Disease-causing missense mutations in actin binding domain 1 of dystrophin induce thermodynamic instability and protein aggregation.
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F-actin clustering and cell dysmotility induced by the pathological W148R missense mutation of filamin B at the actin-binding domainMissense 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.DMD Mutations in 576 Dystrophinopathy Families: A Step Forward in Genotype-Phenotype CorrelationsMuscle structure influences utrophin expression in mdx mice.Missense mutations in dystrophin that trigger muscular dystrophy decrease protein stability and lead to cross-beta aggregates.The ZZ domain of dystrophin in DMD: making sense of missense mutations.A defect in dystrophin causes a novel porcine stress syndrome.Internal deletion compromises the stability of dystrophinIn vitro stability of therapeutically relevant, internally truncated dystrophins.Creatine kinase B is necessary to limit myoblast fusion during myogenesis.Scan-statistic approach identifies clusters of rare disease variants in LRP2, a gene linked and associated with autism spectrum disorders, in three datasets.Disease-proportional proteasomal degradation of missense dystrophinsComprehensive analysis for genetic diagnosis of Dystrophinopathies in Japan.Cancer associated missense mutations in BAP1 catalytic domain induce amyloidogenic aggregation: A new insight in enzymatic inactivation.Dystrophin and Spectrin, Two Highly Dissimilar Sisters of the Same Family.The carboxy-terminal third of dystrophin enhances actin binding activity.The Structurally Plastic CH2 Domain Is Linked to Distinct Functions of Fimbrins/Plastins.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.Flexibility in the N-terminal actin-binding domain: clues from in silico mutations and molecular dynamics.Structural Interface Forms and Their Involvement in Stabilization of Multidomain Proteins or Protein ComplexesNovel mutation in spectrin-like repeat 1 of dystrophin central domain causes protein misfolding and mild Becker muscular dystrophy.Thermodynamic stability, unfolding kinetics, and aggregation of the N-terminal actin-binding domains of utrophin and dystrophin.Functional correction of dystrophin actin binding domain mutations by genome editing.Modulation of Protein Quality Control and Proteasome to Autophagy Switch in Immortalized Myoblasts from Duchenne Muscular Dystrophy Patients.Mouse models of two missense mutations in actin binding domain 1 of dystrophin associated with Duchenne or Becker muscular dystrophy.A dystroglycan mutation (p.Cys667Phe) associated to muscle-eye-brain disease with multicystic leucodystrophy results in ER-retention of the mutant protein.Independent variability of microtubule perturbations associated with dystrophinopathy.Second international workshop for glycosylation defects in muscular dystrophies, 11-12 November, 2010, Charlotte, USA.
P2860
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P2860
Disease-causing missense mutations in actin binding domain 1 of dystrophin induce thermodynamic instability and protein aggregation.
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2010 nî lūn-bûn
@nan
2010 թուականի Մայիսին հրատարակուած գիտական յօդուած
@hyw
2010 թվականի մայիսին հրատարակված գիտական հոդված
@hy
2010年の論文
@ja
2010年論文
@yue
2010年論文
@zh-hant
2010年論文
@zh-hk
2010年論文
@zh-mo
2010年論文
@zh-tw
2010年论文
@wuu
name
Disease-causing missense mutat ...... ility and protein aggregation.
@ast
Disease-causing missense mutat ...... ility and protein aggregation.
@en
Disease-causing missense mutat ...... ility and protein aggregation.
@nl
type
label
Disease-causing missense mutat ...... ility and protein aggregation.
@ast
Disease-causing missense mutat ...... ility and protein aggregation.
@en
Disease-causing missense mutat ...... ility and protein aggregation.
@nl
prefLabel
Disease-causing missense mutat ...... ility and protein aggregation.
@ast
Disease-causing missense mutat ...... ility and protein aggregation.
@en
Disease-causing missense mutat ...... ility and protein aggregation.
@nl
P2093
P2860
P356
P1476
Disease-causing missense mutat ...... ility and protein aggregation.
@en
P2093
Davin M Henderson
James M Ervasti
P2860
P304
P356
10.1073/PNAS.1001517107
P407
P577
2010-05-10T00:00:00Z