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Although individual PTMs are clearly crucial in mediating protein structure-function relationships, until recently the potential for different modifications to influence each other through cooperation or competition had not been explored.
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In relation to the topic of this review most studies have examined the potential of epigenetic modification to influence future offspring greater adiposity and adverse cardiometabolic health than their cognitive function.
Our results show that PERP expression causes nuclear localization of p53 and increases the level of transcriptionally active p53 protein, which also presents posttranslational modifications known to influence the p53 MDM2 interaction and to enhance the pro-apoptotic gene transcription.
This could be of interest when investigating and developing mesh modification strategies to influence this early acute reaction.
These modifications were designed to influence hydrophobic hydrophilic balance as well as maintain the proton sponge effect in order to create an efficient vector with low toxicity.
Based on the premise that the interaction of chromatin modifications is hypothesized to influence CpG methylation, we present a closeness measure to characterize the regulatory interactions of epigenomic features.
Post-translational modifications are known to influence protein characteristics such as protein folding and stability, thus modulating biological processes like cell growth and migration [ 11].
Cells often chemically modify histones by adding acetyl or methyl groups, and these modifications are known to influence what proteins can bind to the nucleosomes, which ultimately influences what genes are expressed in the cell at a given time.
Interestingly, tubulin post-translational modifications were shown to influence the recruitment of protein complexes such as MAPs (i.e. Tau, MAP1B) or plus-end tracking proteins (p150Glued, EB1, CLIP170) onto microtubules (Verhey and Gaertig, 2007).
This cognitive modification is expected to influence the respond latency in respondents.
Site specific modification of the parent antibiotic was achieved with either PEG-acrylate or acrylamide functionalities, and the site of modification was found to influence antibiotic activity.
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