메뉴 건너뛰기




Volumn 8, Issue 18, 2008, Pages 3822-3832

Multiplexed glycoproteomic analysis of glycosylation disorders by sequential yolk immunoglobulins immunoseparation and MALDI-TOF MS

Author keywords

Congenital disorders of glycosylation; Galactosemia; Glycosylation; Hereditary fructose intolerance; Immunoseparation

Indexed keywords

ALPHA 1 ANTITRYPSIN; FRUCTOSE; GLYCOPEPTIDASE; GLYCOPROTEIN; IMMUNOGLOBULIN Y; TRANSFERRIN;

EID: 53549110284     PISSN: 16159853     EISSN: 16159861     Source Type: Journal    
DOI: 10.1002/pmic.200700496     Document Type: Article
Times cited : (44)

References (47)
  • 1
    • 25844442417 scopus 로고    scopus 로고
    • Genetic defects in the human glycome
    • Freeze, H. H., Aebi, M., Genetic defects in the human glycome. Curr. Opin. Struct. Biol. 2005, 15, 490-498.
    • (2005) Curr. Opin. Struct. Biol , vol.15 , pp. 490-498
    • Freeze, H.H.1    Aebi, M.2
  • 2
    • 2942557120 scopus 로고    scopus 로고
    • Congenital disorders of glycosylation (CDG): Update and new developments
    • Jaeken, J., Congenital disorders of glycosylation (CDG): update and new developments. J. Inherit. Metab. Dis. 2004, 27, 423-426.
    • (2004) J. Inherit. Metab. Dis , vol.27 , pp. 423-426
    • Jaeken, J.1
  • 3
    • 3442881366 scopus 로고    scopus 로고
    • Congenital disorders of glycosylation: A booming chapter of pediatrics
    • Jaeken, J., Carchon, H., Congenital disorders of glycosylation: a booming chapter of pediatrics. Curr. Opin. Pediatr. 2004, 16, 434-439.
    • (2004) Curr. Opin. Pediatr , vol.16 , pp. 434-439
    • Jaeken, J.1    Carchon, H.2
  • 4
    • 33644853797 scopus 로고    scopus 로고
    • Conserved oligomeric Golgi complex subunit 1 deficiency reveals a previously uncharacterized congenital disorder of glycosylation type II
    • Foulquier, F., Vasile, E., Schollen, E., Callewaert, N. et al., Conserved oligomeric Golgi complex subunit 1 deficiency reveals a previously uncharacterized congenital disorder of glycosylation type II. Proc Natl. Acad. Sci. USA 2006, 103, 3764-3769.
    • (2006) Proc Natl. Acad. Sci. USA , vol.103 , pp. 3764-3769
    • Foulquier, F.1    Vasile, E.2    Schollen, E.3    Callewaert, N.4
  • 5
    • 33847773480 scopus 로고    scopus 로고
    • Borderline mental development in a congenital disorder of glycosylation (CDG) type la patient with multisystemic involvement
    • Barone, R., Sturiale, L., Fiumara,A., Uziel, G. et al., Borderline mental development in a congenital disorder of glycosylation (CDG) type la patient with multisystemic involvement. J. Inherit. Metab. Dis. 2007, 30, 107.
    • (2007) J. Inherit. Metab. Dis , vol.30 , pp. 107
    • Barone, R.1    Sturiale, L.2    Fiumara, A.3    Uziel, G.4
  • 6
    • 0031909015 scopus 로고    scopus 로고
    • Isoforms and levels of transferrin, antithrombin, alpha(1)-antitrypsin and thyroxine-binding globulin in 48 patients with carbohydrate-deficient glycoprotein syndrome type I
    • Stibler, H., Holzbach, U., Kristiansson, B., Isoforms and levels of transferrin, antithrombin, alpha(1)-antitrypsin and thyroxine-binding globulin in 48 patients with carbohydrate-deficient glycoprotein syndrome type I. Scan. J. Clin. Lab. Invest. 1998, 58, 55-61.
