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Facioscapulohumeral dystrophy: the path to consensus on pathophysiologyIntrinsic epigenetic regulation of the D4Z4 macrosatellite repeat in a transgenic mouse model for FSHDFacioscapulohumeral dystrophy: incomplete suppression of a retrotransposed geneCalpain 3 is a rapid-action, unidirectional proteolytic switch central to muscle remodelingAHNAK, a novel component of the dysferlin protein complex, redistributes to the cytoplasm with dysferlin during skeletal muscle regenerationSelf-regulated alternative splicing at the AHNAK locusCalpain 3 is a modulator of the dysferlin protein complex in skeletal muscleNovel protein-protein interactions inferred from literature contextPopulation-based incidence and prevalence of facioscapulohumeral dystrophyA unifying genetic model for facioscapulohumeral muscular dystrophyThe FSHD2 Gene SMCHD1 Is a Modifier of Disease Severity in Families Affected by FSHD1RNA transcripts, miRNA-sized fragments and proteins produced from D4Z4 units: new candidates for the pathophysiology of facioscapulohumeral dystrophyHypomethylation of D4Z4 in 4q-linked and non-4q-linked facioscapulohumeral muscular dystrophyDigenic inheritance of an SMCHD1 mutation and an FSHD-permissive D4Z4 allele causes facioscapulohumeral muscular dystrophy type 2Clinical trial preparedness in facioscapulohumeral muscular dystrophy: Clinical, tissue, and imaging outcome measures 29-30 May 2015, Rochester, New York.Comparison of dysferlin expression in human skeletal muscle with that in monocytes for the diagnosis of dysferlin myopathy.Protein studies in dysferlinopathy patients using llama-derived antibody fragments selected by phage display.Reliable and controllable antibody fragment selections from Camelid non-immune libraries for target validation.Specific loss of histone H3 lysine 9 trimethylation and HP1gamma/cohesin binding at D4Z4 repeats is associated with facioscapulohumeral dystrophy (FSHD).Differential recognition of vascular and parenchymal beta amyloid deposition.A community standard format for the representation of protein affinity reagents.Proteomic analysis of the dysferlin protein complex unveils its importance for sarcolemmal maintenance and integrityMechanism and timing of mitotic rearrangements in the subtelomeric D4Z4 repeat involved in facioscapulohumeral muscular dystrophy.Contractions of D4Z4 on 4qB subtelomeres do not cause facioscapulohumeral muscular dystrophy.The D4Z4 repeat-mediated pathogenesis of facioscapulohumeral muscular dystrophyDNA polymorphism and epigenetic marks modulate the affinity of a scaffold/matrix attachment region to the nuclear matrix.Interspecies translation of disease networks increases robustness and predictive accuracy.Molecular and phenotypic characterization of a mouse model of oculopharyngeal muscular dystrophy reveals severe muscular atrophy restricted to fast glycolytic fibres.Facioscapulohumeral muscular dystrophy is uniquely associated with one of the two variants of the 4q subtelomere.DUX4-induced gene expression is the major molecular signature in FSHD skeletal muscleAsymmetric bidirectional transcription from the FSHD-causing D4Z4 array modulates DUX4 production.Expression profiling of FSHD muscle supports a defect in specific stages of myogenic differentiation.In vivo detection of amyloid-β deposits using heavy chain antibody fragments in a transgenic mouse model for Alzheimer's diseaseComprehensive expression analysis of FSHD candidate genes at the mRNA and protein level.Therapeutic exon skipping for dysferlinopathies?A cascade of complex subtelomeric duplications during the evolution of the hominoid and Old World monkey genomes.Selection of VHH antibody fragments that recognize different Aβ depositions using complex immune libraries.A genome-wide signature of glucocorticoid receptor binding in neuronal PC12 cells.Sarcomeric dysfunction contributes to muscle weakness in facioscapulohumeral muscular dystrophy.Distinguishing the 4qA and 4qB variants is essential for the diagnosis of facioscapulohumeral muscular dystrophy in the Chinese population.
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description
researcher ORCID ID = 0000-0001-8103-711X
@en
wetenschapper
@nl
name
Silvère M van der Maarel
@ast
Silvère M van der Maarel
@en
Silvère M van der Maarel
@nl
type
label
Silvère M van der Maarel
@ast
Silvère M van der Maarel
@en
Silvère M van der Maarel
@nl
altLabel
van der Maarel SM
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prefLabel
Silvère M van der Maarel
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Silvère M van der Maarel
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Silvère M van der Maarel
@nl
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P21
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P496
0000-0001-8103-711X