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Volumn 46, Issue 3, 1999, Pages 727-738

Carbohydrate-deficient glycoprotein syndromes

Author keywords

Carbohydrate deficient glycoprotein syndrome; N linked glycosylation

Indexed keywords

DOLICHOL; GLYCOPROTEIN; MANNOSE; OLIGOSACCHARIDE; TRANSFERRIN;

EID: 0033250344     PISSN: 0001527X     EISSN: None     Source Type: Journal    
DOI: 10.18388/abp.1999_4145     Document Type: Review
Times cited : (4)

References (85)
  • 1
    • 0032501263 scopus 로고    scopus 로고
    • CDGS-I a recently discovered hereditary metabolic disease. Multiple organ manifestations, incidence 1/80.000, difficult to treat
    • Kristiansson, B., Stibler, H., Hagberg, B. & Wahlstrom, J. (1998) CDGS-I a recently discovered hereditary metabolic disease. Multiple organ manifestations, incidence 1/80.000, difficult to treat. Lakartidningen 95, 5742-5748.
    • (1998) Lakartidningen , vol.95 , pp. 5742-5748
    • Kristiansson, B.1    Stibler, H.2    Hagberg, B.3    Wahlstrom, J.4
  • 2
    • 0025830558 scopus 로고
    • Clinical presentation and natural course of the carbohydrate-deficient glycoprotein syndrome
    • Jaeken, J., Hagberg, B. & Strømme, P. (1991) Clinical presentation and natural course of the carbohydrate-deficient glycoprotein syndrome. Acta Paediatr. Scand. (Suppl.) 375, 6-13.
    • (1991) Acta Paediatr. Scand. (Suppl.) , vol.375 , pp. 6-13
    • Jaeken, J.1    Hagberg, B.2    Strømme, P.3
  • 3
    • 0031979479 scopus 로고    scopus 로고
    • Lysosomal enzyme activities in serum and leukocytes from patients with carbohydrate-deficient glycoprotein syndrome type IA (phosphomannomutase deficiency)
    • Barone, R., Carchon, H., Jansen, E., Pavone, L., Fiumara, A., Bosshard, N.U., Gitzelmann, R. & Jaeken, J. (1998) Lysosomal enzyme activities in serum and leukocytes from patients with carbohydrate-deficient glycoprotein syndrome type IA (phosphomannomutase deficiency). J. Inher. Metab. Dis. 21, 167-172.
    • (1998) J. Inher. Metab. Dis. , vol.21 , pp. 167-172
    • Barone, R.1    Carchon, H.2    Jansen, E.3    Pavone, L.4    Fiumara, A.5    Bosshard, N.U.6    Gitzelmann, R.7    Jaeken, J.8
  • 5
    • 0031019482 scopus 로고    scopus 로고
    • Syndrome of the month: Carbohydrate-deficient glycoprotein syndrome (CDG) type I
    • Jaeken, J., Matthijs, G., Barone, R. & Carchon, H. (1997) Syndrome of the month: Carbohydrate-deficient glycoprotein syndrome (CDG) type I. J. Med. Genet. 34, 73-76.
    • (1997) J. Med. Genet. , vol.34 , pp. 73-76
    • Jaeken, J.1    Matthijs, G.2    Barone, R.3    Carchon, H.4
  • 6
    • 2542423826 scopus 로고    scopus 로고
    • Carbohydrate-deficient glycoprotein syndrome
    • Krasnewich, D. & Gahl, W.A. (1997) Carbohydrate-deficient glycoprotein syndrome. Adv. Pediatr. 215, 145-157.
    • (1997) Adv. Pediatr. , vol.215 , pp. 145-157
    • Krasnewich, D.1    Gahl, W.A.2
  • 7
    • 84878788105 scopus 로고
    • Studies on glycoconjugates. LXIV. Complete structure of two carbohydrate units of human serotransferrin
    • Spik, G., Bayard, B., Fournet, B., Strecker, Bouquuelet, S. & Montreuil, J. (1975) Studies on glycoconjugates. LXIV. Complete structure of two carbohydrate units of human serotransferrin. FEBS Lett. 50, 296-299.
    • (1975) FEBS Lett. , vol.50 , pp. 296-299
    • Spik, G.1    Bayard, B.2    Fournet, B.3    Strecker, B.S.4    Montreuil, J.5
  • 8
    • 0031935176 scopus 로고    scopus 로고
    • Determination of glycan structures and molecular masses of the glycovariants of serum transferrin from a patient with carbohydrate deficient syndrome type II
    • Coddeville, B., Carchon, H., Jaeken, J., Briand, G. & Spik, G. (1998) Determination of glycan structures and molecular masses of the glycovariants of serum transferrin from a patient with carbohydrate deficient syndrome type II. Glycoconj. J. 15, 265-273.
    • (1998) Glycoconj. J. , vol.15 , pp. 265-273
    • Coddeville, B.1    Carchon, H.2    Jaeken, J.3    Briand, G.4    Spik, G.5
  • 9
    • 0018611016 scopus 로고
    • Clinical significance of abnormal heterogeneity of transferrin in relation to alcohol consumption
    • Stibler, H., Borg, S. & Allgulander, C. (1979) Clinical significance of abnormal heterogeneity of transferrin in relation to alcohol consumption. Acta Med. Scand. 206, 275-281.
    • (1979) Acta Med. Scand. , vol.206 , pp. 275-281
    • Stibler, H.1    Borg, S.2    Allgulander, C.3
  • 11
    • 0000249979 scopus 로고
    • Familial psychomotor retardation with markedly fluctuating serum prolactin, FSH and GH levels, partial TBG deficiency, increased serum arylsulphatase A and increased CSF protein: A new syndrome?
    • Jaeken, J., Vanderschueren-Lodeweyck, M., Casaer, P., Snoeck, L., Corbeel, L., Eggermont, E. & Eeckels, R. (1980) Familial psychomotor retardation with markedly fluctuating serum prolactin, FSH and GH levels, partial TBG deficiency, increased serum arylsulphatase A and increased CSF protein: A new syndrome? Pediatr. Res. 14, 179.
