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Volumn 145, Issue , 2016, Pages 214-225

Freezing effects on the acute myeloid leukemia cell proteome and phosphoproteome revealed using optimal quantitative workflows

Author keywords

Acute myeloid leukemia; Biomarkers; Phosphoproteomics; Proteomics

Indexed keywords

AMINO ACID; ANION TRANSPORT PROTEIN; CARBONATE DEHYDRATASE I; HEMOGLOBIN GAMMA CHAIN; LIQUID NITROGEN; MITOCHONDRIAL PROTEIN; NUCLEIC ACID BINDING PROTEIN; OXIDOREDUCTASE; PEROXIREDOXIN 2; PHOSPHATASE; PHOSPHATIDYLINOSITOL 3,4,5 TRISPHOSPHATE 5 PHOSPHATASE 1; PHOSPHOPEPTIDE; PROTEOME; REDUCED NICOTINAMIDE ADENINE DINUCLEOTIDE DEHYDROGENASE (UBIQUINONE); THIOREDOXIN; THROMBIN; UNCLASSIFIED DRUG; APOPTOSIS REGULATORY PROTEIN; MITOGEN ACTIVATED PROTEIN KINASE; TUMOR MARKER;

EID: 84990946552     PISSN: 18743919     EISSN: 18767737     Source Type: Journal    
DOI: 10.1016/j.jprot.2016.03.049     Document Type: Article
Times cited : (32)

References (79)
  • 1
    • 70349256226 scopus 로고    scopus 로고
    • The 2008 revision of the World Health Organization (WHO) classification of myeloid neoplasms and acute leukemia: rationale and important changes
    • [1] Vardiman, J.W., Thiele, J., Arber, D.A., Brunning, R.D., Borowitz, M.J., Porwit, A., et al. The 2008 revision of the World Health Organization (WHO) classification of myeloid neoplasms and acute leukemia: rationale and important changes. Blood 114 (2009), 937–951.
    • (2009) Blood , vol.114 , pp. 937-951
    • Vardiman, J.W.1    Thiele, J.2    Arber, D.A.3    Brunning, R.D.4    Borowitz, M.J.5    Porwit, A.6
  • 2
    • 77955914238 scopus 로고    scopus 로고
    • Refinement of cytogenetic classification in acute myeloid leukemia: determination of prognostic significance of rare recurring chromosomal abnormalities among 5876 younger adult patients treated in the United Kingdom Medical Research Council trials
    • [2] Grimwade, D., Hills, R.K., Moorman, A.V., Walker, H., Chatters, S., Goldstone, A.H., et al. Refinement of cytogenetic classification in acute myeloid leukemia: determination of prognostic significance of rare recurring chromosomal abnormalities among 5876 younger adult patients treated in the United Kingdom Medical Research Council trials. Blood 116 (2010), 354–365.
    • (2010) Blood , vol.116 , pp. 354-365
    • Grimwade, D.1    Hills, R.K.2    Moorman, A.V.3    Walker, H.4    Chatters, S.5    Goldstone, A.H.6
  • 3
    • 0032188805 scopus 로고    scopus 로고
    • The importance of diagnostic cytogenetics on outcome in AML: analysis of 1,612 patients entered into the MRC AML 10 trial. The Medical Research Council Adult and Children's Leukaemia Working Parties
    • [3] Grimwade, D., Walker, H., Oliver, F., Wheatley, K., Harrison, C., Harrison, G., et al. The importance of diagnostic cytogenetics on outcome in AML: analysis of 1,612 patients entered into the MRC AML 10 trial. The Medical Research Council Adult and Children's Leukaemia Working Parties. Blood 92 (1998), 2322–2333.
    • (1998) Blood , vol.92 , pp. 2322-2333
    • Grimwade, D.1    Walker, H.2    Oliver, F.3    Wheatley, K.4    Harrison, C.5    Harrison, G.6
  • 4
    • 73949097021 scopus 로고    scopus 로고
    • How I treat acute promyelocytic leukemia
    • [4] Tallman, M.S., Altman, J.K., How I treat acute promyelocytic leukemia. Blood 114 (2009), 5126–5135.
    • (2009) Blood , vol.114 , pp. 5126-5135
    • Tallman, M.S.1    Altman, J.K.2
  • 5
    • 84964697446 scopus 로고    scopus 로고
    • Global cell proteome profiling, phospho-signaling and quantitative proteomics for identification of new biomarkers in acute myeloid leukemia patients
    • [5] Aasebo, E., Forthun, R.B., Berven, F., Selheim, F., Hernandez-Valladares, M., Global cell proteome profiling, phospho-signaling and quantitative proteomics for identification of new biomarkers in acute myeloid leukemia patients. Curr. Pharm. Biotechnol. 17 (2016), 52–70.
    • (2016) Curr. Pharm. Biotechnol. , vol.17 , pp. 52-70
    • Aasebo, E.1    Forthun, R.B.2    Berven, F.3    Selheim, F.4    Hernandez-Valladares, M.5
  • 6
    • 84875699641 scopus 로고    scopus 로고
    • Kinase-substrate enrichment analysis provides insights into the heterogeneity of signaling pathway activation in leukemia cells
    • [6] Casado, P., Rodriguez-Prados, J.C., Cosulich, S.C., Guichard, S., Vanhaesebroeck, B., Joel, S., et al. Kinase-substrate enrichment analysis provides insights into the heterogeneity of signaling pathway activation in leukemia cells. Sci. Signal., 6, 2013, rs6.
