메뉴 건너뛰기




Volumn 77, Issue , 2012, Pages 561-576

Comparability of differential proteomics data generated from paired archival fresh-frozen and formalin-fixed samples by GeLC-MS/MS and spectral counting

Author keywords

Archival samples; Biorepository; FFPE; GeLC MS MS; Spectral counting

Indexed keywords

FORMALDEHYDE; PARAFFIN; PROTEOME;

EID: 84870393717     PISSN: 18743919     EISSN: 18767737     Source Type: Journal    
DOI: 10.1016/j.jprot.2012.09.033     Document Type: Article
Times cited : (48)

References (117)
  • 1
    • 33749455064 scopus 로고    scopus 로고
    • Capillary separations enabling tissue proteomics-based biomarker discovery
    • Guo T., Lee C.S., Wang W., DeVoe D.L., Balgley B.M. Capillary separations enabling tissue proteomics-based biomarker discovery. Electrophoresis 2006, 27:3523-3532.
    • (2006) Electrophoresis , vol.27 , pp. 3523-3532
    • Guo, T.1    Lee, C.S.2    Wang, W.3    DeVoe, D.L.4    Balgley, B.M.5
  • 2
    • 33747030845 scopus 로고    scopus 로고
    • Protein biomarker discovery and validation: the long and uncertain path to clinical utility
    • Rifai N., Gillette M.A., Carr S.A. Protein biomarker discovery and validation: the long and uncertain path to clinical utility. Nat Biotechnol 2006, 24:971-983.
    • (2006) Nat Biotechnol , vol.24 , pp. 971-983
    • Rifai, N.1    Gillette, M.A.2    Carr, S.A.3
  • 3
    • 72849127075 scopus 로고    scopus 로고
    • Comparison of multidimensional shotgun technologies targeting tissue proteomics
    • Fang X., Balgley B.M., Wang W., Park D.M., Lee C.S. Comparison of multidimensional shotgun technologies targeting tissue proteomics. Electrophoresis 2009, 30:4063-4070.
    • (2009) Electrophoresis , vol.30 , pp. 4063-4070
    • Fang, X.1    Balgley, B.M.2    Wang, W.3    Park, D.M.4    Lee, C.S.5
  • 4
    • 0034461996 scopus 로고    scopus 로고
    • Quantitative molecular analysis of laser-microdissected paraffin-embedded human tissues
    • Lehmann U., Bock O., Glockner S., Kreipe H. Quantitative molecular analysis of laser-microdissected paraffin-embedded human tissues. Pathobiol 2000, 68:202-208.
    • (2000) Pathobiol , vol.68 , pp. 202-208
    • Lehmann, U.1    Bock, O.2    Glockner, S.3    Kreipe, H.4
  • 5
    • 20444500954 scopus 로고    scopus 로고
    • Technology insight: application of molecular techniques to formalin-fixed paraffin-embedded tissues from breast cancer
    • Paik S., Kim C.Y., Song Y.K., Kim W.S. Technology insight: application of molecular techniques to formalin-fixed paraffin-embedded tissues from breast cancer. Nat Clin Pract Oncol 2005, 2:246-254.
    • (2005) Nat Clin Pract Oncol , vol.2 , pp. 246-254
    • Paik, S.1    Kim, C.Y.2    Song, Y.K.3    Kim, W.S.4
  • 6
    • 79959928424 scopus 로고    scopus 로고
    • Excavation of a buried treasure-DNA, mRNA, miRNA and protein analysis in formalin fixed, paraffin embedded tissues
    • Klopfleisch R., Weiss A.T., Gruber A.D. Excavation of a buried treasure-DNA, mRNA, miRNA and protein analysis in formalin fixed, paraffin embedded tissues. Histol Histopathol 2011, 26:797-810.
    • (2011) Histol Histopathol , vol.26 , pp. 797-810
    • Klopfleisch, R.1    Weiss, A.T.2    Gruber, A.D.3
  • 7
    • 79953072078 scopus 로고    scopus 로고
    • The use of formalin fixed wax embedded tissue for proteomic analysis
    • Ralton L.D., Murray G.I. The use of formalin fixed wax embedded tissue for proteomic analysis. J Clin Pathol 2011, 64:297-302.
    • (2011) J Clin Pathol , vol.64 , pp. 297-302
    • Ralton, L.D.1    Murray, G.I.2
  • 9
    • 33646908503 scopus 로고    scopus 로고
    • Identification of formaldehyde-induced modifications in proteins: reactions with insulin
    • Metz B., Kersten G.F.A., Baart G.J.E., de Jong A., Meiring H., ten Hove J., et al. Identification of formaldehyde-induced modifications in proteins: reactions with insulin. Bioconjug Chem 2006, 17:815-822.
    • (2006) Bioconjug Chem , vol.17 , pp. 815-822
    • Metz, B.1    Kersten, G.F.A.2    Baart, G.J.E.3    de Jong, A.4    Meiring, H.5    ten Hove, J.6
  • 10
    • 0025829609 scopus 로고
    • Antigen retrieval in formalin-fixed, paraffin-embedded tissues: an enhancement method for immunohistochemical staining based on microwave oven heating of tissue sections
    • Shi S., Key M., Kalra K. Antigen retrieval in formalin-fixed, paraffin-embedded tissues: an enhancement method for immunohistochemical staining based on microwave oven heating of tissue sections. J Histochem Cytochem 1991, 39:741-748.
    • (1991) J Histochem Cytochem , vol.39 , pp. 741-748
    • Shi, S.1    Key, M.2    Kalra, K.3
  • 11
    • 78650814932 scopus 로고    scopus 로고
    • Antigen retrieval immunohistochemistry: review and future prospects in research and diagnosis over two decades
    • Shi S.R., Shi Y., Taylor C.R. Antigen retrieval immunohistochemistry: review and future prospects in research and diagnosis over two decades. J Histochem Cytochem 2011, 59:13-32.
    • (2011) J Histochem Cytochem , vol.59 , pp. 13-32
    • Shi, S.R.1    Shi, Y.2    Taylor, C.R.3
  • 12
    • 84858994198 scopus 로고    scopus 로고
    • Setting proteins free: progresses and achievements in proteomics of formalin-fixed, paraffin-embedded tissues
    • Tanca A., Pagnozzi D., Addis M.F. Setting proteins free: progresses and achievements in proteomics of formalin-fixed, paraffin-embedded tissues. Proteomics Clin Appl 2012, 6:7-21.
    • (2012) Proteomics Clin Appl , vol.6 , pp. 7-21
    • Tanca, A.1    Pagnozzi, D.2    Addis, M.F.3
  • 14
    • 33646698472 scopus 로고    scopus 로고
    • Protein extraction from formalin-fixed, paraffin-embedded tissue sections: quality evaluation by mass spectrometry
    • Shi S.R., Liu C., Balgley B.M., Lee C., Taylor C.R. Protein extraction from formalin-fixed, paraffin-embedded tissue sections: quality evaluation by mass spectrometry. J Histochem Cytochem 2006, 54:739-743.
