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Volumn 6, Issue 9, 2007, Pages 1621-1637

Mascot file parsing and quantification (MFPaQ), a new software to parse, validate, and quantify proteomics data generated by ICAT and SILAC mass spectrometric analyses: Application to the proteomics study of membrane proteins from primary human endothelial cells

Author keywords

[No Author keywords available]

Indexed keywords

2',5' OLIGOADENYLATE SYNTHETASE; ENOYL COENZYME A HYDRATASE; FERRITIN; GAMMA INTERFERON; GUANINE NUCLEOTIDE BINDING PROTEIN; HETEROGENEOUS NUCLEAR RIBONUCLEOPROTEIN; HETEROGENEOUS NUCLEAR RIBONUCLEOPROTEIN F; HLA ANTIGEN CLASS 1; INTERCELLULAR ADHESION MOLECULE 1; ISOCITRATE DEHYDROGENASE (NADP); L SELECTIN; LOW DENSITY LIPOPROTEIN RECEPTOR; LYMPHOTOXIN; LYMPHOTOXIN BETA; LYSOSOME ASSOCIATED MEMBRANE PROTEIN 2; MAJOR HISTOCOMPATIBILITY ANTIGEN CLASS 1; MEMBRANE PROTEIN; NICOTINAMIDE METHYLTRANSFERASE; PHOSPHOLIPID SCRAMBLASE 1; PYRUVATE DEHYDROGENASE COMPLEX; PYRUVATE DEHYDROGENASE COMPLEX E2; RHO GUANINE NUCLEOTIDE BINDING PROTEIN; SCRAMBLASE; THROMBOSPONDIN 1; TRYPTOPHAN TRANSFER RNA LIGASE; TUMOR NECROSIS FACTOR ALPHA; TUMOR NECROSIS FACTOR RECEPTOR; TUMOR NECROSIS FACTOR RECEPTOR 5; UNCLASSIFIED DRUG; VASCULAR CELL ADHESION MOLECULE 1;

EID: 34848925460     PISSN: 15359476     EISSN: None     Source Type: Journal    
DOI: 10.1074/mcp.T600069-MCP200     Document Type: Article
Times cited : (81)

References (48)
  • 1
    • 33645704767 scopus 로고    scopus 로고
    • Quantitative proteomic comparison of rat mitochondria from muscle, heart, and liver
    • Forner, F., Foster, L. J., Campanaro, S., Valle, G., and Mann, M. (2006) Quantitative proteomic comparison of rat mitochondria from muscle, heart, and liver. Mol. Cell. Proteomics 5, 608-619
    • (2006) Mol. Cell. Proteomics , vol.5 , pp. 608-619
    • Forner, F.1    Foster, L.J.2    Campanaro, S.3    Valle, G.4    Mann, M.5
  • 2
    • 33646564676 scopus 로고    scopus 로고
    • Label-free protein quantification using LC-coupled ion trap or FT mass spectrometry: Reproducibility, linearity, and application with complex proteomes
    • Wang, G., Wu, W. W., Zeng, W., Chou, C. L., and Shen, R. F. (2006) Label-free protein quantification using LC-coupled ion trap or FT mass spectrometry: reproducibility, linearity, and application with complex proteomes. J. Proteome Res. 5, 1214-1223
    • (2006) J. Proteome Res , vol.5 , pp. 1214-1223
    • Wang, G.1    Wu, W.W.2    Zeng, W.3    Chou, C.L.4    Shen, R.F.5
  • 3
    • 17844394177 scopus 로고    scopus 로고
    • Statistical and computational methods for comparative proteomic profiling using liquid chromatography-tandem mass spectrometry
    • Listgarten, J., and Emili, A. (2005) Statistical and computational methods for comparative proteomic profiling using liquid chromatography-tandem mass spectrometry. Mol. Cell. Proteomics 4, 419-434
    • (2005) Mol. Cell. Proteomics , vol.4 , pp. 419-434
    • Listgarten, J.1    Emili, A.2
  • 4
    • 14344250874 scopus 로고    scopus 로고
    • Informatics platform for global proteomic profiling and biomarker discovery using liquid chromatography-tandem mass spectrometry
    • Radulovic, D., Jelveh, S., Ryu, S., Hamilton, T. G., Foss, E., Mao, Y., and Emili, A. (2004) Informatics platform for global proteomic profiling and biomarker discovery using liquid chromatography-tandem mass spectrometry. Mol. Cell. Proteornics 3, 984-997
    • (2004) Mol. Cell. Proteornics , vol.3 , pp. 984-997
    • Radulovic, D.1    Jelveh, S.2    Ryu, S.3    Hamilton, T.G.4    Foss, E.5    Mao, Y.6    Emili, A.7
  • 6
    • 0037326081 scopus 로고    scopus 로고
