Evidence map›Paper›PMID 25418089›Full record

ArticleBiophysical journal2014

FRET-based trilateration of probes bound within functional ryanodine receptors.

Bengt Svensson, Tetsuro Oda, Florentin R Nitu, Yi Yang, Iustin Cornea, Ye Chen-Izu, James D Fessenden, Donald M Bers, David D Thomas, Razvan L Cornea

Open access · bronzeAbstract readValidation Study
In one paragraph

Article in Biophysical journal, 2014. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 13 papers.

0numbers the graph read from it
0cells of the map it votes in
13citing papers in PubMed
1.4field-weighted citation impact, top 19% 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

13 citing papers in PubMed, 19 citations in OpenAlex.

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4 · The record

Corrections and comments

5 · Who and what money

Authors and funding

10 authors at 3 institutions in 1 country.

Bengt SvenssonDepartment of Biochemistry, Molecular Biology and Biophysics, University of Minnesota, Minneapolis, Minnesota.
Tetsuro OdaDepartment of Pharmacology, University of California, Davis, California.
Florentin R NituDepartment of Biochemistry, Molecular Biology and Biophysics, University of Minnesota, Minneapolis, Minnesota.
Yi YangDepartment of Pharmacology, University of California, Davis, California.
Iustin CorneaDepartment of Biochemistry, Molecular Biology and Biophysics, University of Minnesota, Minneapolis, Minnesota.
Ye Chen-IzuDepartment of Pharmacology, University of California, Davis, California.
James D FessendenDepartment of Anesthesia, Perioperative and Pain Medicine, Brigham and Women's Hospital, Boston, Massachusetts.
Donald M BersDepartment of Pharmacology, University of California, Davis, California.
David D ThomasDepartment of Biochemistry, Molecular Biology and Biophysics, University of Minnesota, Minneapolis, Minnesota.
Razvan L CorneaDepartment of Biochemistry, Molecular Biology and Biophysics, University of Minnesota, Minneapolis, Minnesota. Electronic address: corne002@umn.edu.
University of Minnesota · USUniversity of California, Davis · USBrigham and Women's Hospital · 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
Site-Directed Oxidative Modification of Muscle Protein Structural DynamicsR37AG026160 · NIA · UNIVERSITY OF MINNESOTA · PI THOMAS, DAVID D · 2011 to 2020
$4.5M
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 R01AR059124NIAMS NIH HHS T32 AR007612NIA NIH HHS R37 AG026160NIA NIH HHS R37AG26160NIGMS NIH HHS R01 GM027906NIGMS NIH HHS R01GM27906
6 · The paper itself

Abstract

To locate the biosensor peptide DPc10 bound to ryanodine receptor (RyR) Ca(2+) channels, we developed an approach that combines fluorescence resonance energy transfer (FRET), simulated-annealing, cryo-electron microscopy, and crystallographic data. DPc10 is identical to the 2460-2495 segment within the cardiac muscle RyR isoform (RyR2) central domain. DPc10 binding to RyR2 results in a pathologically elevated Ca(2+) leak by destabilizing key interactions between the RyR2 N-terminal and central domains (unzipping). To localize the DPc10 binding site within RyR2, we measured FRET between five single-cysteine variants of the FK506-binding protein (FKBP) labeled with a donor probe, and DPc10 labeled with an acceptor probe (A-DPc10). Effective donor positions were calculated from simulated-annealing constrained by both the RyR cryo-EM map and the FKBP atomic structure docked to the RyR. FRET to A-DPc10 was measured in permeabilized cardiomyocytes via confocal microscopy, converted to distances, and used to trilaterate the acceptor locus within RyR. Additional FRET measurements between donor-labeled calmodulin and A-DPc10 were used to constrain the trilaterations. Results locate the DPc10 probe within RyR domain 3, ?35 Å from the previously docked N-terminal domain crystal structure. This multiscale approach may be useful in mapping other RyR sites of mechanistic interest within FRET range of FKBP.

Indexed as

Binding SitesCalmodulinComputer SimulationCryoelectron MicroscopyCrystallographyFluorescence Resonance Energy TransferHEK293 CellsHumansMicroscopy, ConfocalMolecular StructureMyocytes, CardiacPeptide FragmentsProtein BindingProtein Structure, SecondaryRyanodine Receptor Calcium Release ChannelTacrolimus Binding ProteinsCalmodulinPeptide FragmentsRyanodine Receptor Calcium Release Channelryanodine receptor calcium release channel (2460-2495), synthetictacrolimus binding protein 1BTacrolimus Binding Proteins

Identifiers

PMID25418089
PMCPMC4223179
OpenAlexW2098911738

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.