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Necrotic cells, different from apoptotic ones, release a non-oxidised, immunogenic form of the alarmin HMGB-1 that activates dendritic cells by engaging receptor for advanced glycation endproducts, TLR4, TLR7 and TLR9 receptors.
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Hyaluronan also confers motility directly upon cells by engaging receptors that interact with the cytoskeleton (Turley 1992).
It is initiated by engaging receptors on the surface of the macrophages which express various receptors that participate in target cell recognition and internalization of ligands [ 21].
Our results are compatible with a scenario in which the accumulation of engaged receptor subunits into lipid rafts is required for receptor ubiquitination, a prerequisite for efficient receptor internalization, sorting and delivery to a lysosomal compartment.
Cell pretreatment with UBE1-41 did not abrogate the Ag-induced redistribution of receptor subunits into the detergent-insoluble fractions (Figure S1), supporting the conclusion that the engaged receptor complexes translocate to lipid rafts before the ubiquitination process.
The kinetic-segregation model predicts that elongation of a receptor/ligand complex would abrogate signaling because the increased intermembrane distance leads to less effective segregation of the engaged receptor from tyrosine phosphatases with large ectodomains.
Our findings are compatible with a scenario in which the recruitment of engaged receptor subunits into lipid rafts is required for receptor ubiquitination, and then the ubiquitinated receptors are simply internalized from the plasma membrane location (being raft or not) in which they show competence for interaction with the endocytic machinery including UIM containing proteins.
The infected cell commences to synthesize Env proteins, which, upon insertion in the plasmalemma, engages receptor proteins in neighboring cells and initiate fusions.
To further explore the relationship between the number of engaged receptors and signalling efficiency through calcium rise, we decoupled TCR/CD3 engagement and cell-particle contact formation.
RMS cells also respond to several growth factors that engage receptors with intrinsic tyrosine kinase activity [18, 51].
In summary, our findings shed lights on the central role of lipid raft-dependent FcεRI ubiquitination in controlling the endocytosis of engaged receptors.
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