메뉴 건너뛰기




Volumn 14, Issue 6, 2015, Pages 2367-2384

Mass-spectrometry-based molecular characterization of extracellular vesicles: Lipidomics and proteomics

Author keywords

EV; exosome; extracellular vesicle; lipidomics; mass spectrometry; microparticle; microvesicle; molecular profiling; post translational modifications; proteomics

Indexed keywords

PROTEOME; CONDITIONED MEDIUM; LIPID;

EID: 84930599499     PISSN: 15353893     EISSN: 15353907     Source Type: Journal    
DOI: 10.1021/pr501279t     Document Type: Article
Times cited : (184)

References (184)
  • 2
    • 4444226979 scopus 로고    scopus 로고
    • Identification and proteomic profiling of exosomes in human urine
    • Pisitkun, T.; Shen, R. F.; Knepper, M. A. Identification and proteomic profiling of exosomes in human urine Proc. Natl. Acad. Sci. U. S. A. 2004, 101 (36) 13368-73
    • (2004) Proc. Natl. Acad. Sci. U. S. A. , vol.101 , Issue.36 , pp. 13368-13373
    • Pisitkun, T.1    Shen, R.F.2    Knepper, M.A.3
  • 5
    • 33845618038 scopus 로고    scopus 로고
    • Association of citrullinated proteins with synovial exosomes
    • Skriner, K.; Adolph, K.; Jungblut, P. R.; Burmester, G. R. Association of citrullinated proteins with synovial exosomes Arthritis Rheum. 2006, 54 (12) 3809-14
    • (2006) Arthritis Rheum. , vol.54 , Issue.12 , pp. 3809-3814
    • Skriner, K.1    Adolph, K.2    Jungblut, P.R.3    Burmester, G.R.4
  • 8
    • 18644377363 scopus 로고    scopus 로고
    • Salivary gland epithelial cell exosomes: A source of autoantigenic ribonucleoproteins
    • Kapsogeorgou, E. K.; Abu-Helu, R. F.; Moutsopoulos, H. M.; Manoussakis, M. N. Salivary gland epithelial cell exosomes: A source of autoantigenic ribonucleoproteins Arthritis Rheum. 2005, 52 (5) 1517-21
    • (2005) Arthritis Rheum. , vol.52 , Issue.5 , pp. 1517-1521
    • Kapsogeorgou, E.K.1    Abu-Helu, R.F.2    Moutsopoulos, H.M.3    Manoussakis, M.N.4
  • 10
    • 84890246880 scopus 로고    scopus 로고
    • A Nobel Prize for membrane traffic: Vesicles find their journeys end
    • Mellman, I.; Emr, S. D. A Nobel Prize for membrane traffic: vesicles find their journeys end J. Cell Biol. 2013, 203 (4) 559-61
    • (2013) J. Cell Biol. , vol.203 , Issue.4 , pp. 559-561
    • Mellman, I.1    Emr, S.D.2
  • 11
    • 70350449455 scopus 로고    scopus 로고
    • ExoCarta: A compendium of exosomal proteins and RNA
    • Mathivanan, S.; Simpson, R. J. ExoCarta: A compendium of exosomal proteins and RNA Proteomics 2009, 9 (21) 4997-5000
    • (2009) Proteomics , vol.9 , Issue.21 , pp. 4997-5000
    • Mathivanan, S.1    Simpson, R.J.2
  • 14
    • 84879603171 scopus 로고    scopus 로고
    • Exosomes in tumor microenvironment influence cancer progression and metastasis
    • Kahlert, C.; Kalluri, R. Exosomes in tumor microenvironment influence cancer progression and metastasis J. Mol. Med. (Heidelberg, Ger.) 2013, 91 (4) 431-7
    • (2013) J. Mol. Med. (Heidelberg, Ger.) , vol.91 , Issue.4 , pp. 431-437
    • Kahlert, C.1    Kalluri, R.2
  • 15
    • 79957879331 scopus 로고    scopus 로고
    • Exosomes released by melanoma cells prepare sentinel lymph nodes for tumor metastasis
    • Hood, J. L.; San, R. S.; Wickline, S. A. Exosomes released by melanoma cells prepare sentinel lymph nodes for tumor metastasis Cancer Res. 2011, 71 (11) 3792-801
    • (2011) Cancer Res. , vol.71 , Issue.11 , pp. 3792-3801
    • Hood, J.L.1    San, R.S.2    Wickline, S.A.3
  • 16
    • 68849129712 scopus 로고    scopus 로고
    • Membrane vesicles as conveyors of immune responses
    • Thery, C.; Ostrowski, M.; Segura, E. Membrane vesicles as conveyors of immune responses Nat. Rev. Immunol 2009, 9 (8) 581-93
    • (2009) Nat. Rev. Immunol , vol.9 , Issue.8 , pp. 581-593
    • Thery, C.1    Ostrowski, M.2    Segura, E.3
  • 18
    • 84949934993 scopus 로고    scopus 로고
    • As we wait: Coping with an imperfect nomenclature for extracellular vesicles
    • Gould, S. J.; Raposo, G. As we wait: coping with an imperfect nomenclature for extracellular vesicles J. Extracell. Vesicles 2013, 10.3402/jev.v2i0.2038
    • (2013) J. Extracell. Vesicles
    • Gould, S.J.1    Raposo, G.2
  • 20
    • 0343067073 scopus 로고    scopus 로고
    • Lysosome membrane permeability: Implications for drug delivery
    • Lloyd, J. B. Lysosome membrane permeability: implications for drug delivery Adv. Drug Delivery Rev. 2000, 41 (2) 189-200
    • (2000) Adv. Drug Delivery Rev. , vol.41 , Issue.2 , pp. 189-200
    • Lloyd, J.B.1
  • 21
    • 1542268930 scopus 로고    scopus 로고
    • Lipid vesicles and other colloids as drug carriers on the skin
    • Cevc, G. Lipid vesicles and other colloids as drug carriers on the skin Adv. Drug Delivery Rev. 2004, 56 (5) 675-711
    • (2004) Adv. Drug Delivery Rev. , vol.56 , Issue.5 , pp. 675-711
    • Cevc, G.1
  • 25
    • 45449093192 scopus 로고    scopus 로고
    • MicroRNA signatures of tumor-derived exosomes as diagnostic biomarkers of ovarian cancer
    • Taylor, D. D.; Gercel-Taylor, C. MicroRNA signatures of tumor-derived exosomes as diagnostic biomarkers of ovarian cancer Gynecol. Oncol. 2008, 110 (1) 13-21
    • (2008) Gynecol. Oncol. , vol.110 , Issue.1 , pp. 13-21
    • Taylor, D.D.1    Gercel-Taylor, C.2
  • 27
    • 67949097489 scopus 로고    scopus 로고
    • Exosomes-vesicular carriers for intercellular communication
    • Simons, M.; Raposo, G. Exosomes-vesicular carriers for intercellular communication Curr. Opin. Cell Biol. 2009, 21 (4) 575-581
    • (2009) Curr. Opin. Cell Biol. , vol.21 , Issue.4 , pp. 575-581
    • Simons, M.1    Raposo, G.2
  • 28
    • 84888361975 scopus 로고    scopus 로고
    • Prostasomes: Extracellular vesicles from the prostate
    • Aalberts, M.; Stout, T. A.; Stoorvogel, W. Prostasomes: extracellular vesicles from the prostate Reproduction 2014, 147 (1) R1-14
    • (2014) Reproduction , vol.147 , Issue.1 , pp. 1-14
    • Aalberts, M.1    Stout, T.A.2    Stoorvogel, W.3
  • 29
    • 84874377202 scopus 로고    scopus 로고
    • Extracellular vesicles: Exosomes, microvesicles, and friends
    • Raposo, G.; Stoorvogel, W. Extracellular vesicles: Exosomes, microvesicles, and friends J. Cell Biol. 2013, 200 (4) 373-383
    • (2013) J. Cell Biol. , vol.200 , Issue.4 , pp. 373-383
    • Raposo, G.1    Stoorvogel, W.2
  • 30
    • 43249109372 scopus 로고    scopus 로고
    • Isolation and characterization of exosomes from cell culture supernatants and biological fluids
    • Thery, C.; Amigorena, S.; Raposo, G.; Clayton, A. Isolation and characterization of exosomes from cell culture supernatants and biological fluids Curr. Protoc. Cell Biol. 2006, 10.1002/0471143030.cb0322s30
    • (2006) Curr. Protoc. Cell Biol.
