메뉴 건너뛰기




Volumn 11, Issue 3, 2014, Pages 285-302

Proteomic analysis of tissue samples in translational breast cancer research

Author keywords

breast cancer; gel based proteomics; immunohistochemistry; peptide centric proteomics; protein arrays; tumor heterogeneity

Indexed keywords

BIOLOGICAL MARKER; CYCLOPHILIN A; CYTOCHROME B5; EPIDERMAL GROWTH FACTOR RECEPTOR 2; TAMOXIFEN; TRANSGELIN; PROTEOME; TUMOR MARKER;

EID: 84900991924     PISSN: 14789450     EISSN: 17448387     Source Type: Journal    
DOI: 10.1586/14789450.2014.899469     Document Type: Review
Times cited : (15)

References (147)
  • 2
    • 81555216077 scopus 로고    scopus 로고
    • Gene expression profiling in breast cancer: Classification, prognostication, and prediction
    • Reis-Filho JS, Pusztai L. Gene expression profiling in breast cancer: classification, prognostication, and prediction. Lancet 2011;378(9805):1812-23
    • (2011) Lancet , vol.378 , Issue.9805 , pp. 1812-1823
    • Reis-Filho, J.S.1    Pusztai, L.2
  • 3
    • 84875217358 scopus 로고    scopus 로고
    • A new genome-driven integrated classification of breast cancer and its implications
    • Dawson SJ, Rueda OM, Aparicio S, et al. A new genome-driven integrated classification of breast cancer and its implications. EMBO J 2013;32(5):617-28
    • (2013) EMBO J , vol.32 , Issue.5 , pp. 617-628
    • Dawson, S.J.1    Rueda, O.M.2    Aparicio, S.3
  • 4
    • 84860223306 scopus 로고    scopus 로고
    • Screening for cancer with molecular markers: Progress comes with potential problems
    • Baron JA. Screening for cancer with molecular markers: progress comes with potential problems. Nat Rev Cancer 2012; 12(5):368-71
    • (2012) Nat Rev Cancer , vol.12 , Issue.5 , pp. 368-371
    • Baron, J.A.1
  • 5
    • 84872723383 scopus 로고    scopus 로고
    • Breast cancer biomarker measurements and standards
    • Cole KD, He HJ, Wang L. Breast cancer biomarker measurements and standards. Proteomics Clin Appl 2013;7(1-2):17-29
    • (2013) Proteomics Clin Appl , vol.7 , Issue.1-2 , pp. 17-29
    • Cole, K.D.1    He, H.J.2    Wang, L.3
  • 6
    • 77957833984 scopus 로고    scopus 로고
    • Cancer biomarkers: Can we turn recent failures into success?
    • Diamandis EP. Cancer biomarkers: can we turn recent failures into success? J Natl Cancer Inst 2010;102(19):1462-7
    • (2010) J Natl Cancer Inst , vol.102 , Issue.19 , pp. 1462-1467
    • Diamandis, E.P.1
  • 7
    • 79953032990 scopus 로고    scopus 로고
    • Cancer: Missing the mark
    • Buchen L. Cancer: missing the mark. Nature 2011;471(7339):428-32
    • (2011) Nature , vol.471 , Issue.7339 , pp. 428-432
    • Buchen, L.1
  • 8
    • 80054943335 scopus 로고    scopus 로고
    • Why have protein biomarkers not reached the clinic?
    • Hanash SM. Why have protein biomarkers not reached the clinic? Genome Med 2011; 3(10):66
    • (2011) Genome Med , vol.3 , Issue.10 , pp. 66
    • Hanash, S.M.1
  • 9
    • 84878466403 scopus 로고    scopus 로고
    • Breast cancer biomarkers: Proteomic discovery and translation to clinically relevant samples
    • Chang L, Buxter RC. Breast cancer biomarkers: proteomic discovery and translation to clinically relevant samples. Expert Rev Proteomics 2012;9(6):599-614
    • (2012) Expert Rev Proteomics , vol.9 , Issue.6 , pp. 599-614
    • Chang, L.1    Buxter, R.C.2
  • 10
    • 84864697164 scopus 로고    scopus 로고
    • The failure of protein cancer biomarkers to reach the clinic: Why, and what can be done to address the problem?
    • Diamandis EP. The failure of protein cancer biomarkers to reach the clinic: why, and what can be done to address the problem? BMC Med 2012;10:87
    • (2012) BMC Med , vol.10 , pp. 87
    • Diamandis, E.P.1
  • 11
    • 84870183727 scopus 로고    scopus 로고
    • Proteomic classification of breast cancer
    • Kamel D, Brady B, Tabchy A, et al. Proteomic classification of breast cancer. Curr Drug Targets 2012;13(12):1495-509
    • (2012) Curr Drug Targets , vol.13 , Issue.12 , pp. 1495-1509
    • Kamel, D.1    Brady, B.2    Tabchy, A.3
  • 12
    • 84887108577 scopus 로고    scopus 로고
    • Breast cancer classification by proteomic technologies: Current state of knowledge
    • Lam SW, Jimenez CR, Boven E. Breast cancer classification by proteomic technologies: current state of knowledge. Cancer Treat Rev 2014;40(1):129-38
    • (2014) Cancer Treat Rev , vol.40 , Issue.1 , pp. 129-138
    • Lam, S.W.1    Jimenez, C.R.2    Boven, E.3
  • 13
    • 79955055134 scopus 로고    scopus 로고
    • Proteomics research in breast cancer: Balancing discovery and hypothesis-driven studies
    • Veenstra TD. Proteomics research in breast cancer: balancing discovery and hypothesis-driven studies. Expert Rev Proteomics 2011;8(2):139-41
    • (2011) Expert Rev Proteomics , vol.8 , Issue.2 , pp. 139-141
    • Veenstra, T.D.1
  • 14
    • 81555207451 scopus 로고    scopus 로고
    • Where are all the biomarkers?
    • Veenstra TD. Where are all the biomarkers? Expert Rev Proteomics 2011;8(6):681-3
    • (2011) Expert Rev Proteomics , vol.8 , Issue.6 , pp. 681-683
    • Veenstra, T.D.1
  • 15
    • 67649300635 scopus 로고    scopus 로고
    • Do serum biomarkers really measure breast cancer?
    • Jesneck JL, Mukherjee S, Yurkovetsky Z, et al. Do serum biomarkers really measure breast cancer? BMC Cancer 2009;9:164
    • (2009) BMC Cancer , vol.9 , pp. 164
    • Jesneck, J.L.1    Mukherjee, S.2    Yurkovetsky, Z.3
  • 16
    • 84872017894 scopus 로고    scopus 로고
    • Unleashing the power of proteomics to develop blood-based cancer markers
    • Taguchi A, Hanash SM. Unleashing the power of proteomics to develop blood-based cancer markers. Clin Chem 2013;59(1): 119-26
    • (2013) Clin Chem , vol.59 , Issue.1 , pp. 119-126
    • Taguchi, A.1    Hanash, S.M.2
  • 17
    • 84884407337 scopus 로고    scopus 로고
    • Tumour heterogeneity in the clinic
    • Bedard PL, Hansen AR, Ratain MJ, et al. Tumour heterogeneity in the clinic. Nature 2013;501(7467):355-64
    • (2013) Nature , vol.501 , Issue.7467 , pp. 355-364
    • Bedard, P.L.1    Hansen, A.R.2    Ratain, M.J.3
  • 18
    • 84884377472 scopus 로고    scopus 로고
    • Tumour heterogeneity and cancer cell plasticity
    • Meacham CE, Morrison SJ. Tumour heterogeneity and cancer cell plasticity. Nature 2013;501(7467):328-37
    • (2013) Nature , vol.501 , Issue.7467 , pp. 328-337
    • Meacham, C.E.1    Morrison, S.J.2
  • 19
    • 84884368877 scopus 로고    scopus 로고
    • Influence of tumour micro-environment heterogeneity on therapeutic response
    • Junttila MR, de Sauvage FJ. Influence of tumour micro-environment heterogeneity on therapeutic response. Nature 2013; 501(7467):346-54
    • (2013) Nature , vol.501 , Issue.7467 , pp. 346-354
    • Junttila, M.R.1    De Sauvage, F.J.2
  • 20
    • 84884365015 scopus 로고    scopus 로고
    • The causes and consequences of genetic heterogeneity in cancer evolution
    • Burrell RA, McGranahan N, Bartek J, et al. The causes and consequences of genetic heterogeneity in cancer evolution. Nature 2013;501(7467):338-45
    • (2013) Nature , vol.501 , Issue.7467 , pp. 338-345
    • Burrell, R.A.1    McGranahan, N.2    Bartek, J.3
  • 21
    • 84861527388 scopus 로고    scopus 로고
    • The genomic and transcriptomic architecture of 2 000 breast tumours reveals novel subgroups
    • Curtis C, Shah SP, Chin S-F, et al. The genomic and transcriptomic architecture of 2, 000 breast tumours reveals novel subgroups. Nature 2012;486(7403):346-52
    • (2012) Nature , vol.486 , Issue.7403 , pp. 346-352
    • Curtis, C.1    Shah, S.P.2    Chin, S.-F.3
  • 22
    • 84867082692 scopus 로고    scopus 로고
    • Breast cancer intratumor genetic heterogeneity: Causes and implications
    • Ng CK, Pemberton HN, Reis-Filho JS. Breast cancer intratumor genetic heterogeneity: causes and implications. Expert Rev Anticancer Ther 2012;12(8): 1021-32
    • (2012) Expert Rev Anticancer Ther , vol.12 , Issue.8 , pp. 1021-1032
    • Ng, C.K.1    Pemberton, H.N.2    Reis-Filho, J.S.3
  • 24
    • 84873474915 scopus 로고    scopus 로고
    • Heterogeneity of neoplastic stem cells: Theoretical functional and clinical implications
    • Valent P, Bonnet D, Wohrer S, et al. Heterogeneity of neoplastic stem cells: theoretical, functional, and clinical implications. Cancer Res 2013;73(3): 1037-45
    • (2013) Cancer Res , vol.73 , Issue.3 , pp. 1037-1045
    • Valent, P.1    Bonnet, D.2    Wohrer, S.3
  • 25
    • 38849181724 scopus 로고    scopus 로고
    • Contaminating cells alter gene signatures in whole organ versus laser capture microdissected tumors: A comparison of experimental breast cancers and their lymph node metastases
    • Harrell J C, Dye WW, Harvell DM, et al. Contaminating cells alter gene signatures in whole organ versus laser capture microdissected tumors: a comparison of experimental breast cancers and their lymph node metastases. Clin Exp Metastasis 2008; 25(1):81-8
    • (2008) Clin Exp Metastasis , vol.25 , Issue.1 , pp. 81-88
    • Harrell, J.C.1    Dye, W.W.2    Harvell, D.M.3
  • 26
    • 82355171048 scopus 로고    scopus 로고
    • Reduction of preanalytical variability in specimen procurement for molecular profiling
