{"status":"ok","message-type":"work","message-version":"1.0.0","message":{"indexed":{"date-parts":[[2026,7,30]],"date-time":"2026-07-30T08:39:38Z","timestamp":1785400778715,"version":"3.56.0"},"reference-count":56,"publisher":"MDPI AG","issue":"14","license":[{"start":{"date-parts":[[2026,7,15]],"date-time":"2026-07-15T00:00:00Z","timestamp":1784073600000},"content-version":"vor","delay-in-days":0,"URL":"https:\/\/creativecommons.org\/licenses\/by\/4.0\/"}],"funder":[{"DOI":"10.13039\/501100005668","name":"Funda\u00e7\u00e3o de Apoio \u00e0 Pesquisa do Distrito Federal","doi-asserted-by":"publisher","award":["00193-00002149\/2023-71"],"award-info":[{"award-number":["00193-00002149\/2023-71"]}],"id":[{"id":"10.13039\/501100005668","id-type":"DOI","asserted-by":"publisher"}]},{"name":"Coordena\u00e7\u00e3o de Aperfeicoamento de Pessoal de N\u00edvel Superior","award":["001"],"award-info":[{"award-number":["001"]}]},{"award":["001"],"award-info":[{"award-number":["001"]}],"id":[{"id":"https:\/\/ror.org\/00x0ma614","id-type":"ROR","asserted-by":"publisher"}]}],"content-domain":{"domain":[],"crossmark-restriction":false},"short-container-title":["IJMS"],"abstract":"<jats:p>Congenital disorders of glycosylation (CDG) are a group of inherited metabolic diseases rapidly growing due to the discovery of new subtypes. As with many genetic conditions, their diagnosis can be challenging, impairing proper patient care and causing additional suffering to patients and their families. We have developed an N-glycomics strategy that can provide insightful information towards diagnosing CDG type II (CDG-II). N-glycans released from the plasma of healthy individuals were labeled with deuterated iodomethane, mixed with samples from known or suspected CDG-II individuals, which were derivatized with standard iodomethane, and analyzed by liquid chromatography\u2013mass spectrometry. After identification, relative quantification of 65 glycans was performed, revealing considerable alterations in the N-glycome of several patients. Notably, reduced fucosylation was observed in patients with FUT8-CDG and SLC35C1-CDG. Additionally, individuals with mutations in the MAN1B1 gene exhibited increased amounts of hybrid and oligomannosidic structures, whereas patients with the Golgi homeostasis disorders COG1-CDG and ATP6V0A2-CDG presented marked increases in hypogalactosylated and hyposialylated structures. Multivariate statistical analysis indicated two undiagnosed patients with alterations similar to ATP6V0A2-CDG patients and another two with a profile similar to MAN1B1-CDG patients. Genetic sequencing (targeted gene panel or whole exome sequencing) of these undiagnosed patients revealed variants in the corresponding genes, confirming the diagnosis obtained from the N-glycomics analysis. Our results demonstrate how the analysis of total plasma N-glycans can be used to identify metabolic disorders and diagnose conditions based on their molecular effects on the glycoproteome.<\/jats:p>","DOI":"10.3390\/ijms27146309","type":"journal-article","created":{"date-parts":[[2026,7,16]],"date-time":"2026-07-16T06:49:36Z","timestamp":1784184576000},"page":"6309","update-policy":"https:\/\/doi.org\/10.3390\/mdpi_crossmark_policy","source":"Crossref","is-referenced-by-count":0,"title":["Diagnosis of Congenital Disorders of Glycosylation Type II Subtypes Through Comprehensive N-Glycan Profiling by Mass Spectrometry"],"prefix":"10.3390","volume":"27","author":[{"ORCID":"https:\/\/orcid.org\/0000-0003-4029-3410","authenticated-orcid":false,"given":"Alan R.","family":"M\u00f3l","sequence":"first","affiliation":[{"name":"Laborat\u00f3rio