메뉴 건너뛰기




Volumn 73, Issue 3, 2010, Pages 537-551

Cancer-specific MALDI-TOF profiles of blood serum and plasma: Biological meaning and perspectives

Author keywords

Acute phase proteins; Biomarker; Cancer; MALDI TOF MS

Indexed keywords

ALPHA 1 ANTITRYPSIN; AMYLOID A PROTEIN; APOLIPOPROTEIN; BIOLOGICAL MARKER; COMPLEMENT COMPONENT C3A; COMPLEMENT COMPONENT C4A; CYSTATIN C; EXOPEPTIDASE; HAPTOGLOBIN; PEPTIDE FRAGMENT; PREALBUMIN; TRANSFERRIN; TRYPSIN;

EID: 72149087954     PISSN: 18743919     EISSN: None     Source Type: Journal    
DOI: 10.1016/j.jprot.2009.09.011     Document Type: Review
Times cited : (52)

References (147)
  • 2
    • 33750600311 scopus 로고    scopus 로고
    • Strategies for plasma proteomic profiling of cancers
    • Omenn G.S. Strategies for plasma proteomic profiling of cancers. Proteomics 6 20 (2006) 5662-5673
    • (2006) Proteomics , vol.6 , Issue.20 , pp. 5662-5673
    • Omenn, G.S.1
  • 3
    • 7044224620 scopus 로고    scopus 로고
    • Preoperative sensitivity and specificity for early-stage ovarian cancer when combining cancer antigen CA-125II, CA 15-3, CA 72-4, and macrophage colony-stimulating factor using mixtures of multivariate normal distributions
    • Skates S.J., Horick N., Yu Y., Xu F.J., Berchuck A., Havrilesky L.J., et al. Preoperative sensitivity and specificity for early-stage ovarian cancer when combining cancer antigen CA-125II, CA 15-3, CA 72-4, and macrophage colony-stimulating factor using mixtures of multivariate normal distributions. J Clin Oncol 22 20 (2004) 4059-4066
    • (2004) J Clin Oncol , vol.22 , Issue.20 , pp. 4059-4066
    • Skates, S.J.1    Horick, N.2    Yu, Y.3    Xu, F.J.4    Berchuck, A.5    Havrilesky, L.J.6
  • 4
  • 6
    • 64649086561 scopus 로고    scopus 로고
    • Analytical considerations for mass spectrometry profiling in serum biomarker discovery
    • Whiteley G.R., Colantonio S., Sacconi A., and Saul R.G. Analytical considerations for mass spectrometry profiling in serum biomarker discovery. Clin Lab Med 29 1 (2009) 57-69
    • (2009) Clin Lab Med , vol.29 , Issue.1 , pp. 57-69
    • Whiteley, G.R.1    Colantonio, S.2    Sacconi, A.3    Saul, R.G.4
  • 7
    • 33745442821 scopus 로고    scopus 로고
    • The MALDI-TOF mass spectrometric view of the plasma proteome and peptidome
    • Hortin G.L. The MALDI-TOF mass spectrometric view of the plasma proteome and peptidome. Clin Chem 52 7 (2006) 1223-1237
    • (2006) Clin Chem , vol.52 , Issue.7 , pp. 1223-1237
    • Hortin, G.L.1
  • 8
    • 33846622299 scopus 로고    scopus 로고
    • AFM fishing nanotechnology is the way to reverse the Avogadro number in proteomics
    • Archakov A.I., Ivanov Y.D., Lisitsa A.V., and Zgoda V.G. AFM fishing nanotechnology is the way to reverse the Avogadro number in proteomics. Proteomics 7 1 (2007) 4-9
    • (2007) Proteomics , vol.7 , Issue.1 , pp. 4-9
    • Archakov, A.I.1    Ivanov, Y.D.2    Lisitsa, A.V.3    Zgoda, V.G.4
  • 9
    • 34347266569 scopus 로고    scopus 로고
    • Data analysis of assorted serum peptidome profiles
    • Villanueva J., Philip J., DeNoyer L., and Tempst P. Data analysis of assorted serum peptidome profiles. Nat Protoc 2 3 (2007) 588-602
    • (2007) Nat Protoc , vol.2 , Issue.3 , pp. 588-602
    • Villanueva, J.1    Philip, J.2    DeNoyer, L.3    Tempst, P.4
  • 10
    • 17844394177 scopus 로고    scopus 로고
    • Statistical and computational methods for comparative proteomic profiling using liquid chromatography-tandem mass spectrometry
    • Listgarten J., and Emili A. Statistical and computational methods for comparative proteomic profiling using liquid chromatography-tandem mass spectrometry. Mol Cell Proteomics 4 4 (2005) 419-434
    • (2005) Mol Cell Proteomics , vol.4 , Issue.4 , pp. 419-434
    • Listgarten, J.1    Emili, A.2
  • 12
    • 34248578524 scopus 로고    scopus 로고
    • Sample preparation for serum/plasma profiling and biomarker identification by mass spectrometry
    • Luque-Garcia J.L., and Neubert T.A. Sample preparation for serum/plasma profiling and biomarker identification by mass spectrometry. J Chromatogr A 1153 1-2 (2007) 259-276
    • (2007) J Chromatogr A , vol.1153 , Issue.1-2 , pp. 259-276
    • Luque-Garcia, J.L.1    Neubert, T.A.2
  • 13
    • 19644386500 scopus 로고    scopus 로고
    • Standardized approach to proteome profiling of human serum based on magnetic bead separation and matrix-assisted laser desorption/ionization time-of-flight mass spectrometry
    • Baumann S., Ceglarek U., Fiedler G.M., Lembcke J., Leichtle A., and Thiery J. Standardized approach to proteome profiling of human serum based on magnetic bead separation and matrix-assisted laser desorption/ionization time-of-flight mass spectrometry. Clin Chem 51 6 (2005) 973-980
    • (2005) Clin Chem , vol.51 , Issue.6 , pp. 973-980
    • Baumann, S.1    Ceglarek, U.2    Fiedler, G.M.3    Lembcke, J.4    Leichtle, A.5    Thiery, J.6
  • 14
    • 23944472689 scopus 로고    scopus 로고
    • Immunoassay and antibody microarray analysis of the HUPO Plasma Proteome Project reference specimens: systematic variation between sample types and calibration of mass spectrometry data
    • Haab B.B., Geierstanger B.H., Michailidis G., Vitzthum F., Forrester S., Okon R., et al. Immunoassay and antibody microarray analysis of the HUPO Plasma Proteome Project reference specimens: systematic variation between sample types and calibration of mass spectrometry data. Proteomics 5 13 (2005) 3278-3291
    • (2005) Proteomics , vol.5 , Issue.13 , pp. 3278-3291
    • Haab, B.B.1    Geierstanger, B.H.2    Michailidis, G.3    Vitzthum, F.4    Forrester, S.5    Okon, R.6
  • 15
    • 1242328742 scopus 로고    scopus 로고
    • SELDI-TOF-based serum proteomic pattern diagnostics for early detection of cancer
    • Petricoin E.F., and Liotta L.A. SELDI-TOF-based serum proteomic pattern diagnostics for early detection of cancer. Curr Opin Biotechnol 15 1 (2004) 24-30
    • (2004) Curr Opin Biotechnol , vol.15 , Issue.1 , pp. 24-30
    • Petricoin, E.F.1    Liotta, L.A.2
  • 17
    • 0345166891 scopus 로고    scopus 로고
    • Detection of cancer-specific markers amid massive mass spectral data
    • Zhu W., Wang X., Ma Y., Rao M., Glimm J., and Kovach J.S. Detection of cancer-specific markers amid massive mass spectral data. Proc Natl Acad Sci U S A 100 25 (2003) 14666-14671
    • (2003) Proc Natl Acad Sci U S A , vol.100 , Issue.25 , pp. 14666-14671
    • Zhu, W.1    Wang, X.2    Ma, Y.3    Rao, M.4    Glimm, J.5    Kovach, J.S.6
  • 18
    • 0142027764 scopus 로고    scopus 로고
    • Identification of biomarkers for ovarian cancer using strong anion-exchange ProteinChips: potential use in diagnosis and prognosis
    • Kozak K.R., Amneus M.W., Pusey S.M., Su F., Luong M.N., Luong S.A., et al. Identification of biomarkers for ovarian cancer using strong anion-exchange ProteinChips: potential use in diagnosis and prognosis. Proc Natl Acad Sci U S A 100 21 (2003) 12343-12348
    • (2003) Proc Natl Acad Sci U S A , vol.100 , Issue.21 , pp. 12343-12348
    • Kozak, K.R.1    Amneus, M.W.2    Pusey, S.M.3    Su, F.4    Luong, M.N.5    Luong, S.A.6
  • 19
    • 28444478097 scopus 로고    scopus 로고
    • Characterization of serum biomarkers for detection of early stage ovarian cancer
    • Kozak K.R., Su F., Whitelegge J.P., Faull K., Reddy S., and Farias-Eisner R. Characterization of serum biomarkers for detection of early stage ovarian cancer. Proteomics 5 17 (2005) 4589-4596
    • (2005) Proteomics , vol.5 , Issue.17 , pp. 4589-4596
    • Kozak, K.R.1    Su, F.2    Whitelegge, J.P.3    Faull, K.4    Reddy, S.5    Farias-Eisner, R.6
  • 20
    • 0942265518 scopus 로고    scopus 로고
    • Diagnosis of ovarian cancer using decision tree classification of mass spectral data
    • Vlahou A., Schorge J.O., Gregory B.W., and Coleman R.L. Diagnosis of ovarian cancer using decision tree classification of mass spectral data. J Biomed Biotechnol 2003 5 (2003) 308-314
    • (2003) J Biomed Biotechnol , vol.2003 , Issue.5 , pp. 308-314
    • Vlahou, A.1    Schorge, J.O.2    Gregory, B.W.3    Coleman, R.L.4
  • 21
    • 38749151898 scopus 로고    scopus 로고
    • SELDI-TOF MS whole serum proteomic profiling with IMAC surface does not reliably detect prostate cancer
    • McLerran D., Grizzle W.E., Feng Z., Thompson I.M., Bigbee W.L., Cazares L.H., et al. SELDI-TOF MS whole serum proteomic profiling with IMAC surface does not reliably detect prostate cancer. Clin Chem 54 1 (2008) 53-60
    • (2008) Clin Chem , vol.54 , Issue.1 , pp. 53-60
