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Redox sensor protein. Additionally we are shipping NMRAL1 Antibodies (20) and NMRAL1 Proteins (8) and many more products for this protein.
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These findings suggest that the increased susceptibility of the G6PD-knockdown cells to viral infection was due to impaired NF-kappaB signaling and antiviral response mediated by HSCARG.
After viral infection, HSCARG interacted with tumor necrosis receptor-associated factor 3 (TRAF3) and inhibited its ubiquitination by promoting the recruitment of OTUB1 to TRAF3.
Data indicate that HSCARG and USP7 function in concert in inhibiting polyubiquination of NEMO, thus inhibiting NF-kappaB activity.
HSCARG is involved in DNA damage response through affecting the level of H2A ubiquitination and localization of RAP80 at lesion points.
HSCARG regulated reactive-oxygen-species homeostasis through inhibition of NADPH oxidase activity via regulation of the expression of p47phox.
CRM1 dependent nucleocytoplasmic translocation of HSCARG plays an important role in fine-tuning NF-kappaB signaling
HSCARG is involved in the NF-kappaB signaling pathway, and negatively regulates NF-kappaB activation.
expression, crystallization and preliminary X-ray crystallographic studies of HSCARG at a resolution of 2.4 A; crystals belong to F23 space group, with unit cell parameters a=b=c=223.30A, alpha=beta=gamma=90 degrees
One of the functions regulated by HSCARG may be argininosuccinate synthetase that is involved in NO synthesis
HSCARG regulation of argininosuccinate synthetase activity is crucial for maintaining the intracellular balance between redox state and nitric oxide levels
In response to the changes in the NADPH/NADP(+) ratio within cells, HSCARG, as a redox sensor, associates and dissociates with NADPH to form a new dynamic equilibrium.
HSCARG plays critical roles in regulation of NF-kappaB in response to cellular redox changes by promoting ubiquitination and proteolysis of RelA or COMMD1
Redox sensor protein. Undergoes restructuring and subcellular redistribution in response to changes in intracellular NADPH/NADP(+) levels. At low NADPH concentrations the protein is found mainly as a monomer, and binds argininosuccinate synthase (ASS1), the enzyme involved in nitric oxide synthesis. Association with ASS1 impairs its activity and reduces the production of nitric oxide, which subsecuently prevents apoptosis. Under normal NADPH concentrations, the protein is found as a dimer and hides the binding site for ASS1. The homodimer binds one molecule of NADPH. Has higher affinity for NADPH than for NADP(+). Binding to NADPH is necessary to form a stable dimer (By similarity).
nmrA-like family domain-containing protein 1
, short chain dehydrogenase/reductase family 48A, member 1