Characterization of Alisertib (MLN8237), an investigational small-molecule inhibitor of Aurora A kinase using novel in vivo pharmacodynamic assays. Clin. Cancer Res. 17, 7614-7624 (2011).
    • (2011) Clin. Cancer Res. , vol.17 , pp. 7614-7624
    • Manfredi, M.G.1
  • 10
    • 0036635291 scopus 로고    scopus 로고
    • Glivec (ST1571 Imatinib) a rationally developed, targeted anticancer drug
    • Capdeville, R., Buchdunger, E., Zimmermann, J. & Matter, A. Glivec (ST1571, Imatinib), a rationally developed, targeted anticancer drug. Nat. Rev. Drug Disc. 1, 493-502 (2002).
    • (2002) Nat. Rev. Drug Disc. , vol.1 , pp. 493-502
    • Capdeville, R.1    Buchdunger, E.2    Zimmermann, J.3    Matter, A.4
  • 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. 5, 616-624 (2009).
    • (2009) Nat. Chem. Biol. , vol.5 , pp. 616-624
    • Rix, U.1    Superti-Furga, G.2
  • 12
    • 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. & Peterson, J. R. Comprehensive assay of kinase catalytic activity reveals features of kinase inhibitor selectivity. Nat. Biotechnol. 29, 1039-1045 (2011).
    • (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
  • 13
    • 80755125575 scopus 로고    scopus 로고
    • Comprehensive analysis of kinase inhibitor selectivity
    • Davis, M. I. et al. Comprehensive analysis of kinase inhibitor selectivity. Nat. Biotechnol. 29, 1046-1051 (2011).
    • (2011) Nat. Biotechnol. , vol.29 , pp. 1046-1051
    • Davis, M.I.1
  • 14
    • 84874630073 scopus 로고    scopus 로고
    • Target identification for small bioactive molecules: Finding the needle in the haystack
    • Ziegler, S., Pries, V., Hedberg, C. &Waldmann, H. Target identification for small bioactive molecules: finding the needle in the haystack. Angew. Chem. Int. Ed. 52, 2744-2792 (2013).
    • (2013) Angew. Chem. Int. Ed. , vol.52 , pp. 2744-2792
    • Ziegler, S.1    Pries, V.2    Hedberg, C.3    Waldmann, H.4
  • 15
    • 84887186695 scopus 로고    scopus 로고
    • Target identification of biologically active small molecules via in situ methods
    • Su, Y. et al. Target identification of biologically active small molecules via in situ methods. Curr. Opin. Chem.l Biol. 17, 768-775 (2013).
    • (2013) Curr. Opin. Chem.l Biol. , vol.17 , pp. 768-775
    • Su, Y.1
  • 16
    • 84872545409 scopus 로고    scopus 로고
    • Label transfer reagents to probe p38 MAPK binding partners
    • Andrews, S. S., Hill, Z. B., Perera, B. G. K. & Maly, D. J. Label transfer reagents to probe p38 MAPK binding partners. ChemBiochem 14, 209-216 (2013).
    • (2013) ChemBiochem , vol.14 , pp. 209-216
    • Andrews, S.S.1    Hill, Z.B.2    Perera, B.G.K.3    Maly, D.J.4
  • 17
    • 74949101629 scopus 로고    scopus 로고
    • Activity-based proteome profiling of potential cellular targets of Orlistat-an FDA-approved drug with anti-tumor activities
    • Yang, P.-Y. et al. Activity-based proteome profiling of potential cellular targets of Orlistat-an FDA-approved drug with anti-tumor activities. J. Am. Chem. Soc. 132, 656-666 (2010).
    • (2010) J. Am. Chem. Soc. , vol.132 , pp. 656-666
    • Yang, P.-Y.1
  • 18
    • 80053477145 scopus 로고    scopus 로고
    • Chemical modification and organelle-specific localization of Orlistat-like natural-product-based probes
    • Yang, P.-Y. et al. Chemical modification and organelle-specific localization of Orlistat-like natural-product-based probes. Chem.-Asian. J. 6, 2762-2775 (2011).
