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A key protein family involved in IE binding is the antigenic variant P. falciparum Erythrocyte Membrane 1 (PfEMP1) [ 3- 5].
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These mutations are predominantly in the antigenic sites on HA that are proximal to the RBS (since interfering with receptor binding is the primary target for neutralizing antibodies).
The specific antibody-binding capacity is the mean number of accessible antigenic sites per cell, referred to as antigen density and expressed in sites/cell.
VP6 is the most antigenic and abundant rotavirus structural protein.
RSV-D3 and RSV-C4 also showed some competition at high concentrations (µM) with 101F Fab, indicating the epitope recognized by these VHH is overlapping to some degree, but most binding parts are in the antigenic site II (Fig. 1C).
In order to test the cross-reactivity of the selected antibody clones with other strains of the VEEV as well as with other antigenic complexes, their binding was evaluated in a sandwich antigen catch ELISA by using an Alphavirus specific mAb mixture for capturing and the selected scFv phage for detection.
All three SpTPC immunoprecipitates were associated with significantly greater [P]NAADP binding than controls, with no such associated binding for non-sea urchin control lysate; moreover, binding was blocked by preincubation with specific antigenic peptides, but not by unrelated peptides.
β2GPI is the most important antigenic target of aPL [ 9].
Through such analysis, recombinant MSP3.1-Ct was found to be the 'most antigenic' and MSP3.4-Ct the 'least antigenic'.
The other one is the intracellular secretion of antigenic molecule.
The binding of antigenic peptides to HLA molecules is the most selective step in identifying T-cell epitopes.
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