메뉴 건너뛰기




Volumn 9, Issue 1-2, 2015, Pages 33-47

Coupling enrichment methods with proteomics for understanding and treating disease

Author keywords

Biomarker discovery; Drug target discovery; Exosomes; MAb discovery; Membrane proteomics

Indexed keywords

CATION; CELL MEMBRANE PROTEIN; GLYCOPROTEOME; MONOCLONAL ANTIBODY; NANOPARTICLE; PROTEOME; UNCLASSIFIED DRUG; PROTEIN;

EID: 84922801793     PISSN: 18628346     EISSN: 18628354     Source Type: Journal    
DOI: 10.1002/prca.201400097     Document Type: Review
Times cited : (21)

References (169)
  • 1
    • 79960179572 scopus 로고    scopus 로고
    • The human proteome project: current state and future direction
    • M111 009993
    • Legrain, P., Aebersold, R., Archakov, A., Bairoch, A. et al., The human proteome project: current state and future direction. Mol. Cell. Proteomics 2011, 10, M111 009993.
    • (2011) Mol. Cell. Proteomics , vol.10
    • Legrain, P.1    Aebersold, R.2    Archakov, A.3    Bairoch, A.4
  • 2
    • 84901280454 scopus 로고    scopus 로고
    • Mass spectrometry-based membrane proteomics in cancer biomarker discovery
    • Mermelekas, G., Zoidakis, J., Mass spectrometry-based membrane proteomics in cancer biomarker discovery. Expert. Rev. Mol. Diagn. 2014, 14, 549-563.
    • (2014) Expert. Rev. Mol. Diagn. , vol.14 , pp. 549-563
    • Mermelekas, G.1    Zoidakis, J.2
  • 3
    • 84918582701 scopus 로고    scopus 로고
    • Mass spectrometry-based proteomics: from cancer biology to protein biomarkers, drug targets, and clinical applications
    • Jimenez, C. R., Verheul, H. M., Mass spectrometry-based proteomics: from cancer biology to protein biomarkers, drug targets, and clinical applications. Am. Soc. Clin. Oncol. Educ. Book 2014, 34, e504-e510.
    • (2014) Am. Soc. Clin. Oncol. Educ. Book , vol.34 , pp. e504-e510
    • Jimenez, C.R.1    Verheul, H.M.2
  • 5
    • 84877254190 scopus 로고    scopus 로고
    • Integrated genomic characterization of endometrial carcinoma
    • Kandoth, C., Schultz, N., Cherniack, A. D., Akbani, R. et al., Integrated genomic characterization of endometrial carcinoma. Nature 2013, 497, 67-73.
    • (2013) Nature , vol.497 , pp. 67-73
    • Kandoth, C.1    Schultz, N.2    Cherniack, A.D.3    Akbani, R.4
  • 6
    • 79954617730 scopus 로고    scopus 로고
    • The cardiokine story unfolds: ischemic stress-induced protein secretion in the heart
    • Doroudgar, S., Glembotski, C. C., The cardiokine story unfolds: ischemic stress-induced protein secretion in the heart. Trends Mol. Med. 2011, 17, 207-214.
    • (2011) Trends Mol. Med. , vol.17 , pp. 207-214
    • Doroudgar, S.1    Glembotski, C.C.2
  • 7
    • 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, J. E., Gromov, P., Cabezon, T., Moreira, J. M. 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, 327-344.
    • (2004) Mol. Cell Proteomics , vol.3 , pp. 327-344
    • Celis, J.E.1    Gromov, P.2    Cabezon, T.3    Moreira, J.M.4
  • 8
    • 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., Cabezon, T. 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, 65-89.
    • (2010) Mol. Oncol. , vol.4 , pp. 65-89
    • Gromov, P.1    Gromova, I.2    Bunkenborg, J.3    Cabezon, T.4
  • 9
    • 79551475841 scopus 로고    scopus 로고
    • Advances in membranous vesicle and exosome proteomics improving biological understanding and biomarker discovery
    • Raimondo, F., Morosi, L., Chinello, C., Magni, F. et al., Advances in membranous vesicle and exosome proteomics improving biological understanding and biomarker discovery. Proteomics 2011, 11, 709-720.
    • (2011) Proteomics , vol.11 , pp. 709-720
    • Raimondo, F.1    Morosi, L.2    Chinello, C.3    Magni, F.4
  • 10
    • 79551493048 scopus 로고    scopus 로고
    • Conditioned media from cell lines: a complementary model to clinical specimens for the discovery of disease-specific biomarkers
    • Dowling, P., Clynes, M., Conditioned media from cell lines: a complementary model to clinical specimens for the discovery of disease-specific biomarkers. Proteomics 2011, 11, 794-804.
    • (2011) Proteomics , vol.11 , pp. 794-804
    • Dowling, P.1    Clynes, M.2
  • 12
    • 84861871435 scopus 로고    scopus 로고
    • Glycoproteomics-based identification of cancer biomarkers
    • Kim, E. H., Misek, D. E., Glycoproteomics-based identification of cancer biomarkers. Int. J. Proteomics 2011, 2011, 601937.
    • (2011) Int. J. Proteomics , vol.2011 , pp. 601937
    • Kim, E.H.1    Misek, D.E.2
  • 13
    • 0034614637 scopus 로고    scopus 로고
    • The hallmarks of cancer
    • Hanahan, D., Weinberg, R. A., The hallmarks of cancer. Cell 2000, 100, 57-70.
    • (2000) Cell , vol.100 , pp. 57-70
    • Hanahan, D.1    Weinberg, R.A.2
  • 15
    • 70350013557 scopus 로고    scopus 로고
    • Mislocalized activation of oncogenic RTKs switches downstream signaling outcomes
    • Choudhary, C., Olsen, J. V., Brandts, C., Cox, J. et al., Mislocalized activation of oncogenic RTKs switches downstream signaling outcomes. Mol. Cell 2009, 36, 326-339.
    • (2009) Mol. Cell , vol.36 , pp. 326-339
    • Choudhary, C.1    Olsen, J.V.2    Brandts, C.3    Cox, J.4
  • 16
    • 26844486610 scopus 로고    scopus 로고
    • Phosphoproteome analysis of HeLa cells using stable isotope labeling with amino acids in cell culture (SILAC)
    • Amanchy, R., Kalume, D. E., Iwahori, A., Zhong, J. et al., Phosphoproteome analysis of HeLa cells using stable isotope labeling with amino acids in cell culture (SILAC). J. Proteome Res. 2005, 4, 1661-1671.
    • (2005) J. Proteome Res. , vol.4 , pp. 1661-1671
    • Amanchy, R.1    Kalume, D.E.2    Iwahori, A.3    Zhong, J.4
  • 17
    • 55249083335 scopus 로고    scopus 로고
    • Identification of c-Src tyrosine kinase substrates using mass spectrometry and peptide microarrays
    • Amanchy, R., Zhong, J., Molina, H., Chaerkady, R. et al., Identification of c-Src tyrosine kinase substrates using mass spectrometry and peptide microarrays. J. Proteome Res. 2008, 7, 3900-3910.
    • (2008) J. Proteome Res. , vol.7 , pp. 3900-3910
    • Amanchy, R.1    Zhong, J.2    Molina, H.3    Chaerkady, R.4
  • 18
    • 67650901206 scopus 로고    scopus 로고
    • Quantitative cell signalling analysis reveals down-regulation of MAPK pathway activation in colorectal cancer
    • Gulmann, C., Sheehan, K. M., Conroy, R. M., Wulfkuhle, J. D. et al., Quantitative cell signalling analysis reveals down-regulation of MAPK pathway activation in colorectal cancer. J. Pathol. 2009, 218, 514-519.
    • (2009) J. Pathol. , vol.218 , pp. 514-519
    • Gulmann, C.1    Sheehan, K.M.2    Conroy, R.M.3    Wulfkuhle, J.D.4
  • 19
    • 54749135378 scopus 로고    scopus 로고
    • LKB1 is necessary for Akt-mediated phosphorylation of proapoptotic proteins
    • Zhong, D., Liu, X., Khuri, F. R., Sun, S. Y. et al., LKB1 is necessary for Akt-mediated phosphorylation of proapoptotic proteins. Cancer. Res. 2008, 68, 7270-7277.
    • (2008) Cancer. Res. , vol.68 , pp. 7270-7277
    • Zhong, D.1    Liu, X.2    Khuri, F.R.3    Sun, S.Y.4
  • 20
    • 33746051332 scopus 로고    scopus 로고
    • Enrichment of integral membrane proteins from small amounts of brain tissue
    • Schindler, J., Jung, S., Niedner-Schatteburg, G., Friauf, E. et al., Enrichment of integral membrane proteins from small amounts of brain tissue. J. Neural. Transm. 2006, 113, 995-1013.
    • (2006) J. Neural. Transm. , vol.113 , pp. 995-1013
    • Schindler, J.1    Jung, S.2    Niedner-Schatteburg, G.3    Friauf, E.4
  • 21
    • 72449200207 scopus 로고    scopus 로고
    • Membrane proteomics for leukemia classification and drug target identification
    • Kohnke, P. L., Mulligan, S. P., Christopherson, R. I., Membrane proteomics for leukemia classification and drug target identification. Curr. Opin. Mol. Ther. 2009, 11, 603-610.
    • (2009) Curr. Opin. Mol. Ther. , vol.11 , pp. 603-610
    • Kohnke, P.L.1    Mulligan, S.P.2    Christopherson, R.I.3
  • 22
    • 0345873477 scopus 로고    scopus 로고
    • An optimized method for the isolation and identification of membrane proteins
    • Lehner, I., Niehof, M., Borlak, J., An optimized method for the isolation and identification of membrane proteins. Electrophoresis 2003, 24, 1795-1808.
    • (2003) Electrophoresis , vol.24 , pp. 1795-1808
    • Lehner, I.1    Niehof, M.2    Borlak, J.3
  • 23
    • 84860344567 scopus 로고    scopus 로고
    • Analysis of a membrane-enriched proteome from postmortem human brain tissue in Alzheimer's disease
    • Donovan, L. E., Higginbotham, L., Dammer, E. B., Gearing, M. et al., Analysis of a membrane-enriched proteome from postmortem human brain tissue in Alzheimer's disease. Proteomics Clin. Appl. 2012, 6, 201-211.
    • (2012) Proteomics Clin. Appl. , vol.6 , pp. 201-211
    • Donovan, L.E.1    Higginbotham, L.2    Dammer, E.B.3    Gearing, M.4
  • 24
    • 84858049725 scopus 로고    scopus 로고
    • Protein profiling of microdomains purified from renal cell carcinoma and normal kidney tissue samples
    • Raimondo, F., Morosi, L., Chinello, C., Perego, R. et al., Protein profiling of microdomains purified from renal cell carcinoma and normal kidney tissue samples. Mol. Biosyst. 2012, 8, 1007-1016.