    • (1980) Pediatr. Res. , vol.14 , pp. 179
    • Jaeken, J.1    Vanderschueren-Lodeweyck, M.2    Casaer, P.3    Snoeck, L.4    Corbeel, L.5    Eggermont, E.6    Eeckels, R.7
  • 12
    • 0029585865 scopus 로고
    • Phosphomannomutase deficiency is a cause of carbohydrate-deficient glycoprotein syndrome type I
    • van Schaftingen, E. & Jaeken, J. (1995) Phosphomannomutase deficiency is a cause of carbohydrate-deficient glycoprotein syndrome type I. FEBS Lett. 377, 318-320.
    • (1995) FEBS Lett. , vol.377 , pp. 318-320
    • Van Schaftingen, E.1    Jaeken, J.2
  • 16
    • 17444448342 scopus 로고    scopus 로고
    • Phosphomannose isomerase deficiency - A carbohydrate-deficient glycoprotein syndrome with hepatic-intestinal presentation
    • Jaeken, J., Matthijs, G., Sandubray, J.M., Dionisivici, C., Bertini, E. & Delonlay, P. (1998) Phosphomannose isomerase deficiency - A carbohydrate-deficient glycoprotein syndrome with hepatic-intestinal presentation. Am. J. Hum. Genet. 62, 1535-1539.
    • (1998) Am. J. Hum. Genet. , vol.62 , pp. 1535-1539
    • Jaeken, J.1    Matthijs, G.2    Sandubray, J.M.3    Dionisivici, C.4    Bertini, E.5    Delonlay, P.6
  • 18
    • 0027177255 scopus 로고
    • Carbohydrate-deficient glycoprotein (CDG) syndrome - A new variant, type III
    • Stibler, H., Westerberg, B., Hanefeld, F. & Hagberg, B. (1993) Carbohydrate-deficient glycoprotein (CDG) syndrome - a new variant, type III. Neuropediatrics 24, 51-52.
    • (1993) Neuropediatrics , vol.24 , pp. 51-52
    • Stibler, H.1    Westerberg, B.2    Hanefeld, F.3    Hagberg, B.4
  • 19
    • 0028851977 scopus 로고
    • Carbohydrate-deficient glycoprotein syndrome - A fourth subtype
    • Stibler, H., Stephani, U. & Kutsch, U. (1995) Carbohydrate-deficient glycoprotein syndrome - a fourth subtype. Neuropediatrics 26, 235-237
    • (1995) Neuropediatrics , vol.26 , pp. 235-237
    • Stibler, H.1    Stephani, U.2    Kutsch, U.3
  • 20
    • 0032528886 scopus 로고    scopus 로고
    • A novel carbohydrate-deficient glycoprotein syndrome characterized by a deficiency in glucosylation of the dolichol-linked oligosaccharide
    • Burda, P., Borsig, L., de Rijk-van Andel, J., Wevers, R., Jaeken, J., Carchon, H., Berger, E.G. & Aebi, M. (1998) A novel carbohydrate-deficient glycoprotein syndrome characterized by a deficiency in glucosylation of the dolichol-linked oligosaccharide. J. Clin. Invest. 102, 647-652.
    • (1998) J. Clin. Invest. , vol.102 , pp. 647-652
    • Burda, P.1    Borsig, L.2    De Rijk-Van Andel, J.3    Wevers, R.4    Jaeken, J.5    Carchon, H.6    Berger, E.G.7    Aebi, M.8
  • 22
    • 0027930443 scopus 로고
    • Carbohydrate deficient glycoprotein syndrome type II: A deficiency in Golgi localized N-acetylglucosaminyltransferase II
    • Jaeken, J., Schachter, H., Carchon, H., De Cock, P., Coddeville, B. & Spik, G. (1994) Carbohydrate deficient glycoprotein syndrome type II: A deficiency in Golgi localized N-acetylglucosaminyltransferase II. Arch. Dis. Child. 71, 123-127.
    • (1994) Arch. Dis. Child. , vol.71 , pp. 123-127
    • Jaeken, J.1    Schachter, H.2    Carchon, H.3    De Cock, P.4    Coddeville, B.5    Spik, G.6
  • 23
    • 0029074067 scopus 로고
    • Carbohydrate-deficient glycoprotein syndrome type II - An autosomal recessive N-acetylglucosaminyltransferase II deficiency different from typical hereditary erythroblastic multinuclearity with a positive acidified-serum lysis test (HEMPAS)
    • Charuk, J.H.M., Tan, J., Bernardini, M., Hadelad, S., Reithmeier, R.A.F., Jaeken, J. & Schachter, H. (1995) Carbohydrate-deficient glycoprotein syndrome type II - an autosomal recessive N-acetylglucosaminyltransferase II deficiency different from typical hereditary erythroblastic multinuclearity with a positive acidified-serum lysis test (HEMPAS). Eur. J. Biochem. 230, 797-805.
    • (1995) Eur. J. Biochem. , vol.230 , pp. 797-805
    • Charuk, J.H.M.1    Tan, J.2    Bernardini, M.3    Hadelad, S.4    Reithmeier, R.A.F.5    Jaeken, J.6    Schachter, H.7
  • 24
    • 0018801491 scopus 로고
    • The biosynthesis of the major lipid-linked oligosaccharide of Chinese hamster ovary cells occurs by the ordered addition of mannose residues
    • Chapman, A., Li, E. & Kornfeld, S. (1979) The biosynthesis of the major lipid-linked oligosaccharide of Chinese hamster ovary cells occurs by the ordered addition of mannose residues. J. Biol. Chem. 254, 10243-10249.
    • (1979) J. Biol. Chem. , vol.254 , pp. 10243-10249
    • Chapman, A.1    Li, E.2    Kornfeld, S.3
  • 25
    • 0032904470 scopus 로고    scopus 로고
    • The dolichol pathway of N-linked glycosylation
    • Burda, P. & Aebi, M. (1999) The dolichol pathway of N-linked glycosylation. Biochim. Biophys. Acta 1426, 239-257.
