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Yudong Liu
Researcher at University of North Carolina at Chapel Hill
Publications - 7
Citations - 918
Yudong Liu is an academic researcher from University of North Carolina at Chapel Hill. The author has contributed to research in topics: Active site & Phosphodiesterase. The author has an hindex of 7, co-authored 7 publications receiving 874 citations.
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Journal ArticleDOI
Crystal structure of calcineurin–cyclophilin–cyclosporin shows common but distinct recognition of immunophilin–drug complexes
Qing Huai,Hwa Young Kim,Yudong Liu,Yingdong Zhao,Yingdong Zhao,Angelo Mondragon,Angelo Mondragon,Jun O. Liu,Hengming Ke +8 more
TL;DR: The comparison of CyPA-CsA-CN with FKBP-FK506-CN significantly contributes to understanding the molecular basis of regulation of CN activity by the immunophilin–immunosuppressant.
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Multiple Conformations of Phosphodiesterase-5: Implications for enzyme function and drug development
Huanchen Wang,Yudong Liu,Qing Huai,Jiwen Cai,Jiwen Cai,Roya Zoraghi,Sharron H. Francis,Jackie D. Corbin,Howard Robinson,Zhongcheng Xin,Guiting Lin,Hengming Ke +11 more
TL;DR: In this paper, the crystal structures of a fully active catalytic domain of unliganded PDE5A1 and its complexes with sildenafil or icarisid II were reported.
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Crystal Structures of Phosphodiesterases 4 and 5 in Complex with Inhibitor 3-Isobutyl-1-methylxanthine Suggest a Conformation Determinant of Inhibitor Selectivity
TL;DR: Crystal structures of the catalytic domains of cGMP-specific PDE5A1 and cAMP- specific PDE4D2 in complex with the nonselective inhibitor 3-isobutyl-1-methylxanthine have been determined at medium resolution.
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Three-dimensional structures of PDE4D in complex with roliprams and implication on inhibitor selectivity.
TL;DR: The crystal structures of the PDE4D2 catalytic domain in complex with (R)- or (R,S)-rolipram suggest that inhibitor selectivity is determined by the chemical nature of amino acids and subtle conformational changes of the binding pockets, and the corresponding Y329S mutation in PDE7 may lead to loss of the hydrogen bonds between rolipram and Gln369.
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Structural insight into substrate specificity of phosphodiesterase 10.
TL;DR: Structural studies on substrate specificity suggest that the syn configurations of cAMP and cGMP are the genuine substrates for PDE10 and the specificity is achieved through the different interactions and conformations of the substrates.