de S\u00edntese e An\u00e1lise de Biomol\u00e9culas\u2014LSAB, Instituto de Qu\u00edmica, Universidade de Bras\u00edlia, Bras\u00edlia 70910-900, Brazil"}],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Nilza do C.","family":"Fontes","sequence":"additional","affiliation":[{"name":"Laborat\u00f3rio de Gen\u00e9tica Bioqu\u00edmica, Rede Sarah de Hospitais de Reabilita\u00e7\u00e3o, Bras\u00edlia 70335-901, Brazil"}],"role":[{"vocabulary":"crossref","role":"author"}]},{"ORCID":"https:\/\/orcid.org\/0009-0001-0615-0777","authenticated-orcid":false,"given":"Savana C. L.","family":"Santos","sequence":"additional","affiliation":[{"name":"Laborat\u00f3rio de Biologia Molecular, Rede Sarah de Hospitais de Reabilita\u00e7\u00e3o, Bras\u00edlia 70335-901, Brazil"}],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Cynthia","family":"Costa e Silva","sequence":"additional","affiliation":[{"name":"Laborat\u00f3rio de Biologia Molecular, Rede Sarah de Hospitais de Reabilita\u00e7\u00e3o, Bras\u00edlia 70335-901, Brazil"}],"role":[{"vocabulary":"crossref","role":"author"}]},{"ORCID":"https:\/\/orcid.org\/0000-0002-8809-7825","authenticated-orcid":false,"given":"Gerson da S.","family":"Carvalho","sequence":"additional","affiliation":[{"name":"Hospital de Apoio de Bras\u00edlia, Secretaria de Sa\u00fade do Distrito Federal, Bras\u00edlia 70684-831, Brazil"}],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Bruno J. C. B.","family":"Lima","sequence":"additional","affiliation":[{"name":"Hospital Universit\u00e1rio J\u00falio Muller, Faculdade de Medicina, Universidade Federal de Mato Grosso, Cuiab\u00e1 78048-902, Brazil"}],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Walqu\u00edria D.","family":"de Mello","sequence":"additional","affiliation":[{"name":"Cl\u00ednica de Pediatria do Hospital Infantil Jo\u00e3o Paulo II, Funda\u00e7\u00e3o Hospitalar do Estado de Minas Gerais, Belo Horizonte 30130-110, Brazil"}],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Daniel R.","family":"de Carvalho","sequence":"additional","affiliation":[{"name":"Laborat\u00f3rio de Gen\u00e9tica Bioqu\u00edmica, Rede Sarah de Hospitais de Reabilita\u00e7\u00e3o, Bras\u00edlia 70335-901, Brazil"}],"role":[{"vocabulary":"crossref","role":"author"}]},{"ORCID":"https:\/\/orcid.org\/0000-0002-7613-4414","authenticated-orcid":false,"given":"Eder A.","family":"Barbosa","sequence":"additional","affiliation":[{"name":"Laborat\u00f3rio de S\u00edntese e An\u00e1lise de Biomol\u00e9culas\u2014LSAB, Instituto de Qu\u00edmica, Universidade de Bras\u00edlia, Bras\u00edlia 70910-900, Brazil"}],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Dirk J.","family":"Lefeber","sequence":"additional","affiliation":[{"name":"Translational Metabolic Laboratory, Department of Human Genetics, Donders Center for Brain, Cognition, and Behavior, Radboud University Medical Center, 6525 Nijmegen, The Netherlands"}],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Juliana F.","family":"Mazzeu","sequence":"additional","affiliation":[{"name":"Laborat\u00f3rio de Gen\u00e9tica Cl\u00ednica, Faculdade de Medicina, Universidade de Bras\u00edlia, Bras\u00edlia 70910-900, Brazil"}],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Jaime M.","family":"Brum","sequence":"additional","affiliation":[{"name":"Laborat\u00f3rio de S\u00edntese e An\u00e1lise de Biomol\u00e9culas\u2014LSAB, Instituto de Qu\u00edmica, Universidade de Bras\u00edlia, Bras\u00edlia 70910-900, Brazil"}],"role":[{"vocabulary":"crossref","role":"author"}]},{"ORCID":"https:\/\/orcid.org\/0000-0002-1615-0009","authenticated-orcid":false,"given":"Guilherme