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Sung Hee Baek

Researcher at Seoul National University

Publications -  122
Citations -  15508

Sung Hee Baek is an academic researcher from Seoul National University. The author has contributed to research in topics: Ubiquitin & Ubiquitin ligase. The author has an hindex of 46, co-authored 113 publications receiving 13362 citations. Previous affiliations of Sung Hee Baek include UPRRP College of Natural Sciences & Howard Hughes Medical Institute.

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KDM3A histone demethylase functions as an essential factor for activation of JAK2−STAT3 signaling pathway

TL;DR: Evidence is provided that lysine-specific demethylase 3A (KDM3A) functions as an essential epigenetic enzyme for the activation of JAK2−STAT3 signaling pathway, which is essential for modulating cellular development, differentiation, and homeostasis.
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The role of nuclear PKMζ in memory maintenance.

TL;DR: It is found that protein kinase M ζ is transported to the nucleus in a neural activity-dependent manner and it is shown that the amnesic effect of PKMζ inhibition can be rescued by enhancing histone acetylation level.
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Pontin functions as an essential coactivator for Oct4-dependent lincRNA expression in mouse embryonic stem cells

TL;DR: It is found that Pontin chromatin remodelling factor plays an essential role as a coactivator for Oct4 for maintenance of pluripotency in mouse ES cells, and the Oct4-Pontin module plays critical roles in the regulation of genes involved in ES cell fate determination.
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Elevated Response to Type I IFN Enhances RANKL-Mediated Osteoclastogenesis in Usp18-Knockout Mice

TL;DR: The osteopenia phenotype of mice lacking Usp18 (also called Ubp43), which is a deISGylating enzyme and is known as a negative regulator of type I IFN signaling, is identified and it is suggested that, although type IIFN is known to restrict osteoclast differentiation, the exaggerated activation of the type II IFN response in Usp 18-knockout mice causes an oste Openia phenotype in mice.
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Regulation of HIF-1α stability by lysine methylation.

TL;DR: A new physiologically relevant mechanism that regulates HIF-1α stability in the nucleus in response to cellular oxygen levels is identified, based on the collaboration between the SET7/9 methyltransferase and the LSD1 demethylase.