Evidence map›Paper›PMID 22247554›Full record

ArticleThe Journal of biological chemistry2012

Characterizing phospholamban to sarco(endo)plasmic reticulum Ca2+-ATPase 2a (SERCA2a) protein binding interactions in human cardiac sarcoplasmic reticulum vesicles using chemical cross-linking.

Brandy L Akin, Larry R Jones

Erratum issuedOpen access · hybridAbstract read
In one paragraph

Article in The Journal of biological chemistry, 2012. The graph could read no effect estimate from its abstract, so it casts no vote on the map. An erratum has been issued. Cited by 17 papers.

0numbers the graph read from it
0cells of the map it votes in
17citing papers in PubMed
2.8field-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

17 citing papers in PubMed, 34 citations in OpenAlex.

  1. Article
  2. Article
  3. Article
  4. Article
  5. Article
  6. Phospholamban regulates nuclear CaJournal of molecular and cellular cardiology · 2018
    Article
  7. Article
  8. Unique CaInternational journal of molecular sciences · 2018
    Review
  9. Article
  10. Article
  11. Article
  12. Article
  13. Article
  14. Article
  15. Article
  16. Structural dynamics of muscle protein phosphorylation.Journal of muscle research and cell motility · 2012
    Review
  17. Article
4 · The record

Corrections and comments

  • Erratum issued
5 · Who and what money

Authors and funding

2 authors at 1 institution in 1 country.

Brandy L AkinKrannert Institute of Cardiology and the Department of Medicine, Indiana University School of Medicine, Indianapolis, Indiana 46202, USA.
Larry R Jones
Indiana University School of Medicine

Funding

Structure /Function of Phospholamban in HeartR37HL049428 · NHLBI · INDIANA UNIV-PURDUE UNIV AT INDIANAPOLIS · PI JONES, LARRY RICHARD · 2003 to 2012
$5.0M
STRUCTURE/FUNCTION OF PHOSPHOLAMBAN IN HEARTR01HL049428 · NHLBI · INDIANA UNIV-PURDUE UNIV AT INDIANAPOLIS · PI JONES, LARRY R · 1993 to 2002
$1.2M
NHLBI NIH HHS HL49428NHLBI NIH HHS R01 HL049428NHLBI NIH HHS R37 HL049428
6 · The paper itself

Abstract

Chemical cross-linking was used to study protein binding interactions between native phospholamban (PLB) and SERCA2a in sarcoplasmic reticulum (SR) vesicles prepared from normal and failed human hearts. Lys(27) of PLB was cross-linked to the Ca(2+) pump at the cytoplasmic extension of M4 (at or near Lys(328)) with the homobifunctional cross-linker, disuccinimidyl glutarate (7.7 Å). Cross-linking was augmented by ATP but abolished by Ca(2+) or thapsigargin, confirming in native SR vesicles that PLB binds preferentially to E2 (low Ca(2+) affinity conformation of the Ca(2+)-ATPase) stabilized by ATP. To assess the functional effects of PLB binding on SERCA2a activity, the anti-PLB antibody, 2D12, was used to disrupt the physical interactions between PLB and SERCA2a in SR vesicles. We observed a tight correlation between 2D12-induced inhibition of PLB cross-linking to SERCA2a and 2D12 stimulation of Ca(2+)-ATPase activity and Ca(2+) transport. The results suggest that the inhibitory effect of PLB on Ca(2+)-ATPase activity in SR vesicles results from mutually exclusive binding of PLB and Ca(2+) to the Ca(2+) pump, requiring PLB dissociation for catalytic activation. Importantly, the same result was obtained with SR vesicles prepared from normal and failed human hearts; therefore, we conclude that PLB binding interactions with the Ca(2+) pump are largely unchanged in failing myocardium.

Indexed as

AnimalsAntibodies, Monoclonal, Murine-DerivedCalciumCalcium-Binding ProteinsCell LineCross-Linking ReagentsHeart FailureHumansIon TransportMicrosomesMuscle ProteinsMyocardiumPhospholambanSarcoplasmic ReticulumSarcoplasmic Reticulum Calcium-Transporting ATPasesSpodopteraAntibodies, Monoclonal, Murine-DerivedATP2A2 protein, humanCalciumCalcium-Binding ProteinsCross-Linking ReagentsMuscle ProteinsPhospholambanSarcoplasmic Reticulum Calcium-Transporting ATPasesThapsigargin

Identifiers

PMID22247554
PMCPMC3293560
OpenAlexW2167019758

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.