ArticleJournal of biophysics (Hindawi Publishing Corporation : Online)2009
Tropomyosin period 3 is essential for enhancement of isometric tension in thin filament-reconstituted bovine myocardium.
Article in Journal of biophysics (Hindawi Publishing Corporation : Online), 2009. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 15 papers.
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.
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.
Who cites it
15 citing papers in PubMed, 20 citations in OpenAlex.
- Structural Effects of Disease-Related Mutations in Actin-Binding Period 3 of Tropomyosin.Molecules (Basel, Switzerland) · 2021Article
- Mutations Q93H and E97K inInternational journal of molecular sciences · 2021Article
- Functional significance of HCM mutants of tropomyosin, V95A and D175N, studied withBiophysics and physicobiology · 2019Article
- Transmission of stability information through the N-domain of tropomyosin is interrupted by a stabilizing mutation (A109L) in the hydrophobic core of the stability control region (residues 97-118).The Journal of biological chemistry · 2014Article
- A study of tropomyosin's role in cardiac function and disease using thin-filament reconstituted myocardium.Journal of muscle research and cell motility · 2013Review
- Analysis of the molecular pathogenesis of cardiomyopathy-causing cTnT mutants I79N, ΔE96, and ΔK210.Biophysical journal · 2013Article
- A periodic pattern of evolutionarily conserved basic and acidic residues constitutes the binding interface of actin-tropomyosin.The Journal of biological chemistry · 2013Article
- Regulation of actin-myosin interaction by conserved periodic sites of tropomyosin.Proceedings of the National Academy of Sciences of the United States of America · 2012Article
- Article
- The role of tropomyosin domains in cooperative activation of the actin-myosin interaction.Journal of molecular biology · 2011Article
- Enhanced active cross-bridges during diastole: molecular pathogenesis of tropomyosin's HCM mutations.Biophysical journal · 2011Article
- Thin filament-reconstituted skinned muscle fibers for the study of muscle physiology.Journal of biomedicine & biotechnology · 2011Review
- The role of tropomyosin isoforms and phosphorylation in force generation in thin-filament reconstituted bovine cardiac muscle fibres.Journal of muscle research and cell motility · 2010Article
- What makes tropomyosin an actin binding protein? A perspective.Journal of structural biology · 2010Article
- Periodicities designed in the tropomyosin sequence and structure define its functions.BioarchitectureReview
Corrections and comments
PubMed lists nothing against this paper. Absence here is not a guarantee, only a check that was made.
Authors and funding
5 authors at 2 institutions in 1 country.
Funding
Abstract
Tropomyosin (Tm) consists of 7 quasiequivalent repeats known as "periods," and its specific function may be associated with these periods. To test the hypothesis that either period 2 or 3 promotes force generation by inducing a positive allosteric effect on actin, we reconstituted the thin filament with mutant Tm in which either period 2 (Delta2Tm) or period 3 (Delta3Tm) was deleted. We then studied: isometric tension, stiffness, 6 kinetic constants, and the pCa-tension relationship. N-terminal acetylation of Tm did not cause any differences. The isometric tension in Delta2Tm remained unchanged, and was reduced to approximately 60% in Delta3Tm. Although the kinetic constants underwent small changes, the occupancy of strongly attached cross-bridges was not much different. The Hill factor (cooperativity) did not differ significantly between Delta2Tm (1.79 +/- 0.19) and the control (1.73 +/- 0.21), or Delta3Tm (1.35 +/- 0.22) and the control. In contrast, pCa(50) decreased slightly in Delta2Tm (5.11 +/- 0.07), and increased significantly in Delta3Tm (5.57 +/- 0.09) compared to the control (5.28 +/- 0.04). These results demonstrate that, when ions are present at physiological concentrations in the muscle fiber system, period 3 (but not period 2) is essential for the positive allosteric effect that enhances the interaction between actin and myosin, and increases isometric force of each cross-bridge.
Identifiers
What OpenQuestion holds
Registered trials
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.