    • (2012) Mol. Biosyst. , vol.8 , pp. 1007-1016
    • Raimondo, F.1    Morosi, L.2    Chinello, C.3    Perego, R.4
  • 25
    • 77953762037 scopus 로고    scopus 로고
    • Proteome analysis of a plasma membrane-enriched fraction at the placental feto-maternal barrier
    • Zhang, Q., Schulenborg, T., Tan, T., Lang, B. et al. Proteome analysis of a plasma membrane-enriched fraction at the placental feto-maternal barrier. Proteomics Clin. Appl. 2010, 4, 538-549.
    • (2010) Proteomics Clin. Appl. , vol.4 , pp. 538-549
    • Zhang, Q.1    Schulenborg, T.2    Tan, T.3    Lang, B.4
  • 26
    • 84865808745 scopus 로고    scopus 로고
    • Cell surface protein biotinylation for SDS-PAGE analysis
    • Elia, G., Cell surface protein biotinylation for SDS-PAGE analysis. Methods Mol. Biol. 2012, 869, 361-372.
    • (2012) Methods Mol. Biol. , vol.869 , pp. 361-372
    • Elia, G.1
  • 27
    • 84869503250 scopus 로고    scopus 로고
    • Plasma membrane proteomics identifies bone marrow stromal antigen 2 as a potential therapeutic target in endometrial cancer
    • Yokoyama, T., Enomoto, T., Serada, S., Morimoto, A. et al., Plasma membrane proteomics identifies bone marrow stromal antigen 2 as a potential therapeutic target in endometrial cancer. Int. J. Cancer 2013, 132, 472-484.
    • (2013) Int. J. Cancer , vol.132 , pp. 472-484
    • Yokoyama, T.1    Enomoto, T.2    Serada, S.3    Morimoto, A.4
  • 28
    • 61349113308 scopus 로고    scopus 로고
    • Purification of low-abundance Arabidopsis plasma-membrane protein complexes and identification of candidate components
    • Qi, Y., Katagiri, F., Purification of low-abundance Arabidopsis plasma-membrane protein complexes and identification of candidate components. Plant J. 2009, 57, 932-944.
    • (2009) Plant J. , vol.57 , pp. 932-944
    • Qi, Y.1    Katagiri, F.2
  • 29
    • 84906051047 scopus 로고    scopus 로고
    • Cardiac extracellular proteome profiling and membrane topology analysis using glycoproteomics
    • Tian, Y., Koganti, T., Yao, Z., Cannon, P. et al., Cardiac extracellular proteome profiling and membrane topology analysis using glycoproteomics. Prot. Clin. Appl. 2014, 8, 595-602.
    • (2014) Prot. Clin. Appl , vol.8 , pp. 595-602
    • Tian, Y.1    Koganti, T.2    Yao, Z.3    Cannon, P.4
  • 30
    • 84903692527 scopus 로고    scopus 로고
    • Glycoproteomic analysis of prostate cancer tissues by SWATH mass spectrometry discovers N-acylethanolamine acid amidase and protein tyrosine kinase 7 as signatures for tumor aggressiveness
    • Liu, Y., Chen, J., Sethi, A., Li, Q. K. et al., Glycoproteomic analysis of prostate cancer tissues by SWATH mass spectrometry discovers N-acylethanolamine acid amidase and protein tyrosine kinase 7 as signatures for tumor aggressiveness. Mol. Cell Proteomics 2014, 13, 1753-1768.
    • (2014) Mol. Cell Proteomics , vol.13 , pp. 1753-1768
    • Liu, Y.1    Chen, J.2    Sethi, A.3    Li, Q.K.4
  • 32
    • 84903779338 scopus 로고    scopus 로고
    • Glycoproteomic analysis identifies human glycoproteins secreted from HIV latently infected T cells and reveals their presence in HIV+ plasma
    • Yang, W., Zhou, J. Y., Chen, L., Ao, M. et al. Glycoproteomic analysis identifies human glycoproteins secreted from HIV latently infected T cells and reveals their presence in HIV+ plasma. Clin. Proteomics 2014, 11, 9.
    • (2014) Clin. Proteomics , vol.11 , pp. 9
    • Yang, W.1    Zhou, J.Y.2    Chen, L.3    Ao, M.4
  • 33
    • 84881222169 scopus 로고    scopus 로고
    • Identification, prioritization, and evaluation of glycoproteins for aggressive prostate cancer using quantitative glycoproteomics and antibody-based assays on tissue specimens
    • Chen, J., Xi, J., Tian, Y., Bova, G. S., et al., Identification, prioritization, and evaluation of glycoproteins for aggressive prostate cancer using quantitative glycoproteomics and antibody-based assays on tissue specimens. Proteomics 2013, 13, 2268-2277.
    • (2013) Proteomics , vol.13 , pp. 2268-2277
    • Chen, J.1    Xi, J.2    Tian, Y.3    Bova, G.S.4
  • 34
    • 84873948403 scopus 로고    scopus 로고
    • Characterization of disease-associated N-linked glycoproteins
    • Tian, Y., Zhang, H., Characterization of disease-associated N-linked glycoproteins. Proteomics 2013, 13, 504-511.
    • (2013) Proteomics , vol.13 , pp. 504-511
    • Tian, Y.1    Zhang, H.2
  • 35
    • 84863206749 scopus 로고    scopus 로고
    • Application of glycoproteomics for the discovery of biomarkers in lung cancer
    • Li, Q. K., Gabrielson, E., Zhang, H., Application of glycoproteomics for the discovery of biomarkers in lung cancer. Proteomics Clin. Appl. 2012, 6, 244-256.
    • (2012) Proteomics Clin. Appl. , vol.6 , pp. 244-256
    • Li, Q.K.1    Gabrielson, E.2    Zhang, H.3
  • 36
    • 84863806531 scopus 로고    scopus 로고
    • Metabolic flux increases glycoprotein sialylation: implications for cell adhesion and cancer metastasis
    • M112 017558
    • Almaraz, R. T., Tian, Y., Bhattarcharya, R., Tan, E. et al., Metabolic flux increases glycoprotein sialylation: implications for cell adhesion and cancer metastasis. Mol. Cell Proteomics 2012, 11, M112 017558.
    • (2012) Mol. Cell Proteomics , vol.11
    • Almaraz, R.T.1    Tian, Y.2    Bhattarcharya, R.3    Tan, E.4
  • 37
    • 84876337044 scopus 로고    scopus 로고
    • Quantitative measurements of N-linked glycoproteins in human plasma by SWATH-MS
    • Liu, Y., Huttenhain, R., Surinova, S., Gillet, L. C. et al., Quantitative measurements of N-linked glycoproteins in human plasma by SWATH-MS. Proteomics 2013, 13, 1247-1256.
    • (2013) Proteomics , vol.13 , pp. 1247-1256
    • Liu, Y.1    Huttenhain, R.2    Surinova, S.3    Gillet, L.C.4
  • 38
    • 84875969679 scopus 로고    scopus 로고
    • N-glycoprotein SRMAtlas: a resource of mass spectrometric assays for N-glycosites enabling consistent and multiplexed protein quantification for clinical applications
    • Huttenhain, R., Surinova, S., Ossola, R., Sun, Z. et al., N-glycoprotein SRMAtlas: a resource of mass spectrometric assays for N-glycosites enabling consistent and multiplexed protein quantification for clinical applications. Mol. Cell Proteomics 2013, 12, 1005-1016.
    • (2013) Mol. Cell Proteomics , vol.12 , pp. 1005-1016
    • Huttenhain, R.1    Surinova, S.2    Ossola, R.3    Sun, Z.4
  • 39
    • 84901061074 scopus 로고    scopus 로고
    • Identification of a seven glycopeptide signature for malignant pleural mesothelioma in human serum by selected reaction monitoring
    • Cerciello, F., Choi, M., Nicastri, A., Bausch-Fluck, D. et al., Identification of a seven glycopeptide signature for malignant pleural mesothelioma in human serum by selected reaction monitoring. Clin. Proteomics 2013, 10, 16.
    • (2013) Clin. Proteomics , vol.10 , pp. 16
    • Cerciello, F.1    Choi, M.2    Nicastri, A.3    Bausch-Fluck, D.4
  • 40
    • 84923081608 scopus 로고    scopus 로고
    • Quantitative mass spectrometric analysis of glycoproteins combined with enrichment methods
    • Ahn, Y. H., Kim, J. Y., Yoo, J. S. Quantitative mass spectrometric analysis of glycoproteins combined with enrichment methods. Mass Spectrom. Rev. 2014, doi: 10.1002/mas.21428
    • (2014) Mass Spectrom. Rev
    • Ahn, Y.H.1    Kim, J.Y.2    Yoo, J.S.3
  • 41
    • 84893456266 scopus 로고    scopus 로고
    • Identification of salivary N-glycoproteins and measurement of glycosylation site occupancy by boronate glycoprotein enrichment and liquid chromatography/electrospray ionization tandem mass spectrometry
    • Xu, Y., Bailey, U. M., Punyadeera, C., Schulz, B. L., Identification of salivary N-glycoproteins and measurement of glycosylation site occupancy by boronate glycoprotein enrichment and liquid chromatography/electrospray ionization tandem mass spectrometry. Rapid Commun. Mass Spectrom. 2014, 28, 471-482.
    • (2014) Rapid Commun. Mass Spectrom. , vol.28 , pp. 471-482
    • Xu, Y.1    Bailey, U.M.2    Punyadeera, C.3    Schulz, B.L.4
  • 42
    • 64349089985 scopus 로고    scopus 로고
    • Mass-spectrometric identification and relative quantification of N-linked cell surface glycoproteins
    • Wollscheid, B., Bausch-Fluck, D., Henderson, C., O'Brien, R. et al., Mass-spectrometric identification and relative quantification of N-linked cell surface glycoproteins. Nat. Biotechnol. 2009, 27, 378-386.
    • (2009) Nat. Biotechnol. , vol.27 , pp. 378-386
    • Wollscheid, B.1    Bausch-Fluck, D.2    Henderson, C.3    O'Brien, R.4
  • 43
    • 79958187903 scopus 로고    scopus 로고
    • GlycoFly: a database of drosophila N-linked glycoproteins identified using SPEG-MS techniques
    • Baycin-Hizal, D., Tian, Y., Akan, I., Jacobson, E. et al., GlycoFly: a database of drosophila N-linked glycoproteins identified using SPEG-MS techniques. J. Proteome Res. 2011, 10, 2777-2784.
    • (2011) J. Proteome Res. , vol.10 , pp. 2777-2784
    • Baycin-Hizal, D.1    Tian, Y.2    Akan, I.3    Jacobson, E.4
  • 44
    • 34250014373 scopus 로고    scopus 로고
    • Solid-phase extraction of N-linked glycopeptides
    • Tian, Y., Zhou, Y., Elliott, S., Aebersold, R. et al., Solid-phase extraction of N-linked glycopeptides. Nat. Protoc. 2007, 2, 334-339.