    • Thery, C.1    Amigorena, S.2    Raposo, G.3    Clayton, A.4
  • 31
    • 84888042782 scopus 로고    scopus 로고
    • Comparative proteomics evaluation of plasma exosome isolation techniques and assessment of the stability of exosomes in normal human blood plasma
    • Kalra, H.; Adda, C. G.; Liem, M.; Ang, C. S.; Mechler, A.; Simpson, R. J.; Hulett, M. D.; Mathivanan, S. Comparative proteomics evaluation of plasma exosome isolation techniques and assessment of the stability of exosomes in normal human blood plasma Proteomics 2013, 13 (22) 3354-3364
    • (2013) Proteomics , vol.13 , Issue.22 , pp. 3354-3364
    • Kalra, H.1    Adda, C.G.2    Liem, M.3    Ang, C.S.4    Mechler, A.5    Simpson, R.J.6    Hulett, M.D.7    Mathivanan, S.8
  • 33
    • 84867118648 scopus 로고    scopus 로고
    • Exosomes and microvesicles: Extracellular vesicles for genetic information transfer and gene therapy
    • Lee, Y.; El Andaloussi, S.; Wood, M. J. Exosomes and microvesicles: extracellular vesicles for genetic information transfer and gene therapy Hum. Mol. Genet. 2012, 21 (R1) R125-34
    • (2012) Hum. Mol. Genet. , vol.21 , Issue.R1 , pp. 125-134
    • Lee, Y.1    El Andaloussi, S.2    Wood, M.J.3
  • 34
    • 84862618600 scopus 로고    scopus 로고
    • Tumor-derived microvesicles: Shedding light on novel microenvironment modulators and prospective cancer biomarkers
    • DSouza-Schorey, C.; Clancy, J. W. Tumor-derived microvesicles: shedding light on novel microenvironment modulators and prospective cancer biomarkers Genes Dev. 2012, 26 (12) 1287-99
    • (2012) Genes Dev. , vol.26 , Issue.12 , pp. 1287-1299
    • Dsouza-Schorey, C.1    Clancy, J.W.2
  • 35
    • 84876814290 scopus 로고    scopus 로고
    • Extracellular communication via microRNA: Lipid particles have a new message
    • Rayner, K. J.; Hennessy, E. J. Extracellular communication via microRNA: lipid particles have a new message J. Lipid Res. 2013, 54 (5) 1174-81
    • (2013) J. Lipid Res. , vol.54 , Issue.5 , pp. 1174-1181
    • Rayner, K.J.1    Hennessy, E.J.2
  • 36
    • 79960668648 scopus 로고    scopus 로고
    • Structural components and architectures of RNA exosomes
    • Januszyk, K.; Lima, C. D. Structural components and architectures of RNA exosomes Adv. Exp. Med. Biol. 2010, 702, 9-28
    • (2010) Adv. Exp. Med. Biol. , vol.702 , pp. 9-28
    • Januszyk, K.1    Lima, C.D.2
  • 37
    • 33846502114 scopus 로고    scopus 로고
    • Exosome lipidomics unravels lipid sorting at the level of multivesicular bodies
    • Subra, C.; Laulagnier, K.; Perret, B.; Record, M. Exosome lipidomics unravels lipid sorting at the level of multivesicular bodies Biochimie 2007, 89 (2) 205-12
    • (2007) Biochimie , vol.89 , Issue.2 , pp. 205-212
    • Subra, C.1    Laulagnier, K.2    Perret, B.3    Record, M.4
  • 38
    • 84878629272 scopus 로고    scopus 로고
    • Proteomics, transcriptomics and lipidomics of exosomes and ectosomes
    • Choi, D. S.; Kim, D. K.; Kim, Y. K.; Gho, Y. S. Proteomics, transcriptomics and lipidomics of exosomes and ectosomes Proteomics 2013, 13 (10-11) 1554-71
    • (2013) Proteomics , vol.13 , Issue.1011 , pp. 1554-1571
    • Choi, D.S.1    Kim, D.K.2    Kim, Y.K.3    Gho, Y.S.4
  • 40
    • 84858037808 scopus 로고    scopus 로고
    • Comparison of ultracentrifugation, density gradient separation, and immunoaffinity capture methods for isolating human colon cancer cell line LIM1863-derived exosomes
    • Tauro, B. J.; Greening, D. W.; Mathias, R. A.; Ji, H.; Mathivanan, S.; Scott, A. M.; Simpson, R. J. Comparison of ultracentrifugation, density gradient separation, and immunoaffinity capture methods for isolating human colon cancer cell line LIM1863-derived exosomes Methods 2012, 56 (2) 293-304
    • (2012) Methods , vol.56 , Issue.2 , pp. 293-304
    • Tauro, B.J.1    Greening, D.W.2    Mathias, R.A.3    Ji, H.4    Mathivanan, S.5    Scott, A.M.6    Simpson, R.J.7
  • 41
    • 84867575631 scopus 로고    scopus 로고
    • Comparison of protein, microRNA, and mRNA yields using different methods of urinary exosome isolation for the discovery of kidney disease biomarkers
    • Alvarez, M. L.; Khosroheidari, M.; Ravi, R. K.; DiStefano, J. K. Comparison of protein, microRNA, and mRNA yields using different methods of urinary exosome isolation for the discovery of kidney disease biomarkers Kidney Int. 2012, 82 (9) 1024-1032
    • (2012) Kidney Int. , vol.82 , Issue.9 , pp. 1024-1032
    • Alvarez, M.L.1    Khosroheidari, M.2    Ravi, R.K.3    Distefano, J.K.4
  • 42
    • 77956404647 scopus 로고    scopus 로고
    • Exosomes: Extracellular organelles important in intercellular communication
    • Mathivanan, S.; Ji, H.; Simpson, R. J. Exosomes: Extracellular organelles important in intercellular communication J. Proteomics 2010, 73 (10) 1907-1920
    • (2010) J. Proteomics , vol.73 , Issue.10 , pp. 1907-1920
    • Mathivanan, S.1    Ji, H.2    Simpson, R.J.3
  • 48
    • 0034142287 scopus 로고    scopus 로고
    • Early stages of influenza virus entry into Mv-1 lung cells: Involvement of dynamin
    • Roy, A. M.; Parker, J. S.; Parrish, C. R.; Whittaker, G. R. Early stages of influenza virus entry into Mv-1 lung cells: involvement of dynamin Virology 2000, 267 (1) 17-28
    • (2000) Virology , vol.267 , Issue.1 , pp. 17-28
    • Roy, A.M.1    Parker, J.S.2    Parrish, C.R.3    Whittaker, G.R.4
  • 50
    • 0036737881 scopus 로고    scopus 로고
    • Metabolic origins and clinical significance of LDL heterogeneity
    • Berneis, K. K.; Krauss, R. M. Metabolic origins and clinical significance of LDL heterogeneity J. Lipid Res. 2002, 43 (9) 1363-79
    • (2002) J. Lipid Res. , vol.43 , Issue.9 , pp. 1363-1379
    • Berneis, K.K.1    Krauss, R.M.2
  • 51
    • 85024946724 scopus 로고    scopus 로고
    • The influence of rotor type and centrifugation time on the yield and purity of extracellular vesicles
    • Cvjetkovic, A.; Lotvall, J.; Lasser, C. The influence of rotor type and centrifugation time on the yield and purity of extracellular vesicles J. Extracell. Vesicles 2014, 10.3402/jev.v3.23111
