Evidence map›Paper›PMID 9742444›Full record

ReviewJournal of muscle research and cell motility1998

Troponin T: genetics, properties and function.

S V Perry

Abstract readReview
PubMed Publisher
In one paragraph

Review in Journal of muscle research and cell motility, 1998. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 118 papers.

0numbers the graph read from it
0cells of the map it votes in
118citing papers in PubMed
9.9field-weighted citation impact, top 1% 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

118 citing papers in PubMed, 307 citations in OpenAlex.

  1. Review
  2. Predicting axial muscle-fibre strains in larval zebrafish.The Journal of experimental biology · 2026
    Article
  3. Biomarkers of Cardiovascular Stress: A Historical Review.Journal of cardiovascular development and disease · 2026
    Review
  4. Review
  5. Review
  6. Article
  7. Article
  8. Article
  9. Review
  10. Nucleus Mechanosensing in Cardiomyocytes.International journal of molecular sciences · 2023
    Review
  11. Cardiac troponin T N-domain variant destabilizes the actin interface resulting in disturbed myofilament function.Proceedings of the National Academy of Sciences of the United States of America · 2023
    Article
  12. Article
  13. Article
  14. Article
  15. Allele-specific silencing by RNAi of R92Q and R173W mutations in cardiac troponin T.Experimental biology and medicine (Maywood, N.J.) · 2022
    Article
  16. Review
  17. Review
  18. Review
  19. Article
  20. A Mechanism Underlying Sex-Associated Differences in Ankylosing Spondylitis: Troponin C2, Fast Skeletal Type (TNNC2) and Calcium Signaling Pathway.Medical science monitor : international medical journal of experimental and clinical research · 2020
    Article

58 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

1 author at 1 institution in 1 country.

S V PerryDepartment of Physiology, Medical School, University of Birmingham, UK.
University of Birmingham · GB

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

Troponin T (TnT) is present in striated muscle of vertebrates and invertebrates as a group of homologous proteins with molecular weights usually in the 31-36 kDa range. It occupies a unique role in the regulatory protein system in that it interacts with TnC and TnI of the troponin complex and the proteins of the myofibrillar thin filament, tropomyosin and actin. In the myofibril the molecule is about 18 nm long and for much its length interacts with tropomyosin. The ability of TnT to form a complex with tropomyosin is responsible for locating the troponin complex with a periodicity of 38.5 nm along the thin filament of the myofibril. In addition to it structural role, TnT has the important function of transforming the TnI-TnC complex into a system, the inhibitory activity of which, on the tropomyosin-actomyosin MgATPase of the myofibril, becomes sensitive to calcium ions. Different genes control the expression of TnT in fast skeletal, slow skeletal and cardiac muscles. In all muscles, and particularly in fast skeletal, alternative splicing of mRNA produces a series of isoforms in a developmentally regulated manner. In consequence TnT exists in many more isoforms than any of the other thin filament proteins, the TnT superfamily. Despite the general homology of TnT isoforms, this alternative splicing leads to variable regions close to the N- and C-termini. As the isoforms have slightly different effects on the calcium sensitivity of the actomyosin MgATPase, modulation of the contractile response to calcium can occur during development and in different muscle types. TnT has recently aroused clinical interest in its potential for detecting myocardial damage and the association of mutations in the cardiac isoform with hypertrophic cardiomyopathy.

Indexed as

Amino Acid SequenceAnimalsHumansMolecular Sequence DataTroponin TTroponin T

Identifiers

PMID9742444
OpenAlexW91200975

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.