ArticleJournal of muscle research and cell motility1994
Regulatory domains of myosins: influence of heavy chain on Ca(2+)-binding.
Article in Journal of muscle research and cell motility, 1994. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 10 papers.
What it found
Each row is one number read from the abstract, on the scale the paper reported it, with its interval. Left of the dashed line favours the treatment, right favours the comparator. Under each row is the sentence it came from. New to these charts? A ten-minute tutorial.
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.
Neither the registry nor the abstract names a trial number. If this is a trial report, that itself is worth knowing.
Who cites it
10 citing papers in PubMed.
- Visualizing key hinges and a potential major source of compliance in the lever arm of myosin.Proceedings of the National Academy of Sciences of the United States of America · 2011Article
- Mechanism of catch force: tethering of thick and thin filaments by twitchin.Journal of biomedicine & biotechnology · 2010Article
- The on-off switch in regulated myosins: different triggers but related mechanisms.Journal of molecular biology · 2009Article
- Invertebrate muscles: thin and thick filament structure; molecular basis of contraction and its regulation, catch and asynchronous muscle.Progress in neurobiology · 2008Review
- Regulation by molluscan myosins.Molecular and cellular biochemistry · 1999Review
- Microsecond rotational dynamics of spin-labeled myosin regulatory light chain induced by relaxation and contraction of scallop muscle.Biochemistry · 1998Article
- Amino-acid sequence of squid myosin heavy chain.Journal of muscle research and cell motility · 1998Article
- Sequence variations in the surface loop near the nucleotide binding site modulate the ATP turnover rates of molluscan myosins.Journal of muscle research and cell motility · 1996Article
- Role of essential light chain EF hand domains in calcium binding and regulation of scallop myosin.Proceedings of the National Academy of Sciences of the United States of America · 1995Article
- Role of myosin light chains.Journal of muscle research and cell motility · 1994Review
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.
Funding
Abstract
Light chain binding domains of rabbit skeletal, turkey gizzard and scallop myosin comprised of equimolar amounts of a short heavy chain fragment, essential light chain, and regulatory light chain have been obtained following extensive tryptic digestion. These complexes that are analogous to the regulatory domain prepared previously from scallop myosin by digestion with clostripain resist proteolysis due to the mutual protection of the heavy chain and the light chains, and are common structural features of the myosins studied. Specific Ca(2+)-binding by the regulatory domains reflects the behaviour of intact myosin; only scallop regulatory domain has a specific Ca(2+)-binding site. The heavy chain fragments of the different regulatory domains have been isolated under denaturing conditions and reconstituted with scallop essential light chain and scallop regulatory light chain or turkey gizzard regulatory light chain to yield regulatory domain hybrids. Hybrids containing the turkey gizzard regulatory light chain were used in Ca(2+)-binding studies since they were far more stable than their counterparts with the scallop regulatory light chain. The gizzard hybrid binds Ca2+ with a comparable specificity but somewhat lower affinity than native scallop regulatory domain. The rabbit regulatory domain hybrid also binds Ca2+, although with a reduced affinity and specificity. The results indicate that Ca(2+)-binding ability is determined by the light chains and modified by the heavy chains.
Indexed as
Identifiers
7860702What 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.