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Sequence and structural conservation reveal fingerprint residues in TRP channels | eLife
Source: elifesciences.org
Article summary:
1. Transient receptor potential (TRP) proteins are a large family of cation-selective channels involved in a variety of physiological functions.
2. This study by Deny Cabezas-Bratesco and collaborators draws from multiple bioinformatics approaches to uncover a set of highly conserved amino acid sequence features in group 1 TRP ion channels.
3. These identified features provide insight into the evolution and mechanisms of function of this diverse and important family of ion channel proteins.
Article analysis:
This article is generally reliable, as it draws from multiple sources such as published structural and functional data, phylogenetic reconstruction, sequence statistics, and structural analysis to uncover a set of highly conserved amino acid sequence features in group 1 TRP ion channels. The authors also provide an hypothesis for how differences in the connectivity between these different groups of residues may explain the apparent differences in coupling strategies used by TRP subgroups.
The article does not appear to be biased or one-sided, as it presents both sides equally and does not contain any promotional content or partiality. It also notes possible risks associated with abnormal expression of TRP channels being related to cancer development and progression.
The only potential issue with the article is that it does not explore any counterarguments or missing points of consideration that could challenge its findings or conclusions. However, overall this article appears to be trustworthy and reliable.