    • Espina V, Mueller C. Reduction of preanalytical variability in specimen procurement for molecular profiling. Methods Mol Biol 2012;823:49-57
    • (2012) Methods Mol Biol , vol.823 , pp. 49-57
    • Espina, V.1    Mueller, C.2
  • 27
    • 79953072078 scopus 로고    scopus 로고
    • The use of formalin fixed wax embedded tissue for proteomic analysis
    • Ralton LD, Murray GI. The use of formalin fixed wax embedded tissue for proteomic analysis. J Clin Pathol 2011; 64(4):297-302
    • (2011) J Clin Pathol , vol.64 , Issue.4 , pp. 297-302
    • Ralton, L.D.1    Murray, G.I.2
  • 28
    • 84876136632 scopus 로고    scopus 로고
    • Proteomics studies of formalin-fixed paraffin-embedded tissues
    • Giusti L, Lucacchini A. Proteomics studies of formalin-fixed paraffin-embedded tissues. Expert Rev Proteomics 2013;10(2):165-77
    • (2013) Expert Rev Proteomics , vol.10 , Issue.2 , pp. 165-177
    • Giusti, L.1    Lucacchini, A.2
  • 29
    • 71049141298 scopus 로고    scopus 로고
    • Equivalence of protein inventories obtained from formalin-fixed paraffin-embedded and frozen tissue in multidimensional liquid chromatography-tandem mass spectrometry shotgun proteomic analysis
    • Sprung RW Jr, Brock JW, Tanksley JP. Equivalence of protein inventories obtained from formalin-fixed paraffin-embedded and frozen tissue in multidimensional liquid chromatography-tandem mass spectrometry shotgun proteomic analysis. Mol Cell Proteomics 2009;8(8):1988-98
    • (2009) Mol Cell Proteomics , vol.8 , Issue.8 , pp. 1988-1998
    • Sprung Jr., R.W.1    Brock, J.W.2    Tanksley, J.P.3
  • 30
    • 4344577410 scopus 로고    scopus 로고
    • Laser capture microdissection and advanced molecular analysis of human breast cancer
    • Fuller AP, Palmer-Toy D, Erlander MG, et al. Laser capture microdissection and advanced molecular analysis of human breast cancer. J Mammary Gland Biol Neoplasia 2003;8(3):335-45
    • (2003) J Mammary Gland Biol Neoplasia , vol.8 , Issue.3 , pp. 335-345
    • Fuller, A.P.1    Palmer-Toy, D.2    Erlander, M.G.3
  • 31
    • 64649085620 scopus 로고    scopus 로고
    • Application of laser microdissection and reverse-phase protein microarrays to the molecular profiling of cancer signal pathway networks in the tissue microenvironment
    • Espina V, Wulfkuhle J, Liotta LA. Application of laser microdissection and reverse-phase protein microarrays to the molecular profiling of cancer signal pathway networks in the tissue microenvironment. Clin Lab Med 2009;29:1-13
    • (2009) Clin Lab Med , vol.29 , pp. 1-13
    • Espina, V.1    Wulfkuhle, J.2    Liotta, L.A.3
  • 32
    • 84865793194 scopus 로고    scopus 로고
    • Proteomics pipeline for biomarker discovery of laser capture microdissected breast cancer tissue
    • Liu NQ, Braakman RB, Stingl C, et al. Proteomics pipeline for biomarker discovery of laser capture microdissected breast cancer tissue. J Mammary Gland Biol Neoplasia 2012;17(2):155-64
    • (2012) J Mammary Gland Biol Neoplasia , vol.17 , Issue.2 , pp. 155-164
    • Liu, N.Q.1    Braakman, R.B.2    Stingl, C.3
  • 33
    • 56349132718 scopus 로고    scopus 로고
    • A single lysis solution for the analysis of tissue samples by different proteomic technologies
    • Gromov P, Celis JE, Gromova I, et al. A single lysis solution for the analysis of tissue samples by different proteomic technologies. Mol Oncol 2008;2(4):368-79
    • (2008) Mol Oncol , vol.2 , Issue.4 , pp. 368-379
    • Gromov, P.1    Celis, J.E.2    Gromova, I.3
  • 34
    • 58149345546 scopus 로고    scopus 로고
    • Co-evolution of tumor cells and their microenvironment
    • Polyak K, Haviv I, Campbell IG. Co-evolution of tumor cells and their microenvironment. Trends Genet 2009; 25(1):30-8
    • (2009) Trends Genet , vol.25 , Issue.1 , pp. 30-38
    • Polyak, K.1    Haviv, I.2    Campbell, I.G.3
  • 35
    • 67549125238 scopus 로고    scopus 로고
    • Gene expression profiling of the tumor microenvironment during breast cancer progression
    • Ma XJ, Dahiya S, Richardson E, et al. Gene expression profiling of the tumor microenvironment during breast cancer progression. Breast Cancer Res 2009;11(1): R7
    • (2009) Breast Cancer Res , vol.11 , Issue.1
    • Ma, X.J.1    Dahiya, S.2    Richardson, E.3
  • 36
    • 80053401068 scopus 로고    scopus 로고
    • Breast cancer stem cells, cytokine networks, and the tumor microenvironment
    • Korkaya H, Liu S, Wicha MS. Breast cancer stem cells, cytokine networks, and the tumor microenvironment. J Clin Invest 2011;121:3804-9
    • (2011) J Clin Invest , vol.121 , pp. 3804-3809
    • Korkaya, H.1    Liu, S.2    Wicha, M.S.3
  • 37
    • 84884316078 scopus 로고    scopus 로고
    • Cancer stem cells and niche mircoenvironments
    • Boral D, Nie D. Cancer stem cells and niche mircoenvironments. Front Biosci (Elite Ed) 2012;4:2502-14
    • (2012) Front Biosci (Elite Ed) , vol.4 , pp. 2502-2514
    • Boral, D.1    Nie, D.2
  • 38
    • 84884671789 scopus 로고    scopus 로고
    • Tumor interstitial fluid-a treasure trove of cancer biomarkers
    • Gromov P, Gromova I, Olsen CJ, et al. Tumor interstitial fluid-a treasure trove of cancer biomarkers. Biochim Biophys Acta 2013;1834(11):2259-70
    • (2013) Biochim Biophys Acta , vol.1834 , Issue.11 , pp. 2259-2270
    • Gromov, P.1    Gromova, I.2    Olsen, C.J.3
  • 39
    • 84884675370 scopus 로고    scopus 로고
    • Interstitial fluid-a reflection of the tumor cell microenvironment and secretome
    • Haslene-Hox H, Tenstad O, Wiig H. Interstitial fluid-a reflection of the tumor cell microenvironment and secretome. Biochim Biophys Acta 2013;1834(11): 2347-59
    • (2013) Biochim Biophys Acta , vol.11 , Issue.1834 , pp. 2347-2359
    • Haslene-Hox, H.1    Tenstad, O.2    Wiig, H.3
  • 40
    • 33845572150 scopus 로고    scopus 로고
    • Human body fluid proteome analysis
    • Hu S, Loo JA, Wong DT. Human body fluid proteome analysis. Proteomics 2006; 6(23):6326-53
    • (2006) Proteomics , vol.6 , Issue.23 , pp. 6326-6353
    • Hu, S.1    Loo, J.A.2    Wong, D.T.3
  • 41
    • 2542612884 scopus 로고    scopus 로고
    • Proteomic characterization of the interstitial fluid perfusing the breast tumor microenvironment: A novel resource for biomarker and therapeutic target discovery
    • Celis JE, Gromov P, Cabezón T, et al. Proteomic characterization of the interstitial fluid perfusing the breast tumor microenvironment: a novel resource for biomarker and therapeutic target discovery. Mol Cell Proteomics 2004;3(4):327-44
    • (2004) Mol Cell Proteomics , vol.3 , Issue.4 , pp. 327-344
    • Celis, J.E.1    Gromov, P.2    Cabezón, T.3
  • 42
    • 17844379227 scopus 로고    scopus 로고
    • Identification of extracellular and intracellular signaling components of the mammary adipose tissue and its interstitial fluid in high risk breast cancer patients: Toward dissecting the molecular circuitry of epithelial-adipocyte stromal cell interactions
    • Celis JE, Moreira JM, Cabezón T, et al. Identification of extracellular and intracellular signaling components of the mammary adipose tissue and its interstitial fluid in high risk breast cancer patients: toward dissecting the molecular circuitry of epithelial-adipocyte stromal cell interactions. Mol Cell Proteomics 2005;4(4):492-522
    • (2005) Mol Cell Proteomics , vol.4 , Issue.4 , pp. 492-522
    • Celis, J.E.1    Moreira, J.M.2    Cabezón, T.3
  • 43
    • 72549105117 scopus 로고    scopus 로고
    • Up-regulated proteins in the fluid bathing the tumour cell microenvironment as potential serological markers for early detection of cancer of the breast
    • Gromov P, Gromova I, Bunkenborg J, et al. Up-regulated proteins in the fluid bathing the tumour cell microenvironment as potential serological markers for early detection of cancer of the breast. Mol Oncol 2010;4(1):65-89
    • (2010) Mol Oncol , vol.4 , Issue.1 , pp. 65-89
    • Gromov, P.1    Gromova, I.2    Bunkenborg, J.3
  • 44
    • 33644980249 scopus 로고    scopus 로고
    • The intraductal approach to breast cancer biomarker discovery
    • Dua RS, Isacke CM, Gui GP. The intraductal approach to breast cancer biomarker discovery. J Clin Oncol 2006; 24(7):1209-16
    • (2006) J Clin Oncol , vol.24 , Issue.7 , pp. 1209-1216
    • Dua, R.S.1    Isacke, C.M.2    Gui, G.P.3
  • 45
    • 0033450730 scopus 로고    scopus 로고
    • Biological markers of risk in nipple aspirate fluid are associated with residual cancer and tumour size
    • Sauter ER, Ehya H, Babb J, et al. Biological markers of risk in nipple aspirate fluid are associated with residual cancer and tumour size. Br J Cancer 1999;81(7):1222-7
    • (1999) Br J Cancer , vol.81 , Issue.7 , pp. 1222-1227
    • Sauter, E.R.1    Ehya, H.2    Babb, J.3
  • 46
    • 84880025193 scopus 로고    scopus 로고
    • Resolving breast cancer heterogeneity by searching reliable protein cancer biomarkers in the breast fluid secretome
    • Mannello F, Ligi D. Resolving breast cancer heterogeneity by searching reliable protein cancer biomarkers in the breast fluid secretome. BMC Cancer 2013;13:344
    • (2013) BMC Cancer , vol.13 , pp. 344
    • Mannello, F.1    Ligi, D.2
  • 47
    • 0032948126 scopus 로고    scopus 로고
    • 2D protein electrophoresis: Can it be perfected?