    • (1998) Scan. J. Clin. Lab. Invest , vol.58 , pp. 55-61
    • Stibler, H.1    Holzbach, U.2    Kristiansson, B.3
  • 7
    • 0021686784 scopus 로고
    • Sialic acid-deficient serum and cerebrospinal fluid transferrin in a newly recognized genetic syndrome
    • Jaeken, J., van Eijk, H.G., van der Heul, C., Corbeel, I. et al., Sialic acid-deficient serum and cerebrospinal fluid transferrin in a newly recognized genetic syndrome. Clin. Chim. Acta 1984, 144, 245-247.
    • (1984) Clin. Chim. Acta , vol.144 , pp. 245-247
    • Jaeken, J.1    van Eijk, H.G.2    van der Heul, C.3    Corbeel, I.4
  • 8
    • 0025775843 scopus 로고
    • Biochemical characteristics and diagnosis of the carbohydrate deficient glycoprotein syndrome
    • Stibler, H., Jaeken, J., Kristiansson, B., Biochemical characteristics and diagnosis of the carbohydrate deficient glycoprotein syndrome. Acta Paediat. Scand. Suppl. 1991, 375, 21-31.
    • (1991) Acta Paediat. Scand. Suppl , vol.375 , pp. 21-31
    • Stibler, H.1    Jaeken, J.2    Kristiansson, B.3
  • 9
    • 0027503288 scopus 로고
    • Sugar chains of serum transferrin from patients with carbohydrate deficient glycoprotein syndrome. Evidence of asparagine-N-linked oligosaccharide transfer deficiency
    • Yamashita, K., Ideo, H., Ohkura, T., Fukushima, K. et al., Sugar chains of serum transferrin from patients with carbohydrate deficient glycoprotein syndrome. Evidence of asparagine-N-linked oligosaccharide transfer deficiency. J. Biol. Chem. 1993, 268, 5783-5789.
    • (1993) J. Biol. Chem , vol.268 , pp. 5783-5789
    • Yamashita, K.1    Ideo, H.2    Ohkura, T.3    Fukushima, K.4
  • 10
    • 35548972537 scopus 로고    scopus 로고
    • Congenital disorders of glycosylation: A rapidly expanding disease family
    • Jaeken, J., Matthijs, G., Congenital disorders of glycosylation: a rapidly expanding disease family. Annu. Rev. Genomics Hum. Genet. 2007, 8, 261-278.
    • (2007) Annu. Rev. Genomics Hum. Genet , vol.8 , pp. 261-278
    • Jaeken, J.1    Matthijs, G.2
  • 11
    • 33750097998 scopus 로고    scopus 로고
    • The use of mass spectrometry for the proteomic analysis of glycosylation
    • Morelle, W., Canis, K., Chirat, F., Faid, V., Michalski, J. C., The use of mass spectrometry for the proteomic analysis of glycosylation. Proteomics 2006, 6, 3993-4015.
    • (2006) Proteomics , vol.6 , pp. 3993-4015
    • Morelle, W.1    Canis, K.2    Chirat, F.3    Faid, V.4    Michalski, J.C.5
  • 12
    • 33744811996 scopus 로고    scopus 로고
    • Mass spectrometry for congenital disorders of glycosylation, CDG
    • Wada, Y., Mass spectrometry for congenital disorders of glycosylation, CDG. J. Chromatogr. B Analyt. Technol. Biomed. Life Sci. 2006, 838, 3-8.
    • (2006) J. Chromatogr. B Analyt. Technol. Biomed. Life Sci , vol.838 , pp. 3-8
    • Wada, Y.1
  • 13
    • 0027051210 scopus 로고
    • Structure of serum transferrin in carbohydrate-deficient glycoprotein syndrome
    • Wada, Y., Nishikawa, A., Okamoto, N., Inui, K. et al., Structure of serum transferrin in carbohydrate-deficient glycoprotein syndrome. Biochem. Biophys. Res. Commun. 1992, 189, 832-836.
