Evidence map›Paper›PMID 28159896›Full record

ReviewThe Biochemical journal2017

From the research laboratory to the database: the Caenorhabditis elegans kinome in UniProtKB.

Rossana Zaru, Michele Magrane, Claire O'Donovan, UniProt Consortium

Open access · bronzeAbstract readReview
In one paragraph

Review in The Biochemical journal, 2017. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 6 papers.

0numbers the graph read from it
0cells of the map it votes in
6citing papers in PubMed
0.6field-weighted citation impact, top 36% of its field
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

6 citing papers in PubMed, 13 citations in OpenAlex.

  1. Article
  2. Kinome-wide RNAi screening inJournal of biosciences · 2025
    Article
  3. Article
  4. Article
  5. Review
  6. 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

4 authors at 1 institution in 2 countries.

Rossana ZaruEuropean Molecular Biology Laboratory, European Bioinformatics Institute (EMBL-EBI), Wellcome Genome Campus, Hinxton, Cambridge CB10 1SD, U.K. rzaru@ebi.ac.uk.
Michele MagraneEuropean Molecular Biology Laboratory, European Bioinformatics Institute (EMBL-EBI), Wellcome Genome Campus, Hinxton, Cambridge CB10 1SD, U.K.
Claire O'DonovanEuropean Molecular Biology Laboratory, European Bioinformatics Institute (EMBL-EBI), Wellcome Genome Campus, Hinxton, Cambridge CB10 1SD, U.K.
UniProt Consortium
European Bioinformatics Institute · GB

Funding

Predictive Modeling & Optimal Control Framework for Model-Based Epidemic Response in DelawareP20GM103446 · NIGMS · UNIVERSITY OF DELAWARE · PI MELINDA K DUNCAN · 2012 to 2026
$67.2M
Resource ProjectU41HG002273 · NHGRI · UNIVERSITY OF SOUTHERN CALIFORNIA · PI THOMAS, PAUL D. · 2012 to 2021
$34.7M
UniProt: A centralized protein sequence and function resourceU41HG007822 · NHGRI · EUROPEAN MOLECULAR BIOLOGY LABORATORY · PI BATEMAN, ALEX · 2014 to 2017
$21.9M
PRO: A Protein Ontology in Open Biomedical OntologiesR01GM080646 · NIGMS · UNIVERSITY OF DELAWARE · PI WU, CATHY H. · 2007 to 2018
$8.9M
Semantic Literature Annotation and Integrative Panomics Analysis for PTM-Disease Knowledge Network DiscoveryU01GM120953 · NIGMS · UNIVERSITY OF DELAWARE · PI SHANKER, VIJAY K, WU, CATHY H. · 2016 to 2018
$1.1M
British Heart Foundation RG/13/5/30112NHGRI NIH HHS U41 HG002273NHGRI NIH HHS U41 HG007822NIGMS NIH HHS P20 GM103446NIGMS NIH HHS R01 GM080646NIGMS NIH HHS U01 GM120953Parkinson's UK G-1307
6 · The paper itself

Abstract

Protein kinases form one of the largest protein families and are found in all species, from viruses to humans. They catalyze the reversible phosphorylation of proteins, often modifying their activity and localization. They are implicated in virtually all cellular processes and are one of the most intensively studied protein families. In recent years, they have become key therapeutic targets in drug development as natural mutations affecting kinase genes are the cause of many diseases. The vast amount of data contained in the primary literature and across a variety of biological data collections highlights the need for a repository where this information is stored in a concise and easily accessible manner. The UniProt Knowledgebase meets this need by providing the scientific community with a comprehensive, high-quality and freely accessible resource of protein sequence and functional information. Here, we describe the expert curation process for kinases, focusing on the Caenorhabditis elegans kinome. The C. elegans kinome is composed of 438 kinases and almost half of them have been functionally characterized, highlighting that C. elegans is a valuable and versatile model organism to understand the role of kinases in biological processes.

Indexed as

Databases, ProteinUser-Computer InterfaceAmino Acid SequenceAnimalsCaenorhabditis elegansCaenorhabditis elegans ProteinsCoenzymesGene Expression RegulationGene OntologyHumansInternetMolecular Sequence AnnotationProtein KinasesProteomeProteomicsSignal TransductionCaenorhabditis elegans ProteinsCoenzymesProtein KinasesProteomecurationdatabasekinaseUniProtKB

Identifiers

PMID28159896
PMCPMC5290486
OpenAlexW2584555069

What OpenQuestion holds

Textmetadata
LicenceCC BY-NC-ND
Read underepoch 390

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.