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E3 ubiquitin-protein ligase which accepts ubiquitin from an E2 ubiquitin-conjugating enzyme in the form of a thioester and then directly transfers the ubiquitin to targeted substrates. Additionally we are shipping SMURF2 Antibodies (82) and SMURF2 Kits (6) and many more products for this protein.
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results provide the evidence that Smurf2 may play specific roles in glandular secretion, trophoblastic cell invasion, and placentation through mediating the expression of the related proteins of TGF-beta (show TGFB1 Proteins) signaling pathway during early pregnancy
High SMURF2 expression is associated with breast cancer progression.
Smurf2, an E3 ubiquitin ligase (show MUL1 Proteins), interacts with PDE4B (show PDE4B Proteins) and attenuates liver fibrosis through miR (show MLXIP Proteins)-132 mediated CTGF (show CTGF Proteins) inhibition.
Low SMURF2 expression is associated with breast cancer organoid invasiveness.
Results identified Smurf2 as an essential regulator of Topo IIalpha, providing novel insights into its control and into the suggested tumor-suppressor functions of Smurf2.
found that phospho-AIMP2 (show AIMP2 Proteins) dissociated from the multi-tRNA synthetase complex and translocated to the nucleus, where it bound to Smurf2
Ectopic expression of human Smurf2 driven by the Col2a1 (show COL2A1 Proteins) promoter accelerated disc degeneration in Col2a1 (show COL2A1 Proteins)-Smurf2 transgenic mice, and that higher levels of connective tissue growth factor (show CTGF Proteins) protein and mRNA were present in Col2a1 (show COL2A1 Proteins)-Smurf2 transgenic discs, indicate that Smurf2 accelerates disc degeneration via upregulation of connective tissue growth factor (show CTGF Proteins).
data suggest for the first time that the choice of binding partners for SMURF2 can sustain or repress TGFbeta (show TGFB1 Proteins) signaling, and RNF11 (show RNF11 Proteins) may promote TGFbeta (show TGFB1 Proteins)-induced cell migration.
Neddylation of Smurf1 (show SMURF1 Proteins) activates its ubiquitin ligase activity and Smurf2 exerts Nedd8 (show NEDD8 Proteins) ligase activity. This study provided new clues of Smurf2 activation regulation.
The Smurf2 acts in a sumoylation-regulated manner to suppress TGFbeta (show TGFB1 Proteins)-induced Epithelial-mesenchymal transition.
the findings of this study demonstrate that the downregulation of SnoN (show SKIL Proteins) expression in hRPTECs under high-glucose conditions is mediated by the increased expression of Smurf2 through the TGF-b1/Smad (show SMAD1 Proteins) signaling pathway.
Young Smurf2-deficient mice develop milder osteoarthritis in knee articular cartilage compared to WT mice after surgical destabilization of the medial meniscus.
TAT (show TAT Proteins) fused to WW2/WW3 of Smurf2 could interfere with TGF-beta (show TGFB1 Proteins) signaling and reduce ArgI gene expression.
Smurf-mediated endocytosis of Patched1 (show PTCH1 Proteins) is required in sonic hedgehog (show SHH Proteins) signal reception
Data indicate that TNF receptor associated factor 4 (TRAF4 (show TRAF4 Proteins)) recruited the E3-ligase SMURF2, to degrade the IL-25R-inhibitory molecule DAZ associated protein 2 (DAZAP2 (show DAZAP2 Proteins)).
Expression of Smurf2 was increased with age and in response to regenerative stress during serial transplantation, our findings suggest that Smurf2 plays an important role in regulating HSC (show FUT1 Proteins) self-renewal and aging.
Akt (show AKT1 Proteins) regulates osteoblast differentiation by enhancing the protein stability and transcriptional activity of Runx2 (show RUNX2 Proteins) through regulation of degradation of Smurf2.
that Smurf2 is an important nonredundant negative regulator of virus-triggered type I IFN signaling by targeting VISA (show MAVS Proteins) for K48-linked ubiquitination and degradation.
Smurf2 mediates ubiquitination and degradation of YY1 (show YY1 Proteins), a key germinal centre transcription factor.
Smurf2 deficiency increased the susceptibility of mice to spontaneous tumorigenesis, most notably B-cell lymphoma
Data demonstrate that Smurf1 (show SMURF1 Proteins) and Smurf2 have overlapping and distinct functionalities during early frog embryogenesis; collectively, they regulate ectodermal and mesodermal induction and patterning to ensure normal development of Xenopus embryos.
E3 ubiquitin-protein ligase which accepts ubiquitin from an E2 ubiquitin-conjugating enzyme in the form of a thioester and then directly transfers the ubiquitin to targeted substrates. Interacts with SMAD1 and SMAD7 in order to trigger their ubiquitination and proteasome-dependent degradation. In addition, interaction with SMAD7 activates autocatalytic degradation, which is prevented by interaction with SCYE1. Forms a stable complex with the TGF-beta receptor-mediated phosphorylated SMAD2 and SMAD3. In this way, SMAD2 may recruit substrates, such as SNON, for ubiquitin-mediated degradation. Enhances the inhibitory activity of SMAD7 and reduces the transcriptional activity of SMAD2. Coexpression of SMURF2 with SMAD1 results in considerable decrease in steady-state level of SMAD1 protein and a smaller decrease of SMAD2 level (By similarity).
SMAD specific E3 ubiquitin protein ligase 2
, E3 ubiquitin-protein ligase SMURF2-like
, e3 ubiquitin-protein ligase SMURF2-like
, E3 ubiquitin ligase SMURF2
, E3 ubiquitin-protein ligase SMURF2
, SMAD ubiquitination regulatory factor 2
, SMAD-specific E3 ubiquitin-protein ligase 2
, E3 ubiquitin ligase Smurf2