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Such level of interactions has generated in the international community an urgent need to explore the different underlying molecular mechanisms responsible for such modifications, because mutagenic and genotoxic effects have been identified to be closely related to the initial molecular alterations.
Oxidant exposure may trigger the post-translational modification of proteins, and nuclear transport factors are potential candidates for such modifications.
Precise knowledge of all the genes influencing quality and resistance traits is an absolute prerequisite for such modifications.
To identify sites for such modifications, we searched for potential regulatory motifs using bioinformatic prediction algorithms (http://scansite.mit.edu, [25]) and identified a putative protein kinase A (PKA) phosphorylation site at S229 within the POUS domain of Oct4 (Figure 2A).
The key regions in an siRNA duplex for such modifications are the central position, the seed region and the 3'-end of the sense-strand siRNA element, which appear to be related to target RNA cleavage, target RNA recognition and assembly of the antisense-strand (guide) siRNA element into RISCs, respectively.
Whether treatment is temporarily withheld or the dosage reduced and the reasons for such modifications will also be recorded.
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The necessity for such modification was first demonstrated by natural rubber (polymer designation cis-polyisoprene) when it began to be produced commercially in the 18th century.
The study attempted to determine the optimum grafting conditions for such modification.
Cysteines have been used as attachment point for such modification, however, to be susceptible for chemical modification the involved thiol must be in its reduced form.
Previous labeling studies indicated that the C-5 methylation originated from C-3 of serine and is catalyzed by a new enzyme independent of thymidylate synthase (Isono and Suhadolnik, 1976; Isono, 1988), however, the molecular mechanism for such modification remained elusive for decades.
As arginine methylation is also known to occur in budding yeast, it is possible that enzymes responsible for such modification on arginine residues could demonstrate substrate promiscuity, and thus the known arginine methyltransferases Hmt1, Rmt2, and Hsl7 [65], [66], [66] were also included in this screen.
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