    • Mass spectrometric-based approaches in quantitative proteomics
    • Ong, S. E., Foster, L. J., and Mann, M. (2003) Mass spectrometric-based approaches in quantitative proteomics. Methods 29, 124-130
    • (2003) Methods , vol.29 , pp. 124-130
    • Ong, S.E.1    Foster, L.J.2    Mann, M.3
  • 7
    • 20444508181 scopus 로고    scopus 로고
    • Mass spectrometry-based quantitative proteomics
    • Heck, A. J., and Krijgsveld, J. (2004) Mass spectrometry-based quantitative proteomics. Expert Rev. Proteomics 1, 317-326
    • (2004) Expert Rev. Proteomics , vol.1 , pp. 317-326
    • Heck, A.J.1    Krijgsveld, J.2
  • 9
    • 0032875697 scopus 로고    scopus 로고
    • Quantitative analysis of complex protein mixtures using isotope-coded affinity tags
    • Gygi, S. P., Rist, B., Gerber, S. A., Turecek, F., Gelb, M. H., and Aebersold, R. (1999) Quantitative analysis of complex protein mixtures using isotope-coded affinity tags. Nat. Biotechnot. 17, 994-999
    • (1999) Nat. Biotechnot , vol.17 , pp. 994-999
    • Gygi, S.P.1    Rist, B.2    Gerber, S.A.3    Turecek, F.4    Gelb, M.H.5    Aebersold, R.6
  • 10
    • 0036583926 scopus 로고    scopus 로고
    • Stable isotope labeling by amino acids in cell culture, SILAC, as a simple and accurate approach to expression proteomics
    • Ong, S. E., Blagoev, B., Kratchmarova, I., Kristensen, D. B., Steen, H., Pandey, A., and Mann, M. (2002) Stable isotope labeling by amino acids in cell culture, SILAC, as a simple and accurate approach to expression proteomics. Mol. Cell. Proteomics 1, 376-386
    • (2002) Mol. Cell. Proteomics , vol.1 , pp. 376-386
    • Ong, S.E.1    Blagoev, B.2    Kratchmarova, I.3    Kristensen, D.B.4    Steen, H.5    Pandey, A.6    Mann, M.7
  • 11
    • 12944269065 scopus 로고
    • Rapid identification of proteins by peptide-mass fingerprinting
    • Pappin, D. J., Hojrup, P., and Bleasby, A. J. (1993) Rapid identification of proteins by peptide-mass fingerprinting. Curr. Biol. 3, 327-332
    • (1993) Curr. Biol , vol.3 , pp. 327-332
    • Pappin, D.J.1    Hojrup, P.2    Bleasby, A.J.3
  • 12
    • 0000685292 scopus 로고    scopus 로고
    • Protein identification by SEQUEST
    • III (, James, P, ed) p, Springer-Verlag, New York
    • Tabb, D. L., Eng, J. K., and Yates, J. R., III (2000) Protein identification by SEQUEST, in Proteome Research: Mass Spectrometry (James, P., ed) p. 125-142, Springer-Verlag, New York
    • (2000) Proteome Research: Mass Spectrometry , pp. 125-142
    • Tabb, D.L.1    Eng, J.K.2    Yates, J.R.3
  • 13
    • 24044508863 scopus 로고    scopus 로고
    • New data base-independent, sequence tag-based scoring of peptide MS/MS data validates Mowse scores, recovers below threshold data, singles out modified peptices, and assesses the quality of MS/MS techniques
    • Savitski, M. M., Nielsen, M. L., and Zubarev, R. A. (2005) New data base-independent, sequence tag-based scoring of peptide MS/MS data validates Mowse scores, recovers below threshold data, singles out modified peptices, and assesses the quality of MS/MS techniques. Mol. Cell. Proteomics 4, 1180-1188
    • (2005) Mol. Cell. Proteomics , vol.4 , pp. 1180-1188
    • Savitski, M.M.1    Nielsen, M.L.2    Zubarev, R.A.3
  • 14
    • 0042338362 scopus 로고    scopus 로고
    • A statistical model for identifying proteins by tandem mass spectrometry
    • Nesvizhskil, A. I., Keller, A., Kolker, E., and Aebersold, R. (2003) A statistical model for identifying proteins by tandem mass spectrometry. Anal. Chem. 75, 4646-4658
    • (2003) Anal. Chem , vol.75 , pp. 4646-4658
    • Nesvizhskil, A.I.1    Keller, A.2    Kolker, E.3    Aebersold, R.4
  • 15
    • 0037108887 scopus 로고    scopus 로고
