@article {973,
	title = {Four Individuals with a Homozygous Mutation in Exon 1f of the  Gene and Associated Myasthenic Features.},
	journal = {Genes (Basel)},
	volume = {11},
	year = {2020},
	month = {2020 06 27},
	abstract = {<p>We identified the known c.1_9del mutation in the  gene in four unrelated females from consanguineous families of Turkish origin. All individuals presented with slowly progressive limb-girdle weakness without any dermatological findings, and dystrophic changes observed in their muscle biopsies. Additionally, the neurological examination revealed ptosis, facial weakness, fatigability, and muscle cramps in all four cases. In two patients, repetitive nerve stimulation showed a borderline decrement and a high jitter was detected in all patients by single-fiber electromyography. Clinical improvement was observed after treatment with pyridostigmine and salbutamol was started. We further characterize the phenotype of patients with limb-girdle muscular dystrophy R17 clinically, by muscle magnetic resonance imaging (MRI) features and by describing a common 3.8 Mb haplotype in three individuals from the same geographical region. In addition, we review the neuromuscular symptoms associated with  mutations and the role of plectin in the neuromuscular junction.</p>},
	keywords = {Adolescent, Adult, Child, Exons, Female, Homozygote, Humans, Muscular Dystrophies, Limb-Girdle, Mutation, Myasthenic Syndromes, Congenital, Phenotype, Plectin},
	issn = {2073-4425},
	doi = {10.3390/genes11070716},
	author = {Mroczek, Magdalena and Durmus, Hacer and Topf, Ana and Parman, Yesim and Straub, Volker}
}
@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}
}
