메뉴 건너뛰기




Volumn 1834, Issue 11, 2013, Pages 2285-2292

Secretome analysis using a hollow fiber culture system for cancer biomarker discovery

Author keywords

Cancer biomarker; Conditioned medium (CM); Hollow fiber culture (HFC) system; Proteome; Secretome

Indexed keywords

ACTIN; ALPHA 1 ANTITRYPSIN; BIOLOGICAL MARKER; CA 19-9 ANTIGEN; CATHEPSIN B; CATHEPSIN D; CHAPERONIN 60; COLLAGEN TYPE 1; DESMIN; ENTACTIN; GELSOLIN; GLUTAREDOXIN; GLYCERALDEHYDE 3 PHOSPHATE DEHYDROGENASE; LACTATE DEHYDROGENASE; LAMIN A; LAMIN C; LIPOCORTIN 5; PEROXIREDOXIN 1; PHOSPHOGLUCOMUTASE; PROTEIN SH3; RETINAL DEHYDROGENASE; THIOREDOXIN; THIOREDOXIN REDUCTASE; TISSUE INHIBITOR OF METALLOPROTEINASE 1; TRANSGELIN; TUBULIN; TUMOR MARKER; UROKINASE; VIMENTIN;

EID: 84884669027     PISSN: 15709639     EISSN: 18781454     Source Type: Journal    
DOI: 10.1016/j.bbapap.2013.01.033     Document Type: Article
Times cited : (8)

References (79)
  • 1
    • 84859220149 scopus 로고    scopus 로고
    • Secreted proteins as a fundamental source for biomarker discovery
    • M. Stastna, and J.E. Van Eyk Secreted proteins as a fundamental source for biomarker discovery Proteomics 12 2012 722 735
    • (2012) Proteomics , vol.12 , pp. 722-735
    • Stastna, M.1    Van Eyk, J.E.2
  • 2
    • 77956403452 scopus 로고    scopus 로고
    • Proteomics of colorectal cancer: Overview of discovery studies and identification of commonly identified cancer-associated proteins and candidate CRC serum markers
    • C.R. Jimenez, J.C. Knol, G.A. Meijer, and R.J. Fijneman Proteomics of colorectal cancer: overview of discovery studies and identification of commonly identified cancer-associated proteins and candidate CRC serum markers J. Proteomics 73 2010 1873 1895
    • (2010) J. Proteomics , vol.73 , pp. 1873-1895
    • Jimenez, C.R.1    Knol, J.C.2    Meijer, G.A.3    Fijneman, R.J.4
  • 3
    • 65249161129 scopus 로고    scopus 로고
    • Pathway-based biomarker search by high-throughput proteomics profiling of secretomes
    • K. Lawlor, A. Nazarian, L. Lacomis, P. Tempst, and J. Villanueva Pathway-based biomarker search by high-throughput proteomics profiling of secretomes J. Proteome Res. 8 2009 1489 1503
    • (2009) J. Proteome Res. , vol.8 , pp. 1489-1503
    • Lawlor, K.1    Nazarian, A.2    Lacomis, L.3    Tempst, P.4    Villanueva, J.5
  • 4
    • 80053927128 scopus 로고    scopus 로고
    • Comprehensive proteome analysis of malignant pleural effusion for lung cancer biomarker discovery by using multidimensional protein identification technology
    • C.J. Yu, C.L. Wang, C.I. Wang, C.D. Chen, Y.M. Dan, C.C. Wu, Y.C. Wu, I.N. Lee, Y.H. Tsai, Y.S. Chang, and J.S. Yu Comprehensive proteome analysis of malignant pleural effusion for lung cancer biomarker discovery by using multidimensional protein identification technology J. Proteome Res. 10 2011 4671 4682
    • (2011) J. Proteome Res. , vol.10 , pp. 4671-4682
    • Yu, C.J.1    Wang, C.L.2    Wang, C.I.3    Chen, C.D.4    Dan, Y.M.5    Wu, C.C.6    Wu, Y.C.7    Lee, I.N.8    Tsai, Y.H.9    Chang, Y.S.10    Yu, J.S.11
  • 6
    • 78751651074 scopus 로고    scopus 로고
    • Comparison of alternative extraction methods for secretome profiling in human hepatocellular carcinoma cells
    • J. Cao, C. Shen, J. Zhang, J. Yao, H. Shen, Y. Liu, H. Lu, and P. Yang Comparison of alternative extraction methods for secretome profiling in human hepatocellular carcinoma cells Sci. China 54 2011 34 38
    • (2011) Sci. China , vol.54 , pp. 34-38
    • Cao, J.1    Shen, C.2    Zhang, J.3    Yao, J.4    Shen, H.5    Liu, Y.6    Lu, H.7    Yang, P.8
  • 7
    • 23944498611 scopus 로고    scopus 로고
    • Proteomic profiling of human pleural effusion using two-dimensional nano liquid chromatography tandem mass spectrometry
