ArticleJournal of molecular biology2008
An unstable head-rod junction may promote folding into the compact off-state conformation of regulated myosins.
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.
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
8 citing papers in PubMed, 17 citations in OpenAlex.
- Cooperative & competitive binding of anti-myosin tail antibodies revealed by super-resolution microscopy.Archives of biochemistry and biophysics · 2023Article
- Double-headed binding of myosin II to F-actin shows the effect of strain on head structure.Journal of structural biology · 2023Article
- The myosin II coiled-coil domain atomic structure in its native environment.Proceedings of the National Academy of Sciences of the United States of America · 2021Article
- Article
- The central role of the tail in switching off 10S myosin II activity.The Journal of general physiology · 2019Article
- 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
- Structure, interactions and function of the N-terminus of cardiac myosin binding protein C (MyBP-C): who does what, with what, and to whom?Journal of muscle research and cell motility · 2012Review
- Three-dimensional reconstruction of tarantula myosin filaments suggests how phosphorylation may regulate myosin activity.Journal of molecular biology · 2008Article
Corrections and comments
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Authors and funding
10 authors at 3 institutions in 3 countries.
Funding
Abstract
The N-terminal region of myosin's rod-like subfragment 2 (S2) joins the two heads of this dimeric molecule and is key to its function. Previously, a crystal structure of this predominantly coiled-coil region was determined for a short fragment (51 residues plus a leucine zipper) of the scallop striated muscle myosin isoform. In that study, the N-terminal 10-14 residues were found to be disordered. We have now determined the structure of the same scallop peptide in three additional crystal environments. In each of two of these structures, improved order has allowed visualization of the entire N-terminus in one chain of the dimeric peptide. We have also compared the melting temperatures of this scallop S2 peptide with those of analogous peptides from three other isoforms. Taken together, these experiments, along with examination of sequences, point to a diminished stability of the N-terminal region of S2 in regulated myosins, compared with those myosins whose regulation is thin filament linked. It seems plain that this isoform-specific instability promotes the off-state conformation of the heads in regulated myosins. We also discuss how myosin isoforms with varied thermal stabilities share the basic capacity to transmit force efficiently in order to produce contraction in their on states.
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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.