ArticleBioarchitecture2011
The sarcoplasmic reticulum: Actin and tropomodulin hit the links.
Article in Bioarchitecture, 2011. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 7 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
7 citing papers in PubMed, 9 citations in OpenAlex.
- Importance of proteins and mitochondrial changes as freshness indicators in fish muscle post-mortem.Journal of the science of food and agriculture · 2025Review
- Multifunctional roles of tropomodulin-3 in regulating actin dynamics.Biophysical reviews · 2018Review
- Alteration of tropomyosin-binding properties of tropomodulin-1 affects its capping ability and localization in skeletal myocytes.The Journal of biological chemistry · 2013Article
- A two-segment model for thin filament architecture in skeletal muscle.Nature reviews. Molecular cell biology · 2013Article
- Tropomodulins: pointed-end capping proteins that regulate actin filament architecture in diverse cell types.Cytoskeleton (Hoboken, N.J.) · 2012Review
- Tmod1 and CP49 synergize to control the fiber cell geometry, transparency, and mechanical stiffness of the mouse lens.PloS one · 2012Article
- Review
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 1 institution in 1 country.
Funding
Abstract
Skeletal muscle exhibits strikingly regular intracellular sorting of actin and tropomodulin (Tmod) isoforms, which are essential for efficient muscle contraction. A recent study from our laboratory demonstrates that the skeletal muscle sarcoplasmic reticulum (SR) is associated with cytoplasmic γ-actin (γ(cyto)-actin) filaments, which are predominantly capped by Tmod3. When Tmod3 is experimentally induced to vacate its SR compartment, the cytoskeletal organization of SR-associated γ(cyto)-actin is perturbed, leading to SR swelling, depressed SR Ca(2+) release and myofibril misalignment. Based on these findings, Tmod3-capped γ(cyto)-actin filaments mechanically stabilize SR structure and regulate SR function via a novel lateral linkage. Furthermore, by placing these findings in the context of studies in nonmuscle cells, we conclude that Tmodcapped actin filaments are emerging as critical regulators of membrane stability and physiology in a broad assortment of cell types.
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.