    • Celis JE, Gromov P. 2D protein electrophoresis: can it be perfected? Curr Opin Biotechnol 1999;10(1):16-21
    • (1999) Curr Opin Biotechnol , vol.10 , Issue.1 , pp. 16-21
    • Celis, J.E.1    Gromov, P.2
  • 48
    • 84864137133 scopus 로고    scopus 로고
    • Proteome analysis with classical 2D-PAGE
    • May C, Brosseron F, Pfeiffer K, et al. Proteome analysis with classical 2D-PAGE. Methods Mol Biol 2012;893:37-46
    • (2012) Methods Mol Biol , vol.893 , pp. 37-46
    • May, C.1    Brosseron, F.2    Pfeiffer, K.3
  • 49
    • 84864152580 scopus 로고    scopus 로고
    • Differential proteome analysis using 2D-DIGE
    • May C, Brosseron F, Chartowski P, et al. Differential proteome analysis using 2D-DIGE. Methods Mol Biol 2012;893: 75-82
    • (2012) Methods Mol Biol , vol.893 , pp. 75-82
    • May, C.1    Brosseron, F.2    Chartowski, P.3
  • 51
    • 21244495253 scopus 로고    scopus 로고
    • The development of the DIGE system: 2D fluorescence difference gel analysis technology
    • Marouga R, David S, Hawkins E. The development of the DIGE system: 2D fluorescence difference gel analysis technology. Anal Bioanal Chem 2005; 382(3):669-78
    • (2005) Anal Bioanal Chem , vol.382 , Issue.3 , pp. 669-678
    • Marouga, R.1    David, S.2    Hawkins, E.3
  • 52
    • 75549088492 scopus 로고    scopus 로고
    • Application of 2D-DIGE in cancer proteomics toward personalized medicine
    • Kondo T, Hirohashi S. Application of 2D-DIGE in cancer proteomics toward personalized medicine. Methods Mol Biol 2009;577:135-54
    • (2009) Methods Mol Biol , vol.577 , pp. 135-154
    • Kondo, T.1    Hirohashi, S.2
  • 53
    • 53349167583 scopus 로고    scopus 로고
    • Tissue proteomics for cancer biomarker development: Laser microdissection and 2D-DIGE
    • Kondo T. Tissue proteomics for cancer biomarker development: laser microdissection and 2D-DIGE. BMB Rep 2008;41(9):626-34
    • (2008) BMB Rep , vol.41 , Issue.9 , pp. 626-634
    • Kondo, T.1
  • 54
    • 0037112454 scopus 로고    scopus 로고
    • Proteomics of human breast ductal carcinoma in situ
    • Wulfkuhle JD, Sgroi DC, Krutzsch H, et al. Proteomics of human breast ductal carcinoma in situ. Cancer Res 2002;62(22): 6740-9
    • (2002) Cancer Res , vol.62 , Issue.22 , pp. 6740-6749
    • Wulfkuhle, J.D.1    Sgroi, D.C.2    Krutzsch, H.3
  • 55
    • 0142213550 scopus 로고    scopus 로고
    • High-throughput proteomic analysis of human infiltrating ductal carcinoma of the breast
    • Somiari RI, Sullivan A, Russell S, et al. High-throughput proteomic analysis of human infiltrating ductal carcinoma of the breast. Proteomics 2003;3(10):1863-73
    • (2003) Proteomics , vol.3 , Issue.10 , pp. 1863-1873
    • Somiari, R.I.1    Sullivan, A.2    Russell, S.3
  • 56
    • 33751211815 scopus 로고    scopus 로고
    • Comparative proteome analysis of breast cancer and adjacent normal breast tissues in human
    • Deng SS, Xing TY, Zhou HY, et al. Comparative proteome analysis of breast cancer and adjacent normal breast tissues in human. Genomics Proteomics Bioinformatics 2006;4(3):165-72
    • (2006) Genomics Proteomics Bioinformatics , vol.4 , Issue.3 , pp. 165-172
    • Deng, S.S.1    Xing, T.Y.2    Zhou, H.Y.3
  • 57
    • 78649332349 scopus 로고    scopus 로고
    • Discovery and verification of protein differences between Er positive/Her2/neu negative breast tumor tissue and matched adjacent normal breast tissue
    • Weitzel LR, Byers T, Allen J, et al. Discovery and verification of protein differences between Er positive/Her2/neu negative breast tumor tissue and matched adjacent normal breast tissue. Breast Cancer Res Treat 2010;124(2):297-305
    • (2010) Breast Cancer Res Treat , vol.124 , Issue.2 , pp. 297-305
    • Weitzel, L.R.1    Byers, T.2    Allen, J.3
  • 58
    • 84863596486 scopus 로고    scopus 로고
    • Breast cancer proteomics reveals a positive correlation between glyoxalase 1 expression and high tumor grade
    • Fonseca-Sánchez MA, Rodŕiguez Cuevas S, Mendoza-Hernández G, et al. Breast cancer proteomics reveals a positive correlation between glyoxalase 1 expression and high tumor grade. Int J Oncol 2012;41(2): 670-80
    • (2012) Int J Oncol , vol.41 , Issue.2 , pp. 670-680
    • Fonseca-Sánchez, M.A.1    Rodŕiguez Cuevas, S.2    Mendoza-Hernández, G.3
  • 59
    • 84863235668 scopus 로고    scopus 로고
    • Comparisons of protein expression profiles of different stages of lymh nodes metastasis in breast cancer
    • Lee HH, Lim CA, Cheong YT, et al. Comparisons of protein expression profiles of different stages of lymh nodes metastasis in breast cancer. Int J Bio Sci 2012;8(3): 353-62
    • (2012) Int J Bio Sci , vol.8 , Issue.3 , pp. 353-362
    • Lee, H.H.1    Lim, C.A.2    Cheong, Y.T.3
  • 60
    • 28644439593 scopus 로고    scopus 로고
    • Proteomic study reveals that proteins involved in metabolic and detoxification pathways are highly expressed in HER-2/neu-positive breast cancer
    • Zhang D, Tai LK, Wong LL, et al. Proteomic study reveals that proteins involved in metabolic and detoxification pathways are highly expressed in HER-2/neu-positive breast cancer. Mol Cell Proteomics 2005;4(11):1686-96
    • (2005) Mol Cell Proteomics , vol.4 , Issue.11 , pp. 1686-1696
    • Zhang, D.1    Tai, L.K.2    Wong, L.L.3
  • 61
    • 18844363152 scopus 로고    scopus 로고
    • Proteomics of breast cancer: Enhanced expression of cytokeratin19 in human epidermal growth factor receptor type 2 positive breast tumors
    • Zhang D, Tai LK, Wong LL, et al. Proteomics of breast cancer: enhanced expression of cytokeratin19 in human epidermal growth factor receptor type 2 positive breast tumors. Proteomics 2005;5(7):1797-805
    • (2005) Proteomics , vol.5 , Issue.7 , pp. 1797-1805
    • Zhang, D.1    Tai, L.K.2    Wong, L.L.3
  • 62
    • 38949187296 scopus 로고    scopus 로고
    • Proteomic characterization of differentially expressed proteins in breast cancer: Expression of hnRNP H1, RKIP and GRP78 is strongly associated with HER-2/neu status
    • Zhang D, Tai LK, Wong LL, et al. Proteomic characterization of differentially expressed proteins in breast cancer: expression of hnRNP H1, RKIP and GRP78 is strongly associated with HER-2/neu status. Proteomics Clin Appl 2008;2(1): 99-107
    • (2008) Proteomics Clin Appl , vol.2 , Issue.1 , pp. 99-107
    • Zhang, D.1    Tai, L.K.2    Wong, L.L.3
  • 63
    • 67650388533 scopus 로고    scopus 로고
    • Identification of differentially expressed proteins in triple-negative breast carcinomas using DIGE and mass spectrometry
    • Schulz DM, Böllner C, Thomas G, et al. Identification of differentially expressed proteins in triple-negative breast carcinomas using DIGE and mass spectrometry. J Proteome Res 2009;8(7):3430-8
    • (2009) J Proteome Res , vol.8 , Issue.7 , pp. 3430-3438
    • Schulz, D.M.1    Böllner, C.2    Thomas, G.3
  • 64
    • 53549124106 scopus 로고    scopus 로고
    • Characterisation of tumoral markers correlated with ErbB2 (HER2/Neu) overexpression and metastasis in breast cancer
    • Durán MC, Vega F, Moreno-Bueno G, et al. Characterisation of tumoral markers correlated with ErbB2 (HER2/Neu) overexpression and metastasis in breast cancer. Proteomics Clin Appl 2008;2(9): 1313-26
    • (2008) Proteomics Clin Appl , vol.2 , Issue.9 , pp. 1313-1326
    • Durán, M.C.1    Vega, F.2    Moreno-Bueno, G.3
  • 65