    • (1999) Biochim. Biophys. Acta , vol.1426 , pp. 239-257
    • Burda, P.1    Aebi, M.2
  • 26
    • 0000247045 scopus 로고
    • 2-protein
    • (Montreuil, J., Vliegenthart, J.F.G. & Schachter, H., eds.) Elsevier Science B.V., Amsterdam
    • 2-protein; in Glycoproteins (Montreuil, J., Vliegenthart, J.F.G. & Schachter, H., eds.) pp. 145-152, Elsevier Science B.V., Amsterdam.
    • (1995) Glycoproteins , pp. 145-152
    • Verbert, A.1
  • 27
    • 0030980125 scopus 로고    scopus 로고
    • The role of the lipid matrix in the biosynthesis of dolichyl-linked oligosaccharides
    • Schutzbach, J.S. (1997) The role of the lipid matrix in the biosynthesis of dolichyl-linked oligosaccharides. Glycoconjugate J. 14, 175-182.
    • (1997) Glycoconjugate J. , vol.14 , pp. 175-182
    • Schutzbach, J.S.1
  • 28
    • 0029991763 scopus 로고    scopus 로고
    • Biochemistry, molecular biology and genetics of the oligosaccharyltransferase
    • Silberstein, S. & Gelmore, R. (1996) Biochemistry, molecular biology and genetics of the oligosaccharyltransferase. FASEB J. 10, 849-858.
    • (1996) FASEB J. , vol.10 , pp. 849-858
    • Silberstein, S.1    Gelmore, R.2
  • 29
    • 0030881717 scopus 로고    scopus 로고
    • Quality control in the secretory pathway: The role of calrericulin, calnexin, and BiP in the retension of glycoproteins with C-terminal truncations
    • Zhang, J.X., Braakman, I., Mattach, K.E. & Helenius, A. (1997) Quality control in the secretory pathway: The role of calrericulin, calnexin, and BiP in the retension of glycoproteins with C-terminal truncations. Mol. Biol. Cell 8, 1943-1954.
    • (1997) Mol. Biol. Cell , vol.8 , pp. 1943-1954
    • Zhang, J.X.1    Braakman, I.2    Mattach, K.E.3    Helenius, A.4
  • 30
    • 0033548479 scopus 로고    scopus 로고
    • Trimming and readdition of glucose to N-linked oligosaccharides determines calnexin association of a substrate glycoprotein in living cells
    • Cannon, K.S. & Helenius, A. (1999) Trimming and readdition of glucose to N-linked oligosaccharides determines calnexin association of a substrate glycoprotein in living cells. J. Biol. Chem. 274, 7537-7544.
    • (1999) J. Biol. Chem. , vol.274 , pp. 7537-7544
    • Cannon, K.S.1    Helenius, A.2
  • 31
    • 77956836494 scopus 로고
    • Biosynthesis 2c. Glycosyltransferases involved in the synthesis of N-glycan antennae
    • (Montreuil, J., Vliegenthart, J.F.G. & Schachter, H., eds.) Elsevier Science B.V., Amsterdam
    • Schachter, H. (1995) Biosynthesis 2c. Glycosyltransferases involved in the synthesis of N-glycan antennae; in Glycoproteins (Montreuil, J., Vliegenthart, J.F.G. & Schachter, H., eds.) pp. 153-199, Elsevier Science B.V., Amsterdam.
    • (1995) Glycoproteins , pp. 153-199
    • Schachter, H.1
  • 32
    • 0039740716 scopus 로고    scopus 로고
    • Adding the finishing touches: Terminal elaborations
    • Kluwer Academic Publishers, Boston, Dordrecht, London
    • Bill, R.M., Revers, L. & Wilson, I.B.H. (1998) Adding the finishing touches: terminal elaborations; in Protein Glycosylation, pp. 329-408, Kluwer Academic Publishers, Boston, Dordrecht, London.
    • (1998) Protein Glycosylation , pp. 329-408
    • Bill, R.M.1    Revers, L.2    Wilson, I.B.H.3
  • 33
    • 0031711820 scopus 로고    scopus 로고
    • Transporters of nucleotide sugars, ATP, and nucleotide sulfate in the endoplasmic reticulum and Golgi apparatus
    • Hirschberg, C.B., Robbins, P.W. & Abeijon, C. (1998) Transporters of nucleotide sugars, ATP, and nucleotide sulfate in the endoplasmic reticulum and Golgi apparatus. Annu. Rev. Biochem. 67, 49-69.
    • (1998) Annu. Rev. Biochem. , vol.67 , pp. 49-69
    • Hirschberg, C.B.1    Robbins, P.W.2    Abeijon, C.3
  • 34
    • 0027957037 scopus 로고
    • Normal N-oligosaccharyltransferase activity in fibroblasts from patients with carbohydrate-deficient glycoprotein syndrome
    • Knauer, R., Lehle, F., Hanefeld, F. & von Figura, K. (1994) Normal N-oligosaccharyltransferase activity in fibroblasts from patients with carbohydrate-deficient glycoprotein syndrome. J. Inher. Metab. Dis. 17, 541-544.
    • (1994) J. Inher. Metab. Dis. , vol.17 , pp. 541-544
    • Knauer, R.1    Lehle, F.2    Hanefeld, F.3    Von Figura, K.4
  • 35
    • 0028207536 scopus 로고
    • Major defects of carbohydrate-deficient glycoprotein syndrome is not found in the synthesis of dolichyl phosphate on N-acetylglucosaminyl-pyrophosphoryl-dolichol
    • Yasugi, E.M., Nakasuji, M., Dohi, T. & Oshima, M. (1994) Major defects of carbohydrate-deficient glycoprotein syndrome is not found in the synthesis of dolichyl phosphate on N-acetylglucosaminyl-pyrophosphoryl-dolichol. Biochem. Biophys. Res. Commun. 200, 816-820.
