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Volumn 20, Issue 8, 2009, Pages 1504-1513

Probing Akt-Inhibitor Interaction by Chemical Cross-Linking and Mass Spectrometry

Author keywords

[No Author keywords available]

Indexed keywords

AKT ACTIVATION; ANTI-TUMOR AGENTS; CELL SURVIVAL; CHEMICAL CROSS-LINKING; CONFORMATIONAL CHANGE; DRUG DISCOVERY; HUMAN MALIGNANCIES; INTER-DOMAIN; KINASE DOMAINS; NOVEL STRATEGIES; OPEN CONFORMATION; PLASMA MEMBRANES; QUANTITATIVE COMPARISON; REGULATORY DOMAIN; THERAPEUTIC STRATEGY; UNILAMELLAR VESICLE;

EID: 67650725991     PISSN: 10440305     EISSN: None     Source Type: Journal    
DOI: 10.1016/j.jasms.2009.04.004     Document Type: Article
Times cited : (15)

References (39)
  • 1
    • 0035499454 scopus 로고    scopus 로고
    • Ten Years of Protein Kinase B Signaling: A Hard Akt to Follow
    • Brazil D.P., and Hemmings B.A. Ten Years of Protein Kinase B Signaling: A Hard Akt to Follow. Trends Biochem. Sci. 26 (2001) 657-664
    • (2001) Trends Biochem. Sci. , vol.26 , pp. 657-664
    • Brazil, D.P.1    Hemmings, B.A.2
  • 2
    • 0034845958 scopus 로고    scopus 로고
    • PKB/Akt: A Key Mediator of Cell Proliferation, Survival, and Insulin Responses?
    • Lawlor M.A., and Alessi D.R. PKB/Akt: A Key Mediator of Cell Proliferation, Survival, and Insulin Responses?. J. Cell Sci. 114 (2001) 2903-2910
    • (2001) J. Cell Sci. , vol.114 , pp. 2903-2910
    • Lawlor, M.A.1    Alessi, D.R.2
  • 3
    • 0037205048 scopus 로고    scopus 로고
    • The Phosphoinositide 3-kinase Pathway
    • Cantley L.C. The Phosphoinositide 3-kinase Pathway. Science 296 (2002) 1655-1657
    • (2002) Science , vol.296 , pp. 1655-1657
    • Cantley, L.C.1
  • 4
    • 0030702123 scopus 로고    scopus 로고
    • Akt Phosphorylation of BAD Couples Survival Signals to the Cell-Intrinsic Death Machinery
    • Datta S.R., Dudek H., Tao X., Masters S., Fu H., Gotoh Y., and Greenberg M.E. Akt Phosphorylation of BAD Couples Survival Signals to the Cell-Intrinsic Death Machinery. Cell 91 (1997) 231-241
    • (1997) Cell , vol.91 , pp. 231-241
    • Datta, S.R.1    Dudek, H.2    Tao, X.3    Masters, S.4    Fu, H.5    Gotoh, Y.6    Greenberg, M.E.7
  • 8
    • 0036185848 scopus 로고    scopus 로고
    • The Protein Kinase B/Akt Signaling Pathway in Human Malignancy
    • Nicholson K.M., and Anderson N.G. The Protein Kinase B/Akt Signaling Pathway in Human Malignancy. Cell Signal 14 (2002) 381-395
    • (2002) Cell Signal , vol.14 , pp. 381-395
    • Nicholson, K.M.1    Anderson, N.G.2
  • 11
    • 0034604067 scopus 로고    scopus 로고
    • Frequent Activation of AKT2 and Induction of Apoptosis by Inhibition of Phosphoinositide-3-OH Kinase/Akt Pathway in Human Ovarian Cancer
    • Yuan Z.Q., Sun M., Feldman R.I., Wang G., Ma X., Jiang C., Coppola D., Nicosia S.V., and Cheng J.Q. Frequent Activation of AKT2 and Induction of Apoptosis by Inhibition of Phosphoinositide-3-OH Kinase/Akt Pathway in Human Ovarian Cancer. Oncogene 19 (2000) 2324-2330
    • (2000) Oncogene , vol.19 , pp. 2324-2330
    • Yuan, Z.Q.1    Sun, M.2    Feldman, R.I.3    Wang, G.4    Ma, X.5    Jiang, C.6    Coppola, D.7    Nicosia, S.V.8    Cheng, J.Q.9
  • 12
    • 26444448463 scopus 로고    scopus 로고
    • The Survival Kinases Akt and Pim as Potential Pharmacological Targets
    • Amaravadi A., and Thompson C.B. The Survival Kinases Akt and Pim as Potential Pharmacological Targets. J. Clin. Invest. 115 (2005) 2618-2624
    • (2005) J. Clin. Invest. , vol.115 , pp. 2618-2624