    • (2006) J Histochem Cytochem , vol.54 , pp. 739-743
    • Shi, S.R.1    Liu, C.2    Balgley, B.M.3    Lee, C.4    Taylor, C.R.5
  • 15
    • 33846629961 scopus 로고    scopus 로고
    • Quantitative protein analysis from formalin-fixed tissues: implications for translational clinical research and nanoscale molecular diagnosis
    • Becker K.F., Schott C., Hipp S., Metzger V., Porschewski P., Beck R., et al. Quantitative protein analysis from formalin-fixed tissues: implications for translational clinical research and nanoscale molecular diagnosis. J Pathol 2007, 211:370-378.
    • (2007) J Pathol , vol.211 , pp. 370-378
    • Becker, K.F.1    Schott, C.2    Hipp, S.3    Metzger, V.4    Porschewski, P.5    Beck, R.6
  • 16
    • 62849124399 scopus 로고    scopus 로고
    • Development and validation of a novel protein extraction methodology for quantitation of protein expression in formalin-fixed paraffin-embedded tissues using western blotting
    • Nirmalan N.J., Harnden P., Selby P.J., Banks R.E. Development and validation of a novel protein extraction methodology for quantitation of protein expression in formalin-fixed paraffin-embedded tissues using western blotting. J Pathol 2009, 217:497-506.
    • (2009) J Pathol , vol.217 , pp. 497-506
    • Nirmalan, N.J.1    Harnden, P.2    Selby, P.J.3    Banks, R.E.4
  • 17
    • 68549098247 scopus 로고    scopus 로고
    • Generation of high-quality protein extracts from formalin-fixed, paraffin-embedded tissues
    • Addis M.F., Tanca A., Pagnozzi D., Crobu S., Fanciulli G., Cossu-Rocca P., et al. Generation of high-quality protein extracts from formalin-fixed, paraffin-embedded tissues. Proteomics 2009, 9:3815-3823.
    • (2009) Proteomics , vol.9 , pp. 3815-3823
    • Addis, M.F.1    Tanca, A.2    Pagnozzi, D.3    Crobu, S.4    Fanciulli, G.5    Cossu-Rocca, P.6
  • 18
    • 77954378942 scopus 로고    scopus 로고
    • Proteome, phosphoproteome, and N-glycoproteome are quantitatively preserved in formalin-fixed paraffin-embedded tissue and analyzable by high-resolution mass spectrometry
    • Ostasiewicz P., Zielinska D.F., Mann M., Wiśniewski J.R. Proteome, phosphoproteome, and N-glycoproteome are quantitatively preserved in formalin-fixed paraffin-embedded tissue and analyzable by high-resolution mass spectrometry. J Proteome Res 2010, 9:3688-3700.
    • (2010) J Proteome Res , vol.9 , pp. 3688-3700
    • Ostasiewicz, P.1    Zielinska, D.F.2    Mann, M.3    Wiśniewski, J.R.4
  • 20
    • 80655142296 scopus 로고    scopus 로고
    • Standardization of a sample preparation and analytical workflow for proteomics of archival endometrial cancer tissue
    • Alkhas A., Hood B.L., Oliver K., Teng P.-n., Oliver J., Mitchell D., et al. Standardization of a sample preparation and analytical workflow for proteomics of archival endometrial cancer tissue. J Proteome Res 2011, 10:5264-5271.
    • (2011) J Proteome Res , vol.10 , pp. 5264-5271
    • Alkhas, A.1    Hood, B.L.2    Oliver, K.3    Teng, P.-N.4    Oliver, J.5    Mitchell, D.6
  • 21
    • 84859583476 scopus 로고    scopus 로고
    • Pressure-assisted protein extraction: a novel method for recovering proteins from archival tissue for proteomic analysis
    • Fowler C.B., Waybright T.J., Veenstra T.D., O'Leary T.J., Mason J.T. Pressure-assisted protein extraction: a novel method for recovering proteins from archival tissue for proteomic analysis. J Proteome Res 2012, 11:2602-2608.
    • (2012) J Proteome Res , vol.11 , pp. 2602-2608
    • Fowler, C.B.1    Waybright, T.J.2    Veenstra, T.D.3    O'Leary, T.J.4    Mason, J.T.5
  • 22
    • 27144544744 scopus 로고    scopus 로고
    • Identification of proteins from formalin-fixed paraffin-embedded cells by LC-MS/MS
    • Crockett D.K., Lin Z., Vaughn C.P., Lim M.S., Elenitoba-Johnson K.S.J. Identification of proteins from formalin-fixed paraffin-embedded cells by LC-MS/MS. Lab Invest 2005, 85:1405-1415.
    • (2005) Lab Invest , vol.85 , pp. 1405-1415
    • Crockett, D.K.1    Lin, Z.2    Vaughn, C.P.3    Lim, M.S.4    Elenitoba-Johnson, K.S.J.5
  • 25
    • 34250840587 scopus 로고    scopus 로고
    • Proteome analysis of microdissected formalin-fixed and paraffin-embedded tissue specimens
    • Guo T., Wang W., Rudnick P.A., Song T., Li J., Zhuang Z., et al. Proteome analysis of microdissected formalin-fixed and paraffin-embedded tissue specimens. J Histochem Cytochem 2007, 55:763-772.
    • (2007) J Histochem Cytochem , vol.55 , pp. 763-772
    • Guo, T.1    Wang, W.2    Rudnick, P.A.3    Song, T.4    Li, J.5    Zhuang, Z.6
  • 26
    • 33947572920 scopus 로고    scopus 로고
    • Development of efficient protein extraction methods for shotgun proteome analysis of formalin-fixed tissues
    • Jiang X., Jiang X., Feng S., Tian R., Ye M., Zou H. Development of efficient protein extraction methods for shotgun proteome analysis of formalin-fixed tissues. J Proteome Res 2007, 6:1038-1047.
    • (2007) J Proteome Res , vol.6 , pp. 1038-1047
    • Jiang, X.1    Jiang, X.2    Feng, S.3    Tian, R.4    Ye, M.5    Zou, H.6
  • 27
    • 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 R.W., Brock J.W.C., Tanksley J.P., Li M., Washington M.K., Slebos R.J.C., et al. 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, 8:1988-1998.
    • (2009) Mol Cell Proteomics , vol.8 , pp. 1988-1998
    • Sprung, R.W.1    Brock, J.W.C.2    Tanksley, J.P.3    Li, M.4    Washington, M.K.5    Slebos, R.J.C.6
  • 28
    • 79960858195 scopus 로고    scopus 로고
    • Utility of formalin-fixed, paraffin-embedded liver biopsy specimens for global proteomic analysis in nonalcoholic steatohepatitis
    • Bell L.N., Saxena R., Mattar S.G., You J., Wang M., Chalasani N. Utility of formalin-fixed, paraffin-embedded liver biopsy specimens for global proteomic analysis in nonalcoholic steatohepatitis. Proteomics Clin Appl 2011, 5:397-404.
