ArticleJournal of muscle research and cell motility1988
Phosphorylatable serine residues are located in a non-helical tailpiece of a catch muscle myosin.
Article in Journal of muscle research and cell motility, 1988. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 9 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
9 citing papers in PubMed, 30 citations in OpenAlex.
- Mechanism of catch force: tethering of thick and thin filaments by twitchin.Journal of biomedicine & biotechnology · 2010Article
- Caenorhabditis elegans unc-82 encodes a serine/threonine kinase important for myosin filament organization in muscle during growth.Genetics · 2010Article
- Invertebrate muscles: thin and thick filament structure; molecular basis of contraction and its regulation, catch and asynchronous muscle.Progress in neurobiology · 2008Review
- Molecular basis of the catch state in molluscan smooth muscles: a catchy challenge.Journal of muscle research and cell motility · 2008Review
- Myorod, a thick filament protein in molluscan smooth muscles: isolation, polymerization and interaction with myosin.Journal of muscle research and cell motility · 2001Article
- A structural model for phosphorylation control of Dictyostelium myosin II thick filament assembly.The Journal of cell biology · 1999Article
- Hydrophobicity variations along the surface of the coiled-coil rod may mediate striated muscle myosin assembly in Caenorhabditis elegans.The Journal of cell biology · 1996Article
- A nucleation--elongation mechanism for the self-assembly of side polar sheets of smooth muscle myosin.The EMBO journal · 1991Article
- Monoclonal antibodies detect and stabilize conformational states of smooth muscle myosin.The Journal of cell biology · 1989Article
Corrections and comments
PubMed lists nothing against this paper. Absence here is not a guarantee, only a check that was made.
Authors and funding
3 authors at 1 institution in 1 country.
Funding
Abstract
Myosin from a molluscan catch muscle displays unusual properties: when phosphorylated in the rod by an endogenous heavy-chain kinase, myosin solubility is enhanced and the molecule folds (Castellani & Cohen, Proc. natn. Acad. Sci. U.S.A. 84, (1987) 4058-62). We have now localized the sites of phosphorylation to the carboxy-terminal end of the rod by selective proteolytic cleavage. Two major stretches of sequence, 18 and 21 residues long, have been identified, each containing a single residue of phosphoserine. Analysis of the amino-acid sequence of these two peptides indicates that they form a non-helical tailpiece. We discuss how phosphorylation of this tailpiece might influence enzymatic activity in catch muscle thick filaments.
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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.