메뉴 건너뛰기




Volumn 33, Issue 3, 2016, Pages 345-358

Clinical diagnostics and therapy monitoring in the congenital disorders of glycosylation

Author keywords

Congenital disorders of glycosylation; Glycomics; Protein specific glycosylation; Transferrin

Indexed keywords

BIOLOGICAL MARKER; GLYCOPROTEIN; PLASMA PROTEIN; TRANSFERRIN;

EID: 84953275208     PISSN: 02820080     EISSN: 15734986     Source Type: Journal    
DOI: 10.1007/s10719-015-9639-x     Document Type: Article
Times cited : (64)

References (126)
  • 1
    • 84863006290 scopus 로고    scopus 로고
    • Identifying cancer biomarkers by mass spectrometry-based glycomics
    • COI: 1:CAS:528:DC%2BC38Xpt12ku7c%3D, PID: 22740464
    • Mechref, Y., et al.: Identifying cancer biomarkers by mass spectrometry-based glycomics. Electrophoresis 33(12), 1755–1767 (2012)
    • (2012) Electrophoresis , vol.33 , Issue.12 , pp. 1755-1767
    • Mechref, Y.1
  • 2
    • 84867745540 scopus 로고    scopus 로고
    • The bisecting GlcNAc in cell growth control and tumor progression
    • COI: 1:CAS:528:DC%2BC38XhsV2qsb%2FI, PID: 22476631
    • Miwa, H.E., et al.: The bisecting GlcNAc in cell growth control and tumor progression. Glycoconj. J. 29(8–9), 609–618 (2012)
    • (2012) Glycoconj. J. , vol.29 , Issue.8-9 , pp. 609-618
    • Miwa, H.E.1
  • 3
    • 84885637740 scopus 로고    scopus 로고
    • Targeting aberrant sialylation in cancer cells using a fluorinated sialic acid analog impairs adhesion, migration, and in vivo tumor growth
    • PID: 23974695, COI: 1:CAS:528:DC%2BC3sXhsFOhur3F
    • Büll, C., et al.: Targeting aberrant sialylation in cancer cells using a fluorinated sialic acid analog impairs adhesion, migration, and in vivo tumor growth. Mol. Cancer Ther. 12(10), 1935–1946 (2013)
    • (2013) Mol. Cancer Ther. , vol.12 , Issue.10 , pp. 1935-1946
    • Büll, C.1
  • 4
    • 58149391280 scopus 로고    scopus 로고
    • Glycosylation of serum proteins in inflammatory diseases
    • COI: 1:CAS:528:DC%2BD1MXhsVOitw%3D%3D, PID: 19126970
    • Gornik, O., Lauc, G.: Glycosylation of serum proteins in inflammatory diseases. Dis. Markers 25(4–5), 267–278 (2008)
    • (2008) Dis. Markers , vol.25 , Issue.4-5 , pp. 267-278
    • Gornik, O.1    Lauc, G.2
  • 5
    • 84891836688 scopus 로고    scopus 로고
    • The role of protein glycosylation in Alzheimer disease
    • PID: 24279329, COI: 1:CAS:528:DC%2BC2cXosV2h
    • Schedin‐Weiss, S., Winblad, B., Tjernberg, L.O.: The role of protein glycosylation in Alzheimer disease. FEBS J. 281(1), 46–62 (2014)
    • (2014) FEBS J. , vol.281 , Issue.1 , pp. 46-62
    • Schedin‐Weiss, S.1    Winblad, B.2    Tjernberg, L.O.3
  • 6
    • 0017835519 scopus 로고
    • The glycosylation of hemoglobin: relevance to diabetes mellitus
    • COI: 1:CAS:528:DyaE1cXhvVOht7w%3D, PID: 635569
    • Bunn, H.F., Gabbay, K.H., Gallop, P.M.: The glycosylation of hemoglobin: relevance to diabetes mellitus. Science 200(4337), 21–27 (1978)
    • (1978) Science , vol.200 , Issue.4337 , pp. 21-27
    • Bunn, H.F.1    Gabbay, K.H.2    Gallop, P.M.3
  • 7
    • 84875424999 scopus 로고    scopus 로고
    • Mutations in HNF1A result in marked alterations of plasma glycan profile
    • COI: 1:CAS:528:DC%2BC3sXpvFCrsr4%3D, PID: 23274891
    • Thanabalasingham, G., et al.: Mutations in HNF1A result in marked alterations of plasma glycan profile. Diabetes 62(4), 1329–1337 (2013)
    • (2013) Diabetes , vol.62 , Issue.4 , pp. 1329-1337
    • Thanabalasingham, G.1
  • 8
    • 84893734160 scopus 로고    scopus 로고
    • Solving glycosylation disorders: fundamental approaches reveal complicated pathways
    • COI: 1:CAS:528:DC%2BC2cXitV2is7c%3D, PID: 24507773
    • Freeze, H.H., et al.: Solving glycosylation disorders: fundamental approaches reveal complicated pathways. Am. J. Hum. Genet. 94(2), 161–175 (2014)
    • (2014) Am. J. Hum. Genet. , vol.94 , Issue.2 , pp. 161-175
    • Freeze, H.H.1
  • 10
    • 84975671787 scopus 로고    scopus 로고
    • Congenital disorders of glycosylation, in physician’s guide to the diagnosis, treatment, and follow-up of inherited metabolic diseases
    • Jaeken, J., van den Heuvel L.: Congenital disorders of glycosylation, in physician’s guide to the diagnosis, treatment, and follow-up of inherited metabolic diseases. Springer. p. 483–512 (2014)
    • (2014) Springer , pp. 483-512
    • Jaeken, J.1    van den Heuvel, L.2
  • 11
    • 84862905517 scopus 로고    scopus 로고
    • Diseases of glycosylation beyond classical congenital disorders of glycosylation
    • COI: 1:CAS:528:DC%2BC38Xjt1egtbc%3D
    • Hennet, T.: Diseases of glycosylation beyond classical congenital disorders of glycosylation. Biochimica et Biophysica Acta (BBA)-General Subjects 1820(9), 1306–1317 (2012)
    • (2012) Biochimica et Biophysica Acta (BBA)-General Subjects , vol.1820 , Issue.9 , pp. 1306-1317
    • Hennet, T.1
  • 12
    • 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., et al.: Congenital disorders of glycosylation: new defects and still counting. J. Inherit. Metab. Dis. 37(4), 609–617 (2014)
    • (2014) J. Inherit. Metab. Dis. , vol.37 , Issue.4 , pp. 609-617
    • Scott, K.1
  • 13
    • 0036840817 scopus 로고    scopus 로고
    • Congenital disorders of glycosylation: a review
    • PID: 12409504
    • Grünewald, S., Matthijs, G., Jaeken, J.: Congenital disorders of glycosylation: a review. Pediatr. Res. 52(5), 618–624 (2002)
    • (2002) Pediatr. Res. , vol.52 , Issue.5 , pp. 618-624
    • Grünewald, S.1    Matthijs, G.2    Jaeken, J.3
  • 14
    • 84893419976 scopus 로고    scopus 로고
    • Congenital disorders of glycosylation and intellectual disability
    • PID: 23798010
    • Wolfe, L.A., Krasnewich, D.: Congenital disorders of glycosylation and intellectual disability. Developmental disabilities research reviews 17(3), 211–225 (2013)
    • (2013) Developmental disabilities research reviews , vol.17 , Issue.3 , pp. 211-225
    • Wolfe, L.A.1    Krasnewich, D.2
  • 15
    • 33744811996 scopus 로고    scopus 로고
    • Mass spectrometry for congenital disorders of glycosylation, CDG
    • COI: 1:CAS:528:DC%2BD28Xls1ejsL0%3D
    • Wada, Y.: Mass spectrometry for congenital disorders of glycosylation, CDG. J. Chromatogr. B 838(1), 3–8 (2006)
    • (2006) J. Chromatogr. B , vol.838 , Issue.1 , pp. 3-8
    • Wada, Y.1
  • 16
    • 34447097453 scopus 로고    scopus 로고
    • Analysis of protein glycosylation by mass spectrometry
    • COI: 1:CAS:528:DC%2BD2sXhtFahur3O, PID: 17585300
    • Morelle, W., Michalski, J.-C.: Analysis of protein glycosylation by mass spectrometry. Nat. Protoc. 2(7), 1585–1602 (2007)
