ArticleThe Journal of cell biology1988
Gelsolin has three actin-binding sites.
Article in The Journal of cell biology, 1988. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 50 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
50 citing papers in PubMed.
- Mechanism of actin filament severing and capping by gelsolin.Nature structural & molecular biology · 2025Article
- Structures and mechanisms of actin ATP hydrolysis.Proceedings of the National Academy of Sciences of the United States of America · 2022Article
- Article
- Yersinia effector YopO uses actin as bait to phosphorylate proteins that regulate actin polymerization.Nature structural & molecular biology · 2015Article
- ATP and ADP actin states.Biopolymers · 2013Article
- Prediction and dissection of widely-varying association rate constants of actin-binding proteins.PLoS computational biology · 2012Article
- Actin filament severing by cofilin is more important for assembly than constriction of the cytokinetic contractile ring.The Journal of cell biology · 2011Article
- Mammalian tropomodulins nucleate actin polymerization via their actin monomer binding and filament pointed end-capping activities.The Journal of biological chemistry · 2010Article
- Modulation of actin structure and function by phosphorylation of Tyr-53 and profilin binding.Proceedings of the National Academy of Sciences of the United States of America · 2008Article
- Mapping the cofilin binding site on yeast G-actin by chemical cross-linking.Journal of molecular biology · 2008Article
- Characterization of the enzymatic activity of the actin cross-linking domain from the Vibrio cholerae MARTX Vc toxin.The Journal of biological chemistry · 2008Article
- Thymosin beta4 induces a conformational change in actin monomers.Biophysical journal · 2006Article
- Topological assignment of the N-terminal extension of plasma gelsolin to the gelsolin surface.The Biochemical journal · 2005Article
- Solution properties of tetramethylrhodamine-modified G-actin.Biophysical journal · 2003Article
- Steered molecular dynamics simulations on the "tail helix latch" hypothesis in the gelsolin activation process.Biophysical journal · 2002Article
- Mutational analysis of human profilin I reveals a second PI(4,5)-P2 binding site neighbouring the poly(L-proline) binding site.BMC biochemistry · 2002Article
- Actin dynamics in platelets.International review of cytology · 2002Review
- VASP protects actin filaments from gelsolin: an in vitro study with implications for platelet actin reorganizations.Cell motility and the cytoskeleton · 2000Article
- Murine adseverin (D5), a novel member of the gelsolin family, and murine adseverin are induced by interleukin-9 in T-helper lymphocytes.Molecular and cellular biology · 1998Article
- The interaction of Arp2/3 complex with actin: nucleation, high affinity pointed end capping, and formation of branching networks of filaments.Proceedings of the National Academy of Sciences of the United States of America · 1998Article
Corrections and comments
PubMed lists nothing against this paper. Absence here is not a guarantee, only a check that was made.
Authors and funding
1 author.
Funding
Abstract
Gelsolin, a Ca2+-modulated actin filament-capping and -severing protein, complexes with two actin monomers. Studies designed to localize binding sites on proteolytic fragments identify three distinct actin-binding peptides. 14NT, a 14-kD fragment that contains the NH2 terminal, will depolymerize F-actin. This peptide forms a 1:1 complex with G-actin which blocks the exchange of etheno-ATP from bound actin. The estimated association and dissociation rates for this complex are 0.3 microM-1 s-1 and 1.35 x 10(-6) s-1 which gives a maximum calculated Kd = 4.5 x 10(-12) M. 26NT, the adjacent peptide on the NH2-terminal half of gelsolin, binds to both G- and F-actin. This fragment has little or no intrinsic severing activity and will bind to F-actin to nearly stoichiometric ratios. The interactions of 14NT and 26NT with actin are largely Ca2+ independent and one of these sites, probably 14NT, is the EGTA-stable site identified in the intact protein. 41CT, the COOH-terminal half of gelsolin, forms a rapidly reversible 1:1 complex with actin, Kd = 25 nM, that slows but does not block etheno-ATP exchange. This interaction is Ca2+ dependent and is the exchangeable site in the intact protein. One of these sites is hidden in the intact protein, but cleavage into half fragments exposes all three and removes the Ca2+ dependence of severing.
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.