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Within these complexes, ubiquitination of both receptors and β-arrestins introduces another level of regulation that can influence compartmentalization, trafficking and signalling properties of the complex (Becuwe et al., 2012).
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Association with β-arrestin also influences compartmentalization of complexes in the cellular milieu including internalization, recycling and degradation through their ability to bind other structural and regulatory proteins (Moore et al., 2006).
Interestingly, dual S-acylation was shown to influence protein compartmentalization to specialized plasmalemmal microdomains [ 33- 35].
The regional methylation differences we observe here might correlate with the density of other marks of active/inactive chromatin as proposed by Eckhardt et al. [ 33] and/or reflect (or influence) regional compartmentalization within the nucleus [ 67].
Increase in atmospheric oxygen is believed to have influenced cellular compartmentalization and thus to have been instrumental in the evolution of eukaryotes [ 36].
The uptake of these complex ligands may be facilitated by CXCL16, which may influence this differential compartmentalization [ 9].
Malignant growth may provoke histone modifications, which are epigenetic regulators of chromatin and can influence the genome compartmentalization.
Gene transcription at the nuclear periphery is also under the influence of the compartmentalization of chromatin domains and regulatory factors [ 20- 22].
Although some sirtuins may have redundant functions, their substrate specificity may also be influenced by intracellular compartmentalization, by different tissue expression patterns and distinct enzymatic activities.
The constrained localization of these enzymes leads to differential concentrations of the PIPs within various cellular compartments; in turn, this compartmentalization influences PIPs signalling and protein recruitment activities.
Since Cav-1 and Cav-2 can modulate channel endocytosis leading to channel degradation or inactivation (31– 36, 36) and Cav-2 can also regulate membrane protein trafficking independently from Cav-1 (37), the results obtained here suggest that the differences in the associations with Cav-2 could influence K346T channels' membrane compartmentalization, stability and trafficking.
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