@article {31,
	title = {SRD5A3-CDG: Expanding the phenotype of a congenital disorder of glycosylation with emphasis on adult onset features.},
	journal = {Am J Med Genet A},
	volume = {170},
	year = {2016},
	month = {2016 Dec},
	pages = {3165-3171},
	abstract = {<p>Increasing numbers of congenital disorders of glycosylation (CDG) have been reported recently resulting in an expansion of the phenotypes associated with this group of disorders. SRD5A3 codes for polyprenol reductase which converts polyprenol to dolichol. This is a major pathway for dolichol biosynthesis for N-glycosylation, O-mannosylation, C-mannosylation, and GPI anchor synthesis. We present the features of five individuals (three children and two adults) with mutations in SRD5A3 focusing on the variable eye and skin involvement. We compare that to 13 affected individuals from the literature including five adults allowing us to delineate the features that may develop over time with this disorder including kyphosis, retinitis pigmentosa, and cataracts. {\textcopyright} 2016 Wiley Periodicals, Inc.</p>},
	keywords = {3-Oxo-5-alpha-Steroid 4-Dehydrogenase, Adult, Child, Congenital Disorders of Glycosylation, Dolichols, Eye, Female, Glycosylation, Homozygote, Humans, Male, Membrane Proteins, Mutation, Phenotype, Skin, Tretinoin},
	issn = {1552-4833},
	doi = {10.1002/ajmg.a.37875},
	author = {Wheeler, Patricia G and Ng, Bobby G and Sanford, Laura and Sutton, V Reid and Bartholomew, Dennis W and Pastore, Matthew T and Bamshad, Michael J and Kircher, Martin and Buckingham, Kati J and Nickerson, Deborah A and Shendure, Jay and Freeze, Hudson H}
}
@article {265,
	title = {Solving glycosylation disorders: fundamental approaches reveal complicated pathways.},
	journal = {Am J Hum Genet},
	volume = {94},
	year = {2014},
	month = {2014 Feb 06},
	pages = {161-75},
	abstract = {<p>Over 100 human genetic disorders result from mutations in glycosylation-related genes. In 2013, a new glycosylation disorder was reported every 17 days. This trend will probably continue given that at least 2\% of the human genome encodes glycan-biosynthesis and -recognition proteins. Established biosynthetic pathways provide many candidate genes, but finding unanticipated mutated genes will offer new insights into glycosylation. Simple glycobiomarkers can be used in narrowing the candidates identified by exome and genome sequencing, and those can be validated by glycosylation analysis of serum or cells from affected individuals. Model organisms will expand the understanding of these mutations{\textquoteright} impact on glycosylation and pathology. Here, we highlight some recently discovered glycosylation disorders and the barriers, breakthroughs, and surprises they presented. We predict that some glycosylation disorders might occur with greater frequency than current estimates of their prevalence. Moreover, the prevalence of some disorders differs substantially between European and African Americans.</p>},
	keywords = {Congenital Disorders of Glycosylation, Exome, Genome, Human, Glucose, Glycogen, Glycosylation, Homeostasis, Humans, Mannose, Mutation},
	issn = {1537-6605},
	doi = {10.1016/j.ajhg.2013.10.024},
	author = {Freeze, Hudson H and Chong, Jessica X and Bamshad, Michael J and Ng, Bobby G}
}
