ArticleBiophysical journal1997
Three-dimensional image reconstruction of reconstituted smooth muscle thin filaments: effects of caldesmon.
Article in Biophysical journal, 1997. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 20 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
20 citing papers in PubMed, 56 citations in OpenAlex.
- Smooth muscle contractile cytoskeleton in health and disease.Journal of muscle research and cell motility · 2026Review
- The propensity for tropomyosin twisting in the presence and absence of F-actin.Archives of biochemistry and biophysics · 2016Article
- Structure and dynamics of the actin-based smooth muscle contractile and cytoskeletal apparatus.Journal of muscle research and cell motility · 2012Review
- Acrylodan-labeled smooth muscle tropomyosin reports differences in the effects of troponin and caldesmon in the transition from the active state to the inactive state.Biochemistry · 2011Article
- Tropomyosin position on F-actin revealed by EM reconstruction and computational chemistry.Biophysical journal · 2011Article
- siRNA-mediated knockdown of h-caldesmon in vascular smooth muscle.American journal of physiology. Heart and circulatory physiology · 2009Article
- Structural basis for the activation of muscle contraction by troponin and tropomyosin.Journal of molecular biology · 2009Article
- Effect of actin C-terminal modification on tropomyosin isoforms binding and thin filament regulation.Biochimica et biophysica acta · 2009Article
- Multiple crystal structures of actin dimers and their implications for interactions in the actin filament.Acta crystallographica. Section D, Biological crystallography · 2008Article
- Modulation of actin mechanics by caldesmon and tropomyosin.Cell motility and the cytoskeleton · 2008Article
- Caldesmon and the regulation of cytoskeletal functions.Advances in experimental medicine and biology · 2008Review
- Gestalt-binding of tropomyosin to actin filaments.Journal of muscle research and cell motility · 2008Review
- Fesselin binds to actin and myosin and inhibits actin-activated ATPase activity.Journal of muscle research and cell motility · 2005Article
- Cooperative regulation of myosin-actin interactions by a continuous flexible chain I: actin-tropomyosin systems.Biophysical journal · 2003Article
- Troponin-tropomyosin: an allosteric switch or a steric blocker?Biophysical journal · 2002Article
- Myosin light chain kinase binding to a unique site on F-actin revealed by three-dimensional image reconstruction.The Journal of cell biology · 2001Article
- Caldesmon inhibits nonmuscle cell contractility and interferes with the formation of focal adhesions.Molecular biology of the cell · 1999Article
- Characterization of the functional properties of smooth muscle caldesmon domain 4a: evidence for an independent inhibitory actin-tropomyosin binding domain.The Biochemical journal · 1998Article
- Determination of the gelsolin binding site on F-actin: implications for severing and capping.Biophysical journal · 1998Article
- Cofilin changes the twist of F-actin: implications for actin filament dynamics and cellular function.The Journal of cell biology · 1997Article
Corrections and comments
PubMed lists nothing against this paper. Absence here is not a guarantee, only a check that was made.
Authors and funding
5 authors at 2 institutions in 2 countries.
Funding
Abstract
Caldesmon inhibits actomyosin ATPase and filament sliding in vitro, and therefore may play a role in modulating smooth and non-muscle motile activities. A bacterially expressed caldesmon fragment, 606C, which consists of the C-terminal 150 amino acids of the intact molecule, possesses the same inhibitory properties as full-length caldesmon and was used in our structural studies to examine caldesmon function. Three-dimensional image reconstruction was carried out from electron micrographs of negatively stained, reconstituted thin filaments consisting of actin and smooth muscle tropomyosin both with and without added 606C. Helically arranged actin monomers and tropomyosin strands were observed in both cases. In the absence of 606C, tropomyosin adopted a position on the inner edge of the outer domain of actin monomers, with an apparent connection to sub-domain 1 of actin. In 606C-containing filaments that inhibited acto-HMM ATPase activity, tropomyosin was found in a different position, in association with the inner domain of actin, away from the majority of strong myosin binding sites. The effect of caldesmon on tropomyosin position therefore differs from that of troponin on skeletal muscle filaments, implying that caldesmon and troponin act by different structural mechanisms.
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.