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Volumn 13, Issue 6, 2013, Pages 992-1001

Mapping O-glycosylation of apolipoprotein C-III in MALDI-FT-ICR protein profiles

Author keywords

FT ICR MS; Glycomics; Glycoproteomics; High mass accuracy; High resolution proteomics; Protein profile

Indexed keywords

APOLIPOPROTEIN C3; GLYCAN; ISOPROTEIN; SIALIC ACID;

EID: 84874986856     PISSN: 16159853     EISSN: 16159861     Source Type: Journal    
DOI: 10.1002/pmic.201200293     Document Type: Article
Times cited : (25)

References (47)
  • 1
    • 79955462941 scopus 로고    scopus 로고
    • The first decade of MALDI protein profiling: a lesson in translational biomarker research
    • Albrethsen, J., The first decade of MALDI protein profiling: a lesson in translational biomarker research. J. Proteomics 2011, 74, 765-773.
    • (2011) J. Proteomics , vol.74 , pp. 765-773
    • Albrethsen, J.1
  • 2
    • 79953032990 scopus 로고    scopus 로고
    • Missing the mark
    • Buchen, L., Missing the mark. Nature 2011, 471, 428-432.
    • (2011) Nature , vol.471 , pp. 428-432
    • Buchen, L.1
  • 3
    • 77954512738 scopus 로고    scopus 로고
    • Proteomics retrenches
    • Mitchell, P., Proteomics retrenches. Nat. Biotech. 2010, 28, 665-670.
    • (2010) Nat. Biotech. , vol.28 , pp. 665-670
    • Mitchell, P.1
  • 5
    • 78149488962 scopus 로고    scopus 로고
    • Counting the proteins in plasma
    • Anderson, N. L., Counting the proteins in plasma. Clin. Chem. 2010, 56, 1775-1776.
    • (2010) Clin. Chem. , vol.56 , pp. 1775-1776
    • Anderson, N.L.1
  • 6
    • 77951623830 scopus 로고    scopus 로고
    • Integrating high-throughput technologies in the quest for effective biomarkers for ovarian cancer
    • Kulasingam, V., Pavlou, M. P., Diamandis, E. P., Integrating high-throughput technologies in the quest for effective biomarkers for ovarian cancer. Nat. Rev. Cancer 2010, 10, 371-378.
    • (2010) Nat. Rev. Cancer , vol.10 , pp. 371-378
    • Kulasingam, V.1    Pavlou, M.P.2    Diamandis, E.P.3
  • 7
    • 28044437780 scopus 로고    scopus 로고
    • Reliability of human serum protein profiles generated with C8 magnetic beads assisted MALDI-TOF mass spectrometry
    • de Noo, M. E., Tollenaar, R. A. E., Özalp, A., Kuppen, P. J. K. et al., Reliability of human serum protein profiles generated with C8 magnetic beads assisted MALDI-TOF mass spectrometry. Anal. Chem. 2005, 77, 7232-7241.
    • (2005) Anal. Chem. , vol.77 , pp. 7232-7241
    • de Noo, M.E.1    Tollenaar, R.A.E.2    Özalp, A.3    Kuppen, P.J.K.4
  • 9
    • 34248334942 scopus 로고    scopus 로고
    • Reproducibility in protein profiling by MALDI-TOF mass spectrometry
    • Albrethsen, J., Reproducibility in protein profiling by MALDI-TOF mass spectrometry. Clin. Chem. 2007, 53, 852-858.
    • (2007) Clin. Chem. , vol.53 , pp. 852-858
    • Albrethsen, J.1
  • 10
    • 63049101911 scopus 로고    scopus 로고
    • Serum protein profiling by solid phase extraction and mass spectrometry: a future diagnostics tool?
    • Callesen, A. K., Madsen, J. S., Vach, W., Kruse, T. A. et al., Serum protein profiling by solid phase extraction and mass spectrometry: a future diagnostics tool? Proteomics 2009, 9, 1428-1441.
    • (2009) Proteomics , vol.9 , pp. 1428-1441
    • Callesen, A.K.1    Madsen, J.S.2    Vach, W.3    Kruse, T.A.4
  • 11
    • 84857847927 scopus 로고    scopus 로고
    • Multiplex targeted proteomic assay for biomarker detection in plasma: a pancreatic cancer biomarker case study
    • Pan, S., Chen, R., Brand, R. E., Hawley, S. et al., Multiplex targeted proteomic assay for biomarker detection in plasma: a pancreatic cancer biomarker case study. J. Proteome Res. 2012, 11, 1937-1948.
