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Although the possibility of not recovering all minor isoforms and rare modifications cannot be ruled out in our analysis, the MS data already suggests that the AT1R activation/inhibition causes fluctuation of several interesting and perhaps unique isoforms (i.e., Q96QV6, H2Q, H2AAme1, H2AQAc and H2AL) and PTM (Table 2), which must alter the composition of the nucleosome.
Other rare modifications in CS, such as 2-O-or 3-O-sulfation of the GlcA moieties, have also been reported (Prabhakar et al., 2005).
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Although 3-O-sulfation is a relatively rare modification, and to date very few proteins have been described that are influenced by it [ 78], several studies have described their alteration in different tumors.
Although various O-mannose glycopeptides could be identified from total brain tissue [ 13, 14], α-DG still remains the only mammalian glycoprotein clearly identified to contain this rare modification.
This rare modification to the heteroxenous (two host) life cycle is thought to have occurred relatively recently and may be responsible for the expansion of this parasite to nearly every continent [ 1].
We noted that the Femto substrate consistently detected rarer modifications, H3K9me2 and H3K4me3, at a higher level relative to total H3 than did the Pico substrate.
Like with other inherited rare disorders, modification of the primary genetic defects is not yet realistic.
Thus, 5-meC is a rare DNA modification in drosophila but absent in yeast.
Presently, one focus is the rare-earth modification of Y to modulate its acidity and cracking activity.
Assembly of Aβ16 22 is sensitive to variation in primary structure, but it is rare that destabilizing modifications abrogate aggregation.
However, some identifications arise from low sequence coverage making conclusions about isoforms challenging and observation of posttranslational modifications rare.
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