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Cheol O. Joe

Researcher at KAIST

Publications -  72
Citations -  6558

Cheol O. Joe is an academic researcher from KAIST. The author has contributed to research in topics: Phosphorylation & Protein kinase C. The author has an hindex of 28, co-authored 72 publications receiving 5553 citations. Previous affiliations of Cheol O. Joe include Korea University.

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Journal ArticleDOI

Guidelines for the use and interpretation of assays for monitoring autophagy

Daniel J. Klionsky, +1287 more
- 01 Apr 2012 - 
TL;DR: These guidelines are presented for the selection and interpretation of methods for use by investigators who aim to examine macroautophagy and related processes, as well as for reviewers who need to provide realistic and reasonable critiques of papers that are focused on these processes.
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BTB domain-containing speckle-type POZ protein (SPOP) serves as an adaptor of Daxx for ubiquitination by Cul3-based ubiquitin ligase.

TL;DR: It is shown that SPOP serves as an adaptor of Daxx for the ubiquitination by Cul3-based ubiquitin ligase and subsequent degradation by the proteasome, and SPOP/Cul3-ubiquit in ligase plays an essential role in the control of Dxx level and, thus, in the regulation of DAXx-mediated cellular processes, including transcriptional regulation and apoptosis.
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Gating connexin 43 channels reconstituted in lipid vesicles by mitogen-activated protein kinase phosphorylation.

TL;DR: Permeability, and therefore activity of the reconstituted Cx43 channels, were directly dependent on the state of Cx 43 phosphorylation, and a direct correlation between gap junctional permeability and the phosphorylated state was shown.
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Folate receptor mediated intracellular protein delivery using PLL–PEG–FOL conjugate

TL;DR: The enhanced cellular uptake of FITC-BSA by KB cells in a specific manner was attributed to folate receptor-mediated endocytosis of the complexes having folate moieties on the surface, suggesting that the PLL-PEG-FOL di-block copolymer could be potentially applied for intracellular delivery of a wide range of other biological active agents that have negative charges on thesurface.
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Activation of death-inducing signaling complex (DISC) by pro-apoptotic C-terminal fragment of RIP.

TL;DR: It is suggested that the C-terminal fragment of RIP produced by caspase-8 activates death-inducing signaling complex (DISC), attenuates NF-κB activation, and thereby amplifies the activation of caspases-8 which initiates the downstream apoptotic events.