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The TPR domain of CHIP is known to mediate an interaction with Hsp70 [43].
The vertebrate and Drosophila NuRD complexes also contain the methyl-CpG-binding protein MBD2/3, which is proposed to mediate an interaction between NuRD and methylated DNA [17].
In addition to a BAG domain, BAG1 contains a ubiquitin-like domain which may mediate an interaction with the 26S proteasome [54].
Here, we report that the C-terminus of PC-1 contains at least one polyproline domain that is able to mediate an interaction with Src-homology 3 domains (SH3).
Using the GST-fused SH3 domain of NPHP1 (GST-NPHP1-SH3) and the histidine tagged C-terminus of PC-1, we found that these two domains are indeed able to interact in vitro (Figure 2A and Figure S1C), suggesting that the C-tail of PC-1 contains motifs able to mediate an interaction with the SH3 domain of NPHP1.
Therefore, we hypothesized that Nck could mediate an interaction between EphB1 and Caskin1.
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The poly-lysine (pK) incorporated into pIX locales in AdLucIXpK has been shown to mediate Ad interaction with cellular heparan sulfate proteoglycans (HSPGs), resulting in CAR-independent virus-cell binding and transduction [13].
Like its vertebrate counterparts, Zyx102 displays three carboxy-terminal LIM domains, a potential nuclear export signal, and three proline-rich motifs, one of which matches the consensus for mediating an interaction with Ena/VASP (Drosophila Enabled/Vasodilator-stimulated phosphoprotein) proteins.
Two macromolecular complexes responsible for mediating an interaction with mannose-containing receptors were purified from fimA- Escherichia coli by mannose affinity chromatography and ion-exchange chromatography.
They are defined as 'a chemical that carries information that mediates an interaction among two individuals and results in an adaptive response in the receiver.
Here we identify a novel domain in the PC-1 C-terminal tail, a polyproline motif mediating an interaction with Src homology domain 3 (SH3).
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