27 Papers
55 Citations
Weiwei He is an academic researcher from East China University of Science and Technology. The author has contributed to research in topics: Chemistry & Biology. The author has an hindex of 11, co-authored 21 publications. Previous affiliations of Weiwei He include Scripps Research Institute & University of Science and Technology of China.
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Papers
CMT2D neuropathy is linked to the neomorphic binding activity of glycyl-tRNA synthetase
Weiwei He,Ge Bai,Huihao Zhou,Na Wei,Nicholas M. White,Janelle L. Lauer,Huaqing Liu,Yi Shi,Calin Dan Dumitru,Karen Lettieri,Veronica I. Shubayev,Albena Jordanova,Velina Guergueltcheva,Patrick R. Griffin,Robert W. Burgess,Samuel L. Pfaff,Xiang-Lei Yang +16 more
TL;DR: This work reports that GlyRSCMT2D acquires a neomorphic binding activity that directly antagonizes an essential signalling pathway for motor neuron survival, and indicates that the VEGF–Nrp1 signalling axis is an actionable target for treating CMT2d.
Total Synthesis and Stereochemical Assignment of Delavatine A: Rh-Catalyzed Asymmetric Hydrogenation of Indene-Type Tetrasubstituted Olefins and Kinetic Resolution through Pd-Catalyzed Triflamide-Directed C–H Olefination
Zhongyin Zhang,Jinxin Wang,Jian Li,Fan Yang,Guodu Liu,Wenjun Tang,Weiwei He,Jian-Jun Fu,Yun-Heng Shen,Ang Li,Wei-Dong Zhang,Wei-Dong Zhang +11 more
TL;DR: In the synthesis, the triflamide served as not only an effective directing group for C-H bond activation but also a versatile functional group for further elaborations, enabling two different yet related approaches to a key intermediate 28 in excellent enantiopurity.
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Dispersed disease-causing neomorphic mutations on a single protein promote the same localized conformational opening
TL;DR: Results showed that a helix-turn-helix WHEP domain that was appended to GlyRS in metazoans can regulate the neomorphic structural change, and that the gain of function of the CMT mutants might be due to the loss offunction of the WHEPdomain as a regulator.
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Evolutionary Gain of Alanine Mischarging to Noncognate tRNAs with a G4:U69 Base Pair.
Litao Sun,Ana Cristina Gomes,Weiwei He,Huihao Zhou,Xiaoyun Wang,David W. Pan,Paul Schimmel,Tao Pan,Xiang-Lei Yang +8 more
TL;DR: The expanded tRNA specificity of AlaRS appears to be an evolutionary gain-of-function to provide posttranscriptional alanine substitutions in eukaryotic proteins for potential regulations.
42
Structural insights into the substrate tunnel of Saccharomyces cerevisiae carbonic anhydrase Nce103
Yan-Bin Teng,Yong-Liang Jiang,Yong-Xing He,Weiwei He,Fu-Ming Lian,Yuxing Chen,Cong-Zhao Zhou +6 more
TL;DR: The quaternary structure of Nce103 resembles the typical plant type β-CAs of known structure, with an N-terminal arm indispensable for the enzymatic activity.