    • Amaravadi, A.1    Thompson, C.B.2
  • 13
    • 0031913246 scopus 로고    scopus 로고
    • Mechanism of Activation and Function of Protein Kinase B
    • Alessi D.R., and Cohen P. Mechanism of Activation and Function of Protein Kinase B. Curr. Opin. Genet. Dev. 8 (1998) 55-62
    • (1998) Curr. Opin. Genet. Dev. , vol.8 , pp. 55-62
    • Alessi, D.R.1    Cohen, P.2
  • 14
    • 0036295728 scopus 로고    scopus 로고
    • Molecular Mechanism for the Regulation of Protein Kinase B/Akt by Hydrophobic Motif Phosphorylation
    • Yang J., Cron P., Thompson V., Good V.M., Hess D., Hemmings B.A., and Barford D. Molecular Mechanism for the Regulation of Protein Kinase B/Akt by Hydrophobic Motif Phosphorylation. Mol. Cell 9 (2002) 1227-1240
    • (2002) Mol. Cell , vol.9 , pp. 1227-1240
    • Yang, J.1    Cron, P.2    Thompson, V.3    Good, V.M.4    Hess, D.5    Hemmings, B.A.6    Barford, D.7
  • 15
    • 33745610132 scopus 로고    scopus 로고
    • Interdomain Conformational Changes in Akt Activation Revealed by Chemical Cross-linking and Tandem Mass Spectrometry
    • Huang B.X., and Kim H.-Y. Interdomain Conformational Changes in Akt Activation Revealed by Chemical Cross-linking and Tandem Mass Spectrometry. Mol. Cell. Proteom. 5 (2006) 1045-1053
    • (2006) Mol. Cell. Proteom. , vol.5 , pp. 1045-1053
    • Huang, B.X.1    Kim, H.-Y.2
  • 18
    • 0034632791 scopus 로고    scopus 로고
    • 3-(Hydroxymethyl)-Bearing Phosphatidylinositol Ether Lipid Analogs and Carbonate Surrogates Block PI3-K, Akt, and Cancer Cell Growth
    • Hu Y., Qiao L., Wang S., Rong S., Meuillet E.J., Berggren M., Gallegos A., Powis G., and Kozikowski A.P. 3-(Hydroxymethyl)-Bearing Phosphatidylinositol Ether Lipid Analogs and Carbonate Surrogates Block PI3-K, Akt, and Cancer Cell Growth. J. Med. Chem. 43 (2003) 3045-3051
    • (2003) J. Med. Chem. , vol.43 , pp. 3045-3051
    • Hu, Y.1    Qiao, L.2    Wang, S.3    Rong, S.4    Meuillet, E.J.5    Berggren, M.6    Gallegos, A.7    Powis, G.8    Kozikowski, A.P.9
  • 19
    • 11144222174 scopus 로고    scopus 로고
    • Inhibition of Akt Kinase Activity by a Peptide Spanning the βA Strand of the Proto-oncogene TCL1
    • Hiromura M., Okada F., Obata T., Auguin D., Shibata T., Roumestand C., and Noguchi M. Inhibition of Akt Kinase Activity by a Peptide Spanning the βA Strand of the Proto-oncogene TCL1. J. Biol. Chem. 279 (2004) 53407-53418
    • (2004) J. Biol. Chem. , vol.279 , pp. 53407-53418
    • Hiromura, M.1    Okada, F.2    Obata, T.3    Auguin, D.4    Shibata, T.5    Roumestand, C.6    Noguchi, M.7
  • 20
    • 0026095665 scopus 로고
    • A Retroviral Oncogene, Akt, Encoding a Serine-threonine Kinase Containing a SH2-like Region
    • Bellacosa A., Testa J.R., Staal S.P., and Tsichlis P.N. A Retroviral Oncogene, Akt, Encoding a Serine-threonine Kinase Containing a SH2-like Region. Science 254 (1991) 274-277
    • (1991) Science , vol.254 , pp. 274-277
    • Bellacosa, A.1    Testa, J.R.2    Staal, S.P.3    Tsichlis, P.N.4
  • 21
    • 0037162293 scopus 로고    scopus 로고
    • High-resolution Structure of the Pleckstrin Homology Domain of Protein Kinase B/Akt Bound to Phosphatidylinositol (3,4,5)-Trisphosphate
    • Thomas C.C., Deak M., Alessi D.R., and van Aalten D.M.F. High-resolution Structure of the Pleckstrin Homology Domain of Protein Kinase B/Akt Bound to Phosphatidylinositol (3,4,5)-Trisphosphate. Curr. Biol. 12 (2002) 1256-1262
    • (2002) Curr. Biol. , vol.12 , pp. 1256-1262
    • Thomas, C.C.1    Deak, M.2    Alessi, D.R.3    van Aalten, D.M.F.4
