메뉴 건너뛰기




Volumn 39, Issue 6, 2016, Pages 765-780

Immunological aspects of congenital disorders of glycosylation (CDG): a review

Author keywords

[No Author keywords available]

Indexed keywords

ALPHA MANNOSIDASE; CARRIER PROTEINS AND BINDING PROTEINS; DOLICHOL KINASE; ISOMERASE; MAGNESIUM TRANSPORTER 1; MANNOSE OLIGOSACCHARIDE 1,2 ALPHA MANNOSIDASE; MANNOSYLOLIGOSACCHARIDE GLYCOSIDASE; PHOSPHOGLUCOMUTASE 3; PHOSPHOMANNOMUTASE 2; PHOSPHOTRANSFERASE; UNCLASSIFIED DRUG; URIDINE DIPHOSPHATE N ACETYLGLUCOSAMINE;

EID: 84978113399     PISSN: 01418955     EISSN: 15732665     Source Type: Journal    
DOI: 10.1007/s10545-016-9954-9     Document Type: Review
Times cited : (50)

References (123)
  • 1
    • 84884170771 scopus 로고    scopus 로고
    • Impaired NADPH oxidase activity in peripheral blood lymphocytes of galactosemia patients
    • Al-Essa M, Dhaunsi GS, Al-Qabandi W, Khan I (2013) Impaired NADPH oxidase activity in peripheral blood lymphocytes of galactosemia patients. Exp Biol Med 238:779–786
    • (2013) Exp Biol Med , vol.238 , pp. 779-786
    • Al-Essa, M.1    Dhaunsi, G.S.2    Al-Qabandi, W.3    Khan, I.4
  • 2
    • 77956185954 scopus 로고    scopus 로고
    • A novel role for the IgG Fc glycan: the anti-inflammatory activity of sialylated IgG Fcs
    • COI: 1:CAS:528:DC%2BC3cXntlOjtL8%3D, PID: 20480216
    • Anthony RM, Ravetch JV (2010) A novel role for the IgG Fc glycan: the anti-inflammatory activity of sialylated IgG Fcs. J Clin Immunol 30(Suppl 1):S9–14
    • (2010) J Clin Immunol , vol.30 , pp. S9-S14
    • Anthony, R.M.1    Ravetch, J.V.2
  • 3
    • 0032754473 scopus 로고    scopus 로고
    • On the frequency of protein glycosylation, as deduced from analysis of the SWISS-PROT database
    • COI: 1:CAS:528:DyaK1MXnsVKmt7o%3D, PID: 10580125
    • Apweiler R, Hermjakob H, Sharon N (1999) On the frequency of protein glycosylation, as deduced from analysis of the SWISS-PROT database. Biochim Biophys Acta 1473:4–8
    • (1999) Biochim Biophys Acta , vol.1473 , pp. 4-8
    • Apweiler, R.1    Hermjakob, H.2    Sharon, N.3
  • 4
    • 40849142196 scopus 로고    scopus 로고
    • Risk assessment of acute vascular events in congenital disorder of glycosylation type Ia
    • Arnoux JB, Boddaert N, Valayannopoulos V et al (2008) Risk assessment of acute vascular events in congenital disorder of glycosylation type Ia. Mol Genet Metab 93:444–449
    • (2008) Mol Genet Metab , vol.93 , pp. 444-449
    • Arnoux, J.B.1    Boddaert, N.2    Valayannopoulos, V.3
  • 5
    • 36448952375 scopus 로고    scopus 로고
    • CD1 antigen presentation: how it works
    • COI: 1:CAS:528:DC%2BD2sXhtlCrsLzK, PID: 18037897
    • Barral DC, Brenner MB (2007) CD1 antigen presentation: how it works. Nat Rev Immunol 7:929–941
    • (2007) Nat Rev Immunol , vol.7 , pp. 929-941
    • Barral, D.C.1    Brenner, M.B.2
  • 6
    • 67649827394 scopus 로고    scopus 로고
    • Glycoimmunology: ignore at your peril!
    • COI: 1:CAS:528:DC%2BD1MXhsFGls7bP, PID: 19594625
    • Baum LG, Crocker PR (2009) Glycoimmunology: ignore at your peril! Immunol Rev 230:5–8
    • (2009) Immunol Rev , vol.230 , pp. 5-8
    • Baum, L.G.1    Crocker, P.R.2
  • 7
    • 0031669243 scopus 로고    scopus 로고
    • Abnormal surface expression of sialoglycans on B lymphocyte cell lines from patients with carbohydrate deficient glycoprotein syndrome I A (CDGS I A)
    • COI: 1:CAS:528:DyaK1cXmsFOktLk%3D, PID: 9719677
    • Bergmann M, Gross HJ, Abdelatty F, Möller P, Jaeken J, Schwartz-Albiez R (1998) Abnormal surface expression of sialoglycans on B lymphocyte cell lines from patients with carbohydrate deficient glycoprotein syndrome I A (CDGS I A). Glycobiology 8:963–972
    • (1998) Glycobiology , vol.8 , pp. 963-972
    • Bergmann, M.1    Gross, H.J.2    Abdelatty, F.3    Möller, P.4    Jaeken, J.5    Schwartz-Albiez, R.6
  • 8
    • 84991371044 scopus 로고
    • Classic galactosemia and clinical variant galactosemia. In Pagon RA, Adam MP
    • Eds.) GeneReviews, Seattle
    • Berry GT (1993) Classic galactosemia and clinical variant galactosemia. In Pagon RA, Adam MP, Ardinger HH et al (Eds.) GeneReviews, Seattle
    • (1993) Ardinger HH et al
    • Berry, G.T.1
  • 9
    • 84931572301 scopus 로고    scopus 로고
    • Classic galactosemia and clinical variant galactosemia
    • GeneReviews, Seattle
    • Berry G (2000) Classic galactosemia and clinical variant galactosemia. GeneReviews, Seattle
    • (2000)
    • Berry, G.1
  • 11
    • 34249895141 scopus 로고    scopus 로고
    • Recurrent infections and immunological dysfunction in congenital disorder of glycosylation Ia (CDG Ia)
    • COI: 1:CAS:528:DC%2BD28Xnsl2ju7o%3D, PID: 16826448
    • Blank C, Smith LA, Hammer DA (2006) Recurrent infections and immunological dysfunction in congenital disorder of glycosylation Ia (CDG Ia). J Inherit Metab Dis 29:592
    • (2006) J Inherit Metab Dis , vol.29 , pp. 592
    • Blank, C.1    Smith, L.A.2    Hammer, D.A.3
  • 12
    • 33746867852 scopus 로고    scopus 로고
    • Classical galactosaemia revisited
    • COI: 1:CAS:528:DC%2BD28Xnsl2ju7k%3D, PID: 16838075
    • Bosch AM (2006) Classical galactosaemia revisited. J Inherit Metab Dis 29:516–525
    • (2006) J Inherit Metab Dis , vol.29 , pp. 516-525
    • Bosch, A.M.1
  • 13
    • 84957438729 scopus 로고    scopus 로고
    • Inflammatory markers in pediatric stroke: an attempt to better understanding the pathophysiology
    • PID: 26778232
    • Buerki SE, Grandgirard D, Datta AN et al (2016) Inflammatory markers in pediatric stroke: an attempt to better understanding the pathophysiology. Eur J Paediatr Neurol 20:252–60
    • (2016) Eur J Paediatr Neurol , vol.20 , pp. 252-260
    • Buerki, S.E.1    Grandgirard, D.2    Datta, A.N.3
  • 14
    • 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
    • COI: 1:CAS:528:DC%2BD3sXotFKrsL4%3D, PID: 12773475
    • Butler M, Quelhas D, Critchley AJ et al (2003) 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 13:601–622
    • (2003) Glycobiology , vol.13 , pp. 601-622
    • Butler, M.1    Quelhas, D.2    Critchley, A.J.3
  • 15
  • 16
    • 84937564714 scopus 로고    scopus 로고
    • Viral resistance of MOGS-CDG patients implies a broad-spectrum strategy against acute virus infections
    • PID: 25318123
    • Chang J, Block TM, Guo JT (2015) Viral resistance of MOGS-CDG patients implies a broad-spectrum strategy against acute virus infections. Antivir Ther 20:257–259
    • (2015) Antivir Ther , vol.20 , pp. 257-259
    • Chang, J.1    Block, T.M.2    Guo, J.T.3
  • 17
    • 18544384105 scopus 로고    scopus 로고