    • (2014) J. Extracell. Vesicles
    • Cvjetkovic, A.1    Lotvall, J.2    Lasser, C.3
  • 52
    • 33747030845 scopus 로고    scopus 로고
    • Protein biomarker discovery and validation: The long and uncertain path to clinical utility
    • Rifai, N.; Gillette, M. A.; Carr, S. A. Protein biomarker discovery and validation: the long and uncertain path to clinical utility Nat. Biotechnol. 2006, 24 (8) 971-83
    • (2006) Nat. Biotechnol. , vol.24 , Issue.8 , pp. 971-983
    • Rifai, N.1    Gillette, M.A.2    Carr, S.A.3
  • 53
    • 84864009269 scopus 로고    scopus 로고
    • Quantitative proteomic analysis of exosomes from HIV-1-infected lymphocytic cells
    • Li, M.; Aliotta, J. M.; Asara, J. M.; Tucker, L.; Quesenberry, P.; Lally, M.; Ramratnam, B. Quantitative proteomic analysis of exosomes from HIV-1-infected lymphocytic cells Proteomics 2012, 12 (13) 2203-11
    • (2012) Proteomics , vol.12 , Issue.13 , pp. 2203-2211
    • Li, M.1    Aliotta, J.M.2    Asara, J.M.3    Tucker, L.4    Quesenberry, P.5    Lally, M.6    Ramratnam, B.7
  • 54
    • 84884138140 scopus 로고    scopus 로고
    • Thematic Review Series: High Density Lipoprotein Structure, Function, and Metabolism Proteomic diversity of high density lipoproteins: Our emerging understanding of its importance in lipid transport and beyond
    • Shah, A. S.; Tan, L.; Long, J. L.; Davidson, W. S. Thematic Review Series: High Density Lipoprotein Structure, Function, and Metabolism Proteomic diversity of high density lipoproteins: our emerging understanding of its importance in lipid transport and beyond J. Lipid Res. 2013, 54 (10) 2575-2585
    • (2013) J. Lipid Res. , vol.54 , Issue.10 , pp. 2575-2585
    • Shah, A.S.1    Tan, L.2    Long, J.L.3    Davidson, W.S.4
  • 57
    • 84874600636 scopus 로고    scopus 로고
    • Two Distinct Populations of Exosomes Are Released from LIM1863 Colon Carcinoma Cell-Derived Organoids
    • Tauro, B. J.; Greening, D. W.; Mathias, R. A.; Mathivanan, S.; Ji, H.; Simpson, R. J. Two Distinct Populations of Exosomes Are Released from LIM1863 Colon Carcinoma Cell-Derived Organoids Mol. Cell. Proteomics 2013, 12 (3) 587-598
    • (2013) Mol. Cell. Proteomics , vol.12 , Issue.3 , pp. 587-598
    • Tauro, B.J.1    Greening, D.W.2    Mathias, R.A.3    Mathivanan, S.4    Ji, H.5    Simpson, R.J.6
  • 58
    • 76649094917 scopus 로고    scopus 로고
    • Proteomics Analysis of A33 Immunoaffinity-Purified Exosomes Released from the Human Colon Tumor Cell Line LIM1215 Reveals a Tissue-Specific Protein Signature
    • Mathivanan, S.; Lim, J. W. E.; Tauro, B. J.; Ji, H.; Moritz, R. L.; Simpson, R. J. Proteomics Analysis of A33 Immunoaffinity-Purified Exosomes Released from the Human Colon Tumor Cell Line LIM1215 Reveals a Tissue-Specific Protein Signature Mol. Cell. Proteomics 2010, 9 (2) 197-208
    • (2010) Mol. Cell. Proteomics , vol.9 , Issue.2 , pp. 197-208
    • Mathivanan, S.1    Lim, J.W.E.2    Tauro, B.J.3    Ji, H.4    Moritz, R.L.5    Simpson, R.J.6
  • 59
    • 53049107224 scopus 로고    scopus 로고
    • Proteomic analysis of exosomes from human neural stem cells by flow field-flow fractionation and nanoflow liquid chromatography-tandem mass spectrometry
    • Kang, D. J.; Oh, S.; Ahn, S. M.; Lee, B. H.; Moon, M. H. Proteomic analysis of exosomes from human neural stem cells by flow field-flow fractionation and nanoflow liquid chromatography-tandem mass spectrometry J. Proteome Res. 2008, 7 (8) 3475-3480
    • (2008) J. Proteome Res. , vol.7 , Issue.8 , pp. 3475-3480
    • Kang, D.J.1    Oh, S.2    Ahn, S.M.3    Lee, B.H.4    Moon, M.H.5
  • 61
    • 50949128891 scopus 로고    scopus 로고
    • Discrimination between exosomes and HIV-1: Purification of both vesicles from cell-free supernatants
    • Cantin, R.; Diou, J.; Belanger, D.; Tremblay, A. M.; Gilbert, C. Discrimination between exosomes and HIV-1: Purification of both vesicles from cell-free supernatants J. Immunol. Methods 2008, 338 (1-2) 21-30
    • (2008) J. Immunol. Methods , vol.338 , Issue.12 , pp. 21-30
    • Cantin, R.1    Diou, J.2    Belanger, D.3    Tremblay, A.M.4    Gilbert, C.5
  • 62
    • 33745026603 scopus 로고
    • The distribution and chemical composition of ultracentrifugally separated lipoproteins in human serum
    • Havel, R. J.; Eder, H. A.; Bragdon, J. H. The distribution and chemical composition of ultracentrifugally separated lipoproteins in human serum J. Clin. Invest. 1955, 34 (9) 1345-53
    • (1955) J. Clin. Invest. , vol.34 , Issue.9 , pp. 1345-1353
    • Havel, R.J.1    Eder, H.A.2    Bragdon, J.H.3
  • 63
    • 0030040562 scopus 로고    scopus 로고
    • The mechanism of human plasma phospholipid transfer protein-induced enlargement of high-density lipoprotein particles: Evidence for particle fusion
    • Lusa, S.; Jauhiainen, M.; Metso, J.; Somerharju, P.; Ehnholm, C. The mechanism of human plasma phospholipid transfer protein-induced enlargement of high-density lipoprotein particles: evidence for particle fusion Biochem. J. 1996, 313 (Pt 1) 275-82
    • (1996) Biochem. J. , vol.313 , Issue.PART 1 , pp. 275-282
    • Lusa, S.1    Jauhiainen, M.2    Metso, J.3    Somerharju, P.4    Ehnholm, C.5
  • 64
    • 78149409316 scopus 로고    scopus 로고
    • Export of microRNAs and microRNA-protective protein by mammalian cells
    • Wang, K.; Zhang, S.; Weber, J.; Baxter, D.; Galas, D. J. Export of microRNAs and microRNA-protective protein by mammalian cells Nucleic Acids Res. 2010, 38 (20) 7248-59
    • (2010) Nucleic Acids Res. , vol.38 , Issue.20 , pp. 7248-7259
    • Wang, K.1    Zhang, S.2    Weber, J.3    Baxter, D.4    Galas, D.J.5
  • 65
    • 77954956306 scopus 로고    scopus 로고
    • Lipidomics: Coming to grips with lipid diversity
    • Shevchenko, A.; Simons, K. Lipidomics: coming to grips with lipid diversity Nat. Rev. Mol. Cell Biol. 2010, 11 (8) 593-8
    • (2010) Nat. Rev. Mol. Cell Biol. , vol.11 , Issue.8 , pp. 593-598
    • Shevchenko, A.1    Simons, K.2
  • 67
    • 22144478635 scopus 로고    scopus 로고
    • The emerging field of lipidomics
