ArticleThe Biochemical journal2003
Interactions of the two heads of scallop (Argopecten irradians) heavy meromyosin with actin: influence of calcium and nucleotides.
Article in The Biochemical journal, 2003. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 6 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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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
6 citing papers in PubMed, 16 citations in OpenAlex.
- The biochemically defined super relaxed state of myosin-A paradox.The Journal of biological chemistry · 2024Article
- Biochemical Activities of the Wiskott-Aldrich Syndrome Homology Region 2 Domains of Sarcomere Length Short (SALS) Protein.The Journal of biological chemistry · 2016Article
- Modeling smooth muscle myosin's two heads: long-lived enzymatic roles and phosphorylation-dependent equilibria.Biophysical journal · 2010Article
- Invertebrate muscles: thin and thick filament structure; molecular basis of contraction and its regulation, catch and asynchronous muscle.Progress in neurobiology · 2008Review
- Calcium regulates scallop muscle by changing myosin flexibility.European biophysics journal : EBJ · 2006Article
- 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
Corrections and comments
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Authors and funding
3 authors at 1 institution in 1 country.
Funding
Abstract
We recently proposed a co-operative model for the influence of calcium and ADP on scallop ( Argopecten irradians ) muscle heavy meromyosin (scHMM), in which scHMM exists in two conformations (designated 'off' and 'on'), and calcium and ADP are allosteric effectors of the equilibrium between the off and on conformations [Nyitrai, Szent-Gyorgyi and Geeves (2002) Biochem. J. 365, 19-30]. Here we examine the influence of actin on scHMM. In the absence of nucleotide, both heads of scHMM bind very tightly to actin, independent of the presence of calcium. In the absence of calcium, ADP dissociates scHMM from actin completely, and little evidence of ternary complex formation can be found (actin affinity >20 microM). The off state of scHMM therefore does not interact with actin. In the presence of calcium, ADP and actin lower each other's affinity for scHMM by 30-50-fold, although both heads remain strongly attached to actin (actin affinity 0.17 microM). Detailed analysis suggests that the second head contributes far more to the overall binding energy than is the case for mammalian skeletal muscle HMM. This is consistent with a different stereochemical relationship between the two heads in scallop and mammalian HMM molecules.
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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.