메뉴 건너뛰기




Volumn 9, Issue 3-4, 2015, Pages 383-395

Role of phosphoproteomics in the development of personalized cancer therapies

Author keywords

Mass spectrometry; Network biology; Precision medicine; Systems biology

Indexed keywords

B RAF KINASE; BCR ABL PROTEIN; BIOLOGICAL MARKER; EPIDERMAL GROWTH FACTOR RECEPTOR 2; GEFITINIB; GLYCOGEN SYNTHASE KINASE 3BETA; HYDROXYMETHYLGLUTARYL COENZYME A REDUCTASE KINASE; IMATINIB; MITOGEN ACTIVATED PROTEIN KINASE; PHOSPHATIDYLINOSITOL 3 KINASE; PHOSPHATIDYLINOSITOL 3 KINASE INHIBITOR; PHOSPHOPROTEIN; PROTEIN KINASE B; SORAFENIB; TRASTUZUMAB; VEMURAFENIB; PHOSPHOPEPTIDE;

EID: 84928055838     PISSN: 18628346     EISSN: 18628354     Source Type: Journal    
DOI: 10.1002/prca.201400104     Document Type: Review
Times cited : (39)

References (93)
  • 1
    • 84890641204 scopus 로고    scopus 로고
    • The coming of age of phosphoproteomics-from large data sets to inference of protein functions
    • Roux, P. P., Thibault, P., The coming of age of phosphoproteomics-from large data sets to inference of protein functions. Mol. Cell. Proteomics 2013, 12, 3453-3464.
    • (2013) Mol. Cell. Proteomics , vol.12 , pp. 3453-3464
    • Roux, P.P.1    Thibault, P.2
  • 2
    • 84886583205 scopus 로고    scopus 로고
    • Phosphoproteomics-based network medicine
    • Liu, Z., Wang, Y., Xue, Y., Phosphoproteomics-based network medicine. FEBS J. 2013, 280, 5696-5704.
    • (2013) FEBS J. , vol.280 , pp. 5696-5704
    • Liu, Z.1    Wang, Y.2    Xue, Y.3
  • 3
    • 84855572697 scopus 로고    scopus 로고
    • Mapping in vivo signal transduction defects by phosphoproteomics
    • Stasyk, T., Huber, L. A., Mapping in vivo signal transduction defects by phosphoproteomics. Trends Mol. Med. 2012, 18, 43-51.
    • (2012) Trends Mol. Med. , vol.18 , pp. 43-51
    • Stasyk, T.1    Huber, L.A.2
  • 4
    • 79951523091 scopus 로고    scopus 로고
    • Biological signalling activity measurements using mass spectrometry
    • Cutillas, P. R., Jorgensen, C., Biological signalling activity measurements using mass spectrometry. Biochem. J. 2011, 434, 189-199.
    • (2011) Biochem. J. , vol.434 , pp. 189-199
    • Cutillas, P.R.1    Jorgensen, C.2
  • 5
    • 84905855506 scopus 로고    scopus 로고
    • Adaptive protein and phosphoprotein networks which promote therapeutic sensitivity or acquired resistance
    • Haley, J., White, F. M., Adaptive protein and phosphoprotein networks which promote therapeutic sensitivity or acquired resistance. Biochem. Soc. Trans. 2014, 42, 758-764.
    • (2014) Biochem. Soc. Trans. , vol.42 , pp. 758-764
    • Haley, J.1    White, F.M.2
  • 6
    • 84905861302 scopus 로고    scopus 로고
    • Approaches for measuring signalling plasticity in the context of resistance to targeted cancer therapies
    • Wilkes, E. H., Casado, P., Cutillas, P. R., Approaches for measuring signalling plasticity in the context of resistance to targeted cancer therapies. Biochem. Soc. Trans. 2014, 42, 791-797.
    • (2014) Biochem. Soc. Trans. , vol.42 , pp. 791-797
    • Wilkes, E.H.1    Casado, P.2    Cutillas, P.R.3
  • 7
    • 79959476700 scopus 로고    scopus 로고
    • The evolution of protein kinase inhibitors from antagonists to agonists of cellular signaling
    • Dar, A. C., Shokat, K. M., The evolution of protein kinase inhibitors from antagonists to agonists of cellular signaling. Ann. Rev. Biochem. 2011, 80, 769-795.
    • (2011) Ann. Rev. Biochem. , vol.80 , pp. 769-795
    • Dar, A.C.1    Shokat, K.M.2
  • 8
    • 0037093092 scopus 로고    scopus 로고
    • Imatinib induces hematologic and cytogenetic responses in patients with chronic myelogenous leukemia in myeloid blast crisis: results of a phase II study
    • Sawyers, C. L., Hochhaus, A., Feldman, E., Goldman, J. M. et al., Imatinib induces hematologic and cytogenetic responses in patients with chronic myelogenous leukemia in myeloid blast crisis: results of a phase II study. Blood 2002, 99, 3530-3539.
    • (2002) Blood , vol.99 , pp. 3530-3539
    • Sawyers, C.L.1    Hochhaus, A.2    Feldman, E.3    Goldman, J.M.4
  • 9
    • 70350435633 scopus 로고    scopus 로고
    • Shifting paradigms: the seeds of oncogene addiction
    • Sawyers, C. L., Shifting paradigms: the seeds of oncogene addiction. Nat. Med. 2009, 15, 1158-1161.
    • (2009) Nat. Med. , vol.15 , pp. 1158-1161
    • Sawyers, C.L.1
  • 10
    • 79952284127 scopus 로고    scopus 로고
    • Hallmarks of cancer: the next generation
    • Hanahan, D., Weinberg, R. A., Hallmarks of cancer: the next generation. Cell 2011, 144, 646-674.
    • (2011) Cell , vol.144 , pp. 646-674
    • Hanahan, D.1    Weinberg, R.A.2
  • 11
    • 16644393213 scopus 로고    scopus 로고
    • The PIK3CA gene is mutated with high frequency in human breast cancers
    • Bachman, K. E., Argani, P., Samuels, Y., Silliman, N. et al., The PIK3CA gene is mutated with high frequency in human breast cancers. Cancer Biol. Ther. 2004, 3, 772-775.