    • Wenk, M. R. The emerging field of lipidomics Nat. Rev. Drug Discovery 2005, 4 (7) 594-610
    • (2005) Nat. Rev. Drug Discovery , vol.4 , Issue.7 , pp. 594-610
    • Wenk, M.R.1
  • 69
    • 0345599951 scopus 로고    scopus 로고
    • Lipid raft-associated protein sorting in exosomes
    • de Gassart, A.; Geminard, C.; Fevrier, B.; Raposo, G.; Vidal, M. Lipid raft-associated protein sorting in exosomes Blood 2003, 102 (13) 4336-4344
    • (2003) Blood , vol.102 , Issue.13 , pp. 4336-4344
    • De Gassart, A.1    Geminard, C.2    Fevrier, B.3    Raposo, G.4    Vidal, M.5
  • 70
    • 84922340030 scopus 로고    scopus 로고
    • The neutral sphingomyelinase pathway regulates packaging of the prion protein into exosomes
    • Guo, B. B.; Bellingham, S. A.; Hill, A. F. The neutral sphingomyelinase pathway regulates packaging of the prion protein into exosomes J. Biol. Chem. 2015, 290 (6) 3455-67
    • (2015) J. Biol. Chem. , vol.290 , Issue.6 , pp. 3455-3467
    • Guo, B.B.1    Bellingham, S.A.2    Hill, A.F.3
  • 72
    • 33845261493 scopus 로고
    • A rapid method of total lipid extraction and purification
    • Bligh, E. G.; Dyer, W. J. A rapid method of total lipid extraction and purification Can. J. Biochem. Physiol 1959, 37 (8) 911-7
    • (1959) Can. J. Biochem. Physiol , vol.37 , Issue.8 , pp. 911-917
    • Bligh, E.G.1    Dyer, W.J.2
  • 73
    • 80255140521 scopus 로고    scopus 로고
    • Lipid analysis and lipidomics by structurally selective ion mobility-mass spectrometry
    • Kliman, M.; May, J. C.; McLean, J. A. Lipid analysis and lipidomics by structurally selective ion mobility-mass spectrometry Biochim. Biophys. Acta 2011, 1811 (11) 935-45
    • (2011) Biochim. Biophys. Acta , vol.1811 , Issue.11 , pp. 935-945
    • Kliman, M.1    May, J.C.2    McLean, J.A.3
  • 74
  • 75
    • 67651162183 scopus 로고    scopus 로고
    • Global analysis of triacylglycerols including oxidized molecular species by reverse-phase high resolution LC/ESI-QTOF MS/MS
    • Ikeda, K.; Oike, Y.; Shimizu, T.; Taguchi, R. Global analysis of triacylglycerols including oxidized molecular species by reverse-phase high resolution LC/ESI-QTOF MS/MS J. Chromatogr. B: Anal. Technol. Biomed. Life Sci. 2009, 877 (25) 2639-47
    • (2009) J. Chromatogr. B: Anal. Technol. Biomed. Life Sci. , vol.877 , Issue.25 , pp. 2639-2647
    • Ikeda, K.1    Oike, Y.2    Shimizu, T.3    Taguchi, R.4
  • 76
    • 33645523236 scopus 로고    scopus 로고
    • LC-MS-based method for the qualitative and quantitative analysis of complex lipid mixtures
    • Sommer, U.; Herscovitz, H.; Welty, F. K.; Costello, C. E. LC-MS-based method for the qualitative and quantitative analysis of complex lipid mixtures J. Lipid Res. 2006, 47 (4) 804-814
    • (2006) J. Lipid Res. , vol.47 , Issue.4 , pp. 804-814
    • Sommer, U.1    Herscovitz, H.2    Welty, F.K.3    Costello, C.E.4
  • 77
    • 78650599232 scopus 로고    scopus 로고
    • Sphingolipid profiling of human plasma and FPLC-separated lipoprotein fractions by hydrophilic interaction chromatography tandem mass spectrometry
    • Scherer, M.; Bottcher, A.; Schmitz, G.; Liebisch, G. Sphingolipid profiling of human plasma and FPLC-separated lipoprotein fractions by hydrophilic interaction chromatography tandem mass spectrometry Biochim. Biophys. Acta 2011, 1811 (2) 68-75
    • (2011) Biochim. Biophys. Acta , vol.1811 , Issue.2 , pp. 68-75
    • Scherer, M.1    Bottcher, A.2    Schmitz, G.3    Liebisch, G.4
  • 78
  • 79
    • 84855412135 scopus 로고    scopus 로고
    • Profiling and characterizing skin ceramides using reversed-phase liquid chromatography-quadrupole time-of-flight mass spectrometry
    • tKindt, R.; Jorge, L.; Dumont, E.; Couturon, P.; David, F.; Sandra, P.; Sandra, K. Profiling and characterizing skin ceramides using reversed-phase liquid chromatography-quadrupole time-of-flight mass spectrometry Anal. Chem. 2012, 84 (1) 403-11
    • (2012) Anal. Chem. , vol.84 , Issue.1 , pp. 403-411
    • Tkindt, R.1    Jorge, L.2    Dumont, E.3    Couturon, P.4    David, F.5    Sandra, P.6    Sandra, K.7
  • 80
    • 84856328361 scopus 로고    scopus 로고
    • Shotgun lipidomics on a LTQ Orbitrap mass spectrometer by successive switching between acquisition polarity modes
    • Schuhmann, K.; Almeida, R.; Baumert, M.; Herzog, R.; Bornstein, S. R.; Shevchenko, A. Shotgun lipidomics on a LTQ Orbitrap mass spectrometer by successive switching between acquisition polarity modes J. Mass Spectrom. 2012, 47 (1) 96-104
    • (2012) J. Mass Spectrom. , vol.47 , Issue.1 , pp. 96-104
    • Schuhmann, K.1    Almeida, R.2    Baumert, M.3    Herzog, R.4    Bornstein, S.R.5    Shevchenko, A.6
  • 81
    • 84886018924 scopus 로고    scopus 로고
    • Functional group selective derivatization and gas-phase fragmentation reactions of plasmalogen glycerophospholipids
    • Fhaner, C. J.; Liu, S.; Zhou, X.; Reid, G. E. Functional group selective derivatization and gas-phase fragmentation reactions of plasmalogen glycerophospholipids Mass Spectrom. 2013, 10.5702/massspectrometry.S0015
    • (2013) Mass Spectrom.
    • Fhaner, C.J.1    Liu, S.2    Zhou, X.3    Reid, G.E.4
  • 82
    • 79952119926 scopus 로고    scopus 로고
    • Lipidomics profiling by high-resolution LC-MS and high-energy collisional dissociation fragmentation: Focus on characterization of mitochondrial cardiolipins and monolysocardiolipins
    • Bird, S. S.; Marur, V. R.; Sniatynski, M. J.; Greenberg, H. K.; Kristal, B. S. Lipidomics profiling by high-resolution LC-MS and high-energy collisional dissociation fragmentation: focus on characterization of mitochondrial cardiolipins and monolysocardiolipins Anal. Chem. 2011, 83 (3) 940-9
    • (2011) Anal. Chem. , vol.83 , Issue.3 , pp. 940-949
    • Bird, S.S.1    Marur, V.R.2    Sniatynski, M.J.3    Greenberg, H.K.4    Kristal, B.S.5
  • 83
    • 0024444617 scopus 로고
    • Asymmetric distribution of phospholipids in the membrane of vesicles released during in vitro maturation of guinea pig reticulocytes: Evidence precluding a role for "aminophospholipid translocase"