    • Congenital disorders of glycosylation type Ig is defined by a deficiency in dolichyl-P-mannose:Man7GlcNAc2-PP-dolichyl mannosyltransferase
    • COI: 1:CAS:528:DC%2BD38XlsVWhtLw%3D, PID: 11983712
    • Chantret I, Dupré T, Delenda C et al (2002) Congenital disorders of glycosylation type Ig is defined by a deficiency in dolichyl-P-mannose:Man7GlcNAc2-PP-dolichyl mannosyltransferase. J Biol Chem 277:25815–25822
    • (2002) J Biol Chem , vol.277 , pp. 25815-25822
    • Chantret, I.1    Dupré, T.2    Delenda, C.3
  • 18
    • 43449103089 scopus 로고    scopus 로고
    • The skeletal manifestations of the congenital disorders of glycosylation
    • COI: 1:CAS:528:DC%2BD1cXhsVOnsrrL, PID: 18462449
    • Coman D, Irving M, Kannu P, Jaeken J, Savarirayan R (2008) The skeletal manifestations of the congenital disorders of glycosylation. Clin Genet 73:507–515
    • (2008) Clin Genet , vol.73 , pp. 507-515
    • Coman, D.1    Irving, M.2    Kannu, P.3    Jaeken, J.4    Savarirayan, R.5
  • 19
    • 84893869670 scopus 로고    scopus 로고
    • N-glycan abnormalities in children with galactosemia
    • COI: 1:CAS:528:DC%2BC3sXhvFaltL%2FJ, PID: 24359113
    • Coss KP, Hawkes CP, Adamczyk B et al (2014) N-glycan abnormalities in children with galactosemia. J Proteome Res 13:385–94
    • (2014) J Proteome Res , vol.13 , pp. 385-394
    • Coss, K.P.1    Hawkes, C.P.2    Adamczyk, B.3
  • 20
  • 21
    • 84899977749 scopus 로고    scopus 로고
    • Congenital disorder of fucosylation type 2c (LADII) presenting with short stature and developmental delay with minimal adhesion defect
    • COI: 1:CAS:528:DC%2BC2cXnslCqsLk%3D, PID: 24403049
    • Dauber A, Ercan A, Lee J et al (2014) Congenital disorder of fucosylation type 2c (LADII) presenting with short stature and developmental delay with minimal adhesion defect. Hum Mol Genet 23:2880–2887
    • (2014) Hum Mol Genet , vol.23 , pp. 2880-2887
    • Dauber, A.1    Ercan, A.2    Lee, J.3
  • 22
    • 70249092078 scopus 로고    scopus 로고
    • MGAT2 deficiency (CDG-IIa): the life of J
    • PID: 19419693
    • de Cock P, Jaeken J (2009) MGAT2 deficiency (CDG-IIa): the life of J. Biochim Biophys Acta 1792:844–846
    • (2009) Biochim Biophys Acta , vol.1792 , pp. 844-846
    • de Cock, P.1    Jaeken, J.2
  • 23
    • 0027410273 scopus 로고
    • Inflammation-induced expression of sialyl Lewis X-containing glycan structures on alpha 1-acid glycoprotein (orosomucoid) in human sera
    • PID: 7679706
    • De Graaf TW, Van der Stelt ME, Anbergen MG, van Dijk W (1993) Inflammation-induced expression of sialyl Lewis X-containing glycan structures on alpha 1-acid glycoprotein (orosomucoid) in human sera. J Exp Med 177:657–666
    • (1993) J Exp Med , vol.177 , pp. 657-666
    • De Graaf, T.W.1    Van der Stelt, M.E.2    Anbergen, M.G.3    van Dijk, W.4
  • 25
    • 0035136834 scopus 로고    scopus 로고
    • A broad spectrum of clinical presentations in congenital disorders of glycosylation I: a series of 26 cases
    • PID: 11134235
    • de Lonlay P, Seta N, Barrot S et al (2001) A broad spectrum of clinical presentations in congenital disorders of glycosylation I: a series of 26 cases. J Med Genet 38:14–19
    • (2001) J Med Genet , vol.38 , pp. 14-19
    • de Lonlay, P.1    Seta, N.2    Barrot, S.3
  • 26
    • 0033939884 scopus 로고    scopus 로고
    • A novel disorder caused by defective biosynthesis of N-linked oligosaccharides due to glucosidase I deficiency
    • PID: 10788335
    • De Praeter CM, Gerwig GJ, Bause E et al (2000) A novel disorder caused by defective biosynthesis of N-linked oligosaccharides due to glucosidase I deficiency. Am J Hum Genet 66:1744–1756
    • (2000) Am J Hum Genet , vol.66 , pp. 1744-1756
    • De Praeter, C.M.1    Gerwig, G.J.2    Bause, E.3
  • 27
    • 84924745297 scopus 로고    scopus 로고
    • GALNT3 gene mutation-associated chronic recurrent multifocal osteomyelitis and familial hyperphosphatemic familial tumoral calcinosis
    • PID: 25351881
    • Demellawy DE, Chang N, de Nanassy J, Nasr A (2015) GALNT3 gene mutation-associated chronic recurrent multifocal osteomyelitis and familial hyperphosphatemic familial tumoral calcinosis. Scand J Rheumatol 44:170–172
    • (2015) Scand J Rheumatol , vol.44 , pp. 170-172
    • Demellawy, D.E.1    Chang, N.2    de Nanassy, J.3    Nasr, A.4
  • 28
    • 84925536233 scopus 로고    scopus 로고
    • Identification of a novel mutation in MAGT1 and progressive multifocal leucoencephalopathy in a 58-year-old man with XMEN disease
    • Dhalla F, Murray S, Sadler R et al (2015) Identification of a novel mutation in MAGT1 and progressive multifocal leucoencephalopathy in a 58-year-old man with XMEN disease. J Clin Immunol 35:112–118
    • (2015) J Clin Immunol , vol.35 , pp. 112-118
    • Dhalla, F.1    Murray, S.2    Sadler, R.3
  • 29
    • 31644444886 scopus 로고    scopus 로고
    • Congenital disorder of glycosylation (CDG) Ig: report on a patient and review of the literature
    • PID: 16435218
    • Di Rocco M, Hennet T, Grubenmann CE et al (2005) Congenital disorder of glycosylation (CDG) Ig: report on a patient and review of the literature. J Inherit Metab Dis 28:1162–1164
    • (2005) J Inherit Metab Dis , vol.28 , pp. 1162-1164
    • Di Rocco, M.1    Hennet, T.2    Grubenmann, C.E.3
  • 30
    • 0034491915 scopus 로고    scopus 로고
    • Defect in N-glycosylation of proteins is tissue-dependent in congenital disorders of glycosylation Ia
    • PID: 11159919
    • Dupré T, Barnier A, de Lonlay P et al (2000) Defect in N-glycosylation of proteins is tissue-dependent in congenital disorders of glycosylation Ia. Glycobiology 10:1277–1281
    • (2000) Glycobiology , vol.10 , pp. 1277-1281
    • Dupré, T.1    Barnier, A.2    de Lonlay, P.3
  • 31
    • 11444252182 scopus 로고    scopus 로고
    • Molecular and clinical description of the first US patients with congenital disorder of glycosylation Ig
    • COI: 1:CAS:528:DC%2BD2MXis1Sqsg%3D%3D, PID: 15639192
    • Eklund EA, Newell JW, Sun L et al (2005) Molecular and clinical description of the first US patients with congenital disorder of glycosylation Ig. Mol Genet Metab 84:25–31
    • (2005) Mol Genet Metab , vol.84 , pp. 25-31
    • Eklund, E.A.1    Newell, J.W.2    Sun, L.3
  • 32
    • 0034210961 scopus 로고    scopus 로고
    • Fucose supplementation in leukocyte adhesion deficiency type II
    • COI: 1:CAS:528:DC%2BD3cXjsl2it7g%3D, PID: 10877554
    • Etzioni A, Tonetti M (2000) Fucose supplementation in leukocyte adhesion deficiency type II. Blood 95:3641–3643
    • (2000) Blood , vol.95 , pp. 3641-3643
    • Etzioni, A.1    Tonetti, M.2
  • 33
    • 0026448082 scopus 로고
    • Brief report: recurrent severe infections caused by a novel leukocyte adhesion deficiency