    • (2007) Nat. Protoc. , vol.2 , Issue.7 , pp. 1585-1602
    • Morelle, W.1    Michalski, J.-C.2
  • 17
    • 68249131729 scopus 로고    scopus 로고
    • Automated measurement of permethylated serum N-glycans by MALDI–linear ion trap mass spectrometry
    • COI: 1:CAS:528:DC%2BD1MXhtVSlsbzE, PID: 19577739
    • Guillard, M., et al.: Automated measurement of permethylated serum N-glycans by MALDI–linear ion trap mass spectrometry. Carbohydr. Res. 344(12), 1550–1557 (2009)
    • (2009) Carbohydr. Res. , vol.344 , Issue.12 , pp. 1550-1557
    • Guillard, M.1
  • 18
    • 79961168515 scopus 로고    scopus 로고
    • The impact of mass spectrometry in the diagnosis of congenital disorders of glycosylation
    • COI: 1:CAS:528:DC%2BC3MXptVOjurg%3D, PID: 21384227
    • Sturiale, L., Barone, R., Garozzo, D.: The impact of mass spectrometry in the diagnosis of congenital disorders of glycosylation. J. Inherit. Metab. Dis. 34(4), 891–899 (2011)
    • (2011) J. Inherit. Metab. Dis. , vol.34 , Issue.4 , pp. 891-899
    • Sturiale, L.1    Barone, R.2    Garozzo, D.3
  • 19
    • 0035107128 scopus 로고    scopus 로고
    • Rapid determination of transferrin isoforms by immunoaffinity liquid chromatography and electrospray mass spectrometry
    • COI: 1:CAS:528:DC%2BD3MXhvVOgtbw%3D, PID: 11238305
    • Lacey, J.M., et al.: Rapid determination of transferrin isoforms by immunoaffinity liquid chromatography and electrospray mass spectrometry. Clin. Chem. 47(3), 513–518 (2001)
    • (2001) Clin. Chem. , vol.47 , Issue.3 , pp. 513-518
    • Lacey, J.M.1
  • 20
    • 84893589222 scopus 로고    scopus 로고
    • Multiple phenotypes in phosphoglucomutase 1 deficiency
    • COI: 1:CAS:528:DC%2BC2cXisFaktLY%3D, PID: 24499211
    • Tegtmeyer, L.C., et al.: Multiple phenotypes in phosphoglucomutase 1 deficiency. N. Engl. J. Med. 370(6), 533–542 (2014)
    • (2014) N. Engl. J. Med. , vol.370 , Issue.6 , pp. 533-542
    • Tegtmeyer, L.C.1
  • 21
    • 84872795097 scopus 로고    scopus 로고
    • Approaches to homozygosity mapping and exome sequencing for the identification of novel types of CDG
    • COI: 1:CAS:528:DC%2BC3sXovVSntA%3D%3D, PID: 22983704
    • Matthijs, G., et al.: Approaches to homozygosity mapping and exome sequencing for the identification of novel types of CDG. Glycoconj. J. 30(1), 67–76 (2013)
    • (2013) Glycoconj. J. , vol.30 , Issue.1 , pp. 67-76
    • Matthijs, G.1
  • 22
    • 78650401291 scopus 로고    scopus 로고
    • Congenital disorders of glycosylation
    • COI: 1:CAS:528:DC%2BC3MXhsFKht70%3D, PID: 21175687
    • Jaeken, J.: Congenital disorders of glycosylation. Ann. N. Y. Acad. Sci. 1214(1), 190–198 (2010)
    • (2010) Ann. N. Y. Acad. Sci. , vol.1214 , Issue.1 , pp. 190-198
    • Jaeken, J.1
  • 23
    • 0021686784 scopus 로고
    • Sialic acid-deficient serum and cerebrospinal fluid transferrin in a newly recognized genetic syndrome
    • COI: 1:STN:280:DyaL2M7lt1Giuw%3D%3D, PID: 6543331
    • Jaeken, J., et al.: Sialic acid-deficient serum and cerebrospinal fluid transferrin in a newly recognized genetic syndrome. Clin. Chim. Acta 144(2), 245–247 (1984)
    • (1984) Clin. Chim. Acta , vol.144 , Issue.2 , pp. 245-247
    • Jaeken, J.1
  • 24
    • 0242267940 scopus 로고    scopus 로고
    • Improved HPLC method for carbohydrate-deficient transferrin in serum
    • COI: 1:CAS:528:DC%2BD3sXosleqsL8%3D, PID: 14578320
    • Helander, A., Husa, A., Jeppsson, J.-O.: Improved HPLC method for carbohydrate-deficient transferrin in serum. Clin. Chem. 49(11), 1881–1890 (2003)
    • (2003) Clin. Chem. , vol.49 , Issue.11 , pp. 1881-1890
    • Helander, A.1    Husa, A.2    Jeppsson, J.-O.3
  • 25
    • 1642533464 scopus 로고    scopus 로고
    • Diagnosis of congenital disorders of glycosylation by capillary zone electrophoresis of serum transferrin
    • COI: 1:CAS:528:DC%2BD2cXovFWgsw%3D%3D, PID: 14633925
    • Carchon, H.A., et al.: Diagnosis of congenital disorders of glycosylation by capillary zone electrophoresis of serum transferrin. Clin. Chem. 50(1), 101–111 (2004)
    • (2004) Clin. Chem. , vol.50 , Issue.1 , pp. 101-111
    • Carchon, H.A.1
  • 26
    • 34447249066 scopus 로고    scopus 로고
    • Characterization of transferrin glycoforms in human serum by CE-UV and CE-ESI-MS
    • PID: 17523137, COI: 1:CAS:528:DC%2BD2sXnslyrs78%3D
    • Sanz‐Nebot, V., et al.: Characterization of transferrin glycoforms in human serum by CE-UV and CE-ESI-MS. Electrophoresis 28(12), 1949–1957 (2007)
    • (2007) Electrophoresis , vol.28 , Issue.12 , pp. 1949-1957
    • Sanz‐Nebot, V.1
  • 27
    • 79961169660 scopus 로고    scopus 로고
    • How to find and diagnose a CDG due to defective N-glycosylation
    • PID: 21739167
    • Lefeber, D.J., Morava, E., Jaeken, J.: How to find and diagnose a CDG due to defective N-glycosylation. J. Inherit. Metab. Dis. 34(4), 849–852 (2011)
    • (2011) J. Inherit. Metab. Dis. , vol.34 , Issue.4 , pp. 849-852
    • Lefeber, D.J.1    Morava, E.2    Jaeken, J.3
  • 28
    • 31644447885 scopus 로고    scopus 로고
    • Genetic variants of transferrin in the diagnosis of protein hypoglycosylation
    • COI: 1:CAS:528:DC%2BD28Xnt1GhtQ%3D%3D, PID: 16435226
    • Albahri, Z., et al.: Genetic variants of transferrin in the diagnosis of protein hypoglycosylation. J. Inherit. Metab. Dis. 28(6), 1184–1188 (2005)
    • (2005) J. Inherit. Metab. Dis. , vol.28 , Issue.6 , pp. 1184-1188
    • Albahri, Z.1
  • 29
    • 84920273372 scopus 로고    scopus 로고
    • Transferrin variants: Pitfalls in the diagnostics of congenital disorders of glycosylation
    • PID: 25305627, COI: 1:CAS:528:DC%2BC2cXhslGjtr3F
    • Zühlsdorf, A., et al.: Transferrin variants: Pitfalls in the diagnostics of congenital disorders of glycosylation. Clin. Biochem. 48(1), 11–13 (2015)
    • (2015) Clin. Biochem. , vol.48 , Issue.1 , pp. 11-13
    • Zühlsdorf, A.1
  • 30
    • 0017809978 scopus 로고
    • Transferrin: evidence for two common subtypes of the TfC allele
    • PID: 669722
    • Kühnl, P., Spielmann, W.: Transferrin: evidence for two common subtypes of the TfC allele. Hum. Genet. 43(1), 91–95 (1978)
    • (1978) Hum. Genet. , vol.43 , Issue.1 , pp. 91-95
    • Kühnl, P.1    Spielmann, W.2
  • 31
    • 84952308445 scopus 로고    scopus 로고
    • High-resolution Qtof-MS glycoprofiling of intact transferrin for diagnosis and subtype identification in the congenital disorders of glycosylation, Translational Res
    • van Scherpenzeel, M., et al.: High-resolution Qtof-MS glycoprofiling of intact transferrin for diagnosis and subtype identification in the congenital disorders of glycosylation. Translational Res, (2015)
    • (2015) et al.