    • Vidal, M.; Sainte-Marie, J.; Philippot, J. R.; Bienvenue, A. Asymmetric distribution of phospholipids in the membrane of vesicles released during in vitro maturation of guinea pig reticulocytes: evidence precluding a role for "aminophospholipid translocase" J. Cell. Physiol. 1989, 140 (3) 455-62
    • (1989) J. Cell. Physiol. , vol.140 , Issue.3 , pp. 455-462
    • Vidal, M.1    Sainte-Marie, J.2    Philippot, J.R.3    Bienvenue, A.4
  • 84
    • 0013495952 scopus 로고    scopus 로고
    • Proteomic and biochemical analyses of human B cell-derived exosomes. Potential implications for their function and multivesicular body formation
    • Wubbolts, R.; Leckie, R. S.; Veenhuizen, P. T.; Schwarzmann, G.; Mobius, W.; Hoernschemeyer, J.; Slot, J. W.; Geuze, H. J.; Stoorvogel, W. Proteomic and biochemical analyses of human B cell-derived exosomes. Potential implications for their function and multivesicular body formation J. Biol. Chem. 2003, 278 (13) 10963-72
    • (2003) J. Biol. Chem. , vol.278 , Issue.13 , pp. 10963-10972
    • Wubbolts, R.1    Leckie, R.S.2    Veenhuizen, P.T.3    Schwarzmann, G.4    Mobius, W.5    Hoernschemeyer, J.6    Slot, J.W.7    Geuze, H.J.8    Stoorvogel, W.9
  • 87
    • 20344369564 scopus 로고    scopus 로고
    • Annexins: Linking Ca2+ signalling to membrane dynamics
    • Gerke, V.; Creutz, C. E.; Moss, S. E. Annexins: linking Ca2+ signalling to membrane dynamics Nat. Rev. Mol. Cell Biol. 2005, 6 (6) 449-61
    • (2005) Nat. Rev. Mol. Cell Biol. , vol.6 , Issue.6 , pp. 449-461
    • Gerke, V.1    Creutz, C.E.2    Moss, S.E.3
  • 88
    • 84916230879 scopus 로고    scopus 로고
    • Tumor and endothelial cell-derived microvesicles carry distinct CEACAMs and influence T-cell behavior
    • Muturi, H. T.; Dreesen, J. D.; Nilewski, E.; Jastrow, H.; Giebel, B.; Ergun, S.; Singer, B. B. Tumor and endothelial cell-derived microvesicles carry distinct CEACAMs and influence T-cell behavior PLoS One 2013, 8 (9) e74654
    • (2013) PLoS One , vol.8 , Issue.9 , pp. 74654
    • Muturi, H.T.1    Dreesen, J.D.2    Nilewski, E.3    Jastrow, H.4    Giebel, B.5    Ergun, S.6    Singer, B.B.7
  • 89
    • 84928057135 scopus 로고    scopus 로고
    • Exosomes in bodily fluids are a highly stable resource of disease biomarkers
    • Boukouris, S.; Mathivanan, S. Exosomes in bodily fluids are a highly stable resource of disease biomarkers Proteomics: Clin. Appl. 2015, 9 (3-4) 358-67
    • (2015) Proteomics: Clin. Appl. , vol.9 , Issue.34 , pp. 358-367
    • Boukouris, S.1    Mathivanan, S.2
  • 91
    • 67650151167 scopus 로고    scopus 로고
    • Bottom-Up Proteomics
    • Armirotti, A. Bottom-Up Proteomics Curr. Anal. Chem. 2009, 5 (2) 116-130
    • (2009) Curr. Anal. Chem. , vol.5 , Issue.2 , pp. 116-130
    • Armirotti, A.1
  • 92
    • 0033485648 scopus 로고    scopus 로고
    • Activated platelets release two types of membrane vesicles: Microvesicles by surface shedding and exosomes derived from exocytosis of multivesicular bodies and alpha-granules
    • Heijnen, H. F.; Schiel, A. E.; Fijnheer, R.; Geuze, H. J.; Sixma, J. J. Activated platelets release two types of membrane vesicles: microvesicles by surface shedding and exosomes derived from exocytosis of multivesicular bodies and alpha-granules Blood 1999, 94 (11) 3791-9
    • (1999) Blood , vol.94 , Issue.11 , pp. 3791-3799
    • Heijnen, H.F.1    Schiel, A.E.2    Fijnheer, R.3    Geuze, H.J.4    Sixma, J.J.5
  • 94
    • 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.; Pitto, M. Advances in membranous vesicle and exosome proteomics improving biological understanding and biomarker discovery Proteomics 2011, 11 (4) 709-720
    • (2011) Proteomics , vol.11 , Issue.4 , pp. 709-720
    • Raimondo, F.1    Morosi, L.2    Chinello, C.3    Magni, F.4    Pitto, M.5
  • 95
    • 10644236207 scopus 로고    scopus 로고
    • Proteomic analysis of melanoma-derived exosomes by two-dimensional polyacrylamide gel electrophoresis and mass spectrometry
    • Mears, R.; Craven, R. A.; Hanrahan, S.; Totty, N.; Upton, C.; Young, S. L.; Patel, P.; Selby, P. J.; Banks, R. E. Proteomic analysis of melanoma-derived exosomes by two-dimensional polyacrylamide gel electrophoresis and mass spectrometry Proteomics 2004, 4 (12) 4019-4031
    • (2004) Proteomics , vol.4 , Issue.12 , pp. 4019-4031
    • Mears, R.1    Craven, R.A.2    Hanrahan, S.3    Totty, N.4    Upton, C.5    Young, S.L.6    Patel, P.7    Selby, P.J.8    Banks, R.E.9
  • 98
    • 0026409298 scopus 로고
    • Blue native electrophoresis for isolation of membrane protein complexes in enzymatically active form
    • Schagger, H.; von Jagow, G. Blue native electrophoresis for isolation of membrane protein complexes in enzymatically active form Anal. Biochem. 1991, 199 (2) 223-31
    • (1991) Anal. Biochem. , vol.199 , Issue.2 , pp. 223-231
    • Schagger, H.1    Von Jagow, G.2
  • 99
    • 0028214450 scopus 로고
    • Analysis of molecular masses and oligomeric states of protein complexes by blue native electrophoresis and isolation of membrane protein complexes by two-dimensional native electrophoresis
    • Schagger, H.; Cramer, W. A.; von Jagow, G. Analysis of molecular masses and oligomeric states of protein complexes by blue native electrophoresis and isolation of membrane protein complexes by two-dimensional native electrophoresis Anal. Biochem. 1994, 217 (2) 220-30
    • (1994) Anal. Biochem. , vol.217 , Issue.2 , pp. 220-230
    • Schagger, H.1    Cramer, W.A.2    Von Jagow, G.3
  • 100
    • 84930601056 scopus 로고    scopus 로고
    • Two-Dimensional Non-Denaturing Gel Electrophoresis for Characterization of Proteins in Multi-Molecular Particles by Mass Spectrometry.
    • 1 st ed. A. R. Ivanov; A. V. Lazarev, Springer: New York
    • Serwer, P.; Weintraub, S. T. Two-Dimensional Non-Denaturing Gel Electrophoresis for Characterization of Proteins in Multi-Molecular Particles by Mass Spectrometry. In Sample Preparation in Biological Mass Spectrometry, 1 st ed.; A. R. Ivanov; A. V. Lazarev, Eds.; Springer: New York, 2011.
