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Gookin, S. et al. A map of protein dynamics during cell-cycle progression and cell-cycle exit.
Delta analysis of 16 proteins representing core structural complexes spanning the centromeric chromatin-microtubule interface, when correlated with mechanical states of spindle-attached kinetochores, provided a nanometer-scale map of protein position and mechanical properties of protein linkages.
I applied this method to numerous time points through the yeast meiotic program in parallel with mRNA-seq and molecular staging to generate a rich atlas of meiotic events and gene expression and the first high-resolution map of protein synthesis through a developmental program (Brar et al., Science, 2012).
This research resulted in creating a map of protein interactions to explain human diseases.
Paralog retention within the module is thus an important factor in shaping the map of protein complexes.
Unfortunately, we do not have a map of protein complexes prior to gene duplications and we have to rely on the indirect evidence of ancestral state.
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Towards this goal, Baserga and colleagues have recently undertaken a systematic yeast two-hybrid analysis of the UtpA and UtpB complexes to provide a comprehensive map of protein-protein interactions within these complexes [21], [22].
The above analysis results in a map of proteins within the SAE complex.
A global map of protein-protein interactions in cellular systems provides key insights into the workings of an organism.
CLIP-Seq, with the ability to provide a genome-wide map of protein-RNA interactions, has been increasingly used to decipher RBP-mediated posttranscriptional regulation.
To date, generating a high resolution and precise map of protein-RNA interactions still remains a big challenge, which requires novel experimental, computational, and statistical solutions.
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