    • (2013) Sci. Signal. , vol.6 , pp. rs6
    • Casado, P.1    Rodriguez-Prados, J.C.2    Cosulich, S.C.3    Guichard, S.4    Vanhaesebroeck, B.5    Joel, S.6
  • 7
    • 3242683662 scopus 로고    scopus 로고
    • Single cell profiling of potentiated phospho-protein networks in cancer cells
    • [7] Irish, J.M., Hovland, R., Krutzik, P.O., Perez, O.D., Bruserud, O., Gjertsen, B.T., et al. Single cell profiling of potentiated phospho-protein networks in cancer cells. Cell 118 (2004), 217–228.
    • (2004) Cell , vol.118 , pp. 217-228
    • Irish, J.M.1    Hovland, R.2    Krutzik, P.O.3    Perez, O.D.4    Bruserud, O.5    Gjertsen, B.T.6
  • 8
    • 84908331600 scopus 로고    scopus 로고
    • Cell-surface receptors transactivation mediated by g protein-coupled receptors
    • [8] Cattaneo, F., Guerra, G., Parisi, M., De Marinis, M., Tafuri, D., Cinelli, M., et al. Cell-surface receptors transactivation mediated by g protein-coupled receptors. Int. J. Mol. Sci. 15 (2014), 19700–19728.
    • (2014) Int. J. Mol. Sci. , vol.15 , pp. 19700-19728
    • Cattaneo, F.1    Guerra, G.2    Parisi, M.3    De Marinis, M.4    Tafuri, D.5    Cinelli, M.6
  • 9
    • 84920774454 scopus 로고    scopus 로고
    • STAT3 as a possible therapeutic target in human malignancies: lessons from acute myeloid leukemia
    • [9] Bruserud, O., Nepstad, I., Hauge, M., Hatfield, K.J., Reikvam, H., STAT3 as a possible therapeutic target in human malignancies: lessons from acute myeloid leukemia. Expert. Rev. Hematol. 8 (2015), 29–41.
    • (2015) Expert. Rev. Hematol. , vol.8 , pp. 29-41
    • Bruserud, O.1    Nepstad, I.2    Hauge, M.3    Hatfield, K.J.4    Reikvam, H.5
  • 10
    • 84962247464 scopus 로고    scopus 로고
    • Functional crosstalk between WNT signaling and tyrosine kinase signaling in cancer
    • [10] Anastas, J.N., Functional crosstalk between WNT signaling and tyrosine kinase signaling in cancer. Semin. Oncol. 42 (2015), 820–831.
    • (2015) Semin. Oncol. , vol.42 , pp. 820-831
    • Anastas, J.N.1
  • 11
    • 84895800838 scopus 로고    scopus 로고
    • Global phosphoproteome analysis of human bone marrow reveals predictive phosphorylation markers for the treatment of acute myeloid leukemia with quizartinib
    • [11] Schaab, C., Oppermann, F.S., Klammer, M., Pfeifer, H., Tebbe, A., Oellerich, T., et al. Global phosphoproteome analysis of human bone marrow reveals predictive phosphorylation markers for the treatment of acute myeloid leukemia with quizartinib. Leukemia 28 (2014), 716–719.
    • (2014) Leukemia , vol.28 , pp. 716-719
    • Schaab, C.1    Oppermann, F.S.2    Klammer, M.3    Pfeifer, H.4    Tebbe, A.5    Oellerich, T.6
  • 12
    • 84925379439 scopus 로고    scopus 로고
    • FLT3-ITD and TLR9 use Bruton tyrosine kinase to activate distinct transcriptional programs mediating AML cell survival and proliferation
    • [12] Oellerich, T., Mohr, S., Corso, J., Beck, J., Dobele, C., Braun, H., et al. FLT3-ITD and TLR9 use Bruton tyrosine kinase to activate distinct transcriptional programs mediating AML cell survival and proliferation. Blood 125 (2015), 1936–1947.
    • (2015) Blood , vol.125 , pp. 1936-1947
    • Oellerich, T.1    Mohr, S.2    Corso, J.3    Beck, J.4    Dobele, C.5    Braun, H.6
  • 13
    • 0347123341 scopus 로고    scopus 로고
    • Differential expression of histone post-translational modifications in acute myeloid and chronic lymphocytic leukemia determined by high-pressure liquid chromatography and mass spectrometry
    • [13] Zhang, L., Freitas, M.A., Wickham, J., Parthun, M.R., Klisovic, M.I., Marcucci, G., et al. Differential expression of histone post-translational modifications in acute myeloid and chronic lymphocytic leukemia determined by high-pressure liquid chromatography and mass spectrometry. J. Am. Soc. Mass Spectrom. 15 (2004), 77–86.
    • (2004) J. Am. Soc. Mass Spectrom. , vol.15 , pp. 77-86
    • Zhang, L.1    Freitas, M.A.2    Wickham, J.3    Parthun, M.R.4    Klisovic, M.I.5    Marcucci, G.6
  • 14
    • 84922391197 scopus 로고    scopus 로고
    • Fast, efficient, and quality-controlled phosphopeptide enrichment from minute sample amounts using titanium dioxide
    • [14] Dickhut, C., Radau, S., Zahedi, R.P., Fast, efficient, and quality-controlled phosphopeptide enrichment from minute sample amounts using titanium dioxide. Methods Mol. Biol. 1156 (2014), 417–430.
    • (2014) Methods Mol. Biol. , vol.1156 , pp. 417-430
    • Dickhut, C.1    Radau, S.2    Zahedi, R.P.3
  • 15
    • 34248640261 scopus 로고    scopus 로고
    • Highly selective enrichment of phosphorylated peptides using titanium dioxide
    • [15] Thingholm, T.E., Jorgensen, T.J., Jensen, O.N., Larsen, M.R., Highly selective enrichment of phosphorylated peptides using titanium dioxide. Nat. Protoc. 1 (2006), 1929–1935.
