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To distinguish between these models, we directly compared binding of MW1 and 3B5H10 to normal and expanded polyQ repeats within huntingtin exon 1 fusion proteins.
We recently compared binding of 111In-DOTA-JR11 111In-DOTA-JR11 111In-DOTA-JR11to ZR75–1 and 111In-DOTA-Tyr3-octreotate 111In-DOTA-Tyr3-octreotate 111In-DOTA-Tyr3-octreotate 111In-DOTA-Tyr3-octreotatenalizatoon assay to investigate differences in SSTR agonist and antagonist binding to cell lines with endogenous and exogenous SSTR expression.
To address this question step by step we compared binding of LRRK2 mutants with ARHGEF7 in vitro.
In addition, we compared binding of peptide-free and peptide-loaded DR1 using an equilibrium sandwich ELISA assay (Fig. 4E).
We compared binding of Z11Z13-16Ald and E11E13-16Ald and found no difference (data not shown) thus suggesting that AtraPBP1 alone cannot discriminate stereoisomers of the major constituent of the sex pheromone.
Since the approach of binding studies of the isolated, epitope-labelled domains to suspended cells is very artificial we further characterized and compared binding of the full length and truncated TcdA to cell surfaces of intact cells.
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Far-Western analysis was used to compare binding of WRN488 1432 and WRN239 499 to p300.
To determine if both binding sites contributed equally, we performed a quantitative experiment to compare binding of the different forms of LITAF to Itch WW domains.
Electrophoretic mobility shift assays (EMSA) were performed to compare binding of recombinant ERRα and ERRγ proteins between 32P-labeled PPARA and authentic, previously described ERR binding sequences [28].
Although first SPR studies for trastuzumab were inconclusive [48], further experimentation is needed to compare binding of these antibodies to both the HER2/neu antigen and Fcγ receptor.
We tested this hypothesis by comparing binding of sumoylated and free HDAC1-FLAG to GST-CoREST using GST pull-down assays (Figure 6A).
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