    • (2011) Chem.-Asian. J. , vol.6 , pp. 2762-2775
    • Yang, P.-Y.1
  • 19
    • 84876461949 scopus 로고    scopus 로고
    • Modulation of fatty acid synthase enzyme activity and expression during Hepatitis C virus replication
    • Nasheri, N. et al.Modulation of fatty acid synthase enzyme activity and expression during Hepatitis C virus replication. Chem. Biol. 20, 570-582 (2013).
    • (2013) Chem. Biol. , vol.20 , pp. 570-582
    • Nasheri, N.1
  • 20
    • 80053898528 scopus 로고    scopus 로고
    • Identification of acyl protein thioesterases 1 and 2 as the cellular targets of the Ras-signaling modulators Palmostatin B and M
    • Rusch, M. et al. Identification of acyl protein thioesterases 1 and 2 as the cellular targets of the Ras-signaling modulators Palmostatin B and M. Angew. Chem. Int. Ed. 50, 9838-9842 (2011).
    • (2011) Angew. Chem. Int. Ed. , vol.50 , pp. 9838-9842
    • Rusch, M.1
  • 21
    • 84864241593 scopus 로고    scopus 로고
    • Antibiotic activity and target discovery of three-membered natural product-derived heterocycles in pathogenic bacteria
    • Pitscheider, M., Maeusbacher, N. & Sieber, S. A. Antibiotic activity and target discovery of three-membered natural product-derived heterocycles in pathogenic bacteria. Chem. Sci. 3, 2035-2041 (2012).
    • (2012) Chem. Sci. , vol.3 , pp. 2035-2041
    • Pitscheider, M.1    Maeusbacher, N.2    Sieber, S.A.3
  • 22
    • 84906307152 scopus 로고    scopus 로고
    • A road map to evaluate the proteome-wide selectivity of covalent kinase inhibitors
    • Lanning, B. R. et al. A road map to evaluate the proteome-wide selectivity of covalent kinase inhibitors. Nat. Chem. Biol. 10, 760-767 (2014).
    • (2014) Nat. Chem. Biol. , vol.10 , pp. 760-767
    • Lanning, B.R.1
  • 23
    • 84869453987 scopus 로고    scopus 로고
    • Affinity-based probes based on type II kinase inhibitors
    • Ranjitkar, P. et al. Affinity-based probes based on type II kinase inhibitors. J. Am. Chem. Soc. 134, 19017-19025 (2012).
    • (2012) J. Am. Chem. Soc. , vol.134 , pp. 19017-19025
    • Ranjitkar, P.1
  • 24
    • 84871335698 scopus 로고    scopus 로고
    • Active site profiling reveals coupling between domains in SRC-family kinases
    • Krishnamurty, R. et al. Active site profiling reveals coupling between domains in SRC-family kinases. Nat. Chem. Biol. 9, 43-50 (2013).
    • (2013) Nat. Chem. Biol. , vol.9 , pp. 43-50
    • Krishnamurty, R.1
  • 25
    • 84863116427 scopus 로고    scopus 로고
    • Cell-based proteome profiling of potential Dasatinib targets by use of affinity-based probes
    • Shi, H., Zhang, C.-J., Chen, G. Y. J. & Yao, S. Q. Cell-based proteome profiling of potential Dasatinib targets by use of affinity-based probes. J. Am. Chem. Soc. 134, 3001-3014 (2012).
    • (2012) J. Am. Chem. Soc. , vol.134 , pp. 3001-3014
    • Shi, H.1    Zhang, C.-J.2    Chen, G.Y.J.3    Yao, S.Q.4
  • 26
    • 80053498767 scopus 로고    scopus 로고
    • Proteome profiling reveals potential cellular targets of staurosporine using a clickable cell-permeable probe
    • Shi, H., Cheng, X., Sze, S. K. & Yao, S. Q. Proteome profiling reveals potential cellular targets of staurosporine using a clickable cell-permeable probe. Chem. Commun. 47, 11306-11308 (2011).
