ArticleFEBS letters2012
Myosin filament assembly requires a cluster of four positive residues located in the rod domain.
Article in FEBS letters, 2012. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 5 papers.
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
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.
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Who cites it
5 citing papers in PubMed, 14 citations in OpenAlex.
- Research into the physiology of myosins - a personal odyssey.European journal of translational myology · 2025Article
- Thick filament-associated myosin undergoes frequent replacement at the tip of the thick filament.FEBS open bio · 2022Article
- High-intensity ultrasound improves the physical stability of myofibrillar protein emulsion at low ionic strength by destroying and suppressing myosin molecular assembly.Ultrasonics sonochemistry · 2021Article
- Myosin: Formation and maintenance of thick filaments.Animal science journal = Nihon chikusan Gakkaiho · 2019Review
- Skip residues modulate the structural properties of the myosin rod and guide thick filament assembly.Proceedings of the National Academy of Sciences of the United States of America · 2015Article
Corrections and comments
PubMed lists nothing against this paper. Absence here is not a guarantee, only a check that was made.
Authors and funding
4 authors at 1 institution in 1 country.
Funding
Abstract
Myosin has an intrinsic ability to organize into ordered thick filaments that mediate muscle contraction. Here, we use surface plasmon resonance and light scattering analysis to further characterize the molecular determinants that guide myosin filament assembly. Both assays identify a cluster of lysine and arginine residues as important for myosin polymerization in vitro. Moreover, in cardiomyocytes, replacement of these charged residues by alanine severely affects the incorporation of myosin into the distal ends of the sarcomere. Our findings show that a novel assembly element with a distinct charge profile is present at the C-terminus of sarcomeric myosins.
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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.