Browse our anti-Vinexin (Sorbs3) Antibodies

Mouse (Murine) Sorbin and SH3 Domain Containing 3 (Sorbs3) interaction partners

1. These observations reveal a critical role of vinexin alpha and CAP in mechanotransduction and MSC differentiation.

2. Differential roles of SORBS proteins in mechanotransduction.

3. Vinexin beta deficiency attenuates atherogenesis primarily by suppressing vascular inflammation and inactivating Akt-nuclear factor kappaB signaling. Our data suggest that vinexin beta could be a therapeutic target for the treatment of atherosclerosis.

4. The results indicate that lipid rafts play an important role in extracellular matrix stiffness regulation of cell migration via expression vinculin and its interaction with vinexin alpha.

5. Our findings revealed that Vinexin-beta acts as a novel modulator of ischaemic injury

6. Vinexin-beta increases myocardial infarction-induced mortality and worsens cardiac dysfunction through aggravation of myocardial apoptosis and inflammatory response.

7. In the absence of retinoic acid (RA), vinexinbeta does not occupy RARgamma target gene promoters and sequesters nonphosphorylated RARgamma out of promoters

8. vinexin (-/-) mice exhibited a delay in cutaneous wound healing in both the back skin and tail without affecting the proliferation of keratinocytes

9. regulates the anchorage dependence of ERK2 activation stimulated by epidermal growth factor

10. vinexin is a novel substrate of ERK2 and may play roles in ERK-dependent cell regulation

11. phosphorylation of the AF-1 domain controls RARgamma-mediated transcription through triggering the dissociation of vinexin beta

12. gamma isoform seems to be implicated in regulation of Sox9 gene expression by modulating MAPK cascade in fetal gonads

13. vinexins are recruited to focal adhesions by activated vinculin

14. Data report the identification of the cytoskeletal protein vinexin as a protein interacting with SHIP2.

15. The testicular vinexin pattern underwent significant changes after developmental exposure to 17beta-estradiol (E(2)).

16. v-Src-mediated transformation suppresses the expression of focal adhesion protein vinexin.

17. vinexin alpha is tyrosine phosphorylated in v-Src-transformed cells, and this tyrosine phosphorylation of vinexin alpha attenuates the association of vinexin alpha with vinculin.

Human Sorbin and SH3 Domain Containing 3 (Sorbs3) interaction partners

1. Vinexin beta deficiency attenuates atherogenesis primarily by suppressing vascular inflammation and inactivating Akt-nuclear factor kappaB signaling. Our data suggest that vinexin beta could be a therapeutic target for the treatment of atherosclerosis.

2. The chromosome 8p tumor suppressor genes SORBS3 and SH2D4A are physically and functionally linked and provide a molecular mechanism of inhibiting STAT3-mediated IL-6 signaling in hepatocellular carcinoma cells.

3. Study identified possible epigenetic influence on differential gene expression in SORBS3 under obese conditions.

4. Our findings revealed that Vinexin-beta acts as a novel modulator of ischaemic injury

5. Taken together, the findings suggest that vinexin beta modulates NS5A phosphorylation via its interaction with NS5A, thereby regulating hepatitis C virus replication, implicating vinexin beta in the viral life cycle.

6. Vinexin knockdown using siRNA delayed migration of both HaCaT human keratinocytes and A431 epidermoid carcinoma cells in scratch assay but did not affect cell proliferation.

7. regulates cytoskeletal organization and signal transduction--review

8. vinexin is a novel substrate of ERK2 and may play roles in ERK-dependent cell regulation

9. phosphorylation of the AF-1 domain controls RARgamma-mediated transcription through triggering the dissociation of vinexin beta

10. These results suggest that vinexin beta plays a role in maintaining the phosphorylation of EGFR on the plasma membrane through the regulation of c-Cbl.

11. Vinexin is enriched at the leading edge of migrating cells, lamellipodia and and focal adhesions in well-spread cells.

12. Rhotekin forms a complex with vinexin and may play a role at focal adhesions.