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Our study has revealed the unique genetic backgrounds of MCAD deficiency among Japanese, based on the largest series of non-Caucasian cases.
17 VUS (37%; 7 in ACADM, 9 in GALT, and 1 in PAH) were reclassified from uncertain (6 to benign or likely benign and 11 to pathogenic or likely pathogenic). We identified common types of missing information that would have helped make a definitive classification and categorized this information by ease and cost to obtain
Subjects with neonatal symptoms, or neonatal abnormal labs, or neonatal triggers were more likely to have at least one copy of the severe c.985A>G ACADM gene mutation
Exclusively breastfed neonates with MCAD are at risk for early metabolic decompensation. As breastfeeding rates increase, close management of feeding difficulties is essential for all neonates awaiting newborn screening results
The in silico structural changes in medium-chain acyl-CoA dehydrogenase (hMCAD) p.K329E variant protein affect the disturbed oligomeric profile, thermal stability, and conformational flexibility, with respect to the wild-type.
LCHAD and MCAD are differentially expressed in maternal and fetal tissues during normal late pregnancy, which may represent a metabolic adaptation in response to physiological maternal dyslipidemia during late pregnancy.
Study determined three mutations (p.R53C, p.R281S and p.G362E) in MCAD protein predisposing for MCAD deficiency which seems to be unique to Japanese population.
our study demonstrates that not all mutations identified in children with abnormal NBS profiles suggestive of MCAD deficiency result in a total loss in MCAD activity and function
The c.600-18G > A variant activates a cryptic splice site, which competes with the natural splice site.
mutations in the ACADM gene lower the temperature threshold at which medium-chain acyl-CoA dehydrogenase deficiency loss-of-function occurs.
Segregation studies in the Gypsy families showed that 93/123 relatives were carriers of the acyl-coenzyme A dehydrogenase G985 allele, suggesting its high prevalence in this ethnic group.
Identify an ACADM founder mutation for MCADD in Saudi Arabian population.
This supports that c.1161A>G is a functional SNP, which leads to higher MCAD expression, perhaps due to improved splicing. This study is a proof of principle that synonymous SNPs are not neutral.
medium chain acyl-CoA dehydrogenase involve in the metabolism of phenylbutyrate.
Subjects with variant ACADM genotypes and residual MCAD enzyme activities <10% should be considered to have the same risks as patients with classical ACADM genotypes
The octanoyl-CoA oxidation rate, therefore, allows a risk assessment at birth and the identification of new ACADM genotypes associated with asymptomatic disease variants.
A novel variant in the Medium-Chain Acyl-CoA Dehydrogenase (MCAD) gene was identified in a Greek cohort of neonates with suspected MCAD deficiency.
physiological concentrations of flavin adenine dinucleotide resulted in a spectacular enhancement of the thermal stabilities of MCADH and prevented enzymatic activity loss
The mutation in Medium-chain acyl-CoA dehydrogenase deficiency is the first report of the c.461T>G mutation in the acyl-CoA dehydrogenase gene.
classification of genotypes with at least one variant of unknown significance in individuals who are carriers of, or affected with, MCAD deficiency of the following genotypes: c.985A>G/wildtype, c.199T>C/c.985A>G and c.985A>G/c.985A>G
Investigation of ACADM in relation to fat deposition traits.
Investigation of structure of enzyme (from kidney) complexed with FAD analogs (e.g., 8-NH2-FAD) and acyl-CoA (e.g., octanoyl-CoA).
ACADM and ALDH2 were predicted to be the target genes of miR-224
the transcriptional regulatory circuits involved in the control of MCAD gene expression under hypoxic conditions are modulated by upstream factors that are sensitive to the levels of oxygen
MCAD is reduced in liver, heart & kidney in lipopolysaccharide-induced acute phase response; binding liver nuclear extracts to ERRalpha response element found in promoter region of MCAD was decreased during APR, suggesting less transcription of MCAD
The MCAD-/- mice developed an organic aciduria and fatty liver, and showed profound cold intolerance at 4 degrees C with prior fasting.
MCAD deficiency in mice leads to specific changes in hepatic carbohydrate management on exposure to metabolic stress.
A high-fat diet increases adiposity but maintains mitochondrial oxidative enzymes (MCAD/citrate synthase) without affecting development of heart failure with pressure overload.
This gene encodes the medium-chain specific (C4 to C12 straight chain) acyl-Coenzyme A dehydrogenase. The homotetramer enzyme catalyzes the initial step of the mitochondrial fatty acid beta-oxidation pathway. Defects in this gene cause medium-chain acyl-CoA dehydrogenase deficiency, a disease characterized by hepatic dysfunction, fasting hypoglycemia, and encephalopathy, which can result in infantile death. Alternatively spliced transcript variants encoding different isoforms have been found for this gene.
acyl-Coenzyme A dehydrogenase, C-4 to C-12 straight chain
, medium-chain specific acyl-CoA dehydrogenase, mitochondrial
, medium-chain acyl-CoA dehydrogenase
, acyl-Coenzyme A dehydrogenase, C-4 to C-12 straight chain, nuclear gene encoding mitochondrial protein
, C-4 to C-12 straight chain acyl-coenzyme A dehydrogenase
, acyl-coenzyme A dehydrogenase, C-4 to C-12 straight chain
, acyl-CoA dehydrogenase, C-4 to C-12 straight chain
, medium-chain specific acyl-CoA dehydrogenase, mitochondrial-like
, Acyl-Coenzyme A dehydrogenase C-4 to C-12 straight-chain
, Acyl-Coenzyme A dehydrogenase, C-4 to C-12 straight-chain
, acyl-Coenzyme A dehydrogenase, medium chain
, mitochondrial medium-chain specific acyl-Co dehydrogenase-like protein