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Jae-Yeon Choi

Researcher at National Jewish Health

Publications -  25
Citations -  890

Jae-Yeon Choi is an academic researcher from National Jewish Health. The author has contributed to research in topics: Phosphatidylserine decarboxylase & Phosphatidylethanolamine. The author has an hindex of 16, co-authored 23 publications receiving 796 citations.

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Gem1 and ERMES Do Not Directly Affect Phosphatidylserine Transport from ER to Mitochondria or Mitochondrial Inheritance

TL;DR: It is shown that ERMES and Gem1 have no direct role in the transport of phosphatidylserine from the ER to mitochondria during the synthesis ofosphatidylethanolamine (PE), as PS to PE conversion is not affected in ERmES or gem1 mutants.
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Host cell lipids control cholesteryl ester synthesis and storage in intracellular Toxoplasma

TL;DR: This study demonstrated that T. gondii diverts cholesterol from low‐density lipoproteins for cholesteryl ester synthesis and storage in lipid bodies, and indicated that host lipids govern neutral lipid synthesis in Toxoplasma and that interference with mechanisms of host lipid storage is detrimental to parasite survival in mammalian cells.
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Phosphatidylserine transport to the mitochondria is regulated by ubiquitination

TL;DR: Using in vivo and in vitro phospholipid synthesis/transport measurements, it is demonstrated that the pstA1-1 mutant is defective in PtdSer transport between the MAM and mitochondria, providing compelling evidence that interorganelle Ptd Ser traffic is regulated by ubiquitination.
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In vivo evidence for the specificity of Plasmodium falciparum phosphoethanolamine methyltransferase and its coupling to the Kennedy pathway.

TL;DR: Interestingly, a mutation in the yeast choline-phosphate cytidylyltransferase gene abrogates the complementation by Pfpmt thus demonstrating that Pf pmt activity is directly coupled to the Kennedy pathway for the de novo synthesis of phosphatidylcholine.
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The CWH8 gene encodes a dolichyl pyrophosphate phosphatase with a luminally oriented active site in the endoplasmic reticulum of Saccharomyces cerevisiae.

TL;DR: The specificity, subcellular location, and topological orientation of this novel enzyme are consistent with a role in the re-utilization of the glycosyl carrier lipid for additional rounds of lipid intermediate biosynthesis after its release during proteinN-glycosylation reactions.