@article {378,
	title = {Survival beyond the perinatal period expands the phenotypes caused by mutations in GLE1.},
	journal = {Am J Med Genet A},
	volume = {173},
	year = {2017},
	month = {2017 Nov},
	pages = {3098-3103},
	abstract = {<p>Mutations in GLE1 underlie Lethal Congenital Contracture syndrome (LCCS) and Lethal Arthrogryposis with Anterior Horn Cell Disease (LAAHD). Both LCCS and LAAHD are characterized by reduced fetal movements, congenital contractures, and a severe form of motor neuron disease that results in fetal death or death in the perinatal period, respectively. We identified bi-allelic mutations in GLE1 in two unrelated individuals with motor delays, feeding difficulties, and respiratory insufficiency who survived beyond the perinatal period. Each affected child had missense variants predicted to result in amino acid substitutions near the C-terminus of GLE1 that are predicted to disrupt protein-protein interaction or GLE1 protein targeting. We hypothesize that mutations that preserve function of the coiled-coil domain of GLE1 cause LAAHD whereas mutations that abolish the function of the coiled-coil domain cause LCCS. The phenotype of LAAHD is now expanded to include multiple individuals surviving into childhood suggesting that LAAHD is a misnomer and should be re-named Arthrogryposis with Anterior Horn Cell Disease (AAHD).</p>},
	keywords = {Arthrogryposis, Child, Preschool, Female, Genetic Predisposition to Disease, Humans, Male, Motor Disorders, Motor Neuron Disease, Mutation, Nucleocytoplasmic Transport Proteins, Pedigree, Pregnancy},
	issn = {1552-4833},
	doi = {10.1002/ajmg.a.38406},
	author = {Said, Edith and Chong, Jessica X and Hempel, Maja and Denecke, Jonas and Soler, Paul and Strom, Tim and Nickerson, Deborah A and Kubisch, Christian and Bamshad, Michael J and Lessel, Davor}
}
@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}
}
