Evidence map›Paper›PMID 26585961›Full record

ArticleJournal of muscle research and cell motility2016

Calsequestrins in skeletal and cardiac muscle from adult Danio rerio.

Sandra Furlan, Simone Mosole, Marta Murgia, Nagarjuna Nagaraj, Francesco Argenton, Pompeo Volpe, Alessandra Nori

Open access · greenAbstract read
PubMed Publisher
In one paragraph

Article in Journal of muscle research and cell motility, 2016. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 6 papers.

0numbers the graph read from it
0cells of the map it votes in
6citing papers in PubMed
–field-weighted citation impact, top 90% 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

6 citing papers in PubMed, 10 citations in OpenAlex.

  1. Article
  2. Article
  3. Modeling Human Cardiac Arrhythmias: Insights from Zebrafish.Journal of cardiovascular development and disease · 2022
    Review
  4. Article
  5. Calsequestrin, a key protein in striated muscle health and disease.Journal of muscle research and cell motility · 2021
    Review
  6. 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

7 authors at 3 institutions in 2 countries.

Sandra FurlanInstitute of Neuroscience Consiglio Nazionale delle Ricerche, Viale G. Colombo 3, 35121, Padua, Italy.
Simone MosoleDepartment of Biomedical Sciences, Istituto Interuniversitario di Miologia, University of Padova, Viale G. Colombo 3, 35121, Padua, Italy.
Marta MurgiaDepartment of Biomedical Sciences, Istituto Interuniversitario di Miologia, University of Padova, Viale G. Colombo 3, 35121, Padua, Italy.
Nagarjuna NagarajDepartment of Proteomics and Signal Transduction, Max-Planck-Institute of Biochemistry, Am Klopferspitz 18, 82152, Martinsried, Germany.
Francesco ArgentonDepartment of Biology, University of Padova, Via U.Bassi 58/B, 35121, Padua, Italy.
Pompeo VolpeInstitute of Neuroscience Consiglio Nazionale delle Ricerche, Viale G. Colombo 3, 35121, Padua, Italy.
Alessandra NoriDepartment of Biomedical Sciences, Istituto Interuniversitario di Miologia, University of Padova, Viale G. Colombo 3, 35121, Padua, Italy. alessandra.nori@unipd.it.ORCID 0000-0003-3968-9450
University of Padua · ITMax Planck Institute of Biochemistry · DENeuroscience Institute · IT

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

Calsequestrin (Casq) is a high capacity, low affinity Ca(2+)-binding protein, critical for Ca(2+)-buffering in cardiac and skeletal muscle sarcoplasmic reticulum. All vertebrates have multiple genes encoding for different Casq isoforms. Increasing interest has been focused on mammalian and human Casq genes since mutations of both cardiac (Casq2) and skeletal muscle (Casq1) isoforms cause different, and sometime severe, human pathologies. Danio rerio (zebrafish) is a powerful model for studying function and mutations of human proteins. In this work, expression, biochemical properties cellular and sub-cellular localization of D. rerio native Casq isoforms are investigated. By quantitative PCR, three mRNAs were detected in skeletal muscle and heart with different abundances. Three zebrafish Casqs: Casq1a, Casq1b and Casq2 were identified by mass spectrometry (Data are available via ProteomeXchange with identifier PXD002455). Skeletal and cardiac zebrafish calsequestrins share properties with mammalian Casq1 and Casq2. Skeletal Casqs were found primarily, but not exclusively, at the sarcomere Z-line level where terminal cisternae of sarcoplasmic reticulum are located.

Indexed as

AnimalsCalsequestrinMuscle, SkeletalMutationMyocardiumProtein IsoformsZebrafishZebrafish ProteinsCalsequestrinProtein IsoformsZebrafish ProteinsAnimal modelsCa2+-binding proteinsDanio rerioSarcoplasmic reticulum

Identifiers

PMID26585961
OpenAlexW2180578305

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.