ArticleThe Journal of cell biology1979
Chick brain actin and myosin. Isolation and characterization.
Article in The Journal of cell biology, 1979. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 13 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
13 citing papers in PubMed, 49 citations in OpenAlex.
- Expression of actin and myosin genes during PC12 cell differentiation.Neurochemical research · 1991Article
- Incorporation of nascent myosin heavy chains into thick filaments of cardiac myocytes in thyroid-treated rabbits.The Journal of cell biology · 1987Article
- Activation of myosin ATPase by actin isolated from cultured BHK cells and the effect of gelsolin.Journal of muscle research and cell motility · 1987Article
- Purification, characterization and substrate specificity of calmodulin-dependent myosin light-chain kinase from bovine brain.The Biochemical journal · 1987Article
- Myosin from pancreatic acinar carcinoma cells. Isolation, characterization and demonstration of heavy- and light-chain phosphorylation.The Biochemical journal · 1987Article
- Role of stress fiber-like structures in assembling nascent myofibrils in myosheets recovering from exposure to ethyl methanesulfonate.The Journal of cell biology · 1986Article
- The relationship between stress fiber-like structures and nascent myofibrils in cultured cardiac myocytes.The Journal of cell biology · 1984Article
- Differences in the organization of actin in the growth cones compared with the neurites of cultured neurons from chick embryos.The Journal of cell biology · 1983Article
- Phosphorylation and actin activation of brain myosin.The EMBO journal · 1983Article
- Actin from pig and rat uterus.The Biochemical journal · 1981Article
- Physical and enzymatic properties of myosin from porcine brain.Biophysical journal · 1980Article
- Identification of recombinant phages containing sequences from different rat myosin heavy chain genes.Nucleic acids research · 1980Article
- Molecular motors in axonal transport. Cellular and molecular biology of kinesin.Molecular neurobiologyReview
Corrections and comments
PubMed lists nothing against this paper. Absence here is not a guarantee, only a check that was made.
Authors and funding
2 authors at 1 institution in 1 country.
Funding
No grant is acknowledged in the PubMed record.
Abstract
Brain actin extracted from an acetone powder of chick brains was purified by a cycle of polymerization-depolymerization followed by molecular sieve chromatography. The brain actin had a subunit molecular weight of 42,000 daltons as determined by co-electrophoresis with muscle actin. It underwent salt-dependent g to f transformation to form double helical actin filaments which could be "decorated" by muscle myosin subfragment 1. A critical concentration for polymerization of 1.3 microM was determined by measuring either the change in viscosity or absorbance at 232 nm. Brain actin was also capable of stimulating the ATPase activity of muscle myosin. Brain myosin was isolated from whole chick brain by a procedure involving high salt extraction, ammonium sulfate fractionation and molecular sieve chromatography. The purified myosin was composed of a 200,000-dalton heavy chain and three lower molecular weight light chains. In 0.6 M KCl the brain myosin had ATPase activity which was inhibited by Mg++, stimulated by Ca++, and maximally activated by EDTA. When dialyzed against 0.1 M KCl, the brain myosin self-assembled into short bipolar filaments. The bipolar filaments associated with each other to form long concatamers, and this association was enhanced by high concentrations of Mg++ ion. The brain myosin did not interact with chicken skeletal muscle myosin to form hybrid filaments. Furthermore, antibody recognition studies demonstrated that myosins from chicken brain, skeletal muscle, and smooth muscle were unique.
Indexed as
Identifiers
What 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.