    • COI: 1:STN:280:DyaK3s%2FmtlWgsQ%3D%3D, PID: 1279426
    • Etzioni A, Frydman M, Pollack S et al (1992) Brief report: recurrent severe infections caused by a novel leukocyte adhesion deficiency. N Engl J Med 327:1789–1792
    • (1992) N Engl J Med , vol.327 , pp. 1789-1792
    • Etzioni, A.1    Frydman, M.2    Pollack, S.3
  • 34
    • 84857061299 scopus 로고    scopus 로고
    • Genetic disorders of glycosylation
    • Varki A, Cummings R, Esko J, (eds), Cold Spring Harbor Laboratory Press, New York
    • Freeze H, Schachter H et al (2009) Genetic disorders of glycosylation. In: Varki A, Cummings R, Esko J (eds) Essentials of glycobiology, 2nd edn. Cold Spring Harbor Laboratory Press, New York
    • (2009) Essentials of glycobiology
    • Freeze, H.1    Schachter, H.2
  • 35
    • 0026758991 scopus 로고
    • Rambam-Hasharon syndrome of psychomotor retardation, short stature, defective neutrophil motility, and Bombay phenotype
    • COI: 1:STN:280:DyaK3s7kt1Oqsw%3D%3D, PID: 1488976
    • Frydman M, Etzioni A, Eidlitz-Markus T et al (1992) Rambam-Hasharon syndrome of psychomotor retardation, short stature, defective neutrophil motility, and Bombay phenotype. Am J Med Genet 44:297–302
    • (1992) Am J Med Genet , vol.44 , pp. 297-302
    • Frydman, M.1    Etzioni, A.2    Eidlitz-Markus, T.3
  • 36
    • 84865365078 scopus 로고    scopus 로고
    • Insights into complexity of congenital disorders of glycosylation
    • COI: 1:CAS:528:DC%2BC38XhsVens7jK
    • Goreta SS, Dabelic S, Dumic J (2012) Insights into complexity of congenital disorders of glycosylation. Biochem Med 22:156–170
    • (2012) Biochem Med , vol.22 , pp. 156-170
    • Goreta, S.S.1    Dabelic, S.2    Dumic, J.3
  • 37
    • 0037106328 scopus 로고    scopus 로고
    • ALG12 mannosyltransferase defect in congenital disorder of glycosylation type lg
    • COI: 1:CAS:528:DC%2BD38XmvVamu7s%3D, PID: 12217961
    • Grubenmann CE, Frank CG, Kjaergaard S, Berger EG, Aebi M, Hennet T (2002) ALG12 mannosyltransferase defect in congenital disorder of glycosylation type lg. Hum Mol Genet 11:2331–2339
    • (2002) Hum Mol Genet , vol.11 , pp. 2331-2339
    • Grubenmann, C.E.1    Frank, C.G.2    Kjaergaard, S.3    Berger, E.G.4    Aebi, M.5    Hennet, T.6
  • 38
    • 1542329546 scopus 로고    scopus 로고
    • Deficiency of the first mannosylation step in the N-glycosylation pathway causes congenital disorder of glycosylation type Ik
    • COI: 1:CAS:528:DC%2BD2cXht1Klu78%3D, PID: 14709599
    • Grubenmann CE, Frank CG, Hülsmeier AJ et al (2004) Deficiency of the first mannosylation step in the N-glycosylation pathway causes congenital disorder of glycosylation type Ik. Hum Mol Genet 13:535–542
    • (2004) Hum Mol Genet , vol.13 , pp. 535-542
    • Grubenmann, C.E.1    Frank, C.G.2    Hülsmeier, A.J.3
  • 39
    • 70349089028 scopus 로고    scopus 로고
    • The clinical spectrum of phosphomannomutase 2 deficiency (CDG-Ia)
    • PID: 19272306
    • Grunewald S (2009) The clinical spectrum of phosphomannomutase 2 deficiency (CDG-Ia). Biochim Biophys Acta 1792:827–834
    • (2009) Biochim Biophys Acta , vol.1792 , pp. 827-834
    • Grunewald, S.1
  • 42
    • 84898961017 scopus 로고    scopus 로고
    • N-glycosylation deficiency reduces ICAM-1 induction and impairs inflammatory response
    • COI: 1:CAS:528:DC%2BC2cXktlert70%3D, PID: 24474243
    • He P, Srikrishna G, Freeze HH (2014) N-glycosylation deficiency reduces ICAM-1 induction and impairs inflammatory response. Glycobiology 24:392–398
    • (2014) Glycobiology , vol.24 , pp. 392-398
    • He, P.1    Srikrishna, G.2    Freeze, H.H.3
  • 43
    • 33646580079 scopus 로고    scopus 로고
    • Leukocyte adhesion deficiency II patients with a dual defect of the GDP-fucose transporter
    • Helmus Y, Denecke J, Yakubenia S et al (2006) Leukocyte adhesion deficiency II patients with a dual defect of the GDP-fucose transporter. Blood 107:3959–3966
    • (2006) Blood , vol.107 , pp. 3959-3966
    • Helmus, Y.1    Denecke, J.2    Yakubenia, S.3
  • 44
    • 0031887163 scopus 로고    scopus 로고
    • Pericardial effusion in glycanosis CDG type I (MIM 212 065): an inflammatory endoplasmic reticulum overload response?
    • COI: 1:STN:280:DyaK1c7mtlehtg%3D%3D, PID: 9504796
    • Heyne K, Mayatepek E, Walther F, Weidinger S, Pahl HL (1998) Pericardial effusion in glycanosis CDG type I (MIM 212 065): an inflammatory endoplasmic reticulum overload response? Eur J Pediatr 157:168–169
    • (1998) Eur J Pediatr , vol.157 , pp. 168-169
    • Heyne, K.1    Mayatepek, E.2    Walther, F.3    Weidinger, S.4    Pahl, H.L.5
  • 45
    • 0037370699 scopus 로고    scopus 로고
    • Insights into leukocyte adhesion deficiency type 2 from a novel mutation in the GDP-fucose transporter gene
    • COI: 1:CAS:528:DC%2BD3sXhslCrsb8%3D, PID: 12406889
    • Hidalgo A, Ma S, Peired AJ, Weiss LA, Cunningham-Rundles C, Frenette PS (2003) Insights into leukocyte adhesion deficiency type 2 from a novel mutation in the GDP-fucose transporter gene. Blood 101:1705–1712
    • (2003) Blood , vol.101 , pp. 1705-1712
    • Hidalgo, A.1    Ma, S.2    Peired, A.J.3    Weiss, L.A.4    Cunningham-Rundles, C.5    Frenette, P.S.6
  • 46
    • 84901267574 scopus 로고    scopus 로고
    • Deficiency of subunit 6 of the conserved oligomeric golgi complex (COG6-CDG): second patient, different phenotype
    • COI: 1:STN:280:DC%2BC3svgsVagtQ%3D%3D, PID: 23430903
    • Huybrechts S, De Laet C, Bontems P et al (2012) Deficiency of subunit 6 of the conserved oligomeric golgi complex (COG6-CDG): second patient, different phenotype. JIMD Rep 4:103–108
    • (2012) JIMD Rep , vol.4 , pp. 103-108
    • Huybrechts, S.1    De Laet, C.2    Bontems, P.3
  • 47
    • 84949254878 scopus 로고    scopus 로고
    • Mutations in PIGY: expanding the phenotype of inherited glycosylphosphatidylinositol deficiencies
    • COI: 1:CAS:528:DC%2BC2MXitVykt7vO, PID: 26293662
    • Ilkovski B, Pagnamenta AT, O’Grady GL et al (2015) Mutations in PIGY: expanding the phenotype of inherited glycosylphosphatidylinositol deficiencies. Hum Mol Genet 24:6146–6159
    • (2015) Hum Mol Genet , vol.24 , pp. 6146-6159
    • Ilkovski, B.1    Pagnamenta, A.T.2    O’Grady, G.L.3
  • 48
    • 0034110643 scopus 로고    scopus 로고
    • Genotypes and phenotypes of patients in the UK with carbohydrate-deficient glycoprotein syndrome type I
    • COI: 1:CAS:528:DC%2BD3cXjtlyrsLc%3D, PID: 10801058
    • Imtiaz F, Worthington V, Champion M et al (2000) Genotypes and phenotypes of patients in the UK with carbohydrate-deficient glycoprotein syndrome type I. J Inherit Metab Dis 23:162–174
