Qiang Gao
5 Papers
Qiang Gao is an academic researcher. The author has contributed to research in topics: Cancer & Cancer cell. The author has an hindex of 5, co-authored 5 publications.
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Papers
Dependence on the Pyrimidine Biosynthetic Enzyme DHODH Is a Synthetic Lethal Vulnerability in Mutant KRAS-Driven Cancers
Malvika Koundinya,Judith Sudhalter,Albane Courjaud,Bruno Lionne,Gaetan Touyer,Luc Bonnet,Isabelle Menguy,Isabelle Schreiber,Christelle Perrault,Stephanie Vougier,Brigitte Benhamou,Bailin Zhang,Timothy He,Qiang Gao,Patricia Gee,Daniel Simard,M. Paola Castaldi,Ronald Tomlinson,Stephan Reiling,Matthieu Barrague,Richard Newcombe,Hui Cao,Yanjun Wang,Fangxian Sun,Joshua Murtie,Mark Munson,Eric Yang,David Harper,Monsif Bouaboula,Jack Pollard,Claudine Grepin,Carlos Garcia-Echeverria,Hong Cheng,Francisco Adrian,Christopher Winter,Stuart Licht,Ivan Cornella-Taracido,Rosalia Arrebola,Aaron J. Morris +38 more
TL;DR: A high-throughput synthetic lethal screen for small molecules that selectively inhibit the growth of KRAS mutant cell lines in soft agar is reported, identifying the target of the most KRAS-selective chemical series as dihydroorotate dehydrogenase (DHODH).
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Identification of the endosomal sorting complex required for transport-I (ESCRT-I) as an important modulator of anti-miR uptake by cancer cells
Timothy R. Wagenaar,Tatiana Tolstykh,Chaomei Shi,Lan Jiang,Jingxin Zhang,Zhifang Li,Qunyan Yu,Hui Qu,Fangxian Sun,Hui Cao,Jack Pollard,Shujia Dai,Qiang Gao,Bailin Zhang,Heike Arlt,May Cindhuchao,Dietmar Hoffmann,Madelyn Light,Karin Jensen,Joern Hopke,Richard Newcombe,Carlos Garcia-Echeverria,Christopher Winter,Sonya Zabludoff,Dmitri Wiederschain +24 more
TL;DR: Data support an important role for the ESCRT-I complex in the regulation of productive free uptake of anti-miRs and reveal potential avenues for improving oligonucleotide free uptake by cancer cells.
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Evaluation of Cancer Dependence and Druggability of PRP4 Kinase Using Cellular, Biochemical, and Structural Approaches.
Qiang Gao,Ingrid Mechin,Nayantara Kothari,Zhuyan Guo,Gejing Deng,Kimberly Haas,Jessica McManus,Dietmar Hoffmann,Anlai Wang,Dmitri Wiederschain,Jennifer L. Rocnik,Werngard Czechtizky,Xin Chen,Larry R. McLean,Heike Arlt,David P. Harper,Feng Liu,Tahir Majid,Vinod Patel,Christoph Lengauer,Carlos Garcia-Echeverria,Bailin Zhang,Hong Cheng,Marion Dorsch,Shih Min A Huang +24 more
TL;DR: This work verified the requirement of enzymatic activity of PRP4 in regulating cancer cell growth and identified an array of potential novel substrates through orthogonal proteomics approaches and unveiled for the first time unique features ofPRP4 kinase domain and its potential mode of interaction with a low molecular weight inhibitor.
PIM inhibitors target CD25-positive AML cells through concomitant suppression of STAT5 activation and degradation of MYC oncogene
Zhuyan Guo,Anlai Wang,Weidong Zhang,Mikhail Levit,Qiang Gao,Claude Barberis,Michel Tabart,Jingxin Zhang,Dietmar Hoffmann,Dmitri Wiederschain,Jennifer Rocnik,Fangxian Sun,Josh Murtie,Christoph Lengauer,Stefan Gross,Bailin Zhang,Hong Cheng,Vinod F. Patel,Laurent Schio,Francisco Adrian,Marion Dorsch,Carlos Garcia-Echeverria,Shih Min A Huang +22 more
TL;DR: It is shown that CD25, a bona fide STAT5 regulated gene, is a mechanistically relevant predictive biomarker for sensitivity to PIM kinase inhibitors and highlights the importance of STAT5 and MYC in rendering cancer cells sensitive to Pim inhibitors.
Selective Inhibition of Mutant Isocitrate Dehydrogenase 1 (IDH1) via Disruption of a Metal Binding Network by an Allosteric Small Molecule
Gejing Deng,Junqing Shen,Ming Yin,Jessica McManus,Magali Mathieu,Patricia Gee,Timothy He,Chaomei Shi,Olivier Bedel,Larry R. McLean,Frank Le-Strat,Ying Zhang,Jean-Pierre Marquette,Qiang Gao,Bailin Zhang,Alexey Rak,Dietmar Hoffmann,Eamonn Rooney,Aurelie Vassort,Walter Englaro,Yi Li,Vinod Patel,Francisco Adrian,Stefan Gross,Dmitri Wiederschain,Hong Cheng,Stuart Licht +26 more
TL;DR: Results show that targeting a divalent cation binding residue can enable selective inhibition of mutant IDH1 and suggest that differences in magnesium binding between wild-type and mutant enzymes may contribute to the inhibitors' selectivity for the mutant enzyme.