    • (2011) Sample Preparation in Biological Mass Spectrometry
    • Serwer, P.1    Weintraub, S.T.2
  • 101
    • 0036676445 scopus 로고    scopus 로고
    • Exosomes: Composition, Biogenesis, and Function
    • Thery, C.; Zitvogel, L.; Amigorena, S. Exosomes: Composition, Biogenesis, and Function Nat. Rev. Immunol. 2002, 2 (8) 569-79
    • (2002) Nat. Rev. Immunol. , vol.2 , Issue.8 , pp. 569-579
    • Thery, C.1    Zitvogel, L.2    Amigorena, S.3
  • 102
    • 74049141968 scopus 로고    scopus 로고
    • Two Rabs for exosome release
    • Pfeffer, S. R. Two Rabs for exosome release Nat. Cell Biol. 2010, 12 (1) 3-4
    • (2010) Nat. Cell Biol. , vol.12 , Issue.1 , pp. 3-4
    • Pfeffer, S.R.1
  • 104
  • 106
    • 0034254524 scopus 로고    scopus 로고
    • Follicular dendritic cells carry MHC class II-expressing microvesicles at their surface
    • Denzer, K.; van Eijk, M.; Kleijmeer, M. J.; Jakobson, E.; de Groot, C.; Geuze, H. J. Follicular dendritic cells carry MHC class II-expressing microvesicles at their surface J. Immunol. 2000, 165 (3) 1259-65
    • (2000) J. Immunol. , vol.165 , Issue.3 , pp. 1259-1265
    • Denzer, K.1    Van Eijk, M.2    Kleijmeer, M.J.3    Jakobson, E.4    De Groot, C.5    Geuze, H.J.6
  • 112
    • 79953078280 scopus 로고    scopus 로고
    • Morphologic and proteomic characterization of exosomes released by cultured extravillous trophoblast cells
    • Atay, S.; Gercel-Taylor, C.; Kesimer, M.; Taylor, D. D. Morphologic and proteomic characterization of exosomes released by cultured extravillous trophoblast cells Exp. Cell Res. 2011, 317 (8) 1192-1202
    • (2011) Exp. Cell Res. , vol.317 , Issue.8 , pp. 1192-1202
    • Atay, S.1    Gercel-Taylor, C.2    Kesimer, M.3    Taylor, D.D.4
  • 115
    • 84892547223 scopus 로고    scopus 로고
    • Comprehensive proteomic profiling of outer membrane vesicles from Campylobacter jejuni
    • Jang, K. S.; Sweredoski, M. J.; Graham, R. L.; Hess, S.; Clemons, W. M. Comprehensive proteomic profiling of outer membrane vesicles from Campylobacter jejuni J. Proteomics 2013, 98, 90-98
    • (2013) J. Proteomics , vol.98 , pp. 90-98
    • Jang, K.S.1    Sweredoski, M.J.2    Graham, R.L.3    Hess, S.4    Clemons, W.M.5
  • 116
    • 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.; Kislinger, T. 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 (4) 694-701
    • (2014) Biochem. Biophys. Res. Commun. , vol.445 , Issue.4 , pp. 694-701
    • Sinha, A.1    Ignatchenko, V.2    Ignatchenko, A.3    Mejia-Guerrero, S.4    Kislinger, T.5
  • 119
    • 67349266694 scopus 로고    scopus 로고
    • Universal sample preparation method for proteome analysis
    • Wisniewski, J. R.; Zougman, A.; Nagaraj, N.; Mann, M. Universal sample preparation method for proteome analysis Nat. Methods 2009, 6 (5) 359-U60
    • (2009) Nat. Methods , vol.6 , Issue.5 , pp. 359-U60
    • Wisniewski, J.R.1    Zougman, A.2    Nagaraj, N.3    Mann, M.4
  • 122
    • 36448962323 scopus 로고    scopus 로고
    • MudPIT: Multidimensional protein identification technology
    • Delahunty, C. M.; Yates, J. R., 3rd MudPIT: multidimensional protein identification technology Biotechniques 2007, 43 (5) 563-565
    • (2007) Biotechniques , vol.43 , Issue.5 , pp. 563-565
    • Delahunty, C.M.1    Yates, J.R.2
  • 123
    • 30344451098 scopus 로고    scopus 로고
    • Two-dimensional separation of peptides using RP-RP-HPLC system with different pH in first and second separation dimensions
    • Gilar, M.; Olivova, P.; Daly, A. E.; Gebler, J. C. Two-dimensional separation of peptides using RP-RP-HPLC system with different pH in first and second separation dimensions J. Sep. Sci. 2005, 28 (14) 1694-703
    • (2005) J. Sep. Sci. , vol.28 , Issue.14 , pp. 1694-1703
    • Gilar, M.1    Olivova, P.2    Daly, A.E.3    Gebler, J.C.4
  • 124
    • 65249120179 scopus 로고    scopus 로고
    • Proteomic Analysis of Human Parotid Gland Exosomes by Multidimensional Protein Identification Technology (MudPIT)
    • Gonzalez-Begne, M.; Lu, B. W.; Han, X. M.; Hagen, F. K.; Hand, A. R.; Melvin, J. E.; Yates, J. R. Proteomic Analysis of Human Parotid Gland Exosomes by Multidimensional Protein Identification Technology (MudPIT) J. Proteome Res. 2009, 8 (3) 1304-1314
    • (2009) J. Proteome Res. , vol.8 , Issue.3 , pp. 1304-1314
    • Gonzalez-Begne, M.1    Lu, B.W.2    Han, X.M.3    Hagen, F.K.4    Hand, A.R.5    Melvin, J.E.6    Yates, J.R.7
  • 125
    • 84862956256 scopus 로고    scopus 로고
    • Proteomic analysis of urine exosomes by multidimensional protein identification technology (MudPIT)
    • Wang, Z.; Hill, S.; Luther, J. M.; Hachey, D. L.; Schey, K. L. Proteomic analysis of urine exosomes by multidimensional protein identification technology (MudPIT) Proteomics 2012, 12 (2) 329-38
    • (2012) Proteomics , vol.12 , Issue.2 , pp. 329-338
    • Wang, Z.1    Hill, S.2    Luther, J.M.3    Hachey, D.L.4    Schey, K.L.5
  • 126
    • 82755198858 scopus 로고    scopus 로고
    • Electrostatic repulsion-hydrophilic interaction chromatography (ERLIC) versus strong cation exchange (SCX) for fractionation of iTRAQ-labeled peptides
    • Hao, P.; Qian, J.; Ren, Y.; Sze, S. K. Electrostatic repulsion-hydrophilic interaction chromatography (ERLIC) versus strong cation exchange (SCX) for fractionation of iTRAQ-labeled peptides J. Proteome Res. 2011, 10 (12) 5568-74
    • (2011) J. Proteome Res. , vol.10 , Issue.12 , pp. 5568-5574
    • Hao, P.1    Qian, J.2    Ren, Y.3    Sze, S.K.4
  • 127
    • 84892651699 scopus 로고    scopus 로고
    • Picoelectrospray Ionization Mass Spectrometry Using Narrow-Bore Chemically Etched Emitters
    • Marginean, I.; Tang, K.; Smith, R. D.; Kelly, R. T. Picoelectrospray Ionization Mass Spectrometry Using Narrow-Bore Chemically Etched Emitters J. Am. Soc. Mass Spectrom. 2013, 25 (1) 30-6
    • (2013) J. Am. Soc. Mass Spectrom. , vol.25 , Issue.1 , pp. 30-36
    • Marginean, I.1    Tang, K.2    Smith, R.D.3    Kelly, R.T.4
  • 128
    • 0142072517 scopus 로고    scopus 로고
    • Low-attomole electrospray ionization MS and MS/MS analysis of protein tryptic digests using 20 microm-i.d. Polystyrene-divinylbenzene monolithic capillary columns
    • Ivanov, A. R.; Zang, L.; Karger, B. L. Low-attomole electrospray ionization MS and MS/MS analysis of protein tryptic digests using 20 microm-i.d. polystyrene-divinylbenzene monolithic capillary columns Anal. Chem. 2003, 75 (20) 5306-16
    • (2003) Anal. Chem. , vol.75 , Issue.20 , pp. 5306-5316
    • Ivanov, A.R.1    Zang, L.2    Karger, B.L.3
  • 129
    • 84930426234 scopus 로고    scopus 로고
    • An Integrated Platform for Isolation, Processing and Mass Spectrometry-Based Proteomic Profiling of Rare Cells in Whole Blood
    • Li, S.; Plouffe, B. D.; Belov, A. M.; Ray, S.; Wang, X.; Murthy, S. K.; Karger, B. L.; Ivanov, A. R. An Integrated Platform for Isolation, Processing and Mass Spectrometry-Based Proteomic Profiling of Rare Cells in Whole Blood Mol. Cell Proteomics 2015, 10.1074/mcp.M114.045724
    • (2015) Mol. Cell Proteomics
    • Li, S.1    Plouffe, B.D.2    Belov, A.M.3    Ray, S.4    Wang, X.5    Murthy, S.K.6    Karger, B.L.7    Ivanov, A.R.8
