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Volumn 178, Issue 1, 2011, Pages 12-18

Innovative proteomics for the discovery of systemically accessible cancer biomarkers suitable for imaging and targeted therapies

Author keywords

[No Author keywords available]

Indexed keywords

ANTINEOPLASTIC AGENT; CYTOTOXIC AGENT; GEMTUZUMAB OZOGAMICIN; IBRITUMOMAB TIUXETAN; LIGAND; MONOCLONAL ANTIBODY L19 I 131; RITUXIMAB; TOSITUMOMAB I 131; TUMOR MARKER; UNCLASSIFIED DRUG;

EID: 79251490378     PISSN: 00029440     EISSN: 15252191     Source Type: Journal    
DOI: 10.1016/j.ajpath.2010.08.004     Document Type: Review
Times cited : (17)

References (49)
  • 1
    • 44449085539 scopus 로고    scopus 로고
    • Paul Ehrlich's magic bullet concept: 100 Years of progress
    • DOI 10.1038/nrc2394, PII NRC2394
    • Strebhardt K, Ullrich A: Paul Ehrlich's magic bullet concept: 100 years of progress. Nat Rev Cancer 2008, 8:473-480 (Pubitemid 351752547)
    • (2008) Nature Reviews Cancer , vol.8 , Issue.6 , pp. 473-480
    • Strebhardt, K.1    Ullrich, A.2
  • 2
    • 37149046901 scopus 로고    scopus 로고
    • Identification of accessible human cancer biomarkers using ex vivo chemical proteomic strategies
    • DOI 10.1586/14789450.4.6.727
    • Kischel P, Waltregny D, Castronovo V: Identification of accessible human cancer biomarkers using ex vivo chemical proteomic strategies. Expert Rev Proteomics 2007, 4:727-739 (Pubitemid 350261439)
    • (2007) Expert Review of Proteomics , vol.4 , Issue.6 , pp. 727-739
    • Kischel, P.1    Waltregny, D.2    Castronovo, V.3
  • 4
    • 77954563922 scopus 로고    scopus 로고
    • Role of inflammatory cells and mediators in tumor invasion and metastasis
    • Mantovani A: Role of inflammatory cells and mediators in tumor invasion and metastasis. Cancer Metastasis Rev 2010, 29:241
    • (2010) Cancer Metastasis Rev , vol.29 , pp. 241
    • Mantovani, A.1
  • 7
    • 77950477378 scopus 로고    scopus 로고
    • Targeted treatment of acute myeloid leukemia in older adults: Role of gemtuzumab ozogamicin
    • Duong HK, Sekeres MA: Targeted treatment of acute myeloid leukemia in older adults: role of gemtuzumab ozogamicin. Clin Interv Aging 2009, 4:197-205
    • (2009) Clin Interv Aging , vol.4 , pp. 197-205
    • Duong, H.K.1    Sekeres, M.A.2
  • 9
    • 34347371248 scopus 로고    scopus 로고
    • Iodine 131 tositumomab in the treatment of non-Hodgkin's lymphoma
    • Smith S, Sweetenham JW: Iodine 131 tositumomab in the treatment of non-Hodgkin's lymphoma. Future Oncol 2007, 3:255-262
    • (2007) Future Oncol , vol.3 , pp. 255-262
    • Smith, S.1    Sweetenham, J.W.2
  • 10
    • 33644518982 scopus 로고    scopus 로고
    • Fibronectin as target for tumor therapy
    • Kaspar M, Zardi L, Neri D: Fibronectin as target for tumor therapy. Int J Cancer 2006, 118:1331-1339
    • (2006) Int J Cancer , vol.118 , pp. 1331-1339
    • Kaspar, M.1    Zardi, L.2    Neri, D.3
  • 14
    • 33744811140 scopus 로고    scopus 로고
    • Tumor-targeting properties of novel antibodies specific to the large isoform of tenascin-C
    • DOI 10.1158/1078-0432.CCR-05-2804
    • Brack SS, Silacci M, Birchler M, Neri D: Tumor-targeting properties of novel antibodies specific to the large isoform of tenascin-C. Clin Cancer Res 2006, 12:3200-3208 (Pubitemid 43837370)
    • (2006) Clinical Cancer Research , vol.12 , Issue.10 , pp. 3200-3208
    • Brack, S.S.1    Silacci, M.2    Birchler, M.3    Neri, D.4