    • (2000) J Inherit Metab Dis , vol.23 , pp. 162-174
    • Imtiaz, F.1    Worthington, V.2    Champion, M.3
  • 49
    • 84867880363 scopus 로고    scopus 로고
    • MGAT2-CDG (CDG-IIa) and dysmorphism
    • PID: 23023920
    • Jaeken J (2012) MGAT2-CDG (CDG-IIa) and dysmorphism. Am J Med Genet 158A:2974–2975
    • (2012) Am J Med Genet , vol.158A , pp. 2974-2975
    • Jaeken, J.1
  • 50
    • 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-Lodeweyckx 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-Lodeweyckx, M.2    Casaer, P.3    Snoeck, L.4    Corbeel, L.5    Eggermont, E.6    Eeckels, R.7
  • 51
    • 0027432264 scopus 로고
    • Carbohydrate-deficient glycoprotein syndrome type II
    • COI: 1:STN:280:DyaK2c7nt12rsg%3D%3D, PID: 8127054
    • Jaeken J, De Cock P, Stibler H et al (1993) Carbohydrate-deficient glycoprotein syndrome type II. J Inherit Metab Dis 16:1041
    • (1993) J Inherit Metab Dis , vol.16 , pp. 1041
    • Jaeken, J.1    De Cock, P.2    Stibler, H.3
  • 52
    • 0027930443 scopus 로고
    • Carbohydrate deficient glycoprotein syndrome type II: a deficiency in Golgi localised N-acetyl-glucosaminyltransferase II
    • COI: 1:STN:280:DyaK2M%2FjtFaitw%3D%3D, PID: 7944531
    • Jaeken J, Schachter H, Carchon H, De Cock P, Coddeville B, Spik G (1994) Carbohydrate deficient glycoprotein syndrome type II: a deficiency in Golgi localised N-acetyl-glucosaminyltransferase 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
  • 53
    • 0031019482 scopus 로고    scopus 로고
    • Carbohydrate deficient glycoprotein (CDG) syndrome type I
    • COI: 1:STN:280:DyaK2s7osVyrtg%3D%3D, PID: 9032653
    • Jaeken J, Matthijs G, Barone R, Carchon H (1997) Carbohydrate deficient glycoprotein (CDG) syndrome 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
  • 54
  • 55
    • 0027299744 scopus 로고
    • Sialyltransferase: a novel acute-phase reactant
    • COI: 1:STN:280:DyaK3s3nvV2qsQ%3D%3D, PID: 7684961
    • Jamieson JC, McCaffrey G, Harder PG (1993) Sialyltransferase: a novel acute-phase reactant. Comp Biochem Physiol B 105:29–33
    • (1993) Comp Biochem Physiol B , vol.105 , pp. 29-33
    • Jamieson, J.C.1    McCaffrey, G.2    Harder, P.G.3
  • 56
    • 3042937932 scopus 로고    scopus 로고
    • T cell recognition of Tn-glycosylated peptide antigens
    • COI: 1:CAS:528:DyaK28Xks1egt7o%3D, PID: 8647215
    • Jensen T, Galli-Stampino L, Mouritsen S et al (1996) T cell recognition of Tn-glycosylated peptide antigens. Eur J Immunol 26:1342–9
    • (1996) Eur J Immunol , vol.26 , pp. 1342-1349
    • Jensen, T.1    Galli-Stampino, L.2    Mouritsen, S.3
  • 57
    • 84879464716 scopus 로고    scopus 로고
    • From discrete dilated cardiomyopathy to successful cardiac transplantation in congenital disorders of glycosylation due to dolichol kinase deficiency (DK1-CDG)
    • COI: 1:CAS:528:DC%2BC3sXjvFeqt7c%3D, PID: 22327749
    • Kapusta L, Zucker N, Frenckel G et al (2013) From discrete dilated cardiomyopathy to successful cardiac transplantation in congenital disorders of glycosylation due to dolichol kinase deficiency (DK1-CDG). Heart Fail Rev 18:187–196
    • (2013) Heart Fail Rev , vol.18 , pp. 187-196
    • Kapusta, L.1    Zucker, N.2    Frenckel, G.3
  • 58
    • 0034821669 scopus 로고    scopus 로고
    • Congenital disorder of glycosylation type Ia (CDG-Ia): phenotypic spectrum of the R141H/F119L genotype
    • COI: 1:STN:280:DC%2BD3MvntFOlsw%3D%3D, PID: 11517108
    • Kjaergaard S, Schwartz M, Skovby F (2001) Congenital disorder of glycosylation type Ia (CDG-Ia): phenotypic spectrum of the R141H/F119L genotype. Arch Dis Child 85:236–239
    • (2001) Arch Dis Child , vol.85 , pp. 236-239
    • Kjaergaard, S.1    Schwartz, M.2    Skovby, F.3
  • 59
    • 0021076548 scopus 로고
    • Galactose inhibition of neonatal neutrophil function
    • COI: 1:STN:280:DyaL2c%2FpsFWkug%3D%3D, PID: 6657498
    • Kobayashi RH, Kettelhut BV, Kobayashi AL (1983) Galactose inhibition of neonatal neutrophil function. Pediatr Infect Dis 2:442–445
    • (1983) Pediatr Infect Dis , vol.2 , pp. 442-445
    • Kobayashi, R.H.1    Kettelhut, B.V.2    Kobayashi, A.L.3
  • 60
    • 1542344374 scopus 로고    scopus 로고
    • Congenital disorder of glycosylation type Ik (CDG-Ik): a defect of mannosyltransferase I
    • COI: 1:CAS:528:DC%2BD2cXitV2gs7o%3D, PID: 14973782
    • Kranz C, Denecke J, Lehle L et al (2004) Congenital disorder of glycosylation type Ik (CDG-Ik): a defect of mannosyltransferase I. Am J Hum Genet 74:545–551
    • (2004) Am J Hum Genet , vol.74 , pp. 545-551
    • Kranz, C.1    Denecke, J.2    Lehle, L.3
  • 61
    • 34249884225 scopus 로고    scopus 로고
    • Expanding spectrum of congenital disorder of glycosylation Ig (CDG-Ig): sibs with a unique skeletal dysplasia, hypogammaglobulinemia, cardiomyopathy, genital malformations, and early lethality
    • COI: 1:CAS:528:DC%2BD2sXntlOhsr0%3D, PID: 17506107
    • Kranz C, Basinger AA, Güçsavaş-Calikoğlu M et al (2007a) Expanding spectrum of congenital disorder of glycosylation Ig (CDG-Ig): sibs with a unique skeletal dysplasia, hypogammaglobulinemia, cardiomyopathy, genital malformations, and early lethality. Am J Med Genet A 143A:1371–1378
    • (2007) Am J Med Genet A , vol.143A , pp. 1371-1378
    • Kranz, C.1    Basinger, A.A.2    Güçsavaş-Calikoğlu, M.3
  • 62
    • 33847228036 scopus 로고    scopus 로고
    • A defect in dolichol phosphate biosynthesis causes a new inherited disorder with death in early infancy
    • COI: 1:CAS:528:DC%2BD2sXit1Wlu7k%3D, PID: 17273964
    • Kranz C, Jungeblut C, Denecke J et al (2007b) A defect in dolichol phosphate biosynthesis causes a new inherited disorder with death in early infancy. Am J Hum Genet 80:433–440
    • (2007) Am J Hum Genet , vol.80 , pp. 433-440
    • Kranz, C.1    Jungeblut, C.2    Denecke, J.3
  • 63
    • 84871567838 scopus 로고    scopus 로고
    • An unusual presentation of galactosemia: hemophagocytic lymphohistiocytosis
    • PID: 24385729
    • Kundak AA, Zenciroğlu A, Yaralı N et al (2012) An unusual presentation of galactosemia: hemophagocytic lymphohistiocytosis. Turk J Haematol 29:401–404
    • (2012) Turk J Haematol , vol.29 , pp. 401-404
    • Kundak, A.A.1    Zenciroğlu, A.2    Yaralı, N.3
  • 64
    • 79960915373 scopus 로고    scopus 로고
    • Signaling role for Mg(2+) revealed by immunodeficiency due to loss of MagT1
    • COI: 1:CAS:528:DC%2BC3MXpsFaht78%3D, PID: 21796205
    • Li FY, Chaigne-Delalande B, Kanellopoulou C et al (2011) Signaling role for Mg(2+) revealed by immunodeficiency due to loss of MagT1. Nature 475:471–476
    • (2011) Nature , vol.475 , pp. 471-476
