@article {283,
	title = {A new congenital disorder of glycosylation caused by a mutation in SSR4, the signal sequence receptor 4 protein of the TRAP complex.},
	journal = {Hum Mol Genet},
	volume = {23},
	year = {2014},
	month = {2014 Mar 15},
	pages = {1602-5},
	abstract = {<p>Nearly 50 congenital disorders of glycosylation (CDG) are known, but many patients biochemically diagnosed with CDG do not have mutations in known genes. Here, we describe a 16-year-old male who was born with microcephaly, developed intellectual disability, gastroesophageal reflux and a seizure disorder. We identified a de novo variant in the X-linked SSR4 gene which encodes a protein of the heterotetrameric translocon-associated protein (TRAP) complex. The c.316delT causes a p.F106Sfs*53 in SSR4 and also reduces expression of other TRAP complex proteins. The glycosylation marker Glyc-ER-GFP was used to confirm the underglycosylation in fibroblasts from the patient. Overexpression of the wild-type SSR4 allele partially restores glycosylation of the marker and of the other members of the TRAP complex. This is the first evidence that the TRAP complex, which binds to the oligosaccharyltransferase complex, is directly involved in N-glycosylation. </p>},
	keywords = {Adolescent, Calcium-Binding Proteins, Cells, Cultured, Chromosomes, Human, X, Congenital Disorders of Glycosylation, Glycosylation, Humans, Male, Membrane Glycoproteins, Point Mutation, Receptors, Cytoplasmic and Nuclear, Receptors, Peptide},
	issn = {1460-2083},
	doi = {10.1093/hmg/ddt550},
	author = {Losfeld, Marie Estelle and Ng, Bobby G and Kircher, Martin and Buckingham, Kati J and Turner, Emily H and Eroshkin, Alexey and Smith, Joshua D and Shendure, Jay and Nickerson, Deborah A and Bamshad, Michael J and Freeze, Hudson H}
}
@article {305,
	title = {Mosaicism of the UDP-galactose transporter SLC35A2 causes a congenital disorder of glycosylation.},
	journal = {Am J Hum Genet},
	volume = {92},
	year = {2013},
	month = {2013 Apr 04},
	pages = {632-6},
	abstract = {<p>Biochemical analysis and whole-exome sequencing identified mutations in the Golgi-localized UDP-galactose transporter SLC35A2 that define an undiagnosed X-linked congenital disorder of glycosylation (CDG) in three unrelated families. Each mutation reduced UDP-galactose transport, leading to galactose-deficient glycoproteins. Two affected males were somatic mosaics, suggesting that a wild-type SLC35A2 allele may be required for survival. In infancy, the commonly used biomarker transferrin showed abnormal glycosylation, but its appearance became normal later in childhood, without any corresponding clinical improvement. This may indicate selection against cells carrying the mutant allele. To detect other individuals with such mutations, we suggest transferrin testing in infancy. Here, we report somatic mosaicism in CDG, and our work stresses the importance of combining both genetic and biochemical diagnoses.</p>},
	keywords = {Biological Transport, Case-Control Studies, Child, Child, Preschool, Congenital Disorders of Glycosylation, Exome, Female, Glycosylation, Humans, Male, Monosaccharide Transport Proteins, Mosaicism, Mutation, Spectrometry, Mass, Electrospray Ionization, Transferrin, Uridine Diphosphate Galactose},
	issn = {1537-6605},
	doi = {10.1016/j.ajhg.2013.03.012},
	author = {Ng, Bobby G and Buckingham, Kati J and Raymond, Kimiyo and Kircher, Martin and Turner, Emily H and He, Miao and Smith, Joshua D and Eroshkin, Alexey and Szybowska, Marta and Losfeld, Marie E and Chong, Jessica X and Kozenko, Mariya and Li, Chumei and Patterson, Marc C and Gilbert, Rodney D and Nickerson, Deborah A and Shendure, Jay and Bamshad, Michael J and Freeze, Hudson H}
}
