ArticleProceedings of the National Academy of Sciences of the United States of America1981
Characterization of brevin, a serum protein that shortens actin filaments.
Article in Proceedings of the National Academy of Sciences of the United States of America, 1981. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 18 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
18 citing papers in PubMed, 91 citations in OpenAlex.
- Dominant negative mutant actins identified in flightless Drosophila can be classified into three classes.The Journal of biological chemistry · 2010Article
- Angiopathic consequences of saturating the plasma scavenger system for actin.Proceedings of the National Academy of Sciences of the United States of America · 1990Article
- Gelsolin modulation in epithelial and stromal cells of mammary carcinoma.The American journal of pathology · 1989Article
- Microheterogeneity of actin gels formed under controlled linear shear.The Journal of cell biology · 1988Article
- Role of group-specific component (vitamin D binding protein) in clearance of actin from the circulation in the rabbit.The Journal of clinical investigation · 1988Article
- Identification of a polyphosphoinositide-modulated domain in gelsolin which binds to the sides of actin filaments.The Journal of cell biology · 1988Article
- The F-actin capping proteins of Physarum polycephalum: cap42(a) is very similar, if not identical, to fragmin and is structurally and functionally very homologous to gelsolin; cap42(b) is Physarum actin.The EMBO journal · 1987Article
- Microinjection of gelsolin into living cells.The Journal of cell biology · 1987Article
- Actin-severing activity copurifies with phosphofructokinase.Proceedings of the National Academy of Sciences of the United States of America · 1986Article
- The actin filament-severing domain of plasma gelsolin.The Journal of cell biology · 1986Article
- Role of plasma gelsolin and the vitamin D-binding protein in clearing actin from the circulation.The Journal of clinical investigation · 1986Article
- Definition of an N-terminal actin-binding domain and a C-terminal Ca2+ regulatory domain in human brevin.The Journal of cell biology · 1986Article
- Secretory cell actin-binding proteins: identification of a gelsolin-like protein in chromaffin cells.The Journal of cell biology · 1986Article
- Immuno-identification of Ca2+-induced conformational changes in human gelsolin and brevin.The Journal of cell biology · 1986Article
- A re-evaluation of cytoplasmic gelsolin localization.The Journal of cell biology · 1986Article
- Kinetic analysis of F-actin depolymerization in the presence of platelet gelsolin and gelsolin-actin complexes.The Journal of cell biology · 1985Article
- The role of cytoskeletal and cytocontractile elements in pathologic processes.The American journal of pathology · 1983Review
- Article
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
Abstract
We have purified a protein from rabbit serum with a molecular weight of 90,000 that inhibits the polymerization of actin measured viscometrically and that we have named "brevin" (from the Latin breviare, to shorten). From the extent of purification, we estimate that this inhibitor constitutes 0.3% of the total protein in plasma and serum. Brevin is also present in sera from humans and rats. Almost all of the activity in blood is extracellular; only 1% is present in platelets or other cellular elements. Several lines of evidence indicate that brevin is the same protein as the factor described by Fagraeus and Norberg [Fagraeus, A. & Norberg, R. (1978) Curr. Top. Microbiol. Immunol. 82, 1-13] as an actin-depolymerizing factor (ADF). If ADF and brevin are identical, then "ADF" is an inappropriate name because we find that the protein shortens actin filaments without depolymerizing them. Thus, brevin causes little change in the critical concentration of monomeric actin, even though the inhibitor binds to monomeric actin complexed to DNase I-agarose. Binding of brevin to filaments was demonstrated by sedimenting the inhibitor with F-actin. From the amounts of actin and brevin sedimented, and from the lengths of filaments measured by electron microscopy, we calculated that the stoichiometry of binding is one brevin molecule per filament over a wide range of inhibitor concentrations. This stoichiometry suggests that brevin inhibits polymerization by binding at the end of elongating actin filaments, a mechanism similar to that proposed for several intracellular actin-binding proteins and for the cytochalasins. Its abundance suggests that brevin plays an important physiological role in serum, but one not directly concerned with intracellular motility. Therefore its relationship to cytoplasmic actin-binding proteins remains to be determined.
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.