  • 130
    • 66149091950 scopus 로고    scopus 로고
    • Improved electrospray ionization efficiency compensates for diminished chromatographic resolution and enables proteomics analysis of tyrosine signaling in embryonic stem cells
    • Ficarro, S. B.; Zhang, Y.; Lu, Y.; Moghimi, A. R.; Askenazi, M.; Hyatt, E.; Smith, E. D.; Boyer, L.; Schlaeger, T. M.; Luckey, C. J.; Marto, J. A. Improved electrospray ionization efficiency compensates for diminished chromatographic resolution and enables proteomics analysis of tyrosine signaling in embryonic stem cells Anal. Chem. 2009, 81 (9) 3440-7
    • (2009) Anal. Chem. , vol.81 , Issue.9 , pp. 3440-3447
    • Ficarro, S.B.1    Zhang, Y.2    Lu, Y.3    Moghimi, A.R.4    Askenazi, M.5    Hyatt, E.6    Smith, E.D.7    Boyer, L.8    Schlaeger, T.M.9    Luckey, C.J.10    Marto, J.A.11
  • 131
  • 133
    • 67049098565 scopus 로고    scopus 로고
    • Characterization of vesicles secreted from insulinoma NIT-1 cells
    • Lee, H. S.; Jeong, J.; Lee, K. J. Characterization of vesicles secreted from insulinoma NIT-1 cells J. Proteome Res. 2009, 8 (6) 2851-62
    • (2009) J. Proteome Res. , vol.8 , Issue.6 , pp. 2851-2862
    • Lee, H.S.1    Jeong, J.2    Lee, K.J.3
  • 136
    • 0037051906 scopus 로고    scopus 로고
    • Differential stability of tetraspanin-tetraspanin interactions: Role of palmitoylation
    • Charrin, S.; Manie, S.; Oualid, M.; Billard, M.; Boucheix, C.; Rubinstein, E. Differential stability of tetraspanin-tetraspanin interactions: role of palmitoylation FEBS Lett. 2002, 516 (1-3) 139-44
    • (2002) FEBS Lett. , vol.516 , Issue.13 , pp. 139-144
    • Charrin, S.1    Manie, S.2    Oualid, M.3    Billard, M.4    Boucheix, C.5    Rubinstein, E.6
  • 137
    • 11244304502 scopus 로고    scopus 로고
    • Palmitoylation supports assembly and function of integrin-tetraspanin complexes
    • Yang, X.; Kovalenko, O. V.; Tang, W.; Claas, C.; Stipp, C. S.; Hemler, M. E. Palmitoylation supports assembly and function of integrin-tetraspanin complexes J. Cell Biol. 2004, 167 (6) 1231-40
    • (2004) J. Cell Biol. , vol.167 , Issue.6 , pp. 1231-1240
    • Yang, X.1    Kovalenko, O.V.2    Tang, W.3    Claas, C.4    Stipp, C.S.5    Hemler, M.E.6
  • 138
    • 34250325547 scopus 로고    scopus 로고
    • Higher-order oligomerization targets plasma membrane proteins and HIV gag to exosomes
    • Fang, Y.; Wu, N.; Gan, X.; Yan, W. H.; Morrell, J. C.; Gould, S. J. Higher-order oligomerization targets plasma membrane proteins and HIV gag to exosomes PLoS Biology 2007, 5 (6) 1267-1283
    • (2007) PLoS Biology , vol.5 , Issue.6 , pp. 1267-1283
    • Fang, Y.1    Wu, N.2    Gan, X.3    Yan, W.H.4    Morrell, J.C.5    Gould, S.J.6
  • 139
    • 79954568598 scopus 로고    scopus 로고
    • Protein Targeting to Exosomes/Microvesicles by Plasma Membrane Anchors
    • Shen, B. Y.; Wu, N.; Yang, J. M.; Gould, S. J. Protein Targeting to Exosomes/Microvesicles by Plasma Membrane Anchors J. Biol. Chem. 2011, 286 (16) 14383-14395
    • (2011) J. Biol. Chem. , vol.286 , Issue.16 , pp. 14383-14395
    • Shen, B.Y.1    Wu, N.2    Yang, J.M.3    Gould, S.J.4
  • 142
    • 36749004371 scopus 로고    scopus 로고
    • Top-Down MS, a powerful complement to the high capabilities of proteolysis proteomics
    • McLafferty, F. W.; Breuker, K.; Jin, M.; Han, X.; Infusini, G.; Jiang, H.; Kong, X.; Begley, T. P. Top-Down MS, a powerful complement to the high capabilities of proteolysis proteomics FEBS J. 2007, 274 (24) 6256-68
    • (2007) FEBS J. , vol.274 , Issue.24 , pp. 6256-6268
    • McLafferty, F.W.1    Breuker, K.2    Jin, M.3    Han, X.4    Infusini, G.5    Jiang, H.6    Kong, X.7    Begley, T.P.8
  • 144
    • 56149087277 scopus 로고    scopus 로고
    • Native mass spectrometry: A bridge between interactomics and structural biology
    • Heck, A. J. Native mass spectrometry: a bridge between interactomics and structural biology Nat. Methods 2008, 5 (11) 927-33
    • (2008) Nat. Methods , vol.5 , Issue.11 , pp. 927-933
    • Heck, A.J.1
  • 145
    • 65249137629 scopus 로고    scopus 로고
    • Global and site-specific quantitative phosphoproteomics: Principles and applications
    • Macek, B.; Mann, M.; Olsen, J. V. Global and site-specific quantitative phosphoproteomics: principles and applications Annu. Rev. Pharmacol. Toxicol. 2009, 49, 199-221
    • (2009) Annu. Rev. Pharmacol. Toxicol. , vol.49 , pp. 199-221
    • Macek, B.1    Mann, M.2    Olsen, J.V.3
  • 147
    • 43049139913 scopus 로고    scopus 로고
    • Intercellular transfer of the oncogenic receptor EGFRvIII by microvesicles derived from tumour cells
    • Al-Nedawi, K.; Meehan, B.; Micallef, J.; Lhotak, V.; May, L.; Guha, A.; Rak, J. Intercellular transfer of the oncogenic receptor EGFRvIII by microvesicles derived from tumour cells Nat. Cell Biol. 2008, 10 (5) 619-24
    • (2008) Nat. Cell Biol. , vol.10 , Issue.5 , pp. 619-624
    • Al-Nedawi, K.1    Meehan, B.2    Micallef, J.3    Lhotak, V.4    May, L.5    Guha, A.6    Rak, J.7
  • 149
    • 0035958546 scopus 로고    scopus 로고
    • Ubiquitin-dependent sorting into the multivesicular body pathway requires the function of a conserved endosomal protein sorting complex, ESCRT-I
    • Katzmann, D. J.; Babst, M.; Emr, S. D. Ubiquitin-dependent sorting into the multivesicular body pathway requires the function of a conserved endosomal protein sorting complex, ESCRT-I Cell 2001, 106 (2) 145-55
    • (2001) Cell , vol.106 , Issue.2 , pp. 145-155
    • Katzmann, D.J.1    Babst, M.2    Emr, S.D.3
  • 156
    • 80054033461 scopus 로고    scopus 로고
    • A proteome-wide, quantitative survey of in vivo ubiquitylation sites reveals widespread regulatory roles
    • Wagner, S. A.; Beli, P.; Weinert, B. T.; Nielsen, M. L.; Cox, J.; Mann, M.; Choudhary, C. A proteome-wide, quantitative survey of in vivo ubiquitylation sites reveals widespread regulatory roles Mol. Cell. Proteomics 2011, 10 (10) M111.013284
    • (2011) Mol. Cell. Proteomics , vol.10 , Issue.10 , pp. 111013284
    • Wagner, S.A.1    Beli, P.2    Weinert, B.T.3    Nielsen, M.L.4    Cox, J.5    Mann, M.6    Choudhary, C.7
  • 157
    • 84915822550 scopus 로고    scopus 로고
    • Ubiquitinated proteins in exosomes secreted by myeloid-derived suppressor cells
    • Burke, M. C.; Oei, M. S.; Edwards, N. J.; Ostrand-Rosenberg, S.; Fenselau, C. Ubiquitinated proteins in exosomes secreted by myeloid-derived suppressor cells J. Proteome Res. 2014, 13 (12) 5965-72
    • (2014) J. Proteome Res. , vol.13 , Issue.12 , pp. 5965-5972
    • Burke, M.C.1    Oei, M.S.2    Edwards, N.J.3    Ostrand-Rosenberg, S.4    Fenselau, C.5
  • 162
    • 84883242484 scopus 로고    scopus 로고
    • The sweet and sour of serological glycoprotein tumor biomarker quantification
    • Kuzmanov, U.; Kosanam, H.; Diamandis, E. P. The sweet and sour of serological glycoprotein tumor biomarker quantification BMC Med. 2013, 11, 31
    • (2013) BMC Med. , vol.11 , pp. 31
    • Kuzmanov, U.1    Kosanam, H.2    Diamandis, E.P.3
  • 163
    • 84856637730 scopus 로고    scopus 로고