    • (2012) J. Proteome Res. , vol.11 , pp. 1937-1948
    • Pan, S.1    Chen, R.2    Brand, R.E.3    Hawley, S.4
  • 12
    • 79960214321 scopus 로고    scopus 로고
    • A targeted proteomics-based pipeline for verification of biomarkers in plasma
    • Whiteaker, J. R., Lin, C., Kennedy, J., Hou, L. et al., A targeted proteomics-based pipeline for verification of biomarkers in plasma. Nat. Biotechnol. 2011, 29, 625-634.
    • (2011) Nat. Biotechnol. , vol.29 , pp. 625-634
    • Whiteaker, J.R.1    Lin, C.2    Kennedy, J.3    Hou, L.4
  • 13
    • 0029771981 scopus 로고    scopus 로고
    • Resolution and chemical formula identification of aromatic hydrocarbons and aromatic compounds containing sulfur, nitrogen, or oxygen in petroleum distillates and refinery streams
    • Guan, S., Marshall, A. G., Scheppele, S. E., Resolution and chemical formula identification of aromatic hydrocarbons and aromatic compounds containing sulfur, nitrogen, or oxygen in petroleum distillates and refinery streams. Anal. Chem. 1996, 68, 46-71.
    • (1996) Anal. Chem. , vol.68 , pp. 46-71
    • Guan, S.1    Marshall, A.G.2    Scheppele, S.E.3
  • 14
    • 75149144996 scopus 로고    scopus 로고
    • A dual pressure linear ion trap Orbitrap instrument with very high sequencing speed
    • Olsen, J. V., Schwartz, J. C., Griep-Raming, J., Nielsen, M. L. et al., A dual pressure linear ion trap Orbitrap instrument with very high sequencing speed. Mol. Cell. Proteomics 2009, 8, 2759-2769.
    • (2009) Mol. Cell. Proteomics , vol.8 , pp. 2759-2769
    • Olsen, J.V.1    Schwartz, J.C.2    Griep-Raming, J.3    Nielsen, M.L.4
  • 15
    • 30744476222 scopus 로고    scopus 로고
    • Performance of a linear ion trap-Orbitrap hybrid for peptide analysis
    • Yates, J. R., Cociorva, D., Liao, L., Zabrouskov, V., Performance of a linear ion trap-Orbitrap hybrid for peptide analysis. Anal. Chem. 2005, 78, 493-500.
    • (2005) Anal. Chem. , vol.78 , pp. 493-500
    • Yates, J.R.1    Cociorva, D.2    Liao, L.3    Zabrouskov, V.4
  • 16
    • 81555215504 scopus 로고    scopus 로고
    • Precision profiling and identification of human serum peptides using Fourier transform ion cyclotron resonance mass spectrometry
    • Nicolardi, S., Palmblad, M., Hensbergen, P. J., Tollenaar, R. A. E. M. et al., Precision profiling and identification of human serum peptides using Fourier transform ion cyclotron resonance mass spectrometry. Rapid Commun. Mass Spectrom. 2011, 25, 3457-3463.
    • (2011) Rapid Commun. Mass Spectrom. , vol.25 , pp. 3457-3463
    • Nicolardi, S.1    Palmblad, M.2    Hensbergen, P.J.3    Tollenaar, R.A.E.M.4
  • 17
    • 34547093160 scopus 로고    scopus 로고
    • Investigation of human protein variants and their frequency in the general population
    • Nedelkov, D., Phillips, D. A., Tubbs, K. A., Nelson, R. W., Investigation of human protein variants and their frequency in the general population. Mol. Cell. Proteomics 2007, 6, 1183-1187.
    • (2007) Mol. Cell. Proteomics , vol.6 , pp. 1183-1187
    • Nedelkov, D.1    Phillips, D.A.2    Tubbs, K.A.3    Nelson, R.W.4
  • 18
    • 77956548344 scopus 로고    scopus 로고
    • A well-characterised peak identification list of MALDI MS profile peaks for human blood serum
    • Tiss, A., Smith, C., Menon, U., Jacobs, I. et al., A well-characterised peak identification list of MALDI MS profile peaks for human blood serum. Proteomics 2010, 10, 3388-3392.
