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Seung-Won Park

Researcher at Rutgers University

Publications -  5
Citations -  774

Seung-Won Park is an academic researcher from Rutgers University. The author has contributed to research in topics: MSL complex & RNA. The author has an hindex of 5, co-authored 5 publications receiving 752 citations. Previous affiliations of Seung-Won Park include University of Medicine and Dentistry of New Jersey.

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Discovery of functional elements in 12 Drosophila genomes using evolutionary signatures

TL;DR: This work uses the genomes of 12 Drosophila species for the de novo discovery of functional elements in the fly, and identifies several classes of pre- and post-transcriptional regulatory motifs, and predicts individual motif instances with high confidence.
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An Evolutionarily Conserved Domain of roX2 RNA Is Sufficient for Induction of H4-Lys16 Acetylation on the Drosophila X Chromosome

TL;DR: It is suggested that roX RNAs might play important roles in regulating enzymatic activity of the MSL complex, and conserved primary sequences, such as GUUNUACG, in the 3′ end of both roX1 and roX2 RNAs are found.
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Regulation of histone H4 Lys16 acetylation by predicted alternative secondary structures in roX noncoding RNAs.

TL;DR: A model in which the functional redundancy between roX1 and roX2 RNAs is based, at least in part, on short GUUNUACG sequences that regulate the activity of the MSL complex is supported.
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MSL cis-spreading from roX gene up-regulates the neighboring genes.

TL;DR: The molecular and genetic data suggest that cis-spreading of the MSL complex from high-affinity sites including the roX gene results in upregulation of the neighboring genes, which are targets for dosage compensation in the male X chromosome.
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Regulation of the catalytic function of topoisomerase II alpha through association with RNA.

TL;DR: An unexpected finding is found that an RNA-binding activity is intrinsically associated with topoisomerase IIalpha, which is engaged in diverse nuclear events such as DNA replication, transcription and the formation or maintenance of heterochromatin.