    • Li, F.Y.1    Chaigne-Delalande, B.2    Kanellopoulou, C.3
  • 65
    • 84897065262 scopus 로고    scopus 로고
    • Severe, fatal multisystem manifestations in a patient with dolichol kinase-congenital disorder of glycosylation
    • COI: 1:CAS:528:DC%2BC3sXhs1yqsLvE, PID: 24144945
    • Lieu MT, Ng BG, Rush JS et al (2013) Severe, fatal multisystem manifestations in a patient with dolichol kinase-congenital disorder of glycosylation. Mol Genet Metab 110:484–489
    • (2013) Mol Genet Metab , vol.110 , pp. 484-489
    • Lieu, M.T.1    Ng, B.G.2    Rush, J.S.3
  • 66
    • 0017806089 scopus 로고
    • Effect of galactose on free radical reactions of polymorphonuclear leukocytes
    • COI: 1:CAS:528:DyaE1cXkt1aisbo%3D, PID: 209746
    • Litchfield WJ, Wells WW (1978) Effect of galactose on free radical reactions of polymorphonuclear leukocytes. Arch Biochem Biophys 188:26–30
    • (1978) Arch Biochem Biophys , vol.188 , pp. 26-30
    • Litchfield, W.J.1    Wells, W.W.2
  • 67
    • 77956096967 scopus 로고    scopus 로고
    • Fatal outcome due to deficiency of subunit 6 of the conserved oligomeric Golgi complex leading to a new type of congenital disorders of glycosylation
    • PID: 20605848
    • Lübbehusen J, Thiel C, Rind N et al (2010) Fatal outcome due to deficiency of subunit 6 of the conserved oligomeric Golgi complex leading to a new type of congenital disorders of glycosylation. Hum Mol Genet 19:3623–3633
    • (2010) Hum Mol Genet , vol.19 , pp. 3623-3633
    • Lübbehusen, J.1    Thiel, C.2    Rind, N.3
  • 68
    • 0040293459 scopus 로고    scopus 로고
    • A new type of carbohydrate-deficient glycoprotein syndrome due to a decreased import of GDP-fucose into the golgi
    • PID: 10473542
    • Lübke T, Marquardt T, von Figura K, Körner C (1999) A new type of carbohydrate-deficient glycoprotein syndrome due to a decreased import of GDP-fucose into the golgi. J Biol Chem 274:25986–25989
    • (1999) J Biol Chem , vol.274 , pp. 25986-25989
    • Lübke, T.1    Marquardt, T.2    von Figura, K.3    Körner, C.4
  • 69
    • 0035165830 scopus 로고    scopus 로고
    • Discontinuation of fucose therapy in LADII causes rapid loss of selectin ligands and rise of leukocyte counts
    • PID: 11133780
    • Lühn K, Marquardt T, Harms E, Vestweber D (2001) Discontinuation of fucose therapy in LADII causes rapid loss of selectin ligands and rise of leukocyte counts. Blood 97:330–332
    • (2001) Blood , vol.97 , pp. 330-332
    • Lühn, K.1    Marquardt, T.2    Harms, E.3    Vestweber, D.4
  • 70
    • 84945280026 scopus 로고    scopus 로고
    • Susceptibility to infections, without concomitant hyper-IgE, reported in 1976, is caused by hypomorphic mutation in the phosphoglucomutase 3 (PGM3) gene
    • COI: 1:CAS:528:DC%2BC2MXhslWrurvJ, PID: 26482871
    • Lundin KE, Hamasy A, Backe PH et al (2015) Susceptibility to infections, without concomitant hyper-IgE, reported in 1976, is caused by hypomorphic mutation in the phosphoglucomutase 3 (PGM3) gene. Clin Immunol 161:366–372
    • (2015) Clin Immunol , vol.161 , pp. 366-372
    • Lundin, K.E.1    Hamasy, A.2    Backe, P.H.3
  • 71
    • 85119038728 scopus 로고    scopus 로고
    • Glycans instructing immunity: the emerging role of altered glycosylation in clinical immunology
    • PID: 26125015
    • Lyons JJ, Milner JD, Rosenzweig SD (2015) Glycans instructing immunity: the emerging role of altered glycosylation in clinical immunology. Front Pediatr 3:54
    • (2015) Front Pediatr , vol.3 , pp. 54
    • Lyons, J.J.1    Milner, J.D.2    Rosenzweig, S.D.3
  • 73
    • 0033506410 scopus 로고    scopus 로고
    • Leukocyte adhesion deficiency II syndrome, a generalized defect in fucose metabolism
    • COI: 1:STN:280:DyaK1M3osVKrtQ%3D%3D, PID: 10356134
    • Marquardt T, Brune T, Lühn K et al (1999a) Leukocyte adhesion deficiency II syndrome, a generalized defect in fucose metabolism. J Pediatr 134:681–688
    • (1999) J Pediatr , vol.134 , pp. 681-688
    • Marquardt, T.1    Brune, T.2    Lühn, K.3
  • 74
    • 0032763425 scopus 로고    scopus 로고
    • Correction of leukocyte adhesion deficiency type II with oral fucose
    • COI: 1:CAS:528:DyaK1MXnvFOjs7Y%3D, PID: 10590041
    • Marquardt T, Lühn K, Srikrishna G, Freeze HH, Harms E, Vestweber D (1999b) Correction of leukocyte adhesion deficiency type II with oral fucose. Blood 94:3976–3985
    • (1999) Blood , vol.94 , pp. 3976-3985
    • Marquardt, T.1    Lühn, K.2    Srikrishna, G.3    Freeze, H.H.4    Harms, E.5    Vestweber, D.6
  • 75
    • 0031005847 scopus 로고    scopus 로고
    • Mutations in PMM2, a phosphomannomutase gene on chromosome 16p13, in carbohydrate-deficient glycoprotein type I syndrome (Jaeken syndrome)
    • COI: 1:CAS:528:DyaK2sXivFKhsbg%3D, PID: 9140401
    • Matthijs G, Schollen E, Pardon E et al (1997) Mutations in PMM2, a phosphomannomutase gene on chromosome 16p13, in carbohydrate-deficient glycoprotein type I syndrome (Jaeken syndrome). Nat Genet 16:88–92
    • (1997) Nat Genet , vol.16 , pp. 88-92
    • Matthijs, G.1    Schollen, E.2    Pardon, E.3
  • 76
    • 0023949659 scopus 로고
    • Tumoral calcinosis revisited—common and uncommon features. Report of ten cases and review
    • COI: 1:STN:280:DyaL1c3htFGqtw%3D%3D, PID: 3366131
    • Metzker A, Eisenstein B, Oren J, Samuel R (1988) Tumoral calcinosis revisited—common and uncommon features. Report of ten cases and review. Eur J Pediatr 147:128–132
    • (1988) Eur J Pediatr , vol.147 , pp. 128-132
    • Metzker, A.1    Eisenstein, B.2    Oren, J.3    Samuel, R.4
  • 77
    • 42749084689 scopus 로고    scopus 로고
    • Oligosaccharyltransferase-subunit mutations in nonsyndromic mental retardation
    • COI: 1:CAS:528:DC%2BD1cXlvFeqt7o%3D, PID: 18455129
    • Molinari F, Foulquier F, Tarpey PS et al (2008) Oligosaccharyltransferase-subunit mutations in nonsyndromic mental retardation. Am J Hum Genet 82:1150–1157
    • (2008) Am J Hum Genet , vol.82 , pp. 1150-1157
    • Molinari, F.1    Foulquier, F.2    Tarpey, P.S.3
  • 78
    • 84964313430 scopus 로고    scopus 로고
    • 29 French adult patients with PMM2-congenital disorder of glycosylation: outcome of the classical pediatric phenotype and depiction of a late-onset phenotype
    • PID: 25497157
    • Monin ML, Mignot C, De Lonlay P et al (2014) 29 French adult patients with PMM2-congenital disorder of glycosylation: outcome of the classical pediatric phenotype and depiction of a late-onset phenotype. Orphanet J Rare Dis 9:207
    • (2014) Orphanet J Rare Dis , vol.9 , pp. 207
    • Monin, M.L.1    Mignot, C.2    De Lonlay, P.3
  • 79
    • 84867180277 scopus 로고    scopus 로고
