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Our findings revealed that Vinexin-beta acts as a novel modulator of ischaemic injury
Vinexin-beta increases myocardial infarction-induced mortality and worsens cardiac dysfunction through aggravation of myocardial apoptosis and inflammatory response.
vinexin (-/-) mice exhibited a delay in cutaneous wound healing in both the back skin and tail without affecting the proliferation of keratinocytes
regulates the anchorage dependence of ERK2 activation stimulated by epidermal growth factor (show EGF Proteins)
vinexin is a novel substrate of ERK2 and may play roles in ERK (show EPHB2 Proteins)-dependent cell regulation
phosphorylation of the AF-1 (show Psmd4 Proteins) domain controls RARgamma-mediated transcription through triggering the dissociation of vinexin beta
gamma isoform seems to be implicated in regulation of Sox9 (show SOX9 Proteins) gene expression by modulating MAPK cascade in fetal gonads
vinexins are recruited to focal adhesions by activated vinculin (show VCL Proteins)
Data report the identification of the cytoskeletal protein (show ADD3 Proteins) vinexin as a protein interacting with SHIP2 (show INPPL1 Proteins).
The testicular vinexin pattern underwent significant changes after developmental exposure to 17beta-estradiol (E(2)).
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.
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.
phosphorylation of the AF-1 (show EFNA5 Proteins) domain controls RARgamma-mediated transcription through triggering the dissociation of vinexin beta
These results suggest that vinexin beta plays a role in maintaining the phosphorylation of EGFR (show EGFR Proteins) on the plasma membrane through the regulation of c-Cbl (show CBL Proteins).
Vinexin is enriched at the leading edge of migrating cells, lamellipodia and and focal adhesions in well-spread cells.
Rhotekin (show RTKN Proteins) forms a complex with vinexin and may play a role at focal adhesions.
This gene encodes an SH3 domain-containing adaptor protein. The presence of SH3 domains play a role in this protein's ability to bind other cytoplasmic molecules and contribute to cystoskeletal organization, cell adhesion and migration, signaling, and gene expression. Multiple transcript variants encoding different isoforms have been found for this gene.
sorbin and SH3 domain containing 3
, vinexin beta (SH3-containing adaptor molecule-1)
, SH3 domain protein 4
, SH3 domain-containing protein SH3P3
, SH3-containing adapter molecule 1
, vinexin alpha
, vinexin beta
, sorbin and SH3 domain-containing protein 3