    • (2004) Cancer Biol. Ther. , vol.3 , pp. 772-775
    • Bachman, K.E.1    Argani, P.2    Samuels, Y.3    Silliman, N.4
  • 12
    • 11144358645 scopus 로고    scopus 로고
    • High frequency of mutations of the PIK3CA gene in human cancers
    • Samuels, Y., Wang, Z., Bardelli, A., Silliman, N. et al., High frequency of mutations of the PIK3CA gene in human cancers. Science 2004, 304, 554.
    • (2004) Science , vol.304 , pp. 554
    • Samuels, Y.1    Wang, Z.2    Bardelli, A.3    Silliman, N.4
  • 13
    • 51849111524 scopus 로고    scopus 로고
    • NVP-BEZ235, a dual PI3K/mTOR inhibitor, prevents PI3K signaling and inhibits the growth of cancer cells with activating PI3K mutations
    • Serra, V., Markman, B., Scaltriti, M., Eichhorn, P. J. et al., NVP-BEZ235, a dual PI3K/mTOR inhibitor, prevents PI3K signaling and inhibits the growth of cancer cells with activating PI3K mutations. Cancer Res. 2008, 68, 8022-8030.
    • (2008) Cancer Res. , vol.68 , pp. 8022-8030
    • Serra, V.1    Markman, B.2    Scaltriti, M.3    Eichhorn, P.J.4
  • 14
    • 0036894746 scopus 로고    scopus 로고
    • BRAF and RAS mutations in human lung cancer and melanoma
    • Brose, M. S., Volpe, P., Feldman, M., Kumar, M. et al., BRAF and RAS mutations in human lung cancer and melanoma. Cancer Res. 2002, 62, 6997-7000.
    • (2002) Cancer Res. , vol.62 , pp. 6997-7000
    • Brose, M.S.1    Volpe, P.2    Feldman, M.3    Kumar, M.4
  • 15
    • 18444374405 scopus 로고    scopus 로고
    • Mutations of the BRAF gene in human cancer
    • Davies, H., Bignell, G. R., Cox, C., Stephens, P. et al., Mutations of the BRAF gene in human cancer. Nature 2002, 417, 949-954.
    • (2002) Nature , vol.417 , pp. 949-954
    • Davies, H.1    Bignell, G.R.2    Cox, C.3    Stephens, P.4
  • 16
    • 79959795786 scopus 로고    scopus 로고
    • Improved survival with vemurafenib in melanoma with BRAF V600E mutation
    • Chapman, P. B., Hauschild, A., Robert, C., Haanen, J. B. et al., Improved survival with vemurafenib in melanoma with BRAF V600E mutation. N. Engl. J. Med. 2011, 364, 2507-2516.
    • (2011) N. Engl. J. Med. , vol.364 , pp. 2507-2516
    • Chapman, P.B.1    Hauschild, A.2    Robert, C.3    Haanen, J.B.4
  • 17
    • 69949162760 scopus 로고    scopus 로고
    • Gefitinib or carboplatin-paclitaxel in pulmonary adenocarcinoma
    • Mok, T. S., Wu, Y. L., Thongprasert, S., Yang, C. H. et al., Gefitinib or carboplatin-paclitaxel in pulmonary adenocarcinoma. N. Engl. J. Med. 2009, 361, 947-957.
    • (2009) N. Engl. J. Med. , vol.361 , pp. 947-957
    • Mok, T.S.1    Wu, Y.L.2    Thongprasert, S.3    Yang, C.H.4
  • 18
    • 2342624080 scopus 로고    scopus 로고
    • EGFR mutations in lung cancer: correlation with clinical response to gefitinib therapy
    • Paez, J. G., Janne, P. A., Lee, J. C., Tracy, S. et al., EGFR mutations in lung cancer: correlation with clinical response to gefitinib therapy. Science 2004, 304, 1497-1500.
    • (2004) Science , vol.304 , pp. 1497-1500
    • Paez, J.G.1    Janne, P.A.2    Lee, J.C.3    Tracy, S.4
  • 19
    • 48649107474 scopus 로고    scopus 로고
    • Efficacy of everolimus in advanced renal cell carcinoma: a double-blind, randomised, placebo-controlled phase III trial
    • Motzer, R. J., Escudier, B., Oudard, S., Hutson, T. E. et al., Efficacy of everolimus in advanced renal cell carcinoma: a double-blind, randomised, placebo-controlled phase III trial. Lancet 2008, 372, 449-456.
    • (2008) Lancet , vol.372 , pp. 449-456
    • Motzer, R.J.1    Escudier, B.2    Oudard, S.3    Hutson, T.E.4
  • 20
    • 84874144193 scopus 로고    scopus 로고
    • Personalized cancer medicine: molecular diagnostics, predictive biomarkers, and drug resistance
    • Gonzalez de Castro, D., Clarke, P. A., Al-Lazikani, B., Workman, P., Personalized cancer medicine: molecular diagnostics, predictive biomarkers, and drug resistance. Clin. Pharmacol. Ther. 2013, 93, 252-259.
    • (2013) Clin. Pharmacol. Ther. , vol.93 , pp. 252-259
    • Gonzalez de Castro, D.1    Clarke, P.A.2    Al-Lazikani, B.3    Workman, P.4
  • 21
    • 0036467826 scopus 로고    scopus 로고
    • Efficacy and safety of trastuzumab as a single agent in first-line treatment of HER2-overexpressing metastatic breast cancer
    • Vogel, C. L., Cobleigh, M. A., Tripathy, D., Gutheil, J. C. et al., Efficacy and safety of trastuzumab as a single agent in first-line treatment of HER2-overexpressing metastatic breast cancer. J. Clin. Oncol. 2002, 20, 719-726.
    • (2002) J. Clin. Oncol. , vol.20 , pp. 719-726
    • Vogel, C.L.1    Cobleigh, M.A.2    Tripathy, D.3    Gutheil, J.C.4
  • 22
    • 70149093912 scopus 로고    scopus 로고
    • Recurring mutations found by sequencing an acute myeloid leukemia genome
    • Mardis, E. R., Ding, L., Dooling, D. J., Larson, D. E. et al., Recurring mutations found by sequencing an acute myeloid leukemia genome. N. Engl. J.Med. 2009, 361, 1058-1066.
