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TRIM63 encodes a member of the RING zinc finger protein family found in striated muscle and iris. Additionally we are shipping TRIM63 Antibodies (127) and TRIM63 Kits (6) and many more products for this protein.
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role of the muscle specific (show EIF3K Proteins) E3s MuRF-1 and MAFbx (show FBXO32 Proteins) in skeletal muscle wasting during various pathologies, as well as their regulation by modifiable lifestyle factors, were explored (review)
the involvement of oxidative stress in the atrophy of COPD peripheral muscle cells in vitro, via the FoxO1/MuRF1/atrogin-1 signaling pathway of the ubiquitin/proteasome system
The mitochondrial damage-cGAS-STING-IRF3 (show IRF3 Proteins) pathway is critically involved in metabolic stress-induced endothelial inflammation.
Altogether, these results suggest a novel function for p63 (show RPE65 Proteins) as a contributor to muscular atrophic processes via the regulation of multiple genes, including the muscle atrophy gene Trim63.
A novel protein aggregate myopathies and cardiomyopathy resulting from combined homozygous MuRF1 null mutation and heterozygous MuRF3 (show TRIM54 Proteins) missense mutation.
Vitamin D3 might have an inhibitory effect on the expression of MAFbx (show FBXO32 Proteins) and MuRF1 in skeletal muscle.
MURF1 expression intended to be increased in the skeletal muscle of patients with malignant disease even before cancer related cachexia weight loss.
TRIM63 gene expression involved in skin hyperpigmentation.
Expression of USP19 correlates with that of MuRF1 and MAFbx/atrogin-1 (show FBXO32 Proteins) in skeletal muscles
Skeletal muscle atrophy induced by Angiotensin II involves activation of MuRF1 expression.
Oligonol-mediated downregulation of Atrogin-1 (show FBXO32 Proteins) and MuRF1 gene expression alleviates muscle loss and improves the impaired myotube formation, indicating that oligonol supplementation may be useful for the attenuation of myotube loss.
the present study indicates that excessive glucocorticoids increased ubiquitin-proteasome system -dependent protein proteolysis via stimulating MuRF1, but not atrogin-1 (show FBXO32 Proteins).
Dexamethasone-induced MuRF1 upregulation was significantly attenuated in C2C12 myotubes by resveratrol in vitro, but this effect on C2C12 myotubes was abrogated by a knockdown of NF-kappaB (show NFKB1 Proteins), suggesting that the beneficial effect of resveratrol was NF-kappaB (show NFKB1 Proteins) dependent. Our findings provide novel information about the ability of resveratrol to prevent or treat muscle atrophy induced by CKD.
Iron-induced skeletal muscle atrophy is suggested to involve the E3 ubiquitin ligase (show MUL1 Proteins) mediated by the reduction of Akt (show AKT1 Proteins)-FOXO3a (show FOXO3 Proteins) signaling by oxidative stress.
MAFbx (show FBXO32 Proteins) mRNA expression was decreased in old mice relative to adult mice, whereas MuRF1 mRNA expression was less affected by ageing
MuRF1 directly interacts with PPARalpha (show PPARA Proteins), mono-ubiquitinates it, and targets it for nuclear export to inhibit fatty acid oxidation in a proteasome independent manner.
Increased Expression of MuRF1 Is Associated with Radiation-induced Laryngeal Muscle Atrophy.
MURF1 was upregulated in cancer cachexia mice.
Sunitinib is able to restrain the overactivation of STAT3 (show STAT3 Proteins) and MuRF-1 pathways, involved in enhanced muscle protein catabolism during cancer cachexia.
this study shows that aspartate suppresses lipopolysaccharide-induced MuRF1 expression in skeletal muscle via activation of Akt (show AKT1 Proteins) signaling, and inhibition of AMPKa and FOXO1 (show FOXO1 Proteins) signaling
The findings reveal a novel mechanism by which Ca2 (show CA2 Proteins)+ overload disrupts myofibril integrity by activating a Calcineurin-FoxO (show FOXO3 Proteins)-MuRF1-proteosome signaling pathway.
This gene encodes a member of the RING zinc finger protein family found in striated muscle and iris. The product of this gene is an E3 ubiquitin ligase that localizes to the Z-line and M-line lattices of myofibrils. This protein plays an important role in the atrophy of skeletal and cardiac muscle and is required for the degradation of myosin heavy chain proteins, myosin light chain, myosin binding protein, and for muscle-type creatine kinase.
E3 ubiquitin-protein ligase TRIM63
, iris ring finger protein
, muscle specific ring finger protein 2
, muscle-specific RING finger protein 1
, ring finger protein 28
, striated muscle RING zinc finger protein
, tripartite motif-containing protein 63
, muscle ring finger protein 1
, tripartite motif protein 63
, tripartite motif-containing 63
, ring finger protein 30
, muscle specific ring finger protein 1
, muscle specific RING finger protein-1
, e3 ubiquitin-protein ligase TRIM63-like
, tripartite motif containing 63
, tripartite motif containing 63a