ArticleThe Journal of cell biology1993
Three-dimensional reconstruction of caldesmon-containing smooth muscle thin filaments.
Article in The Journal of cell biology, 1993. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 19 papers.
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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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Who cites it
19 citing papers in PubMed, 71 citations in OpenAlex.
- The unique biology of catch muscles: insights into structure, function, and robotics innovations.Frontiers in bioengineering and biotechnology · 2025Review
- Research Advances in the Role of the Tropomyosin Family in Cancer.International journal of molecular sciences · 2023Review
- Tropomyosin diffusion over actin subunits facilitates thin filament assembly.Structural dynamics (Melville, N.Y.) · 2016Article
- A Drosophila melanogaster model of diastolic dysfunction and cardiomyopathy based on impaired troponin-T function.Circulation research · 2014Article
- Structure and dynamics of the actin-based smooth muscle contractile and cytoskeletal apparatus.Journal of muscle research and cell motility · 2012Review
- Effects of basic calponin on the flexural mechanics and stability of F-actin.Cytoskeleton (Hoboken, N.J.) · 2012Article
- Electron microscopy and three-dimensional reconstruction of native thin filaments reveal species-specific differences in regulatory strand densities.Biochemical and biophysical research communications · 2010Article
- Vinculin nucleates actin polymerization and modifies actin filament structure.The Journal of biological chemistry · 2009Article
- Caldesmon and the regulation of cytoskeletal functions.Advances in experimental medicine and biology · 2008Review
- The structure of the vertebrate striated muscle thin filament: a tribute to the contributions of Jean Hanson.Journal of muscle research and cell motility · 2004Review
- Myosin light chain kinase binding to a unique site on F-actin revealed by three-dimensional image reconstruction.The Journal of cell biology · 2001Article
- Three-dimensional reconstruction of thin filaments containing mutant tropomyosin.Biophysical journal · 2000Article
- Tropomyosin positions in regulated thin filaments revealed by cryoelectron microscopy.Biophysical journal · 1999Article
- 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
- The size and shape of caldesmon and its fragments in solution studied by dynamic light scattering and hydrodynamic model calculations.Biophysical journal · 1997Article
- Affinity and structure of complexes of tropomyosin and caldesmon domains.Biophysical journal · 1996Article
- Mode of caldesmon binding to smooth muscle thin filament: possible projection of the amino-terminal of caldesmon from native thin filament.Biophysical journal · 1995Article
- Determination of the alpha-actinin-binding site on actin filaments by cryoelectron microscopy and image analysis.The Journal of cell biology · 1994Article
Corrections and comments
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Authors and funding
3 authors at 1 institution in 1 country.
Funding
Abstract
Caldesmon is known to inhibit actomyosin ATPase and filament sliding in vitro, and may play a role in modulating smooth muscle contraction as well as in diverse cellular processes including cytokinesis and exocytosis. However, the structural basis of caldesmon action has not previously been apparent. We have recorded electron microscope images of negatively stained thin filaments containing caldesmon and tropomyosin which were isolated from chicken gizzard smooth muscle in EGTA. Three-dimensional helical reconstructions of these filaments show actin monomers whose bilobed shape and connectivity are very similar to those previously seen in reconstructions of frozen-hydrated skeletal muscle thin filaments. In addition, a continuous thin strand of density follows the long-pitch actin helices, in contact with the inner domain of each actin monomer. Gizzard thin filaments treated with Ca2+/calmodulin, which dissociated caldesmon but not tropomyosin, have also been reconstructed. Under these conditions, reconstructions also reveal a bilobed actin monomer, as well as a continuous surface strand that appears to have moved to a position closer to the outer domain of actin. The strands seen in both EGTA- and Ca2+/calmodulin-treated filaments thus presumably represent tropomyosin. It appears that caldesmon can fix tropomyosin in a particular position on actin in the absence of calcium. An influence of caldesmon on tropomyosin position might, in principle, account for caldesmon's ability to modulate actomyosin interaction in both smooth muscles and non-muscle cells.
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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.