    • (1994) Biochem. Biophys. Res. Commun. , vol.200 , pp. 816-820
    • Yasugi, E.M.1    Nakasuji, M.2    Dohi, T.3    Oshima, M.4
  • 36
    • 0025064062 scopus 로고
    • Biosynthesis of glucosyl phosphatidylinositol membrane anchors
    • Doering, T., Masterson, W.J., Hart, G.W. & Englund, P.T. (1990) Biosynthesis of glucosyl phosphatidylinositol membrane anchors. J. Biol. Chem. 265, 611-614.
    • (1990) J. Biol. Chem. , vol.265 , pp. 611-614
    • Doering, T.1    Masterson, W.J.2    Hart, G.W.3    Englund, P.T.4
  • 37
    • 1842413048 scopus 로고    scopus 로고
    • C-Mannosylation of human RNase 2 is an intracellular process performed by a variety of cultured cells
    • Krieg, J., Glasner, W., Vicentini, A., Doncey, M.A., Löffler, A., Hess, D. & Hofsteenge, J. 1997) C-Mannosylation of human RNase 2 is an intracellular process performed by a variety of cultured cells. J. Biol. Chem. 272, 26687-26692.
    • (1997) J. Biol. Chem. , vol.272 , pp. 26687-26692
    • Krieg, J.1    Glasner, W.2    Vicentini, A.3    Doncey, M.A.4    Löffler, A.5    Hess, D.6    Hofsteenge, J.7
  • 39
    • 0031881719 scopus 로고    scopus 로고
    • Protein C-mannosylation is enzyme-catalysed and uses dolichyl phosphate-mannose as a precursor
    • Doncey, M.A., Hess, D., Cacan, R. & Hofsteenge, J. (1998) Protein C-mannosylation is enzyme-catalysed and uses dolichyl phosphate-mannose as a precursor. Mol. Biol. Cell 9, 291-300.
    • (1998) Mol. Biol. Cell , vol.9 , pp. 291-300
    • Doncey, M.A.1    Hess, D.2    Cacan, R.3    Hofsteenge, J.4
  • 40
    • 0031882332 scopus 로고    scopus 로고
    • Recognition signal for C-mannosylation of Trp-7 in RNase 2 consists of sequence Trp-xx-Trp
    • Krieg, J., Hartmann, S., Vicentini, A., Gläsner, W., Hess, D. & Hofsteenge, J. (1998) Recognition signal for C-mannosylation of Trp-7 in RNase 2 consists of sequence Trp-xx-Trp. Mol. Biol. Cell 9, 301-309.
    • (1998) Mol. Biol. Cell , vol.9 , pp. 301-309
    • Krieg, J.1    Hartmann, S.2    Vicentini, A.3    Gläsner, W.4    Hess, D.5    Hofsteenge, J.6
  • 42
    • 0002328891 scopus 로고
    • Carbohydrate metabolism. II. Special pathways
    • (Devlin, A., ed.) 3rd edn., Wiley-Liss, New York
    • Schwartz, N.B. (1992) Carbohydrate metabolism. II. Special pathways; in Textbook of Biochemistry with Clinical Correlations (Devlin, A., ed.) pp. 359-386, 3rd edn., Wiley-Liss, New York.
    • (1992) Textbook of Biochemistry with Clinical Correlations , pp. 359-386
    • Schwartz, N.B.1
  • 43
    • 0038599459 scopus 로고    scopus 로고
    • Abnormal synthesis of mannose 1-phosphate derived carbohydrates in carbohydrate-deficient glycoprotein syndrome type I fibroblasts with phosphomannomutase deficiency
    • Körner, Ch., Lehle, L. & von Figura, K. (1998) Abnormal synthesis of mannose 1-phosphate derived carbohydrates in carbohydrate-deficient glycoprotein syndrome type I fibroblasts with phosphomannomutase deficiency. Glycobiology 8, 165-171.
    • (1998) Glycobiology , vol.8 , pp. 165-171
    • Körner, Ch.1    Lehle, L.2    Von Figura, K.3
  • 44
    • 0031214067 scopus 로고    scopus 로고
    • Abnormal metabolism of mannose in families with carbohydrate deficient glycoprotein syndrome type I
    • Panneerselvam, K., Etchison, J.R., Skovby, F. & Freeze, H.H. (1997) Abnormal metabolism of mannose in families with carbohydrate deficient glycoprotein syndrome type I. Biochem. Mol. Med. 61, 161-167.
    • (1997) Biochem. Mol. Med. , vol.61 , pp. 161-167
    • Panneerselvam, K.1    Etchison, J.R.2    Skovby, F.3    Freeze, H.H.4
  • 45
    • 0029995127 scopus 로고    scopus 로고
    • Carbohydrate deficient glycoprotein syndrome-like transferrin isoelectric focusing pattern in untreated fructosaemia
    • Adamowicz, M. & Pronicka, E. (1996) Carbohydrate deficient glycoprotein syndrome-like transferrin isoelectric focusing pattern in untreated fructosaemia. Eur. J. Pediatr. 155, 347-348.
    • (1996) Eur. J. Pediatr. , vol.155 , pp. 347-348
    • Adamowicz, M.1    Pronicka, E.2
  • 46
    • 0031945356 scopus 로고    scopus 로고
    • Hereditary fructose intolerance
    • Ali, M., Rellos, P. & Cox, T.M. (1998) Hereditary fructose intolerance. J. Med. Genet. 35, 353-365.
    • (1998) J. Med. Genet. , vol.35 , pp. 353-365
    • Ali, M.1    Rellos, P.2    Cox, T.M.3
  • 47
    • 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. (1996) Inhibition of phosphomannose isomerase by fructose 1-phosphate: An explanation for defective N-glycosylation in hereditary fructose intolerance. Pediatr. Res. 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
  • 48
    • 0027970923 scopus 로고
    • Carbohydrate-deficient glycoprotein syndrome: Not an N-linked oligosaccharide processing defect, but an abnormality in lipid-linked oligosaccharide biosynthesis?