    • (2011) Proteomics Clin Appl , vol.5 , pp. 397-404
    • Bell, L.N.1    Saxena, R.2    Mattar, S.G.3    You, J.4    Wang, M.5    Chalasani, N.6
  • 29
    • 79960350722 scopus 로고    scopus 로고
    • Protein phosphorylation analysis in archival clinical cancer samples by shotgun and targeted proteomics approaches
    • Gámez-Pozo A., Sánchez-Navarro I., Calvo E., Díaz E., Miguel-Martín M., López R., et al. Protein phosphorylation analysis in archival clinical cancer samples by shotgun and targeted proteomics approaches. Mol Biosyst 2011, 7:2368.
    • (2011) Mol Biosyst , vol.7 , pp. 2368
    • Gámez-Pozo, A.1    Sánchez-Navarro, I.2    Calvo, E.3    Díaz, E.4    Miguel-Martín, M.5    López, R.6
  • 30
    • 39749160439 scopus 로고    scopus 로고
    • Proteomic analysis of laser-captured paraffin-embedded tissues: a molecular portrait of head and neck cancer progression
    • Patel V., Hood B.L., Molinolo A.A., Lee N.H., Conrads T.P., Braisted J.C., et al. Proteomic analysis of laser-captured paraffin-embedded tissues: a molecular portrait of head and neck cancer progression. Clin Cancer Res 2008, 14:1002-1014.
    • (2008) Clin Cancer Res , vol.14 , pp. 1002-1014
    • Patel, V.1    Hood, B.L.2    Molinolo, A.A.3    Lee, N.H.4    Conrads, T.P.5    Braisted, J.C.6
  • 32
    • 84880037648 scopus 로고    scopus 로고
    • LC/MS-based quantitative proteomic analysis of paraffin-embedded archival melanomas reveals potential proteomic biomarkers associated with metastasis
    • Huang S.K., Darfler M.M., Nicholl M.B., You J., Bemis K.G., Tegeler T.J., et al. LC/MS-based quantitative proteomic analysis of paraffin-embedded archival melanomas reveals potential proteomic biomarkers associated with metastasis. PLoS One 2009, 4:e4430.
    • (2009) PLoS One , vol.4
    • Huang, S.K.1    Darfler, M.M.2    Nicholl, M.B.3    You, J.4    Bemis, K.G.5    Tegeler, T.J.6
  • 33
    • 77950518174 scopus 로고    scopus 로고
    • Proteomic analysis of laser-microdissected paraffin-embedded tissues: (1) stage-related protein candidates upon non-metastatic lung adenocarcinoma
    • Kawamura T., Nomura M., Tojo H., Fujii K., Hamasaki H., Mikami S., et al. Proteomic analysis of laser-microdissected paraffin-embedded tissues: (1) stage-related protein candidates upon non-metastatic lung adenocarcinoma. J Proteomics 2010, 73:1089-1099.
    • (2010) J Proteomics , vol.73 , pp. 1089-1099
    • Kawamura, T.1    Nomura, M.2    Tojo, H.3    Fujii, K.4    Hamasaki, H.5    Mikami, S.6
  • 34
    • 77952764025 scopus 로고    scopus 로고
    • Quantitative proteomic analysis of formalin-fixed and paraffin-embedded nasopharyngeal carcinoma using iTRAQ labeling, two-dimensional liquid chromatography, and tandem mass spectrometry
    • Xiao Z., Li G., Chen Y., Li M., Peng F., Li C., et al. Quantitative proteomic analysis of formalin-fixed and paraffin-embedded nasopharyngeal carcinoma using iTRAQ labeling, two-dimensional liquid chromatography, and tandem mass spectrometry. J Histochem Cytochem 2010, 58:517-527.
    • (2010) J Histochem Cytochem , vol.58 , pp. 517-527
    • Xiao, Z.1    Li, G.2    Chen, Y.3    Li, M.4    Peng, F.5    Li, C.6
  • 35
    • 79952392534 scopus 로고    scopus 로고
    • Differential proteomic analysis of late-stage and recurrent breast cancer from formalin-fixed paraffin-embedded tissues
    • Bateman N.W., Sun M., Bhargava R., Hood B.L., Darfler M.M., Kovatich A.J., et al. Differential proteomic analysis of late-stage and recurrent breast cancer from formalin-fixed paraffin-embedded tissues. J Proteome Res 2011, 10:1323-1332.
    • (2011) J Proteome Res , vol.10 , pp. 1323-1332
    • Bateman, N.W.1    Sun, M.2    Bhargava, R.3    Hood, B.L.4    Darfler, M.M.5    Kovatich, A.J.6
  • 36
    • 78651516681 scopus 로고    scopus 로고
    • Proteomic analysis of formalin-fixed, paraffin-embedded lung neuroendocrine tumor samples from hospital archives
    • Tanca A., Addis M.F., Pagnozzi D., Cossu-Rocca P., Tonelli R., Falchi G., et al. Proteomic analysis of formalin-fixed, paraffin-embedded lung neuroendocrine tumor samples from hospital archives. J Proteomics 2011, 74:359-370.
    • (2011) J Proteomics , vol.74 , pp. 359-370
    • Tanca, A.1    Addis, M.F.2    Pagnozzi, D.3    Cossu-Rocca, P.4    Tonelli, R.5    Falchi, G.6
  • 37
    • 79960011243 scopus 로고    scopus 로고
    • High recovery FASP applied to the proteomic analysis of microdissected formalin fixed paraffin embedded cancer tissues retrieves known colon cancer markers
    • Wisniewski J.R., Ostasiewicz P., Mann M. High recovery FASP applied to the proteomic analysis of microdissected formalin fixed paraffin embedded cancer tissues retrieves known colon cancer markers. J Proteome Res 2011, 10:3040-3049.
    • (2011) J Proteome Res , vol.10 , pp. 3040-3049
    • Wisniewski, J.R.1    Ostasiewicz, P.2    Mann, M.3
  • 38
    • 84859270363 scopus 로고    scopus 로고
    • Label-free protein profiling of formalin-fixed paraffin-embedded (FFPE) heart tissue reveals immediate mitochondrial impairment after ionising radiation
    • Azimzadeh O., Scherthan H., Yentrapalli R., Barjaktarovic Z., Ueffing M., Conrad M., et al. Label-free protein profiling of formalin-fixed paraffin-embedded (FFPE) heart tissue reveals immediate mitochondrial impairment after ionising radiation. J Proteomics 2012, 75:2384-2395.
    • (2012) J Proteomics , vol.75 , pp. 2384-2395
    • Azimzadeh, O.1    Scherthan, H.2    Yentrapalli, R.3    Barjaktarovic, Z.4    Ueffing, M.5    Conrad, M.6
  • 39
    • 70249095601 scopus 로고    scopus 로고
    • Protein extraction of formalin-fixed, paraffin-embedded tissue enables robust proteomic profiles by mass spectrometry
    • Scicchitano M.S., Dalmas D.A., Boyce R.W., Thomas H.C., Frazier K.S. Protein extraction of formalin-fixed, paraffin-embedded tissue enables robust proteomic profiles by mass spectrometry. J Histochem Cytochem 2009, 57:849-860.
