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Soon Ji Yoo

Researcher at Kyung Hee University

Publications -  44
Citations -  4557

Soon Ji Yoo is an academic researcher from Kyung Hee University. The author has contributed to research in topics: Ubiquitin ligase & Inhibitor of apoptosis. The author has an hindex of 22, co-authored 43 publications receiving 4337 citations. Previous affiliations of Soon Ji Yoo include California Institute of Technology & UPRRP College of Natural Sciences.

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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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The Drosophila caspase inhibitor DIAP1 is essential for cell survival and is negatively regulated by HID.

TL;DR: It is proposed that RPR, HID, and GRIM promote apoptosis by disrupting productive IAP-caspase interactions and that DIAP1 is required to block apoptosis-inducing caspase activity.
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Hid, Rpr and Grim negatively regulate DIAP1 levels through distinct mechanisms

TL;DR: In this article, it was shown that Head involution defective (Hid), Reaper (Rpr) and Grim downregulate Drosophila melanogaster IAP1 (DIAP) protein levels.
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The Drosophila Caspase DRONC Cleaves following Glutamate or Aspartate and Is Regulated by DIAP1, HID, and GRIM *

TL;DR: It is shown that the Drosophila caspase DRONC cleaves COOH-terminal to glutamate as well as aspartate, which suggests that DRonC acts to promote cell death.
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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.