Evidence map›Paper›PMID 10747195›Full record

ArticleThe Journal of physiology2000

Regulation of force and unloaded sliding speed in single thin filaments: effects of regulatory proteins and calcium.

E Homsher, D M Lee, C Morris, D Pavlov, L S Tobacman

Open access · greenAbstract read
In one paragraph

Article in The Journal of physiology, 2000. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 51 papers.

0numbers the graph read from it
0cells of the map it votes in
51citing papers in PubMed
6.7field-weighted citation impact, top 3% 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

51 citing papers in PubMed, 95 citations in OpenAlex.

  1. Review
  2. Article
  3. Article
  4. Article
  5. Force Measurements From Myofibril to Filament.Frontiers in physiology · 2021
    Review
  6. Article
  7. Article
  8. Review
  9. Article
  10. Article
  11. Article
  12. Article
  13. Article
  14. Structural determinants of muscle thin filament cooperativity.Archives of biochemistry and biophysics · 2016
    Review
  15. Review
  16. Article
  17. Review
  18. Review
  19. 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

5 authors at 3 institutions in 1 country.

E HomsherDepartment of Physiology, School of Medicine, UCLA, Los Angeles, CA 90095, USA. ehomsher@physiology.medsch.ucla.edu
D M Lee
C Morris
D Pavlov
L S Tobacman
University of California, Los Angeles · USUCLA Medical Center · USUniversity of Iowa · US

Funding

CARDIAC CONTRACTILE PROTEIN COOPERATIVITYR01HL038834 · NHLBI · UNIVERSITY OF IOWA · PI TOBACMAN, LARRY S · 1992 to 2009
$3.6M
MUSCLE ENERGETICS AND CHEMOMECHANICAL TRANSDUCTIONR01AR030988 · NIAMS · UNIVERSITY OF CALIFORNIA LOS ANGELES · PI HOMSHER, EARL E · 1986 to 2007
$1.9M
CARDIAC CONTRACTILE PROTEIN COOPERATIVITYR29HL038834 · NHLBI · UNIVERSITY OF IOWA · PI TOBACMAN, LARRY S · 1987 to 1991
–
NHLBI NIH HHS HL-38834NHLBI NIH HHS R01 HL038834NIAMS NIH HHS AR-30988NIAMS NIH HHS R01 AR030988
6 · The paper itself

Abstract

1. Measurements of the unloaded sliding speed of and isometric force exerted on single thin filaments in in vitro motility assays were made to evaluate the role of regulatory proteins in the control of unloaded thin filament sliding speed and isometric force production. 2. Regulated actin filaments were reconstituted from rabbit F-actin, native bovine cardiac tropomyosin (nTm), and either native bovine cardiac troponin (nTn), troponin containing a TnC mutant, CBMII, in which the sole regulatory site in cardiac TnC (site II) is inactivated (CBMII-Tn), or troponin containing a point mutation in TnT (I79N, where isoleucine at position 79 is replaced with asparagine) associated with familial hypertrophic cardiomyopathy (FHC). 3. Addition of regulatory proteins to the thin filament increases both the unloaded sliding speed and the isometric force exerted by myosin heads on the thin filaments. 4. Variation of thin filament activation by varying [Ca2+] or the fraction of CBMII/TnC bound to the thin filament at pCa 5, had little effect on the unloaded filament sliding speed until the fraction of the thin filament containing calcium bound to TnC was less than 0.15. These results suggest that [Ca2+] primarily affects the number of attached and cycling crossbridges. 5. The presence of the FHC TnT mutant increased the thin filament sliding speed but reduced the isometric force that heavy meromyosin exerted on regulated thin filaments. These latter results, together with the increased sliding speed and isometric force seen in the presence of regulatory proteins, suggest that thin filament regulatory proteins exert significant allosteric effects on the interaction of crossbridges with the thin filament.

Indexed as

ActinsAdenine NucleotidesAmino Acid SubstitutionAnimalsCattleHeartIsometric ContractionModels, BiologicalMovementMuscle, SkeletalMyocardiumPoint MutationRabbitsTropomyosinTroponinTroponin CActinsAdenine NucleotidesTropomyosinTroponinTroponin C

Identifiers

PMID10747195
PMCPMC2269863
OpenAlexW2124750538

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.