    • (2009) J Histochem Cytochem , vol.57 , pp. 849-860
    • Scicchitano, M.S.1    Dalmas, D.A.2    Boyce, R.W.3    Thomas, H.C.4    Frazier, K.S.5
  • 40
    • 79955448303 scopus 로고    scopus 로고
    • Initial development and validation of a novel extraction method for quantitative mining of the formalin-fixed, paraffin-embedded tissue proteome for biomarker investigations
    • Nirmalan N.J., Hughes C., Peng J., McKenna T., Langridge J., Cairns D.A., et al. Initial development and validation of a novel extraction method for quantitative mining of the formalin-fixed, paraffin-embedded tissue proteome for biomarker investigations. J Proteome Res 2011, 10:896-906.
    • (2011) J Proteome Res , vol.10 , pp. 896-906
    • Nirmalan, N.J.1    Hughes, C.2    Peng, J.3    McKenna, T.4    Langridge, J.5    Cairns, D.A.6
  • 41
    • 79957658095 scopus 로고    scopus 로고
    • Impact of fixation time on GeLC-MS/MS proteomic profiling of formalin-fixed, paraffin-embedded tissues
    • Tanca A., Pagnozzi D., Falchi G., Biosa G., Rocca S., Foddai G., et al. Impact of fixation time on GeLC-MS/MS proteomic profiling of formalin-fixed, paraffin-embedded tissues. J Proteomics 2011, 74:1015-1021.
    • (2011) J Proteomics , vol.74 , pp. 1015-1021
    • Tanca, A.1    Pagnozzi, D.2    Falchi, G.3    Biosa, G.4    Rocca, S.5    Foddai, G.6
  • 42
    • 1842499791 scopus 로고    scopus 로고
    • Profiling core proteomes of human cell lines by one-dimensional PAGE and liquid chromatography-tandem mass spectrometry
    • Schirle M. Profiling core proteomes of human cell lines by one-dimensional PAGE and liquid chromatography-tandem mass spectrometry. Mol Cell Proteomics 2003, 2:1297-1305.
    • (2003) Mol Cell Proteomics , vol.2 , pp. 1297-1305
    • Schirle, M.1
  • 44
    • 77950641486 scopus 로고    scopus 로고
    • Workflow comparison for label-free, quantitative secretome proteomics for cancer biomarker discovery: method evaluation, differential analysis, and verification in serum
    • Piersma S.R., Fiedler U., Span S., Lingnau A., Pham T.V., Hoffmann S., et al. Workflow comparison for label-free, quantitative secretome proteomics for cancer biomarker discovery: method evaluation, differential analysis, and verification in serum. J Proteome Res 2010, 9:1913-1922.
    • (2010) J Proteome Res , vol.9 , pp. 1913-1922
    • Piersma, S.R.1    Fiedler, U.2    Span, S.3    Lingnau, A.4    Pham, T.V.5    Hoffmann, S.6
  • 45
    • 77958056802 scopus 로고    scopus 로고
    • Direct comparison of stable isotope labeling by amino acids in cell culture and spectral counting for quantitative proteomics
    • Collier T.S., Sarkar P., Franck W.L., Rao B.M., Dean R.A., Muddiman D.C. Direct comparison of stable isotope labeling by amino acids in cell culture and spectral counting for quantitative proteomics. Anal Chem 2010, 82:8696-8702.
    • (2010) Anal Chem , vol.82 , pp. 8696-8702
    • Collier, T.S.1    Sarkar, P.2    Franck, W.L.3    Rao, B.M.4    Dean, R.A.5    Muddiman, D.C.6
  • 46
    • 80054014368 scopus 로고    scopus 로고
    • Comparison of stable-isotope labeling with amino acids in cell culture and spectral counting for relative quantification of protein expression
    • Collier T.S., Randall S.M., Sarkar P., Rao B.M., Dean R.A., Muddiman D.C. Comparison of stable-isotope labeling with amino acids in cell culture and spectral counting for relative quantification of protein expression. Rapid Commun Mass Spectrom 2011, 25:2524-2532.
    • (2011) Rapid Commun Mass Spectrom , vol.25 , pp. 2524-2532
    • Collier, T.S.1    Randall, S.M.2    Sarkar, P.3    Rao, B.M.4    Dean, R.A.5    Muddiman, D.C.6
  • 47
    • 78049523510 scopus 로고    scopus 로고
    • Metastatic canine mammary carcinomas can be identified by a gene expression profile that partly overlaps with human breast cancer profiles
    • Klopfleisch R., Lenze D., Hummel M., Gruber A.D. Metastatic canine mammary carcinomas can be identified by a gene expression profile that partly overlaps with human breast cancer profiles. BMC Cancer 2010, 10:618.
    • (2010) BMC Cancer , vol.10 , pp. 618
    • Klopfleisch, R.1    Lenze, D.2    Hummel, M.3    Gruber, A.D.4
  • 48
    • 80053930592 scopus 로고    scopus 로고
    • Is there a malignant progression associated with a linear change in protein expression levels from normal canine mammary gland to metastatic mammary tumors?
    • Klose P., Weise C., Bondzio A., Multhaup G., Einspanier R., Gruber A.D., et al. Is there a malignant progression associated with a linear change in protein expression levels from normal canine mammary gland to metastatic mammary tumors?. J Proteome Res 2011, 10:4405-4415.
    • (2011) J Proteome Res , vol.10 , pp. 4405-4415
    • Klose, P.1    Weise, C.2    Bondzio, A.3    Multhaup, G.4    Einspanier, R.5    Gruber, A.D.6
  • 49
    • 81555195417 scopus 로고    scopus 로고
    • Mammography and ultrasound imaging of preinvasive and invasive canine spontaneous mammary cancer and their similarities to human breast cancer
    • Mohammed S.I., Meloni G.B., Pinna Parpaglia M.L., Marras V., Burrai G.P., Meloni F., et al. Mammography and ultrasound imaging of preinvasive and invasive canine spontaneous mammary cancer and their similarities to human breast cancer. Cancer Prev Res (Phila) 2011, 4:1790-1798.
    • (2011) Cancer Prev Res (Phila) , vol.4 , pp. 1790-1798
    • Mohammed, S.I.1    Meloni, G.B.2    Pinna Parpaglia, M.L.3    Marras, V.4    Burrai, G.P.5    Meloni, F.6
  • 50
    • 84857276564 scopus 로고    scopus 로고
    • Canine tumors: a spontaneous animal model of human carcinogenesis
    • Pinho S.S., Carvalho S., Cabral J., Reis C.A., Gartner F. Canine tumors: a spontaneous animal model of human carcinogenesis. Transl Res 2012, 159:165-172.
    • (2012) Transl Res , vol.159 , pp. 165-172
    • Pinho, S.S.1    Carvalho, S.2    Cabral, J.3    Reis, C.A.4    Gartner, F.5
  • 53
    • 67650345724 scopus 로고    scopus 로고
    • Improvements to the percolator algorithm for peptide identification from shotgun proteomics data sets
    • Spivak M., Weston J., Bottou L., Kall L., Noble W.S. Improvements to the percolator algorithm for peptide identification from shotgun proteomics data sets. J Proteome Res 2009, 8:3737-3745.