    • McLerran, D.1    Grizzle, W.E.2    Feng, Z.3    Thompson, I.M.4    Bigbee, W.L.5    Cazares, L.H.6
  • 22
    • 38749100576 scopus 로고    scopus 로고
    • Identification of serum biomarkers for nasopharyngeal carcinoma by proteomic analysis
    • Wei Y.S., Zheng Y.H., Liang W.B., Zhang J.Z., Yang Z.H., Lv M.L., et al. Identification of serum biomarkers for nasopharyngeal carcinoma by proteomic analysis. Cancer 112 3 (2008) 544-551
    • (2008) Cancer , vol.112 , Issue.3 , pp. 544-551
    • Wei, Y.S.1    Zheng, Y.H.2    Liang, W.B.3    Zhang, J.Z.4    Yang, Z.H.5    Lv, M.L.6
  • 23
    • 38949145743 scopus 로고    scopus 로고
    • Serum proteomics and biomarkers in hepatocellular carcinoma and chronic liver disease
    • Zinkin N.T., Grall F., Bhaskar K., Otu H.H., Spentzos D., Kalmowitz B., et al. Serum proteomics and biomarkers in hepatocellular carcinoma and chronic liver disease. Clin Cancer Res 14 2 (2008) 470-477
    • (2008) Clin Cancer Res , vol.14 , Issue.2 , pp. 470-477
    • Zinkin, N.T.1    Grall, F.2    Bhaskar, K.3    Otu, H.H.4    Spentzos, D.5    Kalmowitz, B.6
  • 24
    • 3042543533 scopus 로고    scopus 로고
    • Serum protein profiling by SELDI mass spectrometry: detection of multiple variants of serum amyloid alpha in renal cancer patients
    • Tolson J., Bogumil R., Brunst E., Beck H., Elsner R., Humeny A., et al. Serum protein profiling by SELDI mass spectrometry: detection of multiple variants of serum amyloid alpha in renal cancer patients. Lab Invest 84 7 (2004) 845-856
    • (2004) Lab Invest , vol.84 , Issue.7 , pp. 845-856
    • Tolson, J.1    Bogumil, R.2    Brunst, E.3    Beck, H.4    Elsner, R.5    Humeny, A.6
  • 25
    • 33646730482 scopus 로고    scopus 로고
    • Identification of complement C3a as a candidate biomarker in human chronic hepatitis C and HCV-related hepatocellular carcinoma using a proteomics approach
    • Lee I.N., Chen C.H., Sheu J.C., Lee H.S., Huang G.T., Chen D.S., et al. Identification of complement C3a as a candidate biomarker in human chronic hepatitis C and HCV-related hepatocellular carcinoma using a proteomics approach. Proteomics 6 9 (2006) 2865-2873
    • (2006) Proteomics , vol.6 , Issue.9 , pp. 2865-2873
    • Lee, I.N.1    Chen, C.H.2    Sheu, J.C.3    Lee, H.S.4    Huang, G.T.5    Chen, D.S.6
  • 26
    • 4143067096 scopus 로고    scopus 로고
    • Three biomarkers identified from serum proteomic analysis for the detection of early stage ovarian cancer
    • Zhang Z., Bast Jr. R.C., Yu Y., Li J., Sokoll L.J., Rai A.J., et al. Three biomarkers identified from serum proteomic analysis for the detection of early stage ovarian cancer. Cancer Res 64 16 (2004) 5882-5890
    • (2004) Cancer Res , vol.64 , Issue.16 , pp. 5882-5890
    • Zhang, Z.1    Bast Jr., R.C.2    Yu, Y.3    Li, J.4    Sokoll, L.J.5    Rai, A.J.6
  • 27
    • 33745085581 scopus 로고    scopus 로고
    • Identification of serum biomarkers for colon cancer by proteomic analysis
    • Ward D.G., Suggett N., Cheng Y., Wei W., Johnson H., Billingham L.J., et al. Identification of serum biomarkers for colon cancer by proteomic analysis. Br J Cancer 94 12 (2006) 1898-1905
    • (2006) Br J Cancer , vol.94 , Issue.12 , pp. 1898-1905
    • Ward, D.G.1    Suggett, N.2    Cheng, Y.3    Wei, W.4    Johnson, H.5    Billingham, L.J.6
  • 28
    • 33748325683 scopus 로고    scopus 로고
    • Discovery and identification of potential biomarkers in a prospective study of chronic lymphoid malignancies using SELDI-TOF-MS
    • Miguet L., Bogumil R., Decloquement P., Herbrecht R., Potier N., Mauvieux L., et al. Discovery and identification of potential biomarkers in a prospective study of chronic lymphoid malignancies using SELDI-TOF-MS. J Proteome Res 5 9 (2006) 2258-2269
    • (2006) J Proteome Res , vol.5 , Issue.9 , pp. 2258-2269
    • Miguet, L.1    Bogumil, R.2    Decloquement, P.3    Herbrecht, R.4    Potier, N.5    Mauvieux, L.6
  • 29
    • 12944252957 scopus 로고    scopus 로고
    • Serum levels of an isoform of apolipoprotein A-II as a potential marker for prostate cancer
    • Malik G., Ward M.D., Gupta S.K., Trosset M.W., Grizzle W.E., Adam B.L., et al. Serum levels of an isoform of apolipoprotein A-II as a potential marker for prostate cancer. Clin Cancer Res 11 3 (2005) 1073-1085
    • (2005) Clin Cancer Res , vol.11 , Issue.3 , pp. 1073-1085
    • Malik, G.1    Ward, M.D.2    Gupta, S.K.3    Trosset, M.W.4    Grizzle, W.E.5    Adam, B.L.6
  • 30
    • 33947430973 scopus 로고    scopus 로고
    • Posttranslational modifications of transthyretin are serum markers in patients with mycosis fungoides
    • Escher N., Kaatz M., Melle C., Hipler C., Ziemer M., Driesch D., et al. Posttranslational modifications of transthyretin are serum markers in patients with mycosis fungoides. Neoplasia 9 3 (2007) 254-259
    • (2007) Neoplasia , vol.9 , Issue.3 , pp. 254-259
    • Escher, N.1    Kaatz, M.2    Melle, C.3    Hipler, C.4    Ziemer, M.5    Driesch, D.6
  • 31
    • 33751520049 scopus 로고    scopus 로고
    • Increase diagnostic efficacy by combined use of fingerprint markers in mass spectrometry-plasma peptidomes from nasopharyngeal cancer patients for example
    • Chang J.T., Chen L.C., Wei S.Y., Chen Y.J., Wang H.M., Liao C.T., et al. Increase diagnostic efficacy by combined use of fingerprint markers in mass spectrometry-plasma peptidomes from nasopharyngeal cancer patients for example. Clin Biochem 39 12 (2006) 1144-1151
    • (2006) Clin Biochem , vol.39 , Issue.12 , pp. 1144-1151
    • Chang, J.T.1    Chen, L.C.2    Wei, S.Y.3    Chen, Y.J.4    Wang, H.M.5    Liao, C.T.6
  • 32
    • 28044447188 scopus 로고    scopus 로고
    • Oral cancer plasma tumor marker identified with bead-based affinity-fractionated proteomic technology
    • Cheng A.J., Chen L.C., Chien K.Y., Chen Y.J., Chang J.T., Wang H.M., et al. Oral cancer plasma tumor marker identified with bead-based affinity-fractionated proteomic technology. Clin Chem 51 12 (2005) 2236-2244
    • (2005) Clin Chem , vol.51 , Issue.12 , pp. 2236-2244
    • Cheng, A.J.1    Chen, L.C.2    Chien, K.Y.3    Chen, Y.J.4    Chang, J.T.5    Wang, H.M.6
  • 33
    • 37549011764 scopus 로고    scopus 로고
    • Differential capture of serum proteins for expression profiling and biomarker discovery in pre- and posttreatment head and neck cancer samples
    • Freed G.L., Cazares L.H., Fichandler C.E., Fuller T.W., Sawyer C.A., Stack Jr. B.C., et al. Differential capture of serum proteins for expression profiling and biomarker discovery in pre- and posttreatment head and neck cancer samples. Laryngoscope 118 1 (2008) 61-68
    • (2008) Laryngoscope , vol.118 , Issue.1 , pp. 61-68
    • Freed, G.L.1    Cazares, L.H.2    Fichandler, C.E.3    Fuller, T.W.4    Sawyer, C.A.5    Stack Jr., B.C.6
  • 34
    • 1542617944 scopus 로고    scopus 로고
    • Serum peptide profiling by magnetic particle-assisted, automated sample processing and MALDI-TOF mass spectrometry
    • Villanueva J., Philip J., Entenberg D., Chaparro C.A., Tanwar M.K., Holland E.C., et al. Serum peptide profiling by magnetic particle-assisted, automated sample processing and MALDI-TOF mass spectrometry. Anal Chem 76 6 (2004) 1560-1570
    • (2004) Anal Chem , vol.76 , Issue.6 , pp. 1560-1570
    • Villanueva, J.1    Philip, J.2    Entenberg, D.3    Chaparro, C.A.4    Tanwar, M.K.5    Holland, E.C.6
  • 35
    • 33750621983 scopus 로고    scopus 로고
    • Serum peptidome patterns that distinguish metastatic thyroid carcinoma from cancer-free controls are unbiased by gender and age
    • Villanueva J., Martorella A.J., Lawlor K., Philip J., Fleisher M., Robbins R.J., et al. Serum peptidome patterns that distinguish metastatic thyroid carcinoma from cancer-free controls are unbiased by gender and age. Mol Cell Proteomics 5 10 (2006) 1840-1852
    • (2006) Mol Cell Proteomics , vol.5 , Issue.10 , pp. 1840-1852
    • Villanueva, J.1    Martorella, A.J.2    Lawlor, K.3    Philip, J.4    Fleisher, M.5    Robbins, R.J.6
  • 37
    • 35148834673 scopus 로고    scopus 로고
    • Candidate markers for the detection of hepatocellular carcinoma in low-molecular weight fraction of serum
    • Goldman R., Ressom H.W., Abdel-Hamid M., Goldman L., Wang A., Varghese R.S., et al. Candidate markers for the detection of hepatocellular carcinoma in low-molecular weight fraction of serum. Carcinogenesis 28 10 (2007) 2149-2153
    • (2007) Carcinogenesis , vol.28 , Issue.10 , pp. 2149-2153
    • Goldman, R.1    Ressom, H.W.2    Abdel-Hamid, M.3    Goldman, L.4    Wang, A.5    Varghese, R.S.6
  • 38