    • Y.C. Tyan, H.Y. Wu, W.W. Lai, W.C. Su, and P.C. Liao Proteomic profiling of human pleural effusion using two-dimensional nano liquid chromatography tandem mass spectrometry J. Proteome Res. 4 2005 1274 1286
    • (2005) J. Proteome Res. , vol.4 , pp. 1274-1286
    • Tyan, Y.C.1    Wu, H.Y.2    Lai, W.W.3    Su, W.C.4    Liao, P.C.5
  • 11
    • 81855166737 scopus 로고    scopus 로고
    • Mining the malignant ascites proteome for pancreatic cancer biomarkers
    • H. Kosanam, S. Makawita, B. Judd, A. Newman, and E.P. Diamandis Mining the malignant ascites proteome for pancreatic cancer biomarkers Proteomics 11 2011 4551 4558
    • (2011) Proteomics , vol.11 , pp. 4551-4558
    • Kosanam, H.1    Makawita, S.2    Judd, B.3    Newman, A.4    Diamandis, E.P.5
  • 12
    • 84885689078 scopus 로고    scopus 로고
    • Proteomic analysis of breast tissue and nipple aspirate fluid for breast cancer detection
    • R.L. Ruhlen, and E.R. Sauter Proteomic analysis of breast tissue and nipple aspirate fluid for breast cancer detection Biomark. Med. 1 2007 251 260
    • (2007) Biomark. Med. , vol.1 , pp. 251-260
    • Ruhlen, R.L.1    Sauter, E.R.2
  • 13
    • 37149054901 scopus 로고    scopus 로고
    • Proteomics of nipple aspirate fluid, breast cyst fluid, milk, and colostrum
    • R.L. Ruhlen, and E.R. Sauter Proteomics of nipple aspirate fluid, breast cyst fluid, milk, and colostrum Proteomics Clin. Appl. 1 2007 845 852
    • (2007) Proteomics Clin. Appl. , vol.1 , pp. 845-852
    • Ruhlen, R.L.1    Sauter, E.R.2
  • 14
    • 70350747771 scopus 로고    scopus 로고
    • Proteomics and the lung: Analysis of bronchoalveolar lavage fluid
    • P. Govender, M.J. Dunn, and S.C. Donnelly Proteomics and the lung: analysis of bronchoalveolar lavage fluid Proteomics Clin. Appl. 3 2009 1044 1051
    • (2009) Proteomics Clin. Appl. , vol.3 , pp. 1044-1051
    • Govender, P.1    Dunn, M.J.2    Donnelly, S.C.3
  • 15
    • 79958745909 scopus 로고    scopus 로고
    • Defining salivary biomarkers using mass spectrometry-based proteomics: A systematic review
    • S.K. Al-Tarawneh, M.B. Border, C.F. Dibble, and S. Bencharit Defining salivary biomarkers using mass spectrometry-based proteomics: a systematic review OMICS 15 2011 353 361
    • (2011) OMICS , vol.15 , pp. 353-361
    • Al-Tarawneh, S.K.1    Border, M.B.2    Dibble, C.F.3    Bencharit, S.4
  • 16
    • 84863981406 scopus 로고    scopus 로고
    • Mass spectrometry-based salivary proteomics for the discovery of head and neck squamous cell carcinoma
    • T. Jarai, G. Maasz, A. Burian, A. Bona, E. Jambor, I. Gerlinger, and L. Mark Mass spectrometry-based salivary proteomics for the discovery of head and neck squamous cell carcinoma Pathol. Oncol. Res. 18 2012 623 628
    • (2012) Pathol. Oncol. Res. , vol.18 , pp. 623-628
    • Jarai, T.1    Maasz, G.2    Burian, A.3    Bona, A.4    Jambor, E.5    Gerlinger, I.6    Mark, L.7
  • 21
    • 79551493048 scopus 로고    scopus 로고
    • Conditioned media from cell lines: A complementary model to clinical specimens for the discovery of disease-specific biomarkers
    • P. Dowling, and M. Clynes Conditioned media from cell lines: a complementary model to clinical specimens for the discovery of disease-specific biomarkers Proteomics 11 2011 794 804
    • (2011) Proteomics , vol.11 , pp. 794-804
    • Dowling, P.1    Clynes, M.2
  • 22
    • 71549131311 scopus 로고    scopus 로고
    • Cell secretome analysis using hollow fiber culture system leads to the discovery of CLIC1 protein as a novel plasma marker for nasopharyngeal carcinoma
    • Y.H. Chang, C.C. Wu, K.P. Chang, J.S. Yu, Y.C. Chang, and P.C. Liao Cell secretome analysis using hollow fiber culture system leads to the discovery of CLIC1 protein as a novel plasma marker for nasopharyngeal carcinoma J. Proteome Res. 8 2009 5465 5474
