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Surface Plasmon Resonance Binding assay, performed on the synthesized compounds, allow to identify a series of molecules able to potently interact with the target enzyme and to disclose an interesting hit: compound 2b showed to interact with the ATP binding site in the N-terminus domain of Hsp90 and to efficiently inhibit the chaperone activity.
In human fibroblasts, Ptgs2 has been showed to interact with Cav1 (Caveolin 1) [ 45], which is the main component of the caveolae plasma membranes.
The G2019S LRRK2 mutation, the most common mutation found in familial PD phenotypes, has been showed to interact with a-Syn during chaperone-mediated autophagy and consequently, promote a-Syn dysfunction [ 54].
OR83b-Or22a complex is also showed to interact through C-terminal ends in both the models (transmembrane region and dual template dimer model), indicating C-terminus plays important role in oligomerization.
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DLF1 has also been shown to interact with maize Hd3a/FT.
Marine organisms (particularly phytoplankton) have shown to interact with ENPs leading to negative repercussions [9 11].
Uranyl has been shown to interact with catechol in aqueous solutions.
However, recently hTIM-1 was shown to interact with NPC1, a fusion receptor for filovirus.
Even anions such a [BPh4]− have been shown to interact with the cationic centres.
P34 has also been shown to interact with vegetative storage proteins and NADH-dependent hydroxypyruvate reductase.
They are shown to interact with DNA, suggesting that this biomolecule may be the parasite target.
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Justyna Jupowicz-Kozak
CEO of Professional Science Editing for Scientists @ prosciediting.com