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The reversible posttranslational modification of proteins by the addition of small ubiquitin-like SUMO proteins (see SUMO1\; MIM 601912) is required for numerous biologic processes. Additionally we are shipping ULP1 Antibodies (60) and many more products for this protein.
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The present study examined dynamic changes in SENP3 expression in the cerebral cortex and in its cellular localization.
The p53-independent tumor suppressive functions of p19(Arf) may be mediated by its ability to antagonize Senp3, thereby inducing cell cycle arrest by abnormally elevating the cellular levels of SUMOylated proteins.
SENP3 knockdown reduced cadmium-induced caspase 3 (show CASP3 Proteins) cleavage and cell death in PC12 cells, while SENP3 overexpression enhanced cell death.
Our data identified SUMOylation as a previously undescribed post-translational modification of STAT3 (show STAT3 Proteins) and SENP3 as a critical positive modulator of tobacco- or cytokine-induced STAT3 (show STAT3 Proteins) activation.
The data demonstrate that SUMO2 (show SUMO2 Proteins) conjugation and SENP3-driven deSUMOylation of PELP1 (show PELP1 Proteins) is instrumental for ordered progression of ribosome maturation, and they provide molecular insight into the dynamics of ribosome maturation.
our findings for the first time specifically supported that SUMO-specific protease 3 might play an important role in the regulation of epithelial ovarian cancer progression and could serve as a potential biomarker for prognosis as well as provide a promising therapeutic target against epithelial ovarian cancer
In early-onset pre-eclampsia, enhanced deSUMOylation of HIF1A (show HIF1A Proteins) by SENP3 may in part contribute to increased HIF1A (show HIF1A Proteins) activity and stability found in this pathology.
High SENP3 expression is associated with stomach neoplasms.
SENP3, which is increased in gastric cancer cells, potentiates the transcriptional activity of FOXC2 (show FOXC2 Proteins) through de-SUMOylation, in favor of the induction of specific mesenchymal gene expression in gastric cancer metastasis.
Evidence show that mTOR (show FRAP1 Proteins)-mediated phosphorylation of SENP3 facilitates the interaction with NPM1 (show NPM1 Proteins), thereby promoting nucleolar targeting.
SENP3 is associated with MLL1/MLL2 complexes and catalyzes deSUMOylation of RbBP5 (show RBBP5 Proteins).
ROS (show ROS1 Proteins) induced SENP3 redistribution from the nucleoli to the nucleoplasm.
The reversible posttranslational modification of proteins by the addition of small ubiquitin-like SUMO proteins (see SUMO1\; MIM 601912) is required for numerous biologic processes. SUMO-specific proteases, such as SENP3, are responsible for the initial processing of SUMO precursors to generate a C-terminal diglycine motif required for the conjugation reaction. They also have isopeptidase activity for the removal of SUMO from high molecular mass SUMO conjugates (Di Bacco et al., 2006
SUMO-1-specific protease 3
, SUMO/sentrin specific protease 3
, sentrin-specific protease 3
, sentrin/SUMO-specific protease SENP3
, smt3-specific isopeptidase 1
, sentrin/SUMO-specific protease 3
, SUMO/sentrin specific peptidase 3