    • Defining the phenotype in congenital disorder of glycosylation due to ALG1 mutations
    • PID: 22966035
    • Morava E, Vodopiutz J, Lefeber DJ et al (2012) Defining the phenotype in congenital disorder of glycosylation due to ALG1 mutations. Pediatrics 130:e1034–1039
    • (2012) Pediatrics , vol.130 , pp. e1034-e1039
    • Morava, E.1    Vodopiutz, J.2    Lefeber, D.J.3
  • 80
    • 0028213490 scopus 로고
    • Glycosidases of the asparagine-linked oligosaccharide processing pathway
    • COI: 1:CAS:528:DyaK2cXltVamtLw%3D, PID: 8054711
    • Moremen KW, Trimble RB, Herscovics A (1994) Glycosidases of the asparagine-linked oligosaccharide processing pathway. Glycobiology 4:113–125
    • (1994) Glycobiology , vol.4 , pp. 113-125
    • Moremen, K.W.1    Trimble, R.B.2    Herscovics, A.3
  • 81
    • 84905190318 scopus 로고    scopus 로고
    • Diagnosis of ALG12-CDG by exome sequencing in a case of severe skeletal dysplasia
    • COI: 1:CAS:528:DC%2BC2MXmtVamtLs%3D, PID: 25019053
    • Murali C, Lu JT, Jain M et al (2014) Diagnosis of ALG12-CDG by exome sequencing in a case of severe skeletal dysplasia. Mol Genet Metab Rep 1:213–219
    • (2014) Mol Genet Metab Rep , vol.1 , pp. 213-219
    • Murali, C.1    Lu, J.T.2    Jain, M.3
  • 82
    • 33751181881 scopus 로고    scopus 로고
    • Altered granulopoietic profile and exaggerated acute neutrophilic inflammation in mice with targeted deficiency in the sialyltransferase ST6Gal I
    • COI: 1:CAS:528:DC%2BD28Xht1ahsL%2FI, PID: 16849643
    • Nasirikenari M, Segal BH, Ostberg JR, Urbasic A, Lau JT (2006) Altered granulopoietic profile and exaggerated acute neutrophilic inflammation in mice with targeted deficiency in the sialyltransferase ST6Gal I. Blood 108:3397–3405
    • (2006) Blood , vol.108 , pp. 3397-3405
    • Nasirikenari, M.1    Segal, B.H.2    Ostberg, J.R.3    Urbasic, A.4    Lau, J.T.5
  • 83
    • 17444429987 scopus 로고    scopus 로고
    • Unusual presentation of congenital disorder of glycosylation type 1a: congenital persistent thrombocytopenia, hypertrophic cardiomyopathy and hydrops-like aspect due to marked peripheral oedema
    • PID: 15645285
    • Noelle V, Knuepfer M, Pulzer F et al (2005) Unusual presentation of congenital disorder of glycosylation type 1a: congenital persistent thrombocytopenia, hypertrophic cardiomyopathy and hydrops-like aspect due to marked peripheral oedema. Eur J Pediatr 164:223–226
    • (2005) Eur J Pediatr , vol.164 , pp. 223-226
    • Noelle, V.1    Knuepfer, M.2    Pulzer, F.3
  • 84
    • 77950355708 scopus 로고    scopus 로고
    • Retinal hemorrhages associated with meningitis in a child with a congenital disorder of glycosylation
    • PID: 19851897
    • Ong BB, Gole GA, Robertson T, McGill J, de Lore D, Crawford M (2009) Retinal hemorrhages associated with meningitis in a child with a congenital disorder of glycosylation. Forensic Sci Med Pathol 5:307–312
    • (2009) Forensic Sci Med Pathol , vol.5 , pp. 307-312
    • Ong, B.B.1    Gole, G.A.2    Robertson, T.3    McGill, J.4    de Lore, D.5    Crawford, M.6
  • 85
    • 68349117151 scopus 로고    scopus 로고
    • Long-term evolution of eight Spanish patients with CDG type Ia: typical and atypical manifestations
    • PID: 18948042
    • Pérez-Dueñas B, García-Cazorla A, Pineda M et al (2009) Long-term evolution of eight Spanish patients with CDG type Ia: typical and atypical manifestations. Eur J Paediatr Neurol 13:444–451
    • (2009) Eur J Paediatr Neurol , vol.13 , pp. 444-451
    • Pérez-Dueñas, B.1    García-Cazorla, A.2    Pineda, M.3
  • 86
    • 84881618216 scopus 로고    scopus 로고
    • XLID-causing mutations and associated genes challenged in light of data from large-scale human exome sequencing
    • COI: 1:CAS:528:DC%2BC3sXhtFCitrvO, PID: 23871722
    • Piton A, Redin C, Mandel JL (2013) XLID-causing mutations and associated genes challenged in light of data from large-scale human exome sequencing. Am J Hum Genet 93:368–383
    • (2013) Am J Hum Genet , vol.93 , pp. 368-383
    • Piton, A.1    Redin, C.2    Mandel, J.L.3
  • 87
    • 81855168333 scopus 로고    scopus 로고
    • Conserved oligomeric Golgi complex specifically regulates the maintenance of Golgi glycosylation machinery
    • COI: 1:CAS:528:DC%2BC3MXhsFSlu7fJ, PID: 21421995
    • Pokrovskaya ID, Willett R, Smith RD, Morelle W, Kudlyk T, Lupashin VV (2011) Conserved oligomeric Golgi complex specifically regulates the maintenance of Golgi glycosylation machinery. Glycobiology 21:1554–1569
    • (2011) Glycobiology , vol.21 , pp. 1554-1569
    • Pokrovskaya, I.D.1    Willett, R.2    Smith, R.D.3    Morelle, W.4    Kudlyk, T.5    Lupashin, V.V.6
  • 88
    • 0033679579 scopus 로고    scopus 로고
    • The ST3Gal-I sialyltransferase controls CD8+ T lymphocyte homeostasis by modulating O-glycan biosynthesis
    • COI: 1:CAS:528:DC%2BD3cXisVWku7o%3D, PID: 10755614
    • Priatel JJ, Chui D, Hiraoka N et al (2000) The ST3Gal-I sialyltransferase controls CD8+ T lymphocyte homeostasis by modulating O-glycan biosynthesis. Immunity 12:273–283
    • (2000) Immunity , vol.12 , pp. 273-283
    • Priatel, J.J.1    Chui, D.2    Hiraoka, N.3
  • 89
    • 0025785382 scopus 로고
    • A new variant of the carbohydrate deficient glycoproteins syndrome
    • COI: 1:STN:280:DyaK387it1Oktg%3D%3D, PID: 1770799
    • Ramaekers VT, Stibler H, Kint J, Jaeken J (1991) A new variant of the carbohydrate deficient glycoproteins syndrome. J Inherit Metab Dis 14:385–388
    • (1991) J Inherit Metab Dis , vol.14 , pp. 385-388
    • Ramaekers, V.T.1    Stibler, H.2    Kint, J.3    Jaeken, J.4
  • 90
    • 58249104091 scopus 로고    scopus 로고
    • Congenital disorder of glycosylation Ia: new differentially expressed proteins identified by 2-DE
    • COI: 1:CAS:528:DC%2BD1MXotlyrsQ%3D%3D, PID: 19101518
    • Richard E, Vega AI, Pérez B et al (2009) Congenital disorder of glycosylation Ia: new differentially expressed proteins identified by 2-DE. Biochem Biophys Res Commun 379:267–271
    • (2009) Biochem Biophys Res Commun , vol.379 , pp. 267-271
    • Richard, E.1    Vega, A.I.2    Pérez, B.3
  • 91
    • 84890435880 scopus 로고    scopus 로고
    • ALG1-CDG: a new case with early fatal outcome
    • COI: 1:CAS:528:DC%2BC3sXhslGntbzL, PID: 24157261
    • Rohlfing AK, Rust S, Reunert J et al (2014) ALG1-CDG: a new case with early fatal outcome. Gene 534:345–351
    • (2014) Gene , vol.534 , pp. 345-351
    • Rohlfing, A.K.1    Rust, S.2    Reunert, J.3
  • 92
    • 84893821185 scopus 로고    scopus 로고
    • Skin manifestations in CDG
    • COI: 1:CAS:528:DC%2BC2cXhsFGls73E, PID: 24554337
    • Rymen D, Jaeken J (2014) Skin manifestations in CDG. J Inherit Metab Dis 37:699–708