    • Differential glycomics of epithelial membrane glycoproteins from urinary exovesicles reveals shifts toward complex-type N-glycosylation in classical galactosemia
    • Staubach, S.; Schadewaldt, P.; Wendel, U.; Nohroudi, K.; Hanisch, F. G. Differential glycomics of epithelial membrane glycoproteins from urinary exovesicles reveals shifts toward complex-type N-glycosylation in classical galactosemia J. Proteome Res. 2012, 11 (2) 906-16
    • (2012) J. Proteome Res. , vol.11 , Issue.2 , pp. 906-916
    • Staubach, S.1    Schadewaldt, P.2    Wendel, U.3    Nohroudi, K.4    Hanisch, F.G.5
  • 168
    • 43149108354 scopus 로고    scopus 로고
    • Functional role of N-glycosylation from ADAM10 in processing, localization, and activity of the enzyme
    • Escrevente, C.; Morais, V. A.; Keller, S.; Soares, C. M.; Altevogt, P.; Costa, J. Functional role of N-glycosylation from ADAM10 in processing, localization, and activity of the enzyme Biochim. Biophys. Acta 2008, 1780 (6) 905-13
    • (2008) Biochim. Biophys. Acta , vol.1780 , Issue.6 , pp. 905-913
    • Escrevente, C.1    Morais, V.A.2    Keller, S.3    Soares, C.M.4    Altevogt, P.5    Costa, J.6
  • 169
    • 79953081976 scopus 로고    scopus 로고
    • Interaction and uptake of exosomes by ovarian cancer cells
    • Escrevente, C.; Keller, S.; Altevogt, P.; Costa, J. Interaction and uptake of exosomes by ovarian cancer cells BMC Cancer 2011, 11, 108
    • (2011) BMC Cancer , vol.11 , pp. 108
    • Escrevente, C.1    Keller, S.2    Altevogt, P.3    Costa, J.4
  • 170
    • 34247396011 scopus 로고    scopus 로고
    • A practical recipe for stable isotope labeling by amino acids in cell culture (SILAC)
    • Ong, S. E.; Mann, M. A practical recipe for stable isotope labeling by amino acids in cell culture (SILAC) Nat. Protoc. 2006, 1 (6) 2650-60
    • (2006) Nat. Protoc. , vol.1 , Issue.6 , pp. 2650-2660
    • Ong, S.E.1    Mann, M.2
  • 171
    • 84909580521 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. 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 (21-22) 2628-2629
    • (2014) Proteomics , vol.14 , Issue.2122 , pp. 2628-2629
    • Jeppesen, D.K.1
  • 173
    • 84899844127 scopus 로고    scopus 로고
    • Quantitative proteomics of extracellular vesicles released from human monocyte-derived macrophages upon β-glucan stimulation
    • Cypryk, W.; Ohman, T.; Eskelinen, E. L.; Matikainen, S.; Nyman, T. A. Quantitative proteomics of extracellular vesicles released from human monocyte-derived macrophages upon β-glucan stimulation J. Proteome Res. 2014, 13 (5) 2468-77
    • (2014) J. Proteome Res. , vol.13 , Issue.5 , pp. 2468-2477
    • Cypryk, W.1    Ohman, T.2    Eskelinen, E.L.3    Matikainen, S.4    Nyman, T.A.5
  • 174
    • 84875798802 scopus 로고    scopus 로고
    • Bovine milk proteome: Quantitative changes in normal milk exosomes, milk fat globule membranes, and whey proteomes resulting from Staphylococcus aureus mastitis
    • Reinhardt, T. A.; Sacco, R. E.; Nonnecke, B. J.; Lippolis, J. D. Bovine milk proteome: quantitative changes in normal milk exosomes, milk fat globule membranes, and whey proteomes resulting from Staphylococcus aureus mastitis J. Proteomics 2013, 82, 141-54
    • (2013) J. Proteomics , vol.82 , pp. 141-154
    • Reinhardt, T.A.1    Sacco, R.E.2    Nonnecke, B.J.3    Lippolis, J.D.4
  • 175
    • 84861678077 scopus 로고    scopus 로고
    • A multiplex quantitative proteomics strategy for protein biomarker studies in urinary exosomes
    • Raj, D. A.; Fiume, I.; Capasso, G.; Pocsfalvi, G. A multiplex quantitative proteomics strategy for protein biomarker studies in urinary exosomes Kidney Int. 2012, 81 (12) 1263-72
    • (2012) Kidney Int. , vol.81 , Issue.12 , pp. 1263-1272
    • Raj, D.A.1    Fiume, I.2    Capasso, G.3    Pocsfalvi, G.4
  • 176
    • 84919741824 scopus 로고    scopus 로고
    • Cavin-1/PTRF alters prostate cancer cell-derived extracellular vesicle content and internalization to attenuate extracellular vesicle-mediated osteoclastogenesis and osteoblast proliferation
    • Inder, K. L.; Ruelcke, J. E.; Petelin, L.; Moon, H.; Choi, E.; Rae, J.; Blumenthal, A.; Hutmacher, D.; Saunders, N. A.; Stow, J. L.; Parton, R. G.; Hill, M. M. Cavin-1/PTRF alters prostate cancer cell-derived extracellular vesicle content and internalization to attenuate extracellular vesicle-mediated osteoclastogenesis and osteoblast proliferation J. Extracell. Vesicles 2014, 10.3402/jev.v3.23784
    • (2014) J. Extracell. Vesicles
    • Inder, K.L.1    Ruelcke, J.E.2    Petelin, L.3    Moon, H.4    Choi, E.5    Rae, J.6    Blumenthal, A.7    Hutmacher, D.8    Saunders, N.A.9    Stow, J.L.10    Parton, R.G.11    Hill, M.M.12
  • 177
    • 84864817826 scopus 로고    scopus 로고
    • Characterization of membrane-shed microvesicles from cytokine-stimulated β-cells using proteomics strategies
    • Palmisano, G.; Jensen, S. S.; Le Bihan, M. C.; Laine, J.; McGuire, J. N.; Pociot, F.; Larsen, M. R. Characterization of membrane-shed microvesicles from cytokine-stimulated β-cells using proteomics strategies Mol. Cell Proteomics 2012, 11 (8) 230-43
    • (2012) Mol. Cell Proteomics , vol.11 , Issue.8 , pp. 230-243
    • Palmisano, G.1    Jensen, S.S.2    Le Bihan, M.C.3    Laine, J.4    McGuire, J.N.5    Pociot, F.6    Larsen, M.R.7
  • 178
    • 84885149616 scopus 로고    scopus 로고
    • Activin A suppresses osteoblast mineralization capacity by altering extracellular matrix (ECM) composition and impairing matrix vesicle (MV) production
    • Alves, R. D.; Eijken, M.; Bezstarosti, K.; Demmers, J. A.; van Leeuwen, J. P. Activin A suppresses osteoblast mineralization capacity by altering extracellular matrix (ECM) composition and impairing matrix vesicle (MV) production Mol. Cell Proteomics 2013, 12 (10) 2890-900
    • (2013) Mol. Cell Proteomics , vol.12 , Issue.10 , pp. 2890-2900
    • Alves, R.D.1    Eijken, M.2    Bezstarosti, K.3    Demmers, J.A.4    Van Leeuwen, J.P.5
  • 179
    • 85007427694 scopus 로고    scopus 로고
    • Quantitative proteomics of extracellular vesicles derived from human primary and metastatic colorectal cancer cells
    • Choi, D. S.; Choi, D. Y.; Hong, B. S.; Jang, S. C.; Kim, D. K.; Lee, J.; Kim, Y. K.; Kim, K. P.; Gho, Y. S. Quantitative proteomics of extracellular vesicles derived from human primary and metastatic colorectal cancer cells J. Extracell. Vesicles 2012, 10.3402/jev.v1i0.18704
    • (2012) J. Extracell. Vesicles
    • Choi, D.S.1    Choi, D.Y.2    Hong, B.S.3    Jang, S.C.4    Kim, D.K.5    Lee, J.6    Kim, Y.K.7    Kim, K.P.8    Gho, Y.S.9
  • 183
    • 84887818159 scopus 로고    scopus 로고
    • Proteomic analysis of urinary exosomes in cardiovascular and associated kidney diseases by two-dimensional electrophoresis and LC-MS/MS
    • Zubiri, I.; Vivanco, F.; Alvarez-Llamas, G. Proteomic analysis of urinary exosomes in cardiovascular and associated kidney diseases by two-dimensional electrophoresis and LC-MS/MS Methods Mol. Biol. 2013, 1000, 209-20
    • (2013) Methods Mol. Biol. , vol.1000 , pp. 209-220
    • Zubiri, I.1    Vivanco, F.2    Alvarez-Llamas, G.3


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.