    • (2009) N. Engl. J.Med. , vol.361 , pp. 1058-1066
    • Mardis, E.R.1    Ding, L.2    Dooling, D.J.3    Larson, D.E.4
  • 23
    • 78249261016 scopus 로고    scopus 로고
    • Accumulation of driver and passenger mutations during tumor progression
    • Bozic, I., Antal, T., Ohtsuki, H., Carter, H. et al., Accumulation of driver and passenger mutations during tumor progression. Proc. Natl. Acad. Sci. USA 2010, 107, 18545-18550.
    • (2010) Proc. Natl. Acad. Sci. USA , vol.107 , pp. 18545-18550
    • Bozic, I.1    Antal, T.2    Ohtsuki, H.3    Carter, H.4
  • 24
    • 24744453982 scopus 로고    scopus 로고
    • Somatic mutations of the protein kinase gene family in human lung cancer
    • Davies, H., Hunter, C., Smith, R., Stephens, P. et al., Somatic mutations of the protein kinase gene family in human lung cancer. Cancer Res. 2005, 65, 7591-7595.
    • (2005) Cancer Res. , vol.65 , pp. 7591-7595
    • Davies, H.1    Hunter, C.2    Smith, R.3    Stephens, P.4
  • 25
    • 77950243447 scopus 로고    scopus 로고
    • Drugging the PI3 kinome: from chemical tools to drugs in the clinic
    • Workman, P., Clarke, P. A., Raynaud, F. I., van Montfort, R. L., Drugging the PI3 kinome: from chemical tools to drugs in the clinic. Cancer Res. 2010, 70, 2146-2157.
    • (2010) Cancer Res. , vol.70 , pp. 2146-2157
    • Workman, P.1    Clarke, P.A.2    Raynaud, F.I.3    van Montfort, R.L.4
  • 26
    • 51449095342 scopus 로고    scopus 로고
    • Targeting the PI3K-AKT-mTOR pathway: progress, pitfalls, and promises
    • Yap, T. A., Garrett, M. D., Walton, M. I., Raynaud, F. et al., Targeting the PI3K-AKT-mTOR pathway: progress, pitfalls, and promises. Curr. Opin. Pharmacol. 2008, 8, 393-412.
    • (2008) Curr. Opin. Pharmacol. , vol.8 , pp. 393-412
    • Yap, T.A.1    Garrett, M.D.2    Walton, M.I.3    Raynaud, F.4
  • 27
    • 77953761653 scopus 로고    scopus 로고
    • Correlating phosphatidylinositol 3-kinase inhibitor efficacy with signaling pathway status: in silico and biological evaluations
    • Dan, S., Okamura, M., Seki, M., Yamazaki, K. et al., Correlating phosphatidylinositol 3-kinase inhibitor efficacy with signaling pathway status: in silico and biological evaluations. Cancer Res. 2010, 70, 4982-4994.
    • (2010) Cancer Res. , vol.70 , pp. 4982-4994
    • Dan, S.1    Okamura, M.2    Seki, M.3    Yamazaki, K.4
  • 28
    • 84864803277 scopus 로고    scopus 로고
    • Phosphoproteomic analysis of leukemia cells under basal and drug-treated conditions identifies markers of kinase pathway activation and mechanisms of resistance
    • Alcolea, M. P., Casado, P., Rodriguez-Prados, J. C., Vanhaesebroeck, B., Cutillas, P. R., Phosphoproteomic analysis of leukemia cells under basal and drug-treated conditions identifies markers of kinase pathway activation and mechanisms of resistance. Mol. Cell. Proteomics 2012, 11, 453-466.
    • (2012) Mol. Cell. Proteomics , vol.11 , pp. 453-466
    • Alcolea, M.P.1    Casado, P.2    Rodriguez-Prados, J.C.3    Vanhaesebroeck, B.4    Cutillas, P.R.5
  • 29
    • 84876795631 scopus 로고    scopus 로고
    • Phosphoproteomics data classify hematological cancer cell lines according to tumor type and sensitivity to kinase inhibitors
    • Casado, P., Alcolea, M. P., Iorio, F., Rodriguez-Prados, J. C. et al., Phosphoproteomics data classify hematological cancer cell lines according to tumor type and sensitivity to kinase inhibitors. Genome Biol. 2013, 14, R37.
    • (2013) Genome Biol. , vol.14 , pp. R37
    • Casado, P.1    Alcolea, M.P.2    Iorio, F.3    Rodriguez-Prados, J.C.4
  • 30
    • 84863338519 scopus 로고    scopus 로고
    • PI3K/AKT/mTOR inhibitors in patients with breast and gynecologic malignancies harboring PIK3CA mutations
    • Janku, F., Wheler, J. J., Westin, S. N., Moulder, S. L. et al., PI3K/AKT/mTOR inhibitors in patients with breast and gynecologic malignancies harboring PIK3CA mutations. J. Clin. Oncol. 2012, 30, 777-782.
    • (2012) J. Clin. Oncol. , vol.30 , pp. 777-782
    • Janku, F.1    Wheler, J.J.2    Westin, S.N.3    Moulder, S.L.4
  • 31
    • 84890056861 scopus 로고    scopus 로고
    • What a tangled web we weave: emerging resistance mechanisms to inhibition of the phosphoinositide 3-kinase pathway
    • Klempner, S. J., Myers, A. P., Cantley, L. C., What a tangled web we weave: emerging resistance mechanisms to inhibition of the phosphoinositide 3-kinase pathway. Cancer Discov. 2013, 3, 1345-1354.
    • (2013) Cancer Discov. , vol.3 , pp. 1345-1354
    • Klempner, S.J.1    Myers, A.P.2    Cantley, L.C.3
  • 33
    • 84883624766 scopus 로고    scopus 로고
    • mTORC1 inhibition is required for sensitivity to PI3K p110alpha inhibitors in PIK3CA-mutant breast cancer
    • Elkabets, M., Vora, S., Juric, D., Morse, N. et al., mTORC1 inhibition is required for sensitivity to PI3K p110alpha inhibitors in PIK3CA-mutant breast cancer. Sci. Trans. Med. 2013, 5, 196ra199.
    • (2013) Sci. Trans. Med. , vol.5 , pp. 196ra199
    • Elkabets, M.1    Vora, S.2    Juric, D.3    Morse, N.4
  • 35
    • 78651330430 scopus 로고    scopus 로고
    • COSMIC: mining complete cancer genomes in the Catalogue of Somatic Mutations in Cancer
    • Forbes, S. A., Bindal, N., Bamford, S., Cole, C. et al., COSMIC: mining complete cancer genomes in the Catalogue of Somatic Mutations in Cancer. Nucleic Acids Res. 2011, 39, D945-D950.