    • (2006) Nat. Protoc. , vol.1 , pp. 1929-1935
    • Thingholm, T.E.1    Jorgensen, T.J.2    Jensen, O.N.3    Larsen, M.R.4
  • 16
    • 84947976150 scopus 로고    scopus 로고
    • The use of titanium dioxide for selective enrichment of phosphorylated peptides
    • [16] Thingholm, T.E., Larsen, M.R., The use of titanium dioxide for selective enrichment of phosphorylated peptides. Methods Mol. Biol. 1355 (2016), 135–146.
    • (2016) Methods Mol. Biol. , vol.1355 , pp. 135-146
    • Thingholm, T.E.1    Larsen, M.R.2
  • 17
    • 84947996475 scopus 로고    scopus 로고
    • Phosphopeptide enrichment by immobilized metal affinity chromatography
    • [17] Thingholm, T.E., Larsen, M.R., Phosphopeptide enrichment by immobilized metal affinity chromatography. Methods Mol. Biol. 1355 (2016), 123–133.
    • (2016) Methods Mol. Biol. , vol.1355 , pp. 123-133
    • Thingholm, T.E.1    Larsen, M.R.2
  • 18
    • 42649139982 scopus 로고    scopus 로고
    • SIMAC (sequential elution from IMAC), a phosphoproteomics strategy for the rapid separation of monophosphorylated from multiply phosphorylated peptides
    • [18] Thingholm, T.E., Jensen, O.N., Robinson, P.J., Larsen, M.R., SIMAC (sequential elution from IMAC), a phosphoproteomics strategy for the rapid separation of monophosphorylated from multiply phosphorylated peptides. Mol. Cell. Proteomics 7 (2008), 661–671.
    • (2008) Mol. Cell. Proteomics , vol.7 , pp. 661-671
    • Thingholm, T.E.1    Jensen, O.N.2    Robinson, P.J.3    Larsen, M.R.4
  • 19
    • 84947998541 scopus 로고    scopus 로고
    • Sequential elution from IMAC (SIMAC): an efficient method for enrichment and separation of mono- and multi-phosphorylated peptides
    • [19] Thingholm, T.E., Larsen, M.R., Sequential elution from IMAC (SIMAC): an efficient method for enrichment and separation of mono- and multi-phosphorylated peptides. Methods Mol. Biol. 1355 (2016), 147–160.
    • (2016) Methods Mol. Biol. , vol.1355 , pp. 147-160
    • Thingholm, T.E.1    Larsen, M.R.2
  • 20
    • 0035176551 scopus 로고    scopus 로고
    • New strategies in the treatment of acute myelogenous leukemia (AML): in vitro culture of aml cells—the present use in experimental studies and the possible importance for future therapeutic approaches
    • [20] Bruserud, O., Gjertsen, B.T., Foss, B., Huang, T.S., New strategies in the treatment of acute myelogenous leukemia (AML): in vitro culture of aml cells—the present use in experimental studies and the possible importance for future therapeutic approaches. Stem Cells 19 (2001), 1–11.
    • (2001) Stem Cells , vol.19 , pp. 1-11
    • Bruserud, O.1    Gjertsen, B.T.2    Foss, B.3    Huang, T.S.4
  • 21
    • 0038712179 scopus 로고    scopus 로고
    • Flt3-mediated signaling in human acute myelogenous leukemia (AML) blasts: a functional characterization of Flt3-ligand effects in AML cell populations with and without genetic Flt3 abnormalities
    • [21] Bruserud, O., Hovland, R., Wergeland, L., Huang, T.S., Gjertsen, B.T., Flt3-mediated signaling in human acute myelogenous leukemia (AML) blasts: a functional characterization of Flt3-ligand effects in AML cell populations with and without genetic Flt3 abnormalities. Haematologica 88 (2003), 416–428.
    • (2003) Haematologica , vol.88 , pp. 416-428
    • Bruserud, O.1    Hovland, R.2    Wergeland, L.3    Huang, T.S.4    Gjertsen, B.T.5
  • 22
    • 39149089296 scopus 로고    scopus 로고
    • Release of angiopoietin-1 by primary human acute myelogenous leukemia cells is associated with mutations of nucleophosmin, increased by bone marrow stromal cells and possibly antagonized by high systemic angiopoietin-2 levels
    • [22] Hatfield, K.J., Hovland, R., Oyan, A.M., Kalland, K.H., Ryningen, A., Gjertsen, B.T., et al. Release of angiopoietin-1 by primary human acute myelogenous leukemia cells is associated with mutations of nucleophosmin, increased by bone marrow stromal cells and possibly antagonized by high systemic angiopoietin-2 levels. Leukemia 22 (2008), 287–293.
    • (2008) Leukemia , vol.22 , pp. 287-293
    • Hatfield, K.J.1    Hovland, R.2    Oyan, A.M.3    Kalland, K.H.4    Ryningen, A.5    Gjertsen, B.T.6
  • 23
    • 84908619731 scopus 로고    scopus 로고
    • Performance of super-SILAC based quantitative proteomics for comparison of different acute myeloid leukemia (AML) cell lines
    • [23] Aasebo, E., Vaudel, M., Mjaavatten, O., Gausdal, G., Van der Burgh, A., Gjertsen, B.T., et al. Performance of super-SILAC based quantitative proteomics for comparison of different acute myeloid leukemia (AML) cell lines. Proteomics 14 (2014), 1971–1976.