    • (2007) Nat. Protoc , vol.2 , pp. 334-339
    • Tian, Y.1    Zhou, Y.2    Elliott, S.3    Aebersold, R.4
  • 45
    • 84900385507 scopus 로고    scopus 로고
    • Glycopeptide capture for cell surface proteomics
    • Lee, M. C., Sun, B., Glycopeptide capture for cell surface proteomics. J. Vis. Exp. 2014, 87, e51349.
    • (2014) J. Vis. Exp. , vol.87 , pp. e51349
    • Lee, M.C.1    Sun, B.2
  • 46
    • 84870241467 scopus 로고    scopus 로고
    • A new method for quantitative analysis of cell surface glycoproteome
    • Sun, Z., Chen, R., Cheng, K., Liu, H. et al., A new method for quantitative analysis of cell surface glycoproteome. Proteomics 2012, 12, 3328-3337.
    • (2012) Proteomics , vol.12 , pp. 3328-3337
    • Sun, Z.1    Chen, R.2    Cheng, K.3    Liu, H.4
  • 47
    • 84893178816 scopus 로고    scopus 로고
    • Characterization of the membrane proteome and N-glycoproteome in BV-2 mouse microglia by liquid chromatography-tandem mass spectrometry
    • Han, D., Moon, S., Kim, Y., Min, H. et al., Characterization of the membrane proteome and N-glycoproteome in BV-2 mouse microglia by liquid chromatography-tandem mass spectrometry. BMC Genomics 2014, 15, 95.
    • (2014) BMC Genomics , vol.15 , pp. 95
    • Han, D.1    Moon, S.2    Kim, Y.3    Min, H.4
  • 48
    • 0038699625 scopus 로고    scopus 로고
    • Identification and quantification of N-linked glycoproteins using hydrazide chemistry, stable isotope labeling and mass spectrometry
    • Zhang, H., Li, X. J., Martin, D. B., Aebersold, R., Identification and quantification of N-linked glycoproteins using hydrazide chemistry, stable isotope labeling and mass spectrometry. Nat. Biotechnol. 2003, 21, 660-666.
    • (2003) Nat. Biotechnol. , vol.21 , pp. 660-666
    • Zhang, H.1    Li, X.J.2    Martin, D.B.3    Aebersold, R.4
  • 49
    • 84871954135 scopus 로고    scopus 로고
    • Glycoproteomics enabled by tagging sialic acid- or galactose-terminated glycans
    • Ramya, T. N., Weerapana, E., Cravatt, B. F., Paulson, J. C. Glycoproteomics enabled by tagging sialic acid- or galactose-terminated glycans. Glycobiology 2013, 23, 211-221.
    • (2013) Glycobiology , vol.23 , pp. 211-221
    • Ramya, T.N.1    Weerapana, E.2    Cravatt, B.F.3    Paulson, J.C.4
  • 50
    • 84874601536 scopus 로고    scopus 로고
    • Enrichment of plasma membrane proteins using nanoparticle pellicles: comparison between silica and higher density nanoparticles
    • Choksawangkarn, W., Kim, S. K., Cannon, J. R., Edwards, N. J. et al., Enrichment of plasma membrane proteins using nanoparticle pellicles: comparison between silica and higher density nanoparticles. J. Proteome Res. 2013, 12, 1134-1141.
    • (2013) J. Proteome Res. , vol.12 , pp. 1134-1141
    • Choksawangkarn, W.1    Kim, S.K.2    Cannon, J.R.3    Edwards, N.J.4
  • 51
    • 79960952981 scopus 로고    scopus 로고
    • Use of colloidal silica-beads for the isolation of cell-surface proteins for mass spectrometry-based proteomics
    • Kim, Y., Elschenbroich, S., Sharma, P., Sepiashvili, L. et al., Use of colloidal silica-beads for the isolation of cell-surface proteins for mass spectrometry-based proteomics. Methods Mol. Biol. 2011, 748, 227-241.
    • (2011) Methods Mol. Biol. , vol.748 , pp. 227-241
    • Kim, Y.1    Elschenbroich, S.2    Sharma, P.3    Sepiashvili, L.4
  • 52
    • 84856972243 scopus 로고    scopus 로고
    • A placental sub-proteome: the apical plasma membrane of the syncytiotrophoblast
    • Vandre, D. D., Ackerman, W. E. t., Tewari, A., Kniss, D. A. et al., A placental sub-proteome: the apical plasma membrane of the syncytiotrophoblast. Placenta 2012, 33, 207-213.
    • (2012) Placenta , vol.33 , pp. 207-213
    • Vandre, D.D.1    Ackerman, W.E.t.2    Tewari, A.3    Kniss, D.A.4
  • 53
    • 56449086663 scopus 로고    scopus 로고
    • Evaluation of two cell surface modification methods for proteomic analysis of plasma membrane from isolated mouse hepatocytes
    • Li, X., Jin, Q., Cao, J., Xie, C. et al., Evaluation of two cell surface modification methods for proteomic analysis of plasma membrane from isolated mouse hepatocytes. Biochim. Biophys. Acta 2009, 1794, 32-41.
    • (2009) Biochim. Biophys. Acta , vol.1794 , pp. 32-41
    • Li, X.1    Jin, Q.2    Cao, J.3    Xie, C.4
  • 54
    • 60849103514 scopus 로고    scopus 로고
    • An in vivo membrane density perturbation strategy for identification of liver sinusoidal surface proteome accessible from the vasculature
    • Li, X., Xie, C., Cao, J., He, Q. et al., An in vivo membrane density perturbation strategy for identification of liver sinusoidal surface proteome accessible from the vasculature. J. Proteome Res. 2009, 8, 123-132.
    • (2009) J. Proteome Res. , vol.8 , pp. 123-132
    • Li, X.1    Xie, C.2    Cao, J.3    He, Q.4
  • 55
    • 66149125323 scopus 로고    scopus 로고
    • Analysis of cell surface proteome changes via label-free, quantitative mass spectrometry
    • Schiess, R., Mueller, L. N., Schmidt, A., Mueller, M. et al., Analysis of cell surface proteome changes via label-free, quantitative mass spectrometry. Mol. Cell Proteomics 2009, 8, 624-638.
    • (2009) Mol. Cell Proteomics , vol.8 , pp. 624-638
    • Schiess, R.1    Mueller, L.N.2    Schmidt, A.3    Mueller, M.4
  • 56
    • 33846548168 scopus 로고    scopus 로고
    • Mass spectrometric detection of tissue proteins in plasma
    • Zhang, H., Liu, A. Y., Loriaux, P., Wollscheid, B. et al., Mass spectrometric detection of tissue proteins in plasma. Mol. Cell Proteomics 2007, 6, 64-71.
    • (2007) Mol. Cell Proteomics , vol.6 , pp. 64-71
    • Zhang, H.1    Liu, A.Y.2    Loriaux, P.3    Wollscheid, B.4
  • 57
    • 84861860481 scopus 로고    scopus 로고
    • Targeted data extraction of the MS/MS spectra generated by data-independent acquisition: a new concept for consistent and accurate proteome analysis
    • O111 016717
    • Gillet, L. C., Navarro, P., Tate, S., Rost, H. et al., Targeted data extraction of the MS/MS spectra generated by data-independent acquisition: a new concept for consistent and accurate proteome analysis. Mol. Cell Proteomics 2012, 11, O111 016717.
    • (2012) Mol. Cell Proteomics , vol.11
    • Gillet, L.C.1    Navarro, P.2    Tate, S.3    Rost, H.4
  • 58
    • 84887359663 scopus 로고    scopus 로고
    • Mass spectrometric protein maps for biomarker discovery and clinical research
    • Liu, Y., Huttenhain, R., Collins, B., Aebersold, R., Mass spectrometric protein maps for biomarker discovery and clinical research. Expert. Rev. Mol. Diagn 2013, 13, 811-825.
    • (2013) Expert. Rev. Mol. Diagn , vol.13 , pp. 811-825
    • Liu, Y.1    Huttenhain, R.2    Collins, B.3    Aebersold, R.4
  • 59
    • 20144383119 scopus 로고    scopus 로고
    • High throughput quantitative analysis of serum proteins using glycopeptide capture and liquid chromatography mass spectrometry
    • Zhang, H., Yi, E. C., Li, X. J., Mallick, P. et al., High throughput quantitative analysis of serum proteins using glycopeptide capture and liquid chromatography mass spectrometry. Mol. Cell Proteomics 2005, 4, 144-155.
    • (2005) Mol. Cell Proteomics , vol.4 , pp. 144-155
    • Zhang, H.1    Yi, E.C.2    Li, X.J.3    Mallick, P.4
  • 60
    • 84873368065 scopus 로고    scopus 로고
    • Statistical inference from multiple iTRAQ experiments without using common reference standards
    • Herbrich, S. M., Cole, R. N., West, K. P., Jr., Schulze, K. et al., Statistical inference from multiple iTRAQ experiments without using common reference standards. J. Proteome Res. 2013, 12, 594-604.
    • (2013) J. Proteome Res. , vol.12 , pp. 594-604
    • Herbrich, S.M.1    Cole, R.N.2    West Jr, K.P.3    Schulze, K.4
  • 61
    • 84887076843 scopus 로고    scopus 로고
    • Plasma membrane proteomics of tumor spheres identify CD166 as a novel marker for cancer stem-like cells in head and neck squamous cell carcinoma
    • Yan, M., Yang, X., Wang, L., Clark, D. et al., Plasma membrane proteomics of tumor spheres identify CD166 as a novel marker for cancer stem-like cells in head and neck squamous cell carcinoma. Mol. Cell Proteomics 2013, 12, 3271-3284.
    • (2013) Mol. Cell Proteomics , vol.12 , pp. 3271-3284
    • Yan, M.1    Yang, X.2    Wang, L.3    Clark, D.4
  • 62
    • 0037685263 scopus 로고    scopus 로고
    • Lectin affinity capture, isotope-coded tagging and mass spectrometry to identify N-linked glycoproteins
    • Kaji, H., Saito, H., Yamauchi, Y., Shinkawa, T. et al., Lectin affinity capture, isotope-coded tagging and mass spectrometry to identify N-linked glycoproteins. Nat. Biotechnol. 2003, 21, 667-672.
    • (2003) Nat. Biotechnol. , vol.21 , pp. 667-672
    • Kaji, H.1    Saito, H.2    Yamauchi, Y.3    Shinkawa, T.4
  • 63
    • 0347134596 scopus 로고    scopus 로고
    • Affinity enrichment of plasma membrane for proteomics analysis
    • Zhang, W., Zhou, G., Zhao, Y., White, M. A. et al., Affinity enrichment of plasma membrane for proteomics analysis. Electrophoresis 2003, 24, 2855-2863.
    • (2003) Electrophoresis , vol.24 , pp. 2855-2863
    • Zhang, W.1    Zhou, G.2    Zhao, Y.3    White, M.A.4
  • 64
    • 61849134438 scopus 로고    scopus 로고
    • Reducing agent-mediated precipitation of high-abundance plasma proteins
    • Warder, S.E., Tucker, L. A., Strelitzer, T. J., McKeegan, E. M. et al., Reducing agent-mediated precipitation of high-abundance plasma proteins. Anal. Biochem. 2009, 387, 184-193.