    • 33646746601 scopus 로고    scopus 로고
    • Enrichment of low molecular weight fraction of serum for MS analysis of peptides associated with hepatocellular carcinoma
    • Orvisky E., Drake S.K., Martin B.M., Abdel-Hamid M., Ressom H.W., Varghese R.S., et al. Enrichment of low molecular weight fraction of serum for MS analysis of peptides associated with hepatocellular carcinoma. Proteomics 6 9 (2006) 2895-2902
    • (2006) Proteomics , vol.6 , Issue.9 , pp. 2895-2902
    • Orvisky, E.1    Drake, S.K.2    Martin, B.M.3    Abdel-Hamid, M.4    Ressom, H.W.5    Varghese, R.S.6
  • 42
    • 33646170428 scopus 로고    scopus 로고
    • Two-dimensional electrophoretic proteome study of serum thermostable fraction from patients with various tumor conditions
    • Goufman E.I., Moshkovskii S.A., Tikhonova O.V., Lokhov P.G., Zgoda V.G., Serebryakova M.V., et al. Two-dimensional electrophoretic proteome study of serum thermostable fraction from patients with various tumor conditions. Biochemistry (Mosc) 71 4 (2006) 354-360
    • (2006) Biochemistry (Mosc) , vol.71 , Issue.4 , pp. 354-360
    • Goufman, E.I.1    Moshkovskii, S.A.2    Tikhonova, O.V.3    Lokhov, P.G.4    Zgoda, V.G.5    Serebryakova, M.V.6
  • 43
    • 23944524368 scopus 로고    scopus 로고
    • Depletion of multiple high-abundance proteins improves protein profiling capacities of human serum and plasma
    • Echan L.A., Tang H.Y., Ali-Khan N., Lee K., and Speicher D.W. Depletion of multiple high-abundance proteins improves protein profiling capacities of human serum and plasma. Proteomics 5 13 (2005) 3292-3303
    • (2005) Proteomics , vol.5 , Issue.13 , pp. 3292-3303
    • Echan, L.A.1    Tang, H.Y.2    Ali-Khan, N.3    Lee, K.4    Speicher, D.W.5
  • 44
    • 23944495100 scopus 로고    scopus 로고
    • Immunoaffinity separation of plasma proteins by IgY microbeads: meeting the needs of proteomic sample preparation and analysis
    • Huang L., Harvie G., Feitelson J.S., Gramatikoff K., Herold D.A., Allen D.L., et al. Immunoaffinity separation of plasma proteins by IgY microbeads: meeting the needs of proteomic sample preparation and analysis. Proteomics 5 13 (2005) 3314-3328
    • (2005) Proteomics , vol.5 , Issue.13 , pp. 3314-3328
    • Huang, L.1    Harvie, G.2    Feitelson, J.S.3    Gramatikoff, K.4    Herold, D.A.5    Allen, D.L.6
  • 45
    • 36549031631 scopus 로고    scopus 로고
    • A rapid, economical, and reproducible method for human serum delipidation and albumin and IgG removal for proteomic analysis
    • Fu Q., Bovenkamp D.E., and Van Eyk J.E. A rapid, economical, and reproducible method for human serum delipidation and albumin and IgG removal for proteomic analysis. Methods Mol Biol 357 (2007) 365-371
    • (2007) Methods Mol Biol , vol.357 , pp. 365-371
    • Fu, Q.1    Bovenkamp, D.E.2    Van Eyk, J.E.3
  • 46
  • 47
    • 25444531409 scopus 로고    scopus 로고
    • Analysis of albumin-associated peptides and proteins from ovarian cancer patients
    • Lowenthal M.S., Mehta A.I., Frogale K., Bandle R.W., Araujo R.P., Hood B.L., et al. Analysis of albumin-associated peptides and proteins from ovarian cancer patients. Clin Chem 51 10 (2005) 1933-1945
    • (2005) Clin Chem , vol.51 , Issue.10 , pp. 1933-1945
    • Lowenthal, M.S.1    Mehta, A.I.2    Frogale, K.3    Bandle, R.W.4    Araujo, R.P.5    Hood, B.L.6
  • 50
    • 34249992814 scopus 로고    scopus 로고
    • Investigation of an albumin-enriched fraction of human serum and its albuminome
    • Gundry R.L., F. Q., Jelinek C.A., Van Eyk J.E., J., and C. R. Investigation of an albumin-enriched fraction of human serum and its albuminome. Proteomics Clin Appl 1 (2007) 73-88
    • (2007) Proteomics Clin Appl , vol.1 , pp. 73-88
    • Gundry, R.L.1    F., Q.2    Jelinek, C.A.3    Van Eyk, J.E.4    J., C., R.5
  • 51
    • 34249864811 scopus 로고    scopus 로고
    • A novel, high-throughput workflow for discovery and identification of serum carrier protein-bound peptide biomarker candidates in ovarian cancer samples
    • Lopez M.F., Mikulskis A., Kuzdzal S., Golenko E., Petricoin III E.F., and Liotta L.A. A novel, high-throughput workflow for discovery and identification of serum carrier protein-bound peptide biomarker candidates in ovarian cancer samples. Clin Chem 53 6 (2007) 1067-1074
    • (2007) Clin Chem , vol.53 , Issue.6 , pp. 1067-1074
    • Lopez, M.F.1    Mikulskis, A.2    Kuzdzal, S.3    Golenko, E.4    Petricoin III, E.F.5    Liotta, L.A.6
  • 52
    • 34247891769 scopus 로고    scopus 로고
    • Serum albumin-associated peptides of patients with uterine endometrial cancer
    • Kikuchi S., Honda K., Handa Y., Kato H., Yamashita K., Umaki T., et al. Serum albumin-associated peptides of patients with uterine endometrial cancer. Cancer Sci 98 6 (2007) 822-829
    • (2007) Cancer Sci , vol.98 , Issue.6 , pp. 822-829
    • Kikuchi, S.1    Honda, K.2    Handa, Y.3    Kato, H.4    Yamashita, K.5    Umaki, T.6
  • 53
    • 36549020565 scopus 로고    scopus 로고
    • Proteomic patterns for classification of ovarian cancer and CTCL serum samples utilizing peak pairs indicative of post-translational modifications
    • Liu C., Shea N., Rucker S., Harvey L., Russo P., Saul R., et al. Proteomic patterns for classification of ovarian cancer and CTCL serum samples utilizing peak pairs indicative of post-translational modifications. Proteomics 7 22 (2007) 4045-4052
    • (2007) Proteomics , vol.7 , Issue.22 , pp. 4045-4052
    • Liu, C.1    Shea, N.2    Rucker, S.3    Harvey, L.4    Russo, P.5    Saul, R.6
  • 55
    • 41549158639 scopus 로고    scopus 로고
    • A sequence-specific exopeptidase activity test (SSEAT) for "functional" biomarker discovery
    • Villanueva J., Nazarian A., Lawlor K., Yi S.S., Robbins R.J., and Tempst P. A sequence-specific exopeptidase activity test (SSEAT) for "functional" biomarker discovery. Mol Cell Proteomics 7 3 (2008) 509-518
    • (2008) Mol Cell Proteomics , vol.7 , Issue.3 , pp. 509-518
    • Villanueva, J.1    Nazarian, A.2    Lawlor, K.3    Yi, S.S.4    Robbins, R.J.5    Tempst, P.6
  • 56
    • 20144377294 scopus 로고    scopus 로고
    • Classification of cancer types by measuring variants of host response proteins using SELDI serum assays
    • Fung E.T., Yip T.T., Lomas L., Wang Z., Yip C., Meng X.Y., et al. Classification of cancer types by measuring variants of host response proteins using SELDI serum assays. Int J Cancer 115 5 (2005) 783-789
    • (2005) Int J Cancer , vol.115 , Issue.5 , pp. 783-789
    • Fung, E.T.1    Yip, T.T.2    Lomas, L.3    Wang, Z.4    Yip, C.5    Meng, X.Y.6
  • 57
    • 33646909090 scopus 로고    scopus 로고
    • Quantification of fragments of human serum inter-alpha-trypsin inhibitor heavy chain 4 by a surface-enhanced laser desorption/ionization-based immunoassay
    • Song J., Patel M., Rosenzweig C.N., Chan-Li Y., Sokoll L.J., Fung E.T., et al. Quantification of fragments of human serum inter-alpha-trypsin inhibitor heavy chain 4 by a surface-enhanced laser desorption/ionization-based immunoassay. Clin Chem 52 6 (2006) 1045-1053
    • (2006) Clin Chem , vol.52 , Issue.6 , pp. 1045-1053
    • Song, J.1    Patel, M.2    Rosenzweig, C.N.3    Chan-Li, Y.4    Sokoll, L.J.5    Fung, E.T.6
  • 58
    • 34548146655 scopus 로고    scopus 로고
    • Diagnostic biomarkers differentiating metastatic melanoma patients from healthy controls identified by an integrated MALDI-TOF mass spectrometry/bioinformatic approach
    • Matharoo-Ball B.R.L., Lancashire L., Ugurel S., Miles A.K., Weston D.J., Rees R., et al. Diagnostic biomarkers differentiating metastatic melanoma patients from healthy controls identified by an integrated MALDI-TOF mass spectrometry/bioinformatic approach. Proteomics Clin Appl 1 6 (2007) 605-620
    • (2007) Proteomics Clin Appl , vol.1 , Issue.6 , pp. 605-620
    • Matharoo-Ball, B.R.L.1    Lancashire, L.2    Ugurel, S.3    Miles, A.K.4    Weston, D.J.5    Rees, R.6
  • 59
    • 0037180757 scopus 로고    scopus 로고
    • Inflammation and cancer
    • Coussens L.M., and Werb Z. Inflammation and cancer. Nature 420 6917 (2002) 860-867
    • (2002) Nature , vol.420 , Issue.6917 , pp. 860-867
    • Coussens, L.M.1    Werb, Z.2
  • 60
    • 33745298519 scopus 로고    scopus 로고
    • Nuclear factor-kappaB in cancer development and progression
    • Karin M. Nuclear factor-kappaB in cancer development and progression. Nature 441 7092 (2006) 431-436
    • (2006) Nature , vol.441 , Issue.7092 , pp. 431-436
    • Karin, M.1
  • 61
    • 38549085951 scopus 로고    scopus 로고
    • Why cancer and inflammation?
