ArticleProceedings of the National Academy of Sciences of the United States of America2004
Actin-destabilizing factors disrupt filaments by means of a time reversal of polymerization.
Article in Proceedings of the National Academy of Sciences of the United States of America, 2004. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 39 papers.
What it found
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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.
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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.
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Who cites it
39 citing papers in PubMed, 72 citations in OpenAlex.
- Multiple Mechanisms to Regulate Actin Functions: "Fundamental" Versus Lineage-Specific Mechanisms and Hierarchical Relationships.Biomolecules · 2025Review
- Cofilin Acts as a Booster for Progression of Malignant Tumors Represented by Glioma.Cancer management and research · 2022Review
- Near-atomic resolution for one state of F-actin.Structure (London, England : 1993) · 2015Article
- Article
- Coordination of the filament stabilizing versus destabilizing activities of cofilin through its secondary binding site on actin.Cytoskeleton (Hoboken, N.J.) · 2014Article
- Disulfide cross-linked antiparallel actin dimer.Biochemistry · 2013Article
- Quantitative analysis of approaches to measure cooperative phosphate release in polymerized actin.Biophysical journal · 2012Article
- Two deafness-causing (DFNA20/26) actin mutations affect Arp2/3-dependent actin regulation.The Journal of biological chemistry · 2012Article
- G146V mutation at the hinge region of actin reveals a myosin class-specific requirement of actin conformations for motility.The Journal of biological chemistry · 2012Article
- The instability of stabilization.Proceedings of the National Academy of Sciences of the United States of America · 2012Article
- mDia1 and formins: screw cap of the actin filament.Biophysics (Nagoya-shi, Japan) · 2012Review
- Cofilin-linked changes in actin filament flexibility promote severing.Biophysical journal · 2011Article
- Structural studies on maturing actin filaments.Bioarchitecture · 2011Article
- An actin cytoskeleton with evolutionarily conserved functions in the absence of canonical actin-binding proteins.Proceedings of the National Academy of Sciences of the United States of America · 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
- Actin filament remodeling by actin depolymerization factor/cofilin.Proceedings of the National Academy of Sciences of the United States of America · 2010Article
- ADF/cofilin: a functional node in cell biology.Trends in cell biology · 2010Review
- Differential effects of caldesmon on the intermediate conformational states of polymerizing actin.The Journal of biological chemistry · 2010Article
- New insights into the regulation of the actin cytoskeleton by tropomyosin.International review of cell and molecular biology · 2010Review
Corrections and comments
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Authors and funding
7 authors at 2 institutions in 1 country.
Funding
Abstract
Actin, one of the most highly conserved and abundant eukaryotic proteins, is constantly being polymerized and depolymerized within cells as part of cellular motility, tissue formation and repair, and embryonic development. Many proteins exist that bind to monomeric or filamentous (F) forms of actin to regulate the polymerization state. It has become increasingly apparent that the ability of different proteins to bind to and regulate actin filament dynamics depends on the ability of the filament to exist in altered conformations. Yet, little is known about how these conformational changes occur at the molecular level. We have destabilized F-actin filaments by forming a disulfide that locks the "hydrophobic plug" to the body of the actin subunit or by altering the C terminus of actin with a tetramethylrhodamine label. We also examined F-actin filaments at short times after the initiation of polymerization. In all three cases, a substantial fraction of protomers can be found in a "tilted" state that also is induced by actin depolymerizing factor/cofilin proteins. These observations suggest that F-actin filaments are annealed over time into a stable filament and that actin-depolymerizing proteins can effect a time reversal of polymerization.
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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.