    • (2009) J. Proteome Res. , vol.8 , pp. 5465-5474
    • Chang, Y.H.1    Wu, C.C.2    Chang, K.P.3    Yu, J.S.4    Chang, Y.C.5    Liao, P.C.6
  • 23
    • 79952382501 scopus 로고    scopus 로고
    • Quantitative secretome analysis reveals that COL6A1 is a metastasis-associated protein using stacking gel-aided purification combined with iTRAQ labeling
    • K.H. Chiu, Y.H. Chang, Y.S. Wu, S.H. Lee, and P.C. Liao Quantitative secretome analysis reveals that COL6A1 is a metastasis-associated protein using stacking gel-aided purification combined with iTRAQ labeling J. Proteome Res. 10 2011 1110 1125
    • (2011) J. Proteome Res. , vol.10 , pp. 1110-1125
    • Chiu, K.H.1    Chang, Y.H.2    Wu, Y.S.3    Lee, S.H.4    Liao, P.C.5
  • 24
    • 77957755656 scopus 로고    scopus 로고
    • Secretome proteomics for discovery of cancer biomarkers
    • M. Makridakis, and A. Vlahou Secretome proteomics for discovery of cancer biomarkers J. Proteomics 73 2010 2291 2305
    • (2010) J. Proteomics , vol.73 , pp. 2291-2305
    • Makridakis, M.1    Vlahou, A.2
  • 25
    • 63849247205 scopus 로고    scopus 로고
    • Proteomics strategies for target identification and biomarker discovery in cancer
    • U. Rajcevic, S.P. Niclou, and C.R. Jimenez Proteomics strategies for target identification and biomarker discovery in cancer Front. Biosci. 14 2009 3292 3303
    • (2009) Front. Biosci. , vol.14 , pp. 3292-3303
    • Rajcevic, U.1    Niclou, S.P.2    Jimenez, C.R.3
  • 26
    • 70349972788 scopus 로고    scopus 로고
    • Discovery of retinoblastoma-associated binding protein 46 as a novel prognostic marker for distant metastasis in nonsmall cell lung cancer by combined analysis of cancer cell secretome and pleural effusion proteome
    • C.L. Wang, C.I. Wang, P.C. Liao, C.D. Chen, Y. Liang, W.Y. Chuang, Y.H. Tsai, H.C. Chen, Y.S. Chang, J.S. Yu, C.C. Wu, and C.J. Yu Discovery of retinoblastoma-associated binding protein 46 as a novel prognostic marker for distant metastasis in nonsmall cell lung cancer by combined analysis of cancer cell secretome and pleural effusion proteome J. Proteome Res. 8 2009 4428 4440
    • (2009) J. Proteome Res. , vol.8 , pp. 4428-4440
    • Wang, C.L.1    Wang, C.I.2    Liao, P.C.3    Chen, C.D.4    Liang, Y.5    Chuang, W.Y.6    Tsai, Y.H.7    Chen, H.C.8    Chang, Y.S.9    Yu, J.S.10    Wu, C.C.11    Yu, C.J.12
  • 27
    • 78650173202 scopus 로고    scopus 로고
    • Collection of in vivo-like liver cell secretome with alternative sample enrichment method using a hollow fiber bioreactor culture system combined with tangential flow filtration for secretomics analysis
    • Y.T. Wen, Y.C. Chang, L.C. Lin, and P.C. Liao Collection of in vivo-like liver cell secretome with alternative sample enrichment method using a hollow fiber bioreactor culture system combined with tangential flow filtration for secretomics analysis Anal. Chim. Acta 684 2011 72 79
    • (2011) Anal. Chim. Acta , vol.684 , pp. 72-79
    • Wen, Y.T.1    Chang, Y.C.2    Lin, L.C.3    Liao, P.C.4
  • 28
    • 60849139466 scopus 로고    scopus 로고
    • Proteomics analysis of nasopharyngeal carcinoma cell secretome using a hollow fiber culture system and mass spectrometry
    • H.Y. Wu, Y.H. Chang, Y.C. Chang, and P.C. Liao Proteomics analysis of nasopharyngeal carcinoma cell secretome using a hollow fiber culture system and mass spectrometry J. Proteome Res. 8 2009 380 389
    • (2009) J. Proteome Res. , vol.8 , pp. 380-389
    • Wu, H.Y.1    Chang, Y.H.2    Chang, Y.C.3    Liao, P.C.4
  • 29
    • 84855430076 scopus 로고    scopus 로고
    • Lectin capture strategy for effective analysis of cell secretome
