ArticleProceedings of the National Academy of Sciences of the United States of America1990
Isolated dystrophin molecules as seen by electron microscopy.
Article in Proceedings of the National Academy of Sciences of the United States of America, 1990. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 26 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
26 citing papers in PubMed, 81 citations in OpenAlex.
- Biophysical characterization of the dystrophin C-terminal domain: Dystrophin interacts differentially with dystrobrevin isoforms.The Journal of biological chemistry · 2024Article
- In vivo dynamics of skeletal muscle Dystrophin in zebrafish embryos revealed by improved FRAP analysis.eLife · 2015Article
- Filamentous structures in skeletal muscle: anchors for the subsarcolemmal space.Medical molecular morphology · 2015Article
- Spectrin-like repeats 11-15 of human dystrophin show adaptations to a lipidic environment.The Journal of biological chemistry · 2011Article
- Utrophin binds laterally along actin filaments and can couple costameric actin with sarcolemma when overexpressed in dystrophin-deficient muscle.Molecular biology of the cell · 2002Article
- Binding of dystrophin's tandem calponin homology domain to F-actin is modulated by actin's structure.Biophysical journal · 2001Article
- short stop is allelic to kakapo, and encodes rod-like cytoskeletal-associated proteins required for axon extension.The Journal of neuroscience : the official journal of the Society for Neuroscience · 2000Article
- Presence of invertebrate dystrophin-like products in obliquely striated muscle of the leech, Pontobdella muricata (Annelida, Hirudinea).The Histochemical journal · 1999Article
- Dystrobrevin and dystrophin: an interaction through coiled-coil motifs.Proceedings of the National Academy of Sciences of the United States of America · 1997Article
- A new model for the interaction of dystrophin with F-actin.The Journal of cell biology · 1996Article
- Stability of the dystrophin rod domain fold: evidence for nested repeating units.Biophysical journal · 1996Article
- Actin interaction with purified dystrophin from electric organ of Torpedo marmorata: possible resemblance with filamin-actin interface.Journal of muscle research and cell motility · 1995Article
- Visualization of the subsarcolemmal cytoskeleton network of mouse skeletal muscle cells by en face views and application to immunoelectron localization of dystrophin.Journal of muscle research and cell motility · 1995Article
- The dystrophin superfamily: variability and complexity.Journal of muscle research and cell motility · 1994Review
- Characterization and localization of a 77 kDa protein related to the dystrophin gene family.The Biochemical journal · 1994Article
- Dystrophin is phosphorylated by endogenous protein kinases.The Biochemical journal · 1993Article
- Expression of the glucose transporter GLUT4 in the muscular dystrophic mdx mouse.The Biochemical journal · 1993Article
- Complementary distributions of vinculin and dystrophin define two distinct sarcolemma domains in smooth muscle.The Journal of cell biology · 1993Article
- Size and localization of dystrophin molecule: immunoelectron microscopic and freeze etching studies of muscle plasma membranes of murine skeletal myofibers.Acta neuropathologica · 1993Article
- Isolation and characterization of different C-terminal fragments of dystrophin expressed in Escherichia coli.The Biochemical journal · 1992Article
Corrections and comments
PubMed lists nothing against this paper. Absence here is not a guarantee, only a check that was made.
Authors and funding
6 authors at 1 institution in 1 country.
Funding
No grant is acknowledged in the PubMed record.
Abstract
Dystrophin, the protein product of the Duchenne muscular dystrophy locus [Hoffman, E. P., Brown, R. H., Jr., & Kunkel, L. M. (1987) Cell 51, 919-928], is expressed in striated and smooth muscles as well as in non-muscle tissues. Examination of its primary structure has revealed that the molecule is composed of four domains, three of which share many features with the membrane cytoskeletal proteins spectrin and actinin. Dystrophin has thus been predicted to adopt a rod shape [Koenig, M., Monaco, A. P. & Kunkel, L. M. (1988) Cell 53, 219-228]. In the present study, we describe its isolation from the chicken gizzard smooth muscle and present electron microscopic images of the molecule. Polyclonal antibodies were first prepared from a dystrophin fragment derived from the chicken skeletal muscle gene (residues 1173-1728). A dystrophin-enriched membrane preparation from chicken gizzard muscle was then purified by passing it through an affinity chromatography column made with the anti-dystrophin antibodies. Electron microscopy of isolated and rotatory-shadowed dystrophin molecules revealed that the lengths measured for the dystrophin monomers (175 +/- 15 nm) are compatible with a structural arrangement of the repeat sequence segments in triple-barrel alpha-helices connected by short-turn regions, as was earlier postulated for the repeat domains of spectrin and actinin. Electron microscopic images indicate that in addition the dystrophin molecules could present the same capacity of self-association in oligomeric structures as these cytoskeletal proteins and may thus be a part of a complex molecular meshwork essential to muscle cell function.
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.