    • Rakoff-Nahoum S. Why cancer and inflammation?. Yale J Biol Med 79 3-4 (2006) 123-130
    • (2006) Yale J Biol Med , vol.79 , Issue.3-4 , pp. 123-130
    • Rakoff-Nahoum, S.1
  • 62
    • 0036915485 scopus 로고    scopus 로고
    • Protein status in pancreatitis-transthyretin is a sensitive biomarker of malnutrition in acute and chronic pancreatitis
    • Lasztity N., Biro L., Nemeth E., Pap A., and Antal M. Protein status in pancreatitis-transthyretin is a sensitive biomarker of malnutrition in acute and chronic pancreatitis. Clin Chem Lab Med 40 12 (2002) 1320-1324
    • (2002) Clin Chem Lab Med , vol.40 , Issue.12 , pp. 1320-1324
    • Lasztity, N.1    Biro, L.2    Nemeth, E.3    Pap, A.4    Antal, M.5
  • 63
    • 0037491109 scopus 로고    scopus 로고
    • The role of visceral proteins in the nutritional assessment of intensive care unit patients
    • Raguso C.A., Dupertuis Y.M., and Pichard C. The role of visceral proteins in the nutritional assessment of intensive care unit patients. Curr Opin Clin Nutr Metab Care 6 2 (2003) 211-216
    • (2003) Curr Opin Clin Nutr Metab Care , vol.6 , Issue.2 , pp. 211-216
    • Raguso, C.A.1    Dupertuis, Y.M.2    Pichard, C.3
  • 64
    • 29444446954 scopus 로고    scopus 로고
    • Protective molecules-C-reactive protein (CRP), serum amyloid P (SAP), pentraxin3 (PTX3), mannose-binding lectin (MBL), and apolipoprotein A1 (Apo A1), and their autoantibodies: prevalence and clinical significance in autoimmunity
    • Kravitz M.S., Pitashny M., and Shoenfeld Y. Protective molecules-C-reactive protein (CRP), serum amyloid P (SAP), pentraxin3 (PTX3), mannose-binding lectin (MBL), and apolipoprotein A1 (Apo A1), and their autoantibodies: prevalence and clinical significance in autoimmunity. J Clin Immunol 25 6 (2005) 582-591
    • (2005) J Clin Immunol , vol.25 , Issue.6 , pp. 582-591
    • Kravitz, M.S.1    Pitashny, M.2    Shoenfeld, Y.3
  • 65
    • 0141739881 scopus 로고    scopus 로고
    • High-density lipoprotein-associated apolipoprotein A-I: the missing link between infection and chronic inflammation?
    • Burger D., and Dayer J.M. High-density lipoprotein-associated apolipoprotein A-I: the missing link between infection and chronic inflammation?. Autoimmun Rev 1 1-2 (2002) 111-117
    • (2002) Autoimmun Rev , vol.1 , Issue.1-2 , pp. 111-117
    • Burger, D.1    Dayer, J.M.2
  • 66
    • 33749327897 scopus 로고    scopus 로고
    • Evaluation of apolipoprotein A1 and posttranslationally modified forms of transthyretin as biomarkers for ovarian cancer detection in an independent study population
    • Moore L.E., Fung E.T., McGuire M., Rabkin C.C., Molinaro A., Wang Z., et al. Evaluation of apolipoprotein A1 and posttranslationally modified forms of transthyretin as biomarkers for ovarian cancer detection in an independent study population. Cancer Epidemiol Biomarkers Prev 15 9 (2006) 1641-1646
    • (2006) Cancer Epidemiol Biomarkers Prev , vol.15 , Issue.9 , pp. 1641-1646
    • Moore, L.E.1    Fung, E.T.2    McGuire, M.3    Rabkin, C.C.4    Molinaro, A.5    Wang, Z.6
  • 67
    • 33645729811 scopus 로고    scopus 로고
    • Identification of serum proteins discriminating colorectal cancer patients and healthy controls using surface-enhanced laser desorption ionisation-time of flight mass spectrometry
    • Engwegen J.Y., Helgason H.H., Cats A., Harris N., Bonfrer J.M., Schellens J.H., et al. Identification of serum proteins discriminating colorectal cancer patients and healthy controls using surface-enhanced laser desorption ionisation-time of flight mass spectrometry. World J Gastroenterol 12 10 (2006) 1536-1544
    • (2006) World J Gastroenterol , vol.12 , Issue.10 , pp. 1536-1544
    • Engwegen, J.Y.1    Helgason, H.H.2    Cats, A.3    Harris, N.4    Bonfrer, J.M.5    Schellens, J.H.6
  • 68
    • 33847120804 scopus 로고    scopus 로고
    • Identification of potential markers for the detection of pancreatic cancer through comparative serum protein expression profiling
    • Ehmann M., Felix K., Hartmann D., Schnolzer M., Nees M., Vorderwulbecke S., et al. Identification of potential markers for the detection of pancreatic cancer through comparative serum protein expression profiling. Pancreas 34 2 (2007) 205-214
    • (2007) Pancreas , vol.34 , Issue.2 , pp. 205-214
    • Ehmann, M.1    Felix, K.2    Hartmann, D.3    Schnolzer, M.4    Nees, M.5    Vorderwulbecke, S.6
  • 69
    • 33646250180 scopus 로고    scopus 로고
    • Biomarker discovery in breast cancer serum using 2-D differential gel electrophoresis/ MALDI-TOF/TOF and data validation by routine clinical assays
    • Huang H.L., Stasyk T., Morandell S., Dieplinger H., Falkensammer G., Griesmacher A., et al. Biomarker discovery in breast cancer serum using 2-D differential gel electrophoresis/ MALDI-TOF/TOF and data validation by routine clinical assays. Electrophoresis 27 8 (2006) 1641-1650
    • (2006) Electrophoresis , vol.27 , Issue.8 , pp. 1641-1650
    • Huang, H.L.1    Stasyk, T.2    Morandell, S.3    Dieplinger, H.4    Falkensammer, G.5    Griesmacher, A.6
  • 70
    • 0038555469 scopus 로고    scopus 로고
    • A strategy for the comparative analysis of serum proteomes for the discovery of biomarkers for hepatocellular carcinoma
    • Steel L.F., Shumpert D., Trotter M., Seeholzer S.H., Evans A.A., London W.T., et al. A strategy for the comparative analysis of serum proteomes for the discovery of biomarkers for hepatocellular carcinoma. Proteomics 3 5 (2003) 601-609
    • (2003) Proteomics , vol.3 , Issue.5 , pp. 601-609
    • Steel, L.F.1    Shumpert, D.2    Trotter, M.3    Seeholzer, S.H.4    Evans, A.A.5    London, W.T.6
  • 71
  • 72
    • 33845611009 scopus 로고    scopus 로고
    • Apolipoprotein CI stimulates the response to lipopolysaccharide and reduces mortality in gram-negative sepsis
    • Berbee J.F., van der Hoogt C.C., Kleemann R., Schippers E.F., Kitchens R.L., van Dissel J.T., et al. Apolipoprotein CI stimulates the response to lipopolysaccharide and reduces mortality in gram-negative sepsis. Faseb J 20 12 (2006) 2162-2164
    • (2006) Faseb J , vol.20 , Issue.12 , pp. 2162-2164
    • Berbee, J.F.1    van der Hoogt, C.C.2    Kleemann, R.3    Schippers, E.F.4    Kitchens, R.L.5    van Dissel, J.T.6
  • 73
    • 5144222255 scopus 로고    scopus 로고
    • Complement: a unique innate immune sensor for danger signals
    • Gasque P. Complement: a unique innate immune sensor for danger signals. Mol Immunol 41 11 (2004) 1089-1098
    • (2004) Mol Immunol , vol.41 , Issue.11 , pp. 1089-1098
    • Gasque, P.1
  • 74
    • 0034861323 scopus 로고    scopus 로고
    • Anaphylatoxins and infectious and non-infectious inflammatory diseases
    • Kohl J. Anaphylatoxins and infectious and non-infectious inflammatory diseases. Mol Immunol 38 2-3 (2001) 175-187
    • (2001) Mol Immunol , vol.38 , Issue.2-3 , pp. 175-187
    • Kohl, J.1
  • 75
    • 28044471999 scopus 로고    scopus 로고
    • Independent validation of candidate breast cancer serum biomarkers identified by mass spectrometry
    • Li J., Orlandi R., White C.N., Rosenzweig J., Zhao J., Seregni E., et al. Independent validation of candidate breast cancer serum biomarkers identified by mass spectrometry. Clin Chem 51 12 (2005) 2229-2235
    • (2005) Clin Chem , vol.51 , Issue.12 , pp. 2229-2235
    • Li, J.1    Orlandi, R.2    White, C.N.3    Rosenzweig, J.4    Zhao, J.5    Seregni, E.6
  • 76
    • 2942542718 scopus 로고    scopus 로고
    • Haptoglobin polymorphisms and iron homeostasis in health and in disease
    • Van Vlierberghe H., Langlois M., and Delanghe J. Haptoglobin polymorphisms and iron homeostasis in health and in disease. Clin Chim Acta 345 1-2 (2004) 35-42
    • (2004) Clin Chim Acta , vol.345 , Issue.1-2 , pp. 35-42
    • Van Vlierberghe, H.1    Langlois, M.2    Delanghe, J.3
  • 77
    • 0033693730 scopus 로고    scopus 로고
    • Haptoglobin: function and polymorphism
    • Wassell J. Haptoglobin: function and polymorphism. Clin Lab 46 11-12 (2000) 547-552
    • (2000) Clin Lab , vol.46 , Issue.11-12 , pp. 547-552
    • Wassell, J.1
  • 78
    • 36749058881 scopus 로고    scopus 로고
    • Glycosylation status of haptoglobin in sera of patients with prostate cancer vs. benign prostate disease or normal subjects