    • Empirical statistical model to estimate the accuracy of peptide identifications made by MS/MS and database search
    • Keller, A., Nesvizhskii, A. I., Kolker, E., and Aebersold, R. (2002) Empirical statistical model to estimate the accuracy of peptide identifications made by MS/MS and database search. Anal. Chem. 74, 5383-5392
    • (2002) Anal. Chem , vol.74 , pp. 5383-5392
    • Keller, A.1    Nesvizhskii, A.I.2    Kolker, E.3    Aebersold, R.4
  • 16
    • 33746408762 scopus 로고    scopus 로고
    • von Haller, P. D., Yi, E., Donohoe, S., Vaughn, K., Keller, A., Nesvizhskii, A. I., Eng, J., Li, X. J., Goodlett, D. R., Aebersold, R., and Watts, J. D. (2003) The application of new software tools to quantitative protein profiling via isotope-coded affinity tag (ICAT) and tandem mass spectrometry: II. Evaluation of tandem mass spectrometry methodologies for large-scale protein analysis, and the application of statistical tools for data analysis and interpretation. Mol. Cell. Proteomics 2, 428-442
    • von Haller, P. D., Yi, E., Donohoe, S., Vaughn, K., Keller, A., Nesvizhskii, A. I., Eng, J., Li, X. J., Goodlett, D. R., Aebersold, R., and Watts, J. D. (2003) The application of new software tools to quantitative protein profiling via isotope-coded affinity tag (ICAT) and tandem mass spectrometry: II. Evaluation of tandem mass spectrometry methodologies for large-scale protein analysis, and the application of statistical tools for data analysis and interpretation. Mol. Cell. Proteomics 2, 428-442
  • 17
    • 0041358793 scopus 로고    scopus 로고
    • OLAV: Towards high-throughput tandem mass spectrometry data identification
    • Colinge, J., Masselot, A., Giron, M., Dessingy, T., and Magnin, J. (2003) OLAV: towards high-throughput tandem mass spectrometry data identification. Proteomics 3, 1454-1463
    • (2003) Proteomics , vol.3 , pp. 1454-1463
    • Colinge, J.1    Masselot, A.2    Giron, M.3    Dessingy, T.4    Magnin, J.5
  • 18
    • 0346874342 scopus 로고    scopus 로고
    • Proteomic characterization of the human centrosome by protein correlation profiling
    • Andersen, J. S., Wilkinson, C. J., Mayor, T., Mortensen, P., Nigg, E. A., and Mann, M. (2003) Proteomic characterization of the human centrosome by protein correlation profiling, Nature 426, 570-574
    • (2003) Nature , vol.426 , pp. 570-574
    • Andersen, J.S.1    Wilkinson, C.J.2    Mayor, T.3    Mortensen, P.4    Nigg, E.A.5    Mann, M.6
  • 22
    • 2542485456 scopus 로고    scopus 로고
    • Plasticity of enclothelial cells: Rapid dedifferentiation of freshly isolated high endothelial venule enclothelial cells outside the lymphoid tissue microenvironment
    • Lacorre, D. A., Baekkevold, E. S., Garrido, I., Brandtzaeg, P., Haraldsen, G., Amalric, F., and Girard, J. P. (2004) Plasticity of enclothelial cells: rapid dedifferentiation of freshly isolated high endothelial venule enclothelial cells outside the lymphoid tissue microenvironment. Blood 103, 4164-4172
    • (2004) Blood , vol.103 , pp. 4164-4172
    • Lacorre, D.A.1    Baekkevold, E.S.2    Garrido, I.3    Brandtzaeg, P.4    Haraldsen, G.5    Amalric, F.6    Girard, J.P.7
  • 24
    • 33749367026 scopus 로고    scopus 로고
    • Protein profiling of sickle cell versus control RBC core membrane skeletons by ICAT technology and tandem mass spectrometry
    • Chou, J., Chouchary, P. K., and Goodman, S. R. (2006) Protein profiling of sickle cell versus control RBC core membrane skeletons by ICAT technology and tandem mass spectrometry. Cell. Mol. Biol. Lett. 11, 326-337
    • (2006) Cell. Mol. Biol. Lett , vol.11 , pp. 326-337
    • Chou, J.1    Chouchary, P.K.2    Goodman, S.R.3
