-
Study discovered a high occurrence of two rare pathogenic variants-the deletion c.310_312delGAG and the substitution c.1138C>T, with allelic frequencies of 64% and 31%, respectively especially in the Roma ethnic group.
-
a link between ACADS susceptibility variants and abnormal beta-oxidation consistent with known altered kinetics of these variants
-
Korean patients with Short-chain acyl-CoA dehydrogenase deficiency showed heterogenous clinical features and ACADS genotype.
-
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.
-
Results show significant upregulation of LASP1 and SCAD protein levels in acute psychotic bipolar disorder samples.
-
IVD mutations in Asian populations are distinct from these in Western populations.
-
physiological concentrations of flavin adenine dinucleotide resulted in a spectacular enhancement of the thermal stabilities of SCAD and prevented enzymatic activity loss
-
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.
-
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
-
Molecular pathogenesis of a novel mutation, G108D, in ACADS identified in subjects with ACADS deficiency.
-
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.
-
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.
-
One of 220 SIDs cases was homozygous for the prevalent MCAD A985G mutation.
-
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.
-
A homozygous variant allele of the SCAD gene, 625G>A, was detected in new case of short-chain acyl-CoA dehydrogenase deficiency.
-
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.
-
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.
-
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.
-
SCAD deficiency cause a disorder that leads to the accumulation of butyrylcarnitine and ethylmalonic acid in blood and urine.
