J
Jenny Chong
Researcher at University of Montana
Publications - 32
Citations - 1972
Jenny Chong is an academic researcher from University of Montana. The author has contributed to research in topics: RNA polymerase II & DNA. The author has an hindex of 17, co-authored 30 publications receiving 1430 citations. Previous affiliations of Jenny Chong include University of California, San Diego.
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BindingDB in 2015: A public database for medicinal chemistry, computational chemistry and systems pharmacology.
TL;DR: The first update of BindingDB since 2007 is provided, focusing on new and unique features and highlighting directions of importance to the field as a whole.
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5-formylcytosine and 5-carboxylcytosine reduce the rate and substrate specificity of RNA polymerase II transcription.
TL;DR: A systematic study of the effects of five different forms of cytosine in DNA on mammalian and yeast RNA polymerase II transcription, providing new insights into potential functional interplay between cytosines methylation status and transcription.
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Molecular basis for 5-carboxycytosine recognition by RNA polymerase II elongation complex
Lanfeng Wang,Yu Zhou,Liang Xu,Rui Xiao,Xingyu Lu,Liang Chen,Jenny Chong,Hairi Li,Chuan He,Xiang-Dong Fu,Dong Wang +10 more
TL;DR: The global effect of increased 5fC/5caC levels on transcription is determined, finding that such DNA modifications indeed retarded Pol II elongation on gene bodies and suggest a novel role for Pol II as a specific and direct epigenetic sensor during transcription elongation.
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Structural basis for the initiation of eukaryotic transcription-coupled DNA repair
Jun Xu,Indrajit Lahiri,Wei Wang,Adam D. Wier,Michael A. Cianfrocco,Jenny Chong,Alissa A. Hare,Peter B. Dervan,Frank DiMaio,Andres E. Leschziner,Dong Wang,Dong Wang +11 more
TL;DR: The structure of the S. cerevisiae Pol II–Rad26 complex solved by cryo-electron microscopy reveals that Rad26 binds to the DNA upstream of Pol II, where it markedly alters its path and elucidate key roles for Rad26 in both TCR and transcription elongation.
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Effect of a monofunctional phenanthriplatin-DNA adduct on RNA polymerase II transcriptional fidelity and translesion synthesis.
TL;DR: This study presents the first systematic mechanistic investigation that addresses how a site-specific phenanthriplatin-DNA d(G) monofunctional adduct affects the Pol II elongation and transcriptional fidelity checkpoint steps and provides the first insights into how the Pol-II transcription machinery processes the most abundant DNA lesion of the mon ofunctional phenanthRIplatin anticancer drug candidate.