    • Fujimura T., Shinohara Y., Tissot B., Pang P.C., Kurogochi M., Saito S., et al. Glycosylation status of haptoglobin in sera of patients with prostate cancer vs. benign prostate disease or normal subjects. Int J Cancer 122 1 (2008) 39-49
    • (2008) Int J Cancer , vol.122 , Issue.1 , pp. 39-49
    • Fujimura, T.1    Shinohara, Y.2    Tissot, B.3    Pang, P.C.4    Kurogochi, M.5    Saito, S.6
  • 79
    • 37049026705 scopus 로고    scopus 로고
    • Identification of putative serum glycoprotein biomarkers for human lung adenocarcinoma by multilectin affinity chromatography and LC-MS/MS
    • Heo S.H., Lee S.J., Ryoo H.M., Park J.Y., and Cho J.Y. Identification of putative serum glycoprotein biomarkers for human lung adenocarcinoma by multilectin affinity chromatography and LC-MS/MS. Proteomics 7 23 (2007) 4292-4302
    • (2007) Proteomics , vol.7 , Issue.23 , pp. 4292-4302
    • Heo, S.H.1    Lee, S.J.2    Ryoo, H.M.3    Park, J.Y.4    Cho, J.Y.5
  • 80
    • 54049138750 scopus 로고    scopus 로고
    • Differentially expressed serum haptoglobin alpha chain isoforms with potential application for diagnosis of head and neck cancer
    • Chen C.B., Su Y.C., Huang T.T., Ho H.C., Chang Y.T., Tung Y.T., et al. Differentially expressed serum haptoglobin alpha chain isoforms with potential application for diagnosis of head and neck cancer. Clin Chim Acta 398 1-2 (2008) 48-52
    • (2008) Clin Chim Acta , vol.398 , Issue.1-2 , pp. 48-52
    • Chen, C.B.1    Su, Y.C.2    Huang, T.T.3    Ho, H.C.4    Chang, Y.T.5    Tung, Y.T.6
  • 81
    • 36049038546 scopus 로고    scopus 로고
    • Haptoglobin and posttranslational glycan-modified derivatives as serum biomarkers for the diagnosis of nonsmall cell lung cancer
    • Hoagland L.F.T., Campa M.J., Gottlin E.B., Herndon II J.E., and Patz Jr. E.F. Haptoglobin and posttranslational glycan-modified derivatives as serum biomarkers for the diagnosis of nonsmall cell lung cancer. Cancer 110 10 (2007) 2260-2268
    • (2007) Cancer , vol.110 , Issue.10 , pp. 2260-2268
    • Hoagland, L.F.T.1    Campa, M.J.2    Gottlin, E.B.3    Herndon II, J.E.4    Patz Jr., E.F.5
  • 83
    • 0033569982 scopus 로고    scopus 로고
    • Serum amyloid A, the major vertebrate acute-phase reactant
    • Uhlar C.M., and Whitehead A.S. Serum amyloid A, the major vertebrate acute-phase reactant. Eur J Biochem 265 2 (1999) 501-523
    • (1999) Eur J Biochem , vol.265 , Issue.2 , pp. 501-523
    • Uhlar, C.M.1    Whitehead, A.S.2
  • 84
    • 0022480472 scopus 로고
    • Serum amyloid A (SAA) variations in patients with cancer: correlation with disease activity, stage, primary site, and prognosis
    • Biran H., Friedman N., Neumann L., Pras M., and Shainkin-Kestenbaum R. Serum amyloid A (SAA) variations in patients with cancer: correlation with disease activity, stage, primary site, and prognosis. J Clin Pathol 39 7 (1986) 794-797
    • (1986) J Clin Pathol , vol.39 , Issue.7 , pp. 794-797
    • Biran, H.1    Friedman, N.2    Neumann, L.3    Pras, M.4    Shainkin-Kestenbaum, R.5
  • 85
    • 0018718840 scopus 로고
    • Serum amyloid A to monitor cancer dissemination
    • Rosenthal C.J., and Sullivan L.M. Serum amyloid A to monitor cancer dissemination. Ann Intern Med 91 3 (1979) 383-390
    • (1979) Ann Intern Med , vol.91 , Issue.3 , pp. 383-390
    • Rosenthal, C.J.1    Sullivan, L.M.2
  • 86
    • 0021748412 scopus 로고
    • Importance of serum amyloid A (SAA) level in monitoring disease activity and response to therapy in patients with prostate cancer
    • Kaneti J., Winikoff Y., Zimlichman S., and Shainkin-Kestenbaum R. Importance of serum amyloid A (SAA) level in monitoring disease activity and response to therapy in patients with prostate cancer. Urol Res 12 5 (1984) 239-241
    • (1984) Urol Res , vol.12 , Issue.5 , pp. 239-241
    • Kaneti, J.1    Winikoff, Y.2    Zimlichman, S.3    Shainkin-Kestenbaum, R.4
  • 87
    • 0035044124 scopus 로고    scopus 로고
    • Serum amyloid A protein (SAA) in colorectal carcinoma
    • Glojnaric I., Casl M.T., Simic D., and Lukac J. Serum amyloid A protein (SAA) in colorectal carcinoma. Clin Chem Lab Med 39 2 (2001) 129-133
    • (2001) Clin Chem Lab Med , vol.39 , Issue.2 , pp. 129-133
    • Glojnaric, I.1    Casl, M.T.2    Simic, D.3    Lukac, J.4
  • 88
    • 33845619138 scopus 로고    scopus 로고
    • Evaluation of serum amyloid A as a biomarker for gastric cancer
    • Chan D.C., Chen C.J., Chu H.C., Chang W.K., Yu J.C., Chen Y.J., et al. Evaluation of serum amyloid A as a biomarker for gastric cancer. Ann Surg Oncol 14 1 (2007) 84-93
    • (2007) Ann Surg Oncol , vol.14 , Issue.1 , pp. 84-93
    • Chan, D.C.1    Chen, C.J.2    Chu, H.C.3    Chang, W.K.4    Yu, J.C.5    Chen, Y.J.6
  • 90
    • 26844545417 scopus 로고    scopus 로고
    • Distinctive serum protein profiles involving abundant proteins in lung cancer patients based upon antibody microarray analysis
    • Gao W.M., Kuick R., Orchekowski R.P., Misek D.E., Qiu J., Greenberg A.K., et al. Distinctive serum protein profiles involving abundant proteins in lung cancer patients based upon antibody microarray analysis. BMC Cancer 5 (2005) 110
    • (2005) BMC Cancer , vol.5 , pp. 110
    • Gao, W.M.1    Kuick, R.2    Orchekowski, R.P.3    Misek, D.E.4    Qiu, J.5    Greenberg, A.K.6
  • 91
    • 34147220127 scopus 로고    scopus 로고
    • Serum amyloid A protein: a potential biomarker correlated with clinical stage of lung cancer
    • Liu D.H., Wang X.M., Zhang L.J., Dai S.W., Liu L.Y., Liu J.F., et al. Serum amyloid A protein: a potential biomarker correlated with clinical stage of lung cancer. Biomed Environ Sci 20 1 (2007) 33-40
    • (2007) Biomed Environ Sci , vol.20 , Issue.1 , pp. 33-40
    • Liu, D.H.1    Wang, X.M.2    Zhang, L.J.3    Dai, S.W.4    Liu, L.Y.5    Liu, J.F.6
  • 92
    • 1642453766 scopus 로고    scopus 로고
    • Identification of serum amyloid a protein as a potentially useful biomarker to monitor relapse of nasopharyngeal cancer by serum proteomic profiling
    • Cho W.C., Yip T.T., Yip C., Yip V., Thulasiraman V., Ngan R.K., et al. Identification of serum amyloid a protein as a potentially useful biomarker to monitor relapse of nasopharyngeal cancer by serum proteomic profiling. Clin Cancer Res 10 1 Pt 1 (2004) 43-52
    • (2004) Clin Cancer Res , vol.10 , Issue.1 PART 1 , pp. 43-52
    • Cho, W.C.1    Yip, T.T.2    Yip, C.3    Yip, V.4    Thulasiraman, V.5    Ngan, R.K.6
  • 93
    • 16244390914 scopus 로고    scopus 로고
    • Identification of serum amyloid A as a biomarker to distinguish prostate cancer patients with bone lesions
    • Le L., Chi K., Tyldesley S., Flibotte S., Diamond D.L., Kuzyk M.A., et al. Identification of serum amyloid A as a biomarker to distinguish prostate cancer patients with bone lesions. Clin Chem 51 4 (2005) 695-707
    • (2005) Clin Chem , vol.51 , Issue.4 , pp. 695-707
    • Le, L.1    Chi, K.2    Tyldesley, S.3    Flibotte, S.4    Diamond, D.L.5    Kuzyk, M.A.6
  • 94
    • 0031788669 scopus 로고    scopus 로고
    • Widespread expression of serum amyloid A in histologically normal human tissues. Predominant localization to the epithelium
    • Urieli-Shoval S., Cohen P., Eisenberg S., and Matzner Y. Widespread expression of serum amyloid A in histologically normal human tissues. Predominant localization to the epithelium. J Histochem Cytochem 46 12 (1998) 1377-1384
    • (1998) J Histochem Cytochem , vol.46 , Issue.12 , pp. 1377-1384
    • Urieli-Shoval, S.1    Cohen, P.2    Eisenberg, S.3    Matzner, Y.4
  • 95
    • 30044449328 scopus 로고    scopus 로고
    • Expression of serum amyloid A, in normal, dysplastic, and neoplastic human colonic mucosa: implication for a role in colonic tumorigenesis
    • Gutfeld O., Prus D., Ackerman Z., Dishon S., Linke R.P., Levin M., et al. Expression of serum amyloid A, in normal, dysplastic, and neoplastic human colonic mucosa: implication for a role in colonic tumorigenesis. J Histochem Cytochem 54 1 (2006) 63-73
    • (2006) J Histochem Cytochem , vol.54 , Issue.1 , pp. 63-73
    • Gutfeld, O.1    Prus, D.2    Ackerman, Z.3    Dishon, S.4    Linke, R.P.5    Levin, M.6
  • 96
    • 29344437560 scopus 로고    scopus 로고
    • Expression of serum amyloid A transcripts in human trophoblast and fetal-derived trophoblast-like choriocarcinoma cells
