Evidence map›Paper›PMID 40735528›Full record

ReviewAnimal cells and systems2025

Troponin I - a comprehensive review of its function, structure, evolution, and role in muscle diseases.

Dongju Han, Younghyun Lim, Soah Lee, Seong-Il Eyun

Abstract readReview
In one paragraph

Review in Animal cells and systems, 2025. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 4 papers.

0numbers the graph read from it
0cells of the map it votes in
4citing papers in PubMed
–field-weighted citation impact
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

4 citing papers in PubMed.

  1. Review
  2. Article
  3. Article
  4. 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

4 authors.

Dongju HanDepartment of Life Science, Chung-Ang University, Seoul, Korea.ORCID https://orcid.org/0009-0000-6046-6492
Younghyun LimDepartment of Life Science, Chung-Ang University, Seoul, Korea.
Soah LeeDepartment of Biopharmaceutical Convergence, Sungkyunkwan University, Suwon, Korea.
Seong-Il EyunDepartment of Life Science, Chung-Ang University, Seoul, Korea.ORCID https://orcid.org/0000-0003-4687-1066

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

The troponin complex is a critical component of thin filaments and plays an essential role in the calcium-mediated regulation of contraction and relaxation in striated muscles, including both cardiac and skeletal muscle. Troponin I, a subunit of this complex, inhibits actomyosin interactions during muscle relaxation. Its function is finely tuned by posttranslational modifications, particularly phosphorylation, which influence calcium sensitivity and actin affinity, thus impacting muscle contraction. Mutations in troponin I are closely associated with various human diseases. Specifically, several mutations in cardiac troponin I have been linked to cardiomyopathies, such as hypertrophic, dilated, and restrictive cardiomyopathies, which affect heart contractility and calcium handling. In this review, we explore the multifaceted aspects of troponin I, including its structure, functional role in muscle contraction, evolution, and the complex interactions between posttranslational modifications and genetic mutations that alter its function and contribute to disease progression.

Indexed as

cardiomyopathyevolution of troponin Igenetic mutations in troponin Ipost-transcriptional modification of troponin ITroponin I

Identifiers

PMID40735528
PMCPMC12305882

What OpenQuestion holds

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Registered trials

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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.