Evidence map›Paper›PMID 27956550›Full record

ArticleThe Journal of biological chemistry2017

Signal Integration at Elongation Factor 2 Kinase: THE ROLES OF CALCIUM, CALMODULIN, AND SER-500 PHOSPHORYLATION.

Clint D J Tavares, David H Giles, Gabriel Stancu, Catrina A Chitjian, Scarlett B Ferguson, Rebecca M Wellmann, Tamer S Kaoud, Ranajeet Ghose, Kevin N Dalby

Open access · hybridAbstract read
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 11 papers.

0numbers the graph read from it
0cells of the map it votes in
11citing papers in PubMed
0.7field-weighted citation impact, top 25% 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

11 citing papers in PubMed, 20 citations in OpenAlex.

  1. Review
  2. Review
  3. ADP enhances the allosteric activation of eukaryotic elongation factor 2 kinase by calmodulin.Proceedings of the National Academy of Sciences of the United States of America · 2023
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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

9 authors at 2 institutions in 1 country.

Clint D J TavaresFrom the Graduate Program in Cell and Molecular Biology, University of Texas, Austin, Texas 78712; Division of Chemical Biology and Medicinal Chemistry, University of Texas, Austin, Texas 78712. Electronic address: clinttavares@utexas.edu.
David H GilesDivision of Chemical Biology and Medicinal Chemistry, University of Texas, Austin, Texas 78712.
Gabriel StancuDivision of Chemical Biology and Medicinal Chemistry, University of Texas, Austin, Texas 78712.
Catrina A ChitjianFrom the Graduate Program in Cell and Molecular Biology, University of Texas, Austin, Texas 78712; Division of Chemical Biology and Medicinal Chemistry, University of Texas, Austin, Texas 78712.
Scarlett B FergusonDivision of Chemical Biology and Medicinal Chemistry, University of Texas, Austin, Texas 78712.
Rebecca M WellmannDivision of Chemical Biology and Medicinal Chemistry, University of Texas, Austin, Texas 78712.
Tamer S KaoudDivision of Chemical Biology and Medicinal Chemistry, University of Texas, Austin, Texas 78712.
Ranajeet Ghosethe Department of Chemistry, City College of New York, New York, New York 10031; the Graduate Center, City University of New York, New York, New York 10016.
Kevin N DalbyFrom the Graduate Program in Cell and Molecular Biology, University of Texas, Austin, Texas 78712; Division of Chemical Biology and Medicinal Chemistry, University of Texas, Austin, Texas 78712. Electronic address: dalby@austin.utexas.edu.
The University of Texas at Austin · USCity University of New York · US

Funding

Mechanism and Specificity of MAP KinasesR01GM059802 · NIGMS · UNIVERSITY OF TEXAS AUSTIN · PI DALBY, KEVIN N · 2001 to 2011
$2.3M
NIGMS NIH HHS R01 GM059802
6 · The paper itself

Abstract

Eukaryotic elongation factor 2 kinase (eEF-2K), the only calmodulin (CaM)-dependent member of the unique α-kinase family, impedes protein synthesis by phosphorylating eEF-2. We recently identified Thr-348 and Ser-500 as two key autophosphorylation sites within eEF-2K that regulate its activity. eEF-2K is regulated by Ca

Indexed as

Amino Acid SubstitutionCalciumCalmodulinCell Line, TumorElongation Factor 2 KinaseHumansMutation, MissensePhosphorylationSerineCalciumCalmodulinEEF2K protein, humanElongation Factor 2 KinaseSerinecalciumcalmodulin (CaM)CaMK-IIIeEF-2KphosphorylationS500DSer-500Thr-348translationtranslation elongation factor

Identifiers

PMID27956550
PMCPMC5290972
OpenAlexW2563920410

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.