ArticleHuman molecular genetics2011
Internal deletion compromises the stability of dystrophin.
Article in Human molecular genetics, 2011. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 27 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
27 citing papers in PubMed, 39 citations in OpenAlex.
- Increase in Full-Length Dystrophin by Exon Skipping in Duchenne Muscular Dystrophy Patients with Single Exon Duplications: An Open-label Study.Journal of neuromuscular diseases · 2024Trial
- The atomic structure of human dystrophin spectrin-like repeat 24.Acta crystallographica. Section F, Structural biology communications · 2026Article
- Multiple modes of AFM reveal distinct mechanical properties for dystrophin and utrophin not manifest by small fragments.Proceedings of the National Academy of Sciences of the United States of America · 2026Article
- Two operational modes of atomic force microscopy reveal similar mechanical properties for homologous regions of dystrophin and utrophin.bioRxiv : the preprint server for biology · 2024Article
- Interrogation of Dystrophin and Dystroglycan Complex Protein Turnover After Exon Skipping Therapy.Journal of neuromuscular diseases · 2021Article
- Pathological evaluation of rats carrying in-frame mutations in the dystrophin gene: a new model of Becker muscular dystrophy.Disease models & mechanisms · 2020Article
- Large in-frame 5' deletions in DMD associated with mild Duchenne muscular dystrophy: Two case reports and a review of the literature.Neuromuscular disorders : NMD · 2019Review
- Distinct mechanical properties in homologous spectrin-like repeats of utrophin.Scientific reports · 2019Article
- Mouse models of two missense mutations in actin-binding domain 1 of dystrophin associated with Duchenne or Becker muscular dystrophy.Human molecular genetics · 2018Article
- An intragenic mutagenesis strategy in Physcomitrella patens to preserve intron splicing.Scientific reports · 2017Article
- Lentiviral vectors can be used for full-length dystrophin gene therapy.Scientific reports · 2017Article
- Lentiviral vectors can be used for full-length dystrophin gene therapy.Scientific reports · 2017Article
- Genome Editing and Muscle Stem Cells as a Therapeutic Tool for Muscular Dystrophies.Current stem cell reports · 2017Review
- Independent variability of microtubule perturbations associated with dystrophinopathy.Human molecular genetics · 2016Article
- Disease-proportional proteasomal degradation of missense dystrophins.Proceedings of the National Academy of Sciences of the United States of America · 2015Article
- In vitro stability of therapeutically relevant, internally truncated dystrophins.Skeletal muscle · 2015Article
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- Microdystrophin ameliorates muscular dystrophy in the canine model of duchenne muscular dystrophy.Molecular therapy : the journal of the American Society of Gene Therapy · 2013Article
- The N-terminal actin-binding tandem calponin-homology (CH) domain of dystrophin is in a closed conformation in solution and when bound to F-actin.Biophysical journal · 2012Article
Corrections and comments
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Authors and funding
5 authors at 1 institution in 2 countries.
Funding
Abstract
Duchenne muscular dystrophy (DMD) is a deadly and common childhood disease caused by mutations that disrupt dystrophin protein expression. Several miniaturized dystrophin/utrophin constructs are utilized for gene therapy, and while these constructs have shown promise in mouse models, the functional integrity of these proteins is not well described. Here, we compare the biophysical properties of full-length dystrophin and utrophin with therapeutically relevant miniaturized constructs using an insect cell expression system. Full-length utrophin, like dystrophin, displayed a highly cooperative melting transition well above 37°C. Utrophin constructs involving N-terminal, C-terminal or internal deletions were remarkably stable, showing cooperative melting transitions identical to full-length utrophin. In contrast, large dystrophin deletions from either the N- or C-terminus exhibited variable stability, as evidenced by melting transitions that differed by 20°C. Most importantly, deletions in the large central rod domain of dystrophin resulted in a loss of cooperative unfolding with increased propensity for aggregation. Our results suggest that the functionality of dystrophin therapeutics based on mini- or micro-constructs may be compromised by the presence of non-native protein junctions that result in protein misfolding, instability and aggregation.
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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.