Evidence map›Paper›PMID 26781665›Full record

ArticleJournal of molecular modeling2016

Interaction of ions with the luminal sides of wild-type and mutated skeletal muscle ryanodine receptors.

Roman Schilling, Rainer H A Fink, Wolfgang B Fischer

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Article in Journal of molecular modeling, 2016. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 3 papers.

0numbers the graph read from it
0cells of the map it votes in
3citing papers in PubMed
0.2field-weighted citation impact, top 37% 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

3 citing papers in PubMed, 5 citations in OpenAlex.

  1. Review
  2. Review
  3. 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

3 authors at 2 institutions in 2 countries.

Roman SchillingMedical Biophysics Group, Institute of Physiology and Pathophysiology, University of Heidelberg, 69120, Heidelberg, Germany.
Rainer H A FinkMedical Biophysics Group, Institute of Physiology and Pathophysiology, University of Heidelberg, 69120, Heidelberg, Germany.
Wolfgang B FischerInstitute of Biophotonics, School of Biomedical Science and Engineering, National Yang-Ming University, 155, Li-Non St., Sec. 2, Taipei, 112, Taiwan. wfischer@ym.edu.tw.
Heidelberg University · DENational Yang Ming Chiao Tung University · TW

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

Ryanodine receptors (RyRs) are the largest known ion channels, and are of central importance for the release of Ca(2+) from the sarco/endoplasmic reticulum (SR/ER) in a variety of cells. In cardiac and skeletal muscle cells, contraction is triggered by the release of Ca(2+) into the cytoplasm and thus depends crucially on correct RyR function. In this work, in silico mutants of the RyR pore were generated and MD simulations were conducted to examine the impact of the mutations on the Ca(2+) distribution. The Ca(2+) distribution pattern on the luminal side of the RyR was most affected by G4898R, D4899Q, E4900Q, R4913E, and D4917A mutations. MD simulations with our wild-type model and various ion species showed a preference for Ca(2+) over other cations at the luminal pore entrance. This Ca(2+)-accumulating characteristic of the luminal RyR side may be essential to the conductance properties of the channel.

Indexed as

CalciumComputer SimulationMuscle, SkeletalMutation, MissenseRyanodine Receptor Calcium Release ChannelAmino Acid SubstitutionHumansCalciumRyanodine Receptor Calcium Release ChannelCalciumIon channelIon dynamicsMolecular dynamics simulationsRyR1

Identifiers

PMID26781665
OpenAlexW2280850576

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.