    • (2009) Anal. Biochem. , vol.387 , pp. 184-193
    • Warder, S.E.1    Tucker, L.A.2    Strelitzer, T.J.3    McKeegan, E.M.4
  • 65
    • 84874800120 scopus 로고    scopus 로고
    • A fast and reproducible method for albumin isolation and depletion from serum and cerebrospinal fluid
    • Holewinski, R. J., Jin, Z. C., Powell, M. J., Maust, M. D. et al., A fast and reproducible method for albumin isolation and depletion from serum and cerebrospinal fluid. Proteomics 2013, 13, 743-750.
    • (2013) Proteomics , vol.13 , pp. 743-750
    • Holewinski, R.J.1    Jin, Z.C.2    Powell, M.J.3    Maust, M.D.4
  • 66
    • 84883199030 scopus 로고    scopus 로고
    • Analysis of peptides by denaturing ultrafiltration and LC-MALDI-TOF-MS
    • An, Y., Goldman, R., Analysis of peptides by denaturing ultrafiltration and LC-MALDI-TOF-MS. Methods Mol. Biol. 2013, 1023, 13-19.
    • (2013) Methods Mol. Biol. , vol.1023 , pp. 13-19
    • An, Y.1    Goldman, R.2
  • 67
    • 84870391101 scopus 로고    scopus 로고
    • Discovery of serum proteomic biomarkers for prediction of response to infliximab (a monoclonal anti-TNF antibody) treatment in rheumatoid arthritis: an exploratory analysis
    • Ortea, I., Roschitzki, B., Ovalles, J. G., Longo, J. L. et al., Discovery of serum proteomic biomarkers for prediction of response to infliximab (a monoclonal anti-TNF antibody) treatment in rheumatoid arthritis: an exploratory analysis. J. Proteomics 2012, 77, 372-382.
    • (2012) J. Proteomics , vol.77 , pp. 372-382
    • Ortea, I.1    Roschitzki, B.2    Ovalles, J.G.3    Longo, J.L.4
  • 68
    • 84885734352 scopus 로고    scopus 로고
    • The plasma proteome identifies expected and novel proteins correlated with micronutrient status in undernourished nepalese children
    • Cole, R. N., Ruczinski, I., Schulze, K., Christian, P. et al., The plasma proteome identifies expected and novel proteins correlated with micronutrient status in undernourished nepalese children. J. Nutr. 2013, 143, 1540-1548.
    • (2013) J. Nutr. , vol.143 , pp. 1540-1548
    • Cole, R.N.1    Ruczinski, I.2    Schulze, K.3    Christian, P.4
  • 69
    • 80052021424 scopus 로고    scopus 로고
    • Proteomic analysis of cancer stem cells in human prostate cancer cells
    • Lee, E. K., Cho, H., Kim, C. W., Proteomic analysis of cancer stem cells in human prostate cancer cells. Biochem. Biophys. Res. Commun. 2011, 412, 279-285.
    • (2011) Biochem. Biophys. Res. Commun. , vol.412 , pp. 279-285
    • Lee, E.K.1    Cho, H.2    Kim, C.W.3
  • 70
    • 21144458164 scopus 로고    scopus 로고
    • Immunoaffinity profiling of tyrosine phosphorylation in cancer cells
    • Rush, J., Moritz, A., Lee, K. A., Guo, A. et al., Immunoaffinity profiling of tyrosine phosphorylation in cancer cells. Nat. Biotechnol. 2005, 23, 94-101.
    • (2005) Nat. Biotechnol. , vol.23 , pp. 94-101
    • Rush, J.1    Moritz, A.2    Lee, K.A.3    Guo, A.4
  • 71
    • 53049108920 scopus 로고    scopus 로고
    • Global impact of oncogenic Src on a phosphotyrosine proteome
    • Luo, W., Slebos, R. J., Hill, S., Li, M. et al., Global impact of oncogenic Src on a phosphotyrosine proteome. J. Proteome Res. 2008, 7, 3447-3460.
    • (2008) J. Proteome Res. , vol.7 , pp. 3447-3460
    • Luo, W.1    Slebos, R.J.2    Hill, S.3    Li, M.4
  • 72
    • 77954572010 scopus 로고    scopus 로고
    • Quantitative phosphoproteomic analysis of T cell receptor signaling in diabetes prone and resistant mice
    • Iwai, L. K., Benoist, C., Mathis, D., White, F. M., Quantitative phosphoproteomic analysis of T cell receptor signaling in diabetes prone and resistant mice. J. Proteome Res. 2010, 9, 3135-3145.
    • (2010) J. Proteome Res. , vol.9 , pp. 3135-3145
    • Iwai, L.K.1    Benoist, C.2    Mathis, D.3    White, F.M.4
  • 73
    • 84895546954 scopus 로고    scopus 로고
    • Phosphorylation of mutant huntingtin at serine 116 modulates neuronal toxicity
    • Watkin, E. E., Arbez, N., Waldron-Roby, E., O'Meally, R. et al., Phosphorylation of mutant huntingtin at serine 116 modulates neuronal toxicity. PLoS One 2014, 9, e88284.
    • (2014) PLoS One , vol.9 , pp. e88284
    • Watkin, E.E.1    Arbez, N.2    Waldron-Roby, E.3    O'Meally, R.4
  • 74
    • 84862317369 scopus 로고    scopus 로고
    • TSLP signaling network revealed by SILAC-based phosphoproteomics
    • M112 017764
    • Zhong, J., Kim, M. S., Chaerkady, R., Wu, X. et al., TSLP signaling network revealed by SILAC-based phosphoproteomics. Mol. Cell Proteomics 2012, 11, M112 017764.
    • (2012) Mol. Cell Proteomics , vol.11
    • Zhong, J.1    Kim, M.S.2    Chaerkady, R.3    Wu, X.4
  • 75
    • 74549168922 scopus 로고    scopus 로고
    • Identifying drug effects via pathway alterations using an integer linear programming optimization formulation on phosphoproteomic data
    • Mitsos, A., Melas, I. N., Siminelakis, P., Chairakaki, A. D. et al., Identifying drug effects via pathway alterations using an integer linear programming optimization formulation on phosphoproteomic data. PLoS Comput. Biol. 2009, 5, e1000591.
    • (2009) PLoS Comput. Biol. , vol.5 , pp. e1000591
    • Mitsos, A.1    Melas, I.N.2    Siminelakis, P.3    Chairakaki, A.D.4
  • 76
    • 67849121794 scopus 로고    scopus 로고
    • Phosphoproteomic analysis of human embryonic stem cells
    • Brill, L. M., Xiong, W., Lee, K. B., Ficarro, S. B. et al., Phosphoproteomic analysis of human embryonic stem cells. Cell Stem Cell 2009, 5, 204-213.
    • (2009) Cell Stem Cell , vol.5 , pp. 204-213
    • Brill, L.M.1    Xiong, W.2    Lee, K.B.3    Ficarro, S.B.4
  • 77
    • 29144511607 scopus 로고    scopus 로고
    • MAPK signalling pathways as molecular targets for anti-inflammatory therapy-from molecular mechanisms to therapeutic benefits
    • Kaminska, B., MAPK signalling pathways as molecular targets for anti-inflammatory therapy-from molecular mechanisms to therapeutic benefits. Biochim. Biophys. Acta 2005, 1754, 253-262.
    • (2005) Biochim. Biophys. Acta , vol.1754 , pp. 253-262
    • Kaminska, B.1
  • 78
    • 33646165882 scopus 로고    scopus 로고
    • New approaches to the treatment of inflammatory disorders small molecule inhibitors of p38 MAP kinase
    • Peifer, C., Wagner, G., Laufer, S., New approaches to the treatment of inflammatory disorders small molecule inhibitors of p38 MAP kinase. Curr. Top Med. Chem. 2006, 6, 113-149.
    • (2006) Curr. Top Med. Chem. , vol.6 , pp. 113-149
    • Peifer, C.1    Wagner, G.2    Laufer, S.3
  • 79
    • 33845432866 scopus 로고    scopus 로고
    • Regulating insulin signaling and beta-cell function through IRS proteins
    • White, M. F., Regulating insulin signaling and beta-cell function through IRS proteins. Can. J. Physiol. Pharmacol. 2006, 84, 725-737.
    • (2006) Can. J. Physiol. Pharmacol. , vol.84 , pp. 725-737
    • White, M.F.1
  • 80
    • 79960821208 scopus 로고    scopus 로고
    • Discovery of cellular substrates for protein kinase A using a peptide array screening protocol
    • Smith, F. D., Samelson, B. K., Scott, J. D., Discovery of cellular substrates for protein kinase A using a peptide array screening protocol. Biochem. J. 2011, 438, 103-110.
    • (2011) Biochem. J. , vol.438 , pp. 103-110
    • Smith, F.D.1    Samelson, B.K.2    Scott, J.D.3
  • 81
    • 84910660856 scopus 로고    scopus 로고
    • Heterogeneity of pancreatic cancer metastases in a single patient revealed by quantitative proteomics
    • Min-Sik Kim, Y. Z., Shinchi Yachida, N. V., Kumar R., Abel M. L. et al., Heterogeneity of pancreatic cancer metastases in a single patient revealed by quantitative proteomics. Am. Soc. Biochem. Mol. Biol. 2014, 13, 2803-2811.
    • (2014) Am. Soc. Biochem. Mol. Biol. , vol.13 , pp. 2803-2811
    • Min-Sik Kim, Y.Z.1    Shinchi Yachida, N.V.2    Kumar, R.3    Abel, M.L.4
  • 82
    • 79952177511 scopus 로고    scopus 로고
    • Identification of novel phosphorylation motifs through an integrative computational and experimental analysis of the human phosphoproteome
    • Amanchy, R., Kandasamy, K., Mathivanan, S., Periaswamy, B. et al., Identification of novel phosphorylation motifs through an integrative computational and experimental analysis of the human phosphoproteome. J. Proteomics Bioinform. 2011, 4, 22-35.
    • (2011) J. Proteomics Bioinform. , vol.4 , pp. 22-35
    • Amanchy, R.1    Kandasamy, K.2    Mathivanan, S.3    Periaswamy, B.4
  • 83
    • 9144236198 scopus 로고    scopus 로고
    • Human protein reference database as a discovery resource for proteomics
    • Peri, S., Navarro, J. D., Kristiansen, T. Z., Amanchy, R. et al., Human protein reference database as a discovery resource for proteomics. Nucleic Acids Res. 2004, 32, D497-D501.
    • (2004) Nucleic Acids Res. , vol.32 , pp. D497-D501
    • Peri, S.1    Navarro, J.D.2    Kristiansen, T.Z.3    Amanchy, R.4
  • 84
    • 10744224197 scopus 로고    scopus 로고
    • Development of human protein reference database as an initial platform for approaching systems biology in humans
    • Peri, S., Navarro, J. D., Amanchy, R., Kristiansen, T. Z. et al., Development of human protein reference database as an initial platform for approaching systems biology in humans. Genome Res. 2003, 13, 2363-2371.
