Evidence map›Paper›PMID 36906144›Full record

ArticleThe Journal of biological chemistry2023

Structures of calmodulin-melittin complexes show multiple binding modes lacking classical anchoring interactions.

Zsolt Dürvanger, Tünde Juhász, Károly Liliom, Veronika Harmat

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

Article in The Journal of biological chemistry, 2023. 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
2.7field-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

5 citing papers in PubMed, 11 citations in OpenAlex.

  1. Review
  2. Calmodulin Interaction Interface with Plasma Membrane CaInternational journal of molecular sciences · 2025
    Article
  3. Article
  4. Review
  5. Review
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

4 authors at 3 institutions in 1 country.

Zsolt DürvangerLaboratory of Structural Chemistry and Biology, Institute of Chemistry, ELTE Eötvös Loránd University, Budapest, Hungary.
Tünde JuhászInstitute of Materials and Environmental Chemistry, Research Centre for Natural Sciences, Budapest, Hungary.
Károly LiliomDepartment of Biophysics and Radiation Biology, Faculty of Medicine, Semmelweis University, Budapest, Hungary.
Veronika HarmatLaboratory of Structural Chemistry and Biology, Institute of Chemistry, ELTE Eötvös Loránd University, Budapest, Hungary; ELKH-ELTE Protein Modelling Research Group, Eötvös Loránd Research Network, Budapest, Hungary. Electronic address: veronika.harmat@ttk.elte.hu.
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) is a Ca

Indexed as

CalmodulinMelittenModels, MolecularAmino Acid SequenceBinding SitesCalciumHumansMolecular Docking SimulationPlasmodium falciparumProtein BindingProtein Structure, QuaternaryCalciumCalmodulinMelittencalmodulin (CaM)crystal structurefuzzy complexlinear motif-binding hub proteinmolecular dynamicsmultiple binding modespolymorphic protein–protein complexprotein complexprotein–protein interaction

Identifiers

PMID36906144
PMCPMC10140167
OpenAlexW4323660270

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.