Evidence map›Paper›PMID 33890716›Full record

ArticleProtein science : a publication of the Protein Society2021

Structural dynamics of the complex of calmodulin with a minimal functional construct of eukaryotic elongation factor 2 kinase and the role of Thr348 autophosphorylation.

Andrea Piserchio, Kimberly Long, Kwangwoon Lee, Eric A Kumar, Rinat Abzalimov, Kevin N Dalby, Ranajeet Ghose

Open access · bronzeAbstract read
PubMed Full text at PMC Publisher
In one paragraph

Article in Protein science : a publication of the Protein Society, 2021. 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
0.8field-weighted citation impact, top 30% 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, 15 citations in OpenAlex.

  1. Article
  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
    Article
  4. Review
  5. Article
  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

7 authors at 3 institutions in 1 country.

Andrea PiserchioDepartment of Chemistry and Biochemistry, The City College of New York, New York, New York, USA.
Kimberly LongDivision of Chemical Biology and Medicinal Chemistry, University of Texas, Austin, Texas, USA.
Kwangwoon LeeDepartment of Chemistry and Biochemistry, The City College of New York, New York, New York, USA.
Eric A KumarDivision of Chemical Biology and Medicinal Chemistry, University of Texas, Austin, Texas, USA.
Rinat AbzalimovBiomolecular Mass Spectrometry Facility, CUNY ASRC, New York, New York, USA.
Kevin N DalbyDivision of Chemical Biology and Medicinal Chemistry, University of Texas, Austin, Texas, USA.
Ranajeet GhoseDepartment of Chemistry and Biochemistry, The City College of New York, New York, New York, USA.ORCID 0000-0002-0763-8686
The Graduate Center, CUNY · USThe University of Texas at Austin · USCity College of New York · US

Funding

Regulation of eEF-2K an Energy and Nutrient SensorR01GM123252 · NIGMS · UNIVERSITY OF TEXAS AT AUSTIN · PI DALBY, KEVIN N, GHOSE, RANAJEET · 2017 to 2024
$2.7M
NIGMS NIH HHS R01 GM123252
6 · The paper itself

Abstract

The calmodulin (CaM) activated α-kinase, eukaryotic elongation factor 2 kinase (eEF-2K), plays a central role in regulating translational elongation by phosphorylating eukaryotic elongation factor 2 (eEF-2), thereby reducing its ability to associate with the ribosome and suppressing global protein synthesis. Using TR (for truncated), a minimal functional construct of eEF-2K, and utilizing hydrogen/deuterium exchange mass spectrometry (HXMS), solution-state nuclear magnetic resonance (NMR) and biochemical approaches, we investigate the conformational changes accompanying complex formation between Ca

Indexed as

Nuclear Magnetic Resonance, BiomolecularAmino Acid SubstitutionCalmodulinElongation Factor 2 KinaseHumansMutation, MissensePhosphorylationProtein Structure, QuaternaryProtein Structure, SecondaryCalmodulinEEF2K protein, humanElongation Factor 2 Kinasealpha kinasecalmodulinhydrogen exchange mass spectrometrysolution NMRtranslational elongation

Identifiers

PMID33890716
PMCPMC8138526
OpenAlexW3152942683

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.