Evidence map›Paper›PMID 28713282›Full record

ArticleFrontiers in physiology2017

The N-Terminal Region of the Ryanodine Receptor Affects Channel Activation.

Andrea Faltinova, Nataša Tomaskova, Marián Antalik, Jozef Sevcik, Alexandra Zahradnikova

Open access · goldAbstract read
In one paragraph

Article in Frontiers in physiology, 2017. 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
0.2field-weighted citation impact, top 44% 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, 6 citations in OpenAlex.

  1. Article
  2. Article
  3. A novel mutation in ryanodine receptor 2 (Frontiers in pediatrics · 2022
    Article
  4. Article
  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

5 authors at 2 institutions in 1 country.

Andrea FaltinovaDepartment of Muscle Cell Research, Institute of Molecular Physiology and Genetics of the Centre of Biosciences, Slovak Academy of SciencesBratislava, Slovakia.
Nataša TomaskovaFaculty of Science, Institute of Chemical Sciences, Pavol Jozef Šafárik UniversityKošice, Slovakia.
Marián AntalikFaculty of Science, Institute of Chemical Sciences, Pavol Jozef Šafárik UniversityKošice, Slovakia.
Jozef SevcikDepartment of Biochemistry and Structural Biology, Institute of Molecular Biology, Slovak Academy of SciencesBratislava, Slovakia.
Alexandra ZahradnikovaDepartment of Muscle Cell Research, Institute of Molecular Physiology and Genetics of the Centre of Biosciences, Slovak Academy of SciencesBratislava, Slovakia.
Slovak Academy of Sciences · SKUniversity of Pavol Jozef Šafárik · SK

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

Mutations in the cardiac ryanodine receptor (RyR2), the ion channel responsible for release of calcium ions from intracellular stores into cytoplasm, are the cause of several inherited cardiac arrhythmias. At the molecular level, disease symptoms can be mimicked by domain peptides from mutation-prone regions of RyR2 that bind to RyR2 and activate it. Here we show that the domain peptide DP

Indexed as

allosteric activationCPVT mutationsdomain peptideplanar lipid bilayerryanodine receptorstructural modeling

Identifiers

PMID28713282
PMCPMC5492033
OpenAlexW2730923464

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.