D.","family":"Brand","sequence":"additional","affiliation":[{"name":"Laborat\u00f3rio de S\u00edntese e An\u00e1lise de Biomol\u00e9culas\u2014LSAB, Instituto de Qu\u00edmica, Universidade de Bras\u00edlia, Bras\u00edlia 70910-900, Brazil"}],"role":[{"vocabulary":"crossref","role":"author"}]}],"member":"1968","published-online":{"date-parts":[[2026,7,15]]},"reference":[{"key":"ref_1","doi-asserted-by":"crossref","first-page":"179","DOI":"10.1203\/00006450-198002000-00117","article-title":"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?: 90","volume":"14","author":"Jaeken","year":"1980","journal-title":"Pediatr. Res."},{"key":"ref_2","doi-asserted-by":"crossref","first-page":"108476","DOI":"10.1016\/j.ymgme.2024.108476","article-title":"Clinical and Biochemical Footprints of Congenital Disorders of Glycosylation: Proposed Nosology","volume":"142","author":"Ng","year":"2024","journal-title":"Mol. Genet. Metab."},{"key":"ref_3","doi-asserted-by":"crossref","first-page":"345","DOI":"10.1007\/s10719-015-9639-x","article-title":"Clinical Diagnostics and Therapy Monitoring in the Congenital Disorders of Glycosylation","volume":"33","author":"Willems","year":"2016","journal-title":"Glycoconj. J."},{"key":"ref_4","doi-asserted-by":"crossref","first-page":"1184","DOI":"10.1007\/s10545-005-0113-y","article-title":"Genetic Variants of Transferrin in the Diagnosis of Protein Hypoglycosylation","volume":"28","author":"Albahri","year":"2005","journal-title":"J. Inherit. Metab. Dis."},{"key":"ref_5","doi-asserted-by":"crossref","first-page":"1310","DOI":"10.1002\/jimd.12273","article-title":"Screening for Abnormal Glycosylation in a Cohort of Adult Liver Disease Patients","volume":"43","author":"Jansen","year":"2020","journal-title":"J. Inherit. Metab. Dis."},{"key":"ref_6","doi-asserted-by":"crossref","unstructured":"Bogda\u0144ska, A., Lipi\u0144ski, P., Szyma\u0144ska-Ro\u017cek, P., Jankowska, I., Socha, P., and Tylki-Szyma\u0144ska, A. (2021). Pediatric Liver Disease Patients and Secondary Glycosylation Abnormalities. Front. Pediatr., 8.","DOI":"10.3389\/fped.2020.613224"},{"key":"ref_7","doi-asserted-by":"crossref","first-page":"123","DOI":"10.1136\/adc.71.2.123","article-title":"Carbohydrate Deficient Glycoprotein Syndrome Type II: A Deficiency in Golgi Localised N-Acetyl-Glucosaminyltransferase II","volume":"71","author":"Jaeken","year":"1994","journal-title":"Arch. Dis. Child."},{"key":"ref_8","doi-asserted-by":"crossref","first-page":"78","DOI":"10.1016\/j.ymgme.2013.05.012","article-title":"Molecular Diagnostic Testing for Congenital Disorders of Glycosylation (CDG): Detection Rate for Single Gene Testing and next Generation Sequencing Panel Testing","volume":"110","author":"Jones","year":"2013","journal-title":"Mol. Genet. Metab."},{"key":"ref_9","doi-asserted-by":"crossref","first-page":"15","DOI":"10.1016\/j.ajhg.2012.05.002","article-title":"TMEM165 Deficiency Causes a Congenital Disorder of Glycosylation","volume":"91","author":"Foulquier","year":"2012","journal-title":"Am. J. Hum. Genet."},{"key":"ref_10","doi-asserted-by":"crossref","first-page":"81","DOI":"10.1186\/s13023-025-03535-4","article-title":"An ALG12-CDG Patient with a Novel Homozygous Intronic Mutation Associated with Low ALG12 mRNA","volume":"20","author":"Andriantsihoarana","year":"2025","journal-title":"Orphanet. J. Rare. Dis."},{"key":"ref_11","doi-asserted-by":"crossref","first-page":"1","DOI":"10.1016\/j.ymgme.2018.11.003","article-title":"The Challenge of CDG Diagnosis","volume":"126","author":"Francisco","year":"2019","journal-title":"Mol. Genet. Metab."