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The main source of data to assemble the network is the study by de Folter et al. [ 15], that provides a semi-exhaustive map of protein-protein interactions between MADS domain proteins based on yeast two-hybrid assays.
Although we aimed to include a relatively large number of known biomarkers and functionally-related proteins to assemble the network, it is evident that false negative and false positive relationships may have influenced our findings.
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Using functional proteomic and genomic approaches, we have assembled the network architecture of yeast Swi/Snf.
Furthermore, the telosome interacts with other proteins, thereby assembling the network of interacting proteins on telomeres.
This can be an important problem while assembling the network structure of either novel pathways (e.g. Iron-Sulfur Cluster biogenesis) or complex pathways with an unclear reaction and regulation network, (e. g. cell cycle).
All of the most central proteins except P62993 (GRB2 - Growth factor receptor-bound protein 2) were into the initial list of 200 vitamin proteins that we used for assembling the network.
The network seeds comprised a total of 105 proteins (Tables S1 and S2), and were used to assemble the PPI network as described in the Methods section.
The obtained PPIs were used to assemble the HF PPI network.
A parallel and complementing way would assemble the metabolic network from literature sources only.
To assemble the PPI network of the S. cerevisiae peroxisome, we identified first the peroxisomal core proteins and then their mutual PPI.
We divide interactions on the basis of their type (A or P) and hence assemble the two networks.
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