Aperçu des produits pour SMURF1 Protéines (SMURF1)

Human SMAD Specific E3 Ubiquitin Protein Ligase 1 (SMURF1) interaction partners

1. Nedd8 (Montrer NEDD8 Protéines) binding to Smurf plays important roles in the regulation of cell migration and the BMP and TGFbeta (Montrer TGFB1 Protéines) signaling pathways.

2. Expression of Smurf1 was increased with WHO grade and was consistent with poor prognosis of gliomas.

3. Smurf1 interacts with and targets Securin (Montrer PTTG1 Protéines), an inhibitor of sister-chromatid separation, for poly-ubiquitination and proteasomal degradation.

4. Smurf1 overexpression decreases USP25 (Montrer USP25 Protéines) protein turnover, and the E3 ligase enzymatic activity of Smurf1 is required for USP25 (Montrer USP25 Protéines) degradation.

5. SMURF1 can be potentially used as a clinical biomarker and target for novel treatment of human GC.

6. Uev1A (Montrer UBE2V1 Protéines) appears to be involved in the BMP signaling pathway in which it collaborates with a ubiquitin E3 ligase Smurf1 to promote Smad1 (Montrer GARS Protéines) degradation in a Ubc13 (Montrer UBE2N Protéines)-independent manner.

7. High smurf1 expression is associated with neoplasms.

8. activation of AMPK (Montrer PRKAA1 Protéines) upregulated Smad6 (Montrer SMAD6 Protéines) and Smurf1 and thereby enhanced their interactions, resulting in its proteosome-dependent degradation of ALK2 (Montrer ACRV1 Protéines).

9. we propose that the PKA-Smurf1-PIPKIgamma pathway has an important role in pulmonary tumorigenesis and imposes substantial clinical impact on development of novel diagnostic markers and therapeutic targets for lung cancer treatment.

10. SMU (Montrer MLXIP Protéines)RF1 is increased in patients with pulmonary arterial hypertension

Mouse (Murine) SMAD Specific E3 Ubiquitin Protein Ligase 1 (SMURF1) interaction partners

1. Smurf1 interacts with and targets Securin (Montrer PTTG1 Protéines), an inhibitor of sister-chromatid separation, for poly-ubiquitination and proteasomal degradation.

2. Six2 (Montrer SIX2 Protéines) mediates the protective effects of GDNF on damaged DA neurons by regulating Smurf1 expression.

3. TGF-beta (Montrer TGFB1 Protéines) inhibited osteoblastic differentiation by inducing the MAPK-ERK (Montrer MAPK1 Protéines) pathway which upregulated the expression of ubiquitin ligase (Montrer RNF123 Protéines) SMURF1 and resulted in reduced presence of osteogenic proteins.

4. demonstration that Smurf1 acts as a brake for integrin activation by controlling Kindlin-2 (Montrer FERMT2 Protéines) protein levels, a new mechanism that permits precise modulation of integrin-mediated cellular functions

5. miR (Montrer MLXIP Protéines)-140-5p and SMURF1 are key regulators of disease pathology in pulmonary arterial hypertension

6. Smurf1 is required for selective autophagy of Mycobacterium tuberculosis and host defense against tuberculosis infection.

7. Smurf1 regulates glucose metabolism and inhibits osteoblast differentiation. Smurf1 function requires the presence of serine 148 (S148) in Smurf1.

8. Smurf1 mediates NGF (Montrer NGFB Protéines) signaling and ubiquitinates RhoA (Montrer RHOA Protéines) in growth cones, regulating the need for local translation and degradation.

9. Smurf-mediated endocytosis of Patched1 (Montrer PTCH1 Protéines) is required in sonic hedgehog (Montrer SHH Protéines) signal reception

10. Inhibition of rhBMP-2-induced ALP (Montrer CCL21A Protéines) activity by intracellular delivery of SMURF1 in murine calvarial preosteoblast cells.

Xenopus laevis SMAD Specific E3 Ubiquitin Protein Ligase 1 (SMURF1) interaction partners

1. Data demonstrate that Smurf1 and Smurf2 (Montrer SMURF2 Protéines) 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.

2. In Xenopus embryos, the BMP pathway is a major physiological target of Smurf1. We propose that in normal development Smurf1 cooperates with secreted BMP antagonists to limit BMP signaling in dorsal ectoderm.