    • (2014) Proteomics , vol.14 , pp. 1971-1976
    • Aasebo, E.1    Vaudel, M.2    Mjaavatten, O.3    Gausdal, G.4    Van der Burgh, A.5    Gjertsen, B.T.6
  • 24
    • 77952226764 scopus 로고    scopus 로고
    • Super-SILAC mix for quantitative proteomics of human tumor tissue
    • [24] Geiger, T., Cox, J., Ostasiewicz, P., Wisniewski, J.R., Mann, M., Super-SILAC mix for quantitative proteomics of human tumor tissue. Nat. Methods 7 (2010), 383–385.
    • (2010) Nat. Methods , vol.7 , pp. 383-385
    • Geiger, T.1    Cox, J.2    Ostasiewicz, P.3    Wisniewski, J.R.4    Mann, M.5
  • 25
    • 84895538371 scopus 로고    scopus 로고
    • Minimal, encapsulated proteomic-sample processing applied to copy-number estimation in eukaryotic cells
    • [25] Kulak, N.A., Pichler, G., Paron, I., Nagaraj, N., Mann, M., Minimal, encapsulated proteomic-sample processing applied to copy-number estimation in eukaryotic cells. Nat. Methods 11 (2014), 319–324.
    • (2014) Nat. Methods , vol.11 , pp. 319-324
    • Kulak, N.A.1    Pichler, G.2    Paron, I.3    Nagaraj, N.4    Mann, M.5
  • 26
    • 84915774615 scopus 로고    scopus 로고
    • Rapid and deep proteomes by faster sequencing on a benchtop quadrupole ultra-high-field Orbitrap mass spectrometer
    • [26] Kelstrup, C.D., Jersie-Christensen, R.R., Batth, T.S., Arrey, T.N., Kuehn, A., Kellmann, M., et al. Rapid and deep proteomes by faster sequencing on a benchtop quadrupole ultra-high-field Orbitrap mass spectrometer. J. Proteome Res. 13 (2014), 6187–6195.
    • (2014) J. Proteome Res. , vol.13 , pp. 6187-6195
    • Kelstrup, C.D.1    Jersie-Christensen, R.R.2    Batth, T.S.3    Arrey, T.N.4    Kuehn, A.5    Kellmann, M.6
  • 27
    • 67349266694 scopus 로고    scopus 로고
    • Universal sample preparation method for proteome analysis
    • [27] Wisniewski, J.R., Zougman, A., Nagaraj, N., Mann, M., Universal sample preparation method for proteome analysis. Nat. Methods 6 (2009), 359–362.
    • (2009) Nat. Methods , vol.6 , pp. 359-362
    • Wisniewski, J.R.1    Zougman, A.2    Nagaraj, N.3    Mann, M.4
  • 28
    • 84905443685 scopus 로고    scopus 로고
    • Multi-enzyme digestion FASP and the ‘Total Protein Approach’-based absolute quantification of the Escherichia coli proteome
    • [28] Wisniewski, J.R., Rakus, D., Multi-enzyme digestion FASP and the ‘Total Protein Approach’-based absolute quantification of the Escherichia coli proteome. J. Proteome 109 (2014), 322–331.
    • (2014) J. Proteome , vol.109 , pp. 322-331
    • Wisniewski, J.R.1    Rakus, D.2
  • 29
    • 57449099865 scopus 로고    scopus 로고
    • MaxQuant enables high peptide identification rates, individualized p.p.b.-range mass accuracies and proteome-wide protein quantification
    • [29] Cox, J., Mann, M., MaxQuant enables high peptide identification rates, individualized p.p.b.-range mass accuracies and proteome-wide protein quantification. Nat. Biotechnol. 26 (2008), 1367–1372.
    • (2008) Nat. Biotechnol. , vol.26 , pp. 1367-1372
    • Cox, J.1    Mann, M.2
  • 30
    • 67649400942 scopus 로고    scopus 로고
    • A practical guide to the MaxQuant computational platform for SILAC-based quantitative proteomics
    • [30] Cox, J., Matic, I., Hilger, M., Nagaraj, N., Selbach, M., Olsen, J.V., et al. A practical guide to the MaxQuant computational platform for SILAC-based quantitative proteomics. Nat. Protoc. 4 (2009), 698–705.
    • (2009) Nat. Protoc. , vol.4 , pp. 698-705
    • Cox, J.1    Matic, I.2    Hilger, M.3    Nagaraj, N.4    Selbach, M.5    Olsen, J.V.6
  • 32
    • 33750456519 scopus 로고    scopus 로고
    • Global, in vivo, and site-specific phosphorylation dynamics in signaling networks
    • [32] Olsen, J.V., Blagoev, B., Gnad, F., Macek, B., Kumar, C., Mortensen, P., et al. Global, in vivo, and site-specific phosphorylation dynamics in signaling networks. Cell 127 (2006), 635–648.
    • (2006) Cell , vol.127 , pp. 635-648
    • Olsen, J.V.1    Blagoev, B.2    Gnad, F.3    Macek, B.4    Kumar, C.5    Mortensen, P.6
  • 33
    • 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
    • [33] 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 13 (2014), 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
  • 34
    • 84891796097 scopus 로고    scopus 로고
    • ProteomeXchange provides globally coordinated proteomics data submission and dissemination
    • [34] Vizcaino, J.A., Deutsch, E.W., Wang, R., Csordas, A., Reisinger, F., Rios, D., et al. ProteomeXchange provides globally coordinated proteomics data submission and dissemination. Nat. Biotechnol. 32 (2014), 223–226.
    • (2014) Nat. Biotechnol. , vol.32 , pp. 223-226
    • Vizcaino, J.A.1    Deutsch, E.W.2    Wang, R.3    Csordas, A.4    Reisinger, F.5    Rios, D.6
  • 37
    • 56449107474 scopus 로고    scopus 로고
    • BioVenn — a web application for the comparison and visualization of biological lists using area-proportional Venn diagrams
    • [37] Hulsen, T., de Vlieg, J., Alkema, W., BioVenn — a web application for the comparison and visualization of biological lists using area-proportional Venn diagrams. BMC Genomics, 9, 2008, 488.