    • 33646556739 scopus 로고    scopus 로고
    • Breast cancer proteomics by laser capture microdissection, sample pooling, 54-cm IPG IEF, and differential iodine radioisotope detection
    • Neubauer H, Clare SE, Kurek R, et al. Breast cancer proteomics by laser capture microdissection, sample pooling, 54-cm IPG IEF, and differential iodine radioisotope detection. Electrophoresis 2006;27(9): 1840-52
    • (2006) Electrophoresis , vol.27 , Issue.9 , pp. 1840-1852
    • Neubauer, H.1    Clare, S.E.2    Kurek, R.3
  • 66
    • 59449107785 scopus 로고    scopus 로고
    • Breast cancer proteomics reveals correlation between estrogen receptor status and differential phosphorylation of PGRMC1
    • Neubauer H, Clare SE, Wozny W, et al. Breast cancer proteomics reveals correlation between estrogen receptor status and differential phosphorylation of PGRMC1. Breast Cancer Res 2008;10(5):R85
    • (2008) Breast Cancer Res , vol.10 , Issue.5
    • Neubauer, H.1    Clare, S.E.2    Wozny, W.3
  • 67
    • 84876927692 scopus 로고    scopus 로고
    • Identification of Potential Glycoprotein Biomarkers in Estrogen Receptor Positive (ER+) and Negative (ER-) Human Breast Cancer Tissues by LC-LTQ/FT-ICR Mass Spectrometry
    • Semaan SM, Wang X, Marshall AG, et al. Identification of Potential Glycoprotein Biomarkers in Estrogen Receptor Positive (ER+) and Negative (ER-) Human Breast Cancer Tissues by LC-LTQ/FT-ICR Mass Spectrometry. J Cancer 2012;3:269-84
    • (2012) J Cancer , vol.3 , pp. 269-284
    • Semaan, S.M.1    Wang, X.2    Marshall, A.G.3
  • 68
    • 84877119709 scopus 로고    scopus 로고
    • Calreticulin expression in infiltrating ductal breast carcinomas: Relationships with disease progression and humoral immune responses
    • Kabbage M, Trimeche M, Bergaoui S, et al. Calreticulin expression in infiltrating ductal breast carcinomas: relationships with disease progression and humoral immune responses. Tumour Biol 2013;34(2):1177-88
    • (2013) Tumour Biol , vol.34 , Issue.2 , pp. 1177-1188
    • Kabbage, M.1    Trimeche, M.2    Bergaoui, S.3
  • 69
    • 37249045988 scopus 로고    scopus 로고
    • Detection of protein alterations in male breast cancer using two dimensional gel electrophoresis and mass spectrometry: The involvement of several pathways in tumorigenesis
    • Chahed K, Kabbage M, Hamrita B, et al. Detection of protein alterations in male breast cancer using two dimensional gel electrophoresis and mass spectrometry: the involvement of several pathways in tumorigenesis. Clin Chim Acta 2008; 388(1-2):106-14
    • (2008) Clin Chim Acta , vol.388 , Issue.1-2 , pp. 106-114
    • Chahed, K.1    Kabbage, M.2    Hamrita, B.3
  • 70
    • 77955465838 scopus 로고    scopus 로고
    • Proteomic profiling of mammary carcinomas identifies C7orf24, a gamma-glutamyl cyclotransferase, as a potential cancer biomarker
    • Gromov P, Gromova I, Friis E, et al. Proteomic profiling of mammary carcinomas identifies C7orf24, a gamma-glutamyl cyclotransferase, as a potential cancer biomarker. J Proteome Res 2010;9(8):3941-53
    • (2010) J Proteome Res , vol.9 , Issue.8 , pp. 3941-3953
    • Gromov, P.1    Gromova, I.2    Friis, E.3
  • 71
    • 57649165218 scopus 로고    scopus 로고
    • Omics-based profiling of carcinoma of the breast and matched regional lymph node metastasis
    • Li J, Gromov P, Gromova I, et al. Omics-based profiling of carcinoma of the breast and matched regional lymph node metastasis. Proteomics 2008;8(23-24): 5038-52
    • (2008) Proteomics , vol.8 , Issue.23-24 , pp. 5038-5052
    • Li, J.1    Gromov, P.2    Gromova, I.3
  • 72
    • 84874046728 scopus 로고    scopus 로고
    • Proteomic profiling of triple-negative breast carcinomas in combination with a three-tier orthogonal technology approach identifies Mage-A4 as potential therapeutic target in estrogen receptor negative breast cancer
    • Cabezón T, Gromova I, Gromov P, et al. Proteomic profiling of triple-negative breast carcinomas in combination with a three-tier orthogonal technology approach identifies Mage-A4 as potential therapeutic target in estrogen receptor negative breast cancer. Mol Cell Proteomics 2013;12(2):381-94
    • (2013) Mol Cell Proteomics , vol.12 , Issue.2 , pp. 381-394
    • Cabezón, T.1    Gromova, I.2    Gromov, P.3
  • 73
    • 55049118192 scopus 로고    scopus 로고
    • 15-prostaglandin dehydrogenase expression alone or in combination with ACSM1 defines a subgroup of the apocrine molecular subtype of breast carcinoma
    • Celis JE, Gromov P, Cabezón T, et al. 15-prostaglandin dehydrogenase expression alone or in combination with ACSM1 defines a subgroup of the apocrine molecular subtype of breast carcinoma. Mol Cell Proteomics 2008;7(10):1795-809
    • (2008) Mol Cell Proteomics , vol.7 , Issue.10 , pp. 1795-1809
    • Celis, J.E.1    Gromov, P.2    Cabezón, T.3
  • 74
    • 67349131843 scopus 로고    scopus 로고
    • Molecular characterization of apocrine carcinoma of the breast: Validation of an apocrine protein signature in a well-defined cohort
    • Celis JE, Cabezón T, Moreira JM, et al. Molecular characterization of apocrine carcinoma of the breast: validation of an apocrine protein signature in a well-defined cohort. Mol Oncol 2009;3(3):220-37
    • (2009) Mol Oncol , vol.3 , Issue.3 , pp. 220-237
    • Celis, J.E.1    Cabezón, T.2    Moreira, J.M.3
  • 75
    • 36549018964 scopus 로고    scopus 로고
    • Identification of a subset of breast carcinomas characterized by expression of cytokeratin 15: Relationship between CK15+ progenitor/amplified cells and pre-malignant lesions and invasive disease
    • Celis JE, Gromova I, Cabezón T, et al. Identification of a subset of breast carcinomas characterized by expression of cytokeratin 15: relationship between CK15+ progenitor/amplified cells and pre-malignant lesions and invasive disease. Mol Oncol 2007;1(3):321-49
    • (2007) Mol Oncol , vol.1 , Issue.3 , pp. 321-349
    • Celis, J.E.1    Gromova, I.2    Cabezón, T.3
  • 76
    • 34248665259 scopus 로고    scopus 로고
    • Characterization of breast precancerous lesions and myoepithelial hyperplasia in sclerosing adenosis with apocrine metaplasia
    • Celis JE, Moreira JM, Gromova I, et al. Characterization of breast precancerous lesions and myoepithelial hyperplasia in sclerosing adenosis with apocrine metaplasia. Mol Oncol 2007;1(1):97-119
    • (2007) Mol Oncol , vol.1 , Issue.1 , pp. 97-119
    • Celis, J.E.1    Moreira, J.M.2    Gromova, I.3
  • 77
    • 33646556150 scopus 로고    scopus 로고
    • Molecular pathology of breast apocrine carcinomas: A protein expression signature specific for benign apocrine metaplasia
    • Celis JE, Gromova I, Gromov P, et al. Molecular pathology of breast apocrine carcinomas: a protein expression signature specific for benign apocrine metaplasia. FEBS Lett 2006;580(12):2935-44
    • (2006) FEBS Lett , vol.580 , Issue.12 , pp. 2935-2944
    • Celis, J.E.1    Gromova, I.2    Gromov, P.3
  • 78
    • 33645467483 scopus 로고    scopus 로고
    • Apocrine cysts of the breast: Biomarkers, origin, enlargement, and relation with cancer phenotype
    • Celis JE, Gromov P, Moreira JM, et al. Apocrine cysts of the breast: biomarkers, origin, enlargement, and relation with cancer phenotype. Mol Cell Proteomics 2006;5(3):462-83
    • (2006) Mol Cell Proteomics , vol.5 , Issue.3 , pp. 462-483
    • Celis, J.E.1    Gromov, P.2    Moreira, J.M.3
