Evidence map›Paper›PMID 21209335›Full record

ArticleProceedings of the National Academy of Sciences of the United States of America2011

Ca2+-dependent structural rearrangements within Na+-Ca2+ exchanger dimers.

Scott A John, Bernard Ribalet, James N Weiss, Kenneth D Philipson, Michela Ottolia

Open access · bronzeAbstract read
In one paragraph

Article in Proceedings of the National Academy of Sciences of the United States of America, 2011. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 31 papers.

0numbers the graph read from it
0cells of the map it votes in
31citing papers in PubMed
11.9field-weighted citation impact, top 1% 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

31 citing papers in PubMed, 67 citations in OpenAlex.

  1. Article
  2. Review
  3. Article
  4. Article
  5. Article
  6. Modulation of the cardiac NaCell calcium · 2020
    Review
  7. Article
  8. Article
  9. Modeling NaJournal of molecular and cellular cardiology · 2016
    Article
  10. Article
  11. Article
  12. Calpain-3-mediated regulation of the Na⁺-Ca²⁺ exchanger isoform 3.Pflugers Archiv : European journal of physiology · 2016
    Article
  13. Palmitoylation of the Na/Ca exchanger cytoplasmic loop controls its inactivation and internalization during stress signaling.FASEB journal : official publication of the Federation of American Societies for Experimental Biology · 2015
    Article
  14. Na+/Ca2+ exchange and Na+/K+-ATPase in the heart.The Journal of physiology · 2015
    Review
  15. Article
  16. Review
  17. Article
  18. Na/Ca exchange and contraction of the heart.Journal of molecular and cellular cardiology · 2013
    Review
  19. Article
  20. 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

5 authors at 1 institution in 2 countries.

Scott A JohnDepartment of Physiology, David Geffen School of Medicine, University of California, Los Angeles, CA 90095-1751, USA.
Bernard Ribalet
James N Weiss
Kenneth D Philipson
Michela Ottolia
University of California, Los Angeles · US

Funding

STRUCTURE/FUNCTION OF CARDIAC SODIUM/CALCIUM EXCHANGER01HL049101 · NHLBI · UNIVERSITY OF CALIFORNIA LOS ANGELES · PI PHILIPSON, KENNETH · 1993 to 2011
$5.8M
NHLBI NIH HHS HL49101NHLBI NIH HHS R01 HL049101
6 · The paper itself

Abstract

Cytoplasmic Ca(2+) is known to regulate Na(+)-Ca(2+) exchanger (NCX) activity by binding to two adjacent Ca(2+)-binding domains (CBD1 and CBD2) located in the large intracellular loop between transmembrane segments 5 and 6. We investigated Ca(2+)-dependent movements as changes in FRET between exchanger proteins tagged with CFP or YFP at position 266 within the large cytoplasmic loop. Data indicate that the exchanger assembles as a dimer in the plasma membrane. Addition of Ca(2+) decreases the distance between the cytoplasmic loops of NCX pairs. The Ca(2+)-dependent movements detected between paired NCXs were abolished by mutating the Ca(2+) coordination sites in CBD1 (D421A, E451A, and D500V), whereas disruption of the primary Ca(2+) coordination site in CBD2 (E516L) had no effect. Thus, the Ca(2+)-induced conformational changes of NCX dimers arise from the movement of CBD1. FRET studies of CBD1, CBD2, and CBD1-CBD2 peptides displayed Ca(2+)-dependent movements with different apparent affinities. CBD1-CBD2 showed a Ca(2+)-dependent phenotype mirroring full-length NCX but distinct from both CBD1 and CBD2.

Indexed as

Protein MultimerizationAnimalsBinding SitesCalciumCell MembraneCytoplasmDogsFemaleFluorescence Resonance Energy TransferHEK293 CellsHumansLuminescent ProteinsMembrane PotentialsMutationOocytesProtein ConformationCalciumLuminescent ProteinsSodium-Calcium Exchanger

Identifiers

PMID21209335
PMCPMC3029690
OpenAlexW2118907843

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.