    • (2009) J Proteome Res , vol.8 , pp. 3737-3745
    • Spivak, M.1    Weston, J.2    Bottou, L.3    Kall, L.4    Noble, W.S.5
  • 56
    • 77954362750 scopus 로고    scopus 로고
    • Quantitative proteomic profiling studies of pancreatic cancer stem cells
    • Dai L., Li C., Shedden K.A., Lee C.J., Quoc H., Simeone D.M., et al. Quantitative proteomic profiling studies of pancreatic cancer stem cells. J Proteome Res 2010, 9:3394-3402.
    • (2010) J Proteome Res , vol.9 , pp. 3394-3402
    • Dai, L.1    Li, C.2    Shedden, K.A.3    Lee, C.J.4    Quoc, H.5    Simeone, D.M.6
  • 58
    • 3242731195 scopus 로고    scopus 로고
    • A model for random sampling and estimation of relative protein abundance in shotgun proteomics
    • Liu H., Sadygov R.G., Yates J.R. A model for random sampling and estimation of relative protein abundance in shotgun proteomics. Anal Chem 2004, 76:4193-4201.
    • (2004) Anal Chem , vol.76 , pp. 4193-4201
    • Liu, H.1    Sadygov, R.G.2    Yates, J.R.3
  • 59
    • 34248230245 scopus 로고    scopus 로고
    • Direct analysis and MALDI imaging of formalin-fixed, paraffin-embedded tissue sections
    • Lemaire R., Desmons A., Tabet J.C., Day R., Salzet M., Fournier I. Direct analysis and MALDI imaging of formalin-fixed, paraffin-embedded tissue sections. J Proteome Res 2007, 6:1295-1305.
    • (2007) J Proteome Res , vol.6 , pp. 1295-1305
    • Lemaire, R.1    Desmons, A.2    Tabet, J.C.3    Day, R.4    Salzet, M.5    Fournier, I.6
  • 60
    • 77950669475 scopus 로고    scopus 로고
    • Quantitative analysis of proteome coverage and recovery rates for upstream fractionation methods in proteomics
    • Fang Y., Robinson D.P., Foster L.J. Quantitative analysis of proteome coverage and recovery rates for upstream fractionation methods in proteomics. J Proteome Res 2010, 9:1902-1912.
    • (2010) J Proteome Res , vol.9 , pp. 1902-1912
    • Fang, Y.1    Robinson, D.P.2    Foster, L.J.3
  • 61
    • 84863611387 scopus 로고    scopus 로고
    • GeLC-MRM quantitation of mutant KRAS oncoprotein in complex biological samples
    • Halvey P.J., Ferrone C.R., Liebler D.C. GeLC-MRM quantitation of mutant KRAS oncoprotein in complex biological samples. J Proteome Res 2012, 11:3908-3913.
    • (2012) J Proteome Res , vol.11 , pp. 3908-3913
    • Halvey, P.J.1    Ferrone, C.R.2    Liebler, D.C.3
  • 62
    • 33644524918 scopus 로고    scopus 로고
    • Mass spectrometry-based proteomics turns quantitative
    • Ong S.E., Mann M. Mass spectrometry-based proteomics turns quantitative. Nat Chem Biol 2005, 1:252-262.
    • (2005) Nat Chem Biol , vol.1 , pp. 252-262
    • Ong, S.E.1    Mann, M.2
  • 63
    • 34848862125 scopus 로고    scopus 로고
    • Label-free LC-MS/MS quantitative proteomics for large-scale biomarker discovery in complex samples
    • Levin Y., Schwarz E., Wang L., Leweke F.M., Bahn S. Label-free LC-MS/MS quantitative proteomics for large-scale biomarker discovery in complex samples. J Sep Sci 2007, 30:2198-2203.
    • (2007) J Sep Sci , vol.30 , pp. 2198-2203
    • Levin, Y.1    Schwarz, E.2    Wang, L.3    Leweke, F.M.4    Bahn, S.5
  • 64
    • 84861442569 scopus 로고    scopus 로고
    • Label-free mass spectrometry-based proteomics for biomarker discovery and validation
    • Pham T.V., Piersma S.R., Oudgenoeg G., Jimenez C.R. Label-free mass spectrometry-based proteomics for biomarker discovery and validation. Expert Rev Mol Diagn 2012, 12:343-359.
    • (2012) Expert Rev Mol Diagn , vol.12 , pp. 343-359
    • Pham, T.V.1    Piersma, S.R.2    Oudgenoeg, G.3    Jimenez, C.R.4
  • 66
    • 40549107755 scopus 로고    scopus 로고
    • Comparative LC-MS: a landscape of peaks and valleys
    • America A.H.P., Cordewener J.H.G. Comparative LC-MS: a landscape of peaks and valleys. Proteomics 2008, 8:731-749.
    • (2008) Proteomics , vol.8 , pp. 731-749
    • America, A.H.P.1    Cordewener, J.H.G.2
  • 67
    • 74049132731 scopus 로고    scopus 로고
    • Label-free, normalized quantification of complex mass spectrometry data for proteomic analysis
    • Griffin N.M., Yu J., Long F., Oh P., Shore S., Li Y., et al. Label-free, normalized quantification of complex mass spectrometry data for proteomic analysis. Nat Biotechnol 2009, 28:83-89.
    • (2009) Nat Biotechnol , vol.28 , pp. 83-89
    • Griffin, N.M.1    Yu, J.2    Long, F.3    Oh, P.4    Shore, S.5    Li, Y.6
  • 68
    • 33646132293 scopus 로고    scopus 로고
    • The roles of heterogeneous nuclear ribonucleoproteins in tumour development and progression
    • Carpenter B., MacKay C., Alnabulsi A., MacKay M., Telfer C., Melvin W.T., et al. The roles of heterogeneous nuclear ribonucleoproteins in tumour development and progression. Biochim Biophys Acta 2006, 1765:85-100.
    • (2006) Biochim Biophys Acta , vol.1765 , pp. 85-100
    • Carpenter, B.1    MacKay, C.2    Alnabulsi, A.3    MacKay, M.4    Telfer, C.5    Melvin, W.T.6
  • 69
    • 67449084504 scopus 로고    scopus 로고
    • Emerging roles of RNA and RNA-binding protein network in cancer cells
    • Kim M.Y., Hur J., Jeong S. Emerging roles of RNA and RNA-binding protein network in cancer cells. BMB Rep 2009, 42:125-130.
    • (2009) BMB Rep , vol.42 , pp. 125-130
    • Kim, M.Y.1    Hur, J.2    Jeong, S.3
  • 70
    • 80052041185 scopus 로고    scopus 로고
    • MicroRNA regulation by RNA-binding proteins and its implications for cancer
    • van Kouwenhove M., Kedde M., Agami R. MicroRNA regulation by RNA-binding proteins and its implications for cancer. Nat Rev Cancer 2011, 11:644-656.
    • (2011) Nat Rev Cancer , vol.11 , pp. 644-656
    • van Kouwenhove, M.1    Kedde, M.2    Agami, R.3
  • 71
    • 84862300106 scopus 로고    scopus 로고
    • Versatility of RNA-binding proteins in cancer
    • Wurth L. Versatility of RNA-binding proteins in cancer. Comp Funct Genomics 2012, 2012:178525.