    • Powell, L.D., Panneerselvam, K., Vij, R., Diaz, S., Manzi, A., Buist, N., Freeze, H. & Varki, A. (1994) Carbohydrate-deficient glycoprotein syndrome: Not an N-linked oligosaccharide processing defect, but an abnormality in lipid-linked oligosaccharide biosynthesis? J. Clin. Invest. 94, 1901-1909.
    • (1994) J. Clin. Invest. , vol.94 , pp. 1901-1909
    • Powell, L.D.1    Panneerselvam, K.2    Vij, R.3    Diaz, S.4    Manzi, A.5    Buist, N.6    Freeze, H.7    Varki, A.8
  • 49
    • 0029095453 scopus 로고
    • Abnormal synthesis of dolichol-linked oligosaccharides in carbohydrate-deficient glycoprotein syndrome
    • Krasnewich, D.M., Holt, G.D., Brantly, M., Skovby, F., Redwine, J. & Gahl, W.A. (1995) Abnormal synthesis of dolichol-linked oligosaccharides in carbohydrate-deficient glycoprotein syndrome. Glycobiology 5, 503-510.
    • (1995) Glycobiology , vol.5 , pp. 503-510
    • Krasnewich, D.M.1    Holt, G.D.2    Brantly, M.3    Skovby, F.4    Redwine, J.5    Gahl, W.A.6
  • 50
    • 0028962872 scopus 로고
    • Carbohydrate-deficient glycoprotein syndrome (CDGS) - Glycosylation, folding, and intracellular transport of newly synthesized glycoproteins
    • Marquardt, T., Ullrich, K., Zimmer, P., Hasilik, A., Deufel, T. & Harms, E. (1995) Carbohydrate-deficient glycoprotein syndrome (CDGS) - glycosylation, folding, and intracellular transport of newly synthesized glycoproteins. Eur. J. Cell Biol. 66, 268-273.
    • (1995) Eur. J. Cell Biol. , vol.66 , pp. 268-273
    • Marquardt, T.1    Ullrich, K.2    Zimmer, P.3    Hasilik, A.4    Deufel, T.5    Harms, E.6
  • 51
    • 0031964547 scopus 로고    scopus 로고
    • Cell surface glycoproteins undergo post-biosynthetic modification of their N-glycans by stepwise demannosylation
    • Porwoll, S., Loch, N., Kannicht, C., Nuck, R., Grunow, D., Reutter, W. & Tauber, R. (1998) Cell surface glycoproteins undergo post-biosynthetic modification of their N-glycans by stepwise demannosylation. J. Biol. Chem. 273, 1075-1085.
    • (1998) J. Biol. Chem. , vol.273 , pp. 1075-1085
    • Porwoll, S.1    Loch, N.2    Kannicht, C.3    Nuck, R.4    Grunow, D.5    Reutter, W.6    Tauber, R.7
  • 52
    • 0345040245 scopus 로고    scopus 로고
    • Nonglucosylated oligosaccharides are transferred to protein in MI8-5 Chinese hamster ovary cells
    • Quellhorst, G.J., Jr., O'Rear, J.L.O., Cacan, R., Verbert, A. & Kraep, S. (1999) Nonglucosylated oligosaccharides are transferred to protein in MI8-5 Chinese hamster ovary cells. Glycobiology 9, 65-72.
    • (1999) Glycobiology , vol.9 , pp. 65-72
    • Quellhorst G.J., Jr.1    O'Rear, J.L.O.2    Cacan, R.3    Verbert, A.4    Kraep, S.5
  • 53
    • 0030957595 scopus 로고    scopus 로고
    • A partial deficiency of dehydrodolichol reduction is a cause of carbohydrate-deficient glycoprotein syndrome type I
    • Ohkura, T., Fukushima, K., Kurisaki, A., Sagami, H., Ogura, K., Ohno, K., Hara-Kuge, S. & Yamashita, K. (1997) A partial deficiency of dehydrodolichol reduction is a cause of carbohydrate-deficient glycoprotein syndrome type I. J. Biol. Chem. 272, 6868-6875.
    • (1997) J. Biol. Chem. , vol.272 , pp. 6868-6875
    • Ohkura, T.1    Fukushima, K.2    Kurisaki, A.3    Sagami, H.4    Ogura, K.5    Ohno, K.6    Hara-Kuge, S.7    Yamashita, K.8
  • 54
    • 0023227217 scopus 로고
    • Primary defect of congenital dyserythropoietic anemia type II. Failure in glycosylation of erythrocyte lactosaminoglycan proteins caused by lowered N-acetylglucosaminyl-transferase II
    • Fukuda, M.N., Dell, A. & Scartezzini, P. (1987) Primary defect of congenital dyserythropoietic anemia type II. Failure in glycosylation of erythrocyte lactosaminoglycan proteins caused by lowered N-acetylglucosaminyl-transferase II. J. Biol. Chem. 262, 7195-7206.
    • (1987) J. Biol. Chem. , vol.262 , pp. 7195-7206
    • Fukuda, M.N.1    Dell, A.2    Scartezzini, P.3
  • 55
    • 0030775892 scopus 로고    scopus 로고
    • Exclusion of three candidate genes as determinants of congenital dyserythropoietic anemia type II (CDAII)
    • Iolascon, A. de Giudice, E.M., Perratta, S., Granatiero, M., Zelante, L. & Gasparini, P. (1997) Exclusion of three candidate genes as determinants of congenital dyserythropoietic anemia type II (CDAII) Blood 90, 4197-4200.
    • (1997) Blood , vol.90 , pp. 4197-4200
    • Iolascon, A.1    De Giudice, E.M.2    Perratta, S.3    Granatiero, M.4    Zelante, L.5    Gasparini, P.6
  • 56
    • 16944367512 scopus 로고    scopus 로고
    • Localization of the congenital dyserythropoietic anemia II locus to chromosome 20qII.2 by genomewide search
    • Gasparini, P., del Givdice, E.M. & Delaunnay, J. (1997) Localization of the congenital dyserythropoietic anemia II locus to chromosome 20qII.2 by genomewide search. Am. J. Hum. Genet. 61, 1112-1116.
