ReviewBiophysical journal1995
Role of skeletal and smooth muscle myosin light chains.
Review in Biophysical journal, 1995. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 11 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
11 citing papers in PubMed, 49 citations in OpenAlex.
- Myosin light chain proteins cooperatively promote sarcomere growth in fast-twitch muscle.Nature communications · 2026Article
- Reassessing the unifying hypothesis for hypercontractility caused by myosin mutations in hypertrophic cardiomyopathy.The EMBO journal · 2024Review
- Intraluminal chloride regulates lung branching morphogenesis: involvement of PIEZO1/PIEZO2.Respiratory research · 2023Article
- Single-molecule analysis reveals that regulatory light chains fine-tune skeletal myosin II function.The Journal of biological chemistry · 2020Article
- Distinct sequences and post-translational modifications in cardiac atrial and ventricular myosin light chains revealed by top-down mass spectrometry.Journal of molecular and cellular cardiology · 2017Article
- Article
- Article
- Common structural motifs for the regulation of divergent class II myosins.The Journal of biological chemistry · 2010Review
- Influence of fast and slow alkali myosin light chain isoforms on the kinetics of stretch-induced force transients of fast-twitch type IIA fibres of rat.Pflugers Archiv : European journal of physiology · 2008Article
- Dependence of cross-bridge kinetics on myosin light chain isoforms in rabbit and rat skeletal muscle fibres.The Journal of physiology · 2006Article
- Thiophosphorylation of myosin light chain increases rigor stiffness of rabbit smooth muscle.The Journal of physiology · 1998Article
Corrections and comments
PubMed lists nothing against this paper. Absence here is not a guarantee, only a check that was made.
Authors and funding
2 authors at 1 institution in 1 country.
Funding
Abstract
A persistent problem with the rotating cross-bridge model for muscle contraction has been the inability to detect any large conformational changes within the myosin molecule to account for a working stroke of 5-10 nm. The recent crystal structure of myosin subfragment-1 suggests a solution to this problem by showing the presence of two distinct domains: a catalytic or motor domain, from which extends a long, 8.5-nm alpha-helix that is stabilized by the regulatory and essential light chains. Rayment et al. (1993) proposed that closure of a cleft in the motor domain could rotate the light chain-binding domain by a sufficient distance to account for the power stroke. With the development of new in vitro motility assays, and the ability to prepare unusual myosins by biochemical and molecular biological methods, we can now examine this hypothesis and explore the role of the light chains in generating force and movement. Here we will review some of these recent data and outline a possible mechanism for how light chains regulate contractile properties.
Indexed as
Identifiers
7787054PMC1281891W1410674031What 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.