Evidence map›Paper›PMID 15908964›Full record

ArticleNature structural & molecular biology2005

Internal structure and visualization of transmembrane domains of the RyR1 calcium release channel by cryo-EM.

Montserrat Samsó, Terence Wagenknecht, P D Allen

Open access · greenAbstract read
In one paragraph

Article in Nature structural & molecular biology, 2005. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 97 papers, 1 of them a synthesis that pooled it.

0numbers the graph read from it
0cells of the map it votes in
97citing papers in PubMed, 1 pooled it
5.5field-weighted citation impact, top 3% 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

97 citing papers in PubMed, 1 synthesis or guideline pooled it, 186 citations in OpenAlex.

  1. Calcium and arrhythmogenesis.Physiological reviews · 2007
    Pooled it
  2. Article
  3. Review
  4. Article
  5. Review
  6. Article
  7. Article
  8. Article
  9. Review
  10. Review
  11. Structural and functional interactions between the CaThe Journal of biological chemistry · 2021
    Article
  12. Article
  13. Regulatory mechanisms of ryanodine receptor/CaJournal of muscle research and cell motility · 2021
    Review
  14. Article
  15. Review
  16. Article
  17. A central core disease mutation in the CaAmerican journal of physiology. Cell physiology · 2019
    Article
  18. Article
  19. Article
  20. Review

37 more citing papers are in PubMed but not listed here.

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 3 institutions in 1 country.

Montserrat SamsóBrigham and Women's Hospital, Harvard Medical School, Boston, Massachusetts 02115, USA. msamso@zeus.bwh.harvard.edu
Terence Wagenknecht
P D Allen
Brigham and Women's Hospital · USHarvard University · USNew York State Department of Health · US

Funding

Single particle reconstructionP01GM062580 · NIGMS · HARVARD MEDICAL SCHOOL · PI HARRISON, STEPHEN COPLAN · 2001 to 2016
$23.7M
ZERNIKE PHASE-CONTRAST IMAGINGP41RR001219 · NCRR · WADSWORTH CENTER · PI WAGENKNECHT, TERENCE C · 1985 to 2010
$11.1M
STRUCTURE OF CHANNELS IN EXCITATION/CONTRACTION COUPLINGR01AR040615 · NIAMS · WADSWORTH CENTER · PI WAGENKNECHT, TERENCE C · 1991 to 2014
$5.6M
Structure Function Studies of RyR1 in a Myogenic KnockoutR01AR043140 · NIAMS · CHILDREN'S HOSPITAL BOSTON · PI ALLEN, PAUL D · 1996 to 2010
$4.8M
NCRR NIH HHS P41 RR001219NCRR NIH HHS RR01219NIAMS NIH HHS AR40615NIAMS NIH HHS P01 AR17605NIAMS NIH HHS R01 AR040615NIAMS NIH HHS R01 AR043140NIAMS NIH HHS R01 AR43140NIGMS NIH HHS GM62580
6 · The paper itself

Abstract

RyR1 is an intracellular calcium channel with a central role in muscle contraction. We obtained a three-dimensional reconstruction of the RyR1 in the closed state at a nominal resolution of approximately 10 A using cryo-EM. The cytoplasmic assembly consists of a series of interconnected tubular structures that merge into four columns that extend into the transmembrane assembly. The transmembrane assembly, which has at least six transmembrane alpha-helices per monomer, has four tilted rods that can be fitted with the inner helices of a closed K(+) channel atomic structure. The rods splay out at the lumenal side and converge into a dense ring at the cytoplasmic side. Another set of four rods emerges from this ring and shapes the inner part of the four columns. The resulting constricted axial structure provides direct continuity between cytoplasmic and transmembrane assemblies, and a possible mechanism for control of channel gating through conformational changes in the cytoplasmic assembly.

Indexed as

AnimalsCell MembraneCryoelectron MicroscopyImage Processing, Computer-AssistedModels, MolecularMuscle, SkeletalProtein ConformationRabbitsRyanodine Receptor Calcium Release ChannelSensitivity and SpecificityRyanodine Receptor Calcium Release Channel

Identifiers

PMID15908964
PMCPMC1925259
OpenAlexW2044219698

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.