    • (1997) Am. J. Hum. Genet. , vol.61 , pp. 1112-1116
    • Gasparini, P.1    Del Givdice, E.M.2    Delaunnay, J.3
  • 57
    • 0028131707 scopus 로고
    • Linkage of a locus for carbohydrate-deficient glycoprotein syndrome type I (CDG1) to chromosome 16p, and linkage dis-equilibrium to microsatellite marker D16S-406
    • Martinsson, T., Bjursell, C., Stibler, H., Kristiansson, B., Skovby, F., Jaeken, J., Blennow, G., Stromme, P., Hanefeld, F. & Wahlstrom, J. (1994) Linkage of a locus for carbohydrate-deficient glycoprotein syndrome type I (CDG1) to chromosome 16p, and linkage dis-equilibrium to microsatellite marker D16S-406. Hum. Mol. Genet. 3, 2037-2042.
    • (1994) Hum. Mol. Genet. , vol.3 , pp. 2037-2042
    • Martinsson, T.1    Bjursell, C.2    Stibler, H.3    Kristiansson, B.4    Skovby, F.5    Jaeken, J.6    Blennow, G.7    Stromme, P.8    Hanefeld, F.9    Wahlstrom, J.10
  • 58
    • 0031081725 scopus 로고    scopus 로고
    • Fine mapping of the gene for carbohydrate-deficient glycoprotein syndrome, type I (CDG1): Linkage disequilibrium and founder effect in Scandinavian families
    • Bjursell, C., Stibler, H., Wahlström, J., Kristiansson, B., Skovby, F., Strömme, P., Blennow, G. & Martinsson, T. (1997) Fine mapping of the gene for carbohydrate-deficient glycoprotein syndrome, type I (CDG1): Linkage disequilibrium and founder effect in Scandinavian families. Genomics 39, 247-253.
    • (1997) Genomics , vol.39 , pp. 247-253
    • Bjursell, C.1    Stibler, H.2    Wahlström, J.3    Kristiansson, B.4    Skovby, F.5    Strömme, P.6    Blennow, G.7    Martinsson, T.8
  • 59
    • 0031981557 scopus 로고    scopus 로고
    • Lack of homozygotes for the most frequent disease allele in carbohydrate-deficient glycoprotein syndrome type IA
    • Matthijs, G., Schollen, E., van Schaftingen, E., Cassiman, J.-J. & Jaeken, J. (1998) Lack of homozygotes for the most frequent disease allele in carbohydrate-deficient glycoprotein syndrome type IA. Am. J. Hum. Genet. 62, 542-550.
    • (1998) Am. J. Hum. Genet. , vol.62 , pp. 542-550
    • Matthijs, G.1    Schollen, E.2    Van Schaftingen, E.3    Cassiman, J.-J.4    Jaeken, J.5
  • 60
    • 0031854537 scopus 로고    scopus 로고
    • Absence of homozygosity for predominant mutations in PMM2 in Danish patients with carbohydrate-deficient glycoprotein syndrome type 1
    • Kjaergaard, S., Skovby, F. & Schwartz, M. (1998) Absence of homozygosity for predominant mutations in PMM2 in Danish patients with carbohydrate-deficient glycoprotein syndrome type 1. Eur. J. Hum. Genet. 6, 331-336.
    • (1998) Eur. J. Hum. Genet. , vol.6 , pp. 331-336
    • Kjaergaard, S.1    Skovby, F.2    Schwartz, M.3
  • 62
    • 0031568887 scopus 로고    scopus 로고
    • PMM (PMM1), the human homologue of SEC53 or yeast phosphomannomutase, is localized on chromosome 22q13
    • Matthijs, G., Schollen, E., Pirard, M., Budarf, M.L., van Schaftigen, E. & Cassiman, J.-J. (1997) PMM (PMM1), the human homologue of SEC53 or yeast phosphomannomutase, is localized on chromosome 22q13. Genomics 40, 41-47.
    • (1997) Genomics , vol.40 , pp. 41-47
    • Matthijs, G.1    Schollen, E.2    Pirard, M.3    Budarf, M.L.4    Van Schaftigen, E.5    Cassiman, J.-J.6
  • 63
    • 0030921189 scopus 로고    scopus 로고
    • Cloning and characterization of human phosphomannomutase, a mammalian homologue of yeast SEC53
    • Hansen, S.H., Frank, S.R., Casanova, J.E. (1997) Cloning and characterization of human phosphomannomutase, a mammalian homologue of yeast SEC53. Glycobiology 7, 829-834.
    • (1997) Glycobiology , vol.7 , pp. 829-834
    • Hansen, S.H.1    Frank, S.R.2    Casanova, J.E.3
  • 64
    • 0031567574 scopus 로고    scopus 로고
    • Comparison of PMM1 with the phosphomannomutase expressed in rat liver and in human cells
    • Pirard, M., Collet, J.-F., Matthijs, G. & van Schaftingen, E. (1997) Comparison of PMM1 with the phosphomannomutase expressed in rat liver and in human cells. FEBS Lett. 411, 251-254.
    • (1997) FEBS Lett. , vol.411 , pp. 251-254
    • Pirard, M.1    Collet, J.-F.2    Matthijs, G.3    Van Schaftingen, E.4
  • 65
    • 0031974540 scopus 로고    scopus 로고
    • Comparative analysis of the phosphomannomutase genes PMM1, PMM2 and PMM2ψ: The sequence variation in the processed pseudogene is a reflection of the mutations found in the functional gene
    • SchoUen, E., Pardon, E., Heykants, L., Renard, J., Doggett, N.A., Callen, D.F., Cassiman, J.-J. & Matthijs, G. (1998) Comparative analysis of the phosphomannomutase genes PMM1, PMM2 and PMM2ψ: The sequence variation in the processed pseudogene is a reflection of the mutations found in the functional gene. Hum. Molec. Genet. 7, 157-164.