    • (2011) Nucleic Acids Res. , vol.39 , pp. D945-D950
    • Forbes, S.A.1    Bindal, N.2    Bamford, S.3    Cole, C.4
  • 36
    • 84859187259 scopus 로고    scopus 로고
    • Systematic identification of genomic markers of drug sensitivity in cancer cells
    • Garnett, M. J., Edelman, E. J., Heidorn, S. J., Greenman, C. D. et al., Systematic identification of genomic markers of drug sensitivity in cancer cells. Nature 2012, 483, 570-575.
    • (2012) Nature , vol.483 , pp. 570-575
    • Garnett, M.J.1    Edelman, E.J.2    Heidorn, S.J.3    Greenman, C.D.4
  • 37
    • 84871679432 scopus 로고    scopus 로고
    • Can we deconstruct cancer, one patient at a time?
    • Blau, C. A., Liakopoulou, E., Can we deconstruct cancer, one patient at a time? Trends Genet. 2013, 29, 6-10.
    • (2013) Trends Genet. , vol.29 , pp. 6-10
    • Blau, C.A.1    Liakopoulou, E.2
  • 38
    • 84863625224 scopus 로고    scopus 로고
    • A CXCL1 paracrine network links cancer chemoresistance and metastasis
    • Acharyya, S., Oskarsson, T., Vanharanta, S., Malladi, S. et al., A CXCL1 paracrine network links cancer chemoresistance and metastasis. Cell 2012, 150, 165-178.
    • (2012) Cell , vol.150 , pp. 165-178
    • Acharyya, S.1    Oskarsson, T.2    Vanharanta, S.3    Malladi, S.4
  • 39
    • 84864285794 scopus 로고    scopus 로고
    • Tumour micro-environment elicits innate resistance to RAF inhibitors through HGF secretion
    • Straussman, R., Morikawa, T., Shee, K., Barzily-Rokni, M. et al., Tumour micro-environment elicits innate resistance to RAF inhibitors through HGF secretion. Nature 2012, 487, 500-504.
    • (2012) Nature , vol.487 , pp. 500-504
    • Straussman, R.1    Morikawa, T.2    Shee, K.3    Barzily-Rokni, M.4
  • 40
    • 67650367598 scopus 로고    scopus 로고
    • Targeting the leukemia microenvironment by CXCR4 inhibition overcomes resistance to kinase inhibitors and chemotherapy in AML
    • Zeng, Z., Shi, Y. X., Samudio, I. J., Wang, R. Y. et al., Targeting the leukemia microenvironment by CXCR4 inhibition overcomes resistance to kinase inhibitors and chemotherapy in AML. Blood 2009, 113, 6215-6224.
    • (2009) Blood , vol.113 , pp. 6215-6224
    • Zeng, Z.1    Shi, Y.X.2    Samudio, I.J.3    Wang, R.Y.4
  • 41
    • 84901928401 scopus 로고    scopus 로고
    • Cross-species proteomics reveals specific modulation of signaling in cancer and stromal cells by phosphoinositide 3-kinase (PI3K) inhibitors
    • Rajeeve, V., Vendrell, I., Wilkes, E., Torbett, N., Cutillas, P. R., Cross-species proteomics reveals specific modulation of signaling in cancer and stromal cells by phosphoinositide 3-kinase (PI3K) inhibitors. Mol. Cell. Proteomics 2014, 13, 1457-1470.
    • (2014) Mol. Cell. Proteomics , vol.13 , pp. 1457-1470
    • Rajeeve, V.1    Vendrell, I.2    Wilkes, E.3    Torbett, N.4    Cutillas, P.R.5
  • 42
    • 84904818154 scopus 로고    scopus 로고
    • The pharmacological point of view of resistance to therapy in tumors
    • Damia, G., Garattini, S., The pharmacological point of view of resistance to therapy in tumors. Cancer Treatment Rev. 2014, 40, 909-916.
    • (2014) Cancer Treatment Rev. , vol.40 , pp. 909-916
    • Damia, G.1    Garattini, S.2
  • 43
    • 84873728334 scopus 로고    scopus 로고
    • Modelling vemurafenib resistance in melanoma reveals a strategy to forestall drug resistance
    • Das Thakur, M., Salangsang, F., Landman, A. S., Sellers, W. R. et al., Modelling vemurafenib resistance in melanoma reveals a strategy to forestall drug resistance. Nature 2013, 494, 251-255.
    • (2013) Nature , vol.494 , pp. 251-255
    • Das Thakur, M.1    Salangsang, F.2    Landman, A.S.3    Sellers, W.R.4
  • 44
    • 84898059073 scopus 로고    scopus 로고
    • An epigenetic mechanism of resistance to targeted therapy in T cell acute lymphoblastic leukemia
    • Knoechel, B., Roderick, J. E., Williamson, K. E., Zhu, J. et al., An epigenetic mechanism of resistance to targeted therapy in T cell acute lymphoblastic leukemia. Nat. Genet. 2014, 46, 364-370.
    • (2014) Nat. Genet. , vol.46 , pp. 364-370
    • Knoechel, B.1    Roderick, J.E.2    Williamson, K.E.3    Zhu, J.4
  • 45
    • 77950809059 scopus 로고    scopus 로고
    • A chromatin-mediated reversible drug-tolerant state in cancer cell subpopulations
    • Sharma, S. V., Lee, D. Y., Li, B., Quinlan, M. P. et al., A chromatin-mediated reversible drug-tolerant state in cancer cell subpopulations. Cell 2010, 141, 69-80.
    • (2010) Cell , vol.141 , pp. 69-80
    • Sharma, S.V.1    Lee, D.Y.2    Li, B.3    Quinlan, M.P.4
  • 46
    • 84922276285 scopus 로고    scopus 로고
    • Feedbacks and adaptive capabilities of the PI3K/Akt/mTOR axis in acute myeloid leukemia revealed by pathway selective inhibition and phosphoproteome analysis
    • Bertacchini, J., Guida, M., Accordi, B., Mediani, L. et al., Feedbacks and adaptive capabilities of the PI3K/Akt/mTOR axis in acute myeloid leukemia revealed by pathway selective inhibition and phosphoproteome analysis. Leukemia 2014, 28, 2197-2205.