    • (2012) Comp Funct Genomics , vol.2012 , pp. 178525
    • Wurth, L.1
  • 73
    • 79960925156 scopus 로고    scopus 로고
    • The cancerous translation apparatus
    • Stumpf C.R., Ruggero D. The cancerous translation apparatus. Curr Opin Genet Dev 2011, 21:474-483.
    • (2011) Curr Opin Genet Dev , vol.21 , pp. 474-483
    • Stumpf, C.R.1    Ruggero, D.2
  • 74
    • 77951432631 scopus 로고    scopus 로고
    • The causes of cancer revisited: "mitochondrial malignancy" and ROS-induced oncogenic transformation - why mitochondria are targets for cancer therapy
    • Ralph S.J., Rodriguez-Enriquez S., Neuzil J., Saavedra E., Moreno-Sanchez R. The causes of cancer revisited: "mitochondrial malignancy" and ROS-induced oncogenic transformation - why mitochondria are targets for cancer therapy. Mol Aspects Med 2010, 31:145-170.
    • (2010) Mol Aspects Med , vol.31 , pp. 145-170
    • Ralph, S.J.1    Rodriguez-Enriquez, S.2    Neuzil, J.3    Saavedra, E.4    Moreno-Sanchez, R.5
  • 75
    • 84855231244 scopus 로고    scopus 로고
    • Targeting mitochondria in fighting cancer
    • Gogvadze V. Targeting mitochondria in fighting cancer. Curr Pharm Des 2011, 17:4034-4046.
    • (2011) Curr Pharm Des , vol.17 , pp. 4034-4046
    • Gogvadze, V.1
  • 77
    • 84857718301 scopus 로고    scopus 로고
    • Preliminary evidences on mitochondrial injury and impaired oxidative metabolism in breast cancer
    • Putignani L., Raffa S., Pescosolido R., Rizza T., Del Chierico F., Leone L., et al. Preliminary evidences on mitochondrial injury and impaired oxidative metabolism in breast cancer. Mitochondrion 2012, 12:363-369.
    • (2012) Mitochondrion , vol.12 , pp. 363-369
    • Putignani, L.1    Raffa, S.2    Pescosolido, R.3    Rizza, T.4    Del Chierico, F.5    Leone, L.6
  • 79
    • 80053517329 scopus 로고    scopus 로고
    • Mechanisms by which the extracellular matrix and integrin signaling act to regulate the switch between tumor suppression and tumor promotion
    • Keely P.J. Mechanisms by which the extracellular matrix and integrin signaling act to regulate the switch between tumor suppression and tumor promotion. J Mammary Gland Biol Neoplasia 2011, 16:205-219.
    • (2011) J Mammary Gland Biol Neoplasia , vol.16 , pp. 205-219
    • Keely, P.J.1
  • 80
    • 81055145534 scopus 로고    scopus 로고
    • Role of TGF-beta and the tumor microenvironment during mammary tumorigenesis
    • Taylor M.A., Lee Y.H., Schiemann W.P. Role of TGF-beta and the tumor microenvironment during mammary tumorigenesis. Gene Expr 2011, 15:117-132.
    • (2011) Gene Expr , vol.15 , pp. 117-132
    • Taylor, M.A.1    Lee, Y.H.2    Schiemann, W.P.3
  • 81
    • 79959510568 scopus 로고    scopus 로고
    • When tumor suppressor TGFbeta meets the HER2 (ERBB2) oncogene
    • Chow A., Arteaga C.L., Wang S.E. When tumor suppressor TGFbeta meets the HER2 (ERBB2) oncogene. J Mammary Gland Biol Neoplasia 2011, 16:81-88.
    • (2011) J Mammary Gland Biol Neoplasia , vol.16 , pp. 81-88
    • Chow, A.1    Arteaga, C.L.2    Wang, S.E.3
  • 82
    • 84859443939 scopus 로고    scopus 로고
    • Transforming growth factor-beta signaling in tumor initiation, progression and therapy in breast cancer: an update
    • Zu X., Zhang Q., Cao R., Liu J., Zhong J., Wen G., et al. Transforming growth factor-beta signaling in tumor initiation, progression and therapy in breast cancer: an update. Cell Tissue Res 2012, 347:73-84.
    • (2012) Cell Tissue Res , vol.347 , pp. 73-84
    • Zu, X.1    Zhang, Q.2    Cao, R.3    Liu, J.4    Zhong, J.5    Wen, G.6
  • 84
    • 77449112686 scopus 로고    scopus 로고
    • Key signalling nodes in mammary gland development and cancer: Myc
    • Hynes N.E., Stoelzle T. Key signalling nodes in mammary gland development and cancer: Myc. Breast Cancer Res 2009, 11:210.
    • (2009) Breast Cancer Res , vol.11 , pp. 210
    • Hynes, N.E.1    Stoelzle, T.2
  • 85
    • 77649275464 scopus 로고    scopus 로고
    • MiR-9, a MYC/MYCN-activated microRNA, regulates E-cadherin and cancer metastasis
    • Ma L., Young J., Prabhala H., Pan E., Mestdagh P., Muth D., et al. miR-9, a MYC/MYCN-activated microRNA, regulates E-cadherin and cancer metastasis. Nat Cell Biol 2010, 12:247-256.
    • (2010) Nat Cell Biol , vol.12 , pp. 247-256
    • Ma, L.1    Young, J.2    Prabhala, H.3    Pan, E.4    Mestdagh, P.5    Muth, D.6
  • 86
    • 20344399167 scopus 로고    scopus 로고
    • Genetic variants of myeloperoxidase and catechol-O-methyltransferase and breast cancer risk
    • Lin S.C., Chou Y.C., Wu M.H., Wu C.C., Lin W.Y., Yu C.P., et al. Genetic variants of myeloperoxidase and catechol-O-methyltransferase and breast cancer risk. Eur J Cancer Prev 2005, 14:257-261.
    • (2005) Eur J Cancer Prev , vol.14 , pp. 257-261
    • Lin, S.C.1    Chou, Y.C.2    Wu, M.H.3    Wu, C.C.4    Lin, W.Y.5    Yu, C.P.6
  • 87
    • 79958706584 scopus 로고    scopus 로고
    • Immunoproteomics of HER2-positive and HER2-negative breast cancer patients with positive lymph nodes
    • Mojtahedi Z., Safaei A., Yousefi Z., Ghaderi A. Immunoproteomics of HER2-positive and HER2-negative breast cancer patients with positive lymph nodes. OMICS 2011, 15:409-418.
    • (2011) OMICS , vol.15 , pp. 409-418
    • Mojtahedi, Z.1    Safaei, A.2    Yousefi, Z.3    Ghaderi, A.4
  • 88
    • 84862590860 scopus 로고    scopus 로고
    • Proteomic-based biosignatures in breast cancer classification and prediction of therapeutic response
    • He J., Whelan S.A., Lu M., Shen D., Chung D.U., Saxton R.E., 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    Shen, D.4    Chung, D.U.5    Saxton, R.E.6
  • 89
    • 77956337524 scopus 로고    scopus 로고
    • Glyceraldehyde-3-phosphate dehydrogenase as a surface associated antigen on human breast cancer cell lines MACL-1 and MGSO-3
    • Correa C.R., Bertollo C.M., Zouain C.S., Goes A.M. Glyceraldehyde-3-phosphate dehydrogenase as a surface associated antigen on human breast cancer cell lines MACL-1 and MGSO-3. Oncol Rep 2010, 24:677-685.