    • (2010) Proteomics , vol.10 , pp. 3388-3392
    • Tiss, A.1    Smith, C.2    Menon, U.3    Jacobs, I.4
  • 19
    • 33745442821 scopus 로고    scopus 로고
    • The MALDI-TOF mass spectrometric view of the plasma proteome and peptidome
    • Hortin, G. L., The MALDI-TOF mass spectrometric view of the plasma proteome and peptidome. Clin. Chem. 2006, 52, 1223-1237.
    • (2006) Clin. Chem. , vol.52 , pp. 1223-1237
    • Hortin, G.L.1
  • 20
    • 0033015655 scopus 로고    scopus 로고
    • Role of ApoCs in lipoprotein metabolism: functional differences between ApoC1, ApoC2, and ApoC3
    • Jong, M. C., Hofker, M. H., Havekes, L. M., Role of ApoCs in lipoprotein metabolism: functional differences between ApoC1, ApoC2, and ApoC3. Arterioscler. Thromb. Vasc. Biol. 1999, 19, 472-484.
    • (1999) Arterioscler. Thromb. Vasc. Biol. , vol.19 , pp. 472-484
    • Jong, M.C.1    Hofker, M.H.2    Havekes, L.M.3
  • 21
    • 34548396842 scopus 로고    scopus 로고
    • Lipoprotein metabolism in chronic renal insufficiency
    • Saland, J., Ginsberg, H. N., Lipoprotein metabolism in chronic renal insufficiency. Ped. Nephrol. 2007, 22, 1095-1112.
    • (2007) Ped. Nephrol. , vol.22 , pp. 1095-1112
    • Saland, J.1    Ginsberg, H.N.2
  • 22
    • 77957340934 scopus 로고    scopus 로고
    • Proteomic characterization of human plasma high density lipoprotein fractionated by gel filtration chromatography
    • Gordon, S. M., Deng, J., Lu, L. J., Davidson, W. S., Proteomic characterization of human plasma high density lipoprotein fractionated by gel filtration chromatography. J. Proteome Res. 2010, 9, 5239-5249.
    • (2010) J. Proteome Res. , vol.9 , pp. 5239-5249
    • Gordon, S.M.1    Deng, J.2    Lu, L.J.3    Davidson, W.S.4
  • 23
    • 0034983440 scopus 로고    scopus 로고
    • Apolipoproteins C-I and C-III as important modulators of lipoprotein metabolism
    • Shachter, N. S., Apolipoproteins C-I and C-III as important modulators of lipoprotein metabolism. Curr. Opin. Lipidol. 2001, 12, 297-304.
    • (2001) Curr. Opin. Lipidol. , vol.12 , pp. 297-304
    • Shachter, N.S.1
  • 24
    • 79956014824 scopus 로고    scopus 로고
    • Complexities of plasma apolipoprotein C-III metabolism
    • Sacks, F. M., Zheng, C., Cohn, J. S., Complexities of plasma apolipoprotein C-III metabolism. J. Lipid Res. 2011, 52, 1067-1070.
    • (2011) J. Lipid Res. , vol.52 , pp. 1067-1070
    • Sacks, F.M.1    Zheng, C.2    Cohn, J.S.3
  • 25
    • 33744809278 scopus 로고    scopus 로고
    • Apolipoprotein C-III isoforms: kinetics and relative implication in lipid metabolism
    • Mauger, J.-F., Couture, P., Bergeron, N., Lamarche, B., Apolipoprotein C-III isoforms: kinetics and relative implication in lipid metabolism. J. Lipid Res. 2006, 47, 1212-1218.
    • (2006) J. Lipid Res. , vol.47 , pp. 1212-1218
    • Mauger, J.-F.1    Couture, P.2    Bergeron, N.3    Lamarche, B.4
  • 26
    • 0021954138 scopus 로고
    • Modulation of lipoprotein-lipase activity by apolipoproteins - effect of apolipoprotein-C-III
    • Wang, C. S., McConathy, W. J., Kloer, H. U., Alaupovic, P., Modulation of lipoprotein-lipase activity by apolipoproteins - effect of apolipoprotein-C-III. J. Clin. Invest. 1985, 75, 384-390.
