Recombinant Human Short-chain specific acyl-CoA dehydrogenase, mitochondrial (ACADS)

1. a link between ACADS susceptibility variants and abnormal beta-oxidation consistent with known altered kinetics of these variants PMID: 28532786
2. Korean patients with Short-chain acyl-CoA dehydrogenase deficiency showed heterogenous clinical features and ACADS genotype. PMID: 27466294
3. Thirteen proteins had significant alteration in protein levels in patients carrying variation c.319C>T in ACADS compared to controls and they belonged to various pathways, such as the antioxidant system and amino acid metabolism. PMID: 24485985
4. Results show significant upregulation of LASP1 and SCAD protein levels in acute psychotic bipolar disorder samples. PMID: 24554194
5. IVD mutations in Asian populations are distinct from these in Western populations. PMID: 22004070
6. physiological concentrations of flavin adenine dinucleotide resulted in a spectacular enhancement of the thermal stabilities of SCAD and prevented enzymatic activity loss PMID: 21968293
7. In glucose-tolerant individuals the minor C-allele of rs2014355 of ACADS was associated with reduced measures of glucose-stimulated insulin release during an oral glucose tolerance test. PMID: 21211036
8. We therefore propose that SCAD misfolding leads to production of ROS, which in turn leads to fission and a grain-like structure of the mitochondrial reticulum. This finding indicates a toxic response elicited by misfolded p.Arg83Cys SCAD proteins PMID: 20371198
9. Molecular pathogenesis of a novel mutation, G108D, in ACADS identified in subjects with ACADS deficiency. PMID: 20376488
10. Reduction of catalytic activity and stability in polymorphic variant of SCAD (Gly185Ser) is caused by decreased flexibility in the tertiary conformation of the mutant enzyme. PMID: 12220177
11. Replacement of the catalytic glutamate in either short-chain acyl-CoA dehydrogenase (SCAD) or isovaleryl-CoA dehydrogenase (IVD)with glycine resulted in a several-fold reduction in affinity for substrate. PMID: 16376132
12. One of 220 SIDs cases was homozygous for the prevalent MCAD A985G mutation. PMID: 18045290
13. The c.319C>T mutation can lead to wide clinical and biochemical phenotypic variability, suggesting a complex multifactorial/polygenic condition. This should be screened for in individuals with multicore myopathy, particularly among the Ashkenazim. PMID: 18054510
14. A homozygous variant allele of the SCAD gene, 625G>A, was detected in new case of short-chain acyl-CoA dehydrogenase deficiency. PMID: 18175080
15. Extensive laboratory investigations indicate that the short-chain acyl-CoA dehydrogenase gene variant is likely preventing or delaying the normal expression of the Prader-Willi syndrome phenotype. PMID: 18184946
16. SCAD deficiency should be considered as a disorder of protein folding that can lead to clinical disease in combination with other genetic and environmental factors. PMID: 18523805
17. A deoxyribonucleic analysis revealed the presence of a 625G>A (G-to-A substitution at nucleotide 625) variant short-chain acyl-coenzyme A dehydrogenase gene polymorphism. PMID: 18539996
18. SCAD deficiency cause a disorder that leads to the accumulation of butyrylcarnitine and ethylmalonic acid in blood and urine. PMID: 18977676

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HGNC: 90

OMIM: 201470

KEGG: hsa:35

STRING: 9606.ENSP00000242592

UniGene: Hs.507076