},{"key":"ref_12","doi-asserted-by":"crossref","first-page":"769","DOI":"10.1002\/jimd.12496","article-title":"Synergistic Use of Glycomics and Single-molecule Molecular Inversion Probes for Identification of Congenital Disorders of Glycosylation Type-1","volume":"45","author":"Ashikov","year":"2022","journal-title":"J. Inherit. Metab. Dis."},{"key":"ref_13","doi-asserted-by":"crossref","first-page":"A0169","DOI":"10.5702\/massspectrometry.A0169","article-title":"Mass Spectrometry as a First-Line Diagnostic Aid for Congenital Disorders of Glycosylation","volume":"14","author":"Wada","year":"2025","journal-title":"Mass Spectrom."},{"key":"ref_14","doi-asserted-by":"crossref","first-page":"639","DOI":"10.1016\/j.trsl.2015.07.005","article-title":"High-Resolution Mass Spectrometry Glycoprofiling of Intact Transferrin for Diagnosis and Subtype Identification in the Congenital Disorders of Glycosylation","volume":"166","author":"Steenbergen","year":"2015","journal-title":"Transl. Res."},{"key":"ref_15","doi-asserted-by":"crossref","first-page":"A0103","DOI":"10.5702\/massspectrometry.A0103","article-title":"Electrospray Ionization Mass Spectrometry of Transferrin: Use of Quadrupole Mass Analyzers for Congenital Disorders of Glycosylation","volume":"11","author":"Wada","year":"2022","journal-title":"Mass Spectrom."},{"key":"ref_16","doi-asserted-by":"crossref","first-page":"102","DOI":"10.1016\/j.cca.2019.02.013","article-title":"Relative Quantification of Plasma N-Glycans in Type II Congenital Disorder of Glycosylation Patients by Mass Spectrometry","volume":"492","author":"Barbosa","year":"2019","journal-title":"Clin. Chim. Acta"},{"key":"ref_17","doi-asserted-by":"crossref","first-page":"178","DOI":"10.1016\/j.ab.2013.07.037","article-title":"Serum N-Glycan and O-Glycan Analysis by Mass Spectrometry for Diagnosis of Congenital Disorders of Glycosylation","volume":"442","author":"Xia","year":"2013","journal-title":"Anal. Biochem."},{"key":"ref_18","doi-asserted-by":"crossref","first-page":"179","DOI":"10.1016\/j.jare.2023.09.002","article-title":"Plasma Glycoproteomics Delivers High-Specificity Disease Biomarkers by Detecting Site-Specific Glycosylation Abnormalities","volume":"61","author":"Wessels","year":"2024","journal-title":"J. Adv. Res."},{"key":"ref_19","doi-asserted-by":"crossref","first-page":"A0084","DOI":"10.5702\/massspectrometry.A0084","article-title":"Matrix-Assisted Laser Desorption\/Ionization Mass Spectrometry to Detect Diagnostic Glycopeptide Markers of Congenital Disorders of Glycosylation","volume":"9","author":"Wada","year":"2020","journal-title":"Mass Spectrom."},{"key":"ref_20","doi-asserted-by":"crossref","first-page":"297","DOI":"10.1007\/s10719-015-9636-0","article-title":"Mass Spectrometry of Transferrin and Apolipoprotein C-III for Diagnosis and Screening of Congenital Disorder of Glycosylation","volume":"33","author":"Wada","year":"2016","journal-title":"Glycoconj. J."},{"key":"ref_21","doi-asserted-by":"crossref","first-page":"593","DOI":"10.1373\/clinchem.2010.153635","article-title":"Plasma N-Glycan Profiling by Mass Spectrometry for Congenital Disorders of Glycosylation Type II","volume":"57","author":"Guillard","year":"2011","journal-title":"Clin. Chem."},{"key":"ref_22","doi-asserted-by":"crossref","first-page":"499","DOI":"10.1007\/s10545-018-0144-9","article-title":"Clinical Glycomics for the Diagnosis of Congenital Disorders of Glycosylation","volume":"41","author":"Lefeber","year":"2018","journal-title":"J. Inherit. Metab. Dis."