    • Kovacevic A., Hammer A., Sundl M., Pfister B., Hrzenjak A., Ray A., et al. Expression of serum amyloid A transcripts in human trophoblast and fetal-derived trophoblast-like choriocarcinoma cells. FEBS Lett 580 1 (2006) 161-167
    • (2006) FEBS Lett , vol.580 , Issue.1 , pp. 161-167
    • Kovacevic, A.1    Hammer, A.2    Sundl, M.3    Pfister, B.4    Hrzenjak, A.5    Ray, A.6
  • 97
    • 72149092979 scopus 로고    scopus 로고
    • Serum amyloid A: an acute-phase protein involved in tumour pathogenesis
    • Malle E., Sodin-Semrl S., and Kovacevic A. Serum amyloid A: an acute-phase protein involved in tumour pathogenesis. Cell Mol Life Sci (2008)
    • (2008) Cell Mol Life Sci
    • Malle, E.1    Sodin-Semrl, S.2    Kovacevic, A.3
  • 98
    • 33750333142 scopus 로고    scopus 로고
    • Molecular interactions of acute phase serum amyloid A: possible involvement in carcinogenesis
    • Vlasova M.A., and Moshkovskii S.A. Molecular interactions of acute phase serum amyloid A: possible involvement in carcinogenesis. Biochemistry (Mosc) 71 10 (2006) 1051-1059
    • (2006) Biochemistry (Mosc) , vol.71 , Issue.10 , pp. 1051-1059
    • Vlasova, M.A.1    Moshkovskii, S.A.2
  • 99
    • 0037441872 scopus 로고    scopus 로고
    • Serum amyloid A induces IL-8 secretion through a G protein-coupled receptor, FPRL1/LXA4R
    • He R., Sang H., and Ye R.D. Serum amyloid A induces IL-8 secretion through a G protein-coupled receptor, FPRL1/LXA4R. Blood 101 4 (2003) 1572-1581
    • (2003) Blood , vol.101 , Issue.4 , pp. 1572-1581
    • He, R.1    Sang, H.2    Ye, R.D.3
  • 100
    • 26444605834 scopus 로고    scopus 로고
    • IKK/NF-kappaB signaling: balancing life and death-a new approach to cancer therapy
    • Luo J.L., Kamata H., and Karin M. IKK/NF-kappaB signaling: balancing life and death-a new approach to cancer therapy. J Clin Invest 115 10 (2005) 2625-2632
    • (2005) J Clin Invest , vol.115 , Issue.10 , pp. 2625-2632
    • Luo, J.L.1    Kamata, H.2    Karin, M.3
  • 101
    • 0034956272 scopus 로고    scopus 로고
    • The role of matrix metalloproteinases in tumor angiogenesis and tumor metastasis
    • John A., and Tuszynski G. The role of matrix metalloproteinases in tumor angiogenesis and tumor metastasis. Pathol Oncol Res 7 1 (2001) 14-23
    • (2001) Pathol Oncol Res , vol.7 , Issue.1 , pp. 14-23
    • John, A.1    Tuszynski, G.2
  • 103
    • 34548440828 scopus 로고    scopus 로고
    • Relation of serum vascular endothelial growth factor as an angiogenesis biomarker with nitric oxide & urokinase-type plasminogen activator in breast cancer patients
    • Konukoglu D., Turhan M.S., Celik V., and Turna H. Relation of serum vascular endothelial growth factor as an angiogenesis biomarker with nitric oxide & urokinase-type plasminogen activator in breast cancer patients. Indian J Med Res 125 6 (2007) 747-751
    • (2007) Indian J Med Res , vol.125 , Issue.6 , pp. 747-751
    • Konukoglu, D.1    Turhan, M.S.2    Celik, V.3    Turna, H.4
  • 104
    • 33644522032 scopus 로고    scopus 로고
    • Urokinase system expression in gastric carcinoma: prognostic impact in an independent patient series and first evidence of predictive value in preoperative biopsy and intestinal metaplasia specimens
    • Beyer B.C., Heiss M.M., Simon E.H., Gruetzner K.U., Babic R., Jauch K.W., et al. Urokinase system expression in gastric carcinoma: prognostic impact in an independent patient series and first evidence of predictive value in preoperative biopsy and intestinal metaplasia specimens. Cancer 106 5 (2006) 1026-1035
    • (2006) Cancer , vol.106 , Issue.5 , pp. 1026-1035
    • Beyer, B.C.1    Heiss, M.M.2    Simon, E.H.3    Gruetzner, K.U.4    Babic, R.5    Jauch, K.W.6
  • 105
    • 33846978442 scopus 로고    scopus 로고
    • Association of the circulating levels of the urokinase system of plasminogen activation with the presence of prostate cancer and invasion, progression, and metastasis
    • Shariat S.F., Roehrborn C.G., McConnell J.D., Park S., Alam N., Wheeler T.M., et al. Association of the circulating levels of the urokinase system of plasminogen activation with the presence of prostate cancer and invasion, progression, and metastasis. J Clin Oncol 25 4 (2007) 349-355
    • (2007) J Clin Oncol , vol.25 , Issue.4 , pp. 349-355
    • Shariat, S.F.1    Roehrborn, C.G.2    McConnell, J.D.3    Park, S.4    Alam, N.5    Wheeler, T.M.6
  • 106
    • 39249085072 scopus 로고    scopus 로고
    • Role of urokinase-type plasminogen activator (uPA) and plasminogen activator inhibitor type 1 (PAI-1) for prognosis in endometrial cancer
    • Steiner E., Pollow K., Hasenclever D., Schormann W., Hermes M., Schmidt M., et al. Role of urokinase-type plasminogen activator (uPA) and plasminogen activator inhibitor type 1 (PAI-1) for prognosis in endometrial cancer. Gynecol Oncol 108 3 (2008) 569-576
    • (2008) Gynecol Oncol , vol.108 , Issue.3 , pp. 569-576
    • Steiner, E.1    Pollow, K.2    Hasenclever, D.3    Schormann, W.4    Hermes, M.5    Schmidt, M.6
  • 107
    • 38649095227 scopus 로고    scopus 로고
    • uPA and PAI-1 in breast cancer: review of their clinical utility and current validation in the prospective NNBC-3 trial
    • Annecke K., Schmitt M., Euler U., Zerm M., Paepke D., Paepke S., et al. uPA and PAI-1 in breast cancer: review of their clinical utility and current validation in the prospective NNBC-3 trial. Adv Clin Chem 45 (2008) 31-45
    • (2008) Adv Clin Chem , vol.45 , pp. 31-45
    • Annecke, K.1    Schmitt, M.2    Euler, U.3    Zerm, M.4    Paepke, D.5    Paepke, S.6
  • 108
    • 0034927828 scopus 로고    scopus 로고
    • Hepatic response to sepsis: interaction between coagulation and inflammatory processes
    • Dhainaut J.F., Marin N., Mignon A., and Vinsonneau C. Hepatic response to sepsis: interaction between coagulation and inflammatory processes. Crit Care Med 29 7 Suppl (2001) S42-S47
    • (2001) Crit Care Med , vol.29 , Issue.7 SUPPL
    • Dhainaut, J.F.1    Marin, N.2    Mignon, A.3    Vinsonneau, C.4
  • 109
    • 54349093030 scopus 로고    scopus 로고
    • Alpha-1 antitrypsin (alpha1-AT) plasma levels in lung, prostate and breast cancer patients
    • El-Akawi Z.J., Al-Hindawi F.K., and Bashir N.A. Alpha-1 antitrypsin (alpha1-AT) plasma levels in lung, prostate and breast cancer patients. Neuro Endocrinol Lett 29 4 (2008)
    • (2008) Neuro Endocrinol Lett , vol.29 , Issue.4
    • El-Akawi, Z.J.1    Al-Hindawi, F.K.2    Bashir, N.A.3
  • 110
    • 48949106841 scopus 로고    scopus 로고
    • Profiling of serum and tissue high abundance acute-phase proteins of patients with epithelial and germ line ovarian carcinoma
    • Chen Y., Lim B.K., Peh S.C., Abdul-Rahman P.S., and Hashim O.H. Profiling of serum and tissue high abundance acute-phase proteins of patients with epithelial and germ line ovarian carcinoma. Proteome Sci 6 (2008) 20
    • (2008) Proteome Sci , vol.6 , pp. 20
    • Chen, Y.1    Lim, B.K.2    Peh, S.C.3    Abdul-Rahman, P.S.4    Hashim, O.H.5
  • 111
    • 12944265461 scopus 로고    scopus 로고
    • Plasma protein profiling for diagnosis of pancreatic cancer reveals the presence of host response proteins
    • Koomen J.M., Shih L.N., Coombes K.R., Li D., Xiao L.C., Fidler I.J., et al. Plasma protein profiling for diagnosis of pancreatic cancer reveals the presence of host response proteins. Clin Cancer Res 11 3 (2005) 1110-1118
    • (2005) Clin Cancer Res , vol.11 , Issue.3 , pp. 1110-1118
    • Koomen, J.M.1    Shih, L.N.2    Coombes, K.R.3    Li, D.4    Xiao, L.C.5    Fidler, I.J.6
  • 112
    • 0036545373 scopus 로고    scopus 로고
    • Novel roles of protease inhibitors in infection and inflammation
    • Hiemstra P.S. Novel roles of protease inhibitors in infection and inflammation. Biochem Soc Trans 30 2 (2002) 116-120
    • (2002) Biochem Soc Trans , vol.30 , Issue.2 , pp. 116-120
    • Hiemstra, P.S.1
  • 113
    • 0025125477 scopus 로고
    • Regulation of antitrypsin and antichymotrypsin synthesis by MCF-7 breast cancer cell sublines
    • Tamir S., Kadner S.S., Katz J., and Finlay T.H. Regulation of antitrypsin and antichymotrypsin synthesis by MCF-7 breast cancer cell sublines. Endocrinology 127 3 (1990) 1319-1328
    • (1990) Endocrinology , vol.127 , Issue.3 , pp. 1319-1328
    • Tamir, S.1    Kadner, S.S.2    Katz, J.3    Finlay, T.H.4
  • 114
    • 1342287837 scopus 로고    scopus 로고