    • (2014) J Inherit Metab Dis , vol.37 , pp. 699-708
    • Rymen, D.1    Jaeken, J.2
  • 93
    • 84892685784 scopus 로고    scopus 로고
    • MAN1B1 deficiency: an unexpected CDG-II
    • PID: 24348268
    • Rymen D, Peanne R, Millón MB et al (2013) MAN1B1 deficiency: an unexpected CDG-II. PLoS Genet 9:e1003989
    • (2013) PLoS Genet , vol.9
    • Rymen, D.1    Peanne, R.2    Millón, M.B.3
  • 94
    • 84948716414 scopus 로고    scopus 로고
    • Key features and clinical variability of COG6-CDG
    • COI: 1:CAS:528:DC%2BC2MXhtlSnt7rE, PID: 26260076
    • Rymen D, Winter J, Van Hasselt PM et al (2015) Key features and clinical variability of COG6-CDG. Mol Genet Metab 116:163–170
    • (2015) Mol Genet Metab , vol.116 , pp. 163-170
    • Rymen, D.1    Winter, J.2    Van Hasselt, P.M.3
  • 95
    • 84899065140 scopus 로고    scopus 로고
    • Glycosylation, hypogammaglobulinemia, and resistance to viral infections
    • COI: 1:CAS:528:DC%2BC2cXnt1GrsrY%3D, PID: 24716661
    • Sadat MA, Moir S, Chun TW et al (2014) Glycosylation, hypogammaglobulinemia, and resistance to viral infections. N Engl J Med 370:1615–1625
    • (2014) N Engl J Med , vol.370 , pp. 1615-1625
    • Sadat, M.A.1    Moir, S.2    Chun, T.W.3
  • 96
    • 84942906413 scopus 로고    scopus 로고
    • N-glycosylation of serum IgG and total glycoproteins in MAN1B1 deficiency
    • COI: 1:CAS:528:DC%2BC2MXhsVegsr3N, PID: 26401844
    • Saldova R, Stöckmann H, O’Flaherty R, Lefeber DJ, Jaeken J, Rudd PM (2015) N-glycosylation of serum IgG and total glycoproteins in MAN1B1 deficiency. J Proteome Res 14:4402–4412
    • (2015) J Proteome Res , vol.14 , pp. 4402-4412
    • Saldova, R.1    Stöckmann, H.2    O’Flaherty, R.3    Lefeber, D.J.4    Jaeken, J.5    Rudd, P.M.6
  • 97
    • 84899629014 scopus 로고    scopus 로고
    • Hypomorphic homozygous mutations in phosphoglucomutase 3 (PGM3) impair immunity and increase serum IgE levels
    • COI: 1:CAS:528:DC%2BC2cXltl2gtrk%3D, PID: 24698316
    • Sassi A, Lazaroski S, Wu G et al (2014) Hypomorphic homozygous mutations in phosphoglucomutase 3 (PGM3) impair immunity and increase serum IgE levels. J Allergy Clin Immunol 133:1410–1419
    • (2014) J Allergy Clin Immunol , vol.133 , pp. 1410-1419
    • Sassi, A.1    Lazaroski, S.2    Wu, G.3
  • 98
    • 84904111497 scopus 로고    scopus 로고
    • Congenital disorders of glycosylation: new defects and still counting
    • COI: 1:CAS:528:DC%2BC2cXosVWqurs%3D, PID: 24831587
    • Scott K, Gadomski T, Kozicz T, Morava E (2014) Congenital disorders of glycosylation: new defects and still counting. J Inherit Metab Dis 37:609–617
    • (2014) J Inherit Metab Dis , vol.37 , pp. 609-617
    • Scott, K.1    Gadomski, T.2    Kozicz, T.3    Morava, E.4
  • 99
    • 84945249873 scopus 로고    scopus 로고
    • Phosphomannomutase deficiency (PMM2-CDG): ataxia and cerebellar assessment
    • PID: 26502900
    • Serrano M, de Diego V, Muchart J et al (2015) Phosphomannomutase deficiency (PMM2-CDG): ataxia and cerebellar assessment. Orphanet J Rare Dis 10:138
    • (2015) Orphanet J Rare Dis , vol.10 , pp. 138
    • Serrano, M.1    de Diego, V.2    Muchart, J.3
  • 100
    • 84883197530 scopus 로고    scopus 로고
    • A novel syndrome of hypohidrosis and intellectual disability is linked to COG6 deficiency
    • COI: 1:CAS:528:DC%2BC3sXht1WitL%2FF, PID: 23606727
    • Shaheen R, Ansari S, Alshammari MJ et al (2013) A novel syndrome of hypohidrosis and intellectual disability is linked to COG6 deficiency. J Med Genet 50:431–436
    • (2013) J Med Genet , vol.50 , pp. 431-436
    • Shaheen, R.1    Ansari, S.2    Alshammari, M.J.3
  • 101
    • 84862134535 scopus 로고    scopus 로고
    • The role of sugars in dendritic cell trafficking
    • PID: 22045510
    • Silva Z, Konstantopoulos K, Videira PA (2012) The role of sugars in dendritic cell trafficking. Ann Biomed Eng 40:777–789
    • (2012) Ann Biomed Eng , vol.40 , pp. 777-789
    • Silva, Z.1    Konstantopoulos, K.2    Videira, P.A.3
  • 103
    • 67649743525 scopus 로고    scopus 로고
    • Glycosylation in immune cell trafficking
    • COI: 1:CAS:528:DC%2BD1MXhsFGls7bF, PID: 19594631
    • Sperandio M, Gleissner CA, Ley K (2009) Glycosylation in immune cell trafficking. Immunol Rev 230:97–113
    • (2009) Immunol Rev , vol.230 , pp. 97-113
    • Sperandio, M.1    Gleissner, C.A.2    Ley, K.3
  • 104
    • 67649794877 scopus 로고    scopus 로고
    • Regulation of Notch signaling during T- and B-cell development by O-fucose glycans
    • COI: 1:CAS:528:DC%2BD1MXhsFGls7fK, PID: 19594638
    • \Stanley P, Guidos CJ (2009) Regulation of Notch signaling during T- and B-cell development by O-fucose glycans. Immunol Rev 230:201–15
    • (2009) Immunol Rev , vol.230 , pp. 201-215
    • Stanley, P.1    Guidos, C.J.2
  • 105
    • 67649839223 scopus 로고    scopus 로고
    • N-Glycans
    • Varki A, Cummings R, Esko J, (eds), Cold Spring Harbor Laboratory Press, New York
    • Stanley P, Schachter H, Taniguchi N et al (2009) N-Glycans. In: Varki A, Cummings R, Esko J (eds) Essentials of glycobiology, 2nd edn. Cold Spring Harbor Laboratory Press, New York
    • (2009) Essentials of glycobiology
    • Stanley, P.1    Schachter, H.2    Taniguchi, N.3
  • 106
    • 0028358262 scopus 로고
    • Carbohydrate-deficient glycoprotein syndrome: clinical expression in adults with a new metabolic disease
    • COI: 1:STN:280:DyaK2c3mtVajtw%3D%3D, PID: 8201322
    • Stibler H, Blennow G, Kristiansson B, Lindehammer H, Hagberg B (1994) Carbohydrate-deficient glycoprotein syndrome: clinical expression in adults with a new metabolic disease. J Neurol Neurosurg Psychiatry 57:552–556
    • (1994) J Neurol Neurosurg Psychiatry , vol.57 , pp. 552-556
    • Stibler, H.1    Blennow, G.2    Kristiansson, B.3    Lindehammer, H.4    Hagberg, B.5
  • 107
    • 84904036824 scopus 로고    scopus 로고
    • PGM3 mutations cause a congenital disorder of glycosylation with severe immunodeficiency and skeletal dysplasia
    • COI: 1:CAS:528:DC%2BC2cXpvFWmtLY%3D, PID: 24931394
    • Stray-Pedersen A, Backe PH, Sorte HS et al (2014) PGM3 mutations cause a congenital disorder of glycosylation with severe immunodeficiency and skeletal dysplasia. Am J Hum Genet 95:96–107
    • (2014) Am J Hum Genet , vol.95 , pp. 96-107
    • Stray-Pedersen, A.1    Backe, P.H.2    Sorte, H.S.3
  • 108
    • 0025779295 scopus 로고
    • Postmortem findings in two patients with the carbohydrate-deficient glycoprotein syndrome
    • Strømme P, Maehlen J, Strøm EH, Torvik A (1991) Postmortem findings in two patients with the carbohydrate-deficient glycoprotein syndrome. Acta Paediatr Scand Suppl 375:55–62
