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Such domains, found in many TFs, are predicted to stabilize protein dimer formation.
The bimolecular fluorescence complementation assay (BiFC) is a method that allows the detection of protein dimer formation in living cells [125].
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ERβ protein stability, dimer formation with ERα and expression of known ER target genes were characterized following endoxifen exposure.
However, we reasoned that this could be because M0, which is known to be present in the recombinant NP1 protein, blocks dimer formation.
Indeed, previous reports have demonstrated that diabetes reduced NO bio-availability without altering eNOS protein and its dimer formation in endothelial cells [ 53, 54].
The functions of these domains include dimer formation (protein-protein interaction) and DNA binding properties (protein-nucleic acid interactions) [51], [52].
One example is the alternative splicing of CCA1, in which the CCA1β protein isoform possesses protein domains required for dimer formation and transcriptional activation but lacks the MYB DNA-binding domain [ 27].
The importance of specific phosphorylation sites in A. thaliana receptor proteins for receptor dimer formation and activation of signaling events was concluded from experiments on the BRI1/BAK1 receptors [ 50].
The substitutions A79V and K82R are placed in the fourth α-helix of C protein, which has been associated with RNA binding, dimer formation, protein stability and infectious particle production23, 24.
We expected this protein to be a dimer, if the N-terminus of the protein is important to dimer formation, as our mutations of NP4, discussed above, had suggested.
The relatively high concentration of purified protein could have promoted dimer formation in our preparations.
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