Evidence map›Paper›PMID 26232335›Full record

ReviewGene2015

Structure and function of cardiac troponin C (TNNC1): Implications for heart failure, cardiomyopathies, and troponin modulating drugs.

Monica X Li, Peter M Hwang

Abstract readReview
In one paragraph

Review in Gene, 2015. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 71 papers.

0numbers the graph read from it
0cells of the map it votes in
71citing papers in PubMed
6.4field-weighted citation impact, top 3% 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

71 citing papers in PubMed, 133 citations in OpenAlex.

  1. Article
  2. Review
  3. Article
  4. Evolutionary and physics-guided modulation of CaJournal of molecular modeling · 2026
    Article
  5. Article
  6. Article
  7. Review
  8. Review
  9. Article
  10. Article
  11. Article
  12. Article
  13. Article
  14. Review
  15. Article
  16. Article
  17. Review
  18. Article
  19. Article
  20. Cardiac Troponin ActivatorJournal of medicinal chemistry · 2024
    Article

11 more citing papers are in PubMed but not listed here.

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

2 authors at 1 institution in 1 country.

Monica X LiDepartment of Medicine, University of Alberta, Edmonton, AB T6G 2G3, Canada; Department of Biochemistry, University of Alberta, Edmonton, AB T6G 2H7, Canada.
Peter M HwangDepartment of Medicine, University of Alberta, Edmonton, AB T6G 2G3, Canada; Department of Biochemistry, University of Alberta, Edmonton, AB T6G 2H7, Canada. Electronic address: phwang1@ualberta.ca.
University of Alberta · CA

Funding

TRAININGU54GM114833 · NIGMS · UNIVERSITY OF CALIFORNIA LOS ANGELES · PI LINDSEY, MERRY L., PING, PEIPEI · 2014 to 2017
$13.8M
The Gene Wiki: Community intelligence applied to gene annotationR01GM089820 · NIGMS · SCRIPPS RESEARCH INSTITUTE, THE · PI SU, ANDREW I · 2010 to 2021
$5.2M
NIGMS NIH HHS GM089820NIGMS NIH HHS GM114833NIGMS NIH HHS R01 GM089820NIGMS NIH HHS U54 GM114833
6 · The paper itself

Abstract

In striated muscle, the protein troponin complex turns contraction on and off in a calcium-dependent manner. The calcium-sensing component of the complex is troponin C, which is expressed from the TNNC1 gene in both cardiac muscle and slow-twitch skeletal muscle (identical transcript in both tissues) and the TNNC2 gene in fast-twitch skeletal muscle. Cardiac troponin C (cTnC) is made up of two globular EF-hand domains connected by a flexible linker. The structural C-domain (cCTnC) contains two high affinity calcium-binding sites that are always occupied by Ca(2+) or Mg(2+) under physiologic conditions, stabilizing an open conformation that remains anchored to the rest of the troponin complex. In contrast, the regulatory N-domain (cNTnC) contains a single low affinity site that is largely unoccupied at resting calcium concentrations. During muscle activation, calcium binding to cNTnC favors an open conformation that binds to the switch region of troponin I, removing adjacent inhibitory regions of troponin I from actin and allowing muscle contraction to proceed. Regulation of the calcium binding affinity of cNTnC is physiologically important, because it directly impacts the calcium sensitivity of muscle contraction. Calcium sensitivity can be modified by drugs that stabilize the open form of cNTnC, post-translational modifications like phosphorylation of troponin I, or downstream thin filament protein interactions that impact the availability of the troponin I switch region. Recently, mutations in cTnC have been associated with hypertrophic or dilated cardiomyopathy. A detailed understanding of how calcium sensitivity is regulated through the troponin complex is necessary for explaining how mutations perturb its function to promote cardiomyopathy and how post-translational modifications in the thin filament affect heart function and heart failure. Troponin modulating drugs are being developed for the treatment of cardiomyopathies and heart failure.

Indexed as

Amino Acid SequenceAnimalsCardiomyopathiesCardiovascular AgentsHeart FailureHumansModels, MolecularMolecular Sequence DataMyocardiumProtein BindingProtein ConformationProtein Processing, Post-TranslationalTroponin CCardiovascular AgentsTroponin CCalcium sensitizerDilated cardiomyopathyHeart failureHypertrophic cardiomyopathyLevosimendanSarcomere modulators

Identifiers

PMID26232335
PMCPMC4567495
OpenAlexW1062333943

What OpenQuestion holds

Textmetadata
LicenceTDM
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.