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Yoon Ki Kim

Researcher at Korea University

Publications -  104
Citations -  6361

Yoon Ki Kim is an academic researcher from Korea University. The author has contributed to research in topics: Translation (biology) & Nonsense-mediated decay. The author has an hindex of 40, co-authored 96 publications receiving 5284 citations. Previous affiliations of Yoon Ki Kim include University of Rochester & Nagoya City University.

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Mammalian Staufen1 recruits Upf1 to specific mRNA 3'UTRs so as to elicit mRNA decay.

TL;DR: An mRNA decay mechanism that involves Stau1, the NMD factor Upf1, and a termination codon is described, suggesting that Arf1 mRNA is a natural target for Stau2-mediated decay, and data indicate that other mRNAs are also natural targets.
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Endoribonucleolytic Cleavage of m6A-Containing RNAs by RNase P/MRP Complex.

TL;DR: In this paper, the authors show that m6A-containing RNAs are subject to endoribonucleolytic cleavage via YTHDF2 (m6A reader protein), HRSP12 (adaptor protein), and RNase P/MRP (endoribon nucleases) via endore-ibonuclear cleavage.
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Upf1 Phosphorylation Triggers Translational Repression during Nonsense-Mediated mRNA Decay

TL;DR: A critical step during NMD is uncovered that converts a pioneer translation initiation complex to a translationally compromised mRNP, and it is shown that phospho-Upf1 functions after nonsense codon recognition during steps that involve the translation initiation factor eIF3 and mRNA decay factors.
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Quantitative microarray profiling provides evidence against widespread coupling of alternative splicing with nonsense-mediated mRNA decay to control gene expression

TL;DR: Using AS microarrays, it is shown that PTC-containing splice variants are generally produced at uniformly low levels across diverse mammalian cells and tissues, independently of the action of NMD.
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LIN28A Is a Suppressor of ER-Associated Translation in Embryonic Stem Cells

TL;DR: A genome-wide view of the molecular function of LIN28A in mouse embryonic stem cells is obtained by carrying out RNA crosslinking-immunoprecipitation-sequencing (CLIP-seq) and ribosome footprinting and it is found that, in addition to let-7 precursors,LIN28A binds to a large number of spliced mRNAs.