Evidence map›Paper›PMID 32821880›Full record

ArticleFASEB bioAdvances2020

Comparison of ligand binding and conformational stability of human calmodulin with its homolog from the malaria parasite

Tünde Juhász, József Kardos, Zsolt Dürvanger, Veronika Harmat, Károly Liliom

Open access · goldAbstract read
In one paragraph

Article in FASEB bioAdvances, 2020. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 4 papers.

0numbers the graph read from it
0cells of the map it votes in
4citing papers in PubMed
1.3field-weighted citation impact, top 18% 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

4 citing papers in PubMed, 8 citations in OpenAlex.

  1. Article
  2. Bisindolylmaleimides New Ligands of CaM Protein.Molecules (Basel, Switzerland) · 2022
    Article
  3. Article
  4. 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

5 authors at 3 institutions in 1 country.

Tünde JuhászInstitute of Materials and Environmental Chemistry Research Centre for Natural Sciences Budapest Hungary.
József KardosDepartment of Biochemistry Institute of Biology ELTE Eötvös Loránd University Budapest Hungary.
Zsolt DürvangerLaboratory of Structural Chemistry and Biology Institute of Chemistry Eötvös Loránd University Budapest Hungary.
Veronika HarmatLaboratory of Structural Chemistry and Biology Institute of Chemistry Eötvös Loránd University Budapest Hungary.
Károly LiliomDepartment of Biophysics and Radiation Biology Faculty of Medicine Semmelweis University Budapest Hungary.
Eötvös Loránd University · HUInstitute of Materials and Environmental Chemistry · HUSemmelweis University · HU

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

Calmodulin (CaM), the key calcium sensor of eukaryotic cells regulating a great number of target proteins, belongs to the most conserved proteins. We compared function and properties of CaMs from two evolutionarily distant species, the human (

Indexed as

binding affinityinhibitor developmentprotein stabilityprotein structuretarget activation

Identifiers

PMID32821880
PMCPMC7429351
OpenAlexW3036217678

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.