    • van Scherpenzeel, M.1
  • 32
    • 79961167779 scopus 로고    scopus 로고
    • Congenital disorders of glycosylation (CDG): it’s (nearly) all in it!
    • COI: 1:CAS:528:DC%2BC3MXptVOjuro%3D, PID: 21384229
    • Jaeken, J.: Congenital disorders of glycosylation (CDG): it’s (nearly) all in it! J. Inherit. Metab. Dis. 34(4), 853–858 (2011)
    • (2011) J. Inherit. Metab. Dis. , vol.34 , Issue.4 , pp. 853-858
    • Jaeken, J.1
  • 33
    • 0036020904 scopus 로고    scopus 로고
    • Analyses of dolichol pyrophosphate–linked oligosaccharides in cell cultures and tissues by fluorophore-assisted carbohydrate electrophoresis
    • COI: 1:CAS:528:DC%2BD38XltlCqtro%3D, PID: 12070078
    • Gao, N., Lehrman, M.A.: Analyses of dolichol pyrophosphate–linked oligosaccharides in cell cultures and tissues by fluorophore-assisted carbohydrate electrophoresis. Glycobiology 12(5), 353–360 (2002)
    • (2002) Glycobiology , vol.12 , Issue.5 , pp. 353-360
    • Gao, N.1    Lehrman, M.A.2
  • 34
    • 84866425378 scopus 로고    scopus 로고
    • Gene identification in the congenital disorders of glycosylation type I by whole-exome sequencing
    • COI: 1:CAS:528:DC%2BC38XhtlGhsbbK, PID: 22492991
    • Timal, S., et al.: Gene identification in the congenital disorders of glycosylation type I by whole-exome sequencing. Hum. Mol. Genet. 21(19), 4151–4161 (2012)
    • (2012) Hum. Mol. Genet. , vol.21 , Issue.19 , pp. 4151-4161
    • Timal, S.1
  • 35
    • 33847354287 scopus 로고    scopus 로고
    • Transferrin and apolipoprotein C-III isofocusing are complementary in the diagnosis of N-and O-glycan biosynthesis defects
    • COI: 1:CAS:528:DC%2BD2sXhs1WrtL0%3D, PID: 17170056
    • Wopereis, S., et al.: Transferrin and apolipoprotein C-III isofocusing are complementary in the diagnosis of N-and O-glycan biosynthesis defects. Clin. Chem. 53(2), 180–187 (2007)
    • (2007) Clin. Chem. , vol.53 , Issue.2 , pp. 180-187
    • Wopereis, S.1
  • 36
    • 38149019274 scopus 로고    scopus 로고
    • Two-dimensional gel electrophoresis of apolipoprotein C-III and other serum glycoproteins for the combined screening of human congenital disorders of O-and N-glycosylation
    • COI: 1:CAS:528:DC%2BD2sXjs1Klt7w%3D
    • Bruneel, A., et al.: Two-dimensional gel electrophoresis of apolipoprotein C-III and other serum glycoproteins for the combined screening of human congenital disorders of O-and N-glycosylation. PROTEOMICS-Clinical Applications 1(3), 321–324 (2007)
    • (2007) PROTEOMICS-Clinical Applications , vol.1 , Issue.3 , pp. 321-324
    • Bruneel, A.1
  • 37
    • 8644240243 scopus 로고    scopus 로고
    • Hydrophilic affinity isolation and MALDI multiple-stage tandem mass spectrometry of glycopeptides for glycoproteomics
    • COI: 1:CAS:528:DC%2BD2cXosVSmt7k%3D, PID: 15538777
    • Wada, Y., Tajiri, M., Yoshida, S.: Hydrophilic affinity isolation and MALDI multiple-stage tandem mass spectrometry of glycopeptides for glycoproteomics. Anal. Chem. 76(22), 6560–6565 (2004)
    • (2004) Anal. Chem. , vol.76 , Issue.22 , pp. 6560-6565
    • Wada, Y.1    Tajiri, M.2    Yoshida, S.3
  • 38
    • 79954626850 scopus 로고    scopus 로고
    • Plasma N-glycan profiling by mass spectrometry for congenital disorders of glycosylation type II
    • COI: 1:CAS:528:DC%2BC3MXkvFCqtro%3D, PID: 21273509
    • Guillard, M., et al.: Plasma N-glycan profiling by mass spectrometry for congenital disorders of glycosylation type II. Clin. Chem. 57(4), 593–602 (2011)
    • (2011) Clin. Chem. , vol.57 , Issue.4 , pp. 593-602
    • Guillard, M.1
  • 39
    • 84884498276 scopus 로고    scopus 로고
    • Serum N-glycan and O-glycan analysis by mass spectrometry for diagnosis of congenital disorders of glycosylation
    • COI: 1:CAS:528:DC%2BC3sXhs1SksLbI, PID: 23928051
    • Xia, B., et al.: Serum N-glycan and O-glycan analysis by mass spectrometry for diagnosis of congenital disorders of glycosylation. Anal. Biochem. 442(2), 178–185 (2013)
    • (2013) Anal. Biochem. , vol.442 , Issue.2 , pp. 178-185
    • Xia, B.1
  • 40
    • 84863201152 scopus 로고    scopus 로고
    • Mass spectrometry of apolipoprotein C-III, a simple analytical method for mucin-type O-glycosylation and its application to an autosomal recessive cutis laxa type-2 (ARCL2) patient
    • COI: 1:CAS:528:DC%2BC38XpsFKnt7c%3D, PID: 22611120
    • Wada, Y., Kadoya, M., Okamoto, N.: Mass spectrometry of apolipoprotein C-III, a simple analytical method for mucin-type O-glycosylation and its application to an autosomal recessive cutis laxa type-2 (ARCL2) patient. Glycobiology 22(8), 1140–1144 (2012)
    • (2012) Glycobiology , vol.22 , Issue.8 , pp. 1140-1144
    • Wada, Y.1    Kadoya, M.2    Okamoto, N.3
  • 41
    • 34250330012 scopus 로고    scopus 로고
    • A rapid mass spectrometric strategy for the characterization of N-and O-glycan chains in the diagnosis of defects in glycan biosynthesis
    • COI: 1:CAS:528:DC%2BD2sXntVSisLg%3D, PID: 17520685
    • Faid, V., et al.: A rapid mass spectrometric strategy for the characterization of N-and O-glycan chains in the diagnosis of defects in glycan biosynthesis. Proteomics 7(11), 1800–1813 (2007)
    • (2007) Proteomics , vol.7 , Issue.11 , pp. 1800-1813
    • Faid, V.1
  • 42
    • 84948701537 scopus 로고    scopus 로고
    • MALDI-TOF MS applied to apoC-III glycoforms of patients with congenital disorders affecting O-glycosylation. Comparison with two-dimensional electrophoresis
    • Yen-Nicolaÿ, S., et al.: MALDI-TOF MS applied to apoC-III glycoforms of patients with congenital disorders affecting O-glycosylation. Comparison with two-dimensional electrophoresis. PROTEOMICS-Clinical Applications, (2015)
    • (2015) PROTEOMICS-Clinical Applications
    • Yen-Nicolaÿ, S.1
  • 43
    • 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., et al.: Diagnostic serum glycosylation profile in patients with intellectual disability as a result of MAN1B1 deficiency. Brain 137(4), 1030–1038 (2014)
    • (2014) Brain , vol.137 , Issue.4 , pp. 1030-1038
    • Van Scherpenzeel, M.1
  • 44
    • 70249111204 scopus 로고    scopus 로고
    • Towards a therapy for phosphomannomutase 2 deficiency, the defect in CDG-Ia patients
    • COI: 1:CAS:528:DC%2BD1MXhtFGqsLvM
    • Freeze, H.H.: Towards a therapy for phosphomannomutase 2 deficiency, the defect in CDG-Ia patients. Biochimica et Biophysica Acta (BBA)-Molecular Basis of Disease 1792(9), 835–840 (2009)
    • (2009) Biochimica et Biophysica Acta (BBA)-Molecular Basis of Disease , vol.1792 , Issue.9 , pp. 835-840
    • Freeze, H.H.1
  • 45
    • 70249148051 scopus 로고    scopus 로고
    • The clinical spectrum of phosphomannose isomerase deficiency, with an evaluation of mannose treatment for CDG-Ib
    • COI: 1:CAS:528:DC%2BD1MXhtFGqsLvN