    • Y. Zhang, X. Tang, L. Yao, K. Chen, W. Jia, X. Hu, and L.X. Xu Lectin capture strategy for effective analysis of cell secretome Proteomics 12 2012 32 36
    • (2012) Proteomics , vol.12 , pp. 32-36
    • Zhang, Y.1    Tang, X.2    Yao, L.3    Chen, K.4    Jia, W.5    Hu, X.6    Xu, L.X.7
  • 30
    • 78649854676 scopus 로고    scopus 로고
    • 2D-DiGE analysis of the human endometrial secretome reveals differences between receptive and nonreceptive states in fertile and infertile women
    • N.J. Hannan, A.N. Stephens, A. Rainczuk, C. Hincks, L.J. Rombauts, and L.A. Salamonsen 2D-DiGE analysis of the human endometrial secretome reveals differences between receptive and nonreceptive states in fertile and infertile women J. Proteome Res. 9 2010 6256 6264
    • (2010) J. Proteome Res. , vol.9 , pp. 6256-6264
    • Hannan, N.J.1    Stephens, A.N.2    Rainczuk, A.3    Hincks, C.4    Rombauts, L.J.5    Salamonsen, L.A.6
  • 31
    • 38649105460 scopus 로고    scopus 로고
    • Application of 2-dimensional difference gel electrophoresis (2D-DIGE) to the study of thrombin-activated human platelet secretome
    • DOI 10.1080/09537100701609035, PII 790039150
    • A. Della Corte, N. Maugeri, A. Pampuch, C. Cerletti, G. de Gaetano, and D. Rotilio Application of 2-dimensional difference gel electrophoresis (2D-DIGE) to the study of thrombin-activated human platelet secretome Platelets 19 2008 43 50 (Pubitemid 351171556)
    • (2008) Platelets , vol.19 , Issue.1 , pp. 43-50
    • Della Corte, A.1    Maugeri, N.2    Pampuch, A.3    Cerletti, C.4    De Gaetano, G.5    Rotilio, D.6
  • 32
    • 21744436492 scopus 로고    scopus 로고
    • Proteomic analyzes of copper metabolism in an in vitro model of Wilson disease using surface enhanced laser desorption/ionization-time of flight-mass spectrometry
    • DOI 10.1002/jcb.20226
    • H. Roelofsen, R. Balgobind, and R.J. Vonk Proteomic analyzes of copper metabolism in an in vitro model of Wilson disease using surface enhanced laser desorption/ionization-time of flight-mass spectrometry J. Cell. Biochem. 93 2004 732 740 (Pubitemid 44264169)
    • (2004) Journal of Cellular Biochemistry , vol.93 , Issue.4 , pp. 732-740
    • Roelofsen, H.1    Balgobind, R.2    Vonk, R.J.3
  • 33
    • 84868314556 scopus 로고    scopus 로고
    • Comparative secretome analyses using a hollow fiber culture system with label-free quantitative proteomics indicates the influence of PARK7 on cell proliferation and migration/invasion in lung adenocarcinoma
    • Y.H. Chang, S.H. Lee, H.C. Chang, Y.L. Tseng, W.W. Lai, C.C. Liao, Y.G. Tsay, and P.C. Liao Comparative secretome analyses using a hollow fiber culture system with label-free quantitative proteomics indicates the influence of PARK7 on cell proliferation and migration/invasion in lung adenocarcinoma J. Proteome Res. 11 2012 5167 5185
    • (2012) J. Proteome Res. , vol.11 , pp. 5167-5185
    • Chang, Y.H.1    Lee, S.H.2    Chang, H.C.3    Tseng, Y.L.4    Lai, W.W.5    Liao, C.C.6    Tsay, Y.G.7    Liao, P.C.8
  • 34
    • 82755161136 scopus 로고    scopus 로고
    • EGFR isoforms in exosomes as a novel method for biomarker discovery in pancreatic cancer
    • W.T. Arscott, and K.A. Camphausen EGFR isoforms in exosomes as a novel method for biomarker discovery in pancreatic cancer Biomark. Med. 5 2011 821
    • (2011) Biomark. Med. , vol.5 , pp. 821
    • Arscott, W.T.1    Camphausen, K.A.2
  • 35
    • 84870853677 scopus 로고    scopus 로고
    • The utility of a high-throughput scanning biosensor in the detection of the pancreatic cancer marker ULBP2
    • Y.F. Chang, J.S. Yu, Y.T. Chang, L.C. Su, C.C. Wu, Y.S. Chang, C.S. Lai, and C. Chou The utility of a high-throughput scanning biosensor in the detection of the pancreatic cancer marker ULBP2 Biosens. Bioelectron. 41 2012 232 237
