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anti-Human MLYCD Antibodies:
anti-Mouse (Murine) MLYCD Antibodies:
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Human Polyclonal MLYCD Primary Antibody for WB - ABIN525162
Kulkarni, Salehzadeh, Fritz, Zierath, Krook, Osler: Mitochondrial regulators of fatty acid metabolism reflect metabolic dysfunction in type 2 diabetes mellitus. in Metabolism: clinical and experimental 2012
Inhibiting PSG1 (show PSG1 Antibodies) can effectively reduce chemoresistance via a transforming growth factor-beta (TGF-beta)-related pathway in ER-negative breast cancer cells.
To identify the active site of MCD, molecular docking and molecular dynamics simulations were performed to explore the interactions of human mitochondrial MCD (HmMCD) and CoA derivatives. The findings reveal that the active site of HmMCD indeed resides in the prominent groove which resembles that of curacin A.
PSG stimulated IDO (show IDO1 Antibodies) activity under the conditions of induction of the monocytes by interferon-gamma (show IFNG Antibodies).
Under conditions of directed induction of phenotypic changes in CD4 (show CD4 Antibodies)(+) lymphocytes to regulatory T cells (Treg), pregnancy-specific at high concentrations (10 and 100 mug/mL) increased FOXP3 (show FOXP3 Antibodies) expression. The evaluation of the spontaneous expression level of FOXP3 (show FOXP3 Antibodies) mRNA showed that pregnancy-specific beta1-glycoprotein (1 and 100 mug/mL) stimulated the expression of this factor in mononuclear cells and isolated CD4 (show CD4 Antibodies)(+) lym...
Our result expands the phenotype of malonyl-CoA decarboxylase deficiency and suggests attentions should be paid to the mild form of disorders, for example, malonyl-CoA decarboxylase deficiency, which usually present a severe disease course.
results identify a non-placental site of PSG expression in the gut (show GUSB Antibodies) and associated tumors, with implications for determining whether PSGs have a role in tumor progression, and utility as tumor biomarkers.
The MLYCD catalytic domain is structurally homologous to those of the GCN5-related N-acetyltransferase superfamily.
Structural asymmetry and disulfide bridges among subunits modulate the activity of human malonyl-CoA decarboxylase.
Our case emphasizes the need for ongoing cardiac disease screening in patients with MCD deficiency and the benefits and limitations of current dietary interventions.
the presence of GAGs on the surface of endothelial cells was required for the ability of PSG1 (show PSG1 Antibodies) to induce tube formation
Decreased fat oxidation in MCD(-/-) mice resulted in the accumulation of lipid intermediates in peripheral tissues, but this was not associated with a worsening of age-associated insulin (show INS Antibodies) resistance and, conversely, improved longevity.
MCD(-/-) mice consistently exhibited cardiac dysfunction and severe metabolic perturbations while on a high-fat, low carbohydrate diet of maternal milk and these gradually resolved post-weaning.
Data indicate that a full-dosage of p53 (show TP53 Antibodies) and an intact ribosomal protein-murine double minute 2 protein (Mdm2 (show MDM2 Antibodies))-p53 (show TP53 Antibodies) pathway are required for the induction of malonyl coA decarboxylase (MCD), a critical regulator of fatty acid oxidation.
SIRT4 deacetylates and represses malonyl CoA decarboxylase, regulating malonyl coA levels.
This study of fatty acid oxidation and malonyl-CoA decarboxylase identifies a critical role for metabolism in both the normal pulmonary circulation (hypoxic pulmonary vasoconstriction) and pulmonary hypertension
In vivo and ex vivo cardiac function is similar in wild-type and mcd-deficient mice; however, deletion of MCD markedly increases glucose oxidation and improves functional recovery of the heart after ischemia.
Mcd deficiency is not detrimental to the heart in obesity in mice.
The product of this gene catalyzes the breakdown of malonyl-CoA to acetyl-CoA and carbon dioxide. Malonyl-CoA is an intermediate in fatty acid biosynthesis, and also inhibits the transport of fatty acyl CoAs into mitochondria. Consequently, the encoded protein acts to increase the rate of fatty acid oxidation. It is found in mitochondria, peroxisomes, and the cytoplasm. Mutations in this gene result in malonyl-CoA decarboyxlase deficiency.
CD66 antigen-like family member F
, fetal liver non-specific cross-reactive antigen 1/2
, pregnancy-specific B-1 glycoprotein
, pregnancy-specific beta-1 glycoprotein C/D
, pregnancy-specific beta-1-glycoprotein 1
, pregnancy-specific glycoprotein 1
, MaLonyl CoA Decarboxylase family member (mlcd-1)
, malonyl coenzyme A decarboxylase
, malonyl-CoA decarboxylase, mitochondrial