Evidence map›Paper›PMID 25132084›Full record

ArticleStructure (London, England : 1993)2014

Structural mapping of divergent regions in the type 1 ryanodine receptor using fluorescence resonance energy transfer.

Mohana Mahalingam, Tanya Girgenrath, Bengt Svensson, David D Thomas, Razvan L Cornea, James D Fessenden

Open access · bronzeAbstract read
In one paragraph

Article in Structure (London, England : 1993), 2014. 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
0.6field-weighted citation impact, top 32% 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, 11 citations in OpenAlex.

  1. Article
  2. Article
  3. Article
  4. Article
  5. 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

6 authors at 2 institutions in 1 country.

Mohana MahalingamDepartment of Anesthesia, Perioperative and Pain Medicine, Brigham and Women's Hospital, Boston, MA 02115, USA.
Tanya GirgenrathDepartment of Anesthesia, Perioperative and Pain Medicine, Brigham and Women's Hospital, Boston, MA 02115, USA.
Bengt SvenssonDepartment of Biochemistry, Molecular Biology and Biophysics, University of Minnesota, Minneapolis, MN 55455, USA.
David D ThomasDepartment of Biochemistry, Molecular Biology and Biophysics, University of Minnesota, Minneapolis, MN 55455, USA.
Razvan L CorneaDepartment of Biochemistry, Molecular Biology and Biophysics, University of Minnesota, Minneapolis, MN 55455, USA.
James D FessendenDepartment of Anesthesia, Perioperative and Pain Medicine, Brigham and Women's Hospital, Boston, MA 02115, USA. Electronic address: jfessenden@partners.org.
Brigham and Women's Hospital · USUniversity of Minnesota · US

Funding

TRAINING PROGRAM IN MUSCLE RESEARCHT32AR007612 · NIAMS · UNIVERSITY OF MINNESOTA TWIN CITIES · PI JAMES M ERVASTI, DAWN A LOWE · 2001 to 2026
$11.3M
Pathophysiological Regulation of Cardiac Myocyte RyR ChannelR01HL092097 · NHLBI · UNIVERSITY OF CALIFORNIA AT DAVIS · PI Donald M Bers, Robyn T Rebbeck · 2010 to 2026
$9.3M
Structural Dynamics of Muscle Calcium ATPase RegulationR01GM027906 · NIGMS · UNIVERSITY OF MINNESOTA TWIN CITIES · PI THOMAS, DAVID D · 1985 to 2016
$8.6M
Mechanisms of Innate and Acquired Host Defense and Tissue Injury in SkinR01AR059126 · NIAMS · UNIVERSITY OF CALIFORNIA LOS ANGELES · PI LEE, DELPHINE J · 2010 to 2014
$1.9M
Conformational measurements of RyR1 using a site-specific labeling methodR01AR059124 · NIAMS · BRIGHAM AND WOMEN'S HOSPITAL · PI FESSENDEN, JAMES D · 2011 to 2015
$1.8M
NHLBI NIH HHS R01 HL092097NHLBI NIH HHS R01HL092097NIAMS NIH HHS R01 AR059124NIAMS NIH HHS R01 AR059126NIAMS NIH HHS R01AR059126NIAMS NIH HHS T32 AR007612NIGMS NIH HHS R01 GM027906NIGMS NIH HHS R01GM027906
6 · The paper itself

Abstract

Ryanodine receptors (RyRs) release Ca(2+) to initiate striated muscle contraction. Three highly divergent regions (DRs) in the RyR protein sequence (DR1, DR2, and DR3) may confer isoform-specific functional properties to the RyRs. We used cell-based fluorescence resonance energy transfer (FRET) measurements to localize these DRs to the cryoelectron microscopic (cryo-EM) map of the skeletal muscle RyR isoform (RyR1). FRET donors were targeted to RyR1 using five different FKBP12.6 variants labeled with Alexa Fluor 488. FRET was then measured to the FRET acceptors, Cy3NTA or Cy5NTA, targeted to decahistidine tags introduced within the DRs. DR2 and DR3 were localized to separate positions within the "clamp" region of the RyR1 cryo-EM map, which is presumed to interface with Cav1.1. DR1 was localized to the "handle" region, near the regulatory calmodulin-binding site on the RyR. These localizations provide insights into the roles of DRs in RyR allosteric regulation during excitation contraction coupling.

Indexed as

Allosteric RegulationAnimalsBinding SitesCaffeineExcitation Contraction CouplingFluorescence Resonance Energy TransferHEK293 CellsHumansModels, MolecularProtein BindingRabbitsRyanodine Receptor Calcium Release ChannelTacrolimus Binding ProteinsCaffeineRyanodine Receptor Calcium Release ChannelTacrolimus Binding Proteins

Identifiers

PMID25132084
PMCPMC4156536
OpenAlexW2142255504

What OpenQuestion holds

Textmetadata
LicenceTDM
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.