  • 79
    • 78349313574 scopus 로고    scopus 로고
    • Tissue proteomics of the human mammary gland: Towards an abridged definition of the molecular phenotypes underlying epithelial normalcy
    • Moreira JM, Cabezon T, Gromova I, et al. Tissue proteomics of the human mammary gland: towards an abridged definition of the molecular phenotypes underlying epithelial normalcy. Mol Oncol 2010;4(6):539-61
    • (2010) Mol Oncol , vol.4 , Issue.6 , pp. 539-561
    • Moreira, J.M.1    Cabezon, T.2    Gromova, I.3
  • 80
    • 84870596405 scopus 로고    scopus 로고
    • Current methods for global proteome identification
    • Vaudel M, Sickmann A, Martens L. Current methods for global proteome identification. Expert Rev Proteomics 2012; 9(5):519-32
    • (2012) Expert Rev Proteomics , vol.9 , Issue.5 , pp. 519-532
    • Vaudel, M.1    Sickmann, A.2    Martens, L.3
  • 81
    • 84876148755 scopus 로고    scopus 로고
    • Protein analysis by shotgun/bottom-up proteomics
    • Zhang Y, Fonslow BR, Shan B, et al. Protein analysis by shotgun/bottom-up proteomics. Chem Rev 2013;113(4): 2343-94
    • (2013) Chem Rev , vol.113 , Issue.4 , pp. 2343-2394
    • Zhang, Y.1    Fonslow, B.R.2    Shan, B.3
  • 82
    • 4444228797 scopus 로고    scopus 로고
    • Proteomic analysis of ductal carcinoma of the breast using laser capture microdissection, LC-MS, and 16O/18O isotopic labeling
    • Zang L, Palmer Toy D, Hancock WS, et al. Proteomic analysis of ductal carcinoma of the breast using laser capture microdissection, LC-MS, and 16O/18O isotopic labeling. J Proteome Res 2004;3(3): 604-12
    • (2004) J Proteome Res , vol.3 , Issue.3 , pp. 604-612
    • Zang, L.1    Palmer Toy, D.2    Hancock, W.S.3
  • 83
    • 79952288667 scopus 로고    scopus 로고
    • ITRAQ protein quantification: A quality-controlled workflow
    • Burkhart JM, Vaudel M, Zahedi RP, et al. iTRAQ protein quantification: a quality-controlled workflow. Proteomics 2011;11(6): 1125-34
    • (2011) Proteomics , vol.11 , Issue.6 , pp. 1125-1134
    • Burkhart, J.M.1    Vaudel, M.2    Zahedi, R.P.3
  • 84
    • 60849093488 scopus 로고    scopus 로고
    • Biomarker discovery in low-grade breast cancer using isobaric stable isotope tags and two-dimensional liquid chromatography tandem mass spectrometry (iTRAQ-2DLC-MS/MS) based quantitative proteomic analysis
    • Bouchal P, Roumeliotis T, Hrstka R, et al. Biomarker discovery in low-grade breast cancer using isobaric stable isotope tags and two-dimensional liquid chromatography tandem mass spectrometry (iTRAQ-2DLC-MS/MS) based quantitative proteomic analysis. J Proteome Res 2009;8(1):362-73
    • (2009) J Proteome Res , vol.8 , Issue.1 , pp. 362-373
    • Bouchal, P.1    Roumeliotis, T.2    Hrstka, R.3
  • 85
    • 84864607976 scopus 로고    scopus 로고
    • Strategy for SRM-based verification of biomarker candidates discovered by iTRAQ method in limited breast cancer tissue samples
    • Muraoka S, Kume H, Watanabe S, et al. Strategy for SRM-based verification of biomarker candidates discovered by iTRAQ method in limited breast cancer tissue samples. J Proteome Res 2012; 11(8): 4201-10
    • (2012) J Proteome Res , vol.11 , Issue.8 , pp. 4201-4210
    • Muraoka, S.1    Kume, H.2    Watanabe, S.3
  • 86
    • 79960396255 scopus 로고    scopus 로고
    • Liquid chromatography-mass spectrometry-based quantitative proteomics
    • Xie F, Liu T, Qian WJ, et al. Liquid chromatography-mass spectrometry-based quantitative proteomics. J Biol Chem 2011; 286(29):25443-9
    • (2011) J Biol Chem , vol.286 , Issue.29 , pp. 25443-25449
    • Xie, F.1    Liu, T.2    Qian, W.J.3
  • 87
    • 78149289532 scopus 로고    scopus 로고
    • In situ proteomic analysis of human breast cancer epithelial cells using laser capture microdissection: Annotation by protein set enrichment analysis and gene ontology
    • Cha S, Imielinski MB, Rejtar T, et al. In situ proteomic analysis of human breast cancer epithelial cells using laser capture microdissection: annotation by protein set enrichment analysis and gene ontology. Mol Cell Proteomics 2010;9(11):2529-44
    • (2010) Mol Cell Proteomics , vol.9 , Issue.11 , pp. 2529-2544
    • Cha, S.1    Imielinski, M.B.2    Rejtar, T.3
  • 88
    • 79952821017 scopus 로고    scopus 로고
    • Differential protein expression profiles in estrogen receptor-positive and-negative breast cancer tissues using label-free quantitative proteomics
    • Rezaul K, Thumar JK, Lundgren DH, et al. Differential protein expression profiles in estrogen receptor-positive and-negative breast cancer tissues using label-free quantitative proteomics. Genes Cancer 2010;1(3):251-71
    • (2010) Genes Cancer , vol.1 , Issue.3 , pp. 251-271
    • Rezaul, K.1    Thumar, J.K.2    Lundgren, D.H.3
  • 89
    • 33244496389 scopus 로고    scopus 로고
    • Peptidomic analysis of breast cancer reveals a putative surrogate marker for estrogen receptor-negative carcinomas
    • Traub F, Jost M, Hess R, et al. Peptidomic analysis of breast cancer reveals a putative surrogate marker for estrogen receptor-negative carcinomas. Lab Invest 2006;86(3):246-53
    • (2006) Lab Invest , vol.86 , Issue.3 , pp. 246-253
    • Traub, F.1    Jost, M.2    Hess, R.3
  • 90
    • 84862590860 scopus 로고    scopus 로고
    • Proteomic-based biosignatures in breast cancer classification and prediction of therapeutic response
    • He J, Whelan SA, Lu M, et al. Proteomic-based biosignatures in breast cancer classification and prediction of therapeutic response. Int J Proteomics 2011;2011:896476
    • (2011) Int J Proteomics , vol.2011 , pp. 896476
    • He, J.1    Whelan, S.A.2    Lu, M.3
  • 91
    • 84861347783 scopus 로고    scopus 로고
    • Stat1 and CD74 overexpression is co-dependent and linked to increased invasion and lymph node metastasis in triple-negative breast cancer
    • Greenwood C, Metodieva G, Al-Janabi K, et al. Stat1 and CD74 overexpression is co-dependent and linked to increased invasion and lymph node metastasis in triple-negative breast cancer. J Proteomics 2012;75(10):3031-40
    • (2012) J Proteomics , vol.75 , Issue.10 , pp. 3031-3040
    • Greenwood, C.1    Metodieva, G.2    Al-Janabi, K.3
  • 92
    • 84859592979 scopus 로고    scopus 로고
    • Differential proteomic analysis of a human breast tumor and its matched bone metastasis identifies cell membrane and extracellular proteins associated with bone metastasis
    • Dumont B, Castronovo V, Peulen O, et al. Differential proteomic analysis of a human breast tumor and its matched bone metastasis identifies cell membrane and extracellular proteins associated with bone metastasis. J Proteome Res 2012;11(4): 2247-60
    • (2012) J Proteome Res , vol.11 , Issue.4 , pp. 2247-2260
    • Dumont, B.1    Castronovo, V.2    Peulen, O.3
  • 93
    • 80051788545 scopus 로고    scopus 로고
    • Differential phosphopeptide expression in a benign breast tissue and triple-negative primary and metastatic breast cancer tissues from the same African-American woman by LC-LTQ/FT-ICR mass spectrometry
    • Semaan SM, Wang X, Stewart PA, et al. Differential phosphopeptide expression in a benign breast tissue, and triple-negative primary and metastatic breast cancer tissues from the same African-American woman by LC-LTQ/FT-ICR mass spectrometry. Biochem Biophys Res Commun 2011; 412(1):127-31