    • (2011) Chem. Commun. , vol.47 , pp. 11306-11308
    • Shi, H.1    Cheng, X.2    Sze, S.K.3    Yao, S.Q.4
  • 27
    • 84882441298 scopus 로고    scopus 로고
    • Design and synthesis of minimalist terminal alkyne-containing diazirine photo-crosslinkers and their incorporation into kinase inhibitors for cell-and tissue-based proteome profiling
    • Li, Z. et al. Design and synthesis of minimalist terminal alkyne-containing diazirine photo-crosslinkers and their incorporation into kinase inhibitors for cell-and tissue-based proteome profiling. Angew. Chem. Int. Ed. 52, 8551-8556 (2013).
    • (2013) Angew. Chem. Int. Ed. , vol.52 , pp. 8551-8556
    • Li, Z.1
  • 28
    • 84904433737 scopus 로고    scopus 로고
    • Minimalist cyclopropene-containing photo-cross-linkers suitable for live-cell imaging and affinity-based protein labeling
    • Li, Z. et al. "Minimalist" cyclopropene-containing photo-cross-linkers suitable for live-cell imaging and affinity-based protein labeling. J. Am. Chem. Soc. 136, 9990-9998 (2014).
    • (2014) J. Am. Chem. Soc. , vol.136 , pp. 9990-9998
    • Li, Z.1
  • 29
    • 45749158648 scopus 로고    scopus 로고
    • Identification of the cellular targets of bioactive small organic molecules using affinity reagents
    • Leslie, B. J. & Hergenrother, P. J. Identification of the cellular targets of bioactive small organic molecules using affinity reagents. Chem. Soc. Rev. 37, 1347-1360 (2008).
    • (2008) Chem. Soc. Rev. , vol.37 , pp. 1347-1360
    • Leslie, B.J.1    Hergenrother, P.J.2
  • 30
    • 80051772487 scopus 로고    scopus 로고
    • Aliphatic diazirines as photoaffinity probes for proteins: Recent developments
    • Das, J. Aliphatic diazirines as photoaffinity probes for proteins: recent developments. Chem. Rev. 111, 4405-4417 (2011).
    • (2011) Chem. Rev. , vol.111 , pp. 4405-4417
    • Das, J.1
  • 33
    • 77953850924 scopus 로고    scopus 로고
    • Drug-resistant Aurora A mutants for cellular target validation of the small molecule kinase inhibitors MLN8054 and MLN8237
    • Sloane, D. A. et al. Drug-resistant Aurora A mutants for cellular target validation of the small molecule kinase inhibitors MLN8054 and MLN8237. ACS Chem. Biol. 5, 563-576 (2010).
    • (2010) ACS Chem. Biol. , vol.5 , pp. 563-576
    • Sloane, D.A.1
  • 34
    • 70349917806 scopus 로고    scopus 로고
    • Bioorthogonal chemistry: Fishing for selectivity in a sea of functionality
    • Sletten, E. M. & Bertozzi, C. R. Bioorthogonal chemistry: fishing for selectivity in a sea of functionality. Angew. Chem. Int. Ed. 48, 6974-6998 (2009).
    • (2009) Angew. Chem. Int. Ed. , vol.48 , pp. 6974-6998
    • Sletten, E.M.1    Bertozzi, C.R.2
  • 35
    • 77950330131 scopus 로고    scopus 로고
    • The use of click chemistry in the emerging field of catalomics
    • Kalesh, K. A., Shi,H., Ge, J. &Yao, S. Q. The use of click chemistry in the emerging field of catalomics. Org. Biomol. Chem. 8, 1749-1762 (2010).
    • (2010) Org. Biomol. Chem. , vol.8 , pp. 1749-1762
    • Kalesh, K.A.1    Shi, H.2    Ge, J.3    Yao, S.Q.4
  • 36
    • 77955891252 scopus 로고    scopus 로고
    • Discovery of pyrrole-indoline-2-ones as Aurora kinase inhibitors with a different inhibition profile
    • Chiang, C.-C. et al. Discovery of pyrrole-indoline-2-ones as Aurora kinase inhibitors with a different inhibition profile. J. Med. Chem. 53, 5929-5941 (2010).
    • (2010) J. Med. Chem. , vol.53 , pp. 5929-5941
    • Chiang, C.-C.1
  • 37
    • 84884181549 scopus 로고    scopus 로고
    • Bioorthogonal labelling of biomolecules: New functional handles and ligation methods
    • Debets, M. F., van Hest, J. C. M. & Rutjes, F. P. J. T. Bioorthogonal labelling of biomolecules: new functional handles and ligation methods. Org. Biomol. Chem. 11, 6439-6455 (2013).