    • De Lonlay, P., Seta, N.: The clinical spectrum of phosphomannose isomerase deficiency, with an evaluation of mannose treatment for CDG-Ib. Biochimica et Biophysica Acta (BBA)-Molecular Basis of Disease 1792(9), 841–843 (2009)
    • (2009) Biochimica et Biophysica Acta (BBA)-Molecular Basis of Disease , vol.1792 , Issue.9 , pp. 841-843
    • De Lonlay, P.1    Seta, N.2
  • 46
    • 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., et al.: Correction of leukocyte adhesion deficiency type II with oral fucose. Blood 94(12), 3976–3985 (1999)
    • (1999) Blood , vol.94 , Issue.12 , pp. 3976-3985
    • Marquardt, T.1
  • 48
    • 34247229178 scopus 로고    scopus 로고
    • Targeted therapy for inherited GPI deficiency
    • COI: 1:CAS:528:DC%2BD2sXksFCmurg%3D, PID: 17442906
    • Almeida, A.M., et al.: Targeted therapy for inherited GPI deficiency. N. Engl. J. Med. 356(16), 1641–1647 (2007)
    • (2007) N. Engl. J. Med. , vol.356 , Issue.16 , pp. 1641-1647
    • Almeida, A.M.1
  • 49
    • 0032869205 scopus 로고    scopus 로고
    • Molecular basis of carbohydrate-deficient glycoprotein syndromes type I with normal phosphomannomutase activity
    • COI: 1:CAS:528:DyaK1MXntlOhurc%3D
    • Freeze, H.H., Aebi, M.: Molecular basis of carbohydrate-deficient glycoprotein syndromes type I with normal phosphomannomutase activity. Biochimica et Biophysica Acta (BBA)-Molecular Basis of Disease 1455(2), 167–178 (1999)
    • (1999) Biochimica et Biophysica Acta (BBA)-Molecular Basis of Disease , vol.1455 , Issue.2 , pp. 167-178
    • Freeze, H.H.1    Aebi, M.2
  • 50
    • 84904100059 scopus 로고    scopus 로고
    • Successful liver transplantation and long-term follow-up in a patient with MPI-CDG
    • PID: 24982104
    • Janssen, M.C., et al.: Successful liver transplantation and long-term follow-up in a patient with MPI-CDG. Pediatrics 134(1), e279–e283 (2014)
    • (2014) Pediatrics , vol.134 , Issue.1 , pp. e279-e283
    • Janssen, M.C.1
  • 51
    • 0015956587 scopus 로고
    • A kinetic study of the isozymes determined by the three human phosphoglucomutase loci PGM1, PGM2 and PGM3
    • COI: 1:CAS:528:DyaE2cXktVSrsr4%3D, PID: 4829444
    • Quick, C.B., Fisher, R.A., Harris, H.: A kinetic study of the isozymes determined by the three human phosphoglucomutase loci PGM1, PGM2 and PGM3. Eur. J. Biochem. 42(2), 511–517 (1974)
    • (1974) Eur. J. Biochem. , vol.42 , Issue.2 , pp. 511-517
    • Quick, C.B.1    Fisher, R.A.2    Harris, H.3
  • 52
    • 0037097344 scopus 로고    scopus 로고
    • Leukocyte adhesion deficiency (LAD) type II/carbohydrate deficient glycoprotein (CDG) IIc founder effect and genotype/phenotype correlation
    • PID: 12116250
    • Etzioni, A., et al.: Leukocyte adhesion deficiency (LAD) type II/carbohydrate deficient glycoprotein (CDG) IIc founder effect and genotype/phenotype correlation. Am. J. Med. Genet. 110(2), 131–135 (2002)
    • (2002) Am. J. Med. Genet. , vol.110 , Issue.2 , pp. 131-135
    • Etzioni, A.1
  • 53
    • 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., et al.: Leukocyte adhesion deficiency II syndrome, a generalized defect in fucose metabolism. J. Pediatr. 134(6), 681–688 (1999)
    • (1999) J. Pediatr. , vol.134 , Issue.6 , pp. 681-688
    • Marquardt, T.1
  • 54
    • 84912041230 scopus 로고    scopus 로고
    • A novel mutation in leukocyte adhesion deficiency type II/CDGIIc
    • COI: 1:CAS:528:DC%2BC2cXhs1Wru7rE, PID: 25239688
    • Cagdas, D., et al.: A novel mutation in leukocyte adhesion deficiency type II/CDGIIc. J. Clin. Immunol. 34(8), 1009–1014 (2014)
    • (2014) J. Clin. Immunol. , vol.34 , Issue.8 , pp. 1009-1014
    • Cagdas, D.1
  • 55
    • 0035863209 scopus 로고    scopus 로고
    • PIG-M transfers the first mannose to glycosylphosphatidylinositol on the lumenal side of the ER
    • COI: 1:CAS:528:DC%2BD3MXhvVCmu7g%3D, PID: 11226175
    • Maeda, Y., et al.: PIG-M transfers the first mannose to glycosylphosphatidylinositol on the lumenal side of the ER. The EMBO journal 20(1–2), 250–261 (2001)
    • (2001) The EMBO journal , vol.20 , Issue.1-2 , pp. 250-261
    • Maeda, Y.1
  • 56
    • 84975639341 scopus 로고    scopus 로고
    • Essentials of glycobiology. 2nd ed
    • Varki, A., et al.: Essentials of glycobiology. 2nd ed. Chapter 13: Cold Spring (2009)
    • (2009) Chapter 13: Cold Spring
    • Varki, A.1
  • 57
    • 77953240454 scopus 로고    scopus 로고
    • Precision mapping of an in vivo N-glycoproteome reveals rigid topological and sequence constraints
    • COI: 1:CAS:528:DC%2BC3cXnsFKmsLc%3D, PID: 20510933
    • Zielinska, D.F., et al.: Precision mapping of an in vivo N-glycoproteome reveals rigid topological and sequence constraints. Cell 141(5), 897–907 (2010)
    • (2010) Cell , vol.141 , Issue.5 , pp. 897-907
    • Zielinska, D.F.1
  • 59
    • 84899065140 scopus 로고    scopus 로고
    • Glycosylation, hypogammaglobulinemia, and resistance to viral infections
    • COI: 1:CAS:528:DC%2BC2cXnt1GrsrY%3D, PID: 24716661
    • Sadat, M.A., et al.: Glycosylation, hypogammaglobulinemia, and resistance to viral infections. N. Engl. J. Med. 370(17), 1615–1625 (2014)
    • (2014) N. Engl. J. Med. , vol.370 , Issue.17 , pp. 1615-1625
    • Sadat, M.A.1
  • 60
    • 84975639655 scopus 로고    scopus 로고
    • Cohen syndrome is associated with major glycosylation defects. Human molecular genetics, p
    • Duplomb, L., et al.: Cohen syndrome is associated with major glycosylation defects. Human molecular genetics, p. ddt630 (2013)
    • (2013) ddt630
    • Duplomb, L.1
  • 61
    • 84925764199 scopus 로고    scopus 로고
    • N-Glycomic changes in serum proteins in type 2 diabetes mellitus correlate with complications and with metabolic syndrome parameters
    • PID: 25793407, COI: 1:CAS:528:DC%2BC2MXhs1Cms7bL
    • Testa, R., et al.: N-Glycomic changes in serum proteins in type 2 diabetes mellitus correlate with complications and with metabolic syndrome parameters. PLoS One 10(3), e0119983 (2015)
    • (2015) PLoS One , vol.10 , Issue.3
    • Testa, R.1
  • 63
    • 84901855345 scopus 로고    scopus 로고
    • Glycosylation as a marker for inflammatory arthritis
    • COI: 1:CAS:528:DC%2BC2cXktlCmsL0%3D, PID: 24643039
    • Albrecht, S., et al.: Glycosylation as a marker for inflammatory arthritis. Cancer Biomark 14, 17–28 (2014)
    • (2014) Cancer Biomark , vol.14 , pp. 17-28
    • Albrecht, S.1
  • 64
    • 84860231407 scopus 로고    scopus 로고
    • Integrated approach toward the discovery of glyco-biomarkers of inflammation-related diseases
    • COI: 1:CAS:528:DC%2BC38XhtFGjurvK, PID: 22380786
    • Angata, T., et al.: Integrated approach toward the discovery of glyco-biomarkers of inflammation-related diseases. Ann. N. Y. Acad. Sci. 1253(1), 159–169 (2012)
    • (2012) Ann. N. Y. Acad. Sci. , vol.1253 , Issue.1 , pp. 159-169