    • (2003) Genome Res. , vol.13 , pp. 2363-2371
    • Peri, S.1    Navarro, J.D.2    Amanchy, R.3    Kristiansen, T.Z.4
  • 85
    • 38949210266 scopus 로고    scopus 로고
    • Human Proteinpedia enables sharing of human protein data
    • Mathivanan, S., Ahmed, M., Ahn, N. G., Alexandre, H. et al., Human Proteinpedia enables sharing of human protein data. Nat. Biotechnol. 2008, 26, 164-167.
    • (2008) Nat. Biotechnol. , vol.26 , pp. 164-167
    • Mathivanan, S.1    Ahmed, M.2    Ahn, N.G.3    Alexandre, H.4
  • 86
    • 58149202157 scopus 로고    scopus 로고
    • Human Proteinpedia: a unified discovery resource for proteomics research
    • Kandasamy, K., Keerthikumar, S., Goel, R., Mathivanan, S. et al., Human Proteinpedia: a unified discovery resource for proteomics research. Nucleic Acids Res. 2009, 37, D773-D781.
    • (2009) Nucleic Acids Res , vol.37 , pp. D773-D781
    • Kandasamy, K.1    Keerthikumar, S.2    Goel, R.3    Mathivanan, S.4
  • 87
    • 84855658379 scopus 로고    scopus 로고
    • Human Protein Reference Database and Human Proteinpedia as resources for phosphoproteome analysis
    • Goel, R., Harsha, H. C., Pandey, A., Prasad, T. S., Human Protein Reference Database and Human Proteinpedia as resources for phosphoproteome analysis. Mol. Biosyst. 2012, 8, 453-463.
    • (2012) Mol. Biosyst. , vol.8 , pp. 453-463
    • Goel, R.1    Harsha, H.C.2    Pandey, A.3    Prasad, T.S.4
  • 88
    • 0035478709 scopus 로고    scopus 로고
    • Analysis of phosphorylated proteins and peptides by mass spectrometry
    • McLachlin, D. T., Chait, B. T., Analysis of phosphorylated proteins and peptides by mass spectrometry. Curr. Opin. Chem. Biol. 2001, 5, 591-602.
    • (2001) Curr. Opin. Chem. Biol. , vol.5 , pp. 591-602
    • McLachlin, D.T.1    Chait, B.T.2
  • 89
    • 0037435030 scopus 로고    scopus 로고
    • Mass spectrometry-based proteomics
    • Aebersold, R., Mann, M., Mass spectrometry-based proteomics. Nature 2003, 422, 198-207.
    • (2003) Nature , vol.422 , pp. 198-207
    • Aebersold, R.1    Mann, M.2
  • 90
    • 0035987473 scopus 로고    scopus 로고
    • Identification of the phosphotyrosine proteome from thrombin activated platelets
    • Maguire, P. B., Wynne, K. J., Harney, D. F., O'Donoghue, N. M. et al., Identification of the phosphotyrosine proteome from thrombin activated platelets. Proteomics 2002, 2, 642-648.
    • (2002) Proteomics , vol.2 , pp. 642-648
    • Maguire, P.B.1    Wynne, K.J.2    Harney, D.F.3    O'Donoghue, N.M.4
  • 91
    • 21144445429 scopus 로고    scopus 로고
    • Phosphotyrosine proteomic study of interferon alpha signaling pathway using a combination of immunoprecipitation and immobilized metal affinity chromatography
    • Zheng, H., Hu, P., Quinn, D. F., Wang, Y. K., Phosphotyrosine proteomic study of interferon alpha signaling pathway using a combination of immunoprecipitation and immobilized metal affinity chromatography. Mol. Cell Proteomics 2005, 4, 721-730.
    • (2005) Mol. Cell Proteomics , vol.4 , pp. 721-730
    • Zheng, H.1    Hu, P.2    Quinn, D.F.3    Wang, Y.K.4
  • 92
    • 33847782587 scopus 로고    scopus 로고
    • Global proteomic profiling of phosphopeptides using electron transfer dissociation tandem mass spectrometry
    • Molina, H., Horn, D. M., Tang, N., Mathivanan, S. et al., Global proteomic profiling of phosphopeptides using electron transfer dissociation tandem mass spectrometry. Proc. Natl. Acad. Sci. USA 2007, 104, 2199-2204.
    • (2007) Proc. Natl. Acad. Sci. USA , vol.104 , pp. 2199-2204
    • Molina, H.1    Horn, D.M.2    Tang, N.3    Mathivanan, S.4
  • 93
    • 33745585792 scopus 로고    scopus 로고
    • Phosphoproteomic analysis of Her2/neu signaling and inhibition
    • Bose, R., Molina, H., Patterson, A. S., Bitok, J. K. et al., Phosphoproteomic analysis of Her2/neu signaling and inhibition. Proc. Natl. Acad. Sci. USA 2006, 103, 9773-9778.
    • (2006) Proc. Natl. Acad. Sci. USA , vol.103 , pp. 9773-9778
    • Bose, R.1    Molina, H.2    Patterson, A.S.3    Bitok, J.K.4
  • 94
    • 40649095957 scopus 로고    scopus 로고
    • Quantitative proteomics using stable isotope labeling with amino acids in cell culture
    • Harsha, H. C., Molina, H., Pandey, A., Quantitative proteomics using stable isotope labeling with amino acids in cell culture. Nat. Protoc. 2008, 3, 505-516.
    • (2008) Nat. Protoc. , vol.3 , pp. 505-516
    • Harsha, H.C.1    Molina, H.2    Pandey, A.3
  • 95
    • 33750456519 scopus 로고    scopus 로고
    • Global, in vivo, and site-specific phosphorylation dynamics in signaling networks
    • Olsen, J. V., Blagoev, B., Gnad, F., Macek, B. et al., Global, in vivo, and site-specific phosphorylation dynamics in signaling networks. Cell 2006, 127, 635-648.
    • (2006) Cell , vol.127 , pp. 635-648
    • Olsen, J.V.1    Blagoev, B.2    Gnad, F.3    Macek, B.4
  • 96
    • 78649849874 scopus 로고    scopus 로고
    • Feasibility of large-scale phosphoproteomics with higher energy collisional dissociation fragmentation
    • Nagaraj, N., D'Souza, R. C., Cox, J., Olsen, J. V. et al., Feasibility of large-scale phosphoproteomics with higher energy collisional dissociation fragmentation. J. Proteome Res. 2010, 9, 6786-6794.
    • (2010) J. Proteome Res. , vol.9 , pp. 6786-6794
    • Nagaraj, N.1    D'Souza, R.C.2    Cox, J.3    Olsen, J.V.4
  • 97
    • 77949686964 scopus 로고    scopus 로고
    • Phosphoproteome analysis of human liver tissue by long-gradient nanoflow LC coupled with multiple stage MS analysis
    • Han, G., Ye, M., Liu, H., Song, C. et al., Phosphoproteome analysis of human liver tissue by long-gradient nanoflow LC coupled with multiple stage MS analysis. Electrophoresis 2010, 31, 1080-1089.
    • (2010) Electrophoresis , vol.31 , pp. 1080-1089
    • Han, G.1    Ye, M.2    Liu, H.3    Song, C.4
  • 98
    • 61649097515 scopus 로고    scopus 로고
    • Temporal perturbation of tyrosine phosphoproteome dynamics reveals the system-wide regulatory networks
    • Oyama, M., Kozuka-Hata, H., Tasaki, S., Semba, K. et al., Temporal perturbation of tyrosine phosphoproteome dynamics reveals the system-wide regulatory networks. Mol. Cell Proteomics 2009, 8, 226-231.
    • (2009) Mol. Cell Proteomics , vol.8 , pp. 226-231
    • Oyama, M.1    Kozuka-Hata, H.2    Tasaki, S.3    Semba, K.4
  • 99
    • 70450280616 scopus 로고    scopus 로고
    • Identification of tyrosine-phosphorylated proteins associated with metastasis and functional analysis of FER in human hepatocellular carcinoma cells
    • Li, H., Ren, Z., Kang, X., Zhang, L. et al., Identification of tyrosine-phosphorylated proteins associated with metastasis and functional analysis of FER in human hepatocellular carcinoma cells. BMC Cancer 2009, 9, 366.
    • (2009) BMC Cancer , vol.9 , pp. 366
    • Li, H.1    Ren, Z.2    Kang, X.3    Zhang, L.4
  • 100
    • 84878654194 scopus 로고    scopus 로고
    • Extracellular vesicles as prospective carriers of oncogenic protein signatures in adult and paediatric brain tumors
    • Garnier, D. J. N., Rak, J., Extracellular vesicles as prospective carriers of oncogenic protein signatures in adult and paediatric brain tumors. Proteomics 2012, 13, 1595-1607.
    • (2012) Proteomics , vol.13 , pp. 1595-1607
    • Garnier, D.J.N.1    Rak, J.2
  • 101
    • 84876927914 scopus 로고    scopus 로고
    • Exosomes reflect the hypoxic status of glioma cells and mediate hypoxia-dependent activation of vascular cells during tumor development
    • Kucharzewska, P., Christianson, H. C., Welch, J. E., Svensson, K. J. et al., Exosomes reflect the hypoxic status of glioma cells and mediate hypoxia-dependent activation of vascular cells during tumor development. Proc. Natl. Acad. Sci. USA 2013, 110, 7312-7317.
    • (2013) Proc. Natl. Acad. Sci. USA , vol.110 , pp. 7312-7317
    • Kucharzewska, P.1    Christianson, H.C.2    Welch, J.E.3    Svensson, K.J.4
  • 102
    • 80053175966 scopus 로고    scopus 로고
    • Microvesicles secreted by macrophages shuttle invasion-potentiating microRNAs into breast cancer cells
    • Yang, M., Chen, J., Su, F., Yu, B. et al., Microvesicles secreted by macrophages shuttle invasion-potentiating microRNAs into breast cancer cells. Mol. Cancer 2011, 10, 117.
    • (2011) Mol. Cancer , vol.10 , pp. 117
    • Yang, M.1    Chen, J.2    Su, F.3    Yu, B.4
  • 103
    • 84897062699 scopus 로고    scopus 로고
    • Exosomal proteome profiling: a potential multi-marker cellular phenotyping tool to characterize hypoxia-induced radiation resistance in breast cancer
    • Thomas, S. N., Liao, Z., Clark, D., Chen, Y. et al., Exosomal proteome profiling: a potential multi-marker cellular phenotyping tool to characterize hypoxia-induced radiation resistance in breast cancer. Proteomes 2013, 1, 87-108.
    • (2013) Proteomes , vol.1 , pp. 87-108
    • Thomas, S.N.1    Liao, Z.2    Clark, D.3    Chen, Y.4
  • 104
    • 84905004665 scopus 로고    scopus 로고
    • Inferring alterations in cell-to-cell communication in HER2+ breast cancer using secretome profiling of three cell models
    • Klinke, D. J., 2nd, Kulkarni, Y. M., Wu, Y., Byrne-Hoffman, C., Inferring alterations in cell-to-cell communication in HER2+ breast cancer using secretome profiling of three cell models. Biotechnol. Bioeng. 2014, 111, 1853-1863.
