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Human CD81 Protein expressed in HEK-293 Cells - ABIN2713788
Goetzl, Mustapic, Kapogiannis, Eitan, Lobach, Goetzl, Schwartz, Miller: Cargo proteins of plasma astrocyte-derived exosomes in Alzheimer's disease. in FASEB journal : official publication of the Federation of American Societies for Experimental Biology 2016
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Human CD81 Protein expressed in Wheat germ - ABIN1348710
Soares, Castro, Tomás, Rodrigues, Gomes-Alves, Bellier, Klatzmann, Carrondo, Alves, Coroadinha: Tetraspanins displayed in retrovirus-derived virus-like particles and their immunogenicity. in Vaccine 2016
Molecular cloning; CD81 expression is widely diffused in spleen tissue
adoptive transfer of wild-type regulatory T cells into CD81-deficient mice was sufficient to promote tumor growth and metastasis; these findings suggested that CD81 modulates adaptive and innate immune responses
CD81-Rac (show AKT1 Proteins) interaction exerts an important regulatory role on the innate and adaptive immunity against bacterial infection and suggests a role for CD81 in the development of novel therapeutic targets during infectious diseases.
Plasmodium yoelii sporozoite rhoptry discharge occurs only in the presence of CD81, providing the first direct evidence for a role of CD81 during sporozoite productive invasion.
In vitro myotubes lacking CD9P-1 (show PTGFRN Proteins) or both CD9 and CD81 fuse with a higher frequency than normal myotubes
Data suggest that GPC3 (show GPC3 Proteins) down-regulates hepatocyte proliferation by binding to hedgehog (show SHH Proteins) (HH) and down-regulating the HH signaling pathway and binding with CD81, thus making it unavailable to bind to Hhex (show HHEX Proteins) and causing its nuclear translocation.
CD81 interacts with the T cell receptor to suppress signaling.
Data show that effective B cell receptor (BCR (show BCR Proteins)) signaling requires collaboration with the coreceptor CD19 (show CD19 Proteins) organized by the CD81-tetraspanin network.
results indicate that the CD19/CD81 complex interacts with CD38 but this interaction is not required to induce proliferation in mouse B lymphocytes
CD81 promotes the microvillus formation and/or extension while tetraspanin CD82 (show CD82 Proteins) inhibits these events. In addition, CD81 enhances the outward bending of the plasma membrane while CD82 (show CD82 Proteins) inhibits it.
Self-renewing hematopoietic stem cells express CD81 during stress-induced proliferation.
CD81 cell surface expression had a negative impact on survival in acute myeloid leukemia (show BCL11A Proteins).
Results from crystallography and molecular dynamics of CD81 long-extracellular loop (LEL) show that its flexibility is an inherent molecular property likely to be tuned by variation in pH and redox conditions. This tuning mechanism would explain the priming role ascribed to CD81LEL in rendering the virus-receptor complex fusogenic during cell entry.
Free energy calculations indicated that the E2/CD81 binding process might follow a two-step model involving (i) the electrostatic interaction-driven initial binding of human-specific E2-site2, followed by (ii) changes in the E2 orientation to facilitate the hydrophobic and van (show TNIP1 Proteins) der (show GDF3 Proteins) Waals interaction-driven binding of E2-site1
A new link between HCV receptor molecules and the hepatocyte glycocalyx, namely, CD81 and Synd-1 (show SDC1 Proteins).
Study used molecular dynamics simulations to gain insights into the role of local conformational flexibility in nanodomain formation in the plasma membrane, using the tetraspanin molecule CD81 as a model; suggest that exposing a flexible domain of CD81 enables binding to interaction partners by circumventing the restriction of orientation and conformational freedom of membrane proteins
The findings suggest that, in contrast with previous models, the ligand-binding site of integrin alphaVbeta3 (show ITGAV Proteins), binds to the constant region (helices A and B) of the EC2 (show TCF15 Proteins) domain of CD9, CD81, and CD151 (show CD151 Proteins) antigens.
Studies have shown that CD81 regulates cell migration and invasion, and has therefore been implicated in tumor growth, cancer progression and metastasis. CD81 is expressed in most types of cancer, and the overexpression or down-regulation of this molecule has been correlated with either good or bad prognosis. [review]
The transmembrane segments of CD81 pack as two largely separated pairs of helices, capped by the large extracellular loop (EC2 (show TCF15 Proteins)) at the outer membrane leaflet. The two pairs of helices converge at the inner leaflet to create an intramembrane pocket with additional electron density corresponding to a bound cholesterol molecule within the cavity.
Results suggest that the CD81 antigen (CD81) expressed by B cells has differential effects on B cell proliferation or apoptosis according to Epstein-Barr virus (EBV) infection and the expression level of CD81.
CD81 expression was lower in systemic sclerosis patients compared to controls independent of disease duration.
The protein encoded by this gene is a member of the transmembrane 4 superfamily, also known as the tetraspanin family. Most of these members are cell-surface proteins that are characterized by the presence of four hydrophobic domains. The proteins mediate signal transduction events that play a role in the regulation of cell development, activation, growth and motility. This encoded protein is a cell surface glycoprotein that is known to complex with integrins. This protein appears to promote muscle cell fusion and support myotube maintenance. Also it may be involved in signal transduction. This gene is localized in the tumor-suppressor gene region and thus it is a candidate gene for malignancies.
, 26 kDa cell surface protein TAPA-1
, target of the antiproliferative antibody 1
, CD81 antigen (target of antiproliferative antibody 1)
, CD 81 antigen