ReviewMolecular and cellular biochemistry1999
Regulation by molluscan myosins.
Review in Molecular and cellular biochemistry, 1999. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 21 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
21 citing papers in PubMed, 48 citations in OpenAlex.
- Structural basis of the super- and hyper-relaxed states of myosin II.The Journal of general physiology · 2022Review
- CRISPR/Cas9 Mediated High Efficiency Knockout of Myosin Essential Light Chain Gene in the Pacific Oyster (Crassostrea Gigas).Marine biotechnology (New York, N.Y.) · 2021Article
- Population structure, genetic connectivity, and adaptation in the Olympia oyster (Evolutionary applications · 2019Article
- Calcium-mediated regulation of recombinant hybrids of full-length Physarum myosin heavy chain with Physarum/scallop myosin light chains.Acta biochimica et biophysica Sinica · 2016Article
- Molecular evolution of troponin I and a role of its N-terminal extension in nematode locomotion.Cytoskeleton (Hoboken, N.J.) · 2016Article
- Temperature dependent measurements reveal similarities between muscle and non-muscle myosin motility.Journal of muscle research and cell motility · 2012Article
- Crystal structure of a phosphorylated light chain domain of scallop smooth-muscle myosin.Biophysical journal · 2011Article
- Initial diameter of the polar body contractile ring is minimized by the centralspindlin complex.Developmental biology · 2011Article
- Head-head interaction characterizes the relaxed state of Limulus muscle myosin filaments.Journal of molecular biology · 2009Article
- Ca2+ -induced tropomyosin movement in scallop striated muscle thin filaments.Journal of molecular biology · 2008Article
- Invertebrate muscles: thin and thick filament structure; molecular basis of contraction and its regulation, catch and asynchronous muscle.Progress in neurobiology · 2008Review
- Blebbistatin stabilizes the helical order of myosin filaments by promoting the switch 2 closed state.Biophysical journal · 2008Article
- Millisecond time-resolved changes occurring in Ca2+-regulated myosin filaments upon relaxation.Journal of molecular biology · 2008Article
- Head-head and head-tail interaction: a general mechanism for switching off myosin II activity in cells.Molecular biology of the cell · 2008Article
- Molecular basis of the catch state in molluscan smooth muscles: a catchy challenge.Journal of muscle research and cell motility · 2008Review
- Myosin cross-bridge kinetics and the mechanism of catch.Biophysical journal · 2007Article
- Evaluation of the symmetric model for myosin-linked regulation: effect of site-directed mutations in the regulatory light chain on scallop myosin.The Biochemical journal · 2003Article
- Ionic interactions play a role in the regulatory mechanism of scallop heavy meromyosin.Biophysical journal · 2003Article
- A kinetic model of the co-operative binding of calcium and ADP to scallop (Argopecten irradians) heavy meromyosin.The Biochemical journal · 2002Article
- Three-dimensional image reconstruction of dephosphorylated smooth muscle heavy meromyosin reveals asymmetry in the interaction between myosin heads and placement of subfragment 2.Proceedings of the National Academy of Sciences of the United States of America · 2001Article
Corrections and comments
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Authors and funding
3 authors at 1 institution in 1 country.
Funding
Abstract
Molluscan myosins are regulated molecules that control muscle contraction by the selective binding of calcium. The essential and the regulatory light chains are regulatory subunits. Scallop myosin is the favorite material for studying the interactions of the light chains with the myosin heavy chain since the regulatory light chains can be reversibly removed from it and its essential light chains can be exchanged. Mutational and structural studies show that the essential light chain binds calcium provided that the Ca-binding loop is stabilized by specific interactions with the regulatory light chain and the heavy chain. The regulatory light chains are inhibitory subunits. Regulation requires the presence of both myosin heads and an intact headrod junction. Heavy meromyosin is regulated and shows cooperative features of activation while subfragment-1 is non-cooperative. The myosin heavy chains of the functionally different phasic striated and the smooth catch muscle myosins are products of a single gene, the isoforms arise from alternative splicing. The differences between residues of the isoforms are clustered at surface loop-1 of the heavy chain and account for the different ATPase activity of the two muscle types. Catch muscles contain two regulatory light chain isoforms, one phosphorylatable by gizzard myosin light chain kinase. Phosphorylation of the light chain does not alter ATPase activity. We could not find evidence that light chain phosphorylation is responsible for the catch state.
Indexed as
Identifiers
10098969W1585870293What 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.