Associated Papers
Diagnostic implications of pitfalls in causal variant identification based on 4577 molecularly characterized families.
AlAbdi L et al.
Nature Communications, 2023
Annotation of 1350 Common Genetic Variants of the 19 ALDH Multigene Family from Global Human Genome Aggregation Database (gnomAD).
Chen CH et al.
Biomolecules, 2021
Pyrroline-5-carboxylate synthase senses cellular stress and modulates metabolism by regulating mitochondrial respiration.
Yang Z et al.
Cell Death and Differentiation, 2021
Novel Compound Missense and Intronic Splicing Mutation in ALDH18A1 Causes Autosomal Recessive Spastic Paraplegia.
Chen YJ et al.
Frontiers in Neurology, 2021
[Clinical features and C12orf65 mutations of autosomal recessive spastic paraplegia-55: a case report].
Lin SZ et al.
Zhongguo Dang Dai Er Ke Za Zhi = Chinese Journal of Contemporary Pediatrics, 2019
P5CS expression study in a new family with ALDH18A1-associated hereditary spastic paraplegia SPG9.
Magini P et al.
Annals of Clinical and Translational Neurology, 2019
Clinical features and genetic spectrum in Chinese patients with recessive hereditary spastic paraplegia.
Wei Q et al.
Translational Neurodegeneration, 2019
Compound heterozygous mutations in two different domains of ALDH18A1 do not affect the amino acid levels in a patient with hereditary spastic paraplegia.
Steenhof M et al.
Neurogenetics, 2018
ALDH18A1-related cutis laxa syndrome with cyclic vomiting.
Nozaki F et al.
Brain & Development, 2016
Mutations in SPATA5 Are Associated with Microcephaly, Intellectual Disability, Seizures, and Hearing Loss.
Tanaka AJ et al.
American Journal of Human Genetics, 2015
Recurrent De Novo Mutations Affecting Residue Arg138 of Pyrroline-5-Carboxylate Synthase Cause a Progeroid Form of Autosomal-Dominant Cutis Laxa.
Fischer-Zirnsak B et al.
American Journal of Human Genetics, 2015
Alteration of ornithine metabolism leads to dominant and recessive hereditary spastic paraplegia.
Coutelier M et al.
Brain : a Journal of Neurology, 2015
MitoFates: improved prediction of mitochondrial targeting sequences and their cleavage sites.
Fukasawa Y et al.
Molecular & Cellular Proteomics : Mcp, 2015
Single amino acid polymorphism in aldehyde dehydrogenase gene superfamily.
Priyadharshini Christy J et al.
Frontiers in Bioscience (landmark Edition), 2015
Loss of ALDH18A1 function is associated with a cellular lipid droplet phenotype suggesting a link between autosomal recessive cutis laxa type 3A and Warburg Micro syndrome.
Handley MT et al.
Molecular Genetics & Genomic Medicine, 2014
Understanding pyrroline-5-carboxylate synthetase deficiency: clinical, molecular, functional, and expression studies, structure-based analysis, and novel therapy with arginine.
Martinelli D et al.
Journal of Inherited Metabolic Disease, 2012
Metabolic cutis laxa syndromes.
Mohamed M et al.
Journal of Inherited Metabolic Disease, 2011
Further expansion of the phenotypic spectrum associated with mutations in ALDH18A1, encoding Δ¹-pyrroline-5-carboxylate synthase (P5CS).
Skidmore DL et al.
American Journal of Medical Genetics. Part A, 2011
Phenotype prediction of deleterious nonsynonymous single nucleotide polymorphisms in human alcohol metabolism-related genes: a bioinformatics study.
Wang LL et al.
Alcohol (fayetteville, N.y.), 2010
Pyrroline-5-carboxylate synthase and proline biosynthesis: from osmotolerance to rare metabolic disease.
Pérez-Arellano I et al.
Protein Science : a Publication of the Protein Society, 2010
Human Delta1-pyrroline-5-carboxylate synthase: function and regulation.
Hu CA et al.
Amino Acids, 2008
Functional genomics and SNP analysis of human genes encoding proline metabolic enzymes.
Hu CA et al.
Amino Acids, 2008
A missense mutation in ALDH18A1, encoding Delta1-pyrroline-5-carboxylate synthase (P5CS), causes an autosomal recessive neurocutaneous syndrome.
Bicknell LS et al.
European Journal of Human Genetics : Ejhg, 2008
Delta1-pyrroline-5-carboxylate synthase deficiency: neurodegeneration, cataracts and connective tissue manifestations combined with hyperammonaemia and reduced ornithine, citrulline, arginine and proline.
Baumgartner MR et al.
European Journal of Pediatrics, 2005
Hyperammonemia with reduced ornithine, citrulline, arginine and proline: a new inborn error caused by a mutation in the gene encoding delta(1)-pyrroline-5-carboxylate synthase.
Baumgartner MR et al.
Human Molecular Genetics, 2000