  • 25
    • 0033594403 scopus 로고    scopus 로고
    • Akt/PKB Localization and 3′ Phosphoinositide Generation at Sites of Epithelial Cell-Matrix and Cell-Cell Interaction
    • Watton S.J., and Downward J. Akt/PKB Localization and 3′ Phosphoinositide Generation at Sites of Epithelial Cell-Matrix and Cell-Cell Interaction. Curr. Biol. 9 (1999) 433-436
    • (1999) Curr. Biol. , vol.9 , pp. 433-436
    • Watton, S.J.1    Downward, J.2
  • 26
    • 0242468741 scopus 로고    scopus 로고
    • Binding of Phosphatidylinositol 3,4,5-Trisphosphate to the Pleckstrin Homology Domain of Protein Kinase B Induces A Conformational Change
    • Milburn C.C., Deak M., Kelly S.M., Price S.M., Alessi D.R., and van Aalten D.M.F. Binding of Phosphatidylinositol 3,4,5-Trisphosphate to the Pleckstrin Homology Domain of Protein Kinase B Induces A Conformational Change. Biochem. J. 375 (2003) 531-538
    • (2003) Biochem. J. , vol.375 , pp. 531-538
    • Milburn, C.C.1    Deak, M.2    Kelly, S.M.3    Price, S.M.4    Alessi, D.R.5    van Aalten, D.M.F.6
  • 27
    • 18744373865 scopus 로고    scopus 로고
    • Crystal Structure of an Activated Akt/Protein Kinase B Ternary Complex with GSK3-peptide and AMP-PNP
    • Yang J., Cron P., Good V.M., Thompson V., Hemmings B.A., and Barford D. Crystal Structure of an Activated Akt/Protein Kinase B Ternary Complex with GSK3-peptide and AMP-PNP. Nat. Struct. Biol. 12 (2002) 940-944
    • (2002) Nat. Struct. Biol. , vol.12 , pp. 940-944
    • Yang, J.1    Cron, P.2    Good, V.M.3    Thompson, V.4    Hemmings, B.A.5    Barford, D.6
  • 28
    • 1242263882 scopus 로고    scopus 로고
    • Solution Structure and Backbone Dynamics of the Pleckstrin Homology Domain of the Human Protein Kinase B (PKB/Akt): Interaction with Inositol Phosphates
    • Auguin D., Barthe P., Auge-Senegas M., Stern M., Noguchi M., and Roumestand C. Solution Structure and Backbone Dynamics of the Pleckstrin Homology Domain of the Human Protein Kinase B (PKB/Akt): Interaction with Inositol Phosphates. J. Biomol. NMR 28 (2004) 137-155
    • (2004) J. Biomol. NMR , vol.28 , pp. 137-155
    • Auguin, D.1    Barthe, P.2    Auge-Senegas, M.3    Stern, M.4    Noguchi, M.5    Roumestand, C.6
  • 29
    • 0038630916 scopus 로고    scopus 로고
    • Monitoring Conformational Changes of Proteins in cells by Fluorescence Lifetime Imaging Microscopy
    • Calleja V., Ameer-beg S.M., Vojnovic B., Woscholski R., Downward J., and Larijani B. Monitoring Conformational Changes of Proteins in cells by Fluorescence Lifetime Imaging Microscopy. Biochem. J. 372 (2003) 33-40
    • (2003) Biochem. J. , vol.372 , pp. 33-40
    • Calleja, V.1    Ameer-beg, S.M.2    Vojnovic, B.3    Woscholski, R.4    Downward, J.5    Larijani, B.6
  • 30
    • 0034705128 scopus 로고    scopus 로고
    • High Throughput Protein Fold Identification by Using Experimental Constraints Derived from Intramolecular Cross-Links and Mass Spectrometry
    • Young M.M., Tang N., Hempel J.C., Oshiro C.M., Taylor E.W., Kuntz I.D., Gibson B.W., and Dollinger G. High Throughput Protein Fold Identification by Using Experimental Constraints Derived from Intramolecular Cross-Links and Mass Spectrometry. Proc. Natl. Acad. Sci. U.S.A. 97 (2000) 5802-5806
    • (2000) Proc. Natl. Acad. Sci. U.S.A. , vol.97 , pp. 5802-5806
    • Young, M.M.1    Tang, N.2    Hempel, J.C.3    Oshiro, C.M.4    Taylor, E.W.5    Kuntz, I.D.6    Gibson, B.W.7    Dollinger, G.8
  • 31
    • 0347286732 scopus 로고    scopus 로고
