@article {808,
	title = {METAP1 mutation is a novel candidate for autosomal recessive intellectual disability.},
	journal = {J Hum Genet},
	volume = {66},
	year = {2021},
	month = {2021 Feb},
	pages = {215-218},
	abstract = {<p>Intellectual disability (ID) is a genetic and clinically heterogeneous common disease and underlying molecular pathogenesis can frequently not be identified by whole-exome/genome testing. Here, we report four siblings born to a consanguineous union who presented with intellectual disability and discuss the METAP1 pathway as a novel etiology of ID. Genomic analyses demonstrated that patients harbor a novel homozygous nonsense mutation in the gene METAP1. METAP1 codes for methionine aminopeptidase 1 (MetAP1) which oversees the co-translational excision of the first methionine remnants in eukaryotes. The loss-of-function mutations to this gene may result in a defect in the translation of many essential proteins within a cell. Improper neuronal function resulting from this loss of essential proteins could lead to neurologic impairment and ID.</p>},
	issn = {1435-232X},
	doi = {10.1038/s10038-020-0820-0},
	author = {{\c C}a{\u g}layan, Ahmet Okay and Aktar, Fesih and Bilguvar, Kaya and Baranoski, Jacob F and Akg{\"u}m{\"u}{\c s}, G{\"o}zde Tu{\u g}ce and Harmanci, Akdes Serin and Erson-Omay, Emine Zeynep and Yasuno, Katsuhito and Caksen, Huseyin and G{\"u}nel, Murat}
}
@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}
}