    • (2011) Biochem Biophys Res Commun , vol.412 , Issue.1 , pp. 127-131
    • Semaan, S.M.1    Wang, X.2    Stewart, P.A.3
  • 94
    • 67650523623 scopus 로고    scopus 로고
    • Identification of a putative protein profile associated with tamoxifen therapy resistance in breast cancer
    • Umar A, Kang H, Timmermans AM, et al. Identification of a putative protein profile associated with tamoxifen therapy resistance in breast cancer. Mol Cell Proteomics 2009; 8(6):1278-94
    • (2009) Mol Cell Proteomics , vol.8 , Issue.6 , pp. 1278-1294
    • Umar, A.1    Kang, H.2    Timmermans, A.M.3
  • 95
    • 84890689655 scopus 로고    scopus 로고
    • Grading breast cancer tissues using molecular portraits
    • Olsson N, Carlsson P, James P, et al. Grading breast cancer tissues using molecular portraits. Mol Cell Proteomics 2013; 12(12):3612-23
    • (2013) Mol Cell Proteomics , vol.12 , Issue.12 , pp. 3612-3623
    • Olsson, N.1    Carlsson, P.2    James, P.3
  • 96
    • 84861811029 scopus 로고    scopus 로고
    • Characterization of breast cancer interstitial fluids by TmT labeling, LTQ-orbitrap velos mass spectrometry, and pathway analysis
    • Raso C, Cosentino C, Gaspari M, et al. Characterization of breast cancer interstitial fluids by TmT labeling, LTQ-orbitrap velos mass spectrometry, and pathway analysis. J Proteome Res 2012;11(6):3199-210
    • (2012) J Proteome Res , vol.11 , Issue.6 , pp. 3199-3210
    • Raso, C.1    Cosentino, C.2    Gaspari, M.3
  • 97
    • 84887083535 scopus 로고    scopus 로고
    • TCPA: A resource for cancer functional proteomics data
    • Li J, Lu Y, Akbani R, et al. TCPA: a resource for cancer functional proteomics data. Nat Methods 2013;10(11):1046-7
    • (2013) Nat Methods , vol.10 , Issue.11 , pp. 1046-1047
    • Li, J.1    Lu, Y.2    Akbani, R.3
  • 98
    • 33746683073 scopus 로고    scopus 로고
    • Applications of antibody array platforms
    • Haab BB. Applications of antibody array platforms. Curr Opin Biotechnol 2006; 17(4):415-21
    • (2006) Curr Opin Biotechnol , vol.17 , Issue.4 , pp. 415-421
    • Haab, B.B.1
  • 99
    • 77954124678 scopus 로고    scopus 로고
    • A biotin label-based antibody array for high-content profiling of protein expression
    • Huang R, Jiang W, Yang J, et al. A biotin label-based antibody array for high-content profiling of protein expression. Cancer Genomics Proteomics 2010;7(3):129-41
    • (2010) Cancer Genomics Proteomics , vol.7 , Issue.3 , pp. 129-141
    • Huang, R.1    Jiang, W.2    Yang, J.3
  • 100
    • 36549067170 scopus 로고    scopus 로고
    • Forward-phase and reverse-phase protein microarray
    • Zong Y, Zhang S, Chen HT, et al. Forward-phase and reverse-phase protein microarray. Methods Mol Biol 2007;381: 363-74
    • (2007) Methods Mol Biol , vol.381 , pp. 363-374
    • Zong, Y.1    Zhang, S.2    Chen, H.T.3
  • 101
    • 34250892135 scopus 로고    scopus 로고
    • The needle in the haystack: Application of breast fine-needle aspirate samples to quantitative protein microarray technology
    • Rapkiewicz A, Espina V, Zujewski JA, et al. The needle in the haystack: application of breast fine-needle aspirate samples to quantitative protein microarray technology. Cancer 2007;111(3):173-84
    • (2007) Cancer , vol.111 , Issue.3 , pp. 173-184
    • Rapkiewicz, A.1    Espina, V.2    Zujewski, J.A.3
  • 102
    • 84934437581 scopus 로고    scopus 로고
    • Reverse phase protein microarrays for clinical applications
    • Pierobon M, Belluco C, Liotta LA, et al. Reverse phase protein microarrays for clinical applications. Methods Mol Biol 2011;785:3-12
    • (2011) Methods Mol Biol , vol.785 , pp. 3-12
    • Pierobon, M.1    Belluco, C.2    Liotta, L.A.3
  • 103
    • 84863615256 scopus 로고    scopus 로고
    • Common protein biomarkers assessed by reverse phase protein arrays show considerable intratumoral heterogeneity in breast cancer tissues
    • Malinowsky K, Raychaudhuri M, Buchner T, et al. Common protein biomarkers assessed by reverse phase protein arrays show considerable intratumoral heterogeneity in breast cancer tissues. PLoS ONE 2012;7(7):e40285
    • (2012) PLoS ONE , vol.7 , Issue.7
    • Malinowsky, K.1    Raychaudhuri, M.2    Buchner, T.3
  • 104
    • 79955941549 scopus 로고    scopus 로고
    • Quantitative proteomic analysis in breast cancer
    • Tabchy A, Hennessy BT, Gonzalez-Angulo AM, et al. Quantitative proteomic analysis in breast cancer. Drugs Today 2011;47(2):169-82
    • (2011) Drugs Today , vol.47 , Issue.2 , pp. 169-182
    • Tabchy, A.1    Hennessy, B.T.2    Gonzalez-Angulo, A.M.3
  • 105
    • 84858268381 scopus 로고    scopus 로고
    • Functional proteomics can define prognosis and predict pathologic complete response in patients with breast cancer
    • Gonzalez-Angulo AM, Hennessy BT, Meric-Bernstam F, et al. Functional proteomics can define prognosis and predict pathologic complete response in patients with breast cancer. Clin Proteomics 2011; 8(1):11
    • (2011) Clin Proteomics , vol.8 , Issue.1 , pp. 11
    • Gonzalez-Angulo, A.M.1    Hennessy, B.T.2    Meric-Bernstam, F.3
  • 106
    • 84884369416 scopus 로고    scopus 로고
    • Multiple protein analysis of formalin-fixed and paraffin-embedded tissue samples with reverse phase protein arrays
    • Assadi M, Lamerz J, Jarutat T, et al. Multiple protein analysis of formalin-fixed and paraffin-embedded tissue samples with reverse phase protein arrays. Mol Cell Proteomics 2013;12(9):2615-22
    • (2013) Mol Cell Proteomics , vol.12 , Issue.9 , pp. 2615-2622
    • Assadi, M.1    Lamerz, J.2    Jarutat, T.3
  • 107
    • 45549107510 scopus 로고    scopus 로고
    • Multiplexed cell signaling analysis of human breast cancer applications for personalized therapy
    • Wulfkuhle JD, Speer R, Pierobon M, et al. Multiplexed cell signaling analysis of human breast cancer applications for personalized therapy. J Proteome Res 2008;7:1508-17
    • (2008) J Proteome Res , vol.7 , pp. 1508-1517
    • Wulfkuhle, J.D.1    Speer, R.2    Pierobon, M.3
  • 108
    • 79955781655 scopus 로고    scopus 로고
    • Protein microarray analysis of mammary epithelial cells from obese and non obese women at high risk for breast cancer: Feasibility data
    • Pilie PG, Ibarra-Drendall C, Troch MM, et al. Protein microarray analysis of mammary epithelial cells from obese and non obese women at high risk for breast cancer: feasibility data. Cancer Epidemiol Biomarkers Prev 2011;20(3):476-82
    • (2011) Cancer Epidemiol Biomarkers Prev , vol.20 , Issue.3 , pp. 476-482
    • Pilie, P.G.1    Ibarra-Drendall, C.2    Troch, M.M.3
  • 109
    • 84859109439 scopus 로고    scopus 로고
    • Pilot and feasibility study: Prospective proteomic profiling of mammary epithelial cells from high-risk women provides evidence of activation of pro-survival pathways
    • Ibarra-Drendall C, Troch MM, Barry WT, et al. Pilot and feasibility study: prospective proteomic profiling of mammary epithelial cells from high-risk women provides evidence of activation of pro-survival pathways. Breast Cancer Res Treat 2012;132:487-98
    • (2012) Breast Cancer Res Treat , vol.132 , pp. 487-498
    • Ibarra-Drendall, C.1    Troch, M.M.2    Barry, W.T.3
  • 110
    • 84855877854 scopus 로고    scopus 로고
    • Proteomic identification of predictive biomarkers of resistance to neoadjuvant chemotherapy in luminal breast cancer: A possible role for 14-3-3 theta/tau and tBID?