    • (1985) J. Clin. Invest. , vol.75 , pp. 384-390
    • Wang, C.S.1    McConathy, W.J.2    Kloer, H.U.3    Alaupovic, P.4
  • 27
    • 24344495315 scopus 로고    scopus 로고
    • A proteomic study of the apolipoproteins in LDL subclasses in patients with the metabolic syndrome and type 2 diabetes
    • Davidsson, P., Hulthe, J., Fagerberg, B., Olsson, B.-M. et al., A proteomic study of the apolipoproteins in LDL subclasses in patients with the metabolic syndrome and type 2 diabetes. J. Lipid Res. 2005, 46, 1999-2006.
    • (2005) J. Lipid Res. , vol.46 , pp. 1999-2006
    • Davidsson, P.1    Hulthe, J.2    Fagerberg, B.3    Olsson, B.-M.4
  • 28
    • 0034102739 scopus 로고    scopus 로고
    • Plasma kinetics of apoC-III and apoE in normolipidemic and hypertriglyceridemic subjects
    • Batal, R., Tremblay, M., Barrett, P. H. R., Jacques, H. et al., Plasma kinetics of apoC-III and apoE in normolipidemic and hypertriglyceridemic subjects. J. Lipid Res. 2000, 41, 706-718.
    • (2000) J. Lipid Res. , vol.41 , pp. 706-718
    • Batal, R.1    Tremblay, M.2    Barrett, P.H.R.3    Jacques, H.4
  • 29
    • 0038742058 scopus 로고    scopus 로고
    • Apolipoprotein C-III, a strong discriminant of coronary risk in men and a determinant of the metabolic syndrome in both genders
    • Onat, A., Hergenc, G., Sansoy, V., Fobker, M. et al., Apolipoprotein C-III, a strong discriminant of coronary risk in men and a determinant of the metabolic syndrome in both genders. Atherosclerosis 2003, 168, 81-89.
    • (2003) Atherosclerosis , vol.168 , pp. 81-89
    • Onat, A.1    Hergenc, G.2    Sansoy, V.3    Fobker, M.4
  • 30
    • 84870387945 scopus 로고    scopus 로고
    • Apolipoprotein C-III as a potential modulator of the association between HDL-cholesterol and incident coronary heart disease
    • Jensen, M. K., Rimm, E. B., Furtado, J. D., Sacks, F. M., Apolipoprotein C-III as a potential modulator of the association between HDL-cholesterol and incident coronary heart disease. J. Am. Heart Assoc. 2012, 1, 1-10.
    • (2012) J. Am. Heart Assoc. , vol.1 , pp. 1-10
    • Jensen, M.K.1    Rimm, E.B.2    Furtado, J.D.3    Sacks, F.M.4
  • 31
    • 79251558494 scopus 로고    scopus 로고
    • Serum apolipoproteins C-I and C-III are reduced in stomach cancer patients: results from MALDI-based peptidome and immuno-based clinical assays
    • Cohen, M., Yossef, R., Erez, T., Kugel, A. et al., Serum apolipoproteins C-I and C-III are reduced in stomach cancer patients: results from MALDI-based peptidome and immuno-based clinical assays. PLoS One 2011, 6, e14540.
    • (2011) PLoS One , vol.6
    • Cohen, M.1    Yossef, R.2    Erez, T.3    Kugel, A.4
  • 32
    • 0242331110 scopus 로고    scopus 로고
    • Apolipoprotein C-III isofocusing in the diagnosis of genetic defects in O-glycan biosynthesis
    • Wopereis, S., Grünewald, S., Morava, É., Penzien, J. M. et al., Apolipoprotein C-III isofocusing in the diagnosis of genetic defects in O-glycan biosynthesis. Clin. Chem. 2003, 49, 1839-1845.
    • (2003) Clin. Chem. , vol.49 , pp. 1839-1845
    • Wopereis, S.1    Grünewald, S.2    Morava, E.3    Penzien, J.M.4
  • 33
    • 33847354287 scopus 로고    scopus 로고
    • Transferrin and apolipoprotein C-III isofocusing are complementary in the diagnosis of N- and O-glycan biosynthesis defects
    • Wopereis, S., Grünewald, S., Huijben, K. M. L. C., Morava, É. et al., Transferrin and apolipoprotein C-III isofocusing are complementary in the diagnosis of N- and O-glycan biosynthesis defects. Clin. Chem. 2006, 53, 180-187.
