@article {184,
	title = {Cerebral visual impairment and intellectual disability caused by PGAP1 variants.},
	journal = {Eur J Hum Genet},
	volume = {23},
	year = {2015},
	month = {2015 Dec},
	pages = {1689-93},
	abstract = {<p>Homozygous variants in PGAP1 (post-GPI attachment to proteins 1) have recently been identified in two families with developmental delay, seizures and/or spasticity. PGAP1 is a member of the glycosylphosphatidylinositol anchor biosynthesis and remodeling pathway and defects in this pathway are a subclass of congenital disorders of glycosylation. Here we performed whole-exome sequencing in an individual with cerebral visual impairment (CVI), intellectual disability (ID), and factor XII deficiency and revealed compound heterozygous variants in PGAP1, c.274_276del (p.(Pro92del)) and c.921_925del (p.(Lys308Asnfs*25)). Subsequently, PGAP1-deficient Chinese hamster ovary (CHO)-cell lines were transfected with either mutant or wild-type constructs and their sensitivity to phosphatidylinositol-specific phospholipase C (PI-PLC) treatment was measured. The mutant constructs could not rescue the PGAP1-deficient CHO cell lines resistance to PI-PLC treatment. In addition, lymphoblastoid cell lines (LCLs) of the affected individual showed no sensitivity to PI-PLC treatment, whereas the LCLs of the heterozygous carrier parents were partially resistant. In conclusion, we report novel PGAP1 variants in a boy with CVI and ID and a proven functional loss of PGAP1 and show, to our knowledge, for the first time this genetic association with CVI. </p>},
	keywords = {Animals, Cell Line, Tumor, Child, CHO Cells, Cricetinae, Cricetulus, Humans, Intellectual Disability, Male, Membrane Proteins, Mutation, Phosphoinositide Phospholipase C, Phosphoric Monoester Hydrolases, Syndrome, Vision Disorders, Visual Perception},
	issn = {1476-5438},
	doi = {10.1038/ejhg.2015.42},
	author = {Bosch, Dani{\"e}lle G M and Boonstra, F Nienke and Kinoshita, Taroh and Jhangiani, Shalini and de Ligt, Joep and Cremers, Frans P M and Lupski, James R and Murakami, Yoshiko and de Vries, Bert B A}
}
@article {162,
	title = {A second locus for Schneckenbecken dysplasia identified by a mutation in the gene encoding inositol polyphosphate phosphatase-like 1 (INPPL1).},
	journal = {Am J Med Genet A},
	volume = {167A},
	year = {2015},
	month = {2015 Oct},
	pages = {2470-3},
	keywords = {Exome, Gene Expression, Genetic Loci, Gestational Age, Homozygote, Humans, Hydrops Fetalis, Infant, Newborn, Male, Mutation, Osteochondrodysplasias, Phosphatidylinositol-3,4,5-Trisphosphate 5-Phosphatases, Phosphoric Monoester Hydrolases, Stillbirth},
	issn = {1552-4833},
	doi = {10.1002/ajmg.a.37173},
	author = {Lee, Hane and Nevarez, Lisette and Lachman, Ralph S and Wilcox, William R and Krakow, Deborah and Cohn, Daniel H}
}
@article {239,
	title = {Opsismodysplasia resulting from an insertion mutation in the SH2 domain, which destabilizes INPPL1.},
	journal = {Am J Med Genet A},
	volume = {164A},
	year = {2014},
	month = {2014 Sep},
	pages = {2407-11},
	keywords = {Adolescent, Amino Acid Sequence, Base Sequence, Child, Child, Preschool, Female, Humans, Infant, Molecular Sequence Data, Mutagenesis, Insertional, Mutation, Osteochondrodysplasias, Phosphatidylinositol-3,4,5-Trisphosphate 5-Phosphatases, Phosphoric Monoester Hydrolases, Protein Stability, Radiography, RNA Splice Sites, src Homology Domains},
	issn = {1552-4833},
	doi = {10.1002/ajmg.a.36640},
	author = {Li, Bing and Krakow, Deborah and Nickerson, Deborah A and Bamshad, Michael J and Chang, Yong and Lachman, Ralph S and Yilmaz, Alev and Kayserili, H{\"u}lya and Cohn, Daniel H}
}
@article {313,
	title = {Whole-genome analysis reveals that mutations in inositol polyphosphate phosphatase-like 1 cause opsismodysplasia.},
	journal = {Am J Hum Genet},
	volume = {92},
	year = {2013},
	month = {2013 Jan 10},
	pages = {137-43},
	abstract = {<p>Opsismodysplasia is a rare, autosomal-recessive skeletal dysplasia characterized by short stature, characteristic facial features, and in some cases severe renal phosphate wasting. We used linkage analysis and whole-genome sequencing of a consanguineous trio to discover that mutations in inositol polyphosphate phosphatase-like 1 (INPPL1) cause opsismodysplasia with or without renal phosphate wasting. Evaluation of 12 families with opsismodysplasia revealed that INPPL1 mutations explain ~60\% of cases overall, including both of the families in our cohort with more than one affected child and 50\% of the simplex cases.</p>},
	keywords = {Child, Child, Preschool, Female, Genome, Human, Humans, Infant, Infant, Newborn, Male, Mutation, Osteochondrodysplasias, Phosphatidylinositol-3,4,5-Trisphosphate 5-Phosphatases, Phosphoric Monoester Hydrolases},
	issn = {1537-6605},
	doi = {10.1016/j.ajhg.2012.11.011},
	author = {Below, Jennifer E and Earl, Dawn L and Shively, Kathryn M and McMillin, Margaret J and Smith, Joshua D and Turner, Emily H and Stephan, Mark J and Al-Gazali, Lihadh I and Hertecant, Jozef L and Chitayat, David and Unger, Sheila and Cohn, Daniel H and Krakow, Deborah and Swanson, James M and Faustman, Elaine M and Shendure, Jay and Nickerson, Deborah A and Bamshad, Michael J}
}