},{"key":"ref_23","doi-asserted-by":"crossref","first-page":"2519","DOI":"10.1007\/s00216-017-0235-8","article-title":"Determination of True Ratios of Different N-Glycan Structures in Electrospray Ionization Mass Spectrometry","volume":"409","author":"Thader","year":"2017","journal-title":"Anal. Bioanal. Chem."},{"key":"ref_24","doi-asserted-by":"crossref","first-page":"101328","DOI":"10.1016\/j.gim.2024.101328","article-title":"Biochemical Testing for Congenital Disorders of Glycosylation: A Technical Standard of the American College of Medical Genetics and Genomics (ACMG)","volume":"27","author":"Hall","year":"2025","journal-title":"Genet. Med."},{"key":"ref_25","doi-asserted-by":"crossref","first-page":"677","DOI":"10.1093\/glycob\/cwm033","article-title":"Tools for Glycomics: Relative Quantitation of Glycans by Isotopic Permethylation Using 13CH3I","volume":"17","author":"Warren","year":"2007","journal-title":"Glycobiology"},{"key":"ref_26","doi-asserted-by":"crossref","first-page":"118","DOI":"10.1016\/j.chroma.2010.10.122","article-title":"Comparison of Hydrophilic-Interaction, Reversed-Phase and Porous Graphitic Carbon Chromatography for Glycan Analysis","volume":"1218","author":"Melmer","year":"2011","journal-title":"J. Chromatogr. A"},{"key":"ref_27","doi-asserted-by":"crossref","first-page":"1030","DOI":"10.1093\/brain\/awu019","article-title":"Diagnostic Serum Glycosylation Profile in Patients with Intellectual Disability as a Result of MAN1B1 Deficiency","volume":"137","author":"Timal","year":"2014","journal-title":"Brain"},{"key":"ref_28","doi-asserted-by":"crossref","first-page":"1073","DOI":"10.1093\/glycob\/9.10.1073","article-title":"Cloning and Expression of a Specific Human A1,2-Mannosidase That Trims Man9GlcNAc2 to Man8GlcNAc2 Isomer B during N-Glycan Biosynthesis","volume":"9","author":"Tremblay","year":"1999","journal-title":"Glycobiology"},{"key":"ref_29","doi-asserted-by":"crossref","unstructured":"Hipgrave Ederveen, A.L., de Haan, N., Baerenfaenger, M., Lefeber, D.J., and Wuhrer, M. (2020). Dissecting Total Plasma and Protein-Specific Glycosylation Profiles in Congenital Disorders of Glycosylation. Int. J. Mol. Sci., 21.","DOI":"10.3390\/ijms21207635"},{"key":"ref_30","doi-asserted-by":"crossref","first-page":"285","DOI":"10.1016\/j.cca.2021.05.016","article-title":"Normal Transferrin Patterns in Congenital Disorders of Glycosylation with Golgi Homeostasis Disruption: Apolipoprotein C-III at the Rescue!","volume":"519","author":"Raynor","year":"2021","journal-title":"Clin. Chim. Acta"},{"key":"ref_31","doi-asserted-by":"crossref","first-page":"257","DOI":"10.1007\/s00018-025-05759-w","article-title":"Glycosphingolipid Synthesis Is Impaired in SLC35A2-CDG and Improves with Galactose Supplementation","volume":"82","author":"Idkowiak","year":"2025","journal-title":"Cell. Mol. Life Sci."},{"key":"ref_32","doi-asserted-by":"crossref","unstructured":"Kodr\u00edkov\u00e1, R., Pakanov\u00e1, Z., Krch\u0148\u00e1k, M., \u0160ediv\u00e1, M., \u0160est\u00e1k, S., Kv\u011bto\u0148, F., Beke, G., \u0160alingov\u00e1, A., Skalick\u00e1, K., and Brennerov\u00e1, K. (2023). N-Glycoprofiling of SLC35A2-CDG: Patient with a Novel Hemizygous Variant. Biomedicines, 11.","DOI":"10.3390\/biomedicines11020580"},{"key":"ref_33","doi-asserted-by":"crossref","first-page":"148","DOI":"10.1002\/humu.23145","article-title":"Mutations in TRAPPC11 Are Associated with a Congenital Disorder of Glycosylation","volume":"38","author":"Matalonga","year":"2017","journal-title":"Hum. Mutat."},{"key":"ref_34","doi-asserted-by":"crossref","first-page":"5784","DOI":"10.1021\/ac500335t","article-title":"High-Throughput Profiling of Protein N-Glycosylation by MALDI-TOF-MS Employing Linkage-Specific Sialic Acid Esterification","volume":"86","author":"Reiding","year":"2014","journal-title":"Anal. Chem."