  • 25
    • 17044432706 scopus 로고    scopus 로고
    • Large-scale evaluation of quantitative reproducibility and proteome coverage using acid cleavable isotope coded affinity tag mass spectrometry for proteomic profiling
    • Molloy, M. P., Donohoe, S., Brzezinski, E. E., Kilby, G. W., Stevenson, T. I., Baker, J. D., Goodlett, D. R., and Gage, D. A. (2005) Large-scale evaluation of quantitative reproducibility and proteome coverage using acid cleavable isotope coded affinity tag mass spectrometry for proteomic profiling. Proteomics 5, 1204-1208
    • (2005) Proteomics , vol.5 , pp. 1204-1208
    • Molloy, M.P.1    Donohoe, S.2    Brzezinski, E.E.3    Kilby, G.W.4    Stevenson, T.I.5    Baker, J.D.6    Goodlett, D.R.7    Gage, D.A.8
  • 26
    • 0029153736 scopus 로고
    • High endothelial venules (HEVs): Specialized endothelium for lymphocyte migration
    • Girard, J. P., and Springer, T. A. (1995) High endothelial venules (HEVs): specialized endothelium for lymphocyte migration. Immunol, Today 16, 449-457
    • (1995) Immunol, Today , vol.16 , pp. 449-457
    • Girard, J.P.1    Springer, T.A.2
  • 27
    • 0027982876 scopus 로고
    • Traffic signals for lymphocyte recirculation and leukocyte emigration: The multistep paradigm
    • Springer, T. A. (1994) Traffic signals for lymphocyte recirculation and leukocyte emigration: the multistep paradigm. Cell 76, 301-314
    • (1994) Cell , vol.76 , pp. 301-314
    • Springer, T.A.1
  • 28
    • 0024296564 scopus 로고
    • Primary structure of ICAM-1 demonstrates interaction between members of the immunoglobulin and integrin supergene families
    • Staunton, D. E., Marlin, S. D., Stratowa, C., Dustin, M. L., and Springer, T. A. (1988) Primary structure of ICAM-1 demonstrates interaction between members of the immunoglobulin and integrin supergene families. Cell 52, 925-933
    • (1988) Cell , vol.52 , pp. 925-933
    • Staunton, D.E.1    Marlin, S.D.2    Stratowa, C.3    Dustin, M.L.4    Springer, T.A.5
  • 29
    • 0027490115 scopus 로고
    • The expression of the adhesion molecules ICAM-1, VCAM-1, PECAM, and E-selectin in human atherosclerosis
    • Davies, M. J., Gordon, J. L., Gearing, A. J., Pigott, R., Woolf, N., Katz, D., and Kyriakopoulos, A. (1993) The expression of the adhesion molecules ICAM-1, VCAM-1, PECAM, and E-selectin in human atherosclerosis. J. Pathol. 171, 223-229
    • (1993) J. Pathol , vol.171 , pp. 223-229
    • Davies, M.J.1    Gordon, J.L.2    Gearing, A.J.3    Pigott, R.4    Woolf, N.5    Katz, D.6    Kyriakopoulos, A.7
  • 30
    • 0025161990 scopus 로고
    • VCAM-1 on activated endothelium interacts with the leukocyte integrin VLA-4 at a site distinct from the VLA-4/fibronectin binding site
    • Elices, M. J., Osborn, L., Takada, Y., Crouse, C., Luhawskyj, S., Homler, M. E., and Lobb, R. R. (1990) VCAM-1 on activated endothelium interacts with the leukocyte integrin VLA-4 at a site distinct from the VLA-4/fibronectin binding site. Cell 60, 577-584
    • (1990) Cell , vol.60 , pp. 577-584
    • Elices, M.J.1    Osborn, L.2    Takada, Y.3    Crouse, C.4    Luhawskyj, S.5    Homler, M.E.6    Lobb, R.R.7
  • 31
    • 0024601050 scopus 로고
    • Endothelial leukocyte adhesion molecule 1: An inducible receptor for neutrophils related to complement regulatory proteins and lectins
    • Bevilacqua, M. P., Stengelin, S., Gimbrone, M. A., Jr., and Seed, B. (1989) Endothelial leukocyte adhesion molecule 1: an inducible receptor for neutrophils related to complement regulatory proteins and lectins. Science 243, 1160-1165
    • (1989) Science , vol.243 , pp. 1160-1165
    • Bevilacqua, M.P.1    Stengelin, S.2    Gimbrone Jr., M.A.3    Seed, B.4