    • (2012) Biosens. Bioelectron. , vol.41 , pp. 232-237
    • Chang, Y.F.1    Yu, J.S.2    Chang, Y.T.3    Su, L.C.4    Wu, C.C.5    Chang, Y.S.6    Lai, C.S.7    Chou, C.8
  • 36
    • 70349972378 scopus 로고    scopus 로고
    • The cell line secretome, a suitable tool for investigating proteins released in vivo by tumors: Application to the study of p53-modulated proteins secreted in lung cancer cells
    • J. Chenau, S. Michelland, F. de Fraipont, V. Josserand, J.L. Coll, M.C. Favrot, and M. Seve The cell line secretome, a suitable tool for investigating proteins released in vivo by tumors: application to the study of p53-modulated proteins secreted in lung cancer cells J. Proteome Res. 8 2009 4579 4591
    • (2009) J. Proteome Res. , vol.8 , pp. 4579-4591
    • Chenau, J.1    Michelland, S.2    De Fraipont, F.3    Josserand, V.4    Coll, J.L.5    Favrot, M.C.6    Seve, M.7
  • 37
    • 79953243174 scopus 로고    scopus 로고
    • Exosomes as biomarker treasure chests for prostate cancer
    • D. Duijvesz, T. Luider, C.H. Bangma, and G. Jenster Exosomes as biomarker treasure chests for prostate cancer Eur. Urol. 59 2011 823 831
    • (2011) Eur. Urol. , vol.59 , pp. 823-831
    • Duijvesz, D.1    Luider, T.2    Bangma, C.H.3    Jenster, G.4
  • 38
    • 53049099609 scopus 로고    scopus 로고
    • Proteomic analysis of conditioned media from the PC3, LNCaP, and 22Rv1 prostate cancer cell lines: Discovery and validation of candidate prostate cancer biomarkers
    • G. Sardana, K. Jung, C. Stephan, and E.P. Diamandis Proteomic analysis of conditioned media from the PC3, LNCaP, and 22Rv1 prostate cancer cell lines: discovery and validation of candidate prostate cancer biomarkers J. Proteome Res. 7 2008 3329 3338
    • (2008) J. Proteome Res. , vol.7 , pp. 3329-3338
    • Sardana, G.1    Jung, K.2    Stephan, C.3    Diamandis, E.P.4
  • 39
    • 33947357719 scopus 로고    scopus 로고
    • Discovery of candidate tumor markers for prostate cancer via proteomic analysis of cell culture - Conditioned medium
    • DOI 10.1373/clinchem.2006.077370
    • G. Sardana, J. Marshall, and E.P. Diamandis Discovery of candidate tumor markers for prostate cancer via proteomic analysis of cell culture-conditioned medium Clin. Chem. 53 2007 429 437 (Pubitemid 46447939)
    • (2007) Clinical Chemistry , vol.53 , Issue.3 , pp. 429-437
    • Sardana, G.1    Marshall, J.2    Diamandis, E.P.3
  • 41
    • 84873125767 scopus 로고    scopus 로고
    • Worldwide Oesophageal Cancer Collaboration guidelines for lymphadenectomy predict survival following neoadjuvant therapy
    • B.M. Stiles, A. Nasar, F.A. Mirza, P.C. Lee, S. Paul, J.L. Port, and N.K. Altorki Worldwide Oesophageal Cancer Collaboration guidelines for lymphadenectomy predict survival following neoadjuvant therapy Eur. J. Cardiothorac. Surg. 42 2012 659 664
    • (2012) Eur. J. Cardiothorac. Surg. , vol.42 , pp. 659-664
    • Stiles, B.M.1    Nasar, A.2    Mirza, F.A.3    Lee, P.C.4    Paul, S.5    Port, J.L.6    Altorki, N.K.7
  • 42
    • 78649300008 scopus 로고    scopus 로고
    • Cancer-related forecast biomarkers: A topic in focus of the Worldwide Innovative Network in Personalized Cancer Medicine
    • WIN
    • M. Schmitt, and V. Lazar Cancer-related forecast biomarkers: a topic in focus of the Worldwide Innovative Network in Personalized Cancer Medicine WIN Bioanalysis 2 2010 851 853
    • (2010) Bioanalysis , vol.2 , pp. 851-853
    • Schmitt, M.1    Lazar, V.2
  • 44
    • 84355165978 scopus 로고    scopus 로고
    • Current status of therapy for breast cancer worldwide and in Japan
    • Y. Park, T. Kitahara, R. Takagi, and R. Kato Current status of therapy for breast cancer worldwide and in Japan World J. Clin. Oncol. 2 2011 125 134