    • Role of imbalance between neutrophil elastase and alpha 1-antitrypsin in cancer development and progression
    • Sun Z., and Yang P. Role of imbalance between neutrophil elastase and alpha 1-antitrypsin in cancer development and progression. Lancet Oncol 5 3 (2004) 182-190
    • (2004) Lancet Oncol , vol.5 , Issue.3 , pp. 182-190
    • Sun, Z.1    Yang, P.2
  • 115
    • 0023182270 scopus 로고
    • Distribution of alpha-1-antitrypsin and haptoglobin phenotypes in bladder cancer patients
    • Benkmann H.G., Hanssen H.P., Ovenbeck R., and Goedde H.W. Distribution of alpha-1-antitrypsin and haptoglobin phenotypes in bladder cancer patients. Hum Hered 37 5 (1987) 290-293
    • (1987) Hum Hered , vol.37 , Issue.5 , pp. 290-293
    • Benkmann, H.G.1    Hanssen, H.P.2    Ovenbeck, R.3    Goedde, H.W.4
  • 116
    • 0028180987 scopus 로고
    • The acute-phase protein alpha 1-antitrypsin inhibits growth and proliferation of human early erythroid progenitor cells (burst-forming units-erythroid) and of human erythroleukemic cells (K562) in vitro by interfering with transferrin iron uptake
    • Graziadei I., Gaggl S., Kaserbacher R., Braunsteiner H., and Vogel W. The acute-phase protein alpha 1-antitrypsin inhibits growth and proliferation of human early erythroid progenitor cells (burst-forming units-erythroid) and of human erythroleukemic cells (K562) in vitro by interfering with transferrin iron uptake. Blood 83 1 (1994) 260-268
    • (1994) Blood , vol.83 , Issue.1 , pp. 260-268
    • Graziadei, I.1    Gaggl, S.2    Kaserbacher, R.3    Braunsteiner, H.4    Vogel, W.5
  • 117
    • 0031042878 scopus 로고    scopus 로고
    • Alpha 1-antitrypsin blocks the release of transforming growth factor-alpha from MCF-7 human breast cancer cells
    • Yavelow J., Tuccillo A., Kadner S.S., Katz J., and Finlay T.H. Alpha 1-antitrypsin blocks the release of transforming growth factor-alpha from MCF-7 human breast cancer cells. J Clin Endocrinol Metab 82 3 (1997) 745-752
    • (1997) J Clin Endocrinol Metab , vol.82 , Issue.3 , pp. 745-752
    • Yavelow, J.1    Tuccillo, A.2    Kadner, S.S.3    Katz, J.4    Finlay, T.H.5
  • 118
    • 34248658381 scopus 로고    scopus 로고
    • alpha-1 antitrypsin inhibits caspase-3 activity, preventing lung endothelial cell apoptosis
    • Petrache I., Fijalkowska I., Medler T.R., Skirball J., Cruz P., Zhen L., et al. alpha-1 antitrypsin inhibits caspase-3 activity, preventing lung endothelial cell apoptosis. Am J Pathol 169 4 (2006) 1155-1166
    • (2006) Am J Pathol , vol.169 , Issue.4 , pp. 1155-1166
    • Petrache, I.1    Fijalkowska, I.2    Medler, T.R.3    Skirball, J.4    Cruz, P.5    Zhen, L.6
  • 119
    • 0035200247 scopus 로고    scopus 로고
    • Alpha-1-antitrypsin stimulates fibroblast proliferation and procollagen production and activates classical MAP kinase signalling pathways
    • Dabbagh K., Laurent G.J., Shock A., Leoni P., Papakrivopoulou J., and Chambers R.C. Alpha-1-antitrypsin stimulates fibroblast proliferation and procollagen production and activates classical MAP kinase signalling pathways. J Cell Physiol 186 1 (2001) 73-81
    • (2001) J Cell Physiol , vol.186 , Issue.1 , pp. 73-81
    • Dabbagh, K.1    Laurent, G.J.2    Shock, A.3    Leoni, P.4    Papakrivopoulou, J.5    Chambers, R.C.6
  • 120
    • 0036910380 scopus 로고    scopus 로고
    • Transthyretin as a thyroid hormone carrier: function revisited
    • Palha J.A. Transthyretin as a thyroid hormone carrier: function revisited. Clin Chem Lab Med 40 12 (2002) 1292-1300
    • (2002) Clin Chem Lab Med , vol.40 , Issue.12 , pp. 1292-1300
    • Palha, J.A.1
  • 121
    • 0027998527 scopus 로고
    • Transthyretin (prealbumin) in health and disease: nutritional implications
    • Ingenbleek Y., and Young V. Transthyretin (prealbumin) in health and disease: nutritional implications. Annu Rev Nutr 14 (1994) 495-533
    • (1994) Annu Rev Nutr , vol.14 , pp. 495-533
    • Ingenbleek, Y.1    Young, V.2
  • 122
    • 0036918569 scopus 로고    scopus 로고
    • Transthyretin: its response to malnutrition and stress injury. Clinical usefulness and economic implications
    • Bernstein L.H., and Ingenbleek Y. Transthyretin: its response to malnutrition and stress injury. Clinical usefulness and economic implications. Clin Chem Lab Med 40 12 (2002) 1344-1348
    • (2002) Clin Chem Lab Med , vol.40 , Issue.12 , pp. 1344-1348
    • Bernstein, L.H.1    Ingenbleek, Y.2
  • 124
    • 0028006184 scopus 로고
    • Plasma prealbumin in women with epithelial ovarian carcinoma
    • Mahlck C.G., and Grankvist K. Plasma prealbumin in women with epithelial ovarian carcinoma. Gynecol Obstet Invest 37 2 (1994) 135-140
    • (1994) Gynecol Obstet Invest , vol.37 , Issue.2 , pp. 135-140
    • Mahlck, C.G.1    Grankvist, K.2
  • 125
    • 34250190259 scopus 로고    scopus 로고
    • Nutritional assessment using prealbumin as an objective criterion to determine whom should not undergo primary radical cytoreductive surgery for ovarian cancer
    • Geisler J.P., Linnemeier G.C., Thomas A.J., and Manahan K.J. Nutritional assessment using prealbumin as an objective criterion to determine whom should not undergo primary radical cytoreductive surgery for ovarian cancer. Gynecol Oncol 106 1 (2007) 128-131
    • (2007) Gynecol Oncol , vol.106 , Issue.1 , pp. 128-131
    • Geisler, J.P.1    Linnemeier, G.C.2    Thomas, A.J.3    Manahan, K.J.4
  • 126
    • 34848815681 scopus 로고    scopus 로고
    • Diagnostic accuracy of MALDI mass spectrometric analysis of unfractionated serum in lung cancer
    • Yildiz P.B., Shyr Y., Rahman J.S., Wardwell N.R., Zimmerman L.J., Shakhtour B., et al. Diagnostic accuracy of MALDI mass spectrometric analysis of unfractionated serum in lung cancer. J Thorac Oncol 2 10 (2007) 893-901
    • (2007) J Thorac Oncol , vol.2 , Issue.10 , pp. 893-901
    • Yildiz, P.B.1    Shyr, Y.2    Rahman, J.S.3    Wardwell, N.R.4    Zimmerman, L.J.5    Shakhtour, B.6
  • 127
    • 0036201712 scopus 로고    scopus 로고
    • Decreased expression of retinol-binding proteins is associated with malignant transformation of the ovarian surface epithelium
    • Roberts D., Williams S.J., Cvetkovic D., Weinstein J.K., Godwin A.K., Johnson S.W., et al. Decreased expression of retinol-binding proteins is associated with malignant transformation of the ovarian surface epithelium. DNA Cell Biol 21 1 (2002) 11-19
    • (2002) DNA Cell Biol , vol.21 , Issue.1 , pp. 11-19
    • Roberts, D.1    Williams, S.J.2    Cvetkovic, D.3    Weinstein, J.K.4    Godwin, A.K.5    Johnson, S.W.6
  • 128
    • 0035847006 scopus 로고    scopus 로고
    • Biochemical basis for depressed serum retinol levels in transthyretin-deficient mice
    • van Bennekum A.M., Wei S., Gamble M.V., Vogel S., Piantedosi R., Gottesman M., et al. Biochemical basis for depressed serum retinol levels in transthyretin-deficient mice. J Biol Chem 276 2 (2001) 1107-1113
    • (2001) J Biol Chem , vol.276 , Issue.2 , pp. 1107-1113
    • van Bennekum, A.M.1    Wei, S.2    Gamble, M.V.3    Vogel, S.4    Piantedosi, R.5    Gottesman, M.6
  • 129
    • 13544254423 scopus 로고    scopus 로고
    • Transferrin: structure, function and potential therapeutic actions
    • Gomme P.T., McCann K.B., and Bertolini J. Transferrin: structure, function and potential therapeutic actions. Drug Discov Today 10 4 (2005) 267-273
    • (2005) Drug Discov Today , vol.10 , Issue.4 , pp. 267-273
    • Gomme, P.T.1    McCann, K.B.2    Bertolini, J.3
  • 130
    • 0023722893 scopus 로고
    • Transferrin synthesis by small cell lung cancer cells acts as an autocrine regulator of cellular proliferation
    • Vostrejs M., Moran P.L., and Seligman P.A. Transferrin synthesis by small cell lung cancer cells acts as an autocrine regulator of cellular proliferation. J Clin Invest 82 1 (1988) 331-339
    • (1988) J Clin Invest , vol.82 , Issue.1 , pp. 331-339
    • Vostrejs, M.1    Moran, P.L.2    Seligman, P.A.3
  • 131
    • 0023944351 scopus 로고
    • Transferrin-like autocrine growth factor, derived from T-lymphoma cells, that inhibits normal T-cell proliferation
    • Morrone G., Corbo L., Turco M.C., Pizzano R., De Felice M., Bridges S., et al. Transferrin-like autocrine growth factor, derived from T-lymphoma cells, that inhibits normal T-cell proliferation. Cancer Res 48 12 (1988) 3425-3429