    • (2014) Leukemia , vol.28 , pp. 2197-2205
    • Bertacchini, J.1    Guida, M.2    Accordi, B.3    Mediani, L.4
  • 47
    • 77953663228 scopus 로고    scopus 로고
    • Only a subset of Met-activated pathways are required to sustain oncogene addiction
    • Bertotti, A., Burbridge, M. F., Gastaldi, S., Galimi, F. et al., Only a subset of Met-activated pathways are required to sustain oncogene addiction. Sci. Signal. 2009, 2, er11.
    • (2009) Sci. Signal. , vol.2 , pp. er11
    • Bertotti, A.1    Burbridge, M.F.2    Gastaldi, S.3    Galimi, F.4
  • 48
    • 33745159317 scopus 로고    scopus 로고
    • Ultrasensitive and absolute quantification of the phosphoinositide 3-kinase/Akt signal transduction pathway by mass spectrometry
    • Cutillas, P. R., Khwaja, A., Graupera, M., Pearce, W. et al., Ultrasensitive and absolute quantification of the phosphoinositide 3-kinase/Akt signal transduction pathway by mass spectrometry. Proc. Natl. Acad. Sci. USA 2006, 103, 8959-8964.
    • (2006) Proc. Natl. Acad. Sci. USA , vol.103 , pp. 8959-8964
    • Cutillas, P.R.1    Khwaja, A.2    Graupera, M.3    Pearce, W.4
  • 49
    • 34248545259 scopus 로고    scopus 로고
    • Mass spectrometry for enzyme assays and inhibitor screening: an emerging application in pharmaceutical research
    • Greis, K. D., Mass spectrometry for enzyme assays and inhibitor screening: an emerging application in pharmaceutical research. Mass Spectrom. Rev. 2007, 26, 324-339.
    • (2007) Mass Spectrom. Rev. , vol.26 , pp. 324-339
    • Greis, K.D.1
  • 50
    • 33846248354 scopus 로고    scopus 로고
    • Functional interrogation of the kinome using nucleotide acyl phosphates
    • Patricelli, M. P., Szardenings, A. K., Liyanage, M., Nomanbhoy, T. K. et al., Functional interrogation of the kinome using nucleotide acyl phosphates. Biochemistry 2007, 46, 350-358.
    • (2007) Biochemistry , vol.46 , pp. 350-358
    • Patricelli, M.P.1    Szardenings, A.K.2    Liyanage, M.3    Nomanbhoy, T.K.4
  • 52
    • 84877336178 scopus 로고    scopus 로고
    • Mass spectrometry based method to increase throughput for kinome analyses using ATP probes
    • McAllister, F. E., Niepel, M., Haas, W., Huttlin, E. et al., Mass spectrometry based method to increase throughput for kinome analyses using ATP probes. Anal. Chem. 2013, 85, 4666-4674.
    • (2013) Anal. Chem. , vol.85 , pp. 4666-4674
    • McAllister, F.E.1    Niepel, M.2    Haas, W.3    Huttlin, E.4
  • 53
    • 84861897793 scopus 로고    scopus 로고
    • Mass spectrometry-based proteomics and network biology
    • Bensimon, A., Heck, A. J., Aebersold, R., Mass spectrometry-based proteomics and network biology. Ann. Rev. Biochem. 2012, 81, 379-405.
    • (2012) Ann. Rev. Biochem. , vol.81 , pp. 379-405
    • Bensimon, A.1    Heck, A.J.2    Aebersold, R.3
  • 54
    • 84855921201 scopus 로고    scopus 로고
    • Modeling signaling networks using high-throughput phospho-proteomics
    • Terfve, C., Saez-Rodriguez, J., Modeling signaling networks using high-throughput phospho-proteomics. Adv. Exp. Med. Biol. 2012, 736, 19-57.
    • (2012) Adv. Exp. Med. Biol. , vol.736 , pp. 19-57
    • Terfve, C.1    Saez-Rodriguez, J.2
  • 55
    • 84877618069 scopus 로고    scopus 로고
    • Is phosphoproteomics ready for clinical research?
    • Iliuk, A. B., Tao, W. A., Is phosphoproteomics ready for clinical research? Clin. Chim. Acta 2013, 420, 23-27.
    • (2013) Clin. Chim. Acta , vol.420 , pp. 23-27
    • Iliuk, A.B.1    Tao, W.A.2
  • 56
    • 84898602164 scopus 로고    scopus 로고
    • Towards defining biomarkers indicating resistances to targeted therapies
    • Stehle, F., Schulz, K., Seliger, B., Towards defining biomarkers indicating resistances to targeted therapies. Biochim. Et Biophys. Acta 2014, 1844, 909-916.
    • (2014) Biochim. Et Biophys. Acta , vol.1844 , pp. 909-916
    • Stehle, F.1    Schulz, K.2    Seliger, B.3
  • 57
    • 84916932567 scopus 로고    scopus 로고
    • Analytical challenges translating mass spectrometry-based phosphoproteomics from discovery to clinical applications
    • Iliuk, A. B., Arrington, J. V., Tao, W. A., Analytical challenges translating mass spectrometry-based phosphoproteomics from discovery to clinical applications. Electrophoresis 2014, in press.
    • (2014) Electrophoresis
    • Iliuk, A.B.1    Arrington, J.V.2    Tao, W.A.3
  • 58
    • 84907205494 scopus 로고    scopus 로고
    • Single step enrichment by Ti4+-IMAC and label free quantitation enables in-depth monitoring of phosphorylation dynamics with high reproducibility and temporal resolution
    • de Graaf, E. L., Giansanti, P., Altelaar, A. F., Heck, A. J., Single step enrichment by Ti4+-IMAC and label free quantitation enables in-depth monitoring of phosphorylation dynamics with high reproducibility and temporal resolution. Mol. Cell. Proteomics 2014, 13, 2426-2434.
    • (2014) Mol. Cell. Proteomics , vol.13 , pp. 2426-2434
    • de Graaf, E.L.1    Giansanti, P.2    Altelaar, A.F.3    Heck, A.J.4
  • 59
    • 79961193839 scopus 로고    scopus 로고
    • Characterization of a TiO(2) enrichment method for label-free quantitative phosphoproteomics
    • Montoya, A., Beltran, L., Casado, P., Rodriguez-Prados, J. C., Cutillas, P. R., Characterization of a TiO(2) enrichment method for label-free quantitative phosphoproteomics. Methods 2011, 54, 370-378.