    • (2013) Org. Biomol. Chem. , vol.11 , pp. 6439-6455
    • Debets, M.F.1    Van Hest, J.C.M.2    Rutjes, F.P.J.T.3
  • 38
    • 84898072114 scopus 로고    scopus 로고
    • Bioorthogonal reactions for labeling proteins
    • Lang, K. & Chin, J. W. Bioorthogonal reactions for labeling proteins. ACS Chem. Biol. 9, 16-20 (2014).
    • (2014) ACS Chem. Biol. , vol.9 , pp. 16-20
    • Lang, K.1    Chin, J.W.2
  • 39
    • 0033529263 scopus 로고    scopus 로고
    • Nuclear and cell membrane effects contribute independently to the induction of apoptosis in human cells exposed to UVB radiation
    • Kulms, D. et al. Nuclear and cell membrane effects contribute independently to the induction of apoptosis in human cells exposed to UVB radiation. Proc. Natl. Acad. Sci. 96, 7974-7979 (1999).
    • (1999) Proc. Natl. Acad. Sci. , vol.96 , pp. 7974-7979
    • Kulms, D.1
  • 40
    • 0031409635 scopus 로고    scopus 로고
    • Induction of oxidativeDNAbase damage in human skin cells by UV and near visible radiation
    • Kvam, E.&Tyrrell, R. M. Induction of oxidativeDNAbase damage in human skin cells by UV and near visible radiation. Carcinogenesis 18, 2379-2384 (1997).
    • (1997) Carcinogenesis , vol.18 , pp. 2379-2384
    • Kvam, E.1    Tyrrell, R.M.2
  • 41
    • 84861912742 scopus 로고    scopus 로고
    • Fast, cell-compatible click chemistry with copperchelating azides for biomolecular labeling
    • Uttamapinant, C. et al. Fast, cell-compatible click chemistry with copperchelating azides for biomolecular labeling. Angew. Chem. Int. Ed. 51, 5852-5856 (2012).
    • (2012) Angew. Chem. Int. Ed. , vol.51 , pp. 5852-5856
    • Uttamapinant, C.1
  • 42
    • 80051727754 scopus 로고    scopus 로고
    • Increasing the efficacy of bioorthogonal click reactions for bioconjugation: A comparative study
    • Besanceney-Webler, C. et al. Increasing the efficacy of bioorthogonal click reactions for bioconjugation: a comparative study. Angew. Chem. Int. Ed. 50, 8051-8056 (2011).
    • (2011) Angew. Chem. Int. Ed. , vol.50 , pp. 8051-8056
    • Besanceney-Webler, C.1
  • 43
    • 72449154666 scopus 로고    scopus 로고
    • Analysis and optimization of copper-catalyzed azide-alkyne cycloaddition for bioconjugation
    • Hong, V., Presolski, S. I., Ma, C. & Finn, M. G. Analysis and optimization of copper-catalyzed azide-alkyne cycloaddition for bioconjugation. Angew. Chem. Int. Ed. 48, 9879-9883 (2009).
    • (2009) Angew. Chem. Int. Ed. , vol.48 , pp. 9879-9883
    • Hong, V.1    Presolski, S.I.2    Ma, C.3    Finn, M.G.4
  • 44
    • 56749104130 scopus 로고    scopus 로고
    • Fluorescent probes for super-resolution imaging in living cells
    • Fernandez-Suarez, M. & Ting, A. Y. Fluorescent probes for super-resolution imaging in living cells. Nat. Rev. Mol. Cell Biol. 9, 929-943 (2008).
    • (2008) Nat. Rev. Mol. Cell Biol. , vol.9 , pp. 929-943
    • Fernandez-Suarez, M.1    Ting, A.Y.2
  • 45
    • 83055180536 scopus 로고    scopus 로고
    • Functional imaging of proteases: Recent advances in the design and application of substrate-based and activity-based probes
    • Edgington, L. E., Verdoes, M.&Bogyo, M. Functional imaging of proteases: recent advances in the design and application of substrate-based and activity-based probes. Curr. Opin. Chem.l Biol. 15, 798-805 (2011).