    • Angata, T.1
  • 66
    • 28544446695 scopus 로고    scopus 로고
    • Biomarkers in cancer staging, prognosis and treatment selection
    • COI: 1:CAS:528:DC%2BD2MXht1WitLbP, PID: 16239904
    • Ludwig, J.A., Weinstein, J.N.: Biomarkers in cancer staging, prognosis and treatment selection. Nat. Rev. Cancer 5(11), 845–856 (2005)
    • (2005) Nat. Rev. Cancer , vol.5 , Issue.11 , pp. 845-856
    • Ludwig, J.A.1    Weinstein, J.N.2
  • 68
    • 84945255805 scopus 로고    scopus 로고
    • Glycosylation-based serum biomarkers for cancer diagnostics and prognostics
    • Kirwan, A., et al.: Glycosylation-based serum biomarkers for cancer diagnostics and prognostics. BioMed Res Int, 2015. (2015)
    • (2015) BioMed Res Int , pp. 2015
    • Kirwan, A.1
  • 69
    • 65349151261 scopus 로고    scopus 로고
    • Profile of native N-linked glycan structures from human serum using high performance liquid chromatography on a microfluidic chip and time-of-flight mass spectrometry
    • COI: 1:CAS:528:DC%2BD1MXltVertrY%3D, PID: 19288519
    • Chu, C.S., et al.: Profile of native N-linked glycan structures from human serum using high performance liquid chromatography on a microfluidic chip and time-of-flight mass spectrometry. Proteomics 9(7), 1939 (2009)
    • (2009) Proteomics , vol.9 , Issue.7 , pp. 1939
    • Chu, C.S.1
  • 70
    • 84938633596 scopus 로고    scopus 로고
    • A method for in-depth structural annotation of human serum glycans that yields biological variations
    • COI: 1:CAS:528:DC%2BC2MXhtVarsrbN, PID: 26086522
    • Song, T., Aldredge, D., Lebrilla, C.B.: A method for in-depth structural annotation of human serum glycans that yields biological variations. Anal. Chem. 87(15), 7754–7762 (2015)
    • (2015) Anal. Chem. , vol.87 , Issue.15 , pp. 7754-7762
    • Song, T.1    Aldredge, D.2    Lebrilla, C.B.3
  • 71
    • 84859396316 scopus 로고    scopus 로고
    • Effective use of mass spectrometry for glycan and glycopeptide structural analysis
    • COI: 1:CAS:528:DC%2BC38XislSqu74%3D, PID: 22360375
    • Leymarie, N., Zaia, J.: Effective use of mass spectrometry for glycan and glycopeptide structural analysis. Anal. Chem. 84(7), 3040–3048 (2012)
    • (2012) Anal. Chem. , vol.84 , Issue.7 , pp. 3040-3048
    • Leymarie, N.1    Zaia, J.2
  • 72
    • 84872680325 scopus 로고    scopus 로고
    • Glycomics using mass spectrometry
    • COI: 1:CAS:528:DC%2BC3sXovVSmtQ%3D%3D, PID: 22532006
    • Wuhrer, M.: Glycomics using mass spectrometry. Glycoconj. J. 30(1), 11–22 (2013)
    • (2013) Glycoconj. J. , vol.30 , Issue.1 , pp. 11-22
    • Wuhrer, M.1
  • 73
    • 84939865360 scopus 로고    scopus 로고
    • Ultra-high throughput, ultrafiltration-based N-glycomics platform for ultra-performance liquid chromatography (ULTRA3)
    • Stoeckmann, H., et al.: Ultra-high throughput, ultrafiltration-based N-glycomics platform for ultra-performance liquid chromatography (ULTRA3). Analytical Chem, (2015)
    • (2015) Analytical Chem
    • Stoeckmann, H.1
  • 74
    • 1942454310 scopus 로고    scopus 로고
    • Noninvasive diagnosis of liver cirrhosis using DNA sequencer–based total serum protein glycomics
    • COI: 1:CAS:528:DC%2BD2cXis1ekt7g%3D, PID: 15152612
    • Callewaert, N., et al.: Noninvasive diagnosis of liver cirrhosis using DNA sequencer–based total serum protein glycomics. Nat. Med. 10(4), 429–434 (2004)
    • (2004) Nat. Med. , vol.10 , Issue.4 , pp. 429-434
    • Callewaert, N.1
  • 75
    • 0031752424 scopus 로고    scopus 로고
    • Helicobacter pylori infection produces reversible glycosylation changes to gastric mucins
    • COI: 1:CAS:528:DyaK1cXmvFyiurY%3D, PID: 9849856
    • Ota, H., et al.: Helicobacter pylori infection produces reversible glycosylation changes to gastric mucins. Virchows Arch. 433(5), 419–426 (1998)
    • (1998) Virchows Arch. , vol.433 , Issue.5 , pp. 419-426
    • Ota, H.1
  • 76
    • 0142059844 scopus 로고    scopus 로고
    • Human uptake and incorporation of an immunogenic nonhuman dietary sialic acid
    • COI: 1:CAS:528:DC%2BD3sXotlGltbs%3D, PID: 14523234
    • Tangvoranuntakul, P., et al.: Human uptake and incorporation of an immunogenic nonhuman dietary sialic acid. Proc. Natl. Acad. Sci. 100(21), 12045–12050 (2003)
    • (2003) Proc. Natl. Acad. Sci. , vol.100 , Issue.21 , pp. 12045-12050
    • Tangvoranuntakul, P.1
  • 77
    • 61849180382 scopus 로고    scopus 로고
    • Variability, heritability and environmental determinants of human plasma N-glycome
    • COI: 1:CAS:528:DC%2BD1cXhsVeksb7O
    • Knezevic, A., et al.: Variability, heritability and environmental determinants of human plasma N-glycome. J. Proteome Res. 8(2), 694–701 (2008)
    • (2008) J. Proteome Res. , vol.8 , Issue.2 , pp. 694-701
    • Knezevic, A.1
  • 78
    • 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., et al.: Detailed glycan analysis of serum glycoproteins of patients with congenital disorders of glycosylation indicates the specific defective glycan processing step and provides an insight into pathogenesis. Glycobiology 13(9), 601–622 (2003)
    • (2003) Glycobiology , vol.13 , Issue.9 , pp. 601-622
    • Butler, M.1
  • 79
    • 60149111900 scopus 로고    scopus 로고
    • Characterization of glycopeptides by combining collision-induced dissociation and electron-transfer dissociation mass spectrometry data
    • COI: 1:CAS:528:DC%2BD1MXptVykug%3D%3D, PID: 19065542
    • Alley, W.R., Mechref, Y., Novotny, M.V.: Characterization of glycopeptides by combining collision-induced dissociation and electron-transfer dissociation mass spectrometry data. Rapid Commun. Mass Spectrom. 23(1), 161–170 (2009)
    • (2009) Rapid Commun. Mass Spectrom. , vol.23 , Issue.1 , pp. 161-170
    • Alley, W.R.1    Mechref, Y.2    Novotny, M.V.3
  • 80
    • 84868123896 scopus 로고    scopus 로고
    • Use of CID/ETD mass spectrometry to analyze glycopeptides
    • Mechref, Y.: Use of CID/ETD mass spectrometry to analyze glycopeptides. Current Protocols Protein Sci: p. 12.11. 1–12.11. 11 (2012)
    • (2012) Current Protocols Protein Sci: p. 12.11. , vol.11 , Issue.11 , pp. 1-12
    • Mechref, Y.1
  • 81
    • 34047164035 scopus 로고    scopus 로고
    • Glycoproteomics based on tandem mass spectrometry of glycopeptides
    • COI: 1:CAS:528:DC%2BD2sXjvFeisLs%3D
    • Wuhrer, M., et al.: Glycoproteomics based on tandem mass spectrometry of glycopeptides. J. Chromatogr. B 849(1), 115–128 (2007)
    • (2007) J. Chromatogr. B , vol.849 , Issue.1 , pp. 115-128
    • Wuhrer, M.1
  • 82
    • 84856692718 scopus 로고    scopus 로고
    • De novo sequencing and homology searching
    • Ma, B., Johnson R.: De novo sequencing and homology searching. Mol. Cell. Proteomics. 11(2): p. O111. 014902 (2012)
    • (2012) Mol. Cell. Proteomics. 11(2) , vol.14902 , pp. O111