    • (1992) Biochem. Biophys. Res. Commun , vol.189 , pp. 832-836
    • Wada, Y.1    Nishikawa, A.2    Okamoto, N.3    Inui, K.4
  • 14
    • 0037320846 scopus 로고    scopus 로고
    • The underglycosylation of plasma alpha 1-antitrypsin in congenital disorders of glycosylation type I is not random
    • Mills, K., Mills, P. B., Clayton, P. T., Mian, N. et al., The underglycosylation of plasma alpha 1-antitrypsin in congenital disorders of glycosylation type I is not random. Glycobiology 2003, 13(2): 73-85.
    • (2003) Glycobiology , vol.13 , Issue.2 , pp. 73-85
    • Mills, K.1    Mills, P.B.2    Clayton, P.T.3    Mian, N.4
  • 15
    • 22044456565 scopus 로고    scopus 로고
    • Glycoproteomics of N-glycosylation by in-gel deglycosylation and matrix-assisted laser desorption/ionisation-time of flight mass spectrometry mapping: Application to congenital disorders of glycosylation
    • Sagi, D., Kienz, P., Denecke, J., Marquardt, T., Peter-Katalinic, J., Glycoproteomics of N-glycosylation by in-gel deglycosylation and matrix-assisted laser desorption/ionisation-time of flight mass spectrometry mapping: application to congenital disorders of glycosylation. Proteomics 2005, 5: 2689-2701.
    • (2005) Proteomics , vol.5 , pp. 2689-2701
    • Sagi, D.1    Kienz, P.2    Denecke, J.3    Marquardt, T.4    Peter-Katalinic, J.5
  • 16
    • 0035213817 scopus 로고    scopus 로고
    • A mutation in the human MPDU1 gene causes congenital disorder of glycosylation type If (CDG-lf)
    • Kranz, C., Denecke, J., Lehrman, M. A., Ray, S. et al., A mutation in the human MPDU1 gene causes congenital disorder of glycosylation type If (CDG-lf). J. Clin. Invest. 2001, 108, 1613-1619.
    • (2001) J. Clin. Invest , vol.108 , pp. 1613-1619
    • Kranz, C.1    Denecke, J.2    Lehrman, M.A.3    Ray, S.4
  • 17
    • 0028178360 scopus 로고
    • Diagnosis of carbohydrate-deficient glycoprotein syndrome by matrix-assisted laser desorption time-of-flight mass spectrometry
    • Wada, Y., Gu, J., Okamoto, N., Inui, K., Diagnosis of carbohydrate-deficient glycoprotein syndrome by matrix-assisted laser desorption time-of-flight mass spectrometry. Biol. Mass Spectrom. 1994, 23, 108-109.
    • (1994) Biol. Mass Spectrom , vol.23 , pp. 108-109
    • Wada, Y.1    Gu, J.2    Okamoto, N.3    Inui, K.4
  • 18
    • 0035107128 scopus 로고    scopus 로고
    • Rapid determination of transferrin isoforms by immunoaffinity liquid chromatography and electrospray mass spectrometry
    • Lacey, J. M., Bergen, H. R., Magera, M. J., Naylor, S., O'Brien, J. F., Rapid determination of transferrin isoforms by immunoaffinity liquid chromatography and electrospray mass spectrometry. Clin. Chem. 2001, 47, 513-518.
    • (2001) Clin. Chem , vol.47 , pp. 513-518
    • Lacey, J.M.1    Bergen, H.R.2    Magera, M.J.3    Naylor, S.4    O'Brien, J.F.5
  • 19
    • 0347989232 scopus 로고    scopus 로고
    • Mass spectrometric analysis of human transferrin in different body fluids
    • Kleinert, P., Küster, T., Durka, S., Ballhausen, D. et al., Mass spectrometric analysis of human transferrin in different body fluids. Clin. Chem. Lab. Med. 2003, 41, 1580-1588.