    • (2010) Oncol Rep , vol.24 , pp. 677-685
    • Correa, C.R.1    Bertollo, C.M.2    Zouain, C.S.3    Goes, A.M.4
  • 90
    • 27944502154 scopus 로고    scopus 로고
    • Breast carcinomas fulfill the Warburg hypothesis and provide metabolic markers of cancer prognosis
    • Isidoro A., Casado E., Redondo A., Acebo P., Espinosa E., Alonso A.M., et al. Breast carcinomas fulfill the Warburg hypothesis and provide metabolic markers of cancer prognosis. Carcinogenesis 2005, 26:2095-2104.
    • (2005) Carcinogenesis , vol.26 , pp. 2095-2104
    • Isidoro, A.1    Casado, E.2    Redondo, A.3    Acebo, P.4    Espinosa, E.5    Alonso, A.M.6
  • 91
    • 45549099294 scopus 로고    scopus 로고
    • Targeting therapy for breast carcinoma by ATP synthase inhibitor aurovertin B
    • Huang T.C., Chang H.Y., Hsu C.H., Kuo W.H., Chang K.J., Juan H.F. Targeting therapy for breast carcinoma by ATP synthase inhibitor aurovertin B. J Proteome Res 2008, 7:1433-1444.
    • (2008) J Proteome Res , vol.7 , pp. 1433-1444
    • Huang, T.C.1    Chang, H.Y.2    Hsu, C.H.3    Kuo, W.H.4    Chang, K.J.5    Juan, H.F.6
  • 92
    • 82955207195 scopus 로고    scopus 로고
    • ATP synthase ecto-alpha-subunit: a novel therapeutic target for breast cancer
    • Pan J., Sun L.-C., Tao Y.-F., Zhou Z., Du X.-L., Peng L., et al. ATP synthase ecto-alpha-subunit: a novel therapeutic target for breast cancer. J Transl Med 2011, 9:211.
    • (2011) J Transl Med , vol.9 , pp. 211
    • Pan, J.1    Sun, L.-C.2    Tao, Y.-F.3    Zhou, Z.4    Du, X.-L.5    Peng, L.6
  • 93
    • 78149332780 scopus 로고    scopus 로고
    • The dilemma: does tissue expression of cathepsin D reflect tumor malignancy? The question: does the assay truly mirror cathepsin D mis-function in the tumor?
    • Nicotra G., Castino R., Follo C., Peracchio C., Valente G., Isidoro C. The dilemma: does tissue expression of cathepsin D reflect tumor malignancy? The question: does the assay truly mirror cathepsin D mis-function in the tumor?. Cancer Biomark 2010, 7:47-64.
    • (2010) Cancer Biomark , vol.7 , pp. 47-64
    • Nicotra, G.1    Castino, R.2    Follo, C.3    Peracchio, C.4    Valente, G.5    Isidoro, C.6
  • 96
    • 79960117895 scopus 로고    scopus 로고
    • Breast cancer cells produce tenascin C as a metastatic niche component to colonize the lungs
    • Oskarsson T., Acharyya S., Zhang X.H., Vanharanta S., Tavazoie S.F., Morris P.G., et al. Breast cancer cells produce tenascin C as a metastatic niche component to colonize the lungs. Nat Med 2011, 17:867-874.
    • (2011) Nat Med , vol.17 , pp. 867-874
    • Oskarsson, T.1    Acharyya, S.2    Zhang, X.H.3    Vanharanta, S.4    Tavazoie, S.F.5    Morris, P.G.6
  • 97
    • 39049160268 scopus 로고    scopus 로고
    • Critical role of the stress chaperone GRP78/BiP in tumor proliferation, survival, and tumor angiogenesis in transgene-induced mammary tumor development
    • Dong D., Ni M., Li J., Xiong S., Ye W., Virrey J.J., et al. Critical role of the stress chaperone GRP78/BiP in tumor proliferation, survival, and tumor angiogenesis in transgene-induced mammary tumor development. Cancer Res 2008, 68:498-505.
    • (2008) Cancer Res , vol.68 , pp. 498-505
    • Dong, D.1    Ni, M.2    Li, J.3    Xiong, S.4    Ye, W.5    Virrey, J.J.6
  • 98
    • 78049381358 scopus 로고    scopus 로고
    • Proteomic and PROTEOMEX profiling of mammary cancer progression in a HER-2/neu oncogene-driven animal model system
    • Croci S., Recktenwald C.V., Lichtenfels R., Nicoletti G., Dressler S.P., De Giovanni C., et al. Proteomic and PROTEOMEX profiling of mammary cancer progression in a HER-2/neu oncogene-driven animal model system. Proteomics 2010, 10:3835-3853.
    • (2010) Proteomics , vol.10 , pp. 3835-3853
    • Croci, S.1    Recktenwald, C.V.2    Lichtenfels, R.3    Nicoletti, G.4    Dressler, S.P.5    De Giovanni, C.6
  • 100
    • 40349106087 scopus 로고    scopus 로고
    • Identification of the functional role of peroxiredoxin 6 in the progression of breast cancer
    • Chang X.Z., Li D.Q., Hou Y.F., Wu J., Lu J.S., Di G.H., et al. Identification of the functional role of peroxiredoxin 6 in the progression of breast cancer. Breast Cancer Res 2007, 9:R76.
    • (2007) Breast Cancer Res , vol.9
    • Chang, X.Z.1    Li, D.Q.2    Hou, Y.F.3    Wu, J.4    Lu, J.S.5    Di, G.H.6
  • 101
  • 102
    • 77956933047 scopus 로고    scopus 로고
    • Heat shock proteins in breast cancer progression-a suitable case for treatment?
    • Calderwood S.K. Heat shock proteins in breast cancer progression-a suitable case for treatment?. Int J Hyperthermia 2010, 26:681-685.
    • (2010) Int J Hyperthermia , vol.26 , pp. 681-685
    • Calderwood, S.K.1
  • 103
    • 77957843649 scopus 로고    scopus 로고
    • Coordinated expression of galectin-3 and galectin-3-binding sites in malignant mammary tumors: implications for tumor metastasis
    • de Oliveira J.T., de Matos A.J., Gomes J., Vilanova M., Hespanhol V., Manninen A., et al. Coordinated expression of galectin-3 and galectin-3-binding sites in malignant mammary tumors: implications for tumor metastasis. Glycobiology 2010, 20:1341-1352.
    • (2010) Glycobiology , vol.20 , pp. 1341-1352
    • de Oliveira, J.T.1    de Matos, A.J.2    Gomes, J.3    Vilanova, M.4    Hespanhol, V.5    Manninen, A.6
  • 104
    • 80054757041 scopus 로고    scopus 로고
    • Overexpression of alpha-enolase correlates with poor survival in canine mammary carcinoma
    • Chu P.Y., Hsu N.C., Liao A.T., Shih N.Y., Hou M.F., Liu C.H. Overexpression of alpha-enolase correlates with poor survival in canine mammary carcinoma. BMC Vet Res 2011, 7:62.