    • (2014) Biotechnol. Bioeng. , vol.111 , pp. 1853-1863
    • Klinke 2nd, D.J.1    Kulkarni, Y.M.2    Wu, Y.3    Byrne-Hoffman, C.4
  • 105
    • 84902161469 scopus 로고    scopus 로고
    • The overexpression of a single oncogene (ERBB2/HER2) alters the proteomic landscape of extracellular vesicles
    • Amorim, M., Fernandes, G., Oliveira, P., Martins-de-Souza, D. et al., The overexpression of a single oncogene (ERBB2/HER2) alters the proteomic landscape of extracellular vesicles. Proteomics 2014, 14, 1472-1479.
    • (2014) Proteomics , vol.14 , pp. 1472-1479
    • Amorim, M.1    Fernandes, G.2    Oliveira, P.3    Martins-de-Souza, D.4
  • 106
    • 84902192560 scopus 로고    scopus 로고
    • Proteomic analysis of hypoxia-induced U373MG glioma secretome reveals novel hypoxia-dependent migration factors
    • Yoon, J. H., Kim, J., Kim, K. L., Kim, D. H. et al., Proteomic analysis of hypoxia-induced U373MG glioma secretome reveals novel hypoxia-dependent migration factors. Proteomics 2014, 14, 1494-1502.
    • (2014) Proteomics , vol.14 , pp. 1494-1502
    • Yoon, J.H.1    Kim, J.2    Kim, K.L.3    Kim, D.H.4
  • 107
    • 84896972245 scopus 로고    scopus 로고
    • The proteomics of prostate cancer exosomes
    • Drake, R. R., Kislinger, T., The proteomics of prostate cancer exosomes. Expert. Rev. Proteomics 2014, 11, 167-177.
    • (2014) Expert. Rev. Proteomics , vol.11 , pp. 167-177
    • Drake, R.R.1    Kislinger, T.2
  • 108
    • 84904253489 scopus 로고    scopus 로고
    • Bladder cancer exosomes contain EDIL-3/del1 and facilitate cancer progression
    • Beckham, C. J., Olsen, J., Yin, P. N., Wu, C. H. et al., Bladder cancer exosomes contain EDIL-3/del1 and facilitate cancer progression. J. Urol. 2014, 192, 583-592.
    • (2014) J. Urol , vol.192 , pp. 583-592
    • Beckham, C.J.1    Olsen, J.2    Yin, P.N.3    Wu, C.H.4
  • 109
    • 84898764220 scopus 로고    scopus 로고
    • Proteomics analysis of cancer exosomes using a novel modified aptamer-based array (SOMAscan) platform
    • Webber, J., Stone, T. C., Katilius, E., Smith, B. C., Gordon, B. et al., Proteomics analysis of cancer exosomes using a novel modified aptamer-based array (SOMAscan) platform. Mol. Cell Proteomics 2014, 13, 1050-1064.
    • (2014) Mol. Cell Proteomics , vol.13 , pp. 1050-1064
    • Webber, J.1    Stone, T.C.2    Katilius, E.3    Smith, B.C.4    Gordon, B.5
  • 110
    • 84897370572 scopus 로고    scopus 로고
    • In-depth proteomic analyses of ovarian cancer cell line exosomes reveals differential enrichment of functional categories compared to the NCI 60 proteome
    • Sinha, A., Ignatchenko, V., Ignatchenko, A., Mejia-Guerrero, S. et al., In-depth proteomic analyses of ovarian cancer cell line exosomes reveals differential enrichment of functional categories compared to the NCI 60 proteome. Biochem. Biophys. Res. Commun. 2014, 445, 694-701.
    • (2014) Biochem. Biophys. Res. Commun. , vol.445 , pp. 694-701
    • Sinha, A.1    Ignatchenko, V.2    Ignatchenko, A.3    Mejia-Guerrero, S.4
  • 111
    • 84895744810 scopus 로고    scopus 로고
    • Quantitative proteomics of fractionated membrane and lumen exosome proteins from isogenic metastatic and nonmetastatic bladder cancer cells reveal differential expression of EMT factors
    • Jeppesen, D. K., Nawrocki, A., Jensen, S. G., Thorsen, K. et al., Quantitative proteomics of fractionated membrane and lumen exosome proteins from isogenic metastatic and nonmetastatic bladder cancer cells reveal differential expression of EMT factors. Proteomics 2014, 14, 699-712.
    • (2014) Proteomics , vol.14 , pp. 699-712
    • Jeppesen, D.K.1    Nawrocki, A.2    Jensen, S.G.3    Thorsen, K.4
  • 112
    • 84920770459 scopus 로고    scopus 로고
    • Exosomal ITGA3 interferes with non-cancerous prostate cell functions and is increased in urine exosomes of metastatic prostate cancer patients
    • Bijnsdorp, I. V., Geldof, A. A., Lavaei, M., Piersma, S. R. et al., Exosomal ITGA3 interferes with non-cancerous prostate cell functions and is increased in urine exosomes of metastatic prostate cancer patients. J. Extracell Vesicles 2013, 2, doi: 10.3402/jev.v2i0.22097
    • (2013) J. Extracell Vesicles , vol.2
    • Bijnsdorp, I.V.1    Geldof, A.A.2    Lavaei, M.3    Piersma, S.R.4
  • 113
    • 84888384111 scopus 로고    scopus 로고
    • Unexpected gain of function for the scaffolding protein plectin due to mislocalization in pancreatic cancer
    • Shin, S. J., Smith, J. A., Rezniczek, G. A., Pan, S. et al., Unexpected gain of function for the scaffolding protein plectin due to mislocalization in pancreatic cancer. Proc. Natl. Acad. Sci. USA 2013, 110, 19414-19419.
    • (2013) Proc. Natl. Acad. Sci. USA , vol.110 , pp. 19414-19419
    • Shin, S.J.1    Smith, J.A.2    Rezniczek, G.A.3    Pan, S.4
  • 114
    • 84884171136 scopus 로고    scopus 로고
    • MicroRNA and protein profiling of brain metastasis competent cell-derived exosomes
    • Camacho, L., Guerrero, P., Marchetti, D., MicroRNA and protein profiling of brain metastasis competent cell-derived exosomes. PLoS One 2013, 8, e73790.
    • (2013) PLoS One , vol.8 , pp. e73790
    • Camacho, L.1    Guerrero, P.2    Marchetti, D.3
  • 115
    • 84885915953 scopus 로고    scopus 로고
    • Increased bisecting N-acetylglucosamine and decreased branched chain glycans of N-linked glycoproteins in expressed prostatic secretions associated with prostate cancer progression
    • Nyalwidhe, J. O., Betesh, L. R., Powers, T. W., Jones, E. E. et al., Increased bisecting N-acetylglucosamine and decreased branched chain glycans of N-linked glycoproteins in expressed prostatic secretions associated with prostate cancer progression. Proteomics Clin. Appl. 2013, 677-689. doi: 10.1002/prca.201200134
    • (2013) Proteomics Clin. Appl , pp. 677-689
    • Nyalwidhe, J.O.1    Betesh, L.R.2    Powers, T.W.3    Jones, E.E.4
  • 116
    • 84880630042 scopus 로고    scopus 로고
    • Identification and characterization of proteins isolated from microvesicles derived from human lung cancer pleural effusions
    • Park, J. O., Choi, D. Y., Choi, D. S., Kim, H. J. et al., Identification and characterization of proteins isolated from microvesicles derived from human lung cancer pleural effusions. Proteomics 2013, 13, 2125-2134.
    • (2013) Proteomics , vol.13 , pp. 2125-2134
    • Park, J.O.1    Choi, D.Y.2    Choi, D.S.3    Kim, H.J.4
  • 117
    • 84877756603 scopus 로고    scopus 로고
    • Differential protein profiling of renal cell carcinoma urinary exosomes
    • Raimondo, F., Morosi, L., Corbetta, S., Chinello, C. et al., Differential protein profiling of renal cell carcinoma urinary exosomes. Mol. Biosyst. 2013, 9, 1220-1233.
    • (2013) Mol. Biosyst. , vol.9 , pp. 1220-1233
    • Raimondo, F.1    Morosi, L.2    Corbetta, S.3    Chinello, C.4
  • 118
    • 84899534559 scopus 로고    scopus 로고
    • Proteomic analysis of saliva in HIV-positive heroin addicts reveals proteins correlated with cognition
    • Dominy, S. S., Brown, J. N., Ryder, M. I., Gritsenko, M. et al., Proteomic analysis of saliva in HIV-positive heroin addicts reveals proteins correlated with cognition. PLoS One 2014, 9, e89366.
    • (2014) PLoS One , vol.9 , pp. e89366
    • Dominy, S.S.1    Brown, J.N.2    Ryder, M.I.3    Gritsenko, M.4
  • 119
    • 84901259449 scopus 로고    scopus 로고
    • The use of nanotrap particles technology in capturing HIV-1 virions and viral proteins from infected cells
    • Jaworski, E., Saifuddin, M., Sampey, G., Shafagati, N. et al., The use of nanotrap particles technology in capturing HIV-1 virions and viral proteins from infected cells. PLoS One 2014, 9, e96778.
    • (2014) PLoS One , vol.9 , pp. e96778
    • Jaworski, E.1    Saifuddin, M.2    Sampey, G.3    Shafagati, N.4
  • 120
    • 84899674650 scopus 로고    scopus 로고
    • Absence of metalloprotease GP63 alters the protein content of leishmania exosomes
    • Hassani, K., Shio, M. T., Martel, C., Faubert, D. et al., Absence of metalloprotease GP63 alters the protein content of leishmania exosomes. PLoS One 2014, 9, e95007.
    • (2014) PLoS One , vol.9 , pp. e95007
    • Hassani, K.1    Shio, M.T.2    Martel, C.3    Faubert, D.4
  • 121
    • 84893823896 scopus 로고    scopus 로고
    • Exosomal proteins in the aqueous humor as novel biomarkers in patients with neovascular age-related macular degeneration
    • Kang, G. Y., Bang, J. Y., Choi, A. J., Yoon, J. et al., Exosomal proteins in the aqueous humor as novel biomarkers in patients with neovascular age-related macular degeneration. J. Proteome Res. 2014, 13, 581-595.
    • (2014) J. Proteome Res. , vol.13 , pp. 581-595
    • Kang, G.Y.1    Bang, J.Y.2    Choi, A.J.3    Yoon, J.4
  • 122
    • 84866426167 scopus 로고    scopus 로고
    • Exosomes: vehicles for the transfer of toxic proteins associated with neurodegenerative diseases
    • Bellingham, S. A., Guo, B. B., Coleman, B. M., Hill, A. F., Exosomes: vehicles for the transfer of toxic proteins associated with neurodegenerative diseases? Front Physiol. 2012, 3, 124.
