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This hypothesis is independently supported by the reported interaction with another partner of ataxin-3, the valosin-containing protein VCP.
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Our experiments reveal that Feo and Klp3A form a complex during cytokinesis and their interaction appears to be regulated by dephosphorylation (Fig 5), similar to the reported interaction between PRC1 and KIF4 in mammals [4].
Indeed, this is supported by the previously reported interactions of Scrib, βPIX and Cdc42.
One of our goals in this paper is to test the validity of a reported interaction by using structural information about the interacting proteins in a cluster.
This is supported by anecdotally reported interactions between numerous participants and the lab coordinator/instructor, in which participants expressed a frustration and dissatisfaction with TA1's level of preparedness and familiarity with in-class activates.
The number of reported interactions might be explained by the fact that omeprazole has been available longer than other PPIs (since 1989).
We made use of a threshold on the quality of reported interactions that are created by STRING by benchmarking the different interaction data sources to KEGG.
Joint regulation activity can be expected by the physical binding of well reported interactions such as MYC-MAX and SMAD2-SMAD4; but other interesting interactions and interaction groups were revealed by the network: SMAD2-SKIL and SMAD4-SKI; E2F4-TFDP1; STAT2-IRF9; NFYA-NFYB-NFYC; USRF-GTF2; SRF-GTF2I and SRF-CEBPB.
The validity of this methodology was demonstrated by confirmation of the previously reported synergistic interaction between cisplatin and 5-FU (data not shown) (Shirasaka et al, 1993; Tsai et al, 1993).
In brief, the binding to TNFR of PGRN and its-derived Atsttrin have been confirmed and extended by the group that originally reported the interactions, and also by numerous independent groups.
Thus, as shown by the simulations reported in this paper, CLR03 interactions with the Lys residues of PAP are not preserved, unlike CLR01, which forms conserved inclusion complexes.
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