ArticleBiophysical journal2007
Interaction forces between F-actin and titin PEVK domain measured with optical tweezers.
Article in Biophysical journal, 2007. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 48 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
48 citing papers in PubMed, 107 citations in OpenAlex.
- TTNCell reports · 2026Article
- Mechanobiological Specialization of Choroid Plexus Macrophages Defined by Titin Expression.bioRxiv : the preprint server for biology · 2026Article
- Titin's Intrinsically Disordered PEVK Domain Modulates Actin Polymerization.International journal of molecular sciences · 2025Article
- Impact of lengthening velocity on the generation of eccentric force by slow-twitch muscle fibers in long stretches.Pflugers Archiv : European journal of physiology · 2024Article
- Article
- Eccentric muscle contractions: from single muscle fibre to whole muscle mechanics.Pflugers Archiv : European journal of physiology · 2023Review
- Ultrastructural and kinetic evidence support that thick filaments slide through the Z-disc.Journal of the Royal Society, Interface · 2022Article
- Application of optical tweezers in cardiovascular research: More than just a measuring tool.Frontiers in bioengineering and biotechnology · 2022Review
- The titin N2B and N2A regions: biomechanical and metabolic signaling hubs in cross-striated muscles.Biophysical reviews · 2021Review
- Titin N2A Domain and Its Interactions at the Sarcomere.International journal of molecular sciences · 2021Review
- Power Amplification Increases With Contraction Velocity During Stretch-Shortening Cycles of Skinned Muscle Fibers.Frontiers in physiology · 2021Article
- Non-cross Bridge Viscoelastic Elements Contribute to Muscle Force and Work During Stretch-Shortening Cycles: Evidence From Whole Muscles and Permeabilized Fibers.Frontiers in physiology · 2021Article
- The Poly-E motif in Titin's PEVK region undergoes pH dependent conformational changes.Biochemistry and biophysics reports · 2020Article
- N2A Titin: Signaling Hub and Mechanical Switch in Skeletal Muscle.International journal of molecular sciences · 2020Review
- Calcium-dependent titin-thin filament interactions in muscle: observations and theory.Journal of muscle research and cell motility · 2020Review
- Cross-Bridges and Sarcomeric Non-cross-bridge Structures Contribute to Increased Work in Stretch-Shortening Cycles.Frontiers in physiology · 2020Article
- Evidence for Muscle Cell-Based Mechanisms of Enhanced Performance in Stretch-Shortening Cycle in Skeletal Muscle.Frontiers in physiology · 2020Review
- Current Understanding of Residual Force Enhancement: Cross-Bridge Component and Non-Cross-Bridge Component.International journal of molecular sciences · 2019Review
- Passive force enhancement in striated muscle.Journal of applied physiology (Bethesda, Md. : 1985) · 2019Review
- Muscle thixotropy-where are we now?Journal of applied physiology (Bethesda, Md. : 1985) · 2019Review
Corrections and comments
- Commented on by
Authors and funding
7 authors at 3 institutions in 2 countries.
Funding
No grant is acknowledged in the PubMed record.
Abstract
Titin is a giant protein that determines the elasticity of striated muscle and is thought to play important roles in numerous regulatory processes. Previous studies have shown that titin's PEVK domain interacts with F-actin, thereby creating viscous forces of unknown magnitude that may modulate muscle contraction. Here we measured, with optical tweezers, the forces necessary to dissociate F-actin from individual molecules of recombinant PEVK fragments rich either in polyE or PPAK motifs. Rupture forces at a stretch rate of 250 nm/s displayed a wide, nonnormal distribution with a peak at approximately 8 pN in the case of both fragments. Dynamic force spectroscopy experiments revealed low spontaneous off-rates that were increased even by low forces. The loading-rate dependence of rupture force was biphasic for polyE in contrast with the monophasic response observed for PPAK. Analysis of the molecular lengths at which rupture occurred indicated that there are numerous actin-binding regions along the PEVK fragments' contour, suggesting that the PEVK domain is a promiscuous actin-binding partner. The complexity of PEVK-actin interaction points to an adaptable viscoelastic mechanism that safeguards sarcomeric structural integrity in the relaxed state and modulates thixotropic behavior during contraction.
Indexed as
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.