    • Ma, B.1    Johnson, R.2
  • 83
    • 84907828149 scopus 로고    scopus 로고
    • Confident assignment of site-specific glycosylation in complex glycoproteins in a single step
    • COI: 1:CAS:528:DC%2BC2cXhsValsbvI, PID: 25153361
    • Khatri, K., et al.: Confident assignment of site-specific glycosylation in complex glycoproteins in a single step. J. Proteome Res. 13(10), 4347–4355 (2014)
    • (2014) J. Proteome Res. , vol.13 , Issue.10 , pp. 4347-4355
    • Khatri, K.1
  • 84
    • 84862317182 scopus 로고    scopus 로고
    • Sequential multiplexed analyte quantification using peptide immunoaffinity enrichment coupled to mass spectrometry
    • Whiteaker, J.R., et al.: Sequential multiplexed analyte quantification using peptide immunoaffinity enrichment coupled to mass spectrometry. Molecular & Cellular Proteomics. 11(6): p. M111. 015347 (2012)
    • (2012) Molecular & Cellular Proteomics. 11(6) , vol.15347 , pp. M111
    • Whiteaker, J.R.1
  • 85
    • 84866517384 scopus 로고    scopus 로고
    • Glycopeptide enrichment and separation for protein glycosylation analysis
    • COI: 1:CAS:528:DC%2BC38XhtlKisr3E, PID: 22997027
    • Ongay, S., et al.: Glycopeptide enrichment and separation for protein glycosylation analysis. J. Sep. Sci. 35(18), 2341–2372 (2012)
    • (2012) J. Sep. Sci. , vol.35 , Issue.18 , pp. 2341-2372
    • Ongay, S.1
  • 86
    • 5644244327 scopus 로고    scopus 로고
    • Approach to the comprehensive analysis of glycoproteins isolated from human serum using a multi-lectin affinity column
    • COI: 1:CAS:528:DC%2BD2cXos1yqtbk%3D, PID: 15543974
    • Yang, Z., Hancock, W.S.: Approach to the comprehensive analysis of glycoproteins isolated from human serum using a multi-lectin affinity column. J. Chromatogr. A 1053(1), 79–88 (2004)
    • (2004) J. Chromatogr. A , vol.1053 , Issue.1 , pp. 79-88
    • Yang, Z.1    Hancock, W.S.2
  • 87
    • 33646873090 scopus 로고    scopus 로고
    • Approaches to the study of N-linked glycoproteins in human plasma using lectin affinity chromatography and nano-HPLC coupled to electrospray linear ion trap—Fourier transform mass spectrometry
    • COI: 1:CAS:528:DC%2BD28XkvVSrs7o%3D, PID: 16497783
    • Wang, Y., Wu, S.-l., Hancock, W.S.: Approaches to the study of N-linked glycoproteins in human plasma using lectin affinity chromatography and nano-HPLC coupled to electrospray linear ion trap—Fourier transform mass spectrometry. Glycobiology 16(6), 514–523 (2006)
    • (2006) Glycobiology , vol.16 , Issue.6 , pp. 514-523
    • Wang, Y.1    Wu, S.-L.2    Hancock, W.S.3
  • 88
    • 84887406672 scopus 로고    scopus 로고
    • N-and O-glycosylation in the murine synaptosome
    • COI: 1:CAS:528:DC%2BC3sXhvFWku7bN, PID: 23816992
    • Trinidad, J.C., et al.: N-and O-glycosylation in the murine synaptosome. Mol. Cell. Proteomics 12(12), 3474–3488 (2013)
    • (2013) Mol. Cell. Proteomics , vol.12 , Issue.12 , pp. 3474-3488
    • Trinidad, J.C.1
  • 89
    • 84861990380 scopus 로고    scopus 로고
    • Selected reaction monitoring-based proteomics: workflows, potential, pitfalls and future directions
    • COI: 1:CAS:528:DC%2BC38XotVSrurg%3D, PID: 22669653
    • Picotti, P., Aebersold, R.: Selected reaction monitoring-based proteomics: workflows, potential, pitfalls and future directions. Nat. Methods 9(6), 555–566 (2012)
    • (2012) Nat. Methods , vol.9 , Issue.6 , pp. 555-566
    • Picotti, P.1    Aebersold, R.2
  • 90
    • 84884273245 scopus 로고    scopus 로고
    • Absolute quantitation of immunoglobulin G and its glycoforms using multiple reaction monitoring
    • COI: 1:CAS:528:DC%2BC3sXht1KltLjP, PID: 23944609
    • Hong, Q., et al.: Absolute quantitation of immunoglobulin G and its glycoforms using multiple reaction monitoring. Anal. Chem. 85(18), 8585–8593 (2013)
    • (2013) Anal. Chem. , vol.85 , Issue.18 , pp. 8585-8593
    • Hong, Q.1
  • 91
    • 38349080026 scopus 로고    scopus 로고
    • N-glycosylation site occupancy in serum glycoproteins using multiple reaction monitoring liquid chromatography-mass spectrometry
    • PID: 17823199, COI: 1:CAS:528:DC%2BD1cXksF2itw%3D%3D
    • Hülsmeier, A.J., Paesold-Burda, P., Hennet, T.: N-glycosylation site occupancy in serum glycoproteins using multiple reaction monitoring liquid chromatography-mass spectrometry. Mol. Cell. Proteomics 6(12), 2132–2138 (2007)
    • (2007) Mol. Cell. Proteomics , vol.6 , Issue.12 , pp. 2132-2138
    • Hülsmeier, A.J.1    Paesold-Burda, P.2    Hennet, T.3
  • 92
    • 84936797513 scopus 로고    scopus 로고
    • Large-scale measurement of absolute protein glycosylation stoichiometry
    • Sun, S., Zhang H.: Large-scale measurement of absolute protein glycosylation stoichiometry. Analytical Chem, (2015)
    • (2015) Analytical Chem
    • Sun, S.1    Zhang, H.2
  • 93
    • 79955563481 scopus 로고    scopus 로고
    • Change of transferrin sialylation differs between mild sepsis and severe sepsis and septic shock
    • COI: 1:CAS:528:DC%2BC38XhsVynsbvP, PID: 21498934
    • Gornik, O., et al.: Change of transferrin sialylation differs between mild sepsis and severe sepsis and septic shock. Intern. Med. 50(8), 861–869 (2011)
    • (2011) Intern. Med. , vol.50 , Issue.8 , pp. 861-869
    • Gornik, O.1
  • 94
    • 84905248156 scopus 로고    scopus 로고
    • Comparison of sialylated N-glycopeptide levels in serum of pancreatic cancer patients, acute pancreatitis patients, and healthy controls
    • COI: 1:CAS:528:DC%2BC2cXht1GhtLbJ, PID: 24841998
    • Kontro, H., et al.: Comparison of sialylated N-glycopeptide levels in serum of pancreatic cancer patients, acute pancreatitis patients, and healthy controls. Proteomics 14(15), 1713–1723 (2014)
    • (2014) Proteomics , vol.14 , Issue.15 , pp. 1713-1723
    • Kontro, H.1
  • 95
    • 77956116587 scopus 로고    scopus 로고
    • OVA1 test for preoperative assessment of ovarian cancer
    • Abraham, J.: OVA1 test for preoperative assessment of ovarian cancer. Commun. Oncol. 7(6), 249–250 (2010)
    • (2010) Commun. Oncol. , vol.7 , Issue.6 , pp. 249-250
    • Abraham, J.1
  • 96
    • 84893679825 scopus 로고    scopus 로고
    • α-1-Antitrypsin deficiency: clinical variability, assessment, and treatment
    • COI: 1:CAS:528:DC%2BC2cXksFChsg%3D%3D, PID: 24380646
    • Stockley, R.A., Turner, A.M.: α-1-Antitrypsin deficiency: clinical variability, assessment, and treatment. Trends Mol. Med. 20(2), 105–115 (2014)
    • (2014) Trends Mol. Med. , vol.20 , Issue.2 , pp. 105-115
    • Stockley, R.A.1    Turner, A.M.2
  • 98
    • 84943348000 scopus 로고    scopus 로고
    • Differentially expressed glycosylated patterns of alpha-1-antitrypsin as serum biomarkers for the diagnosis of lung cancer. Glycobiology: p
    • Liang, Y., et al.: Differentially expressed glycosylated patterns of alpha-1-antitrypsin as serum biomarkers for the diagnosis of lung cancer. Glycobiology: p. cwu115 (2014)
