ReviewJournal of muscle research and cell motility1992
Tightly-bound divalent cation of actin.
Review in Journal of muscle research and cell motility, 1992. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 41 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
41 citing papers in PubMed, 139 citations in OpenAlex.
- Recycling of the actin monomer pool limits the lifetime of network turnover.The EMBO journal · 2023Article
- Mechanism of actin filament nucleation.Biophysical journal · 2021Article
- Myopathy-Sensitive G-Actin Segment 227-235 Is Involved in Salt-Induced Stabilization of Contacts within the Actin Filament.International journal of molecular sciences · 2021Article
- The Roles of Skin Fibroblasts at Local Acupoints in Chrono-Acupuncture.Pain research & management · 2020Article
- Atomic view into Plasmodium actin polymerization, ATP hydrolysis, and fragmentation.PLoS biology · 2019Article
- Structural evidence for the roles of divalent cations in actin polymerization and activation of ATP hydrolysis.Proceedings of the National Academy of Sciences of the United States of America · 2018Article
- Redox regulation of the actin cytoskeleton and its role in the vascular system.Free radical biology & medicine · 2017Review
- Cations Stiffen Actin Filaments by Adhering a Key Structural Element to Adjacent Subunits.The journal of physical chemistry. B · 2016Article
- Actin polymerization is stimulated by actin cross-linking protein palladin.The Biochemical journal · 2016Article
- Regulation of actin by ion-linked equilibria.Biophysical journal · 2013Review
- Organization of F-actin by Fesselin (avian smooth muscle synaptopodin 2).Biochemistry · 2013Article
- ATP and ADP actin states.Biopolymers · 2013Article
- Identification of cation-binding sites on actin that drive polymerization and modulate bending stiffness.Proceedings of the National Academy of Sciences of the United States of America · 2012Article
- The effect of toxins on inorganic phosphate release during actin polymerization.European biophysics journal : EBJ · 2011Article
- Conformational dynamics of actin: effectors and implications for biological function.Cytoskeleton (Hoboken, N.J.) · 2010Review
- The kinetics of cooperative cofilin binding reveals two states of the cofilin-actin filament.Biophysical journal · 2010Article
- In vivo reorganization of the actin cytoskeleton in leaves of Nicotiana tabacum L. transformed with plastin-GFP. Correlation with light-activated chloroplast responses.BMC plant biology · 2009Article
- EFFECT OF PHALLOIDIN ON FILAMENTS POLYMERIZED FROM HEART MUSCLE ADP-ACTIN MONOMERS.Journal of thermal analysis and calorimetry · 2009Article
- Phenotypes induced by NM causing alpha-skeletal muscle actin mutants in fibroblasts, Sol 8 myoblasts and myotubes.BMC research notes · 2009Article
- Development of free-energy-based models for chaperonin containing TCP-1 mediated folding of actin.Journal of the Royal Society, Interface · 2008Review
Corrections and comments
PubMed lists nothing against this paper. Absence here is not a guarantee, only a check that was made.
Authors and funding
4 authors at 2 institutions in 1 country.
Funding
Abstract
Actin is known to undergo reversible monomer-polymer transitions that coincide with various cell activities such as cell shape changes, locomotion, endocytosis and exocytosis. This dynamic state of actin filament self-assembly and disassembly is thought to be regulated by the properties of the monomeric actin molecule and in vivo by the influence of actin-associated proteins. Of major importance to the properties of the monomeric actin molecule are the presence of one tightly-bound ATP and one tightly-bound divalent cation per molecule. In vivo the divalent cation is thought to be Mg2+ (Mg-actin) but in vitro standard purification procedures result in the preparation of Ca-actin. The affinity of actin for a divalent cation at the tight binding site is in the nanomolar range, much higher than earlier thought. The binding kinetics of Mg2+ and Ca2+ at the high affinity site on actin are considered in terms of a simple competitive binding mechanism. This model adequately describes the published observations regarding divalent cation exchange on actin. The effects of the tightly-bound cation, Mg2+ or Ca2+, on nucleotide binding and exchange on actin, actin ATP hydrolysis activity and nucleation and polymerization of actin are discussed. From the characteristics that are reviewed, it is apparent that the nature of the bound divalent cation has a significant effect on the properties of actin.
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.