    • (2006) Clin. Chem. , vol.53 , pp. 180-187
    • Wopereis, S.1    Grünewald, S.2    Huijben, K.M.L.C.3    Morava, E.4
  • 34
    • 0027207133 scopus 로고
    • Sequential ultracentrifugation micromethod for separation of serum-lipoproteins and assays of lipids, apolipoproteins, and lipoprotein particles
    • Brousseau, T., Clavey, V., Bard, J.-M., Fruchart, J.-C., Sequential ultracentrifugation micromethod for separation of serum-lipoproteins and assays of lipids, apolipoproteins, and lipoprotein particles. Clin. Chem. 1993, 39, 960-964.
    • (1993) Clin. Chem. , vol.39 , pp. 960-964
    • Brousseau, T.1    Clavey, V.2    Bard, J.-M.3    Fruchart, J.-C.4
  • 35
    • 0021591252 scopus 로고
    • Two-dimensional electrophoresis of human-plasma apolipoproteins
    • Sprecher, D. L., Taam, L., Brewer, H. B., Two-dimensional electrophoresis of human-plasma apolipoproteins. Clin. Chem. 1984, 30, 2084-2092.
    • (1984) Clin. Chem. , vol.30 , pp. 2084-2092
    • Sprecher, D.L.1    Taam, L.2    Brewer, H.B.3
  • 36
    • 0023183286 scopus 로고
    • Plasma apolipoproteins in tangier disease, as studied with two-dimensional electrophoresis
    • Visvikls, S., Dumon, M.-F., Steinmetz, J., Manabe, T. et al., Plasma apolipoproteins in tangier disease, as studied with two-dimensional electrophoresis. Clin. Chem. 1987, 33, 120-122.
    • (1987) Clin. Chem. , vol.33 , pp. 120-122
    • Visvikls, S.1    Dumon, M.-F.2    Steinmetz, J.3    Manabe, T.4
  • 37
    • 38149019274 scopus 로고    scopus 로고
    • Two-dimensional gel electrophoresis of apolipoprotein C-III and other serum glycoproteins for the combined screening of human congenital disorders of a and N-glycosylation
    • Bruneel, A., Morelle, W., Carre, Y., Habarou, F. et al., Two-dimensional gel electrophoresis of apolipoprotein C-III and other serum glycoproteins for the combined screening of human congenital disorders of a and N-glycosylation. Proteomics Clin. Appl. 2007, 1, 321-324.
    • (2007) Proteomics Clin. Appl. , vol.1 , pp. 321-324
    • Bruneel, A.1    Morelle, W.2    Carre, Y.3    Habarou, F.4
  • 38
    • 0023723480 scopus 로고
    • Analysis of human apolipoproteins-C by isoelectric-focusing in immobilized pH gradients
    • Haase, R., Menke-Möllers, I., Oette, K., Analysis of human apolipoproteins-C by isoelectric-focusing in immobilized pH gradients. Electrophoresis 1988, 9, 569-575.
    • (1988) Electrophoresis , vol.9 , pp. 569-575
    • Haase, R.1    Menke-Möllers, I.2    Oette, K.3
  • 39
    • 0019490864 scopus 로고
    • Separation of the apoprotein components of human very low-density lipoproteins by ion-paired, reversed-phase high-performance liquid-chromatography
    • Hancock, W. S., Bishop, C. A., Gotto, A. M., Harding, D. R. K. et al., Separation of the apoprotein components of human very low-density lipoproteins by ion-paired, reversed-phase high-performance liquid-chromatography. Lipids 1981, 16, 250-259.
    • (1981) Lipids , vol.16 , pp. 250-259
    • Hancock, W.S.1    Bishop, C.A.2    Gotto, A.M.3    Harding, D.R.K.4
  • 40
    • 77952366352 scopus 로고    scopus 로고
    • Quantitative analysis of intact apolipoproteins in human HDL by top-down differential mass spectrometry
    • Mazur, M. T., Cardasis, H. L., Spellman, D. S., Liaw, A. et al., Quantitative analysis of intact apolipoproteins in human HDL by top-down differential mass spectrometry. Proc. Nat. Acad. Sci. USA 2010, 107, 7728-7733.
    • (2010) Proc. Nat. Acad. Sci. USA , vol.107 , pp. 7728-7733
    • Mazur, M.T.1    Cardasis, H.L.2    Spellman, D.S.3    Liaw, A.4
  • 41
    • 27144541237 scopus 로고    scopus 로고
    • Plasma protein profiling: unique and stable features of individuals
    • Nelsestuen, G. L., Zhang, Y., Martinez, M. B., Key, N. S. et al., Plasma protein profiling: unique and stable features of individuals. Proteomics 2005, 5, 4012-4024.