    • (2014) cwu115
    • Liang, Y.1
  • 99
    • 79953704533 scopus 로고    scopus 로고
    • Novel glycan biomarkers for the detection of lung cancer
    • COI: 1:CAS:528:DC%2BC3MXjt1Sgtbk%3D, PID: 21214223
    • Arnold, J.N., et al.: Novel glycan biomarkers for the detection of lung cancer. J. Proteome Res. 10(4), 1755–1764 (2011)
    • (2011) J. Proteome Res. , vol.10 , Issue.4 , pp. 1755-1764
    • Arnold, J.N.1
  • 100
    • 36248972262 scopus 로고    scopus 로고
    • Ovarian cancer is associated with changes in glycosylation in both acute-phase proteins and IgG
    • COI: 1:CAS:528:DC%2BD2sXhtlejsrbL, PID: 17884841
    • Saldova, R., et al.: Ovarian cancer is associated with changes in glycosylation in both acute-phase proteins and IgG. Glycobiology 17(12), 1344–1356 (2007)
    • (2007) Glycobiology , vol.17 , Issue.12 , pp. 1344-1356
    • Saldova, R.1
  • 101
    • 79952389488 scopus 로고    scopus 로고
    • Glycomic and glycoproteomic analysis of serum from patients with stomach cancer reveals potential markers arising from host defense response mechanisms
    • COI: 1:CAS:528:DC%2BC3MXnvVSkuw%3D%3D
    • Bones, J., et al.: Glycomic and glycoproteomic analysis of serum from patients with stomach cancer reveals potential markers arising from host defense response mechanisms. J. Proteome Res. 10(3), 1246–1265 (2010)
    • (2010) J. Proteome Res. , vol.10 , Issue.3 , pp. 1246-1265
    • Bones, J.1
  • 102
    • 33646343959 scopus 로고    scopus 로고
    • Fucosylated haptoglobin is a novel marker for pancreatic cancer: a detailed analysis of the oligosaccharide structure and a possible mechanism for fucosylation
    • COI: 1:CAS:528:DC%2BD28Xks1SisLg%3D, PID: 16385567
    • Okuyama, N., et al.: Fucosylated haptoglobin is a novel marker for pancreatic cancer: a detailed analysis of the oligosaccharide structure and a possible mechanism for fucosylation. Int. J. Cancer 118(11), 2803–2808 (2006)
    • (2006) Int. J. Cancer , vol.118 , Issue.11 , pp. 2803-2808
    • Okuyama, N.1
  • 103
    • 50449103968 scopus 로고    scopus 로고
    • Fucosylated haptoglobin is a novel marker for pancreatic cancer: detailed analyses of oligosaccharide structures
    • COI: 1:CAS:528:DC%2BD1cXhtVGqs7%2FP, PID: 18646007
    • Miyoshi, E., Nakano, M.: Fucosylated haptoglobin is a novel marker for pancreatic cancer: detailed analyses of oligosaccharide structures. Proteomics 8(16), 3257–3262 (2008)
    • (2008) Proteomics , vol.8 , Issue.16 , pp. 3257-3262
    • Miyoshi, E.1    Nakano, M.2
  • 104
    • 79957827175 scopus 로고    scopus 로고
    • Altered glycosylation and expression of plasma alpha-1-acid glycoprotein and haptoglobin in rheumatoid arthritis
    • COI: 1:CAS:528:DC%2BC3MXntFSmtLk%3D
    • Saroha, A., et al.: Altered glycosylation and expression of plasma alpha-1-acid glycoprotein and haptoglobin in rheumatoid arthritis. J. Chromatogr. B 879(20), 1839–1843 (2011)
    • (2011) J. Chromatogr. B , vol.879 , Issue.20 , pp. 1839-1843
    • Saroha, A.1
  • 105
    • 84898876600 scopus 로고    scopus 로고
    • Identification and validation of novel candidate protein biomarkers for the detection of human gastric cancer
    • COI: 1:CAS:528:DC%2BC2cXkt1Sqt7o%3D
    • Humphries, J.M., et al.: Identification and validation of novel candidate protein biomarkers for the detection of human gastric cancer. Biochimica et Biophysica Acta (BBA)-Proteins and Proteomics 1844(5), 1051–1058 (2014)
    • (2014) Biochimica et Biophysica Acta (BBA)-Proteins and Proteomics , vol.1844 , Issue.5 , pp. 1051-1058
    • Humphries, J.M.1
  • 106
    • 61849124770 scopus 로고    scopus 로고
    • Identification and development of fucosylated glycoproteins as biomarkers of primary hepatocellular carcinoma
    • COI: 1:CAS:528:DC%2BD1cXhsFals7jL
    • Comunale, M.A., et al.: Identification and development of fucosylated glycoproteins as biomarkers of primary hepatocellular carcinoma. J. Proteome Res. 8(2), 595–602 (2008)
    • (2008) J. Proteome Res. , vol.8 , Issue.2 , pp. 595-602
    • Comunale, M.A.1
  • 107
    • 77953697951 scopus 로고    scopus 로고
    • Glycosylation of liver acute-phase proteins in pancreatic cancer and chronic pancreatitis
    • COI: 1:CAS:528:DC%2BC3cXktFyru7w%3D, PID: 21137062
    • Sarrats, A., et al.: Glycosylation of liver acute-phase proteins in pancreatic cancer and chronic pancreatitis. PROTEOMICS-Clinical Applications 4(4), 432–448 (2010)
    • (2010) PROTEOMICS-Clinical Applications , vol.4 , Issue.4 , pp. 432-448
    • Sarrats, A.1
  • 108
    • 0028970893 scopus 로고
    • Serum α1-antichymotrypsin level as a marker for Alzheimer-type dementia
    • COI: 1:CAS:528:DyaK2MXpsVShu7c%3D, PID: 8532107
    • Lieberman, J., et al.: Serum α1-antichymotrypsin level as a marker for Alzheimer-type dementia. Neurobiol. Aging 16(5), 747–753 (1995)
    • (1995) Neurobiol. Aging , vol.16 , Issue.5 , pp. 747-753
    • Lieberman, J.1
  • 109
    • 0027274715 scopus 로고
    • Abnormal glycosylation of α2-macroglobulin, a non-acute-phase protein, in patients with autoimmune diseases
    • COI: 1:CAS:528:DyaK2cXhtVCrs7Y%3D, PID: 7691738
    • Saso, L., et al.: Abnormal glycosylation of α2-macroglobulin, a non-acute-phase protein, in patients with autoimmune diseases. Inflammation 17(4), 465–479 (1993)
    • (1993) Inflammation , vol.17 , Issue.4 , pp. 465-479
    • Saso, L.1
  • 110
    • 58149400525 scopus 로고    scopus 로고
    • Fucosylated glycoproteins as markers of liver disease
    • COI: 1:CAS:528:DC%2BD1MXhsVOitA%3D%3D, PID: 19126969
    • Mehta, A., Block, T.M.: Fucosylated glycoproteins as markers of liver disease. Dis. Markers 25(4–5), 259–265 (2008)
    • (2008) Dis. Markers , vol.25 , Issue.4-5 , pp. 259-265
    • Mehta, A.1    Block, T.M.2
  • 111
    • 43949133012 scopus 로고    scopus 로고
    • Low glycosylated ferritin, a good marker for the diagnosis of hemophagocytic syndrome
    • COI: 1:CAS:528:DC%2BD1cXms1egs7w%3D
    • Fardet, L., et al.: Low glycosylated ferritin, a good marker for the diagnosis of hemophagocytic syndrome. Arthritis & Rheumatism 58(5), 1521–1527 (2008)
    • (2008) Arthritis & Rheumatism , vol.58 , Issue.5 , pp. 1521-1527
    • Fardet, L.1
  • 112
    • 84902106515 scopus 로고    scopus 로고
    • Mass-selected site-specific core-fucosylation of ceruloplasmin in alcohol-related hepatocellular carcinoma
    • COI: 1:CAS:528:DC%2BC2cXntlGisb8%3D, PID: 24799124
    • Yin, H., et al.: Mass-selected site-specific core-fucosylation of ceruloplasmin in alcohol-related hepatocellular carcinoma. J. Proteome Res. 13(6), 2887–2896 (2014)
    • (2014) J. Proteome Res. , vol.13 , Issue.6 , pp. 2887-2896
    • Yin, H.1
  • 113
    • 32444436394 scopus 로고    scopus 로고