    • (1988) Cancer Res , vol.48 , Issue.12 , pp. 3425-3429
    • Morrone, G.1    Corbo, L.2    Turco, M.C.3    Pizzano, R.4    De Felice, M.5    Bridges, S.6
  • 132
    • 10744233523 scopus 로고    scopus 로고
    • Transferrin ensures survival of ovarian carcinoma cells when apoptosis is induced by TNFalpha, FasL, TRAIL, or Myc
    • Fassl S., Leisser C., Huettenbrenner S., Maier S., Rosenberger G., Strasser S., et al. Transferrin ensures survival of ovarian carcinoma cells when apoptosis is induced by TNFalpha, FasL, TRAIL, or Myc. Oncogene 22 51 (2003) 8343-8355
    • (2003) Oncogene , vol.22 , Issue.51 , pp. 8343-8355
    • Fassl, S.1    Leisser, C.2    Huettenbrenner, S.3    Maier, S.4    Rosenberger, G.5    Strasser, S.6
  • 133
    • 0030864073 scopus 로고    scopus 로고
    • Transferrin promotes endothelial cell migration and invasion: implication in cartilage neovascularization
    • Carlevaro M.F., Albini A., Ribatti D., Gentili C., Benelli R., Cermelli S., et al. Transferrin promotes endothelial cell migration and invasion: implication in cartilage neovascularization. J Cell Biol 136 6 (1997) 1375-1384
    • (1997) J Cell Biol , vol.136 , Issue.6 , pp. 1375-1384
    • Carlevaro, M.F.1    Albini, A.2    Ribatti, D.3    Gentili, C.4    Benelli, R.5    Cermelli, S.6
  • 134
    • 28444458895 scopus 로고    scopus 로고
    • Proteomic tracking of serum protein isoforms as screening biomarkers of ovarian cancer
    • Ahmed N., Oliva K.T., Barker G., Hoffmann P., Reeve S., Smith I.A., et al. Proteomic tracking of serum protein isoforms as screening biomarkers of ovarian cancer. Proteomics 5 17 (2005) 4625-4636
    • (2005) Proteomics , vol.5 , Issue.17 , pp. 4625-4636
    • Ahmed, N.1    Oliva, K.T.2    Barker, G.3    Hoffmann, P.4    Reeve, S.5    Smith, I.A.6
  • 135
    • 33646067439 scopus 로고    scopus 로고
    • Towards novel anti-cancer strategies based on cystatin function
    • Keppler D. Towards novel anti-cancer strategies based on cystatin function. Cancer Lett 235 2 (2006) 159-176
    • (2006) Cancer Lett , vol.235 , Issue.2 , pp. 159-176
    • Keppler, D.1
  • 136
    • 0028138577 scopus 로고
    • Serum cystatin C, determined by a rapid, automated particle-enhanced turbidimetric method, is a better marker than serum creatinine for glomerular filtration rate
    • Kyhse-Andersen J., Schmidt C., Nordin G., Andersson B., Nilsson-Ehle P., Lindstrom V., et al. Serum cystatin C, determined by a rapid, automated particle-enhanced turbidimetric method, is a better marker than serum creatinine for glomerular filtration rate. Clin Chem 40 10 (1994) 1921-1926
    • (1994) Clin Chem , vol.40 , Issue.10 , pp. 1921-1926
    • Kyhse-Andersen, J.1    Schmidt, C.2    Nordin, G.3    Andersson, B.4    Nilsson-Ehle, P.5    Lindstrom, V.6
  • 137
    • 0031700042 scopus 로고    scopus 로고
    • Serum cystatin C, a new marker of glomerular filtration rate, is increased during malignant progression
    • Kos J., Stabuc B., Cimerman N., and Brunner N. Serum cystatin C, a new marker of glomerular filtration rate, is increased during malignant progression. Clin Chem 44 12 (1998) 2556-2557
    • (1998) Clin Chem , vol.44 , Issue.12 , pp. 2556-2557
    • Kos, J.1    Stabuc, B.2    Cimerman, N.3    Brunner, N.4
  • 138
    • 33847333281 scopus 로고    scopus 로고
    • Cystatin C as a potential marker for relapse in patients with non-Hodgkin B-cell lymphoma
    • Mulaomerovic A., Halilbasic A., Cickusic E., Zavasnik-Bergant T., Begic L., and Kos J. Cystatin C as a potential marker for relapse in patients with non-Hodgkin B-cell lymphoma. Cancer Lett 248 2 (2007) 192-197
    • (2007) Cancer Lett , vol.248 , Issue.2 , pp. 192-197
    • Mulaomerovic, A.1    Halilbasic, A.2    Cickusic, E.3    Zavasnik-Bergant, T.4    Begic, L.5    Kos, J.6
  • 139
    • 12144285600 scopus 로고    scopus 로고
    • Proteases, extracellular matrix, and cancer: a workshop of the path B study section
    • DeClerck Y.A., Mercurio A.M., Stack M.S., Chapman H.A., Zutter M.M., Muschel R.J., et al. Proteases, extracellular matrix, and cancer: a workshop of the path B study section. Am J Pathol 164 4 (2004) 1131-1139
    • (2004) Am J Pathol , vol.164 , Issue.4 , pp. 1131-1139
    • DeClerck, Y.A.1    Mercurio, A.M.2    Stack, M.S.3    Chapman, H.A.4    Zutter, M.M.5    Muschel, R.J.6
  • 140
    • 34648815810 scopus 로고    scopus 로고
    • Emerging roles of proteases in tumour suppression
    • Lopez-Otin C., and Matrisian L.M. Emerging roles of proteases in tumour suppression. Nat Rev Cancer 7 10 (2007) 800-808
    • (2007) Nat Rev Cancer , vol.7 , Issue.10 , pp. 800-808
    • Lopez-Otin, C.1    Matrisian, L.M.2
  • 141
    • 33845267469 scopus 로고    scopus 로고
    • The blood peptidome: a higher dimension of information content for cancer biomarker discovery
    • Petricoin E.F., Belluco C., Araujo R.P., and Liotta L.A. The blood peptidome: a higher dimension of information content for cancer biomarker discovery. Nat Rev Cancer 6 12 (2006) 961-967
    • (2006) Nat Rev Cancer , vol.6 , Issue.12 , pp. 961-967
    • Petricoin, E.F.1    Belluco, C.2    Araujo, R.P.3    Liotta, L.A.4
  • 142
    • 65249087370 scopus 로고    scopus 로고
    • Analysis of the pancreatic tumor progression by a quantitative proteomic approach and immunhistochemical validation
    • Sitek B., Sipos B., Alkatout I., Poschmann G., Stephan C., Schulenborg T., et al. Analysis of the pancreatic tumor progression by a quantitative proteomic approach and immunhistochemical validation. J Proteome Res 8 4 (2009) 1647-1656
    • (2009) J Proteome Res , vol.8 , Issue.4 , pp. 1647-1656
    • Sitek, B.1    Sipos, B.2    Alkatout, I.3    Poschmann, G.4    Stephan, C.5    Schulenborg, T.6
  • 143
    • 23944470664 scopus 로고    scopus 로고
    • Peptidomic analysis of human blood specimens: comparison between plasma specimens and serum by differential peptide display
    • Tammen H., Schulte I., Hess R., Menzel C., Kellmann M., Mohring T., et al. Peptidomic analysis of human blood specimens: comparison between plasma specimens and serum by differential peptide display. Proteomics 5 13 (2005) 3414-3422
    • (2005) Proteomics , vol.5 , Issue.13 , pp. 3414-3422
    • Tammen, H.1    Schulte, I.2    Hess, R.3    Menzel, C.4    Kellmann, M.5    Mohring, T.6
  • 144
    • 34548700125 scopus 로고    scopus 로고
    • Faca V, Krasnoselsky A, Hanash S. Innovative proteomic approaches for cancer biomarker discovery. Biotechniques 2007;43(3):279, 281-3, 285.
    • Faca V, Krasnoselsky A, Hanash S. Innovative proteomic approaches for cancer biomarker discovery. Biotechniques 2007;43(3):279, 281-3, 285.
  • 145
    • 33846001310 scopus 로고    scopus 로고
    • New multi protein patterns differentiate liver fibrosis stages and hepatocellular carcinoma in chronic hepatitis C serum samples
    • Gobel T., Vorderwulbecke S., Hauck K., Fey H., Haussinger D., and Erhardt A. New multi protein patterns differentiate liver fibrosis stages and hepatocellular carcinoma in chronic hepatitis C serum samples. World J Gastroenterol 12 47 (2006) 7604-7612
    • (2006) World J Gastroenterol , vol.12 , Issue.47 , pp. 7604-7612
    • Gobel, T.1    Vorderwulbecke, S.2    Hauck, K.3    Fey, H.4    Haussinger, D.5    Erhardt, A.6
  • 146
    • 34447129750 scopus 로고    scopus 로고
    • Discovery and identification of Serum Amyloid A protein elevated in lung cancer serum
    • Dai S., Wang X., Liu L., Liu J., Wu S., Huang L., et al. Discovery and identification of Serum Amyloid A protein elevated in lung cancer serum. Sci China C Life Sci 50 3 (2007) 305-311
    • (2007) Sci China C Life Sci , vol.50 , Issue.3 , pp. 305-311
    • Dai, S.1    Wang, X.2    Liu, L.3    Liu, J.4    Wu, S.5    Huang, L.6
  • 147
    • 54049083076 scopus 로고    scopus 로고
    • High-abundance polypeptides of the human plasma proteome comprising the top 4 logs of polypeptide abundance
    • Hortin G.L., Sviridov D., and Anderson N.L. High-abundance polypeptides of the human plasma proteome comprising the top 4 logs of polypeptide abundance. Clin Chem 54 10 (2008) 1608-1616
    • (2008) Clin Chem , vol.54 , Issue.10 , pp. 1608-1616
    • Hortin, G.L.1    Sviridov, D.2    Anderson, N.L.3


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.