    • (2008) BMC Genomics , vol.9 , pp. 488
    • Hulsen, T.1    de Vlieg, J.2    Alkema, W.3
  • 38
  • 39
    • 84938748671 scopus 로고    scopus 로고
    • FunRich: an open access standalone functional enrichment and interaction network analysis tool
    • [39] Pathan, M., Keerthikumar, S., Ang, C.S., Gangoda, L., Quek, C.Y., Williamson, N.A., et al. FunRich: an open access standalone functional enrichment and interaction network analysis tool. Proteomics 15 (2015), 2597–2601.
    • (2015) Proteomics , vol.15 , pp. 2597-2601
    • Pathan, M.1    Keerthikumar, S.2    Ang, C.S.3    Gangoda, L.4    Quek, C.Y.5    Williamson, N.A.6
  • 40
    • 84976875034 scopus 로고    scopus 로고
    • PANTHER version 10: expanded protein families and functions, and analysis tools
    • [40] Mi, H., Poudel, S., Muruganujan, A., Casagrande, J.T., Thomas, P.D., PANTHER version 10: expanded protein families and functions, and analysis tools. Nucleic Acids Res. 44 (2016), D336–D342.
    • (2016) Nucleic Acids Res. , vol.44 , pp. D336-D342
    • Mi, H.1    Poudel, S.2    Muruganujan, A.3    Casagrande, J.T.4    Thomas, P.D.5
  • 45
    • 84947968065 scopus 로고    scopus 로고
    • Systems analysis for interpretation of phosphoproteomics data
    • [45] Munk, S., Refsgaard, J.C., Olsen, J.V., Systems analysis for interpretation of phosphoproteomics data. Methods Mol. Biol. 1355 (2016), 341–360.
    • (2016) Methods Mol. Biol. , vol.1355 , pp. 341-360
    • Munk, S.1    Refsgaard, J.C.2    Olsen, J.V.3
  • 47
    • 84901788851 scopus 로고    scopus 로고
    • KinomeXplorer: an integrated platform for kinome biology studies
    • [47] Horn, H., Schoof, E.M., Kim, J., Robin, X., Miller, M.L., Diella, F., et al. KinomeXplorer: an integrated platform for kinome biology studies. Nat. Methods 11 (2014), 603–604.
    • (2014) Nat. Methods , vol.11 , pp. 603-604
    • Horn, H.1    Schoof, E.M.2    Kim, J.3    Robin, X.4    Miller, M.L.5    Diella, F.6
  • 48
    • 84885651630 scopus 로고    scopus 로고
    • Getting intimate with trypsin, the leading protease in proteomics
    • [48] Vandermarliere, E., Mueller, M., Martens, L., Getting intimate with trypsin, the leading protease in proteomics. Mass Spectrom. Rev. 32 (2013), 453–465.
    • (2013) Mass Spectrom. Rev. , vol.32 , pp. 453-465
    • Vandermarliere, E.1    Mueller, M.2    Martens, L.3
  • 49
    • 24944576051 scopus 로고    scopus 로고
    • Identification of insulin receptor substrate 1 serine/threonine phosphorylation sites using mass spectrometry analysis: regulatory role of serine 1223
    • [49] Luo, M., Reyna, S., Wang, L., Yi, Z., Carroll, C., Dong, L.Q., et al. Identification of insulin receptor substrate 1 serine/threonine phosphorylation sites using mass spectrometry analysis: regulatory role of serine 1223. Endocrinology 146 (2005), 4410–4416.
    • (2005) Endocrinology , vol.146 , pp. 4410-4416
    • Luo, M.1    Reyna, S.2    Wang, L.3    Yi, Z.4    Carroll, C.5    Dong, L.Q.6
  • 50
    • 29844456243 scopus 로고    scopus 로고
    • Therapeutic and diagnostic applications of minor histocompatibility antigen HA-1 and HA-2 disparities in allogeneic hematopoietic stem cell transplantation: a survey of different populations
    • [50] Di Terlizzi, S., Zino, E., Mazzi, B., Magnani, C., Tresoldi, C., Perna, S.K., et al. Therapeutic and diagnostic applications of minor histocompatibility antigen HA-1 and HA-2 disparities in allogeneic hematopoietic stem cell transplantation: a survey of different populations. Biol. Blood Marrow Transplant. 12 (2006), 95–101.
    • (2006) Biol. Blood Marrow Transplant. , vol.12 , pp. 95-101
    • Di Terlizzi, S.1    Zino, E.2    Mazzi, B.3    Magnani, C.4    Tresoldi, C.5    Perna, S.K.6
  • 51
    • 84861218728 scopus 로고    scopus 로고
    • Alterations of deadenylase expression in acute leukemias: evidence for poly(a)-specific ribonuclease as a potential biomarker
    • [51] Maragozidis, P., Karangeli, M., Labrou, M., Dimoulou, G., Papaspyrou, K., Salataj, E., et al. Alterations of deadenylase expression in acute leukemias: evidence for poly(a)-specific ribonuclease as a potential biomarker. Acta Haematol. 128 (2012), 39–46.
    • (2012) Acta Haematol. , vol.128 , pp. 39-46
    • Maragozidis, P.1    Karangeli, M.2    Labrou, M.3    Dimoulou, G.4    Papaspyrou, K.5    Salataj, E.6
  • 52
    • 84944691382 scopus 로고    scopus 로고
    • High expression of myocyte enhancer factor 2C (MEF2C) is associated with adverse-risk features and poor outcome in pediatric acute myeloid leukemia: a report from the Children's Oncology Group
    • [52] Laszlo, G.S., Alonzo, T.A., Gudgeon, C.J., Harrington, K.H., Kentsis, A., Gerbing, R.B., et al. High expression of myocyte enhancer factor 2C (MEF2C) is associated with adverse-risk features and poor outcome in pediatric acute myeloid leukemia: a report from the Children's Oncology Group. J. Hematol. Oncol., 8, 2015, 115.