    • (1991) Acta Paediatr Scand Suppl , vol.375 , pp. 55-62
    • Strømme, P.1    Maehlen, J.2    Strøm, E.H.3    Torvik, A.4
  • 109
    • 0036799549 scopus 로고    scopus 로고
    • Deficiency of dolichyl-P-Man:Man7GlcNAc2-PP-dolichyl mannosyltransferase causes congenital disorder of glycosylation type Ig
    • COI: 1:CAS:528:DC%2BD38XotVWls7g%3D, PID: 12093361
    • Thiel C, Schwarz M, Hasilik M et al (2002) Deficiency of dolichyl-P-Man:Man7GlcNAc2-PP-dolichyl mannosyltransferase causes congenital disorder of glycosylation type Ig. Biochem J 367(Pt 1):195–201
    • (2002) Biochem J , vol.367 , pp. 195-201
    • Thiel, C.1    Schwarz, M.2    Hasilik, M.3
  • 110
    • 46749131183 scopus 로고    scopus 로고
    • Pericardial and abdominal fluid accumulation in congenital disorder of glycosylation type Ia
    • COI: 1:CAS:528:DC%2BD1cXosVOnurk%3D, PID: 18571450
    • Truin G, Guillard M, Lefeber DJ et al (2008) Pericardial and abdominal fluid accumulation in congenital disorder of glycosylation type Ia. Mol Genet Metab 94:481–484
    • (2008) Mol Genet Metab , vol.94 , pp. 481-484
    • Truin, G.1    Guillard, M.2    Lefeber, D.J.3
  • 111
    • 34247112772 scopus 로고    scopus 로고
    • Congenital disorder of glycosylation type Ia presenting with hydrops fetalis
    • PID: 17158594
    • van de Kamp JM, Lefeber DJ, Ruijter GJ et al (2007) Congenital disorder of glycosylation type Ia presenting with hydrops fetalis. J Med Genet 44:277–280
    • (2007) J Med Genet , vol.44 , pp. 277-280
    • van de Kamp, J.M.1    Lefeber, D.J.2    Ruijter, G.J.3
  • 112
    • 0001139052 scopus 로고    scopus 로고
    • Glycosylation of alpha1-acid glycoprotein (orosomucoid) in health and disease: occurrence, regulation and possible functional implications
    • Van Dijk W, Brinkman-Van der Linden ECM, Havenaar EC (1998) Glycosylation of alpha1-acid glycoprotein (orosomucoid) in health and disease: occurrence, regulation and possible functional implications. Trens Glycosci Glycotechnol 10:235–245
    • (1998) Trens Glycosci Glycotechnol , vol.10 , pp. 235-245
    • Van Dijk, W.1    Brinkman-Van der Linden, E.C.M.2    Havenaar, E.C.3
  • 113
    • 0035853268 scopus 로고    scopus 로고
    • Increased alpha3-fucosylation of alpha(1)-acid glycoprotein in patients with congenital disorder of glycosylation type IA (CDG-Ia)
    • PID: 11311246
    • Van Dijk W, Koeleman C, Van het Hof B, Poland D, Jakobs C, Jaeken J (2001) Increased alpha3-fucosylation of alpha(1)-acid glycoprotein in patients with congenital disorder of glycosylation type IA (CDG-Ia). FEBS Lett 494:232–235
    • (2001) FEBS Lett , vol.494 , pp. 232-235
    • Van Dijk, W.1    Koeleman, C.2    Van het Hof, B.3    Poland, D.4    Jakobs, C.5    Jaeken, J.6
  • 114
    • 0029585865 scopus 로고
    • Phosphomannomutase deficiency is a cause of carbohydrate-deficient glycoprotein syndrome type I
    • PID: 8549746
    • 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
  • 115
    • 84897585843 scopus 로고    scopus 로고
    • Diagnostic serum glycosylation profile in patients with intellectual disability as a result of MAN1B1 deficiency
    • PID: 24566669
    • Van Scherpenzeel M, Timal S, Rymen D et al (2014) Diagnostic serum glycosylation profile in patients with intellectual disability as a result of MAN1B1 deficiency. Brain 137:1030–1038
    • (2014) Brain , vol.137 , pp. 1030-1038
    • Van Scherpenzeel, M.1    Timal, S.2    Rymen, D.3
  • 116
    • 84859416185 scopus 로고    scopus 로고
    • Multifarious roles of sialic acids in immunity
    • COI: 1:CAS:528:DC%2BC38XhtFGjurrI, PID: 22524423
    • Varki A, Gagneux P (2012) Multifarious roles of sialic acids in immunity. Ann N Y Acad Sci 1253:16–36
    • (2012) Ann N Y Acad Sci , vol.1253 , pp. 16-36
    • Varki, A.1    Gagneux, P.2
  • 117
    • 77955553052 scopus 로고    scopus 로고
    • Association of fungal sepsis and galactosemia
    • PID: 20532692
    • Verma S, Bharti B, Inusha P (2010) Association of fungal sepsis and galactosemia. Indian J Pediatr 77:695–696
    • (2010) Indian J Pediatr , vol.77 , pp. 695-696
    • Verma, S.1    Bharti, B.2    Inusha, P.3
  • 118
    • 84991295154 scopus 로고    scopus 로고
    • Lymphatic edema in congenital disorders of glycosylation
    • PID: 23430905
    • Verstegen RH, Theodore M, van de Klerk H, Morava E (2012) Lymphatic edema in congenital disorders of glycosylation. JIMD Rep 4:113–116
    • (2012) JIMD Rep , vol.4 , pp. 113-116
    • Verstegen, R.H.1    Theodore, M.2    van de Klerk, H.3    Morava, E.4
  • 119
    • 40949126559 scopus 로고    scopus 로고
    • Surface alpha 2-3- and alpha 2-6-sialylation of human monocytes and derived dendritic cells and its influence on endocytosis
    • COI: 1:CAS:528:DC%2BD1cXjsVGjtb8%3D, PID: 18080182
    • Videira PA, Amado IF, Crespo HJ et al (2008) Surface alpha 2-3- and alpha 2-6-sialylation of human monocytes and derived dendritic cells and its influence on endocytosis. Glycoconj J 25:259–68
    • (2008) Glycoconj J , vol.25 , pp. 259-268
    • Videira, P.A.1    Amado, I.F.2    Crespo, H.J.3
  • 120
    • 22844449795 scopus 로고    scopus 로고
    • Gains of glycosylation comprise an unexpectedly large group of pathogenic mutations
    • COI: 1:CAS:528:DC%2BD2MXlslWhs74%3D, PID: 15924140
    • Vogt G, Chapgier A, Yang K et al (2005) Gains of glycosylation comprise an unexpectedly large group of pathogenic mutations. Nat Genet 37:692–700
    • (2005) Nat Genet , vol.37 , pp. 692-700
    • Vogt, G.1    Chapgier, A.2    Yang, K.3
  • 121
    • 0025648036 scopus 로고
    • Long-term prognosis in galactosaemia: results of a survey of 350 cases
    • COI: 1:STN:280:DyaK3M7nvFSrug%3D%3D, PID: 1706789
    • Waggoner DD, Buist NR, Donnell GN (1990) Long-term prognosis in galactosaemia: results of a survey of 350 cases. J Inherit Metab Dis 13:802–818
    • (1990) J Inherit Metab Dis , vol.13 , pp. 802-818
    • Waggoner, D.D.1    Buist, N.R.2    Donnell, G.N.3
  • 123
    • 84899618667 scopus 로고    scopus 로고
    • Autosomal recessive phosphoglucomutase 3 (PGM3) mutations link glycosylation defects to atopy, immune deficiency, autoimmunity, and neurocognitive impairment
    • COI: 1:CAS:528:DC%2BC2cXjs1Kkt7s%3D, PID: 24589341
    • Zhang Y, Yu X, Ichikawa M et al (2014) Autosomal recessive phosphoglucomutase 3 (PGM3) mutations link glycosylation defects to atopy, immune deficiency, autoimmunity, and neurocognitive impairment. J Allergy Clin Immunol 133:1400–1409
    • (2014) J Allergy Clin Immunol , vol.133 , pp. 1400-1409
    • Zhang, Y.1    Yu, X.2    Ichikawa, M.3


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.