Evidence map›Paper›PMID 26526134›Full record

ReviewGene2016

TNNI1, TNNI2 and TNNI3: Evolution, regulation, and protein structure-function relationships.

Juan-Juan Sheng, Jian-Ping Jin

Open access · greenAbstract readReview
In one paragraph

Review in Gene, 2016. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 82 papers.

0numbers the graph read from it
0cells of the map it votes in
82citing papers in PubMed
4.2field-weighted citation impact, top 5% 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

82 citing papers in PubMed, 143 citations in OpenAlex.

  1. Review
  2. Article
  3. ALIGNED Network for rare cerebrovascular diseases: methodology and preliminary results.Neurological sciences : official journal of the Italian Neurological Society and of the Italian Society of Clinical Neurophysiology · 2026
    Article
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  6. Atlas of lysine acetylation in the mouse.bioRxiv : the preprint server for biology · 2026
    Article
  7. Review
  8. Cannabidiol Protects the Neonatal Mouse Heart from Hyperoxia-Induced Injury.International journal of molecular sciences · 2025
    Article
  9. Article
  10. Article
  11. Article
  12. Article
  13. Article
  14. Review
  15. Article
  16. Deletion ofJournal of developmental biology · 2025
    Article
  17. Zoological research · 2025
    Article
  18. Article
  19. Review
  20. Article

22 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.

Juan-Juan ShengDepartment of Physiology, Wayne State University School of Medicine, Detroit, MI 48201, USA.
Jian-Ping JinDepartment of Physiology, Wayne State University School of Medicine, Detroit, MI 48201, USA. Electronic address: jjin@med.wayne.edu.
Wayne State University · US

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
Role of Troponin T Isoforms in Nemaline MyopathyR01AR048816 · NIAMS · WAYNE STATE UNIVERSITY · PI JIN, JIAN-PING · 2003 to 2014
$3.2M
Proteolytic Regulation of Troponin T & Cardiac FunctionR01HL098945 · NHLBI · WAYNE STATE UNIVERSITY · PI JIN, JIAN-PING · 2010 to 2014
$2.0M
NHLBI NIH HHS HL-098945NHLBI NIH HHS R01 HL098945NIAMS NIH HHS AR-048816NIAMS NIH HHS R01 AR048816NIGMS NIH HHS GM089820NIGMS NIH HHS GM114833NIGMS NIH HHS R01 GM089820NIGMS NIH HHS U54 GM114833
6 · The paper itself

Abstract

Troponin I (TnI) is the inhibitory subunit of the troponin complex in the sarcomeric thin filament of striated muscle and plays a central role in the calcium regulation of contraction and relaxation. Vertebrate TnI has evolved into three isoforms encoded by three homologous genes: TNNI1 for slow skeletal muscle TnI, TNNI2 for fast skeletal muscle TnI and TNNI3 for cardiac TnI, which are expressed under muscle type-specific and developmental regulations. To summarize the current knowledge on the TnI isoform genes and products, this review focuses on the evolution, gene regulation, posttranslational modifications, and structure-function relationship of TnI isoform proteins. Their physiological and medical significances are also discussed.

Indexed as

Evolution, MolecularGene Expression RegulationAmino Acid SequenceAnimalsHumansMAP Kinase Kinase KinasesMolecular Sequence DataProtein Processing, Post-TranslationalProtein Serine-Threonine KinasesSequence Homology, Amino AcidStructure-Activity RelationshipTroponin IMAP Kinase Kinase KinasesProtein Serine-Threonine KinasesTNNI1 protein, humanTNNI2 protein, humanTNNI3K protein, humanTroponin ICardiac and skeletal muscleEvolutionGene regulationIsoformPosttranslational modificationTroponin I

Identifiers

PMID26526134
PMCPMC5798203
OpenAlexW1937719427

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.