Associated Papers
Allosteric regulation of UBIAD1 trafficking from ER to Golgi revealed by chemical genetic screening.
Jun DJ et al.
Proceedings of the National Academy of Sciences of the United States of America, 2025
Case Report of Schnyder Corneal Dystrophy-A Rare Lipid Metabolic Disorder of the Cornea.
Stoyanova N et al.
Life (basel, Switzerland), 2025
Peripheral Center Sparing Presentation of Schnyder Corneal Dystrophy.
Busin M et al.
Ophthalmology, 2024
Variant Landscape of 15 Genes Involved in Corneal Dystrophies: Report of 30 Families and Comprehensive Analysis of the Literature.
Zhu D et al.
International Journal of Molecular Sciences, 2023
UbiA prenyltransferase domain-containing protein 1 (UBIAD1) variant c.695 A > G identified in a multigenerational Japanese family with Schnyder corneal dystrophy.
Tsuneya M et al.
Japanese Journal of Ophthalmology, 2023
Naturally occurring UBIAD1 mutations differentially affect menaquinone biosynthesis and vitamin K-dependent carboxylation.
Chen X et al.
The Febs Journal, 2022
Functional study of SCCD pathogenic gene UBIAD1 (Review).
Xie J et al.
Molecular Medicine Reports, 2021
High expression of Matrix Gla Protein in Schnyder corneal dystrophy patients points to an active role of vitamin K in corneal health.
Sarosiak A et al.
Acta Ophthalmologica, 2021
Genome scale analysis of pathogenic variants targetable for single base editing.
Lavrov AV et al.
Bmc Medical Genomics, 2020
Ubiquitin-mediated regulation of sterol homeostasis.
van den Boomen DJH et al.
Current Opinion in Cell Biology, 2020
Schnyder corneal dystrophy-associated UBIAD1 is defective in MK-4 synthesis and resists autophagy-mediated degradation.
Jun DJ et al.
Journal of Lipid Research, 2020
Enhanced ER-associated degradation of HMG CoA reductase causes embryonic lethality associated with Ubiad1 deficiency.
Jo Y et al.
Elife, 2020
Schnyder corneal dystrophy-associated UBIAD1 mutations cause corneal cholesterol accumulation by stabilizing HMG-CoA reductase.
Jiang SY et al.
Plos Genetics, 2019
Schnyder corneal dystrophy-associated UBIAD1 inhibits ER-associated degradation of HMG CoA reductase in mice.
Jo Y et al.
Elife, 2019
Clinical diversity in patients with Schnyder corneal dystrophy-a novel and known UBIAD1 pathogenic variants.
Sarosiak A et al.
Graefe's Archive for Clinical and Experimental Ophthalmology = Albrecht Von Graefes Archiv Fur Klinische Und Experimentelle Ophthalmologie, 2018
Schnyder corneal dystrophy and associated phenotypes caused by novel and recurrent mutations in the UBIAD1 gene.
Evans CJ et al.
Bmc Ophthalmology, 2018
A Mouse Model of Schnyder Corneal Dystrophy with the N100S Point Mutation.
Dong F et al.
Scientific Reports, 2018
Long-Term Outcome After Penetrating Keratoplasty in a Pedigree With the G177E Mutation in the UBIAD1 Gene for Schnyder Corneal Dystrophy.
Kitazawa K et al.
Cornea, 2018
UbiA prenyltransferase domain-containing protein-1 modulates HMG-CoA reductase degradation to coordinate synthesis of sterol and nonsterol isoprenoids.
Schumacher MM et al.
The Journal of Biological Chemistry, 2018
Mutational spectrum of Korean patients with corneal dystrophy.
Chae H et al.
Clinical Genetics, 2016
Programmable editing of a target base in genomic DNA without double-stranded DNA cleavage.
Komor AC et al.
Nature, 2016
Identification of the First De Novo UBIAD1 Gene Mutation Associated with Schnyder Corneal Dystrophy.
Lin BR et al.
Journal of Ophthalmology, 2016
The prenyltransferase UBIAD1 is the target of geranylgeraniol in degradation of HMG CoA reductase.
Schumacher MM et al.
Elife, 2015
Functional characterization of the vitamin K2 biosynthetic enzyme UBIAD1.
Hirota Y et al.
Plos One, 2015
Phenotype-genotype correlation in patients with Schnyder corneal dystrophy.
Nowinska AK et al.
Cornea, 2014
The TERE1 protein interacts with mitochondrial TBL2: regulation of trans-membrane potential, ROS/RNS and SXR target genes.
Fredericks WJ et al.
Journal of Cellular Biochemistry, 2013
The UBIAD1 prenyltransferase links menaquinone-4 [corrected] synthesis to cholesterol metabolic enzymes.
Nickerson ML et al.
Human Mutation, 2013
A novel Golgi retention signal RPWS for tumor suppressor UBIAD1.
Wang X et al.
Plos One, 2013
[Mutation in the UBIAD1 gene of a Chinese family with Schnyder crystal corneal dystrophy].
Tao SY et al.
Zhonghua Yi Xue Za Zhi, 2012
The bladder tumor suppressor protein TERE1 (UBIAD1) modulates cell cholesterol: implications for tumor progression.
Fredericks WJ et al.
Dna and Cell Biology, 2011
Schnyder Corneal Dystrophy in a Saudi Arabian Family with Heterozygous UBIAD1 Mutation (p.L121F).
Al-Ghadeer H et al.
Middle East African Journal of Ophthalmology, 2011
Genotype-phenotype correlation of TGFBI corneal dystrophies in Polish patients.
Nowińska AK et al.
Molecular Vision, 2011
A mutation in the UBIAD1 gene in a Han Chinese family with Schnyder corneal dystrophy.
Du C et al.
Molecular Vision, 2011
UBIAD1 mutation alters a mitochondrial prenyltransferase to cause Schnyder corneal dystrophy.
Nickerson ML et al.
Plos One, 2010
A novel UBIAD1 mutation identified in a Chinese family with Schnyder crystalline corneal dystrophy.
Jing Y et al.
Molecular Vision, 2009
Surgical management and genetic analysis of a Chinese family with the S171P mutation in the UBIAD1 gene, the gene for Schnyder corneal dystrophy.
Mehta JS et al.
The British Journal of Ophthalmology, 2009
In vivo laser confocal microscopy findings and mutational analysis for Schnyder's crystalline corneal dystrophy.
Kobayashi A et al.
Ophthalmology, 2009
Genetic analysis of 14 families with Schnyder crystalline corneal dystrophy reveals clues to UBIAD1 protein function.
Weiss JS et al.
American Journal of Medical Genetics. Part A, 2008
Mutations in the UBIAD1 gene on chromosome short arm 1, region 36, cause Schnyder crystalline corneal dystrophy.
Weiss JS et al.
Investigative Ophthalmology & Visual Science, 2007
Identification of mutations in UBIAD1 following exclusion of coding mutations in the chromosome 1p36 locus for Schnyder crystalline corneal dystrophy.
Yellore VS et al.
Molecular Vision, 2007
Mutations in the UBIAD1 gene, encoding a potential prenyltransferase, are causal for Schnyder crystalline corneal dystrophy.
Orr A et al.
Plos One, 2007