    • (2005) Proteomics , vol.5 , pp. 4012-4024
    • Nelsestuen, G.L.1    Zhang, Y.2    Martinez, M.B.3    Key, N.S.4
  • 42
    • 38149101024 scopus 로고    scopus 로고
    • Automated-serum peptide profiling using novel magnetic C18 beads off-line coupled to MALDI-TOF-MS
    • Jimenez, C. R., El Filali, Z., Knol, J. C., Hoekman, K. et al., Automated-serum peptide profiling using novel magnetic C18 beads off-line coupled to MALDI-TOF-MS. Proteomics Clin. Appl. 2007, 1, 598-604.
    • (2007) Proteomics Clin. Appl. , vol.1 , pp. 598-604
    • Jimenez, C.R.1    El Filali, Z.2    Knol, J.C.3    Hoekman, K.4
  • 43
    • 84863201152 scopus 로고    scopus 로고
    • Mass spectrometry of apolipoprotein C-III, a simple analytical method for mucin-type O-glycosylation, and its application to an autosomal recessive cutis laxa type-2 (ARCL2) patient
    • Wada, Y., Kadoya, M., Okamoto, N., Mass spectrometry of apolipoprotein C-III, a simple analytical method for mucin-type O-glycosylation, and its application to an autosomal recessive cutis laxa type-2 (ARCL2) patient. Glycobiology 2012, 22, 1140-1144.
    • (2012) Glycobiology , vol.22 , pp. 1140-1144
    • Wada, Y.1    Kadoya, M.2    Okamoto, N.3
  • 44
    • 77955918712 scopus 로고    scopus 로고
    • Quality control based on isotopic distributions for high-throughput MALDI-TOF and MALDI-FTICR serum peptide profiling
    • Nicolardi, S., Palmblad, M., Dalebout, H., Bladergroen, M. et al., Quality control based on isotopic distributions for high-throughput MALDI-TOF and MALDI-FTICR serum peptide profiling. J. Am. Soc. Mass Spectrom. 2010, 21, 1515-1525.
    • (2010) J. Am. Soc. Mass Spectrom. , vol.21 , pp. 1515-1525
    • Nicolardi, S.1    Palmblad, M.2    Dalebout, H.3    Bladergroen, M.4
  • 45
    • 84870388699 scopus 로고    scopus 로고
    • Standardized and automated solid-phase extraction procedures for high-throughput proteomics of body fluids
    • Bladergroen, M. R., Derks, R. J. E., Nicolardi, S., de Visser, B. et al., Standardized and automated solid-phase extraction procedures for high-throughput proteomics of body fluids. J. Proteomics 2012, 77, 144-153.
    • (2012) J. Proteomics , vol.77 , pp. 144-153
    • Bladergroen, M.R.1    Derks, R.J.E.2    Nicolardi, S.3    de Visser, B.4
  • 46
    • 84871300591 scopus 로고    scopus 로고
    • Identification of human serum peptides in Fourier transform ion cyclotron resonance precision profiles
    • Nicolardi, S., Dalebout, H., Bladergroen, M. R., Mesker, W. E. et al., Identification of human serum peptides in Fourier transform ion cyclotron resonance precision profiles. Int. J. Proteomics 2012, 6, 804036.
    • (2012) Int. J. Proteomics , vol.6 , pp. 804036
    • Nicolardi, S.1    Dalebout, H.2    Bladergroen, M.R.3    Mesker, W.E.4
  • 47
    • 76149085857 scopus 로고    scopus 로고
    • Deelder, immunoglobulin G glycopeptide profiling by matrix-assisted laser desorption ionization fourier transform ion cyclotron resonance mass spectrometry
    • Selman, M. H. J., McDonnell, L. A., Palmblad, M., Ruhaak, L. R., Deelder, immunoglobulin G glycopeptide profiling by matrix-assisted laser desorption ionization fourier transform ion cyclotron resonance mass spectrometry. Anal. Chem. 2010, 82, 1073-1081.
    • (2010) Anal. Chem. , vol.82 , pp. 1073-1081
    • Selman, M.H.J.1    McDonnell, L.A.2    Palmblad, M.3    Ruhaak, L.R.4


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