    • (2011) Methods , vol.54 , pp. 370-378
    • Montoya, A.1    Beltran, L.2    Casado, P.3    Rodriguez-Prados, J.C.4    Cutillas, P.R.5
  • 60
    • 84875749223 scopus 로고    scopus 로고
    • Automated, reproducible, titania-based phosphopeptide enrichment strategy for label-free quantitative phosphoproteomics
    • Richardson, B. M., Soderblom, E. J., Thompson, J. W., Moseley, M. A., Automated, reproducible, titania-based phosphopeptide enrichment strategy for label-free quantitative phosphoproteomics. J. Biomol. Techn. 2013, 24, 8-16.
    • (2013) J. Biomol. Techn. , vol.24 , pp. 8-16
    • Richardson, B.M.1    Soderblom, E.J.2    Thompson, J.W.3    Moseley, M.A.4
  • 61
    • 84887274297 scopus 로고    scopus 로고
    • Evaluation of quantitative performance of sequential immobilized metal affinity chromatographic enrichment for phosphopeptides
    • Sun, Z., Hamilton, K. L., Reardon, K. F., Evaluation of quantitative performance of sequential immobilized metal affinity chromatographic enrichment for phosphopeptides. Anal. Biochem. 2014, 445, 30-37.
    • (2014) Anal. Biochem. , vol.445 , pp. 30-37
    • Sun, Z.1    Hamilton, K.L.2    Reardon, K.F.3
  • 62
    • 65249161129 scopus 로고    scopus 로고
    • Pathway-based biomarker search by high-throughput proteomics profiling of secretomes
    • Lawlor, K., Nazarian, A., Lacomis, L., Tempst, P., Villanueva, J., Pathway-based biomarker search by high-throughput proteomics profiling of secretomes. J. Proteome Res. 2009, 8, 1489-1503.
    • (2009) J. Proteome Res. , vol.8 , pp. 1489-1503
    • Lawlor, K.1    Nazarian, A.2    Lacomis, L.3    Tempst, P.4    Villanueva, J.5
  • 63
    • 84899524886 scopus 로고    scopus 로고
    • Global phosphoproteomic profiling reveals distinct signatures in B-cell non-Hodgkin lymphomas
    • Rolland, D., Basrur, V., Conlon, K., Wolfe, T. et al., Global phosphoproteomic profiling reveals distinct signatures in B-cell non-Hodgkin lymphomas. Am. J. Pathol. 2014, 184, 1331-1342.
    • (2014) Am. J. Pathol. , vol.184 , pp. 1331-1342
    • Rolland, D.1    Basrur, V.2    Conlon, K.3    Wolfe, T.4
  • 65
    • 84891802882 scopus 로고    scopus 로고
    • Maximizing peptide identification events in proteomic workflows using data-dependent acquisition (DDA)
    • Bateman, N. W., Goulding, S. P., Shulman, N. J., Gadok, A. K. et al., Maximizing peptide identification events in proteomic workflows using data-dependent acquisition (DDA). Mol. Cell. Proteomics 2014, 13, 329-338.
    • (2014) Mol. Cell. Proteomics , vol.13 , pp. 329-338
    • Bateman, N.W.1    Goulding, S.P.2    Shulman, N.J.3    Gadok, A.K.4
  • 66
    • 0036665581 scopus 로고    scopus 로고
    • Quantitative profiling of proteins in complex mixtures using liquid chromatography and mass spectrometry
    • Chelius, D., Bondarenko, P. V., Quantitative profiling of proteins in complex mixtures using liquid chromatography and mass spectrometry. J. Proteome Res. 2002, 1, 317-323.
    • (2002) J. Proteome Res. , vol.1 , pp. 317-323
    • Chelius, D.1    Bondarenko, P.V.2
  • 67
    • 24044467381 scopus 로고    scopus 로고
    • Quantification of gel-separated proteins and their phosphorylation sites by LC-MS using unlabeled internal standards: analysis of phosphoprotein dynamics in a B cell lymphoma cell line
    • Cutillas, P. R., Geering, B., Waterfield, M. D., Vanhaesebroeck, B., Quantification of gel-separated proteins and their phosphorylation sites by LC-MS using unlabeled internal standards: analysis of phosphoprotein dynamics in a B cell lymphoma cell line. Mol. Cell. Proteomics 2005, 4, 1038-1051.
    • (2005) Mol. Cell. Proteomics , vol.4 , pp. 1038-1051
    • Cutillas, P.R.1    Geering, B.2    Waterfield, M.D.3    Vanhaesebroeck, B.4
  • 68
    • 3242688830 scopus 로고    scopus 로고
    • Selective isolation at the femtomole level of phosphopeptides from proteolytic digests using 2D-NanoLC-ESI-MS/MS and titanium oxide precolumns
    • Pinkse, M. W., Uitto, P. M., Hilhorst, M. J., Ooms, B., Heck, A. J., Selective isolation at the femtomole level of phosphopeptides from proteolytic digests using 2D-NanoLC-ESI-MS/MS and titanium oxide precolumns. Anal. Chem. 2004, 76, 3935-3943.
    • (2004) Anal. Chem. , vol.76 , pp. 3935-3943
    • Pinkse, M.W.1    Uitto, P.M.2    Hilhorst, M.J.3    Ooms, B.4    Heck, A.J.5
  • 69
    • 84867041794 scopus 로고    scopus 로고
    • Advances in phosphopeptide enrichment techniques for phosphoproteomics
    • Beltran, L., Cutillas, P. R., Advances in phosphopeptide enrichment techniques for phosphoproteomics. Amino Acids 2012, 43, 1009-1024.
    • (2012) Amino Acids , vol.43 , pp. 1009-1024
    • Beltran, L.1    Cutillas, P.R.2
  • 70
    • 70449392251 scopus 로고    scopus 로고
    • Effect of peptide-to-TiO2 beads ratio on phosphopeptide enrichment selectivity
    • Li, Q. R., Ning, Z. B., Tang, J. S., Nie, S., Zeng, R., Effect of peptide-to-TiO2 beads ratio on phosphopeptide enrichment selectivity. J. Proteome Res. 2009, 8, 5375-5381.