    • Hodgkinson VC, ELFadl D, Agarwal V, et al. Proteomic identification of predictive biomarkers of resistance to neoadjuvant chemotherapy in luminal breast cancer: a possible role for 14-3-3 theta/tau and tBID? J Proteomics 2012;75(4):1276-83
    • (2012) J Proteomics , vol.75 , Issue.4 , pp. 1276-1283
    • Hodgkinson, V.C.1    Elfadl, D.2    Agarwal, V.3
  • 111
    • 84875603543 scopus 로고    scopus 로고
    • Functional proteomics characterization of residual breast cancer after neoadjuvant systemic chemotherapy
    • Gonzalez-Angulo AM, Liu S, Chen H, et al. Functional proteomics characterization of residual breast cancer after neoadjuvant systemic chemotherapy. Ann Oncol 2013; 24(4):909-16
    • (2013) Ann Oncol , vol.24 , Issue.4 , pp. 909-916
    • Gonzalez-Angulo, A.M.1    Liu, S.2    Chen, H.3
  • 112
    • 84884706912 scopus 로고    scopus 로고
    • Functional proteomics characterization of residual triple negative breast cancer after standard neoadjuvant chemotherapy
    • Sohn J, Do KA, Liu S, et al. Functional proteomics characterization of residual triple negative breast cancer after standard neoadjuvant chemotherapy. Ann Oncol 2013;24(10):2522-6
    • (2013) Ann Oncol , vol.24 , Issue.10 , pp. 2522-2526
    • Sohn, J.1    Do, K.A.2    Liu, S.3
  • 113
    • 84880917870 scopus 로고    scopus 로고
    • Profiling phospho-signaling networks in breast cancer using reverse-phase protein arrays
    • Gujral TS, Karp RL, Finski A, et al. Profiling phospho-signaling networks in breast cancer using reverse-phase protein arrays. Oncogene 2013;32(29):3470-6
    • (2013) Oncogene , vol.32 , Issue.29 , pp. 3470-3476
    • Gujral, T.S.1    Karp, R.L.2    Finski, A.3
  • 114
    • 84870356223 scopus 로고    scopus 로고
    • Molecular analysis of HER2 signaling in human breast cancer by functional protein pathway activation mapping
    • Wulfkuhle JD, Berg D, Wolff C, et al. Molecular analysis of HER2 signaling in human breast cancer by functional protein pathway activation mapping. Clin Cancer Res 2012;18(23):6426-35
    • (2012) Clin Cancer Res , vol.18 , Issue.23 , pp. 6426-6435
    • Wulfkuhle, J.D.1    Berg, D.2    Wolff, C.3
  • 115
    • 84879385305 scopus 로고    scopus 로고
    • Reverse-phase protein microarray highlights HER2 signaling activation in immunohistochemistry/FISH/HER2-negative breast cancers
    • Tessitore A, Zazzeroni F, Alesse E. Reverse-phase protein microarray highlights HER2 signaling activation in immunohistochemistry/FISH/HER2-negative breast cancers. Expert Rev Proteomics 2013;10(3):223-6
    • (2013) Expert Rev Proteomics , vol.10 , Issue.3 , pp. 223-226
    • Tessitore, A.1    Zazzeroni, F.2    Alesse, E.3
  • 116
    • 84868473530 scopus 로고    scopus 로고
    • Using protein microarrays to study phosphorylation-mediated signal transduction
    • Zhang H, Pelech S. Using protein microarrays to study phosphorylation-mediated signal transduction. Semin Cell Dev Biol 2012; 23(8):872-82
    • (2012) Semin Cell Dev Biol , vol.23 , Issue.8 , pp. 872-882
    • Zhang, H.1    Pelech, S.2
  • 117
    • 0043125601 scopus 로고    scopus 로고
    • Next generation of protein microarray support materials: Evaluation for protein and antibody microarray applications
    • Angenendt P, Glokler J, Sobek J, et al. Next generation of protein microarray support materials: evaluation for protein and antibody microarray applications. J Chromatogr 2003;1009:97-104
    • (2003) J Chromatogr , vol.1009 , pp. 97-104
    • Angenendt, P.1    Glokler, J.2    Sobek, J.3
  • 118
    • 80054737693 scopus 로고    scopus 로고
    • Phosphoprotein stability in clinical tissue and its relevance for reverse phase protein microarray technology
    • Espina V, Mueller C, Liotta LA. Phosphoprotein stability in clinical tissue and its relevance for reverse phase protein microarray technology. Methods Mol Biol 2011;785:23-43
    • (2011) Methods Mol Biol , vol.785 , pp. 23-43
    • Espina, V.1    Mueller, C.2    Liotta, L.A.3
  • 119
    • 84877100156 scopus 로고    scopus 로고
    • Improved data normalization methods for reverse phase protein microarray analysis of complex biological samples
    • Chiechi A, Mueller C, Boehm KM, et al. Improved data normalization methods for reverse phase protein microarray analysis of complex biological samples. Biotechniques 2012;0(0):1-7
    • (2012) Biotechniques , vol.0 , Issue.0 , pp. 1-7
    • Chiechi, A.1    Mueller, C.2    Boehm, K.M.3
  • 120
    • 70449396493 scopus 로고    scopus 로고
    • Tumor proteomic profiling predicts the susceptibility of breast cancer to chemotherapy
    • He J, Shen D, Chung DU, et al. Tumor proteomic profiling predicts the susceptibility of breast cancer to chemotherapy. Int J Oncol 2009;35(4): 683-92
    • (2009) Int J Oncol , vol.35 , Issue.4 , pp. 683-692
    • He, J.1    Shen, D.2    Chung, D.U.3
  • 121
    • 33645462581 scopus 로고    scopus 로고
    • Surface-enhanced laser desorption/ionization time of flight mass spectrometry protein profiling identifies ubiquitin and ferritin light chain as prognostic biomarkers in node-negative breast cancer tumors
    • Ricolleau G, Charbonnel C, Lodé L, et al. Surface-enhanced laser desorption/ionization time of flight mass spectrometry protein profiling identifies ubiquitin and ferritin light chain as prognostic biomarkers in node-negative breast cancer tumors. Proteomics 2006;6(6):1963-75
    • (2006) Proteomics , vol.6 , Issue.6 , pp. 1963-1975
    • Ricolleau, G.1    Charbonnel, C.2    Lodé, L.3
  • 122
    • 33745274130 scopus 로고    scopus 로고
    • Serum proteomic profiling by matrix-assisted laser desorption-ionization time-of-flight mass spectrometry for cancer diagnosis: Next steps
    • Diamandis EP. Serum proteomic profiling by matrix-assisted laser desorption-ionization time-of-flight mass spectrometry for cancer diagnosis: next steps. Cancer Res 2006; 66(11):5540-1
    • (2006) Cancer Res , vol.66 , Issue.11 , pp. 5540-5541
    • Diamandis, E.P.1
  • 123
    • 84890918909 scopus 로고    scopus 로고
    • Advances in MALDI Mass Spectrometry in Clinical Diagnostic Applications
    • Ng EW, Wong MY, Poon TC. Advances in MALDI Mass Spectrometry in Clinical Diagnostic Applications. Top Curr Chem 2014;336:139-75
    • (2014) Top Curr Chem , vol.336 , pp. 139-175
    • Ng, E.W.1    Wong, M.Y.2    Poon, T.C.3
  • 124
    • 0031304362 scopus 로고    scopus 로고
    • Molecular imaging of biological samples: Localization of peptides and proteins using MALDI-TOF MS
    • Caprioli RM, Farmer TB, Gile J. Molecular imaging of biological samples: localization of peptides and proteins using MALDI-TOF MS. Anal Chem 1997; 69(23):4751-60
    • (1997) Anal Chem , vol.69 , Issue.23 , pp. 4751-4760
    • Caprioli, R.M.1    Farmer, T.B.2    Gile, J.3
  • 125
    • 0033485653 scopus 로고    scopus 로고
    • Direct profiling of proteins in biological tissue sections by MALDI mass spectrometry
    • Chaurand P, Stoeckli M, Caprioli RM. Direct profiling of proteins in biological tissue sections by MALDI mass spectrometry. Anal Chem 1999;71(23): 5263-70
    • (1999) Anal Chem , vol.71 , Issue.23 , pp. 5263-5270
    • Chaurand, P.1    Stoeckli, M.2    Caprioli, R.M.3
  • 126
    • 13444304503 scopus 로고    scopus 로고
    • Imaging mass spectrometry: Principles and potentials
    • Chaurand P, Schwartz SA, Reyzer ML, et al. Imaging mass spectrometry: principles and potentials. Toxicol Pathol 2005;33(1): 92-101
    • (2005) Toxicol Pathol , vol.33 , Issue.1 , pp. 92-101
    • Chaurand, P.1    Schwartz, S.A.2    Reyzer, M.L.3
  • 127
    • 84878665861 scopus 로고    scopus 로고
    • Matrix-assisted laser desorption ionization imaging mass spectrometry: In situ molecular mapping
    • Angel PM, Caprioli RM. Matrix-assisted laser desorption ionization imaging mass spectrometry: in situ molecular mapping. Biochemistry 2013;52(22):3818-28
    • (2013) Biochemistry , vol.52 , Issue.22 , pp. 3818-3828
    • Angel, P.M.1    Caprioli, R.M.2
  • 128
    • 84893859018 scopus 로고    scopus 로고
    • Matrix-assited laser desorption ionization mass spectrometry imaging for peptide and protein analysis: A critical review of on tissue digestion
    • Cillero-Pastor B, Heeren RM. Matrix-assited laser desorption ionization mass spectrometry imaging for peptide and protein analysis: a critical review of on tissue digestion. J Proteome Res 2014;13(2): 325-35
    • (2014) J Proteome Res , vol.13 , Issue.2 , pp. 325-335
    • Cillero-Pastor, B.1    Heeren, R.M.2
  • 129
    • 84879341172 scopus 로고    scopus 로고
    • Current frontiers in clinical research application of MALDI imaging mass spectrometry
    • Neubert P, Walch A. Current frontiers in clinical research application of MALDI imaging mass spectrometry. Expert Rev Proteomics 2013;10(3):259-73
    • (2013) Expert Rev Proteomics , vol.10 , Issue.3 , pp. 259-273
    • Neubert, P.1    Walch, A.2
  • 130
    • 77956407293 scopus 로고    scopus 로고
    • Peptide and protein imaging mass spectrometry in cancer research
    • McDonnell LA, Corthals GL, Willems SM, et al. Peptide and protein imaging mass spectrometry in cancer research. J Proteomics 2010;73(10):1921-44
    • (2010) J Proteomics , vol.73 , Issue.10 , pp. 1921-1944
    • McDonnell, L.A.1    Corthals, G.L.2    Willems, S.M.3
  • 131
    • 34248230245 scopus 로고    scopus 로고
    • Direct analysis and MALDI imaging of formalin-fixed, paraffin embedded tissue sections
    • Lemaire R, Desmons A, Tabet J C, et al. Direct analysis and MALDI imaging of formalin-fixed, paraffin embedded tissue sections. J Proteome Res 2007;6:1295-305
    • (2007) J Proteome Res , vol.6 , pp. 1295-1305
    • Lemaire, R.1    Desmons, A.2    Tabet, J.C.3
  • 132
    • 78349308988 scopus 로고    scopus 로고
    • MALDI direct analysis and imaging of frozen versus FFPE tissues: What strategy for which sample?