    • (1998) Hum. Molec. Genet. , vol.7 , pp. 157-164
    • Schouen, E.1    Pardon, E.2    Heykants, L.3    Renard, J.4    Doggett, N.A.5    Callen, D.F.6    Cassiman, J.-J.7    Matthijs, G.8
  • 66
    • 0028980935 scopus 로고
    • The human UDP-N-acetylglucosamine: Alpha-6-D-manoside-beta-1,2-N-acetylglucosaminyl-transferase II gene (MGAT2) -cloning of genomic DNA, localization to chromosome 14q21, expression in insect cells and purification of the recombinant protein
    • Tan, J., D'Agostaro, G.A.F., Bendiak, B., Reck, F., Sarkar, M., Squire, J.A. & Leong, P. (1995) The human UDP-N-acetylglucosamine: Alpha-6-D-manoside-beta-1,2-N-acetylglucosaminyl-transferase II gene (MGAT2) -cloning of genomic DNA, localization to chromosome 14q21, expression in insect cells and purification of the recombinant protein. Eur. J. Biochem. 231, 317-328.
    • (1995) Eur. J. Biochem. , vol.231 , pp. 317-328
    • Tan, J.1    D'Agostaro, G.A.F.2    Bendiak, B.3    Reck, F.4    Sarkar, M.5    Squire, J.A.6    Leong, P.7
  • 67
    • 0029820486 scopus 로고    scopus 로고
    • Mutations in the MGAT2 gene controlling complex N-glycan synthesis cause carbohydrate-deficient glycoprotein syndrome type II, an autosomal recessive disease with defective brain development
    • Tan, J., Dunn, J., Jaeken, J. & Schachter, H. (1996) Mutations in the MGAT2 gene controlling complex N-glycan synthesis cause carbohydrate-deficient glycoprotein syndrome type II, an autosomal recessive disease with defective brain development. Am. J. Hum. Genet. 59, 810-817.
    • (1996) Am. J. Hum. Genet. , vol.59 , pp. 810-817
    • Tan, J.1    Dunn, J.2    Jaeken, J.3    Schachter, H.4
  • 68
    • 0029984537 scopus 로고    scopus 로고
    • Mannose corrects altered N-glycosylation in carbohydrate-deficient glycoprotein syndrome fibroblasts
    • Panneerselvam, K. & Freeze, H.H. (1996) Mannose corrects altered N-glycosylation in carbohydrate-deficient glycoprotein syndrome fibroblasts. J. Clin. Invest. 97, 1478-1487.
    • (1996) J. Clin. Invest. , vol.97 , pp. 1478-1487
    • Panneerselvam, K.1    Freeze, H.H.2
  • 69
    • 17744411208 scopus 로고    scopus 로고
    • Oral ingestion of mannose elevates blood mannose levels: A first step toward a potential therapy for carbohydrate-deficient glycoprotein syndrome type I
    • Alton, G., Kjaergaard, S., Etchison, J.R., Skovby, F. & Freeze, H.H. (1997) Oral ingestion of mannose elevates blood mannose levels: A first step toward a potential therapy for carbohydrate-deficient glycoprotein syndrome type I. Biol Mol. Med. 60, 127-133.
    • (1997) Biol Mol. Med. , vol.60 , pp. 127-133
    • Alton, G.1    Kjaergaard, S.2    Etchison, J.R.3    Skovby, F.4    Freeze, H.H.5
  • 70
    • 0029986487 scopus 로고    scopus 로고
    • Mannose enters mammalian cells using a specific transporter that is insensitive to glucose
    • Panneerselvam, K. & Freeze, H.H. (1996) Mannose enters mammalian cells using a specific transporter that is insensitive to glucose. J. Biol. Chem. 271, 9417-9421.
    • (1996) J. Biol. Chem. , vol.271 , pp. 9417-9421
    • Panneerselvam, K.1    Freeze, H.H.2
  • 71
    • 0030760044 scopus 로고    scopus 로고
    • Human fibroblasts prefer mannose over glucose as a source of mannose for N-glycosylation. Evidence for the functional importance of transported mannose
    • published erratum J. Biol. Chem. 272, 33444
    • Panneerselvam, K., Etchison, J.R. & Freeze, H.H. (1997) Human fibroblasts prefer mannose over glucose as a source of mannose for N-glycosylation. Evidence for the functional importance of transported mannose. J. Biol. Chem. 272, 23123-23129, published erratum J. Biol. Chem. 272, 33444.
    • (1997) J. Biol. Chem. , vol.272 , pp. 23123-23129
    • Panneerselvam, K.1    Etchison, J.R.2    Freeze, H.H.3
  • 72
    • 0014753459 scopus 로고
    • Specificity of monosaccharide transport in dog kidney
    • Silverman, M., Aganon, M.A. & Chinard, F.P. (1970) Specificity of monosaccharide transport in dog kidney. Am. J. Physiol. 218, 743-750.
    • (1970) Am. J. Physiol. , vol.218 , pp. 743-750
    • Silverman, M.1    Aganon, M.A.2    Chinard, F.P.3
  • 73
    • 0020120006 scopus 로고
    • Renal sugar transport in the winter flounder. VI. Reabsoption of D-mannose
    • Pritchard, J.B., Brooz, G.W. & Kleinzeller, A. (1982) Renal sugar transport in the winter flounder. VI. Reabsoption of D-mannose. Am. J. Physiol. 242, F415-F422.
    • (1982) Am. J. Physiol. , vol.242
    • Pritchard, J.B.1    Brooz, G.W.2    Kleinzeller, A.3
  • 75
    • 0030809002 scopus 로고    scopus 로고
    • Continuous mannose infusion in carbohydrate-deficient glycoprotein syndrome type I
    • Mayatepek, E., Schröder, M., Kohlmüller, D., Bieger, W.P. & Nützenadel, W. (1997) Continuous mannose infusion in carbohydrate-deficient glycoprotein syndrome type I. Acta Paediatr. 86, 1138-1140.