    • (2003) Clin. Chem. Lab. Med , vol.41 , pp. 1580-1588
    • Kleinert, P.1    Küster, T.2    Durka, S.3    Ballhausen, D.4
  • 20
    • 0038042509 scopus 로고    scopus 로고
    • Mass spectrometric analysis of glycans in elucidating the pathogenesis of CDG type IIx
    • Mills, P. B., Mills, K., Mian, N., Winchester, B. G., Clayton, P. T., Mass spectrometric analysis of glycans in elucidating the pathogenesis of CDG type IIx. J. Inherit. Metab. Dis. 2003, 26, 119-134.
    • (2003) J. Inherit. Metab. Dis , vol.26 , pp. 119-134
    • Mills, P.B.1    Mills, K.2    Mian, N.3    Winchester, B.G.4    Clayton, P.T.5
  • 21
    • 10744225031 scopus 로고    scopus 로고
    • Detailed glycan analysis of serum glycoproteins of patients with congenital disorders of glycosylation indicates the specific defective glycan processing step and provides an insight into pathogenesis
    • Butler, M., Quelhas, D., Critchley, A. J., Carchon, H. et al., Detailed glycan analysis of serum glycoproteins of patients with congenital disorders of glycosylation indicates the specific defective glycan processing step and provides an insight into pathogenesis. Glycobiology 2003, 13, (9): 601-622.
    • (2003) Glycobiology , vol.13 , Issue.9 , pp. 601-622
    • Butler, M.1    Quelhas, D.2    Critchley, A.J.3    Carchon, H.4
  • 22
    • 0034491915 scopus 로고    scopus 로고
    • Defect in N-glycosylation of proteins is tissue-dependent in congenital disorders of glycosylation la
    • Dupre, T., Barnier, A., de Lonlay, P., Cormier-Daire, V. et al., Defect in N-glycosylation of proteins is tissue-dependent in congenital disorders of glycosylation la. Glycobiology 2000, 10, 1277-1281.
    • (2000) Glycobiology , vol.10 , pp. 1277-1281
    • Dupre, T.1    Barnier, A.2    de Lonlay, P.3    Cormier-Daire, V.4
  • 23
    • 0030606024 scopus 로고    scopus 로고
    • Diagnostic value of Western blotting in carbohydrate-deficient glycoprotein syndrome
    • Seta, N., Barnier, A., Hochedez, F., Besnard, M. A., Durand, G., Diagnostic value of Western blotting in carbohydrate-deficient glycoprotein syndrome. Clin. Chim. Acta 1996, 254, 131-140.
    • (1996) Clin. Chim. Acta , vol.254 , pp. 131-140
    • Seta, N.1    Barnier, A.2    Hochedez, F.3    Besnard, M.A.4    Durand, G.5
  • 24
    • 4644364677 scopus 로고    scopus 로고
    • Improvement of CDG diagnosis by combined examination of several glycoproteins
    • Fang, J., Peters, V., Assmann, B., Korner, C., Hoffmann, G. F., Improvement of CDG diagnosis by combined examination of several glycoproteins. J. Inherit. Metab. Dis. 2004, 27:(5), 581-590.
    • (2004) J. Inherit. Metab. Dis , vol.27 , Issue.5 , pp. 581-590
    • Fang, J.1    Peters, V.2    Assmann, B.3    Korner, C.4    Hoffmann, G.F.5
  • 25
    • 33847408371 scopus 로고    scopus 로고
    • Head-to-head comparison of serum fractionation techniques
    • Whiteaker, J. R., Zhang, H., Eng, J. K., Fang, R. et al., Head-to-head comparison of serum fractionation techniques. J. Proteome Res. 2007, 6, 828-836.