    • (2015) J. Hematol. Oncol. , vol.8 , pp. 115
    • Laszlo, G.S.1    Alonzo, T.A.2    Gudgeon, C.J.3    Harrington, K.H.4    Kentsis, A.5    Gerbing, R.B.6
  • 53
    • 84897018519 scopus 로고    scopus 로고
    • Myocyte enhancer factor 2C in hematopoiesis and leukemia
    • [53] Cante-Barrett, K., Pieters, R., Meijerink, J.P., Myocyte enhancer factor 2C in hematopoiesis and leukemia. Oncogene 33 (2014), 403–410.
    • (2014) Oncogene , vol.33 , pp. 403-410
    • Cante-Barrett, K.1    Pieters, R.2    Meijerink, J.P.3
  • 54
    • 84901507159 scopus 로고    scopus 로고
    • Molecular mechanisms of nutlin-3 involve acetylation of p53, histones and heat shock proteins in acute myeloid leukemia
    • [54] Haaland, I., Opsahl, J.A., Berven, F.S., Reikvam, H., Fredly, H.K., Haugse, R., et al. Molecular mechanisms of nutlin-3 involve acetylation of p53, histones and heat shock proteins in acute myeloid leukemia. Mol. Cancer, 13, 2014, 116.
    • (2014) Mol. Cancer , vol.13 , pp. 116
    • Haaland, I.1    Opsahl, J.A.2    Berven, F.S.3    Reikvam, H.4    Fredly, H.K.5    Haugse, R.6
  • 55
    • 84874718501 scopus 로고    scopus 로고
    • Hsp27: a novel therapeutic target for pediatric M4/M5 acute myeloid leukemia
    • [55] Yang, L., Cao, L., Yang, M., Tang, D., Kang, R., Min, X., et al. Hsp27: a novel therapeutic target for pediatric M4/M5 acute myeloid leukemia. Oncol. Rep. 29 (2013), 1459–1466.
    • (2013) Oncol. Rep. , vol.29 , pp. 1459-1466
    • Yang, L.1    Cao, L.2    Yang, M.3    Tang, D.4    Kang, R.5    Min, X.6
  • 56
    • 84920687465 scopus 로고    scopus 로고
    • Dominant-negative Ikaros cooperates with BCR-ABL1 to induce human acute myeloid leukemia in xenografts
    • [56] Theocharides, A.P., Dobson, S.M., Laurenti, E., Notta, F., Voisin, V., Cheng, P.Y., et al. Dominant-negative Ikaros cooperates with BCR-ABL1 to induce human acute myeloid leukemia in xenografts. Leukemia 29 (2015), 177–187.
    • (2015) Leukemia , vol.29 , pp. 177-187
    • Theocharides, A.P.1    Dobson, S.M.2    Laurenti, E.3    Notta, F.4    Voisin, V.5    Cheng, P.Y.6
  • 57
    • 2442517390 scopus 로고    scopus 로고
    • DNA microarray screening of differential gene expression in bone marrow samples from AML, non-AML patients and AML cell lines
    • [57] Court, E.L., Smith, M.A., Avent, N.D., Hancock, J.T., Morgan, L.M., Gray, A.G., et al. DNA microarray screening of differential gene expression in bone marrow samples from AML, non-AML patients and AML cell lines. Leuk. Res. 28 (2004), 743–753.
    • (2004) Leuk. Res. , vol.28 , pp. 743-753
    • Court, E.L.1    Smith, M.A.2    Avent, N.D.3    Hancock, J.T.4    Morgan, L.M.5    Gray, A.G.6
  • 58
    • 84902590222 scopus 로고    scopus 로고
    • miR-181b increases drug sensitivity in acute myeloid leukemia via targeting HMGB1 and Mcl-1
    • [58] Lu, F., Zhang, J., Ji, M., Li, P., Du, Y., Wang, H., et al. miR-181b increases drug sensitivity in acute myeloid leukemia via targeting HMGB1 and Mcl-1. Int. J. Oncol. 45 (2014), 383–392.
    • (2014) Int. J. Oncol. , vol.45 , pp. 383-392
    • Lu, F.1    Zhang, J.2    Ji, M.3    Li, P.4    Du, Y.5    Wang, H.6
  • 59
    • 84868327851 scopus 로고    scopus 로고
    • Large-scale quantitative assessment of different in-solution protein digestion protocols reveals superior cleavage efficiency of tandem Lys-C/trypsin proteolysis over trypsin digestion
    • [59] Glatter, T., Ludwig, C., Ahrne, E., Aebersold, R., Heck, A.J., Schmidt, A., Large-scale quantitative assessment of different in-solution protein digestion protocols reveals superior cleavage efficiency of tandem Lys-C/trypsin proteolysis over trypsin digestion. J. Proteome Res. 11 (2012), 5145–5156.
    • (2012) J. Proteome Res. , vol.11 , pp. 5145-5156
    • Glatter, T.1    Ludwig, C.2    Ahrne, E.3    Aebersold, R.4    Heck, A.J.5    Schmidt, A.6
  • 60
    • 84866294361 scopus 로고    scopus 로고
    • Prediction of missed proteolytic cleavages for the selection of surrogate peptides for quantitative proteomics
    • [60] Lawless, C., Hubbard, S.J., Prediction of missed proteolytic cleavages for the selection of surrogate peptides for quantitative proteomics. OMICS 16 (2012), 449–456.
