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To identify the domain of CCN2 responsible for EGFR binding, we applied a series of CCN2-deletion mutant constructs.
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Characterization of RBP-Binding Sites In order to identify hnRNP C binding sites, we applied a peak-finding algorithm that identified clusters of crosslink nucleotides with significant enrichment of crosslink events relative to the local environment (König et al., 2010 ).
Based on the phage-selected binding pattern we applied a simple scoring system combined with an untraditional baseline correction approach to identify novel natural binding partners in the human proteome.
To explore CsA binding proteins, we applied a chemical biology approach.
To delineate the role of RNA modifications in the SGEC B7.2 protein binding properties, we applied a RT-PCR protocol that amplifies the entire coding region of the B7.2 mRNA.
To gain a deeper understanding of the DNA-binding of SeqA we applied a widely used standard ChIP-Chip protocol [ 3].
To select the binding mode of each compound, we applied a qualitative analysis based on the location/orientation of the best 100 docked conformations given by Autodock in relation to the co-crystallised ligand GW409544 (Ali et al., 2008).
We applied a one-binding-state model in a reaction dominant regime to analyze our FRAP data [31].
In order to further assess the role of TBP2 in oocyte transcription functionally, we applied an altered binding specificity mutant reporter system [ 26].
In order to obtain a genome-wide view of PPARγ binding sites, we applied the pair end-tagging technology (ChIP-PET) to map PPARγ binding sites in 3T3-L1 preadipocellscells.
To assess whether HKH40A is capable of binding BiP, we applied microscale thermophoresis (MSN) using the titration of the compound with recombinant human BiP.
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