    • Proteomic analysis of serum associated fucosylated glycoproteins in the development of primary hepatocellular carcinoma
    • COI: 1:CAS:528:DC%2BD28XlvFSg, PID: 16457596
    • Comunale, M.A., et al.: Proteomic analysis of serum associated fucosylated glycoproteins in the development of primary hepatocellular carcinoma. J. Proteome Res. 5(2), 308–315 (2006)
    • (2006) J. Proteome Res. , vol.5 , Issue.2 , pp. 308-315
    • Comunale, M.A.1
  • 114
    • 84921524523 scopus 로고    scopus 로고
    • Identification of potential pancreatic cancer serum markers: increased sialyl-Lewis X on ceruloplasmin
    • PID: 25595436, COI: 1:CAS:528:DC%2BC2MXht12qsbY%3D
    • Balmaña, M., et al.: Identification of potential pancreatic cancer serum markers: increased sialyl-Lewis X on ceruloplasmin. Clin. Chim. Acta 442, 56–62 (2015)
    • (2015) Clin. Chim. Acta , vol.442 , pp. 56-62
    • Balmaña, M.1
  • 115
    • 0037342073 scopus 로고    scopus 로고
    • Positive predictive value of serum thyroglobulin levels, measured during the first year of follow-up after thyroid hormone withdrawal, in thyroid cancer patients
    • COI: 1:CAS:528:DC%2BD3sXit1egu78%3D
    • Baudin, E., et al.: Positive predictive value of serum thyroglobulin levels, measured during the first year of follow-up after thyroid hormone withdrawal, in thyroid cancer patients. The Journal of Clinical Endocrinology & Metabolism 88(3), 1107–1111 (2003)
    • (2003) The Journal of Clinical Endocrinology & Metabolism , vol.88 , Issue.3 , pp. 1107-1111
    • Baudin, E.1
  • 116
    • 84858702695 scopus 로고    scopus 로고
    • Thyroid function in PMM2-CDG: diagnostic approach and proposed management
    • COI: 1:CAS:528:DC%2BC38Xjt1Kjs70%3D, PID: 22386715
    • Mohamed, M., et al.: Thyroid function in PMM2-CDG: diagnostic approach and proposed management. Mol. Genet. Metab. 105(4), 681–683 (2012)
    • (2012) Mol. Genet. Metab. , vol.105 , Issue.4 , pp. 681-683
    • Mohamed, M.1
  • 117
    • 0028791186 scopus 로고
    • Thyroid function tests and characterization of thyroxine-binding globulin in the carbohydrate-deficient glycoprotein syndrome type I
    • COI: 1:CAS:528:DyaK2MXpvFSisro%3D
    • Macchia, P.E., et al.: Thyroid function tests and characterization of thyroxine-binding globulin in the carbohydrate-deficient glycoprotein syndrome type I. The Journal of Clinical Endocrinology & Metabolism 80(12), 3744–3749 (1995)
    • (1995) The Journal of Clinical Endocrinology & Metabolism , vol.80 , Issue.12 , pp. 3744-3749
    • Macchia, P.E.1
  • 118
    • 0034958398 scopus 로고    scopus 로고
    • Serum thyroid-stimulating hormone measurement for assessment of thyroid function and disease
    • COI: 1:CAS:528:DC%2BD3MXltlKis7s%3D
    • Ross, D.S.: Serum thyroid-stimulating hormone measurement for assessment of thyroid function and disease. Endocrinol. Metab. Clin. N. Am. 30(2), 245–264 (2001)
    • (2001) Endocrinol. Metab. Clin. N. Am. , vol.30 , Issue.2 , pp. 245-264
    • Ross, D.S.1
  • 119
    • 84930606343 scopus 로고    scopus 로고
    • Clusterin glycopeptide variant characterization reveals significant site-specific glycan changes in the plasma of clear cell renal cell carcinoma, J Proteome Res
    • Gbormittah, F.O., et al.: Clusterin glycopeptide variant characterization reveals significant site-specific glycan changes in the plasma of clear cell renal cell carcinoma. J Proteome Res, (2015)
    • (2015) et al.
    • Gbormittah, F.O.1
  • 120
    • 34249688237 scopus 로고    scopus 로고
    • Plasma proteomics of pancreatic cancer patients by multi-dimensional liquid chromatography and two-dimensional difference gel electrophoresis (2D-DIGE): up-regulation of leucine-rich alpha-2-glycoprotein in pancreatic cancer
    • COI: 1:CAS:528:DC%2BD2sXmtVGms7c%3D
    • Kakisaka, T., et al.: Plasma proteomics of pancreatic cancer patients by multi-dimensional liquid chromatography and two-dimensional difference gel electrophoresis (2D-DIGE): up-regulation of leucine-rich alpha-2-glycoprotein in pancreatic cancer. J. Chromatogr. B 852(1), 257–267 (2007)
    • (2007) J. Chromatogr. B , vol.852 , Issue.1 , pp. 257-267
    • Kakisaka, T.1
  • 121
    • 26944438148 scopus 로고    scopus 로고
    • POMT2 mutations cause α-dystroglycan hypoglycosylation and Walker-Warburg syndrome
    • PID: 15894594, COI: 1:CAS:528:DC%2BD28Xkt1Crsg%3D%3D
    • van Reeuwijk, J., et al.: POMT2 mutations cause α-dystroglycan hypoglycosylation and Walker-Warburg syndrome. J. Med. Genet. 42(12), 907–912 (2005)
    • (2005) J. Med. Genet. , vol.42 , Issue.12 , pp. 907-912
    • van Reeuwijk, J.1
  • 122
    • 45549091249 scopus 로고    scopus 로고
    • Plasma glycoprotein profiling for colorectal cancer biomarker identification by lectin glycoarray and lectin blot
    • COI: 1:CAS:528:DC%2BD1cXisVyltr0%3D, PID: 18311904
    • Qiu, Y., et al.: Plasma glycoprotein profiling for colorectal cancer biomarker identification by lectin glycoarray and lectin blot. J. Proteome Res. 7(4), 1693–1703 (2008)
    • (2008) J. Proteome Res. , vol.7 , Issue.4 , pp. 1693-1703
    • Qiu, Y.1
  • 123
    • 84880705235 scopus 로고    scopus 로고
    • Identification of kininogen-1 as a serum biomarker for the early detection of advanced colorectal adenoma and colorectal cancer
    • COI: 1:CAS:528:DC%2BC3sXht1ersb7K, PID: 23894665
    • Wang, J., et al.: Identification of kininogen-1 as a serum biomarker for the early detection of advanced colorectal adenoma and colorectal cancer. PLoS One 8, e70519 (2013)
    • (2013) PLoS One , vol.8
    • Wang, J.1
  • 124
    • 84947202830 scopus 로고    scopus 로고
    • Kallistatin, a new and reliable biomarker for the diagnosis of liver cirrhosis, Acta Pharmaceutica Sinica B
    • Cheng, Z., et al.: Kallistatin, a new and reliable biomarker for the diagnosis of liver cirrhosis. Acta Pharmaceutica Sinica B, (2015)
    • (2015) et al.
    • Cheng, Z.1
  • 125
    • 84928349017 scopus 로고    scopus 로고
    • Afamin—A pleiotropic glycoprotein involved in various disease states
    • COI: 1:CAS:528:DC%2BC2MXmvFaltrg%3D, PID: 25892677
    • Dieplinger, H., Dieplinger, B.: Afamin—A pleiotropic glycoprotein involved in various disease states. Clin. Chim. Acta 446, 105–110 (2015)
    • (2015) Clin. Chim. Acta , vol.446 , pp. 105-110
    • Dieplinger, H.1    Dieplinger, B.2
  • 126
    • 84873743426 scopus 로고    scopus 로고
    • Aberrant PSA glycosylation—a sweet predictor of prostate cancer
    • COI: 1:CAS:528:DC%2BC3sXis1Cnu74%3D, PID: 23318363
    • Gilgunn, S., et al.: Aberrant PSA glycosylation—a sweet predictor of prostate cancer. Nature Reviews Urology 10(2), 99–107 (2013)
    • (2013) Nature Reviews Urology , vol.10 , Issue.2 , pp. 99-107
    • Gilgunn, S.1


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.