    • (2011) Curr. Opin. Chem.l Biol. , vol.15 , pp. 798-805
    • Edgington, L.E.1    Verdoes, M.2    Bogyo, M.3
  • 46
    • 0037100740 scopus 로고    scopus 로고
    • Targeting the cell cycle for cancer therapy
    • Carnero, A. Targeting the cell cycle for cancer therapy. Br. J. Cancer 87, 129-133 (2002).
    • (2002) Br. J. Cancer , vol.87 , pp. 129-133
    • Carnero, A.1
  • 47
    • 78649476052 scopus 로고    scopus 로고
    • Shared and separate functions of polo-like kinases and aurora kinases in cancer
    • Lens, S. M. A., Voest, E. E. & Medema, R. H. Shared and separate functions of polo-like kinases and aurora kinases in cancer. Nat. Rev. Cancer 10, 825-841 (2010).
    • (2010) Nat. Rev. Cancer , vol.10 , pp. 825-841
    • Lens, S.M.A.1    Voest, E.E.2    Medema, R.H.3
  • 48
    • 77954356005 scopus 로고    scopus 로고
    • Cdk1 activity is required for mitotic activation of Aurora A during G(2)/M transition of human cells
    • Van Horn, R. D. et al. Cdk1 activity is required for mitotic activation of Aurora A during G(2)/M transition of human cells. J. Biol. Chem. 285, 21849-21857 (2010).
    • (2010) J. Biol. Chem. , vol.285 , pp. 21849-21857
    • Van Horn, R.D.1
  • 49
    • 67650762824 scopus 로고    scopus 로고
    • Super resolution fluorescence microscopy
    • Huang, B., Bates, M. & Zhuang, X. Super resolution fluorescence microscopy. Annu. Rev. Biochem. 78, 993-1016 (2009).
    • (2009) Annu. Rev. Biochem. , vol.78 , pp. 993-1016
    • Huang, B.1    Bates, M.2    Zhuang, X.3
  • 50
    • 13844297577 scopus 로고    scopus 로고
    • Imaging protein molecules using FRET and FLIM microscopy
    • Wallrabe, H. & Periasamy, A. Imaging protein molecules using FRET and FLIM microscopy. Curr. Opin. Biotechnol. 16, 19-27 (2005).
    • (2005) Curr. Opin. Biotechnol. , vol.16 , pp. 19-27
    • Wallrabe, H.1    Periasamy, A.2
  • 51
    • 33645453254 scopus 로고    scopus 로고
    • Global landscape of protein complexes in the yeast Saccharomyces cerevisiae
    • Krogan, N. J. et al. Global landscape of protein complexes in the yeast Saccharomyces cerevisiae. Nature 440, 637-643 (2006).
    • (2006) Nature , vol.440 , pp. 637-643
    • Krogan, N.J.1
  • 52
    • 84881475940 scopus 로고    scopus 로고
    • The CRAPome: A contaminant repository for affinity purification-mass spectrometry data
    • Mellacheruvu, D. et al. The CRAPome: a contaminant repository for affinity purification-mass spectrometry data. Nat. Methods 10, 730-736 (2013).
    • (2013) Nat. Methods , vol.10 , pp. 730-736
    • Mellacheruvu, D.1
  • 54
  • 55
    • 33745972064 scopus 로고    scopus 로고
    • NudC is required for Plk1 targeting to the kinetochore and chromosome congression
    • Nishino, M. et al. NudC is required for Plk1 targeting to the kinetochore and chromosome congression. Curr. Biol. 16, 1414-1421 (2006).
    • (2006) Curr. Biol. , vol.16 , pp. 1414-1421
    • Nishino, M.1
  • 56
    • 84863500157 scopus 로고    scopus 로고
    • Fully functionalized small-molecule probes for integrated phenotypic screening and target identification
    • Cisar, J. S. & Cravatt, B. F. Fully functionalized small-molecule probes for integrated phenotypic screening and target identification. J. Am. Chem. Soc. 134, 10385-10388 (2012).
    • (2012) J. Am. Chem. Soc. , vol.134 , pp. 10385-10388
    • Cisar, J.S.1    Cravatt, B.F.2


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