    • (2012) OMICS , vol.16 , pp. 449-456
    • Lawless, C.1    Hubbard, S.J.2
  • 61
    • 84946865957 scopus 로고    scopus 로고
    • Comparison of different sample preparation protocols reveals lysis buffer-specific extraction biases in gram-negative bacteria and human cells
    • [61] Glatter, T., Ahrne, E., Schmidt, A., Comparison of different sample preparation protocols reveals lysis buffer-specific extraction biases in gram-negative bacteria and human cells. J. Proteome Res. 14 (2015), 4472–4485.
    • (2015) J. Proteome Res. , vol.14 , pp. 4472-4485
    • Glatter, T.1    Ahrne, E.2    Schmidt, A.3
  • 62
    • 84858725817 scopus 로고    scopus 로고
    • Consecutive proteolytic digestion in an enzyme reactor increases depth of proteomic and phosphoproteomic analysis
    • [62] Wisniewski, J.R., Mann, M., Consecutive proteolytic digestion in an enzyme reactor increases depth of proteomic and phosphoproteomic analysis. Anal. Chem. 84 (2012), 2631–2637.
    • (2012) Anal. Chem. , vol.84 , pp. 2631-2637
    • Wisniewski, J.R.1    Mann, M.2
  • 63
    • 84867036962 scopus 로고    scopus 로고
    • Enrichment techniques employed in phosphoproteomics
    • [63] Fila, J., Honys, D., Enrichment techniques employed in phosphoproteomics. Amino Acids 43 (2012), 1025–1047.
    • (2012) Amino Acids , vol.43 , pp. 1025-1047
    • Fila, J.1    Honys, D.2
  • 64
    • 33750003401 scopus 로고    scopus 로고
    • Stress-induced in vitro apoptosis of native human acute myelogenous leukemia (AML) cells shows a wide variation between patients and is associated with low BCL-2:Bax ratio and low levels of heat shock protein 70 and 90
    • [64] Ryningen, A., Ersvaer, E., Oyan, A.M., Kalland, K.H., Vintermyr, O.K., Gjertsen, B.T., et al. Stress-induced in vitro apoptosis of native human acute myelogenous leukemia (AML) cells shows a wide variation between patients and is associated with low BCL-2:Bax ratio and low levels of heat shock protein 70 and 90. Leuk. Res. 30 (2006), 1531–1540.
    • (2006) Leuk. Res. , vol.30 , pp. 1531-1540
    • Ryningen, A.1    Ersvaer, E.2    Oyan, A.M.3    Kalland, K.H.4    Vintermyr, O.K.5    Gjertsen, B.T.6
  • 65
    • 0142245604 scopus 로고    scopus 로고
    • Supplementation of conventional freezing medium with a combination of catalase and trehalose results in better protection of surface molecules and functionality of hematopoietic cells
    • [65] Sasnoor, L.M., Kale, V.P., Limaye, L.S., Supplementation of conventional freezing medium with a combination of catalase and trehalose results in better protection of surface molecules and functionality of hematopoietic cells. J. Hematother. Stem Cell Res. 12 (2003), 553–564.
    • (2003) J. Hematother. Stem Cell Res. , vol.12 , pp. 553-564
    • Sasnoor, L.M.1    Kale, V.P.2    Limaye, L.S.3
  • 67
    • 84959557421 scopus 로고    scopus 로고
    • Differential proteome association study of freeze-thaw damage in ram sperm
    • [67] He, Y., Wang, K., Zhao, X., Zhang, Y., Ma, Y., Hu, J., Differential proteome association study of freeze-thaw damage in ram sperm. Cryobiology 72 (2016), 60–68.
    • (2016) Cryobiology , vol.72 , pp. 60-68
    • He, Y.1    Wang, K.2    Zhao, X.3    Zhang, Y.4    Ma, Y.5    Hu, J.6
  • 68
    • 33846479525 scopus 로고    scopus 로고
    • Kinetics of occurrence of some features of apoptosis during the cryopreservation process of bovine spermatozoa
    • [68] Martin, G., Cagnon, N., Sabido, O., Sion, B., Grizard, G., Durand, P., et al. Kinetics of occurrence of some features of apoptosis during the cryopreservation process of bovine spermatozoa. Hum. Reprod. 22 (2007), 380–388.
    • (2007) Hum. Reprod. , vol.22 , pp. 380-388
    • Martin, G.1    Cagnon, N.2    Sabido, O.3    Sion, B.4    Grizard, G.5    Durand, P.6
  • 69
    • 84938876880 scopus 로고    scopus 로고
    • Enhancer of rudimentary homolog affects the replication stress response through regulation of RNA processing
    • [69] Kavanaugh, G., Zhao, R., Guo, Y., Mohni, K.N., Glick, G., Lacy, M.E., et al. Enhancer of rudimentary homolog affects the replication stress response through regulation of RNA processing. Mol. Cell. Biol. 35 (2015), 2979–2990.
    • (2015) Mol. Cell. Biol. , vol.35 , pp. 2979-2990
    • Kavanaugh, G.1    Zhao, R.2    Guo, Y.3    Mohni, K.N.4    Glick, G.5    Lacy, M.E.6
  • 70
    • 0035432287 scopus 로고    scopus 로고
    • Expression of clpX, an ATPase subunit of the Clp protease, is heat and cold shock inducible in Lactococcus lactis
    • [70] Skinner, M.M., Trempy, J.E., Expression of clpX, an ATPase subunit of the Clp protease, is heat and cold shock inducible in Lactococcus lactis. J. Dairy Sci. 84 (2001), 1783–1785.