  • 18
    • 47249112230 scopus 로고    scopus 로고
    • Biomarker discovery in clinical proteomics: Strategies for exposing low abundant proteins
    • DOI 10.2174/157016408784911927
    • Wang Y, Seneviratne J. Biomarker discovery in clinical proteomics: strategies for exposing low abundant proteins. Current Proteomics 2008, 5:104-114 (Pubitemid 351988581)
    • (2008) Current Proteomics , vol.5 , Issue.2 , pp. 104-114
    • Wang, Y.1    Seneviratne, J.2
  • 19
    • 33750112796 scopus 로고    scopus 로고
    • Protein Equalizer Technology: The quest for a "democratic proteome."
    • Righetti PG, Boschetti E, Lomas L, Citterio A: Protein Equalizer Technology: the quest for a "democratic proteome." Proteomics 20066:3980-3992
    • (2006) Proteomics , vol.6 , pp. 3980-3992
    • Righetti, P.G.1    Boschetti, E.2    Lomas, L.3    Citterio, A.4
  • 22
    • 55749112976 scopus 로고    scopus 로고
    • Membrane proteins and membrane proteomics
    • Tan S, Tan HT, Chung MC: Membrane proteins and membrane proteomics. Proteomics 2008, 8:3924-3932
    • (2008) Proteomics , vol.8 , pp. 3924-3932
    • Tan, S.1    Tan, H.T.2    Chung, M.C.3
  • 23
    • 3543072968 scopus 로고    scopus 로고
    • Purification of biotinylated proteins on streptavidin resin: A protocol for quantitative elution
    • Rybak JN, Scheurer SB, Neri D, Elia G: Purification of biotinylated proteins on streptavidin resin: a protocol for quantitative elution. Proteomics 2004, 4:2296-2299
    • (2004) Proteomics , vol.4 , pp. 2296-2299
    • Rybak, J.N.1    Scheurer, S.B.2    Neri, D.3    Elia, G.4
  • 24
    • 18744399322 scopus 로고    scopus 로고
    • In vivo protein biotinylation for identification of organ-specific antigens accessible from the vasculature
    • Rybak JN, Ettorre A, Kaissling B, Giavazzi R, Neri D, Elia G: In vivo protein biotinylation for identification of organ-specific antigens accessible from the vasculature. Nat Methods 2005, 2:291-298
    • (2005) Nat Methods , vol.2 , pp. 291-298
    • Rybak, J.N.1    Ettorre, A.2    Kaissling, B.3    Giavazzi, R.4    Neri, D.5    Elia, G.6
  • 25
    • 33751416666 scopus 로고    scopus 로고
    • A chemical proteomics approach for the identification of accessible antigens expressed in human kidney cancer
    • Castronovo V, Waltregny D, Kischel P, Roesli C, Elia G, Rybak JN, Neri D: A chemical proteomics approach for the identification of accessible antigens expressed in human kidney cancer. Mol Cell Proteomics 2006, 5:2083-2091
    • (2006) Mol Cell Proteomics , vol.5 , pp. 2083-2091
    • Castronovo, V.1    Waltregny, D.2    Kischel, P.3    Roesli, C.4    Elia, G.5    Rybak, J.N.6    Neri, D.7
  • 26
    • 57349106602 scopus 로고    scopus 로고
    • Identification of new accessible tumor antigens in human colon cancer by ex vivo protein biotinylation and comparative mass spectrometry analysis
    • Conrotto P, Roesli C, Rybak J, Kischel P, Waltregny D, Neri D, Castronovo V: Identification of new accessible tumor antigens in human colon cancer by ex vivo protein biotinylation and comparative mass spectrometry analysis. Int J Cancer 2008, 123:2856-2864
    • (2008) Int J Cancer , vol.123 , pp. 2856-2864
    • Conrotto, P.1    Roesli, C.2    Rybak, J.3    Kischel, P.4    Waltregny, D.5    Neri, D.6    Castronovo, V.7
  • 28
    • 44949173042 scopus 로고    scopus 로고
    • Identification of the surface-accessible, lineage-specific vascular proteome by two-dimensional peptide mapping