    • (2011) BMC Vet Res , vol.7 , pp. 62
    • Chu, P.Y.1    Hsu, N.C.2    Liao, A.T.3    Shih, N.Y.4    Hou, M.F.5    Liu, C.H.6
  • 105
    • 44849101183 scopus 로고    scopus 로고
    • Suppression of adenine nucleotide translocase-2 by vector-based siRNA in human breast cancer cells induces apoptosis and inhibits tumor growth in vitro and in vivo
    • Jang J.Y., Choi Y., Jeon Y.K., Kim C.W. Suppression of adenine nucleotide translocase-2 by vector-based siRNA in human breast cancer cells induces apoptosis and inhibits tumor growth in vitro and in vivo. Breast Cancer Res 2008, 10:R11.
    • (2008) Breast Cancer Res , vol.10
    • Jang, J.Y.1    Choi, Y.2    Jeon, Y.K.3    Kim, C.W.4
  • 107
    • 53049096831 scopus 로고    scopus 로고
    • Functional clustering of metastasis proteins describes plastic adaptation resources of breast-cancer cells to new microenvironments
    • Martin B., Sanz R., Aragues R., Oliva B., Sierra A. Functional clustering of metastasis proteins describes plastic adaptation resources of breast-cancer cells to new microenvironments. J Proteome Res 2008, 7:3242-3253.
    • (2008) J Proteome Res , vol.7 , pp. 3242-3253
    • Martin, B.1    Sanz, R.2    Aragues, R.3    Oliva, B.4    Sierra, A.5
  • 108
    • 55249086768 scopus 로고    scopus 로고
    • Proteomics-based identification of HSP60 as a tumor-associated antigen in early stage breast cancer and ductal carcinoma in situ
    • Desmetz C., Bibeau F., Boissiere F., Bellet V., Rouanet P., Maudelonde T., et al. Proteomics-based identification of HSP60 as a tumor-associated antigen in early stage breast cancer and ductal carcinoma in situ. J Proteome Res 2008, 7:3830-3837.
    • (2008) J Proteome Res , vol.7 , pp. 3830-3837
    • Desmetz, C.1    Bibeau, F.2    Boissiere, F.3    Bellet, V.4    Rouanet, P.5    Maudelonde, T.6
  • 109
    • 34548182286 scopus 로고    scopus 로고
    • Tissue preparation: tissue issues
    • Blow N. Tissue preparation: tissue issues. Nature 2007, 448:959-963.
    • (2007) Nature , vol.448 , pp. 959-963
    • Blow, N.1
  • 110
    • 70350215650 scopus 로고    scopus 로고
    • Tissue is alive: new technologies are needed to address the problems of protein biomarker pre-analytical variability
    • Espina V., Mueller C., Edmiston K., Sciro M., Petricoin E.F., Liotta L.A. Tissue is alive: new technologies are needed to address the problems of protein biomarker pre-analytical variability. Proteomics Clin Appl 2009, 3:874-882.
    • (2009) Proteomics Clin Appl , vol.3 , pp. 874-882
    • Espina, V.1    Mueller, C.2    Edmiston, K.3    Sciro, M.4    Petricoin, E.F.5    Liotta, L.A.6
  • 111
    • 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
  • 112
    • 45749127864 scopus 로고    scopus 로고
    • Mining the archival formalin-fixed paraffin-embedded tissue proteome: opportunities and challenges
    • Nirmalan N.J., Harnden P., Selby P.J., Banks R.E. Mining the archival formalin-fixed paraffin-embedded tissue proteome: opportunities and challenges. Mol Biosyst 2008, 4:712.
    • (2008) Mol Biosyst , vol.4 , pp. 712
    • Nirmalan, N.J.1    Harnden, P.2    Selby, P.J.3    Banks, R.E.4
  • 113
    • 79551641520 scopus 로고    scopus 로고
    • Successful protein extraction from over-fixed and long-term stored formalin-fixed tissues
    • Wolff C., Schott C., Porschewski P., Reischauer B., Becker K.F. Successful protein extraction from over-fixed and long-term stored formalin-fixed tissues. PLoS One 2011, 6:e16353.
    • (2011) PLoS One , vol.6
    • Wolff, C.1    Schott, C.2    Porschewski, P.3    Reischauer, B.4    Becker, K.F.5
  • 114
    • 76149142168 scopus 로고    scopus 로고
    • Repeatability and reproducibility in proteomic identifications by liquid chromatography-tandem mass spectrometry
    • Tabb D.L., Vega-Montoto L., Rudnick P.A., Variyath A.M., Ham A.J., Bunk D.M., et al. Repeatability and reproducibility in proteomic identifications by liquid chromatography-tandem mass spectrometry. J Proteome Res 2010, 9:761-776.
    • (2010) J Proteome Res , vol.9 , pp. 761-776
    • Tabb, D.L.1    Vega-Montoto, L.2    Rudnick, P.A.3    Variyath, A.M.4    Ham, A.J.5    Bunk, D.M.6
  • 115
    • 79951731085 scopus 로고    scopus 로고
    • Application of 2-D DIGE to formalin-fixed, paraffin-embedded tissues
    • Tanca A., Pagnozzi D., Falchi G., Tonelli R., Rocca S., Roggio T., et al. Application of 2-D DIGE to formalin-fixed, paraffin-embedded tissues. Proteomics 2011, 11:1005-1011.
    • (2011) Proteomics , vol.11 , pp. 1005-1011
    • Tanca, A.1    Pagnozzi, D.2    Falchi, G.3    Tonelli, R.4    Rocca, S.5    Roggio, T.6
  • 116
    • 70349136284 scopus 로고    scopus 로고
    • 2-D PAGE and MS analysis of proteins from formalin-fixed, paraffin-embedded tissues
    • Addis M.F., Tanca A., Pagnozzi D., Rocca S., Uzzau S. 2-D PAGE and MS analysis of proteins from formalin-fixed, paraffin-embedded tissues. Proteomics 2009, 9:4329-4339.
    • (2009) Proteomics , vol.9 , pp. 4329-4339
    • Addis, M.F.1    Tanca, A.2    Pagnozzi, D.3    Rocca, S.4    Uzzau, S.5
  • 117
    • 84861715116 scopus 로고    scopus 로고
    • Evaluation of the suitability of archival Bouin-fixed paraffin-embedded tissue specimens to proteomic investigation
    • Tanca A., Addis M.F., Simula M.P., Pagnozzi D., Biosa G., Pisanu S., et al. Evaluation of the suitability of archival Bouin-fixed paraffin-embedded tissue specimens to proteomic investigation. Electrophoresis 2012, 33:1375-1384.
    • (2012) Electrophoresis , vol.33 , pp. 1375-1384
    • Tanca, A.1    Addis, M.F.2    Simula, M.P.3    Pagnozzi, D.4    Biosa, G.5    Pisanu, S.6


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.