    • (2011) World J. Clin. Oncol. , vol.2 , pp. 125-134
    • Park, Y.1    Kitahara, T.2    Takagi, R.3    Kato, R.4
  • 46
    • 84860322847 scopus 로고    scopus 로고
    • A systematic review of worldwide incidence of nonmelanoma skin cancer
    • A. Lomas, J. Leonardi-Bee, and F. Bath-Hextall A systematic review of worldwide incidence of nonmelanoma skin cancer Br. J. Dermatol. 166 2012 1069 1080
    • (2012) Br. J. Dermatol. , vol.166 , pp. 1069-1080
    • Lomas, A.1    Leonardi-Bee, J.2    Bath-Hextall, F.3
  • 48
    • 79955689408 scopus 로고    scopus 로고
    • Breast cancer: A neglected disease for the majority of affected women worldwide
    • O.M. Ginsburg, and R.R. Love Breast cancer: a neglected disease for the majority of affected women worldwide Breast J. 17 2011 289 295
    • (2011) Breast J. , vol.17 , pp. 289-295
    • Ginsburg, O.M.1    Love, R.R.2
  • 51
    • 84867117645 scopus 로고    scopus 로고
    • Exosomes as biomarker enriched microvesicles: Characterization of exosomal proteins derived from a panel of prostate cell lines with distinct AR phenotypes
    • E. Hosseini-Beheshti, S. Pham, H. Adomat, N. Li, and E.S. Tomlinson Guns Exosomes as biomarker enriched microvesicles: characterization of exosomal proteins derived from a panel of prostate cell lines with distinct AR phenotypes Mol. Cell. Proteomics 11 2012 863 885
    • (2012) Mol. Cell. Proteomics , vol.11 , pp. 863-885
    • Hosseini-Beheshti, E.1    Pham, S.2    Adomat, H.3    Li, N.4    Tomlinson Guns, E.S.5
  • 52
    • 84861678077 scopus 로고    scopus 로고
    • A multiplex quantitative proteomics strategy for protein biomarker studies in urinary exosomes
    • D.A. Raj, I. Fiume, G. Capasso, and G. Pocsfalvi A multiplex quantitative proteomics strategy for protein biomarker studies in urinary exosomes Kidney Int. 81 2012 1263 1272
    • (2012) Kidney Int. , vol.81 , pp. 1263-1272
    • Raj, D.A.1    Fiume, I.2    Capasso, G.3    Pocsfalvi, G.4
  • 54
    • 77951152406 scopus 로고    scopus 로고
    • An exosome-based secretion pathway is responsible for protein export from Leishmania and communication with macrophages
    • J.M. Silverman, J. Clos, C.C. de'Oliveira, O. Shirvani, Y. Fang, C. Wang, L.J. Foster, and N.E. Reiner An exosome-based secretion pathway is responsible for protein export from Leishmania and communication with macrophages J. Cell Sci. 123 2010 842 852
    • (2010) J. Cell Sci. , vol.123 , pp. 842-852
    • Silverman, J.M.1    Clos, J.2    De'Oliveira, C.C.3    Shirvani, O.4    Fang, Y.5    Wang, C.6    Foster, L.J.7    Reiner, N.E.8
  • 55
    • 54049088501 scopus 로고    scopus 로고
    • Exosome secretion, including the DNA damage-induced p53-dependent secretory pathway, is severely compromised in TSAP6/Steap3-null mice
    • A. Lespagnol, D. Duflaut, C. Beekman, L. Blanc, G. Fiucci, J.C. Marine, M. Vidal, R. Amson, and A. Telerman Exosome secretion, including the DNA damage-induced p53-dependent secretory pathway, is severely compromised in TSAP6/Steap3-null mice Cell Death Differ. 15 2008 1723 1733
    • (2008) Cell Death Differ. , vol.15 , pp. 1723-1733
    • Lespagnol, A.1    Duflaut, D.2    Beekman, C.3    Blanc, L.4    Fiucci, G.5    Marine, J.C.6    Vidal, M.7    Amson, R.8    Telerman, A.9
  • 56
    • 33646416463 scopus 로고    scopus 로고
    • The regulation of exosome secretion: A novel function of the p53 protein
    • X. Yu, S.L. Harris, and A.J. Levine The regulation of exosome secretion: a novel function of the p53 protein Cancer Res. 66 2006 4795 4801
    • (2006) Cancer Res. , vol.66 , pp. 4795-4801
    • Yu, X.1    Harris, S.L.2    Levine, A.J.3
  • 57
    • 0037096162 scopus 로고    scopus 로고
