ReviewAnnual review of biophysics2011
Actin structure and function.
Review in Annual review of biophysics, 2011. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 593 papers, 1 of them a synthesis that pooled it.
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
593 citing papers in PubMed, 1 synthesis or guideline pooled it, 1,218 citations in OpenAlex.
- Evaluation of common protein biomarkers involved in the pathogenesis of respiratory diseases with proteomic methods: A systematic review.Immunity, inflammation and disease · 2023Pooled it
- The effects of pH on cortex and condensate formation.The Journal of cell biology · 2026Article
- In Vitro Antigiardial Activity and In Silico Target Exploration of Quassinoids Isolated fromInternational journal of molecular sciences · 2026Article
- Proteomic study for the prediction ofHistochemistry and cell biology · 2026Article
- CaMKII generates actin bundle morphology and mechanics distinct from canonical bivalent cross-linkers.bioRxiv : the preprint server for biology · 2026Article
- Form and function of actin impacts actin health and aging.iScience · 2026Article
- Cryo-EM Pipeline for Actin Filament End Structures.Bio-protocol · 2026Article
- Evaluating pharmacological targeting of actin regulatory pathways during aging in C. elegans.Biogerontology · 2026Article
- The Role of Arp2/3 in End-Resection During DNA Double-Strand Break Repair.BioEssays : news and reviews in molecular, cellular and developmental biology · 2026Review
- The prevalence of protein misfolding as a mechanism for hereditary deafness.PLoS genetics · 2026Article
- Alterations of actin in aging.Journal of cell science · 2026Review
- The E3 Ligase RNF115 Aggravates Pathological Cardiac Hypertrophy via Ubiquitin-Mediated Degradation of SPTBN1.Advanced science (Weinheim, Baden-Wurttemberg, Germany) · 2026Article
- The Role of Microfilaments in Cilia Formation and Function.Cytoskeleton (Hoboken, N.J.) · 2026Review
- Biomarkers of Cardiovascular Stress: A Historical Review.Journal of cardiovascular development and disease · 2026Review
- Actin Quantification Using the Filamentous Actin Segmentation Tool (FAST).Bio-protocol · 2026Article
- Quantum Dots Interaction with α-Actinin via Experimental Observations and Computational Predictions.International journal of molecular sciences · 2026Article
- Generalization of negative memories drives the development of psychological distress-related behaviors.Innovation (Cambridge (Mass.)) · 2026Article
- Actin's functional "switch": Constraining C-terminal conformational flexibility disrupts functionally important communication networks.The Journal of biological chemistry · 2026Article
- Integrating Structures and Biology: Cellular and Molecular Interactions with Functionally Graded Spinal Cage Designs.International journal of molecular sciences · 2026Review
- Review
533 more citing papers are in PubMed but not listed here.
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 2 institutions in 2 countries.
Funding
Abstract
Actin is the most abundant protein in most eukaryotic cells. It is highly conserved and participates in more protein-protein interactions than any known protein. These properties, along with its ability to transition between monomeric (G-actin) and filamentous (F-actin) states under the control of nucleotide hydrolysis, ions, and a large number of actin-binding proteins, make actin a critical player in many cellular functions, ranging from cell motility and the maintenance of cell shape and polarity to the regulation of transcription. Moreover, the interaction of filamentous actin with myosin forms the basis of muscle contraction. Owing to its central role in the cell, the actin cytoskeleton is also disrupted or taken over by numerous pathogens. Here we review structures of G-actin and F-actin and discuss some of the interactions that control the polymerization and disassembly 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.