    • (2001) J. Dairy Sci. , vol.84 , pp. 1783-1785
    • Skinner, M.M.1    Trempy, J.E.2
  • 71
    • 38349070819 scopus 로고    scopus 로고
    • Cryopreservation of human hepatocytes alters the mitochondrial respiratory chain complex 1
    • [71] Stephenne, X., Najimi, M., Ngoc, D.K., Smets, F., Hue, L., Guigas, B., et al. Cryopreservation of human hepatocytes alters the mitochondrial respiratory chain complex 1. Cell Transplant. 16 (2007), 409–419.
    • (2007) Cell Transplant. , vol.16 , pp. 409-419
    • Stephenne, X.1    Najimi, M.2    Ngoc, D.K.3    Smets, F.4    Hue, L.5    Guigas, B.6
  • 72
    • 6044263660 scopus 로고    scopus 로고
    • Proteomic analysis of human acute leukemia cells: insight into their classification
    • [72] Cui, J.W., Wang, J., He, K., Jin, B.F., Wang, H.X., Li, W., et al. Proteomic analysis of human acute leukemia cells: insight into their classification. Clin. Cancer Res. 10 (2004), 6887–6896.
    • (2004) Clin. Cancer Res. , vol.10 , pp. 6887-6896
    • Cui, J.W.1    Wang, J.2    He, K.3    Jin, B.F.4    Wang, H.X.5    Li, W.6
  • 73
    • 79954450179 scopus 로고    scopus 로고
    • Proteomic analysis of childhood de novo acute myeloid leukemia and myelodysplastic syndrome/AML: correlation to molecular and cytogenetic analyses
    • [73] Braoudaki, M., Tzortzatou-Stathopoulou, F., Anagnostopoulos, A.K., Papathanassiou, C., Vougas, K., Karamolegou, K., et al. Proteomic analysis of childhood de novo acute myeloid leukemia and myelodysplastic syndrome/AML: correlation to molecular and cytogenetic analyses. Amino Acids 40 (2011), 943–951.
    • (2011) Amino Acids , vol.40 , pp. 943-951
    • Braoudaki, M.1    Tzortzatou-Stathopoulou, F.2    Anagnostopoulos, A.K.3    Papathanassiou, C.4    Vougas, K.5    Karamolegou, K.6
  • 74
    • 33746150544 scopus 로고    scopus 로고
    • Proteomic analysis of acute myeloid leukemia: identification of potential early biomarkers and therapeutic targets
    • [74] Lopez-Pedrera, C., Villalba, J.M., Siendones, E., Barbarroja, N., Gomez-Diaz, C., Rodriguez-Ariza, A., et al. Proteomic analysis of acute myeloid leukemia: identification of potential early biomarkers and therapeutic targets. Proteomics 6:Suppl. 1 (2006), S293–S299.
    • (2006) Proteomics , vol.6 , pp. S293-S299
    • Lopez-Pedrera, C.1    Villalba, J.M.2    Siendones, E.3    Barbarroja, N.4    Gomez-Diaz, C.5    Rodriguez-Ariza, A.6
  • 76
    • 84880860314 scopus 로고    scopus 로고
    • Potential biomarkers for adult acute myeloid leukemia minimal residual disease assessment searched by serum peptidome profiling
    • [76] Bai, J., He, A., Zhang, W., Huang, C., Yang, J., Yang, Y., et al. Potential biomarkers for adult acute myeloid leukemia minimal residual disease assessment searched by serum peptidome profiling. Proteome Sci., 11, 2013, 39.
    • (2013) Proteome Sci. , vol.11 , pp. 39
    • Bai, J.1    He, A.2    Zhang, W.3    Huang, C.4    Yang, J.5    Yang, Y.6
  • 77
    • 35648946797 scopus 로고    scopus 로고
    • p38 MAPK is a likely component of the signal transduction pathway triggering rapid cold hardening in the flesh fly Sarcophaga crassipalpis
    • [77] Fujiwara, Y., Denlinger, D.L., p38 MAPK is a likely component of the signal transduction pathway triggering rapid cold hardening in the flesh fly Sarcophaga crassipalpis. J. Exp. Biol. 210 (2007), 3295–3300.
    • (2007) J. Exp. Biol. , vol.210 , pp. 3295-3300
    • Fujiwara, Y.1    Denlinger, D.L.2
  • 78
    • 27744519095 scopus 로고    scopus 로고
    • Temperature-dependent activation of ERK/MAPK in yolk cells and its role in embryonic diapause termination in the silkworm Bombyx mori
    • [78] Iwata, K., Shindome, C., Kobayashi, Y., Takeda, M., Yamashita, O., Shiomi, K., et al. Temperature-dependent activation of ERK/MAPK in yolk cells and its role in embryonic diapause termination in the silkworm Bombyx mori. J. Insect Physiol. 51 (2005), 1306–1312.
    • (2005) J. Insect Physiol. , vol.51 , pp. 1306-1312
    • Iwata, K.1    Shindome, C.2    Kobayashi, Y.3    Takeda, M.4    Yamashita, O.5    Shiomi, K.6
  • 79
    • 84929082188 scopus 로고    scopus 로고
    • Emerging therapeutic targets in human acute myeloid leukemia (part 2) — bromodomain inhibition should be considered as a possible strategy for various patient subsets
    • [79] Reikvam, H., Hoang, T.T., Bruserud, O., Emerging therapeutic targets in human acute myeloid leukemia (part 2) — bromodomain inhibition should be considered as a possible strategy for various patient subsets. Expert. Rev. Hematol. 8 (2015), 315–327.
    • (2015) Expert. Rev. Hematol. , vol.8 , pp. 315-327
    • Reikvam, H.1    Hoang, T.T.2    Bruserud, O.3


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