ReviewJournal of muscle research and cell motility2015
Non-crossbridge forces in activated striated muscles: a titin dependent mechanism of regulation?
Review in Journal of muscle research and cell motility, 2015. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 14 papers, 1 of them a synthesis that pooled it.
What it found
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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
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Who cites it
14 citing papers in PubMed, 1 synthesis or guideline pooled it, 39 citations in OpenAlex.
- Mechanisms underlying performance impairments following prolonged static stretching without a comprehensive warm-up.European journal of applied physiology · 2021Pooled it
- Eccentric muscle contractions: from single muscle fibre to whole muscle mechanics.Pflugers Archiv : European journal of physiology · 2023Review
- Muscle thixotropy-where are we now?Journal of applied physiology (Bethesda, Md. : 1985) · 2019Review
- A mechanical model of the half-sarcomere which includes the contribution of titin.Journal of muscle research and cell motility · 2019Article
- Does partial titin degradation affect sarcomere length nonuniformities and force in active and passive myofibrils?American journal of physiology. Cell physiology · 2018Article
- A Spatially Explicit Model Shows How Titin Stiffness Modulates Muscle Mechanics and Energetics.Integrative and comparative biology · 2018Article
- Basic science and clinical use of eccentric contractions: History and uncertainties.Journal of sport and health science · 2018Review
- Phosphate increase during fatigue affects crossbridge kinetics in intact mouse muscle at physiological temperature.The Journal of physiology · 2017Article
- Physiological Mechanisms of Eccentric Contraction and Its Applications: A Role for the Giant Titin Protein.Frontiers in physiology · 2017Review
- Thick filament mechano-sensing is a calcium-independent regulatory mechanism in skeletal muscle.Nature communications · 2016Article
- The increase in non-cross-bridge forces after stretch of activated striated muscle is related to titin isoforms.American journal of physiology. Cell physiology · 2016Article
- Effects of aging, exercise, and disease on force transfer in skeletal muscle.American journal of physiology. Endocrinology and metabolism · 2015Review
- Editorial on EMC 2014 special issue.Journal of muscle research and cell motility · 2015Article
- Article
Corrections and comments
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Authors and funding
6 authors at 3 institutions in 3 countries.
Funding
Abstract
When skeletal muscles are stretched during activation in the absence of myosin-actin interactions, the force increases significantly. The force remains elevated throughout the activation period. The mechanism behind this non-crossbridge force, referred to as static tension, is unknown and generates debate in the literature. It has been suggested that the static tension is caused by Ca(2+)-induced changes in the properties of titin molecules that happens during activation and stretch, but a comprehensive evaluation of such possibility is still lacking. This paper reviews the general characteristics of the static tension, and evaluates the proposed mechanism by which titin may change the force upon stretch. Evidence is presented suggesting that an increase in intracellular Ca(2+) concentration leads to Ca(2+) binding to the PEVK region of titin. Such binding increases titin stiffness, which increases the overall sarcomere stiffness and causes the static tension. If this form of Ca(2+)-induced increase in titin stiffness is confirmed in future studies, it may have large implications for understating of the basic mechanisms of muscle contraction.
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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.