    • (1997) Acta Paediatr. , vol.86 , pp. 1138-1140
    • Mayatepek, E.1    Schröder, M.2    Kohlmüller, D.3    Bieger, W.P.4    Nützenadel, W.5
  • 76
    • 0027318961 scopus 로고
    • Biological roles of oligosaccharides: All of the theories are correct
    • Varki, A. (1993) Biological roles of oligosaccharides: All of the theories are correct. Glycobiology 3, 97-130.
    • (1993) Glycobiology , vol.3 , pp. 97-130
    • Varki, A.1
  • 77
    • 0032321747 scopus 로고    scopus 로고
    • Protein N-glycosylation: Molecular genetics and functional significance
    • Kukuruzinska, M.A. & Lennon, K. (1998) Protein N-glycosylation: Molecular genetics and functional significance. Crit. Rev. Oral Biol. Med. 9, 415-448.
    • (1998) Crit. Rev. Oral Biol. Med. , vol.9 , pp. 415-448
    • Kukuruzinska, M.A.1    Lennon, K.2
  • 78
    • 0032889255 scopus 로고    scopus 로고
    • Coagulation abnormalities in the carbohydrate-deficient glycoprotein syndrome: Case report and review of the literature
    • Young, G. & Driscoll, M.C. (1999) Coagulation abnormalities in the carbohydrate-deficient glycoprotein syndrome: Case report and review of the literature. Am. J. Hematol. 60, 66-69.
    • (1999) Am. J. Hematol. , vol.60 , pp. 66-69
    • Young, G.1    Driscoll, M.C.2
  • 79
    • 0029944861 scopus 로고    scopus 로고
    • Effect of exogenous decorin on cell morphology and attachment of decorin-deficient fibroblasts
    • Gu, J. & Wada, Y. (1996) Effect of exogenous decorin on cell morphology and attachment of decorin-deficient fibroblasts. J. Biochem. 119, 743-748.
    • (1996) J. Biochem. , vol.119 , pp. 743-748
    • Gu, J.1    Wada, Y.2
  • 80
    • 0029024820 scopus 로고
    • Aberrant expressions of decorin and biglycan genes in the carbohydrate-deficient glycoprotein syndrome
    • Gu, J. & Wada, Y. (1995) Aberrant expressions of decorin and biglycan genes in the carbohydrate-deficient glycoprotein syndrome. J. Biochem. 117, 1276-1279.
    • (1995) J. Biochem. , vol.117 , pp. 1276-1279
    • Gu, J.1    Wada, Y.2
  • 81
    • 0031004767 scopus 로고    scopus 로고
    • Brain contains HNK-1 immunoreactive O-glycans of the sulfoglucuronyl lactosamine series that terminate in 2-linked or 2,6-linked hexose (mannose)
    • Yuen, C.T., Chai, W., Loveless, R.W., Lawson, A.M., Hargdis, R.U. & Feizi, T. (1997) Brain contains HNK-1 immunoreactive O-glycans of the sulfoglucuronyl lactosamine series that terminate in 2-linked or 2,6-linked hexose (mannose). J. Biol. Chem. 272, 8924-8931.
    • (1997) J. Biol. Chem. , vol.272 , pp. 8924-8931
    • Yuen, C.T.1    Chai, W.2    Loveless, R.W.3    Lawson, A.M.4    Hargdis, R.U.5    Feizi, T.6
  • 82
    • 0031026624 scopus 로고    scopus 로고
    • Structures of sialylated O-linked oligosaccharides of bovine peripheral nerve α-dystroglycan. The role of a novel O-mannosyl-type oligosaccharide in the binding of α-dystroglycan with laminin
    • Chiba, A., Matsumura, K., Yomada, H., Inazu, T., Shimizu, T., Kusunoki, S., Kanazawa, I., Kobata, A. & Endo, T. (1997) Structures of sialylated O-linked oligosaccharides of bovine peripheral nerve α-dystroglycan. The role of a novel O-mannosyl-type oligosaccharide in the binding of α-dystroglycan with laminin. J. Biol. Chem. 272, 2156-2162.
    • (1997) J. Biol. Chem. , vol.272 , pp. 2156-2162
    • Chiba, A.1    Matsumura, K.2    Yomada, H.3    Inazu, T.4    Shimizu, T.5    Kusunoki, S.6    Kanazawa, I.7    Kobata, A.8    Endo, T.9
  • 83
    • 0032508544 scopus 로고    scopus 로고
    • Structural analysis of sequences O-linked to mannose reveals a novel Lewis X structure in craning (dystroglycan) purified from sheep brain
    • Smalheiser, N.R., Haslam, S.M., Button-Smith, M., Morns, H.R. & Dell, A. (1998) Structural analysis of sequences O-linked to mannose reveals a novel Lewis X structure in craning (dystroglycan) purified from sheep brain. J. Biol. Chem. 273, 23698-23703.
    • (1998) J. Biol. Chem. , vol.273 , pp. 23698-23703
    • Smalheiser, N.R.1    Haslam, S.M.2    Button-Smith, M.3    Morns, H.R.4    Dell, A.5
  • 84
    • 0031909015 scopus 로고    scopus 로고
    • Isoforms and levels of transferrin, antithrombin, alpha (1)-antitrypsin and thyroxin-binding globulin in 48 patients with carbohydrate-deficient glycoprotein syndrome type I
    • Stibler, H., Holzbach, U. & Kristiansson, B. (1998) Isoforms and levels of transferrin, antithrombin, alpha (1)-antitrypsin and thyroxin-binding globulin in 48 patients with carbohydrate-deficient glycoprotein syndrome type I. Scand. J. Clin. Lab. Invest. 58, 55-61.
    • (1998) Scand. J. Clin. Lab. Invest. , vol.58 , pp. 55-61
    • Stibler, H.1    Holzbach, U.2    Kristiansson, B.3
  • 85
    • 0031744335 scopus 로고    scopus 로고
    • Disorders in protein glycosylation and potential therapy: Tip of an iceberg?
    • Freeze, H.H. (1998) Disorders in protein glycosylation and potential therapy: Tip of an iceberg? J. Pediatr. 133, 593-600.
    • (1998) J. Pediatr. , vol.133 , pp. 593-600
    • Freeze, H.H.1


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