    • (2007) J. Proteome Res , vol.6 , pp. 828-836
    • Whiteaker, J.R.1    Zhang, H.2    Eng, J.K.3    Fang, R.4
  • 26
    • 33745827045 scopus 로고    scopus 로고
    • Comparative serum glycoproteomics using lectin selected sialic acid glycoproteins with mass spectrometric analysis: Application to pancreatic cancer serum
    • Zhao, J., Simeone, D. M., Heidt, D., Anderson, M. A., Lubman, D. M., Comparative serum glycoproteomics using lectin selected sialic acid glycoproteins with mass spectrometric analysis: application to pancreatic cancer serum. J. Proteome Res. 2006, 5, 1792-1802.
    • (2006) J. Proteome Res , vol.5 , pp. 1792-1802
    • Zhao, J.1    Simeone, D.M.2    Heidt, D.3    Anderson, M.A.4    Lubman, D.M.5
  • 27
    • 25844445924 scopus 로고    scopus 로고
    • Hypoglycosylation with increased fucosylation and branching of serum transferrin N-glycans in untreated galactosemia
    • Sturiale, L., Barone, R., Fiumara, A., Perez, M. et al., Hypoglycosylation with increased fucosylation and branching of serum transferrin N-glycans in untreated galactosemia. Glycobiology 2005, 15, 1268-1276.
    • (2005) Glycobiology , vol.15 , pp. 1268-1276
    • Sturiale, L.1    Barone, R.2    Fiumara, A.3    Perez, M.4
  • 29
    • 0030587060 scopus 로고    scopus 로고
    • Analysis of acidic oligosaccharides and glycopeptides by matrix-assisted laser desorption/ionization time-of-flight mass spectrometry
    • Papac, D. I., Wong, A., Jones, A. J., Analysis of acidic oligosaccharides and glycopeptides by matrix-assisted laser desorption/ionization time-of-flight mass spectrometry. Anal. Chem. 1996, 15, 3215-3223.
    • (1996) Anal. Chem , vol.15 , pp. 3215-3223
    • Papac, D.I.1    Wong, A.2    Jones, A.J.3
  • 30
    • 34447326804 scopus 로고
    • A simple and rapid method for the permethylation of carbohydrates
    • Ciucanu, I., Kerek, F., A simple and rapid method for the permethylation of carbohydrates. Carbohydr. Res. 1984, 131, 209-217.
    • (1984) Carbohydr. Res , vol.131 , pp. 209-217
    • Ciucanu, I.1    Kerek, F.2
  • 31
    • 0025615601 scopus 로고
    • Preparation and desorption mass spectrometry of permethyl and peracetyl derivatives of oligosaccharides
    • Dell, A., Preparation and desorption mass spectrometry of permethyl and peracetyl derivatives of oligosaccharides. Methods Enzymol. 1990, 193, 647-660.
    • (1990) Methods Enzymol , vol.193 , pp. 647-660
    • Dell, A.1
  • 32
    • 24644458130 scopus 로고    scopus 로고
    • Strategies to study human serum transferrin isoforms using integrated liquid chromatography ICPMS, MALDI-TOF, and ESI-Q-TOF detection: Application to chronic alcohol abuse
    • del Castillo Busto, M. E., Monte-Bayòn, M., Gonz̀les-Blanco, E., Meija, J., Sanz-Medel, A., Strategies to study human serum transferrin isoforms using integrated liquid chromatography ICPMS, MALDI-TOF, and ESI-Q-TOF detection: application to chronic alcohol abuse. Anal. Chem. 2005, 77, 5615-5621.
    • (2005) Anal. Chem , vol.77 , pp. 5615-5621
    • del Castillo Busto, M.E.1    Monte-Bayòn, M.2    Gonz̀les-Blanco, E.3    Meija, J.4    Sanz-Medel, A.5
  • 33
    • 0027768796 scopus 로고
    • Electrospray ionization-mass spectrometric analysis of serum transferrin isoforms in patients with carbohydrate-deficient glycoprotein syndrome
    • Yamashita, K., Ohkura, T., Ideo, H., Ohno, K., Kanai, M. K., Electrospray ionization-mass spectrometric analysis of serum transferrin isoforms in patients with carbohydrate-deficient glycoprotein syndrome. J. Biochem. 1993, 114, 766-769.