    • Roesli C, Mumprecht V, Neri D, Detmar M: Identification of the surface-accessible, lineage-specific vascular proteome by two-dimensional peptide mapping. FASEB J 2008, 22:1933-1944
    • (2008) FASEB J , vol.22 , pp. 1933-1944
    • Roesli, C.1    Mumprecht, V.2    Neri, D.3    Detmar, M.4
  • 30
    • 70350518340 scopus 로고    scopus 로고
    • Strategies for analysis of the glycosylation of proteins: Current status and future perspectives
    • Brooks SA: Strategies for analysis of the glycosylation of proteins: current status and future perspectives. Mol Biotechnol 2009, 43: 76-88
    • (2009) Mol Biotechnol , vol.43 , pp. 76-88
    • Brooks, S.A.1
  • 31
    • 0038699625 scopus 로고    scopus 로고
    • Identification and quantification of N-linked glycoproteins using hydrazide chemistry, stable isotope labeling and mass spectrometry
    • Zhang H, Li XJ, Martin DB, Aebersold R: Identification and quantification of N-linked glycoproteins using hydrazide chemistry, stable isotope labeling and mass spectrometry. Nature Biotechnol 2003, 21:660-666
    • (2003) Nature Biotechnol , vol.21 , pp. 660-666
    • Zhang, H.1    Li, X.J.2    Martin, D.B.3    Aebersold, R.4
  • 34
    • 68549098240 scopus 로고    scopus 로고
    • Cell surface and secreted protein profiles of human thyroid cancer cell lines reveal distinct glycoprotein patterns
    • Arcinas A, Yen TY, Kebebew E, Macher BA: Cell surface and secreted protein profiles of human thyroid cancer cell lines reveal distinct glycoprotein patterns. J Proteome Res 2009, 8:3958-3968
    • (2009) J Proteome Res , vol.8 , pp. 3958-3968
    • Arcinas, A.1    Yen, T.Y.2    Kebebew, E.3    Macher, B.A.4
  • 35
    • 61849115201 scopus 로고    scopus 로고
    • Identification of N-glycosylation sites on secreted proteins of human hepatocellular carcinoma cells with a complementary proteomics approach
    • Cao J, Shen C, Wang H, Shen H, Chen Y, Nie A, Yan G, Lu H, Liu Y, Yang P: Identification of N-glycosylation sites on secreted proteins of human hepatocellular carcinoma cells with a complementary proteomics approach. J Proteome Res 2009, 8:662-672
    • (2009) J Proteome Res , vol.8 , pp. 662-672
    • Cao, J.1    Shen, C.2    Wang, H.3    Shen, H.4    Chen, Y.5    Nie, A.6    Yan, G.7    Lu, H.8    Liu, Y.9    Yang, P.10
  • 36
    • 61849164561 scopus 로고    scopus 로고
    • Glycoproteomics analysis of human liver tissue by combination of multiple enzyme digestion and hydrazide chemistry
    • Chen R, Jiang X, Sun D, Han G, Wang F, Ye M, Wang L, Zou H: Glycoproteomics analysis of human liver tissue by combination of multiple enzyme digestion and hydrazide chemistry. J Proteome Res 2009, 8:651-661
    • (2009) J Proteome Res , vol.8 , pp. 651-661
    • Chen, R.1    Jiang, X.2    Sun, D.3    Han, G.4    Wang, F.5    Ye, M.6    Wang, L.7    Zou, H.8
  • 37
    • 63849247205 scopus 로고    scopus 로고
    • Proteomics strategies for target identification and biomarker discovery in cancer
    • Rajcevic U, Niclou SP, Jimenez CR: Proteomics strategies for target identification and biomarker discovery in cancer. Front Biosci 2009, 14:3292-3303
    • (2009) Front Biosci , vol.14 , pp. 3292-3303
    • Rajcevic, U.1    Niclou, S.P.2    Jimenez, C.R.3
  • 38
    • 58149147240 scopus 로고    scopus 로고
    • Sample preparation and fractionation for proteome analysis and cancer biomarker discovery by mass spectrometry
