ArticleJournal of molecular biology2008
Millisecond time-resolved changes occurring in Ca2+-regulated myosin filaments upon relaxation.
Article in Journal of molecular biology, 2008. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 8 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.
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Who cites it
8 citing papers in PubMed.
- "QuickStainer": a rapid negative staining device for improved preservation of molecular structure.Journal of structural biology · 2026Article
- Differences between fast and slow muscles in scallops revealed through proteomics and transcriptomics.BMC genomics · 2018Article
- Unconventional Imaging Methods to Capture Transient Structures during Actomyosin Interaction.International journal of molecular sciences · 2018Review
- Interacting-heads motif has been conserved as a mechanism of myosin II inhibition since before the origin of animals.Proceedings of the National Academy of Sciences of the United States of America · 2018Article
- Structural basis of the relaxed state of a Ca2+-regulated myosin filament and its evolutionary implications.Proceedings of the National Academy of Sciences of the United States of America · 2013Article
- Potentiation in mouse lumbrical muscle without myosin light chain phosphorylation: is resting calcium responsible?The Journal of general physiology · 2013Article
- Role of the tail in the regulated state of myosin 2.Journal of molecular biology · 2011Article
- Negative staining and cryo-negative staining of macromolecules and viruses for TEM.Micron (Oxford, England : 1993) · 2011Review
Corrections and comments
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Authors and funding
2 authors.
Funding
Abstract
Contraction of many muscles is activated in part by the binding of Ca(2+) to, or phosphorylation of, the myosin heads on the surface of the thick filaments. In relaxed muscle, the myosin heads are helically ordered and undergo minimal interaction with actin. On Ca(2+) binding or phosphorylation, the head array becomes disordered, reflecting breakage of the head-head and other interactions that underlie the ordered structure. Loosening of the heads from the filament surface enables them to interact with actin filaments, bringing about contraction. On relaxation, the heads return to their ordered positions on the filament backbone. In scallop striated adductor muscle, the disordering that takes place on Ca(2+) binding occurs on the millisecond time scale, suggesting that it is a key element of muscle activation. Here we have studied the reverse process. Using time-resolved negative staining electron microscopy, we show that the rate of reordering on removal of Ca(2+) also occurs on the same physiological time scale. Direct observation of images together with analysis of their Fourier transforms shows that activated heads regain their axial ordering within 20 ms and become ordered in their final helical positions within 50 ms. This rapid reordering suggests that reformation of the ordered structure, and the head-head and other interactions that underlie it, is a critical element of the relaxation process.
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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.