Evidence map›Paper›PMID 28939764›Full record

ArticleThe Journal of biological chemistry2017

Early emergence of negative regulation of the tyrosine kinase Src by the C-terminal Src kinase.

Barbara Taskinen, Evandro Ferrada, Douglas M Fowler

Open access · hybridAbstract readComparative Study
In one paragraph

Article in The Journal of biological chemistry, 2017. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 5 papers.

0numbers the graph read from it
0cells of the map it votes in
5citing papers in PubMed
0.4field-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

5 citing papers in PubMed, 7 citations in OpenAlex.

  1. Review
  2. Article
  3. The Src module: an ancient scaffold in the evolution of cytoplasmic tyrosine kinases.Critical reviews in biochemistry and molecular biology · 2018
    Review
  4. Phosphorylation control of the ubiquitin ligase Cbl is conserved in choanoflagellates.Protein science : a publication of the Protein Society · 2018
    Article
  5. 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

3 authors at 1 institution in 1 country.

Barbara TaskinenFrom the Department of Genome Sciences, University of Washington, Seattle, Washington 98195-5065 and.ORCID 0000-0003-2989-7563
Evandro FerradaFrom the Department of Genome Sciences, University of Washington, Seattle, Washington 98195-5065 and.
Douglas M FowlerFrom the Department of Genome Sciences, University of Washington, Seattle, Washington 98195-5065 and dfowler@uw.edu.ORCID 0000-0001-7614-1713
University of Washington · US

Funding

Large-Scale Methods for Assessing the Consequences of Mutations in ProteinsR01GM109110 · NIGMS · UNIVERSITY OF WASHINGTON · PI FOWLER, DOUGLAS M · 2014 to 2021
$2.4M
NIGMS NIH HHS R01 GM109110
6 · The paper itself

Abstract

Stringent regulation of tyrosine kinase activity is essential for normal cellular function. In humans, the tyrosine kinase Src is inhibited via phosphorylation of its C-terminal tail by another kinase, C-terminal Src kinase (Csk). Although Src and Csk orthologs are present across holozoan organisms, including animals and protists, the Csk-Src negative regulatory mechanism appears to have evolved gradually. For example, in choanoflagellates, Src and Csk are both active, but the negative regulatory mechanism is reportedly absent. In filastereans, a protist clade closely related to choanoflagellates, Src is active, but Csk is apparently inactive. In this study, we use a combination of bioinformatics,

Indexed as

Amino Acid SequenceAmino Acid SubstitutionAquatic OrganismsChoanoflagellataComputational BiologyConserved SequenceCSK Tyrosine-Protein KinaseKineticsMutationPhylogenyProtein Interaction Domains and MotifsProtozoan ProteinsRecombinant ProteinsSequence AlignmentSequence Homology, Amino AcidSpecies SpecificityCSK protein, humanCSK Tyrosine-Protein KinaseProtozoan ProteinsRecombinant Proteinssrc-Family Kinasesinhibition mechanismmolecular biologynon-receptor tyrosine kinase (nRTK)protein evolutionprotein phosphorylation

Identifiers

PMID28939764
PMCPMC5682962
OpenAlexW2757122057

What OpenQuestion holds

Textmetadata
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.