    • Ahmed FE: Sample preparation and fractionation for proteome analysis and cancer biomarker discovery by mass spectrometry. J Sep Sci 2009, 32:771-798
    • (2009) J Sep Sci , vol.32 , pp. 771-798
    • Ahmed, F.E.1
  • 41
    • 2542640080 scopus 로고    scopus 로고
    • Mass spectrometry as a diagnostic and a cancer biomarker discovery tool: Opportunities and potential limitations
    • Diamandis EP: Mass spectrometry as a diagnostic and a cancer biomarker discovery tool: opportunities and potential limitations. Mol Cell Proteomics 2004, 3:367-378
    • (2004) Mol Cell Proteomics , vol.3 , pp. 367-378
    • Diamandis, E.P.1
  • 42
    • 33748160055 scopus 로고    scopus 로고
    • Ion formation mechanisms in UV-MALDI
    • Knochenmuss R: Ion formation mechanisms in UV-MALDI. Analyst 2006, 131:966-986
    • (2006) Analyst , vol.131 , pp. 966-986
    • Knochenmuss, R.1
  • 43
    • 70350507226 scopus 로고    scopus 로고
    • Electrospray: From ions in solution to ions in the gas phase, what we know now
    • Kebarle P, Verkerk UH: Electrospray: from ions in solution to ions in the gas phase, what we know now. Mass Spectrom Rev 2009, 28: 898-917
    • (2009) Mass Spectrom Rev , vol.28 , pp. 898-917
    • Kebarle, P.1    Verkerk, U.H.2
  • 44
    • 30144443840 scopus 로고    scopus 로고
    • Peptide sequence analysis
    • Medzihradszky KF: Peptide sequence analysis. Methods Enzymol 2005, 402:209-244
    • (2005) Methods Enzymol , vol.402 , pp. 209-244
    • Medzihradszky, K.F.1
  • 45
    • 36448947243 scopus 로고    scopus 로고
    • Rational selection of the optimum MALDI matrix for top-down proteomics by in-source decay
    • Demeure K, Quinton L, Gabelica V, De Pauw E: Rational selection of the optimum MALDI matrix for top-down proteomics by in-source decay. Anal Chem 2007, 79:8678-8685
    • (2007) Anal Chem , vol.79 , pp. 8678-8685
    • Demeure, K.1    Quinton, L.2    Gabelica, V.3    De Pauw, E.4
  • 46
    • 55849104839 scopus 로고    scopus 로고
    • Application of electron transfer dissociation (ETD) for the analysis of posttranslational modifications
    • Wiesner J, Premsler T, Sickmann A: Application of electron transfer dissociation (ETD) for the analysis of posttranslational modifications. Proteomics 2008, 8:4466-4483
    • (2008) Proteomics , vol.8 , pp. 4466-4483
    • Wiesner, J.1    Premsler, T.2    Sickmann, A.3
  • 47
    • 0037435030 scopus 로고    scopus 로고
    • Mass spectrometry-based proteomics
    • Aebersold R, Mann M: Mass spectrometry-based proteomics. Nature 2003, 422:198-207
    • (2003) Nature , vol.422 , pp. 198-207
    • Aebersold, R.1    Mann, M.2
  • 48
    • 35848929694 scopus 로고    scopus 로고
    • Analysis and validation of proteomic data generated by tandem mass spectrometry
    • DOI 10.1038/nmeth1088, PII NMETH1088
    • Nesvizhskii AI, Vitek O, Aebersold R: Analysis and validation of proteomic data generated by tandem mass spectrometry. Nat Methods 2007, 4:787-797 (Pubitemid 350055575)
    • (2007) Nature Methods , vol.4 , Issue.10 , pp. 787-797
    • Nesvizhskii, A.I.1    Vitek, O.2    Aebersold, R.3
  • 49
    • 59149084542 scopus 로고    scopus 로고
    • Targeted proteomic strategy for clinical biomarker discovery
    • Schiess R, Wollscheid B, Aebersold R: Targeted proteomic strategy for clinical biomarker discovery. Mol Oncol 2009, 3: 33-44
    • (2009) Mol Oncol , vol.3 , pp. 33-44
    • Schiess, R.1    Wollscheid, B.2    Aebersold, R.3


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.