    • (1993) J. Biochem , vol.114 , pp. 766-769
    • Yamashita, K.1    Ohkura, T.2    Ideo, H.3    Ohno, K.4    Kanai, M.K.5
  • 34
    • 0029585865 scopus 로고
    • Phosphomannomutase deficiency is a cause of carbohydrate-deficient glycoprotein syndrome type I
    • Van Schaftingen, E., Jaeken, J., Phosphomannomutase deficiency is a cause of carbohydrate-deficient glycoprotein syndrome type I. FEBS Lett. 1995, 377, 318-320.
    • (1995) FEBS Lett , vol.377 , pp. 318-320
    • Van Schaftingen, E.1    Jaeken, J.2
  • 35
    • 0014319864 scopus 로고
    • The application of rivanol for serum transferrin and immunoglobulin G determination
    • Sagan, Z., The application of rivanol for serum transferrin and immunoglobulin G determination. Clin. Chim. Acta 1968, 27, 225-230.
    • (1968) Clin. Chim. Acta , vol.27 , pp. 225-230
    • Sagan, Z.1
  • 36
    • 0023898432 scopus 로고
    • Molecular basis of alpha-1-antitrypsin deficiency
    • Brantly, M., Nukiwa, T., Crystal, R. G., Molecular basis of alpha-1-antitrypsin deficiency. Am. J. Med. 1988, 84, 13-31.
    • (1988) Am. J. Med , vol.84 , pp. 13-31
    • Brantly, M.1    Nukiwa, T.2    Crystal, R.G.3
  • 37
    • 33645100367 scopus 로고    scopus 로고
    • Comprehensive glyco-proteomic analysis of human alphal-antitrypsin and its charge isoforms
    • Kolarich, D., Weber, A., Turecek, P. L., Schwarz, H. P., Altmann, F., Comprehensive glyco-proteomic analysis of human alphal-antitrypsin and its charge isoforms. Proteomics 2006, 6, 3369-3380.
    • (2006) Proteomics , vol.6 , pp. 3369-3380
    • Kolarich, D.1    Weber, A.2    Turecek, P.L.3    Schwarz, H.P.4    Altmann, F.5
  • 38
    • 0035378754 scopus 로고    scopus 로고
    • Analysis by matrix assisted laser desorption/ ionisation time-of-flight mass spectrometry of the post-translational modifications of α1-antitrypsin isoforms separated by 2D-PAGE
    • Mills, P. B., Mills, K., Johnson, A. W., Clayton, P. T., Winchester, B. G., Analysis by matrix assisted laser desorption/ ionisation time-of-flight mass spectrometry of the post-translational modifications of α1-antitrypsin isoforms separated by 2D-PAGE. Proteomics 2001, 1, 778-786.
    • (2001) Proteomics , vol.1 , pp. 778-786
    • Mills, P.B.1    Mills, K.2    Johnson, A.W.3    Clayton, P.T.4    Winchester, B.G.5
  • 39
    • 0034775822 scopus 로고    scopus 로고
    • Identification of α1-antitrypsin variants in plasma with the use of proteomic technology
    • Mills, K., Mills, P. B., Clayton, P. T., Johnson, A. W. et al., Identification of α1-antitrypsin variants in plasma with the use of proteomic technology. Clin. Chem. 2001, 47, 2012-2022.
    • (2001) Clin. Chem , vol.47 , pp. 2012-2022
    • Mills, K.1    Mills, P.B.2    Clayton, P.T.3    Johnson, A.W.4
  • 40
    • 0038732507 scopus 로고    scopus 로고
    • Increased fucosylation and reduced branching of serum glycoprotein N-glycans in all known subtypes of congenital disorder of glycosylation I
    • Callewaert, N., Schollen, E., Vanhecke, A., Jaeken, J. et al., Increased fucosylation and reduced branching of serum glycoprotein N-glycans in all known subtypes of congenital disorder of glycosylation I. Glycobiology 2003, 13, 369-375.