    • (2009) J. Proteome Res. , vol.8 , pp. 5375-5381
    • Li, Q.R.1    Ning, Z.B.2    Tang, J.S.3    Nie, S.4    Zeng, R.5
  • 71
    • 77956304093 scopus 로고    scopus 로고
    • Mass spectrometry in high-throughput proteomics: ready for the big time
    • Nilsson, T., Mann, M., Aebersold, R., Yates, J. R., 3rd et al., Mass spectrometry in high-throughput proteomics: ready for the big time. Nat. Methods 2010, 7, 681-685.
    • (2010) Nat. Methods , vol.7 , pp. 681-685
    • Nilsson, T.1    Mann, M.2    Aebersold, R.3    Yates, J.R.4
  • 73
    • 34848822499 scopus 로고    scopus 로고
    • Quantitative profile of five murine core proteomes using label-free functional proteomics
    • Cutillas, P. R., Vanhaesebroeck, B., Quantitative profile of five murine core proteomes using label-free functional proteomics. Mol. Cell. Proteomics 2007, 6, 1560-1573.
    • (2007) Mol. Cell. Proteomics , vol.6 , pp. 1560-1573
    • Cutillas, P.R.1    Vanhaesebroeck, B.2
  • 74
    • 76649139789 scopus 로고    scopus 로고
    • IDEAL-Q, an automated tool for label-free quantitation analysis using an efficient peptide alignment approach and spectral data validation
    • Tsou, C. C., Tsai, C. F., Tsui, Y. H., Sudhir, P. R. et al., IDEAL-Q, an automated tool for label-free quantitation analysis using an efficient peptide alignment approach and spectral data validation. Mol. Cell. Proteomics 2010, 9, 131-144.
    • (2010) Mol. Cell. Proteomics , vol.9 , pp. 131-144
    • Tsou, C.C.1    Tsai, C.F.2    Tsui, Y.H.3    Sudhir, P.R.4
  • 75
    • 84871259414 scopus 로고    scopus 로고
    • LFQuant: a label-free fast quantitative analysis tool for high-resolution LC-MS/MS proteomics data
    • Zhang, W., Zhang, J., Xu, C., Li, N. et al., LFQuant: a label-free fast quantitative analysis tool for high-resolution LC-MS/MS proteomics data. Proteomics 2012, 12, 3475-3484.
    • (2012) Proteomics , vol.12 , pp. 3475-3484
    • Zhang, W.1    Zhang, J.2    Xu, C.3    Li, N.4
  • 76
    • 78651083717 scopus 로고    scopus 로고
    • A self-validating quantitative mass spectrometry method for assessing the accuracy of high-content phosphoproteomic experiments
    • Casado, P., Cutillas, P. R., A self-validating quantitative mass spectrometry method for assessing the accuracy of high-content phosphoproteomic experiments. Mol. Cell. Proteomics 2011, 10, M110 003079.
    • (2011) Mol. Cell. Proteomics , vol.10
    • Casado, P.1    Cutillas, P.R.2
  • 77
    • 0032555720 scopus 로고    scopus 로고
    • Liquid chromatography-mass spectrometry in forensic and clinical toxicology
    • Maurer, H. H., Liquid chromatography-mass spectrometry in forensic and clinical toxicology. J. Chromatogr. B 1998, 713, 3-25.
    • (1998) J. Chromatogr. B , vol.713 , pp. 3-25
    • Maurer, H.H.1
  • 78
    • 4444353636 scopus 로고    scopus 로고
    • Regulation of protein kinases; controlling activity through activation segment conformation
    • Nolen, B., Taylor, S., Ghosh, G., Regulation of protein kinases; controlling activity through activation segment conformation. Mol. Cell 2004, 15, 661-675.
    • (2004) Mol. Cell , vol.15 , pp. 661-675
    • Nolen, B.1    Taylor, S.2    Ghosh, G.3
  • 79
    • 48149087568 scopus 로고    scopus 로고
    • Non-functional phosphorylations?
    • Lienhard, G. E., Non-functional phosphorylations? Trends Biochem. Sci. 2008, 33, 351-352.
    • (2008) Trends Biochem. Sci. , vol.33 , pp. 351-352
    • Lienhard, G.E.1
  • 80
    • 65349155149 scopus 로고    scopus 로고
    • Weak functional constraints on phosphoproteomes
    • Landry, C. R., Levy, E. D., Michnick, S. W., Weak functional constraints on phosphoproteomes. Trends Genet. 2009, 25, 193-197.
    • (2009) Trends Genet. , vol.25 , pp. 193-197
    • Landry, C.R.1    Levy, E.D.2    Michnick, S.W.3
  • 81
    • 77953563038 scopus 로고    scopus 로고
    • Roles of junk phosphorylation in modulating biomolecular association of phosphorylated proteins?
    • Tan, C. S., Jorgensen, C., Linding, R., Roles of junk phosphorylation in modulating biomolecular association of phosphorylated proteins? Cell Cycle 2010, 9, 1276-1280.
    • (2010) Cell Cycle , vol.9 , pp. 1276-1280
    • Tan, C.S.1    Jorgensen, C.2    Linding, R.3
  • 82
    • 71449120701 scopus 로고    scopus 로고
    • Discrete logic modelling as a means to link protein signalling networks with functional analysis of mammalian signal transduction
    • Saez-Rodriguez, J., Alexopoulos, L. G., Epperlein, J., Samaga, R. et al., Discrete logic modelling as a means to link protein signalling networks with functional analysis of mammalian signal transduction. Mol. Systems Biol. 2009, 5, 331.
    • (2009) Mol. Systems Biol. , vol.5 , pp. 331
    • Saez-Rodriguez, J.1    Alexopoulos, L.G.2    Epperlein, J.3    Samaga, R.4
  • 83
    • 80051692878 scopus 로고    scopus 로고
    • Comparing signaling networks between normal and transformed hepatocytes using discrete logical models
    • Saez-Rodriguez, J., Alexopoulos, L. G., Zhang, M., Morris, M. K. et al., Comparing signaling networks between normal and transformed hepatocytes using discrete logical models. Cancer Res. 2011, 71, 5400-5411.
