Evidence map›Paper›PMID 26891592›Full record

ReviewArchives of biochemistry and biophysics2016

Structural determinants of muscle thin filament cooperativity.

Jeffrey R Moore, Stuart G Campbell, William Lehman

Open access · greenAbstract readReview
In one paragraph

Review in Archives of biochemistry and biophysics, 2016. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 31 papers.

0numbers the graph read from it
0cells of the map it votes in
31citing papers in PubMed
5.2field-weighted citation impact, top 4% 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

31 citing papers in PubMed, 44 citations in OpenAlex.

  1. Article
  2. Review
  3. Article
  4. Modeling cardiac contractile cooperativity across species.The Journal of general physiology · 2025
    Article
  5. Article
  6. Article
  7. Article
  8. Review
  9. Cardiomyocyte Dysfunction in Inherited Cardiomyopathies.International journal of molecular sciences · 2021
    Review
  10. Article
  11. Review
  12. Article
  13. Article
  14. Review
  15. Article
  16. Article
  17. Article
  18. Review
  19. Closing the therapeutic loop.Archives of biochemistry and biophysics · 2019
    Review
  20. 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

3 authors at 3 institutions in 1 country.

Jeffrey R MooreDepartment of Biological Sciences, University of Massachusetts Lowell, One University Avenue, Lowell, MA 018154, USA.
Stuart G CampbellDepartment of Biomedical Engineering, Yale University, 55 Prospect Street, New Haven, CT 06511, USA.
William LehmanDepartment of Physiology & Biophysics, Boston University School of Medicine, 72 East Concord Street, Boston, MA 02118, USA. Electronic address: wlehman@bu.edu.
Boston University · USUniversity of Massachusetts Lowell · USYale University · US

Funding

Yale University Clinical and Translational Science Award ProgramUL1TR000142 · NCATS · YALE UNIVERSITY · PI SHERWIN, ROBERT S · 2012 to 2015
$31.8M
Thin Filaments and Muscle RegulationR37HL036153 · NHLBI · BOSTON UNIVERSITY MEDICAL CAMPUS · PI LEHMAN, WILLIAM J · 2008 to 2017
$4.1M
Molecular Mechanics of Mutant Cardiac MyosinR01HL077280 · NHLBI · UNIVERSITY OF MASSACHUSETTS LOWELL · PI MOORE, JEFFREY R · 2005 to 2014
$3.3M
Cooperativity in the Cardiac Myofilament Interactome in Health and DiseaseR01HL123774 · NHLBI · UNIVERSITY OF MASSACHUSETTS LOWELL · PI MOORE, JEFFREY R · 2016 to 2019
$1.6M
Engineered Tissue for Biomechanical Phenotyping of Cardiomyopathy PatientsR21HL126025 · NHLBI · YALE UNIVERSITY · PI CAMPBELL, STUART G · 2015 to 2016
$458k
NCATS NIH HHS UL1 TR000142NCATS NIH HHS UL1TR000142NHLBI NIH HHS R01 HL077280NHLBI NIH HHS R01HL077280NHLBI NIH HHS R01 HL123774NHLBI NIH HHS R21 HL126025NHLBI NIH HHS R21HL126025NHLBI NIH HHS R37 HL036153NHLBI NIH HHS R37HL036153
6 · The paper itself

Abstract

End-to-end connections between adjacent tropomyosin molecules along the muscle thin filament allow long-range conformational rearrangement of the multicomponent filament structure. This process is influenced by Ca(2+) and the troponin regulatory complexes, as well as by myosin crossbridge heads that bind to and activate the filament. Access of myosin crossbridges onto actin is gated by tropomyosin, and in the case of striated muscle filaments, troponin acts as a gatekeeper. The resulting tropomyosin-troponin-myosin on-off switching mechanism that controls muscle contractility is a complex cooperative and dynamic system with highly nonlinear behavior. Here, we review key information that leads us to view tropomyosin as central to the communication pathway that coordinates the multifaceted effectors that modulate and tune striated muscle contraction. We posit that an understanding of this communication pathway provides a framework for more in-depth mechanistic characterization of myopathy-associated mutational perturbations currently under investigation by many research groups.

Indexed as

ActinsCalciumHumansMuscle ContractionMusclesMyosinsTropomyosinActinsCalciumMyosinsTropomyosinActinCooperativityMyosinThin filamentTropomyosinTroponin

Identifiers

PMID26891592
PMCPMC4792785
OpenAlexW2276337236

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.