  • 32
    • 0027407109 scopus 로고
    • Endothelial-leukocyte adhesion molecules
    • Bevilacqua, M. P. (1993) Endothelial-leukocyte adhesion molecules. Annu. Rev. Immunol. 11, 767-804
    • (1993) Annu. Rev. Immunol , vol.11 , pp. 767-804
    • Bevilacqua, M.P.1
  • 33
    • 33646472414 scopus 로고    scopus 로고
    • Activated leukocyte cell adhesion molecule is a component of the endothelial junction involved in transendothelial monocyte migration
    • Maseclunskas, A., King, J. A., Tan, F., Cochran, R., Stevens, T., Sviridov, D., and Ofori-Acquah, S. F (2006) Activated leukocyte cell adhesion molecule is a component of the endothelial junction involved in transendothelial monocyte migration. FEBS Lett. 580, 2637-2645
    • (2006) FEBS Lett , vol.580 , pp. 2637-2645
    • Maseclunskas, A.1    King, J.A.2    Tan, F.3    Cochran, R.4    Stevens, T.5    Sviridov, D.6    Ofori-Acquah, S.F.7
  • 34
    • 28444482348 scopus 로고    scopus 로고
    • Human guanylate binding protein-1 (hGBP-1) characterizes and establishes a non-angiogenic endothelial cell activation phenotype in inflammatory diseases
    • Naschberger, E., Bauer, M., and Sturzl, M. (2005) Human guanylate binding protein-1 (hGBP-1) characterizes and establishes a non-angiogenic endothelial cell activation phenotype in inflammatory diseases. Adv. Enzyme Regul. 45, 215-227
    • (2005) Adv. Enzyme Regul , vol.45 , pp. 215-227
    • Naschberger, E.1    Bauer, M.2    Sturzl, M.3
  • 35
    • 0022869015 scopus 로고
    • Mechanism of interferon action. Expression of vesicular stomatitis virus G gene in transfected COS cells is inhibited by interferon at the level of protein synthesis
    • Sahni, G., and Samuel, C. E. (1986) Mechanism of interferon action. Expression of vesicular stomatitis virus G gene in transfected COS cells is inhibited by interferon at the level of protein synthesis. J. Biol. Chem. 261, 16764-16768
    • (1986) J. Biol. Chem , vol.261 , pp. 16764-16768
    • Sahni, G.1    Samuel, C.E.2
  • 36
    • 0017176867 scopus 로고
    • Interferon-mediated protein kinase and low-molecular-weight inhibitor of protein synthesis
    • Roberts, W. K., Hovanessian, A., Brown, R. E., Clemens, M. J., and Kerr, I. M. (1976) Interferon-mediated protein kinase and low-molecular-weight inhibitor of protein synthesis. Nature 264, 477-480
    • (1976) Nature , vol.264 , pp. 477-480
    • Roberts, W.K.1    Hovanessian, A.2    Brown, R.E.3    Clemens, M.J.4    Kerr, I.M.5
  • 37
    • 0032951754 scopus 로고    scopus 로고
    • The human 2′,5′-oligoadeny-late synthetase family: Interferon-induced proteins with unique enzymatic properties
    • Rebouillat, D., and Hovanessian, A. G. (1999) The human 2′,5′-oligoadeny-late synthetase family: interferon-induced proteins with unique enzymatic properties. J. Interferon Cytokine Res. 19, 295-308
    • (1999) J. Interferon Cytokine Res , vol.19 , pp. 295-308
    • Rebouillat, D.1    Hovanessian, A.G.2
  • 38
    • 0026343599 scopus 로고
    • Interferon induces tryptophanyl-tRNA synthetase expression in human fibroblasts
    • Rubin, B. Y., Anderson, S. L., Xing, L., Powell, R. J., and Tate, W. P. (1991) Interferon induces tryptophanyl-tRNA synthetase expression in human fibroblasts. J. Biol. Chem. 266, 24245-24248
    • (1991) J. Biol. Chem , vol.266 , pp. 24245-24248
    • Rubin, B.Y.1    Anderson, S.L.2    Xing, L.3    Powell, R.J.4    Tate, W.P.5
  • 39
    • 0032417696 scopus 로고    scopus 로고
    • Identification of genes differentially regulated by interferon a, α, β or γ using olgonucleotide arrays