    • The exosome pathway in K562 cells is regulated by Rab11
    • A. Savina, M. Vidal, and M.I. Colombo The exosome pathway in K562 cells is regulated by Rab11 J. Cell Sci. 115 2002 2505 2515 (Pubitemid 34778068)
    • (2002) Journal of Cell Science , vol.115 , Issue.12 , pp. 2505-2515
    • Savina, A.1    Vidal, M.2    Colombo, M.I.3
  • 59
    • 84858214763 scopus 로고    scopus 로고
    • Secretome of human bronchial epithelial cells in response to the fungal pathogen Aspergillus fumigatus analyzed by differential in-gel electrophoresis
    • A. Fekkar, V. Balloy, C. Pionneau, C. Marinach-Patrice, M. Chignard, and D. Mazier Secretome of human bronchial epithelial cells in response to the fungal pathogen Aspergillus fumigatus analyzed by differential in-gel electrophoresis J. Infect. Dis. 205 2012 1163 1172
    • (2012) J. Infect. Dis. , vol.205 , pp. 1163-1172
    • Fekkar, A.1    Balloy, V.2    Pionneau, C.3    Marinach-Patrice, C.4    Chignard, M.5    Mazier, D.6
  • 61
    • 1242342176 scopus 로고    scopus 로고
    • Oxygen consumption in a hollow fiber bioartificial liver-revisited
    • J.F. Patzer 2nd Oxygen consumption in a hollow fiber bioartificial liver-revisited Artif. Organs 28 2004 83 98
    • (2004) Artif. Organs , vol.28 , pp. 83-98
    • Patzer II, J.F.1
  • 62
  • 63
    • 0032861711 scopus 로고    scopus 로고
    • Bioartificial liver support system using porcine hepatocytes entrapped in a three-dimensional hollow fiber module with collagen gel: An evaluation in the swine acute liver failure model
    • DOI 10.1046/j.1525-1594.1999.06323.x
    • S. Naka, K. Takeshita, T. Yamamoto, T. Tani, and M. Kodama Bioartificial liver support system using porcine hepatocytes entrapped in a three-dimensional hollow fiber module with collagen gel: an evaluation in the swine acute liver failure model Artif. Organs 23 1999 822 828 (Pubitemid 29449114)
    • (1999) Artificial Organs , vol.23 , Issue.9 , pp. 822-828
    • Naka, S.1    Takeshita, K.2    Yamamoto, T.3    Tani, T.4    Kodama, M.5
  • 64
    • 0028929159 scopus 로고
    • High cell-density culture system of hepatocytes entrapped in a three-dimensional hollow fiber module with collagen gel
    • K. Takeshita, H. Ishibashi, M. Suzuki, T. Yamamoto, T. Akaike, and M. Kodama High cell-density culture system of hepatocytes entrapped in a three-dimensional hollow fiber module with collagen gel Artif. Organs 19 1995 191 193
    • (1995) Artif. Organs , vol.19 , pp. 191-193
    • Takeshita, K.1    Ishibashi, H.2    Suzuki, M.3    Yamamoto, T.4    Akaike, T.5    Kodama, M.6
  • 65
    • 0027146385 scopus 로고
    • Mass transfer in a hollow fiber device used as a bioartificial liver
    • DOI 10.1097/00002480-199310000-00012
    • T.D. Giorgio, A.D. Moscioni, J. Rozga, and A.A. Demetriou Mass transfer in a hollow fiber device used as a bioartificial liver ASAIO J. 39 1993 886 892 (Pubitemid 24005178)
    • (1993) ASAIO Journal , vol.39 , Issue.4 , pp. 886-892
    • Giorgio, T.D.1    Moscioni, A.D.2    Rozga, J.3    Demetriou, A.A.4
  • 68
    • 33644653456 scopus 로고    scopus 로고
    • Culture of skin cells in 3D rather than 2D improves their ability to survive exposure to cytotoxic agents
    • DOI 10.1016/j.jbiotec.2005.12.021, PII S0168165605007960
    • T. Sun, S. Jackson, J.W. Haycock, and S. MacNeil Culture of skin cells in 3D rather than 2D improves their ability to survive exposure to cytotoxic agents J. Biotechnol. 122 2006 372 381 (Pubitemid 43327415)
    • (2006) Journal of Biotechnology , vol.122 , Issue.3 , pp. 372-381
    • Sun, T.1    Jackson, S.2    Haycock, J.W.3    MacNeil, S.4
  • 69
    • 0032191388 scopus 로고    scopus 로고
    • Recent advances in producing and selecting functional proteins by using cell-free translation
