Evidence map›Paper›PMID 15189864›Full record

ArticleBiophysical journal2004

Time-resolved charge translocation by sarcoplasmic reticulum Ca-ATPase measured on a solid supported membrane.

Francesco Tadini Buoninsegni, Gianluca Bartolommei, Maria Rosa Moncelli, Giuseppe Inesi, Rolando Guidelli

Open access · bronzeAbstract read
In one paragraph

Article in Biophysical journal, 2004. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 17 papers.

0numbers the graph read from it
0cells of the map it votes in
17citing papers in PubMed
1.1field-weighted citation impact, top 24% 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, 40 citations in OpenAlex.

  1. Article
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  5. Phosphatidylserine flipping by the P4-ATPase ATP8A2 is electrogenic.Proceedings of the National Academy of Sciences of the United States of America · 2019
    Article
  6. Mechanism of the E2 to E1 transition in CaProceedings of the National Academy of Sciences of the United States of America · 2018
    Article
  7. Article
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  17. Structural role of countertransport revealed in Ca(2+) pump crystal structure in the absence of Ca(2+).Proceedings of the National Academy of Sciences of the United States of America · 2005
    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 2 institutions in 2 countries.

Francesco Tadini BuoninsegniDepartment of Chemistry, University of Florence, 50019 Sesto Fiorentino, Italy.
Gianluca Bartolommei
Maria Rosa Moncelli
Giuseppe Inesi
Rolando Guidelli
University of Florence · ITUniversity of Maryland, Baltimore · US

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

Sarcoplasmic reticulum vesicles were adsorbed on an octadecanethiol/phosphatidylcholine mixed bilayer anchored to a gold electrode, and the Ca-ATPase contained in the vesicles was activated by ATP concentration jumps both in the absence and in the presence of K(+) ions and at different pH values. Ca(2+) concentration jumps in the absence of ATP were also carried out. The resulting capacitive current transients were analyzed together with the charge under the transients. The relaxation time constants of the current transients were interpreted on the basis of an equivalent circuit. The current transient after ATP concentration jumps and the charge after Ca(2+) concentration jumps in the absence of ATP exhibit almost the same dependence upon the Ca(2+) concentration, with a half-saturating value of approximately 1.5 microM. The pH dependence of the charge after Ca(2+) translocation demonstrates the occurrence of one H(+) per one Ca(2+) countertransport at pH 7 by direct charge-transfer measurements. The presence of K(+) decreases the magnitude of the current transients without altering their shape; this decrease is explained by K(+) binding to the cytoplasmic side of the pump in the E(1) conformation and being released to the same side during the E(1)-E(2) transition.

Indexed as

Adenosine TriphosphateAnimalsCalciumCalcium-Transporting ATPasesHydrogen-Ion ConcentrationLipid BilayersMuscle, SkeletalPotassiumRabbitsSarcoplasmic ReticulumAdenosine TriphosphateCalciumCalcium-Transporting ATPasesLipid BilayersPotassium

Identifiers

PMID15189864
PMCPMC1304269
OpenAlexW2165327305

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.