ArticleThe Journal of cell biology1994
Determination of the alpha-actinin-binding site on actin filaments by cryoelectron microscopy and image analysis.
Article in The Journal of cell biology, 1994. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 52 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.
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.
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Who cites it
52 citing papers in PubMed.
- Alpha-actinin-1, profilin-1, filamin-A, integrin alpha-M and glutathione synthase were identified to be associated with cognitive and social functions of schizophrenia.Scientific reports · 2025Article
- Five differentially expressed proteins identified to serve as potential blood biomarkers for schizophrenia screening based on proteomics.Frontiers in psychiatry · 2025Article
- Actin Bundles Dynamics and Architecture.Biomolecules · 2023Review
- Article
- Article
- Fascin- and α-Actinin-Bundled Networks Contain Intrinsic Structural Features that Drive Protein Sorting.Current biology : CB · 2016Article
- Postsynaptic actin regulates active zone spacing and glutamate receptor apposition at the Drosophila neuromuscular junction.Molecular and cellular neurosciences · 2014Article
- Z-disc-associated, alternatively spliced, PDZ motif-containing protein (ZASP) mutations in the actin-binding domain cause disruption of skeletal muscle actin filaments in myofibrillar myopathy.The Journal of biological chemistry · 2014Article
- ASB2α, an E3 ubiquitin ligase specificity subunit, regulates cell spreading and triggers proteasomal degradation of filamins by targeting the filamin calponin homology 1 domain.The Journal of biological chemistry · 2013Article
- Structure and dynamics of the actin-based smooth muscle contractile and cytoskeletal apparatus.Journal of muscle research and cell motility · 2012Review
- Arg/Abl2 modulates the affinity and stoichiometry of binding of cortactin to F-actin.Biochemistry · 2012Article
- A helical processing pipeline for EM structure determination of membrane proteins.Methods (San Diego, Calif.) · 2011Review
- Large-scale opening of utrophin's tandem calponin homology (CH) domains upon actin binding by an induced-fit mechanism.Proceedings of the National Academy of Sciences of the United States of America · 2011Article
- Missense mutations in dystrophin that trigger muscular dystrophy decrease protein stability and lead to cross-beta aggregates.Proceedings of the National Academy of Sciences of the United States of America · 2010Article
- The regulatory action of alpha-actinin on actin filaments is enhanced by cofilin.European biophysics journal : EBJ · 2010Article
- Molecular origin of strain softening in cross-linked F-actin networks.Physical review. E, Statistical, nonlinear, and soft matter physics · 2010Article
- Mapping of drebrin binding site on F-actin.Journal of molecular biology · 2010Article
- Opening of tandem calponin homology domains regulates their affinity for F-actin.Nature structural & molecular biology · 2010Article
- Regulation of actin cytoskeleton dynamics in cells.Molecules and cells · 2010Review
- Vinculin nucleates actin polymerization and modifies actin filament structure.The Journal of biological chemistry · 2009Article
Corrections and comments
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Authors and funding
3 authors.
Funding
Abstract
The three-dimensional structure of actin filaments decorated with the actin-binding domain of chick smooth muscle alpha-actinin (alpha A1-2) has been determined to 21-A resolution. The shape and location of alpha A1-2 was determined by subtracting maps of F-actin from the reconstruction of decorated filaments. alpha A1-2 resembles a bell that measures approximately 38 A at its base and extends 42 A from its base to its tip. In decorated filaments, the base of alpha A1-2 is centered about the outer face of subdomain 2 of actin and contacts subdomain 1 of two neighboring monomers along the long-pitch (two-start) helical strands. Using the atomic model of F-actin (Lorenz, M., D. Popp, and K. C. Holmes. 1993. J. Mol. Biol. 234:826-836.), we have been able to test directly the likelihood that specific actin residues, which have been previously identified by others, interact with alpha A1-2. Our results indicate that residues 86-117 and 350-375 comprise distinct binding sites for alpha-actinin on adjacent actin monomers.
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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.