Evidence map›Paper›PMID 27653478›Full record

ArticleBiophysical journal2016

Cardiac Calcium ATPase Dimerization Measured by Cross-Linking and Fluorescence Energy Transfer.

Daniel J Blackwell, Taylor J Zak, Seth L Robia

Open access · bronzeAbstract read
In one paragraph

Article in Biophysical journal, 2016. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 21 papers.

0numbers the graph read from it
0cells of the map it votes in
21citing papers in PubMed
3.1field-weighted citation impact, top 8% 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

21 citing papers in PubMed, 33 citations in OpenAlex.

  1. Review
  2. Article
  3. P-type ATPase magnesium transporter MgtA acts as a dimer.Nature structural & molecular biology · 2025
    Article
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  13. ANS Interacts with the CaJournal of fluorescence · 2020
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  14. Review
  15. Article
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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 1 institution in 1 country.

Daniel J BlackwellCell and Molecular Physiology, Loyola University Chicago, Chicago, Illinois.
Taylor J ZakCell and Molecular Physiology, Loyola University Chicago, Chicago, Illinois.
Seth L RobiaCell and Molecular Physiology, Loyola University Chicago, Chicago, Illinois. Electronic address: srobia@luc.edu.
Loyola University Chicago · US

Funding

Structural Determinants of Calcium Pump RegulationR01HL092321 · NHLBI · LOYOLA UNIVERSITY CHICAGO · PI Seth L Robia · 2008 to 2026
$8.9M
Structure Changes of Ion-motive ATPasesR01HL106189 · NHLBI · LOYOLA UNIVERSITY CHICAGO · PI ROBIA, SETH L · 2011 to 2014
$1.5M
NHLBI NIH HHS R01 HL092321NHLBI NIH HHS R01 HL106189
6 · The paper itself

Abstract

The cardiac sarco/endoplasmic reticulum calcium ATPase (SERCA) establishes the intracellular calcium gradient across the sarcoplasmic reticulum membrane. It has been proposed that SERCA forms homooligomers that increase the catalytic rate of calcium transport. We investigated SERCA dimerization in rabbit left ventricular myocytes using a photoactivatable cross-linker. Western blotting of cross-linked SERCA revealed higher-molecular-weight species consistent with SERCA oligomerization. Fluorescence resonance energy transfer measurements in cells transiently transfected with fluorescently labeled SERCA2a revealed that SERCA readily forms homodimers. These dimers formed in the absence or presence of the SERCA regulatory partner, phospholamban (PLB) and were unaltered by PLB phosphorylation or changes in calcium or ATP. Fluorescence lifetime data are compatible with a model in which PLB interacts with a SERCA homodimer in a stoichiometry of 1:2. Together, these results suggest that SERCA forms constitutive homodimers in live cells and that dimer formation is not modulated by SERCA conformational poise, PLB binding, or PLB phosphorylation.

Indexed as

Adenosine TriphosphateAnimalsBlotting, WesternCalciumCalcium-Binding ProteinsDogsFluorescence Resonance Energy TransferHeart VentriclesHEK293 CellsHumansImmunoprecipitationLuminescent ProteinsModels, MolecularMuscle CellsMutationPhospholambanAdenosine TriphosphateCalciumCalcium-Binding ProteinsLuminescent ProteinsPhospholambanSarcoplasmic Reticulum Calcium-Transporting ATPases

Identifiers

PMID27653478
PMCPMC5034344
OpenAlexW2522133100

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.