ArticleThe Biochemical journal1985
Preparation and characterization of bovine aortic actin.
Article in The Biochemical journal, 1985. 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
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
9 citing papers in PubMed, 20 citations in OpenAlex.
- Definition of a Ca2(+)-sensitive interface in the plasma gelsolin-actin complex.The Biochemical journal · 1991Article
- Comparative study of invertebrate actins: antigenic cross-reactivity versus sequence variability.Journal of muscle research and cell motility · 1989Article
- Structural and functional variations in skeletal-muscle and scallop muscle actins.The Biochemical journal · 1988Article
- A 36 kDa monomeric protein and its complex with a 10 kDa protein both isolated from bovine aorta are calpactin-like proteins that differ in their Ca2+-dependent calmodulin-binding and actin-severing properties.The Biochemical journal · 1988Article
- Antigenic probes locate a serum-gelsolin-interaction site on the C-terminal part of actin.The Biochemical journal · 1987Article
- Actin antibodies. Preparation and characterization of antibodies specific for smooth-muscle actin isoforms.The Biochemical journal · 1987Article
- Structural variations in actins. A study of the immunological reactivity of the N-terminal region.The Biochemical journal · 1986Article
- The thin filaments of smooth muscles.Journal of muscle research and cell motility · 1985Review
- Structural variations in actins. Biochemical and immunological tools for probing the structure of rabbit skeletal-muscle and bovine aortic actins.The Biochemical journal · 1985Article
Corrections and comments
PubMed lists nothing against this paper. Absence here is not a guarantee, only a check that was made.
Authors and funding
5 authors at 2 institutions in 1 country.
Funding
No grant is acknowledged in the PubMed record.
Abstract
A functional vascular smooth-muscle actin from bovine aorta was purified to homogeneity by an original method and was able to polymerize. Aortic actin is composed of two major isoforms and at least two minor ones. This actin was not phosphorylated by either cyclic AMP-dependent protein kinase or C kinase. The physical properties of aortic actin were found to be very similar to those of skeletal-muscle actin, except for amino acid composition (three tryptophan residues instead of four). The aortic actin and skeletal-muscle actin differ in the extent of activation of the Mg-dependent ATPase of skeletal-muscle myosin.
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.