analyses of compact trichinella kinomes reveal a mos-like protein kinase with a unique n-terminal domain

Clicks: 173
ID: 142493
2016
Free PDF
Article Quality & Performance Metrics
Overall Quality
Not rated
Combines reader engagement with the AI quality analysis. This article has not been analysed, so there is no overall score — reader engagement is measured and shown alongside.
AI Quality Assessment
Not analyzed
Readership in this journal
Star

Ranked #157 of 194 articles by views in separation and purification technology

Most read Least read

Bar heights use a square-root scale. Only the 120 most-read articles are drawn; the journal has 194 in total.

Mint this article as an NFT
Not yet minted

Create a permanent, verifiable on-chain record of this article on the Scimatic Network. The NFT is held in your Journament account, and you can withdraw it to your own wallet at any time.

5 SUSD one-off · no wallet required
Sign in to mint
Abstract
Parasitic worms of the genus Trichinella (phylum Nematoda; class Enoplea) represent a complex of at least twelve taxa that infect a range of different host animals, including humans, around the world. They are foodborne, intracellular nematodes, and their life cycles differ substantially from those of other nematodes. The recent characterization of the genomes and transcriptomes of all twelve recognized taxa of Trichinella now allows, for the first time, detailed studies of their molecular biology. In the present study, we defined, curated, and compared the protein kinase complements (kinomes) of Trichinella spiralis and T. pseudospiralis using an integrated bioinformatic workflow employing transcriptomic and genomic data sets. We examined how variation in the kinome might link to unique aspects of Trichinella morphology, biology, and evolution. Furthermore, we utilized in silico structural modeling to discover and characterize a novel, MOS-like kinase with an unusual, previously undescribed N-terminal domain. Taken together, the present findings provide a basis for comparative investigations of nematode kinomes, and might facilitate the identification of Enoplea-specific intervention and diagnostic targets. Importantly, the in silico modeling approach assessed here provides an exciting prospect of being able to identify and classify currently unknown (orphan) kinases, as a foundation for their subsequent structural and functional investigation.
Reference Key
stroehlein2016g3:analyses Use this key to autocite in the manuscript while using SciMatic Manuscript Manager or Thesis Manager
Authors ;Andreas J. Stroehlein;Neil D. Young;Pasi K. Korhonen;Bill C. H. Chang;Paul W. Sternberg;Giuseppe La Rosa;Edoardo Pozio;Robin B. Gasser
Journal separation and purification technology
Year 2016
DOI
10.1534/g3.116.032961
URL
http://g3journal.org/lookup/doi/10.1534/g3.116.032961
Keywords
protein kinases

Citations

No citations found. To add a citation, contact the admin at info@scimatic.org

Comments

No comments yet. Be the first to comment on this article.