},{"key":"ref_35","doi-asserted-by":"crossref","first-page":"2353","DOI":"10.1021\/acs.analchem.6b04150","article-title":"Differentiation of Sialyl Linkage Isomers by One-Pot Sialic Acid Derivatization for Mass Spectrometry-Based Glycan Profiling","volume":"89","author":"Nishikaze","year":"2017","journal-title":"Anal. Chem."},{"key":"ref_36","doi-asserted-by":"crossref","first-page":"309","DOI":"10.1007\/s10719-015-9626-2","article-title":"Human Plasma Protein N-Glycosylation","volume":"33","author":"Clerc","year":"2016","journal-title":"Glycoconj. J."},{"key":"ref_37","doi-asserted-by":"crossref","first-page":"15865","DOI":"10.1021\/acs.chemrev.1c01031","article-title":"High-Throughput Glycomic Methods","volume":"122","author":"Heijs","year":"2022","journal-title":"Chem. Rev."},{"key":"ref_38","doi-asserted-by":"crossref","first-page":"100042","DOI":"10.1016\/j.sampre.2022.100042","article-title":"Sample Preparation Methods for N-Glycomics","volume":"4","author":"Kayili","year":"2022","journal-title":"Adv. Sample Prep."},{"key":"ref_39","doi-asserted-by":"crossref","first-page":"466","DOI":"10.1016\/j.tig.2018.03.002","article-title":"Perspectives on Glycosylation and Its Congenital Disorders","volume":"34","author":"Ng","year":"2018","journal-title":"Trends Genet."},{"key":"ref_40","doi-asserted-by":"crossref","first-page":"144","DOI":"10.1002\/jcp.21744","article-title":"Elevated Golgi pH Impairs Terminal N-Glycosylation by Inducing Mislocalization of Golgi Glycosyltransferases","volume":"220","author":"Rivinoja","year":"2009","journal-title":"J. Cell. Physiol."},{"key":"ref_41","doi-asserted-by":"crossref","first-page":"609","DOI":"10.1007\/s10545-014-9720-9","article-title":"Congenital Disorders of Glycosylation: New Defects and Still Counting","volume":"37","author":"Scott","year":"2014","journal-title":"J. Inherit. Metab. Dis."},{"key":"ref_42","first-page":"1","article-title":"Mass Spectrometry in Clinical Glycomics: The Path from Biomarker Identification to Clinical Implementation","volume":"18","author":"Wuhrer","year":"2020","journal-title":"Clin. Mass Spectrom."},{"key":"ref_43","doi-asserted-by":"crossref","first-page":"5","DOI":"10.1016\/j.trsl.2018.10.005","article-title":"Glycomics in Rare Diseases: From Diagnosis to Mechanism","volume":"206","author":"Davids","year":"2019","journal-title":"Transl. Res."},{"key":"ref_44","doi-asserted-by":"crossref","first-page":"632","DOI":"10.1016\/j.ajhg.2013.03.012","article-title":"Mosaicism of the UDP-Galactose Transporter SLC35A2 Causes a Congenital Disorder of Glycosylation","volume":"92","author":"Ng","year":"2013","journal-title":"Am. J. Hum. Genet."},{"key":"ref_45","doi-asserted-by":"crossref","first-page":"3029","DOI":"10.1093\/hmg\/ddy213","article-title":"Integrating Glycomics and Genomics Uncovers SLC10A7 as Essential Factor for Bone Mineralization by Regulating Post-Golgi Protein Transport and Glycosylation","volume":"27","author":"Ashikov","year":"2018","journal-title":"Hum. Mol. Genet."},{"key":"ref_46","doi-asserted-by":"crossref","unstructured":"Coura, M.d.M.A., Barbosa, E.A., Brand, G.D., Bloch, C., and de Sousa, J.B. (2021). Identification of Differential N-Glycan Compositions in the Serum and Tissue of Colon Cancer Patients by Mass Spectrometry. Biology, 10.","DOI":"10.3390\/biology10040343"},{"key":"ref_47","doi-asserted-by":"crossref","first-page":"105598","DOI":"10.1016\/j.ebiom.2025.105598","article-title":"Blood N-Glycomics Reveals Individuals at Risk for Cognitive Decline and Alzheimer\u2019s Disease","volume":"113","author":"Zhou","year":"2025","journal-title":"eBioMedicine"},{"key":"ref_48","first-page":"908","article-title":"SLC35A2-CDG: Functional Characterization, Expanded Molecular, Clinical, and Biochemical Phenotypes of 30 Unreported Individuals","volume":"40","author":"Ng","year":"2019","journal-title":"Hum. Mutat."