    • Der, S. D., Zhou, A., Williams, B. R., and Silverman, R. H. (1998) Identification of genes differentially regulated by interferon a, α, β or γ using olgonucleotide arrays. Proc. Nati. Acad, Sci. U. S. A. 95, 15623-15628
    • (1998) Proc. Nati. Acad, Sci. U. S. A , vol.95 , pp. 15623-15628
    • Der, S.D.1    Zhou, A.2    Williams, B.R.3    Silverman, R.H.4
  • 41
    • 0035895081 scopus 로고    scopus 로고
    • Identification of CD146 as a component of the enclothelial junction involved in the control of cell-cell cohesion
    • Bardin, N., Anfosso, F., Masse, J. M., Cramer, E., Sabatier, F., Le Bivic, A., Sampol, J., and Dignat-George, F. (2001) Identification of CD146 as a component of the enclothelial junction involved in the control of cell-cell cohesion. Blood 98, 3677-3684
    • (2001) Blood , vol.98 , pp. 3677-3684
    • Bardin, N.1    Anfosso, F.2    Masse, J.M.3    Cramer, E.4    Sabatier, F.5    Le Bivic, A.6    Sampol, J.7    Dignat-George, F.8
  • 42
    • 0030913615 scopus 로고    scopus 로고
    • Expression of MCAM/MUC18 by human melanoma cells leads to increased tumor growth and metastasis
    • Xie, S., Luca, M., Huang, S., Gutman, M., Reich, R., Johnson, J. P., and Bar-Eli, M. (1997) Expression of MCAM/MUC18 by human melanoma cells leads to increased tumor growth and metastasis. Cancer Res. 57, 2295-2303
    • (1997) Cancer Res , vol.57 , pp. 2295-2303
    • Xie, S.1    Luca, M.2    Huang, S.3    Gutman, M.4    Reich, R.5    Johnson, J.P.6    Bar-Eli, M.7
  • 44
    • 33746432742 scopus 로고    scopus 로고
    • von Haller, P. D., Yi, E., Donohoe, S., Vaughn, K., Keller, A., Nesvizhskii, A. I., Eng, J., Li, X. J., Goodlett, D. R., Aebersold, R, and Watts, J. D. (2003) The application of new software tools to quantitative protein profiling via isotope-coded affinity tag (ICAT) and tandem mass spectrometry: 1. Statistically annotated datasets for peptide sequences and proteins identified via the application of ICAT and tandem mass spectrometry to proteins copurifying with T cell lipid rafts. Mol. Cell. Proteomics 2, 426-427
    • von Haller, P. D., Yi, E., Donohoe, S., Vaughn, K., Keller, A., Nesvizhskii, A. I., Eng, J., Li, X. J., Goodlett, D. R., Aebersold, R, and Watts, J. D. (2003) The application of new software tools to quantitative protein profiling via isotope-coded affinity tag (ICAT) and tandem mass spectrometry: 1. Statistically annotated datasets for peptide sequences and proteins identified via the application of ICAT and tandem mass spectrometry to proteins copurifying with T cell lipid rafts. Mol. Cell. Proteomics 2, 426-427
  • 46
    • 3543023287 scopus 로고    scopus 로고
    • Direct proteomic mapping of the lung microvascular endothelial cell surface in vivo and in cell culture
    • Durr, E., Yu, J., Krasinska, K. M., Carver, L. A., Yates, J. R., Testa, J. E., Oh, P., and Schnitzer, J. E. (2004) Direct proteomic mapping of the lung microvascular endothelial cell surface in vivo and in cell culture. Nat. Biotechnol. 22, 985-992
    • (2004) Nat. Biotechnol , vol.22 , pp. 985-992
    • Durr, E.1    Yu, J.2    Krasinska, K.M.3    Carver, L.A.4    Yates, J.R.5    Testa, J.E.6    Oh, P.7    Schnitzer, J.E.8
  • 47
    • 0015822275 scopus 로고
    • Culture of human enclothelial cells derived from umbilical veins. Identification by morphologic and immunologic criteria
    • Jaffe, E. A., Nachman, R. L., Becker, C. G., and Minick, C. R. (1973) Culture of human enclothelial cells derived from umbilical veins. Identification by morphologic and immunologic criteria. J. Clin. Investig. 52, 2745-2756
    • (1973) J. Clin. Investig , vol.52 , pp. 2745-2756
    • Jaffe, E.A.1    Nachman, R.L.2    Becker, C.G.3    Minick, C.R.4


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