    • Chemical Cross-Linking and Mass Spectrometry for Mapping Three-Dimensional Structures of Proteins and Protein Complexes
    • Sinz A. Chemical Cross-Linking and Mass Spectrometry for Mapping Three-Dimensional Structures of Proteins and Protein Complexes. J. Mass Spectrom. 38 (2003) 1225-1237
    • (2003) J. Mass Spectrom. , vol.38 , pp. 1225-1237
    • Sinz, A.1
  • 32
    • 3242772209 scopus 로고    scopus 로고
    • Probing Three-Dimensional Structure of Bovine Serum Albumin by Chemical Cross-Linking and Mass Spectrometry
    • Huang B.X., Dass C., and Kim H.-Y. Probing Three-Dimensional Structure of Bovine Serum Albumin by Chemical Cross-Linking and Mass Spectrometry. J. Am. Soc. Mass Spectrom. 15 (2004) 1237-1247
    • (2004) J. Am. Soc. Mass Spectrom. , vol.15 , pp. 1237-1247
    • Huang, B.X.1    Dass, C.2    Kim, H.-Y.3
  • 33
    • 0035384687 scopus 로고    scopus 로고
    • 18O labeling for Comparative Proteomics: Model Studies with Two Serotypes of Adenovirus
    • 18O labeling for Comparative Proteomics: Model Studies with Two Serotypes of Adenovirus. Anal. Chem. 73 (2001) 2836-2842
    • (2001) Anal. Chem. , vol.73 , pp. 2836-2842
    • Yao, X.1    Freas, A.2    Ramirez, J.3    Demirev, P.A.4    Fenselau, C.5
  • 35
    • 18844423484 scopus 로고    scopus 로고
    • Probing Conformational Changes of Human Serum Albumin Due to Unsaturated Fatty Acid Binding by Chemical Cross-Linking and Mass Spectrometry
    • Huang B.X., Dass C., and Kim H.-Y. Probing Conformational Changes of Human Serum Albumin Due to Unsaturated Fatty Acid Binding by Chemical Cross-Linking and Mass Spectrometry. Biochem. J. 387 (2005) 695-702
    • (2005) Biochem. J. , vol.387 , pp. 695-702
    • Huang, B.X.1    Dass, C.2    Kim, H.-Y.3
  • 36
    • 0942279701 scopus 로고    scopus 로고
    • Substrate Preference in Phosphatidylserine Biosynthesis for Docosahexaenoic Acid Containing Species
    • Kim H.-Y., Bigelow J., and Kevala J.H. Substrate Preference in Phosphatidylserine Biosynthesis for Docosahexaenoic Acid Containing Species. Biochemistry 43 (2001) 1030-1036
    • (2001) Biochemistry , vol.43 , pp. 1030-1036
    • Kim, H.-Y.1    Bigelow, J.2    Kevala, J.H.3
  • 37
    • 3042561796 scopus 로고    scopus 로고
    • Alterations in Hippocampal Phospholipid Profile by Prenatal Exposure to Ethanol
    • Wen Z., and Kim H.-Y. Alterations in Hippocampal Phospholipid Profile by Prenatal Exposure to Ethanol. J. Neurochem. 89 (2004) 1368-1377
    • (2004) J. Neurochem. , vol.89 , pp. 1368-1377
    • Wen, Z.1    Kim, H.-Y.2
  • 38
    • 4544282394 scopus 로고    scopus 로고
    • High-Throughput Comparative Proteome Analysis Using a Quantitative Cysteinyl-Peptide Enrichment Technology
    • Liu T., Qian W.-J., Strittmatter E.F., Camp D.G., Anderson G.A., Thrall B.D., and Smith R.D. High-Throughput Comparative Proteome Analysis Using a Quantitative Cysteinyl-Peptide Enrichment Technology. Anal. Chem. 76 (2004) 5345-5353
    • (2004) Anal. Chem. , vol.76 , pp. 5345-5353
    • Liu, T.1    Qian, W.-J.2    Strittmatter, E.F.3    Camp, D.G.4    Anderson, G.A.5    Thrall, B.D.6    Smith, R.D.7
  • 39
    • 34247346010 scopus 로고    scopus 로고
    • Electrical Properties of Plasma Membrane Modulate Subcellular Distribution of K-Ras
    • Gomez G.A., and Daniotti J.L. Electrical Properties of Plasma Membrane Modulate Subcellular Distribution of K-Ras. FEBS J. 274 (2007) 2210-2228
    • (2007) FEBS J. , vol.274 , pp. 2210-2228
    • Gomez, G.A.1    Daniotti, J.L.2


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