p(HGNC:BAG4)
Thus, BAG4 overexpression disrupted P body organization PubMed:25036637
Thus, BAG4 overexpression disrupted P body organization PubMed:25036637
BAG4, in contrast, interacted with three central components of the These three proteins localize to cytoplasmic structures known as processing bodies, or P bodies, which are involved in mRNA decapping, degradation, and translational silencing (Eulalio et al., 2007): DCP1A, EDC3, and DDX6 (Figure 3E) PubMed:25036637
BAG4, in contrast, interacted with three central components of the These three proteins localize to cytoplasmic structures known as processing bodies, or P bodies, which are involved in mRNA decapping, degradation, and translational silencing (Eulalio et al., 2007): DCP1A, EDC3, and DDX6 (Figure 3E) PubMed:25036637
BAG4, in contrast, interacted with three central components of the These three proteins localize to cytoplasmic structures known as processing bodies, or P bodies, which are involved in mRNA decapping, degradation, and translational silencing (Eulalio et al., 2007): DCP1A, EDC3, and DDX6 (Figure 3E) PubMed:25036637
BAG3 and BAG4 showed a strong association only with the small heat shock protein Hsp27 (Figure 5F) and the mRNA decapping complex member DCP1B, respectively (Figure 5G), whereas BAG1 interacted with several proteasome subunits (Figure S4C) PubMed:25036637
BAG3 and BAG4 showed a strong association only with the small heat shock protein Hsp27 (Figure 5F) and the mRNA decapping complex member DCP1B, respectively (Figure 5G), whereas BAG1 interacted with several proteasome subunits (Figure S4C) PubMed:25036637
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If you find BEL Commons useful in your work, please consider citing: Hoyt, C. T., Domingo-Fernández, D., & Hofmann-Apitius, M. (2018). BEL Commons: an environment for exploration and analysis of networks encoded in Biological Expression Language. Database, 2018(3), 1–11.