Evidence map›Paper›PMID 25830911›Full record

ArticlePloS one2015

Characterization of phospho-(tyrosine)-mimetic calmodulin mutants.

Silviya R Stateva, Valentina Salas, Gustavo Benaim, Margarita Menéndez, Dolores Solís, Antonio Villalobo

Open access · goldAbstract read
In one paragraph

Article in PloS one, 2015. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 18 papers.

0numbers the graph read from it
0cells of the map it votes in
18citing papers in PubMed
2.4field-weighted citation impact, top 11% 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

18 citing papers in PubMed, 31 citations in OpenAlex.

  1. Article
  2. Article
  3. Article
  4. CaBiomolecules · 2023
    Review
  5. Article
  6. Article
  7. Article
  8. Article
  9. Article
  10. Review
  11. Review
  12. Article
  13. Article
  14. Article
  15. Calmodulin and PI3K Signaling inTrends in cancer · 2017
    Review
  16. Review
  17. Article
  18. 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

6 authors at 4 institutions in 2 countries.

Silviya R StatevaInstituto de Investigaciones Biomédicas, Consejo Superior de Investigaciones Científicas and Universidad Autónoma de Madrid, Madrid, Spain.
Valentina SalasInstituto de Investigaciones Biomédicas, Consejo Superior de Investigaciones Científicas and Universidad Autónoma de Madrid, Madrid, Spain; Universidad Central de Venezuela, Facultad de Ciencias, Instituto de Biología Experimental, Caracas, Venezuela.
Gustavo BenaimUniversidad Central de Venezuela, Facultad de Ciencias, Instituto de Biología Experimental, Caracas, Venezuela; Instituto de Estudios Avanzados (IDEA), Caracas, Venezuela.
Margarita MenéndezInstituto de Química Física Rocasolano, Consejo Superior de Investigaciones Científicas, Madrid, Spain.
Dolores SolísInstituto de Química Física Rocasolano, Consejo Superior de Investigaciones Científicas, Madrid, Spain.
Antonio VillaloboInstituto de Investigaciones Biomédicas, Consejo Superior de Investigaciones Científicas and Universidad Autónoma de Madrid, Madrid, Spain.
Consejo Superior de Investigaciones Científicas · ESUniversidad Autónoma de Madrid · ESInstituto de Estudios Avanzados · VEInstituto de Química Física Blas Cabrera · ES

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

Calmodulin (CaM) phosphorylated at different serine/threonine and tyrosine residues is known to exert differential regulatory effects on a variety of CaM-binding enzymes as compared to non-phosphorylated CaM. In this report we describe the preparation and characterization of a series of phospho-(Y)-mimetic CaM mutants in which either one or the two tyrosine residues present in CaM (Y99 and Y138) were substituted to aspartic acid or glutamic acid. It was expected that the negative charge of the respective carboxyl group of these amino acids mimics the negative charge of phosphate and reproduce the effects that distinct phospho-(Y)-CaM species may have on target proteins. We describe some physicochemical properties of these CaM mutants as compared to wild type CaM, after their expression in Escherichia coli and purification to homogeneity, including: i) changes in their electrophoretic mobility in the absence and presence of Ca2+; ii) ultraviolet (UV) light absorption spectra, far- and near-UV circular dichroism data; iii) thermal stability in the absence and presence of Ca2+; and iv) Tb3+-emitted fluorescence upon tyrosine excitation. We also describe some biochemical properties of these CaM mutants, such as their differential phosphorylation by the tyrosine kinase c-Src, and their action as compared to wild type CaM, on the activity of two CaM-dependent enzymes: cyclic nucleotide phosphodiesterase 1 (PDE1) and endothelial nitric oxide synthase (eNOS) assayed in vitro.

Indexed as

MutationAmino Acid SubstitutionAnimalsCalmodulinCattleChemical PhenomenaCyclic Nucleotide Phosphodiesterases, Type 1Nitric Oxide Synthase Type IIIPhosphotyrosineProtein StabilityRatsTemperatureCalmodulinCyclic Nucleotide Phosphodiesterases, Type 1Nitric Oxide Synthase Type IIIPhosphotyrosine

Identifiers

PMID25830911
PMCPMC4382182
OpenAlexW2115290861

What OpenQuestion holds

Textmetadata
LicenceCC BY
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.