C
Cindy Y. Jao
Researcher at Harvard University
Publications - 9
Citations - 1693
Cindy Y. Jao is an academic researcher from Harvard University. The author has contributed to research in topics: Hedgehog signaling pathway & Smoothened. The author has an hindex of 9, co-authored 9 publications receiving 1439 citations. Previous affiliations of Cindy Y. Jao include Howard Hughes Medical Institute.
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Journal ArticleDOI
Exploring RNA transcription and turnover in vivo by using click chemistry.
Cindy Y. Jao,Adrian Salic +1 more
TL;DR: A chemical method to detect RNA synthesis in cells, based on the biosynthetic incorporation of the uridine analog 5-ethynyluridine into newly transcribed RNA, which is described, on average once every 35 uridine residues in total RNA.
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Cellular Cholesterol Directly Activates Smoothened in Hedgehog Signaling
Pengxiang Huang,Daniel Nedelcu,Miyako Watanabe,Cindy Y. Jao,Youngchang Kim,Jing Liu,Adrian Salic +6 more
TL;DR: It is proposed that the endogenous Smoothened activator is cholesterol, not oxysterols, and that vertebrate Hedgehog signaling controls Smootshened by regulating its access to cholesterol.
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Oxysterol binding to the extracellular domain of Smoothened in Hedgehog signaling
TL;DR: In this paper, azasterols were developed to block Hedgehog signaling by binding the oxysterol-binding site of Smoothened and showed that the binding site for oxysterols and azasterol maps to the extracellular, cysteine-rich domain and is completely separable from the site bound by other small molecule modulators, located within the heptahelical bundle.
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Metabolic labeling and direct imaging of choline phospholipids in vivo
TL;DR: This work has developed a simple and robust method to label Cho phospholipids in vivo, based on the metabolic incorporation of the Cho analog propargylcholine (propargyl-Cho) into phospholips, and demonstrates the use of propargy-Cho in cultured cells, by imaging phosphate synthesis, turnover, and subcellular localization by both fluorescence and electron microscopy.
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Dispatched and scube mediate the efficient secretion of the cholesterol-modified hedgehog ligand.
TL;DR: It is demonstrated that Hh ligand secretion from vertebrate cells is accomplished via two distinct and synergistic cholesterol-dependent binding events, mediated by two proteins that are essential for vertebrate Hh signaling: the membrane protein Dispatched and a member of the Scube family of secreted proteins.