Internal deletion compromises the stability of dystrophin
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The Crystal Structures of Dystrophin and Utrophin Spectrin Repeats: Implications for Domain BoundariesMissense mutation Lys18Asn in dystrophin that triggers X-linked dilated cardiomyopathy decreases protein stability, increases protein unfolding, and perturbs protein structure, but does not affect protein function.Lentiviral vectors can be used for full-length dystrophin gene therapyGenome Editing and Muscle Stem Cells as a Therapeutic Tool for Muscular Dystrophies.An intragenic mutagenesis strategy in Physcomitrella patens to preserve intron splicing.Rimmed vacuoles in Becker muscular dystrophy have similar features with inclusion myopathies.Dystrophin quantification: Biological and translational research implications.In vitro stability of therapeutically relevant, internally truncated dystrophins.Dystrophin quantification and clinical correlations in Becker muscular dystrophy: implications for clinical trialsImpacts of dystrophin and utrophin domains on actin structural dynamics: implications for therapeutic design.Disease-proportional proteasomal degradation of missense dystrophinsMicrodystrophin ameliorates muscular dystrophy in the canine model of duchenne muscular dystrophyExon skipping for nonsense mutations in Duchenne muscular dystrophy: too many mutations, too few patients?Engineering multiple U7snRNA constructs to induce single and multiexon-skipping for Duchenne muscular dystrophy.The carboxy-terminal third of dystrophin enhances actin binding activity.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.Thermodynamic stability, unfolding kinetics, and aggregation of the N-terminal actin-binding domains of utrophin and dystrophin.Mouse models of two missense mutations in actin binding domain 1 of dystrophin associated with Duchenne or Becker muscular dystrophy.Independent variability of microtubule perturbations associated with dystrophinopathy.Lentiviral vectors can be used for full-length dystrophin gene therapy.
P2860
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P2860
Internal deletion compromises the stability of dystrophin
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2011 nî lūn-bûn
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2011 թուականի Մայիսին հրատարակուած գիտական յօդուած
@hyw
2011 թվականի մայիսին հրատարակված գիտական հոդված
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2011年の論文
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2011年論文
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2011年論文
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2011年論文
@zh-hk
2011年論文
@zh-mo
2011年論文
@zh-tw
2011年论文
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name
Internal deletion compromises the stability of dystrophin
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Internal deletion compromises the stability of dystrophin
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label
Internal deletion compromises the stability of dystrophin
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Internal deletion compromises the stability of dystrophin
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prefLabel
Internal deletion compromises the stability of dystrophin
@ast
Internal deletion compromises the stability of dystrophin
@en
P2093
P2860
P356
P1476
Internal deletion compromises the stability of dystrophin
@en
P2093
Davin M Henderson
Hanke Heun-Johnson
James M Ervasti
Joseph J Belanto
P2860
P304
P356
10.1093/HMG/DDR199
P577
2011-05-10T00:00:00Z