Evidence map›Paper›PMID 18061662›Full record

ReviewCell calcium2008

Immuno-proteomic approach to excitation--contraction coupling in skeletal and cardiac muscle: molecular insights revealed by the mitsugumins.

Noah Weisleder, Hiroshi Takeshima, Jianjie Ma

Open access · greenAbstract readReview
In one paragraph

Review in Cell calcium, 2008. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 42 papers.

0numbers the graph read from it
0cells of the map it votes in
42citing papers in PubMed
1.5field-weighted citation impact, top 20% 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

42 citing papers in PubMed, 63 citations in OpenAlex.

  1. Review
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  15. A focus on extracellular CaExperimental & molecular medicine · 2017
    Review
  16. Immunological Disorders: Regulation of CaAdvances in experimental medicine and biology · 2017
    Review
  17. Review
  18. Junctophilin-4, a component of the endoplasmic reticulum-plasma membrane junctions, regulates Ca2+ dynamics in T cells.Proceedings of the National Academy of Sciences of the United States of America · 2016
    Article
  19. Review
  20. Review
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

3 authors at 2 institutions in 2 countries.

Noah WeislederDepartment of Physiology and Biophysics, UMDNJ-Robert Wood Johnson Medical School, NJ 08854, USA.
Hiroshi Takeshima
Jianjie Ma
Rutgers, The State University of New Jersey · USKyoto Pharmaceutical University · JP

Funding

Modulation of MG53 Function in Cardiac Membrane RepairR01HL069000 · NHLBI · UNIV OF MED/DENT NJ-R W JOHNSON MED SCH · PI MA, JIANJIE · 2002 to 2016
$5.3M
TRIC, a Novel Modulator of Intracellular Ca HomeostasisR01AG028856 · NIA · UNIV OF MED/DENT NJ-R W JOHNSON MED SCH · PI MA, JIANJIE · 2008 to 2012
$2.1M
NHLBI NIH HHS R01 HL069000NIA NIH HHS R01 AG028856
6 · The paper itself

Abstract

A comprehensive understanding of excitation-contraction (E-C) coupling in skeletal and cardiac muscle requires that all the major components of the Ca(2+) release machinery be resolved. We utilized a unique immuno-proteomic approach to generate a monoclonal antibody library that targets proteins localized to the skeletal muscle triad junction, which provides a structural context to allow efficient E-C coupling. Screening of this library has identified several mitsugumins (MG); proteins that can be localized to the triad junction in mammalian skeletal muscle. Many of these proteins, including MG29 and junctophilin, are important components in maintaining the structural integrity of the triad junction. Other triad proteins, such as calumin, play a more direct role in regulation of muscle Ca(2+) homeostasis. We have recently identified a family of trimeric intracellular cation-selective (TRIC) channels that allow for K(+) movement into the endoplasmic or sarcoplasmic reticulum to counter a portion of the transient negative charge produced by Ca(2+) release into the cytosol. Further study of TRIC channel function and other novel mitsugumins will increase our understanding of E-C coupling and Ca(2+) homoeostasis in muscle physiology and pathophysiology.

Indexed as

Calcium SignalingMuscle ContractionAnimalsAntibodies, MonoclonalCalcium-Binding ProteinsHeartIon ChannelsMembrane ProteinsMiceMuscle ProteinsMuscle, SkeletalProteomicsSynaptophysinAntibodies, MonoclonalCalcium-Binding ProteinsIon ChannelsjunctophilinMembrane ProteinsMg29 protein, mouseMuscle ProteinsSynaptophysin

Identifiers

PMID18061662
PMCPMC3059838
OpenAlexW1980780359

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.