    • (2011) Cancer Res. , vol.71 , pp. 5400-5411
    • Saez-Rodriguez, J.1    Alexopoulos, L.G.2    Zhang, M.3    Morris, M.K.4
  • 84
    • 34250743173 scopus 로고    scopus 로고
    • Systematic discovery of in vivo phosphorylation networks
    • Linding, R., Jensen, L. J., Ostheimer, G. J., van Vugt, M. A. et al., Systematic discovery of in vivo phosphorylation networks. Cell 2007, 129, 1415-1426.
    • (2007) Cell , vol.129 , pp. 1415-1426
    • Linding, R.1    Jensen, L.J.2    Ostheimer, G.J.3    van Vugt, M.A.4
  • 85
    • 84901788851 scopus 로고    scopus 로고
    • KinomeXplorer: an integrated platform for kinome biology studies
    • Horn, H., Schoof, E. M., Kim, J., Robin, X. et al., KinomeXplorer: an integrated platform for kinome biology studies. Nat. Methods 2014, 11, 603-604.
    • (2014) Nat. Methods , vol.11 , pp. 603-604
    • Horn, H.1    Schoof, E.M.2    Kim, J.3    Robin, X.4
  • 86
    • 84875699641 scopus 로고    scopus 로고
    • Kinase-substrate enrichment analysis provides insights into the heterogeneity of signaling pathway activation in leukemia cells
    • Casado, P., Rodriguez-Prados, J. C., Cosulich, S. C., Guichard, S. et al., Kinase-substrate enrichment analysis provides insights into the heterogeneity of signaling pathway activation in leukemia cells. Sci. Signal. 2013, 6, rs6.
    • (2013) Sci. Signal. , vol.6 , pp. rs6
    • Casado, P.1    Rodriguez-Prados, J.C.2    Cosulich, S.C.3    Guichard, S.4
  • 87
    • 84885722700 scopus 로고    scopus 로고
    • Profiles of Basal and stimulated receptor signaling networks predict drug response in breast cancer lines
    • Niepel, M., Hafner, M., Pace, E. A., Chung, M. et al., Profiles of Basal and stimulated receptor signaling networks predict drug response in breast cancer lines. Sci. Signal. 2013, 6, ra84.
    • (2013) Sci. Signal. , vol.6 , pp. ra84
    • Niepel, M.1    Hafner, M.2    Pace, E.A.3    Chung, M.4
  • 88
    • 84895546634 scopus 로고    scopus 로고
    • Environmental stress affects the activity of metabolic and growth factor signaling networks and induces autophagy markers in MCF7 breast cancer cells
    • Casado, P., Bilanges, B., Rajeeve, V., Vanhaesebroeck, B., Cutillas, P. R., Environmental stress affects the activity of metabolic and growth factor signaling networks and induces autophagy markers in MCF7 breast cancer cells. Mol. Cell. Proteomics 2014, 13, 836-848.
    • (2014) Mol. Cell. Proteomics , vol.13 , pp. 836-848
    • Casado, P.1    Bilanges, B.2    Rajeeve, V.3    Vanhaesebroeck, B.4    Cutillas, P.R.5
  • 89
    • 84904111890 scopus 로고    scopus 로고
    • Ischemia in tumors induces early and sustained phosphorylation changes in stress kinase pathways but does not affect global protein levels
    • Mertins, P., Yang, F., Liu, T., Mani, D. R. et al., Ischemia in tumors induces early and sustained phosphorylation changes in stress kinase pathways but does not affect global protein levels. Mol. Cell. Proteomics 2014, 13, 1690-1704.
    • (2014) Mol. Cell. Proteomics , vol.13 , pp. 1690-1704
    • Mertins, P.1    Yang, F.2    Liu, T.3    Mani, D.R.4
  • 90
    • 84904641861 scopus 로고    scopus 로고
    • Intratumor heterogeneity alters most effective drugs in designed combinations
    • Zhao, B., Hemann, M. T., Lauffenburger, D. A., Intratumor heterogeneity alters most effective drugs in designed combinations. Proc. Natl. Acad. Sci. USA 2014, 111, 10773-10778.
    • (2014) Proc. Natl. Acad. Sci. USA , vol.111 , pp. 10773-10778
    • Zhao, B.1    Hemann, M.T.2    Lauffenburger, D.A.3
  • 91
    • 84887065790 scopus 로고    scopus 로고
    • Dual blockade of the PI3K/AKT/mTOR (AZD8055) and RAS/MEK/ERK (AZD6244) pathways synergistically inhibits rhabdomyosarcoma cell growth in vitro and in vivo
    • Renshaw, J., Taylor, K. R., Bishop, R., Valenti, M. et al., Dual blockade of the PI3K/AKT/mTOR (AZD8055) and RAS/MEK/ERK (AZD6244) pathways synergistically inhibits rhabdomyosarcoma cell growth in vitro and in vivo. Clin. Cancer Res. 2013, 19, 5940-5951.
    • (2013) Clin. Cancer Res. , vol.19 , pp. 5940-5951
    • Renshaw, J.1    Taylor, K.R.2    Bishop, R.3    Valenti, M.4
  • 92
    • 84923320201 scopus 로고    scopus 로고
    • Liquid chromatography-high resolution mass spectrometry (LC-HRMS) determination of stimulants, anorectic drugs and phosphodiesterase 5 inhibitors (PDE5I) in food supplements
    • Strano-Rossi, S., Odoardi, S., Castrignano, E., Serpelloni, G., Chiarotti, M., Liquid chromatography-high resolution mass spectrometry (LC-HRMS) determination of stimulants, anorectic drugs and phosphodiesterase 5 inhibitors (PDE5I) in food supplements. J. Pharm. Biomed. Anal. 2014, doi: 10.1016/j.jpba.2014.06.011
    • (2014) J. Pharm. Biomed. Anal.
    • Strano-Rossi, S.1    Odoardi, S.2    Castrignano, E.3    Serpelloni, G.4    Chiarotti, M.5
  • 93
    • 84876081775 scopus 로고    scopus 로고
    • Use of ultra-high pressure liquid chromatography coupled to high resolution mass spectrometry for fast screening in high throughput doping control
    • Musenga, A., Cowan, D. A., Use of ultra-high pressure liquid chromatography coupled to high resolution mass spectrometry for fast screening in high throughput doping control. J. Chromatogr. A 2013, 1288, 82-95.
    • (2013) J. Chromatogr. A , vol.1288 , pp. 82-95
    • Musenga, A.1    Cowan, D.A.2


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.