Evidence map›Paper›PMID 31712308›Full record

ArticleThe Journal of biological chemistry2019

Basic residues within the cardiac troponin T C terminus are required for full inhibition of muscle contraction and limit activation by calcium.

Dylan Johnson, Li Zhu, Maicon Landim-Vieira, Jose Renato Pinto, Joseph M Chalovich

Open access · hybridAbstract read
In one paragraph

Article in The Journal of biological chemistry, 2019. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 13 papers, 1 of them a synthesis that pooled it.

0numbers the graph read from it
0cells of the map it votes in
13citing papers in PubMed, 1 pooled it
1.3field-weighted citation impact, top 17% 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

13 citing papers in PubMed, 1 synthesis or guideline pooled it, 17 citations in OpenAlex.

  1. Pooled it
  2. Thin filament interaction and CaJournal of molecular and cellular cardiology · 2026
    Article
  3. Article
  4. Article
  5. Review
  6. The role of mechanosignaling in the control of myocardial mass.American journal of physiology. Heart and circulatory physiology · 2025
    Review
  7. Article
  8. 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
  9. Low expression of the K280NJournal of molecular and cellular cardiology plus · 2022
    Article
  10. Article
  11. Review
  12. Article
  13. 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

5 authors at 2 institutions in 1 country.

Dylan JohnsonDepartment of Biochemistry and Molecular Biology, Brody School of Medicine at East Carolina University, Greenville, North Carolina 27834.
Li ZhuDepartment of Biochemistry and Molecular Biology, Brody School of Medicine at East Carolina University, Greenville, North Carolina 27834.
Maicon Landim-VieiraDepartment of Biomedical Sciences, College of Medicine, Florida State University, Tallahassee, Florida 32306.
Jose Renato PintoDepartment of Biomedical Sciences, College of Medicine, Florida State University, Tallahassee, Florida 32306.
Joseph M ChalovichDepartment of Biochemistry and Molecular Biology, Brody School of Medicine at East Carolina University, Greenville, North Carolina 27834 chalovichj@ecu.edu.ORCID 0000-0002-1243-4055
East Carolina University · USFlorida State University · US

Funding

Modulators of Cardiomyopathic DiseasesR01HL128683 · NHLBI · FLORIDA STATE UNIVERSITY · PI PINTO, JOSE RENATO · 2016 to 2020
$1.8M
Acting Based Regulation of Smooth Muscle ContractionR01AR035216 · NIAMS · EAST CAROLINA UNIVERSITY · PI CHALOVICH, JOSEPH M · 1986 to 2007
$1.5M
NHLBI NIH HHS R01 HL128683NIAMS NIH HHS R01 AR035216
6 · The paper itself

Abstract

Striated muscle is activated by myosin- and actin-linked processes, with the latter being regulated through changes in the position of tropomyosin relative to the actin surface. The C-terminal region of cardiac troponin T (TnT), a tropomyosin-associated protein, is required for full TnT inactivation at low Ca

Indexed as

Actin CytoskeletonActinsAdenosine TriphosphatasesAlanineAnimalsArginineCalciumFluorescence Resonance Energy TransferFluorescent DyesHumansKineticsLysineMuscle ContractionMutationMyosinsProtein BindingActinsAdenosine TriphosphatasesAlanineArginineCalciumFluorescent DyesLysineMyosinsTNNT2 protein, humanTropomyosinTroponin TATPase activitycardiac musclecross-bridge kineticsfluorescence resonance energy transfer (FRET)high Ala, high activation TnT (HAHA TnT)muscle physiologystates of actintropomyosintroponintroponin T (TnT)

Identifiers

PMID31712308
PMCPMC6926443
OpenAlexW2988081078

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.