    • DOI 10.1016/S0958-1669(98)80042-6
    • L. Jermutus, L.A. Ryabova, and A. Pluckthun Recent advances in producing and selecting functional proteins by using cell-free translation Curr. Opin. Biotechnol. 9 1998 534 548 (Pubitemid 28478978)
    • (1998) Current Opinion in Biotechnology , vol.9 , Issue.5 , pp. 534-548
    • Jermutus, L.1    Ryabova, L.A.2    Pluckthun, A.3
  • 70
    • 0034795182 scopus 로고    scopus 로고
    • CB.Hep-1 hybridoma growth and antibody production using protein-free medium in a hollow fiber bioreactor
    • DOI 10.1023/A:1017921702775
    • R. Valdes, N. Ibarra, M. Gonzalez, T. Alvarez, J. Garcia, R. Llambias, C.A. Perez, O. Quintero, and R. Fischer CB. Hep-1 hybridoma growth and antibody production using protein-free medium in a hollow fiber bioreactor Cytotechnology 35 2001 145 154 (Pubitemid 32943805)
    • (2001) Cytotechnology , vol.35 , Issue.2 , pp. 145-154
    • Valdes, R.1    Ibarra, N.2    Gonzalez, M.3    Alvarez, T.4    Garcia, J.5    Llambias, R.6    Perez, C.A.7    Quintero, O.8    Fischer, R.9
  • 72
    • 0024559010 scopus 로고
    • Optimisation of hybridoma cell growth and monoclonal antibody secretion in a chemically defined, serum- and protein-free culture medium
    • Y.J. Schneider Optimisation of hybridoma cell growth and monoclonal antibody secretion in a chemically defined, serum- and protein-free culture medium J. Immunol. Methods 116 1989 65 77
    • (1989) J. Immunol. Methods , vol.116 , pp. 65-77
    • Schneider, Y.J.1
  • 73
    • 0036597849 scopus 로고    scopus 로고
    • Characterization of a new in vivo hollow fiber model for the study of progression of prostate cancer to androgen independence
    • M.D. Sadar, V.A. Akopian, and E. Beraldi Characterization of a new in vivo hollow fiber model for the study of progression of prostate cancer to androgen independence Mol. Cancer Ther. 1 2002 629 637
    • (2002) Mol. Cancer Ther. , vol.1 , pp. 629-637
    • Sadar, M.D.1    Akopian, V.A.2    Beraldi, E.3
  • 74
    • 3042521098 scopus 로고    scopus 로고
    • Improved prediction of signal peptides: SignalP 3.0
    • DOI 10.1016/j.jmb.2004.05.028, PII S0022283604005972
    • J.D. Bendtsen, H. Nielsen, G. von Heijne, and S. Brunak Improved prediction of signal peptides: SignalP 3.0 J. Mol. Biol. 340 2004 783 795 (Pubitemid 38829638)
    • (2004) Journal of Molecular Biology , vol.340 , Issue.4 , pp. 783-795
    • Bendtsen, J.D.1    Nielsen, H.2    Von Heijne, G.3    Brunak, S.4
  • 75
    • 0031603460 scopus 로고    scopus 로고
    • Prediction of signal peptides and signal anchors by a hidden Markov model
    • H. Nielsen, and A. Krogh Prediction of signal peptides and signal anchors by a hidden Markov model Proc. Int. Conf. Intell. Syst. Mol. Biol. 6 1998 122 130
    • (1998) Proc. Int. Conf. Intell. Syst. Mol. Biol. , vol.6 , pp. 122-130
    • Nielsen, H.1    Krogh, A.2
  • 76
    • 80053345905 scopus 로고    scopus 로고
    • SignalP 4.0: Discriminating signal peptides from transmembrane regions
    • T.N. Petersen, S. Brunak, G. von Heijne, and H. Nielsen SignalP 4.0: discriminating signal peptides from transmembrane regions Nat. Methods 8 2011 785 786
    • (2011) Nat. Methods , vol.8 , pp. 785-786
    • Petersen, T.N.1    Brunak, S.2    Von Heijne, G.3    Nielsen, H.4
  • 79
    • 0034899781 scopus 로고    scopus 로고
    • Evaluation of methods for the prediction of membrane spanning regions
    • S. Moller, M.D. Croning, and R. Apweiler Evaluation of methods for the prediction of membrane spanning regions Bioinformatics 17 2001 646 653 (Pubitemid 32707587)
    • (2001) Bioinformatics , vol.17 , Issue.7 , pp. 646-653
    • Moller, S.1    Croning, M.D.R.2    Apweiler, R.3


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.