    • Wisztorski M, Franck J, Salzet M, et al. MALDI direct analysis and imaging of frozen versus FFPE tissues: what strategy for which sample? Methods Mol Biol 2010;656:303-22
    • (2010) Methods Mol Biol , vol.656 , pp. 303-322
    • Wisztorski, M.1    Franck, J.2    Salzet, M.3
  • 133
    • 80054825298 scopus 로고    scopus 로고
    • Proteomic analysis of formalin-fixed paraffin-embedded tissue by MALDI imaging mass spectrometry
    • Casadonte R, Caprioli RM. Proteomic analysis of formalin-fixed paraffin-embedded tissue by MALDI imaging mass spectrometry. Nat Protoc 2011;6(11): 1695-709
    • (2011) Nat Protoc , vol.6 , Issue.11 , pp. 1695-1709
    • Casadonte, R.1    Caprioli, R.M.2
  • 134
    • 84894084081 scopus 로고    scopus 로고
    • Toward improving the proteomic analysis of formalin-fixed paraffin-embedded tissue
    • Fowler CB, O'Leary TJ, Mason JT. Toward improving the proteomic analysis of formalin-fixed, paraffin-embedded tissue. Expert Rev Proteomics 2013;10(4):389-400
    • (2013) Expert Rev Proteomics , vol.10 , Issue.4 , pp. 389-400
    • Fowler, C.B.1    O'Leary, T.J.2    Mason, J.T.3
  • 135
    • 0036831909 scopus 로고    scopus 로고
    • Direct analysis of laser capture microdissected cells by MALDI mass spectrometry
    • Xu BJ, Caprioli RM, Sanders ME, et al. Direct analysis of laser capture microdissected cells by MALDI mass spectrometry. J Am Soc Mass Spectrom 2002;13(11):1292-7
    • (2002) J Am Soc Mass Spectrom , vol.13 , Issue.11 , pp. 1292-1297
    • Xu, B.J.1    Caprioli, R.M.2    Sanders, M.E.3
  • 136
    • 45549093377 scopus 로고    scopus 로고
    • Differentiating proteomic biomarkers in breast cancer by laser capture microdissection and MALDI MS
    • Sanders ME, Dias EC, Xu BJ, et al. Differentiating proteomic biomarkers in breast cancer by laser capture microdissection and MALDI MS. J Proteome Res 2008;7(4):1500-7
    • (2008) J Proteome Res , vol.7 , Issue.4 , pp. 1500-1507
    • Sanders, M.E.1    Dias, E.C.2    Xu, B.J.3
  • 137
    • 78649877261 scopus 로고    scopus 로고
    • Classification of HER2/neu status in gastric cancer using a breast-cancer derived proteome classifier
    • Balluff B, Elsner M, Kowarsch A, et al. Classification of HER2/neu status in gastric cancer using a breast-cancer derived proteome classifier. J Proteome Res 2010; 9(12):6317-22
    • (2010) J Proteome Res , vol.9 , Issue.12 , pp. 6317-6322
    • Balluff, B.1    Elsner, M.2    Kowarsch, A.3
  • 138
    • 74549178443 scopus 로고    scopus 로고
    • Identification of markers of taxane sensitivity using proteomic and genomic analyses of breast tumors from patients receiving neoadjuvant paclitaxel and radiation
    • Bauer JA, Chakravarthy AB, Rosenbluth JM, et al. Identification of markers of taxane sensitivity using proteomic and genomic analyses of breast tumors from patients receiving neoadjuvant paclitaxel and radiation. Clin Cancer Res 2010;16(2): 681-90
    • (2010) Clin Cancer Res , vol.16 , Issue.2 , pp. 681-690
    • Bauer, J.A.1    Chakravarthy, A.B.2    Rosenbluth, J.M.3
  • 139
    • 84876160864 scopus 로고    scopus 로고
    • Human breast cancer tissues contain abundant phosphatidylcholine(36:1) with high stearoyl-CoA desaturase-1 expression
    • Ide Y, Waki M, Hayasaka T, et al. Human breast cancer tissues contain abundant phosphatidylcholine(36:1) with high stearoyl-CoA desaturase-1 expression. PLoS One 2013;8(4):e61204
    • (2013) PLoS One , vol.8 , Issue.4
    • Ide, Y.1    Waki, M.2    Hayasaka, T.3
  • 140
    • 84884987278 scopus 로고    scopus 로고
    • High-resolution imaging mass spectrometry reveals detailed spatial distribution of phosphatidylinositols in human breast cancer
    • Kawashima M, Iwamoto N, Kawaguchi-Sakita N, et al. High-resolution imaging mass spectrometry reveals detailed spatial distribution of phosphatidylinositols in human breast cancer. Cancer Sci 2013; 104(10):1372-9
    • (2013) Cancer Sci , vol.104 , Issue.10 , pp. 1372-1379
    • Kawashima, M.1    Iwamoto, N.2    Kawaguchi-Sakita, N.3
  • 141
    • 72949100523 scopus 로고    scopus 로고
    • Tissue microarray for routine analysis of breast biomarkers in the clinical laboratory
    • Thomson TA, Zhou C, Chu C, et al. Tissue microarray for routine analysis of breast biomarkers in the clinical laboratory. Am J Clin Pathol 2009;132(6):899-905
    • (2009) Am J Clin Pathol , vol.132 , Issue.6 , pp. 899-905
    • Thomson, T.A.1    Zhou, C.2    Chu, C.3
  • 142
    • 84858200109 scopus 로고    scopus 로고
    • Development of multigene expression signature maps at the protein level from digitized immunohistochemistry slides
    • Metzger GJ, Dankbar SC, Henriksen J, et al. Development of multigene expression signature maps at the protein level from digitized immunohistochemistry slides. PLoS One 2012;7(3):e33520
    • (2012) PLoS One , vol.7 , Issue.3
    • Metzger, G.J.1    Dankbar, S.C.2    Henriksen, J.3
  • 143
    • 84934441223 scopus 로고    scopus 로고
    • Selected reaction monitoring mass spectrometry: A methodology overview
    • Ebhardt HA. Selected reaction monitoring mass spectrometry: a methodology overview. Methods Mol Biol 2014;1072:209-22
    • (2014) Methods Mol Biol , vol.1072 , pp. 209-222
    • Ebhardt, H.A.1
  • 144
    • 84883189721 scopus 로고    scopus 로고
    • Development of MRM-based assays for the absolute quantitation of plasma proteins
    • Kuzyk MA, Parker CE, Domanski D, et al. Development of MRM-based assays for the absolute quantitation of plasma proteins. Methods Mol Biol 2013;1023:53-82
    • (2013) Methods Mol Biol , vol.1023 , pp. 53-82
    • Kuzyk, M.A.1    Parker, C.E.2    Domanski, D.3
  • 145
    • 84888295045 scopus 로고    scopus 로고
    • Method and platform standardization in MRM-based quantitative plasma proteomics
    • Percy AJ, Chambers AG, Yang J, et al. Method and platform standardization in MRM-based quantitative plasma proteomics. J Proteomics 2013;95:66-76
    • (2013) J Proteomics , vol.95 , pp. 66-76
    • Percy, A.J.1    Chambers, A.G.2    Yang, J.3
  • 146
    • 84884675370 scopus 로고    scopus 로고
    • Increased WD-repeat containing protein 1 in interstitial fluid from ovarian carcinomas shown by comparative proteomic analysis of malignant and healthy gynecological tissue
    • Haslene-Hox H, Oveland E, Woie K, et al. Increased WD-repeat containing protein 1 in interstitial fluid from ovarian carcinomas shown by comparative proteomic analysis of malignant and healthy gynecological tissue. Biochim Biophys Acta 2013;1834(11):2347-59
    • (2013) Biochim Biophys Acta , vol.1834 , Issue.11 , pp. 2347-2359
    • Haslene-Hox, H.1    Oveland, E.2    Woie, K.3
  • 147
    • 84868312185 scopus 로고    scopus 로고
    • A strategy for large-scale phosphoproteomics and SRM-based validation of human breast cancer tissue samples
    • Narumi R, Murakami T, Kuga T, et al. A strategy for large-scale phosphoproteomics and SRM-based validation of human breast cancer tissue samples. J Proteome Res 2012; 11(11):5311-2532
    • (2012) J Proteome Res , vol.11 , Issue.11 , pp. 5311-2532
    • Narumi, R.1    Murakami, T.2    Kuga, T.3


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.