    • (2012) Front Physiol , vol.3 , pp. 124
    • Bellingham, S.A.1    Guo, B.B.2    Coleman, B.M.3    Hill, A.F.4
  • 123
    • 84900036747 scopus 로고    scopus 로고
    • Proteomic analysis of cerebrospinal fluid extracellular vesicles: a comprehensive dataset
    • Chiasserini, D., van Weering, J. R., Piersma, S. R., Pham, T. V. et al., Proteomic analysis of cerebrospinal fluid extracellular vesicles: a comprehensive dataset. J. Proteomics 2014, 106C, 191-204.
    • (2014) J. Proteomics , vol.106 C , pp. 191-204
    • Chiasserini, D.1    Weering van, J.R.2    Piersma, S.R.3    Pham, T.V.4
  • 124
    • 84899734394 scopus 로고    scopus 로고
    • Quantitative proteomic analysis of hepatocyte-secreted extracellular vesicles reveals candidate markers for liver toxicity
    • Rodriguez-Suarez, E., Gonzalez, E., Hughes, C., Conde-Vancells, J. et al., Quantitative proteomic analysis of hepatocyte-secreted extracellular vesicles reveals candidate markers for liver toxicity. J. Proteomics 2014, 103, 227-240.
    • (2014) J. Proteomics , vol.103 , pp. 227-240
    • Rodriguez-Suarez, E.1    Gonzalez, E.2    Hughes, C.3    Conde-Vancells, J.4
  • 125
    • 84894578152 scopus 로고    scopus 로고
    • Glioblastoma extracellular vesicles: reservoirs of potential biomarkers
    • Redzic, J. S., Ung, T. H., Graner, M. W., Glioblastoma extracellular vesicles: reservoirs of potential biomarkers. Pharmgenomics Pers. Med. 2014, 7, 65-77.
    • (2014) Pharmgenomics Pers. Med , vol.7 , pp. 65-77
    • Redzic, J.S.1    Ung, T.H.2    Graner, M.W.3
  • 126
    • 27844450020 scopus 로고    scopus 로고
    • Purification, characterization and biological significance of tumor-derived exosomes
    • Koga, K., Matsumoto, K., Akiyoshi, T., Kubo, M. et al., Purification, characterization and biological significance of tumor-derived exosomes. Anticancer Res. 2005, 25, 3703-3707.
    • (2005) Anticancer Res , vol.25 , pp. 3703-3707
    • Koga, K.1    Matsumoto, K.2    Akiyoshi, T.3    Kubo, M.4
  • 127
    • 38048999426 scopus 로고    scopus 로고
    • Proteomic analysis of microvesicles derived from human colorectal cancer cells
    • Choi, D. S., Lee, J. M., Park, G. W., Lim, H. W. et al., Proteomic analysis of microvesicles derived from human colorectal cancer cells. J. Proteome Res. 2007, 6, 4646-4655.
    • (2007) J. Proteome Res. , vol.6 , pp. 4646-4655
    • Choi, D.S.1    Lee, J.M.2    Park, G.W.3    Lim, H.W.4
  • 128
    • 84878630476 scopus 로고    scopus 로고
    • Proteome profiling of exosomes derived from human primary and metastatic colorectal cancer cells reveal differential expression of key metastatic factors and signal transduction components
    • Ji, H., Greening, D. W., Barnes, T. W., Lim, J. W. et al., Proteome profiling of exosomes derived from human primary and metastatic colorectal cancer cells reveal differential expression of key metastatic factors and signal transduction components. Proteomics 2013, 13, 1672-1686.
    • (2013) Proteomics , vol.13 , pp. 1672-1686
    • Ji, H.1    Greening, D.W.2    Barnes, T.W.3    Lim, J.W.4
  • 129
    • 20244373139 scopus 로고    scopus 로고
    • Tumor-derived exosomes are a source of shared tumor rejection antigens for CTL cross-priming
    • Wolfers, J., Lozier, A., Raposo, G., Regnault, A. et al., Tumor-derived exosomes are a source of shared tumor rejection antigens for CTL cross-priming. Nat. Med. 2001, 7, 297-303.
    • (2001) Nat. Med. , vol.7 , pp. 297-303
    • Wolfers, J.1    Lozier, A.2    Raposo, G.3    Regnault, A.4
  • 130
    • 0036120616 scopus 로고    scopus 로고
    • Laser capture microdissection and two-dimensional polyacrylamide gel electrophoresis: evaluation of tissue preparation and sample limitations
    • Craven, R. A., Totty, N., Harnden, P., Selby, P. J. et al., Laser capture microdissection and two-dimensional polyacrylamide gel electrophoresis: evaluation of tissue preparation and sample limitations. Am. J. Pathol. 2002, 160, 815-822.
    • (2002) Am. J. Pathol. , vol.160 , pp. 815-822
    • Craven, R.A.1    Totty, N.2    Harnden, P.3    Selby, P.J.4
  • 131
    • 84865477117 scopus 로고    scopus 로고
    • Melanoma cell-derived exosomes alter macrophage and dendritic cell functions in vitro
    • Marton, A., Vizler, C., Kusz, E., Temesfoi, V. et al., Melanoma cell-derived exosomes alter macrophage and dendritic cell functions in vitro. Immunol. Lett. 2012, 148, 34-38.
    • (2012) Immunol. Lett , vol.148 , pp. 34-38
    • Marton, A.1    Vizler, C.2    Kusz, E.3    Temesfoi, V.4
  • 132
    • 11144353573 scopus 로고    scopus 로고
    • Proteomic analysis of exosomes secreted by human mesothelioma cells
    • Hegmans, J. P., Bard, M. P., Hemmes, A., Luider, T. M. et al., Proteomic analysis of exosomes secreted by human mesothelioma cells. Am. J. Pathol. 2004, 164, 1807-1815.
    • (2004) Am. J. Pathol. , vol.164 , pp. 1807-1815
    • Hegmans, J.P.1    Bard, M.P.2    Hemmes, A.3    Luider, T.M.4
  • 133
    • 70349316341 scopus 로고    scopus 로고
    • Proteomic and immunologic analyses of brain tumor exosomes
    • Graner, M. W., Alzate, O., Dechkovskaia, A. M., Keene, J. D. et al., Proteomic and immunologic analyses of brain tumor exosomes. FASEB J. 2009, 23, 1541-1557.
    • (2009) FASEB J , vol.23 , pp. 1541-1557
    • Graner, M.W.1    Alzate, O.2    Dechkovskaia, A.M.3    Keene, J.D.4
  • 134
    • 55749112807 scopus 로고    scopus 로고
    • Proteomic profiling of exosomes: current perspectives
    • Simpson, R. J., Jensen, S. S., Lim, J. W., Proteomic profiling of exosomes: current perspectives. Proteomics 2008, 8, 4083-4099.
    • (2008) Proteomics , vol.8 , pp. 4083-4099
    • Simpson, R.J.1    Jensen, S.S.2    Lim, J.W.3
  • 136
    • 79960147502 scopus 로고    scopus 로고
    • Exosome isolation for proteomic analyses and RN A profiling
    • Taylor, D. D., Zacharias, W., Gercel-Taylor, C., Exosome isolation for proteomic analyses and RN A profiling. Methods Mol. Biol. 2011, 728, 235-246.
    • (2011) Methods Mol. Biol. , vol.728 , pp. 235-246
    • Taylor, D.D.1    Zacharias, W.2    Gercel-Taylor, C.3
  • 137
    • 85015684168 scopus 로고    scopus 로고
    • The impact of disparate isolation methods for extracellular vesicles on downstream RNA profiling
    • Van Deun, J., Mestdagh, P., Sormunen, R., Cocquyt, V. et al. The impact of disparate isolation methods for extracellular vesicles on downstream RNA profiling. J. Extracell Vesicles 2014, 3, doi: 10.3402/jev.v3.24858
    • (2014) J. Extracell Vesicles , vol.3
    • Deun Van, J.1    Mestdagh, P.2    Sormunen, R.3    Cocquyt, V.4
  • 138
  • 139
    • 84884379486 scopus 로고    scopus 로고
    • Proteome profiling of neuroblastoma-derived exosomes reveal the expression of proteins potentially involved in tumor progression
    • Marimpietri, D., Petretto, A., Raffaghello, L., Pezzolo, A. et al., Proteome profiling of neuroblastoma-derived exosomes reveal the expression of proteins potentially involved in tumor progression. PLoS One 2013, 8, e75054.
    • (2013) PLoS One , vol.8 , pp. e75054
    • Marimpietri, D.1    Petretto, A.2    Raffaghello, L.3    Pezzolo, A.4
  • 140
    • 84877738076 scopus 로고    scopus 로고
    • Urinary exosomes and diabetic nephropathy: a proteomic approach
    • Raimondo, F., Corbetta, S., Morosi, L., Chinello, C. et al., Urinary exosomes and diabetic nephropathy: a proteomic approach. Mol. Biosyst. 2013, 9, 1139-1146.
    • (2013) Mol. Biosyst. , vol.9 , pp. 1139-1146
    • Raimondo, F.1    Corbetta, S.2    Morosi, L.3    Chinello, C.4
  • 141
    • 84893868499 scopus 로고    scopus 로고
    • Exosomes from myeloid-derived suppressor cells carry biologically active proteins
    • Burke, M., Choksawangkarn, W., Edwards, N., Ostrand-Rosenberg, S. et al., Exosomes from myeloid-derived suppressor cells carry biologically active proteins. J. Proteome Res. 2014, 13, 836-843.
    • (2014) J. Proteome Res. , vol.13 , pp. 836-843
    • Burke, M.1    Choksawangkarn, W.2    Edwards, N.3    Ostrand-Rosenberg, S.4
  • 142
    • 84855384454 scopus 로고    scopus 로고
    • Identification and proteomic profiling of exosomes in human cerebrospinal fluid
    • Street, J. M., Barran, P. E., Mackay, C. L., Weidt, S. et al. Identification and proteomic profiling of exosomes in human cerebrospinal fluid. J. Transl. Med. 2012, 10, 5.
    • (2012) J. Transl. Med , vol.10 , pp. 5
    • Street, J.M.1    Barran, P.E.2    Mackay, C.L.3    Weidt, S.4
  • 143
    • 43249109372 scopus 로고    scopus 로고
    • Isolation and characterization of exosomes from cell culture supernatants and biological fluids
    • Unit 3 22
    • Thery, C., Amigorena, S., Raposo, G., Clayton, A., Isolation and characterization of exosomes from cell culture supernatants and biological fluids. Curr. Protoc. Cell Biol. Chapter 2006, 3, Unit 3 22.
    • (2006) Curr. Protoc. Cell Biol. Chapter , vol.3
    • Thery, C.1    Amigorena, S.2    Raposo, G.3    Clayton, A.4
  • 145
    • 77957373390 scopus 로고    scopus 로고
    • Temporal profiling of the secretome during adipogenesis in humans
    • Zhong, J., Krawczyk, S. A., Chaerkady, R., Huang, H. et al., Temporal profiling of the secretome during adipogenesis in humans. J. Proteome Res. 2010, 9, 5228-5238.