},{"key":"ref_49","doi-asserted-by":"crossref","first-page":"181","DOI":"10.1016\/j.ajhg.2013.05.028","article-title":"Recessive TRAPPC11 Mutations Cause a Disease Spectrum of Limb Girdle Muscular Dystrophy and Myopathy with Movement Disorder and Intellectual Disability","volume":"93","author":"Shahrzad","year":"2013","journal-title":"Am. J. Hum. Genet."},{"key":"ref_50","doi-asserted-by":"crossref","unstructured":"Rymen, D., Peanne, R., Mill\u00f3n, M.B., Race, V., Sturiale, L., Garozzo, D., Mills, P., Clayton, P., Asteggiano, C.G., and Quelhas, D. (2013). MAN1B1 Deficiency: An Unexpected CDG-II. PLoS Genet., 9.","DOI":"10.1371\/journal.pgen.1003989"},{"key":"ref_51","doi-asserted-by":"crossref","first-page":"32","DOI":"10.1038\/ng.2007.45","article-title":"Impaired Glycosylation and Cutis Laxa Caused by Mutations in the Vesicular H+-ATPase Subunit ATP6V0A2","volume":"40","author":"Kornak","year":"2008","journal-title":"Nat. Genet."},{"key":"ref_52","doi-asserted-by":"crossref","first-page":"69","DOI":"10.1038\/ng0501-69","article-title":"The Gene Defective in Leukocyte Adhesion Deficiency II Encodes a Putative GDP-Fucose Transporter","volume":"28","author":"Wild","year":"2001","journal-title":"Nat. Genet."},{"key":"ref_53","doi-asserted-by":"crossref","first-page":"73","DOI":"10.1038\/ng0501-73","article-title":"Complementation Cloning Identifies CDG-IIc, a New Type of Congenital Disorders of Glycosylation, as a GDP-Fucose Transporter Deficiency","volume":"28","author":"Marquardt","year":"2001","journal-title":"Nat. Genet."},{"key":"ref_54","doi-asserted-by":"crossref","first-page":"72","DOI":"10.1093\/glycob\/cwz080","article-title":"GlyGen: Computational and Informatics Resources for Glycoscience","volume":"30","author":"York","year":"2020","journal-title":"Glycobiology"},{"key":"ref_55","doi-asserted-by":"crossref","first-page":"1357","DOI":"10.1515\/hsz-2012-0135","article-title":"The GlycanBuilder and GlycoWorkbench Glycoinformatics Tools: Updates and New Developments","volume":"393","author":"Damerell","year":"2012","journal-title":"Biol. Chem."},{"key":"ref_56","doi-asserted-by":"crossref","first-page":"405","DOI":"10.1038\/gim.2015.30","article-title":"Standards and Guidelines for the Interpretation of Sequence Variants: A Joint Consensus Recommendation of the American College of Medical Genetics and Genomics and the Association for Molecular Pathology","volume":"17","author":"Richards","year":"2015","journal-title":"Genet. Med."}],"container-title":["International Journal of Molecular Sciences"],"original-title":[],"language":"en","link":[{"URL":"https:\/\/www.mdpi.com\/1422-0067\/27\/14\/6309\/pdf","content-type":"unspecified","content-version":"vor","intended-application":"similarity-checking"}],"deposited":{"date-parts":[[2026,7,16]],"date-time":"2026-07-16T08:09:01Z","timestamp":1784189341000},"score":1,"resource":{"primary":{"URL":"https:\/\/www.mdpi.com\/1422-0067\/27\/14\/6309"}},"subtitle":[],"short-title":[],"issued":{"date-parts":[[2026,7,15]]},"references-count":56,"journal-issue":{"issue":"14","published-online":{"date-parts":[[2026,7]]}},"alternative-id":["ijms27146309"],"URL":"https:\/\/doi.org\/10.3390\/ijms27146309","relation":{},"ISSN":["1422-0067"],"issn-type":[{"value":"1422-0067","type":"electronic"}],"subject":[],"published":{"date-parts":[[2026,7,15]]}}}