Evidence map›Paper›PMID 27412987›Full record

ArticleG3 (Bethesda, Md.)2016

Analyses of Compact Trichinella Kinomes Reveal a MOS-Like Protein Kinase with a Unique N-Terminal Domain.

Andreas J Stroehlein, Neil D Young, Pasi K Korhonen, Bill C H Chang, Paul W Sternberg, Giuseppe La Rosa, Edoardo Pozio, Robin B Gasser

Abstract read
In one paragraph

Article in G3 (Bethesda, Md.), 2016. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 2 papers.

0numbers the graph read from it
0cells of the map it votes in
2citing papers in PubMed
–field-weighted citation impact
1 · What the graph read from it

What it found

Each row is one number read from the abstract, on the scale the paper reported it, with its interval. Left of the dashed line favours the treatment, right favours the comparator. Under each row is the sentence it came from. New to these charts? A ten-minute tutorial.

The abstract states no effect estimate the extractor could read, or names no intervention and outcome on the map, so this paper lights no cell and moves no belief. It is still indexed, cited and linked below.

2 · The registry

The trial behind it

Trials whose registry record cites this paper, or whose number appears in the abstract. A trial that started after this paper was published is citing it as background, not reporting it.

Neither the registry nor the abstract names a trial number. If this is a trial report, that itself is worth knowing.

3 · Its place in the literature

Who cites it

2 citing papers in PubMed.

  1. Veterinary sciences · 2022
    Article
  2. Article
4 · The record

Corrections and comments

PubMed lists nothing against this paper. Absence here is not a guarantee, only a check that was made.

5 · Who and what money

Authors and funding

8 authors.

Andreas J StroehleinFaculty of Veterinary and Agricultural Sciences, The University of Melbourne, Parkville, Victoria 3010, Australia.
Neil D YoungFaculty of Veterinary and Agricultural Sciences, The University of Melbourne, Parkville, Victoria 3010, Australia.
Pasi K KorhonenFaculty of Veterinary and Agricultural Sciences, The University of Melbourne, Parkville, Victoria 3010, Australia.
Bill C H ChangFaculty of Veterinary and Agricultural Sciences, The University of Melbourne, Parkville, Victoria 3010, Australia Yourgene Bioscience, Shu-Lin District, New Taipei City 23863, Taiwan.
Paul W SternbergHoward Hughes Medical Institute, Chevy Chase, MD 20815-6789 Division of Biology and Biological Engineering, California Institute of Technology, Pasadena, California 91125.
Giuseppe La RosaIstituto Superiore di Sanità, 00161 Rome, Italy.
Edoardo PozioIstituto Superiore di Sanità, 00161 Rome, Italy.
Robin B GasserFaculty of Veterinary and Agricultural Sciences, The University of Melbourne, Parkville, Victoria 3010, Australia robinbg@unimelb.edu.au.

Funding

Howard Hughes Medical InstituteWellcome Trust
6 · The paper itself

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.

Indexed as

AnimalsComputational BiologyGenomeGenomicsHumansProtein ConformationProtein KinasesSpecies SpecificityTranscriptomeTrichinellaTrichinella spiralisTrichinellosisProtein Kinaseskinomeparasitic wormsprotein annotationprotein kinasesTrichinella

Identifiers

PMID27412987
PMCPMC5015942

What OpenQuestion holds

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Registered trials

None linked

Read under generation 80e0d062 · epoch 390. Bibliography from PubMed, PubMed Central and OpenAlex; grants from NIH RePORTER; trial links from ClinicalTrials.gov; estimates, votes and beliefs from the OpenQuestion graph.