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Jae Hong Seol

Researcher at Seoul National University

Publications -  69
Citations -  6286

Jae Hong Seol is an academic researcher from Seoul National University. The author has contributed to research in topics: HslVU & Ubiquitin ligase. The author has an hindex of 35, co-authored 69 publications receiving 5860 citations. Previous affiliations of Jae Hong Seol include UPRRP College of Natural Sciences & University of Tokushima.

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Drosophila pink1 is required for mitochondrial function and interacts genetically with parkin.

TL;DR: Removal of Drosophila PINK1 homologue function results in male sterility, apoptotic muscle degeneration, defects in mitochondrial morphology and increased sensitivity to multiple stresses including oxidative stress, which underscores the importance of mitochondrial dysfunction as a central mechanism of Parkinson's disease pathogenesis.
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Exit from Mitosis Is Triggered by Tem1-Dependent Release of the Protein Phosphatase Cdc14 from Nucleolar RENT Complex

TL;DR: A mutation is identified, net1-1, that bypasses the lethality of tem1 delta and is a key component of a multifunctional complex, denoted RENT (for regulator of nucleolar silencing and telophase), that also contains Cdc14 and the silencing regulator Sir2.
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Skp1 forms multiple protein complexes, including RAVE, a regulator of V-ATPase assembly

TL;DR: The identification of 16 Skp1 and Cdc53-associated proteins in budding yeast and the show that RAVE promotes glucose-triggered assembly of the V-ATPase holoenzyme provide a distinct view of the interactions that link proteins into a comprehensive cellular network.
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Hslv-hslu : a novel atp-dependent protease complex in escherichia coli related to the eukaryotic proteasome

TL;DR: A new type of ATP-dependent protease is isolated from Escherichia coli that encodes two proteins: HslV, a 19-kDa protein similar to proteasome beta subunits, and HslU, a 50- kDa protein related to the ATPase ClpX, which appears to form a complex in which ATP hydrolysis by HSlU is essential for peptide hydrolyisation by the proteasomesome-like component HSlV.