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In order to establish whether the recruitment of wild-type FUS into the cytoplasmic granules with the mutant FUS was due to the two proteins directly interacting, we performed a series of immunoprecipitation experiments.
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To understand how these diverse cellular functions interact, we performed a quantitative epistasis analysis by creating multimutant strains from those individual genes required for glyoxal resistance.
To detect interacting QTLs, we performed a two-dimensional genome-wide linkage scan, but no genetic interactions or epistatic effects were measured.
In order to identify novel MAPK15 interacting proteins, we performed a yeast two-hybrid screening.
To identify putative interacting partners, we performed a screen against a membrane peptide array comprising the AgSmc1 and AgSmc3 ATPase heads and AgScc1.
To elucidate which region of PAA-1 interacts with RSA-1/B″ we performed a genetic screen for interaction suppressors of rsa-1 or598ts rsa-1 or598ts
To investigate whether the MAD2B protein physically interacts with CLTA, we performed a glutathione S-transferase (GST) pull-down assay.
In order to identify proteins that interact with APOBEC3G, we performed a mass spectrometry analysis of proteins co-immunoprecipitated with APOBEC3G from primary CD4+ T cells or 293T cells.
In our search for host factors that interact with transposition, we performed a systematic search for the β-binding motif in transposases.
To verify that Plk4 and CDK11p58 were able to interact directly, we performed an in vitro pull down assay using Maltose-Binding Protein (MBP -tagged CDK11p58 iMBP -taggedon an amylose CDK11p58nd a recombimmobilisedgged full length Plk4 (See Methon section and Figure 4 D).
To identify novel IKK-interacting proteins, we performed an unbiased proteomics screen where we identified TfR1 (transferrin receptor 1).
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