Evidence map›Paper›PMID 19917222›Full record

ArticleBiophysical journal2009

The role of sarcolipin and ATP in the transport of phosphate ion into the sarcoplasmic reticulum.

Lucia Becucci, Rolando Guidelli, Christine B Karim, David D Thomas, Gianluigi Veglia

Open access · bronzeAbstract read
In one paragraph

Article in Biophysical journal, 2009. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 3 papers.

0numbers the graph read from it
0cells of the map it votes in
3citing papers in PubMed
0.9field-weighted citation impact, top 25% 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

3 citing papers in PubMed, 19 citations in OpenAlex.

  1. Article
  2. Article
  3. Oligomeric interactions of sarcolipin and the Ca-ATPase.The Journal of biological chemistry · 2011
    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.

Lucia BecucciChemistry Department, Florence University, Florence, Italy.
Rolando Guidelli
Christine B Karim
David D Thomas
Gianluigi Veglia
University of Minnesota · USUniversity of Florence · IT

Funding

NMR Structural Analysis of Calcium Regulation in MuscleR01GM064742 · NIGMS · UNIVERSITY OF MINNESOTA TWIN CITIES · PI VEGLIA, GIANLUIGI · 2002 to 2019
$7.1M
Structural Basis Of Dilated CardiomyopathyR01GM072701 · NIGMS · UNIVERSITY OF MINNESOTA · PI VEGLIA, GIANLUIGI · 2007 to 2015
$2.4M
Structural Basis of Heart Muscle Function and DiseaseK02HL080081 · NHLBI · UNIVERSITY OF MINNESOTA TWIN CITIES · PI VEGLIA, GIANLUIGI · 2005 to 2009
$539k
NHLBI NIH HHS HL80081NHLBI NIH HHS K02 HL080081NIGMS NIH HHS GM072701NIGMS NIH HHS GM64742NIGMS NIH HHS R01 GM064742NIGMS NIH HHS R01 GM072701
6 · The paper itself

Abstract

In a previous study, sarcolipin (SLN) was shown to form channels selective toward chloride ion when incorporated in a mercury-supported tethered bilayer lipid membrane (tBLM). Its incorporation had only a modest permeabilizing effect on phosphate ion. In this note the resistance of a tBLM membrane incorporating sarcolipin was investigated by electrochemical impedance spectroscopy in aqueous solutions of 0.05 M sodium phosphate of pH ranging from 5.3 to 8, in the presence of ATP, adenosine monophosphate, and phenylphosphonic acid. At pH 5.3, submicromolar additions of ATP increase the conductivity of the tBLM incorporating SLN up to a maximum limiting value. The dependence of the conductivity on the ATP concentration satisfies the Michaelis-Menten equation, with an association constant of 0.1 microM. Phenylphosphonium ion and adenosine monophosphate exert an inhibitory effect on membrane permeabilization to phosphate ions by ATP if they are added before ATP, but not if they are added after it. An explanation for this behavior is provided. In conclusion, SLN acts as an ATP-induced phosphate carrier exhibiting a behavior quite similar to that of the unidentified P(i) transporter described previously. No ion-channel activity is exhibited by the T18A mutant of SLN.

Indexed as

Adenosine MonophosphateAdenosine TriphosphateAlgorithmsAnimalsBiological TransportCell Membrane PermeabilityElectric ConductivityHydrogen-Ion ConcentrationIonsLipid BilayersMercuryModels, BiologicalMuscle ProteinsMutationOrganophosphorus CompoundsPhosphatesAdenosine MonophosphateAdenosine TriphosphateIonsLipid BilayersMercuryMuscle ProteinsOrganophosphorus Compoundsphenylphosphonic acidPhosphatesProteolipidssarcolipinWater

Identifiers

PMID19917222
PMCPMC2776249
OpenAlexW2165507290

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.