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Human Polyclonal Acads Primary Antibody für ELISA, WB - ABIN559744
Leatherbury, Yu, Chatterjee, Walker, Yu, Tian, Lo: A novel mouse model of X-linked cardiac hypertrophy. in American journal of physiology. Heart and circulatory physiology 2008
Show all 2 Pubmed References
Cow (Bovine) Polyclonal Acads Primary Antibody für WB - ABIN2785627
Tein, Elpeleg, Ben-Zeev, Korman, Lossos, Lev, Lerman-Sagie, Leshinsky-Silver, Vockley, Berry, Lamhonwah, Matern, Roe, Gregersen: Short-chain acyl-CoA dehydrogenase gene mutation (c.319C>T) presents with clinical heterogeneity and is candidate founder mutation in individuals of Ashkenazi Jewish origin. in Molecular genetics and metabolism 2008
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 (zeige LASP1 Antikörper) and SCAD protein levels in acute psychotic bipolar disorder samples.
IVD (zeige IVD Antikörper) 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 (zeige INS Antikörper) release during an oral glucose tolerance test.
We therefore propose that SCAD misfolding leads to production of ROS (zeige ROS1 Antikörper), 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.
Results suggest that the decreased beta-oxidation of short-chain fatty acids in Acads-deficient mice fed HF diet produces a state of energy deficiency in the brain.
These results suggest that reduced brown adipose tissue function is not the major factor causing cold sensitivity in acyl-CoA dehydrogenase (zeige ACADM Antikörper) knockout strains.
some variants of SCAD proteins (R22W, G68C, W153R, and R359C) are severely misfolded, which may implicate a role in the pathogenesis of SCAD deficiency
SCAD-deficient mice display altered postingestive responses to dietary fat, providing further evidence for metabolic control of feeding. Acads does not alter acute orosensory response to this fat stimulus.
This gene encodes a a tetrameric mitochondrial flavoprotein, which is a member of the acyl-CoA dehydrogenase family. This enzyme catalyzes the initial step of the mitochondrial fatty acid beta-oxidation pathway. Mutations in this gene have been associated with Short Chain Acyl-CoA Dehydrogenase Deficiency.
acyl-Coenzyme A dehydrogenase, C-2 to C-3 short chain
, butyryl-CoA dehydrogenase
, mitochondrial short-chain specific acyl-CoA dehydrogenase
, short-chain acyl-CoA dehydrogenase
, short-chain specific acyl-CoA dehydrogenase, mitochondrial
, unsaturated acyl-CoA reductase
, short chain acyl-coenzyme A dehydrogenase
, acetyl-Coenzyme A dehydrogenase, short chain
, acyl-Coenzyme A dehydrogenase, short chain
, acyl-CoA dehydrogenase, C-2 to C-3 short chain