Evidence map›Paper›PMID 28445755›Full record

ArticleBiophysical journal2017

Mapping Ryanodine Binding Sites in the Pore Cavity of Ryanodine Receptors.

Van A Ngo, Laura L Perissinotti, Williams Miranda, S R Wayne Chen, Sergei Y Noskov

Open access · bronzeAbstract read
In one paragraph

Article in Biophysical journal, 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
0.9field-weighted citation impact, top 27% 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, 10 citations in OpenAlex.

  1. Trial
  2. Article
  3. 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 1 institution in 1 country.

Van A NgoCenter for Molecular Simulations, Department of Biological Sciences, University of Calgary, Calgary, Alberta, Canada.
Laura L PerissinottiCenter for Molecular Simulations, Department of Biological Sciences, University of Calgary, Calgary, Alberta, Canada.
Williams MirandaCenter for Molecular Simulations, Department of Biological Sciences, University of Calgary, Calgary, Alberta, Canada.
S R Wayne ChenLibin Cardiovascular Institute of Alberta, Department of Physiology and Pharmacology, University of Calgary, Calgary, Alberta, Canada.
Sergei Y NoskovCenter for Molecular Simulations, Department of Biological Sciences, University of Calgary, Calgary, Alberta, Canada. Electronic address: snoskov@ucalgary.ca.
University of Calgary · CA

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

Ryanodine (Ryd) irreversibly targets ryanodine receptors (RyRs), a family of intracellular calcium release channels essential for many cellular processes ranging from muscle contraction to learning and memory. Little is known of the atomistic details about how Ryd binds to RyRs. In this study, we used all-atom molecular dynamics simulations with both enhanced and bidirectional sampling to gain direct insights into how Ryd interacts with major residues in RyRs that were experimentally determined to be critical for its binding. We found that the pyrrolic ring of Ryd displays preference for the R

Indexed as

AnimalsBinding SitesMolecular Docking SimulationMolecular Dynamics SimulationMutationProtein Structure, SecondaryRyanodineRyanodine Receptor Calcium Release ChannelThermodynamicsWaterRyanodineRyanodine Receptor Calcium Release ChannelWater

Identifiers

PMID28445755
PMCPMC5406381
OpenAlexW2608751136

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.