    • (2003) Glycobiology , vol.13 , pp. 369-375
    • Callewaert, N.1    Schollen, E.2    Vanhecke, A.3    Jaeken, J.4
  • 41
    • 0035125320 scopus 로고    scopus 로고
    • High residual activity of PMM2 in patients' fibroblasts: Possible pitfall in the diagnosis of CDG-la (phosphomannomutase deficiency)
    • Grünewald, S., Schollen, E., Van Schaftingen, E., Jaeken, J., Matthijs, G. High residual activity of PMM2 in patients' fibroblasts: possible pitfall in the diagnosis of CDG-la (phosphomannomutase deficiency). Am. J. Hum. Genet. 2001, 68, 347-354.
    • (2001) Am. J. Hum. Genet , vol.68 , pp. 347-354
    • Grünewald, S.1    Schollen, E.2    Van Schaftingen, E.3    Jaeken, J.4    Matthijs, G.5
  • 43
    • 34548026071 scopus 로고    scopus 로고
    • Transferrin hypoglycosylation in hereditary fructose intolerance: Using the clues and avoiding the pitfalls
    • Adamowicz, M., Ploski, R., Rokicki, D., Morava, E. et al., Transferrin hypoglycosylation in hereditary fructose intolerance: using the clues and avoiding the pitfalls. J. Inherit. Metab. Dis. 2007, 30, 407.
    • (2007) J. Inherit. Metab. Dis , vol.30 , pp. 407
    • Adamowicz, M.1    Ploski, R.2    Rokicki, D.3    Morava, E.4
  • 44
    • 0029119644 scopus 로고
    • Galactose-1-phosphate in the pathophysiology of galactosemia
    • Gitzelman, R., Galactose-1-phosphate in the pathophysiology of galactosemia. Eur. J. Pediatr. 1995, 154, S45-S49.
    • (1995) Eur. J. Pediatr , vol.154
    • Gitzelman, R.1
  • 45
    • 0027858239 scopus 로고
    • A new approach to quantitate carbohydrate- deficient transferrin isoforms in alcohol abusers: Partial iron saturation in isoelectric focusing/immunoblotting and laser densitometry
    • Bean, P., Peter, J. B., A new approach to quantitate carbohydrate- deficient transferrin isoforms in alcohol abusers: partial iron saturation in isoelectric focusing/immunoblotting and laser densitometry. Alcohol Clin. Exp. Res. 1993, 17, 1163-1170.
    • (1993) Alcohol Clin. Exp. Res , vol.17 , pp. 1163-1170
    • Bean, P.1    Peter, J.B.2
  • 46
    • 0029957579 scopus 로고    scopus 로고
    • Inhibition of phosphomannose isomerase by fructose 1-phosphate: An explanation for defective N-glycosylation in hereditary fructose intolerance
    • Jaeken, J., Pirard, M., Adamowicz, M., Pronicka, E., van Schaftingen, E., Inhibition of phosphomannose isomerase by fructose 1-phosphate: an explanation for defective N-glycosylation in hereditary fructose intolerance. Pediatr. Res. 1996, 40, 764-766.
    • (1996) Pediatr. Res , vol.40 , pp. 764-766
    • Jaeken, J.1    Pirard, M.2    Adamowicz, M.3    Pronicka, E.4    van Schaftingen, E.5
  • 47
    • 33947192955 scopus 로고    scopus 로고
    • Comparison of the methods for profiling glycoprotein glycans-HUPO Human Disease Glycomics/Proteome Initiative multi-institutional study
    • Wada, Y., Azadi, P., Costello, C. E., Dell, A. et al., Comparison of the methods for profiling glycoprotein glycans-HUPO Human Disease Glycomics/Proteome Initiative multi-institutional study. Glycobiology 2007, 4, 411-422.
    • (2007) Glycobiology , vol.4 , pp. 411-422
    • Wada, Y.1    Azadi, P.2    Costello, C.E.3    Dell, A.4


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.