@article {23,
	title = {Mutations in MBOAT7, Encoding Lysophosphatidylinositol Acyltransferase I, Lead to Intellectual Disability Accompanied by Epilepsy and Autistic Features.},
	journal = {Am J Hum Genet},
	volume = {99},
	year = {2016},
	month = {2016 Oct 06},
	pages = {912-916},
	abstract = {<p>The risk of epilepsy among individuals with intellectual disability (ID) is approximately ten times that of the general population. From a cohort of >5,000 families affected by neurodevelopmental disorders, we identified six consanguineous families harboring homozygous inactivating variants in MBOAT7, encoding lysophosphatidylinositol acyltransferase (LPIAT1). Subjects presented with ID frequently accompanied by epilepsy and autistic features. LPIAT1 is a membrane-bound phospholipid-remodeling enzyme that transfers arachidonic acid (AA) to lysophosphatidylinositol to produce AA-containing phosphatidylinositol. This study suggests a role for AA-containing phosphatidylinositols in the development of ID accompanied by epilepsy and autistic features.</p>},
	keywords = {Acyltransferases, Arachidonic Acid, Autistic Disorder, Child, Child, Preschool, Consanguinity, Epilepsy, Female, Homozygote, Humans, Infant, Intellectual Disability, Lysophospholipids, Male, Membrane Proteins, Mutation, Pedigree, Phosphatidylinositols},
	issn = {1537-6605},
	doi = {10.1016/j.ajhg.2016.07.019},
	author = {Johansen, Anide and Rosti, Rasim O and Musaev, Damir and Sticca, Evan and Harripaul, Ricardo and Zaki, Maha and {\c C}a{\u g}layan, Ahmet Okay and Azam, Matloob and Sultan, Tipu and Froukh, Tawfiq and Reis, Andr{\'e} and Popp, Bernt and Ahmed, Iltaf and John, Peter and Ayub, Muhammad and Ben-Omran, Tawfeg and Vincent, John B and Gleeson, Joseph G and Abou Jamra, Rami}
}
@article {223,
	title = {NGLY1 mutation causes neuromotor impairment, intellectual disability, and neuropathy.},
	journal = {Eur J Med Genet},
	volume = {58},
	year = {2015},
	month = {2015 Jan},
	pages = {39-43},
	abstract = {<p>N-glycanase 1 (NGLY1) is a conserved enzyme that is responsible for the deglycosylation of misfolded N-glycosylated proteins in the cytoplasm prior to their proteasome-mediated degradation. Disruption of this degradation process has been associated with various neurologic diseases including amyotrophic lateral sclerosis and Parkinson{\textquoteright}s disease. Here, we describe two siblings with neuromotor impairment, apparent intellectual disability, corneal opacities, and neuropathy who were found to possess a novel homozygous frame-shift mutation due to a 4 base pair deletion in NGLY1 (c.1533_1536delTCAA, p.Asn511LysfsX51). We hypothesize that this mutation likely limits the capability of neuronal cells to respond to stress due to accumulation of misfolded proteins, thereby impairing their survival and resulting in progressive loss of neurological function. </p>},
	keywords = {Abnormalities, Multiple, Adolescent, Child, Corneal Opacity, Developmental Disabilities, Female, Frameshift Mutation, Genotype, Humans, Intellectual Disability, Male, Movement Disorders, Peptide-N4-(N-acetyl-beta-glucosaminyl) Asparagine Amidase, Peripheral Nervous System Diseases},
	issn = {1878-0849},
	doi = {10.1016/j.ejmg.2014.08.008},
	author = {{\c C}a{\u g}layan, Ahmet Okay and Comu, Sinan and Baranoski, Jacob F and Parman, Yesim and Kaymak{\c c}alan, Hande and Akg{\"u}m{\"u}{\c s}, G{\"o}zde Tu{\u g}ce and Caglar, Caner and D{\"o}len, Duygu and Erson-Omay, Emine Zeynep and Harmanci, Akdes Serin and Mishra-Gorur, Ketu and Freeze, Hudson H and Yasuno, Katsuhito and Bilguvar, Kaya and G{\"u}nel, Murat}
}
