Evidence map›Paper›PMID 24139989›Full record

ArticleStructure (London, England : 1993)2013

Conformational dynamics inside amino-terminal disease hotspot of ryanodine receptor.

Xiaowei Zhong, Ying Liu, Li Zhu, Xing Meng, Ruiwu Wang, Filip Van Petegem, Terence Wagenknecht, S R Wayne Chen, Zheng Liu

Abstract read
In one paragraph

Article in Structure (London, England : 1993), 2013. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 14 papers.

0numbers the graph read from it
0cells of the map it votes in
14citing papers in PubMed
–field-weighted citation impact
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

14 citing papers in PubMed.

  1. Article
  2. Review
  3. Article
  4. Article
  5. Article
  6. Review
  7. Article
  8. A guide to the 3D structure of the ryanodine receptor type 1 by cryoEM.Protein science : a publication of the Protein Society · 2017
    Review
  9. Structures of the colossal RyR1 calcium release channel.Current opinion in structural biology · 2016
    Review
  10. Article
  11. Review
  12. Article
  13. Article
  14. 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

9 authors.

Xiaowei ZhongDepartment of Physiology and Pharmacology, University of Calgary, Calgary, AB T2N 4N1, Canada; Department of Biochemistry and Molecular Biology, University of Calgary, Calgary, AB T2N 4N1, Canada.
Ying Liu
Li Zhu
Xing Meng
Ruiwu Wang
Filip Van Petegem
Terence Wagenknecht
S R Wayne Chen
Zheng Liu

Funding

STRUCTURE OF CHANNELS IN EXCITATION/CONTRACTION COUPLINGR01AR040615 · NIAMS · WADSWORTH CENTER · PI WAGENKNECHT, TERENCE C · 1991 to 2014
$5.6M
Molecular Basis of Cardiac Arrhythmia and Sudden DeathR01HL075210 · NHLBI · UNIVERSITY OF CALGARY · PI CHEN, SUI RONG WAYNE · 2005 to 2013
$2.6M
Structural Basis of Dysfunctional Calcium Release Channels in Heart DiseaseR01HL095541 · NHLBI · WADSWORTH CENTER · PI LIU, ZHENG · 2010 to 2013
$1.5M
CIHRNHLBI NIH HHS R01 HL075210NHLBI NIH HHS R01HL075210NHLBI NIH HHS R01 HL095541NHLBI NIH HHS R01HL095541NIAMS NIH HHS R01 AR040615NIAMS NIH HHS R01AR040615
6 · The paper itself

Abstract

The N-terminal region of both skeletal and cardiac ryanodine receptor is a disease mutation hotspot. Recently, a crystal structure of the RyR1 fragment (residues 1-559) was solved. This N-terminal structure contains three separate domains, A, B, and C, and was docked into a central vestibule in a full-length RyR1 cryo-EM map. Here, we reconstructed three-dimensional cryo-EM structures of two GFP-tagged RyR2s with GFP inserted after residue Glu-310 and Ser-437, respectively. The structures of RyR2E310-GFP and RyR2S437-GFP displayed an extra mass on domain B and C, directly validating the predicted docking model. Next, we revealed domain movements in molecular dynamics flexible fitting models in both the closed and open state cryo-EM maps. To further probe the conformational changes, we generated FRET pairs by inserting CFP or YFP in two selected domains, FRET studies of three dual-insertion pairs and three co-expressed single-insertion pairs showed the dynamic structural changes within the N-terminal domains.

Indexed as

AnimalsBacterial ProteinsCaffeineCryoelectron MicroscopyFluorescence Resonance Energy TransferGreen Fluorescent ProteinsHEK293 CellsHumansLuminescent ProteinsMiceMolecular Docking SimulationProtein BindingProtein Interaction Domains and MotifsProtein Structure, SecondaryRecombinant Fusion ProteinsRyanodine Receptor Calcium Release ChannelBacterial ProteinsCaffeineCyan Fluorescent ProteinGreen Fluorescent ProteinsLuminescent ProteinsRecombinant Fusion ProteinsRyanodine Receptor Calcium Release Channelyellow fluorescent protein, Bacteria

Identifiers

PMID24139989
PMCPMC3826818

What OpenQuestion holds

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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.