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We engineered DBs by selecting Fab fragments with fast off-rate kinetics, which allowed us to demonstrate that stable target binding was achieved only upon simultaneous, cooperative binding to both epitopes.
ICR65, however, cross-reacted with mAbs binding to both epitopes.
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Almost all allergen-specific antibodies were mutated, and binding to both conformational and linear allergen epitopes was detected.
The layer formation seems to hinder aPL binding to β2GPI epitopes close to D5 [16].
Both the mouse 13H11 MAb and the three prototypic cluster II human MAbs (98-6, 126-6, and 167-D) blocked 2F5 binding to gp41 epitopes to variable degrees; the combination of 98-6 and 13H11 completely blocked 2F5 binding.
Epitope mapping was performed with all antibodies to verify binding to linear epitopes.
The inhibition is mediated via antibody binding to epitopes outside of the CD81 binding site in E2, possibly by preventing conformational changes in E2 that are required for CD81 binding.
Based on the calculated binding affinity to MHC, epitopes were selected for ELISpot assays (IC50 < 50 nM, Supplementary Table 1).
In contrast, 2F5 showed a reduced binding to proteoliposomes, suggesting that the 2F5 epitope was differently exposed in both contexts.
Similar to antibodies, molecular scaffolds binding to PCSK9 close to its LDLR binding epitopes reduce the free PCSK9 and subsequently the LDL-C concentration in cynomolgus monkeys [ 118].
In addition, corresponding to the ability of FUV and TCH binding to the seLe antigens, these two GI NoVs develop an extra Le epitope binding site, making their binding interfaces trivalent, interacting with the Gal, H epitope/acetamido and Le epitope, respectively, while the NV binding interface is bivalent, consisting of the Gal and the H epitope/acetamido binding sites only.
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