    • (2010) J. Proteome Res , vol.9 , pp. 5228-5238
    • Zhong, J.1    Krawczyk, S.A.2    Chaerkady, R.3    Huang, H.4
  • 146
    • 84860381828 scopus 로고    scopus 로고
    • A proteomics approach for the identification and cloning of monoclonal antibodies from serum
    • Cheung, W. C., Beausoleil, S. A., Zhang, X., Sato, S. et al., A proteomics approach for the identification and cloning of monoclonal antibodies from serum. Nat. Biotechnol. 2012, 30, 447-452.
    • (2012) Nat. Biotechnol , vol.30 , pp. 447-452
    • Cheung, W.C.1    Beausoleil, S.A.2    Zhang, X.3    Sato, S.4
  • 147
    • 84874223925 scopus 로고    scopus 로고
    • Molecular deconvolution of the monoclonal antibodies that comprise the polyclonal serum response
    • Wine, Y., Boutz, D. R., Lavinder, J. J., Miklos, A. E. et al., Molecular deconvolution of the monoclonal antibodies that comprise the polyclonal serum response. Proc. Natl. Acad. Sci. USA 2013, 110, 2993-2998.
    • (2013) Proc. Natl. Acad. Sci. USA , vol.110 , pp. 2993-2998
    • Wine, Y.1    Boutz, D.R.2    Lavinder, J.J.3    Miklos, A.E.4
  • 148
    • 0033434080 scopus 로고    scopus 로고
    • Probability-based protein identification by searching sequence databases using mass spectrometry data
    • Perkins, D. N., Pappin, D. J., Creasy, D. M., Cottrell, J. S., Probability-based protein identification by searching sequence databases using mass spectrometry data. Electrophoresis 1999, 20, 3551-3567.
    • (1999) Electrophoresis , vol.20 , pp. 3551-3567
    • Perkins, D.N.1    Pappin, D.J.2    Creasy, D.M.3    Cottrell, J.S.4
  • 149
    • 79958164837 scopus 로고    scopus 로고
    • A guide through the computational analysis of isotope-labeled mass spectrometry-based quantitative proteomics data: an application study
    • Albaum, S. P., Hahne, H., Otto, A., Haussmann, U. et al. A guide through the computational analysis of isotope-labeled mass spectrometry-based quantitative proteomics data: an application study. Proteome Sci 2011, 9, 30.
    • (2011) Proteome Sci , vol.9 , pp. 30
    • Albaum, S.P.1    Hahne, H.2    Otto, A.3    Haussmann, U.4
  • 150
    • 0000857494 scopus 로고
    • An approach to correlate tandem mass spectral data of peptides with amino acid sequences in a protein database
    • Eng, J. K., McCormack, A. L., Yates, J. R., An approach to correlate tandem mass spectral data of peptides with amino acid sequences in a protein database. J. Am. Soc. Mass Spectrom. 1994, 5, 976-989.
    • (1994) J. Am. Soc. Mass Spectrom. , vol.5 , pp. 976-989
    • Eng, J.K.1    McCormack, A.L.2    Yates, J.R.3
  • 151
    • 77950660595 scopus 로고    scopus 로고
    • TagRecon: high-throughput mutation identification through sequence tagging
    • Dasari, S., Chambers, M. C., Slebos, R. J., Zimmerman, L. J. et al. TagRecon: high-throughput mutation identification through sequence tagging. J. Proteome Res. 2010, 9, 1716-1726.
    • (2010) J. Proteome Res. , vol.9 , pp. 1716-1726
    • Dasari, S.1    Chambers, M.C.2    Slebos, R.J.3    Zimmerman, L.J.4
  • 153
    • 20644442887 scopus 로고    scopus 로고
    • MSight: an image analysis software for liquid chromatography-mass spectrometry
    • Palagi, P. M., Walther, D., Quadroni, M., Catherinet, S. et al., MSight: an image analysis software for liquid chromatography-mass spectrometry. Proteomics 2005, 5, 2381-2384.
    • (2005) Proteomics , vol.5 , pp. 2381-2384
    • Palagi, P.M.1    Walther, D.2    Quadroni, M.3    Catherinet, S.4
  • 154
    • 10744233766 scopus 로고    scopus 로고
    • Quantification of proteins and metabolites by mass spectrometry without isotopic labeling or spiked standards
    • Wang, W., Zhou, H., Lin, H., Roy, S. et al., Quantification of proteins and metabolites by mass spectrometry without isotopic labeling or spiked standards. Anal. Chem. 2003, 75, 4818-4826.
    • (2003) Anal. Chem. , vol.75 , pp. 4818-4826
    • Wang, W.1    Zhou, H.2    Lin, H.3    Roy, S.4
  • 155
    • 84891760956 scopus 로고    scopus 로고
    • Data, information, knowledge and principle: back to metabolism in KEGG
    • Kanehisa, M., Goto, S., Sato, Y., Kawashima, M. et al. Data, information, knowledge and principle: back to metabolism in KEGG. Nucleic Acids Res. 2014, 42, D199-D205.
    • (2014) Nucleic Acids Res , vol.42 , pp. D199-D205
    • Kanehisa, M.1    Goto, S.2    Sato, Y.3    Kawashima, M.4
  • 156
    • 0033982936 scopus 로고    scopus 로고
    • KEGG: kyoto encyclopedia of genes and genomes
    • Kanehisa, M., Goto, S., KEGG: kyoto encyclopedia of genes and genomes. Nucleic Acids Res. 2000, 28, 27-30.
    • (2000) Nucleic Acids Res , vol.28 , pp. 27-30
    • Kanehisa, M.1    Goto, S.2
  • 158
    • 38449101120 scopus 로고    scopus 로고
    • Integration of biological networks and gene expression data using Cytoscape
    • Cline, M. S., Smoot, M., Cerami, E., Kuchinsky, A. et al., Integration of biological networks and gene expression data using Cytoscape. Nat. Protoc. 2007, 2, 2366-2382.
    • (2007) Nat. Protoc. , vol.2 , pp. 2366-2382
    • Cline, M.S.1    Smoot, M.2    Cerami, E.3    Kuchinsky, A.4
  • 159
    • 61449172037 scopus 로고    scopus 로고
    • Systematic and integrative analysis of large gene lists using DAVID bioinformatics resources
    • Huang da W., Sherman, B. T., Lempicki, R. A., Systematic and integrative analysis of large gene lists using DAVID bioinformatics resources. Nat. Protoc. 2009, 4, 44-57.
    • (2009) Nat. Protoc , vol.4 , pp. 44-57
    • Huang da, W.1    Sherman, B.T.2    Lempicki, R.A.3
  • 160
    • 58549112996 scopus 로고    scopus 로고
    • Bioinformatics enrichment tools: paths toward the comprehensive functional analysis of large gene lists
    • Huang da W., Sherman, B. T., Lempicki, R. A., Bioinformatics enrichment tools: paths toward the comprehensive functional analysis of large gene lists. Nucleic Acids Res. 2009, 37, 1-13.
    • (2009) Nucleic Acids Res , vol.37 , pp. 1-13
    • Huang da, W.1    Sherman, B.T.2    Lempicki, R.A.3
  • 161
    • 0035910270 scopus 로고    scopus 로고
    • Predicting transmembrane protein topology with a hidden Markov model: application to complete genomes
    • Krogh, A., Larsson, B., von Heijne, G., Sonnhammer, E. L., Predicting transmembrane protein topology with a hidden Markov model: application to complete genomes. J. Mol. Biol. 2001, 305, 567-580.
    • (2001) J. Mol. Biol , vol.305 , pp. 567-580
    • Krogh, A.1    Larsson, B.2    Heijne von, G.3    Sonnhammer, E.L.4
  • 162
    • 2142657817 scopus 로고    scopus 로고
    • A combined transmembrane topology and signal peptide prediction method
    • Kall, L., Krogh, A., Sonnhammer, E. L., A combined transmembrane topology and signal peptide prediction method. J. Mol. Biol. 2004, 338, 1027-1036.
    • (2004) J. Mol. Biol , vol.338 , pp. 1027-1036
    • Kall, L.1    Krogh, A.2    Sonnhammer, E.L.3
  • 163
    • 0034697980 scopus 로고    scopus 로고
    • Predicting subcellular localization of proteins based on their N-terminal amino acid sequence
    • Emanuelsson, O., Nielsen, H., Brunak, S., von Heijne, G., Predicting subcellular localization of proteins based on their N-terminal amino acid sequence. J. Mol. Biol. 2000, 300, 1005-1016.
    • (2000) J. Mol. Biol , vol.300 , pp. 1005-1016
    • Emanuelsson, O.1    Nielsen, H.2    Brunak, S.3    Heijne von, G.4
  • 164
    • 3042692704 scopus 로고    scopus 로고
    • Feature-based prediction of non-classical and leaderless protein secretion
    • Bendtsen, J. D., Jensen, L. J., Blom, N., Von Heijne, G. et al., Feature-based prediction of non-classical and leaderless protein secretion. Protein Eng. Des. Sel. 2004, 17, 349-356.
    • (2004) Protein Eng. Des. Sel , vol.17 , pp. 349-356
    • Bendtsen, J.D.1    Jensen, L.J.2    Blom, N.3    Heijne Von, G.4
  • 165
    • 0027105007 scopus 로고
    • A knowledge base for predicting protein localization sites in eukaryotic cells
    • Nakai, K., Kanehisa, M., A knowledge base for predicting protein localization sites in eukaryotic cells. Genomics 1992, 14, 897-911.
    • (1992) Genomics , vol.14 , pp. 897-911
    • Nakai, K.1    Kanehisa, M.2
  • 167
    • 13444269483 scopus 로고    scopus 로고
    • SPD-a web-based secreted protein database
    • Chen, Y., Zhang, Y., Yin, Y., Gao, G. et al., SPD-a web-based secreted protein database. Nucleic Acids Res. 2005, 33, D169-D173.
    • (2005) Nucleic Acids Res , vol.33 , pp. D169-D173
    • Chen, Y.1    Zhang, Y.2    Yin, Y.3    Gao, G.4
  • 168
    • 84867045160 scopus 로고    scopus 로고
    • Current challenges in software solutions for mass spectrometry-based quantitative proteomics
    • Cappadona, S., Baker, P. R., Cutillas, P. R., Heck, A. J. et al., Current challenges in software solutions for mass spectrometry-based quantitative proteomics. Amino Acids 2005, 43, 1087-1108.
    • (2005) Amino Acids , vol.43 , pp. 1087-1108
    • Cappadona, S.1    Baker, P.R.2    Cutillas, P.R.3    Heck, A.J.4
  • 169
    • 5344244656 scopus 로고    scopus 로고
    • R: A Language and Environment for Statistical Computing. R Foundation for Statistical Computing, Vienna, Austria
    • R Core Team. R: A Language and Environment for Statistical Computing. R Foundation for Statistical Computing, Vienna, Austria. 2013. http://www.R-project.org/
    • (2013)


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.