Li Xie
University of Montana
17 Papers
52 Citations
Li Xie is an academic researcher from University of Montana. The author has contributed to research in topics: Drug discovery & Systems biology. The author has an hindex of 12, co-authored 17 publications. Previous affiliations of Li Xie include University of California, San Diego & Scripps Health.
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Papers
Drug discovery using chemical systems biology: identification of the protein-ligand binding network to explain the side effects of CETP inhibitors.
TL;DR: A novel computational strategy is introduced to identify protein-ligand binding profiles on a genome-wide scale and applies it to elucidating the molecular mechanisms associated with the adverse drug effects of Cholesteryl Ester Transfer Protein (CETP) inhibitors.
Drug off-target effects predicted using structural analysis in the context of a metabolic network model.
TL;DR: This study represents a novel integration of structural and systems biology and a first step towards computational systems medicine and has important implications for drug development and personalized medicine.
Structure-based Systems Biology for Analyzing Off-target Binding
Lei Xie,Li Xie,Philip E. Bourne +2 more
TL;DR: There is significant interest in determining a priori what off-targets exist on a proteome-wide scale, and the need to understand the impact of such binding on the complete biological system, with the ultimate goal of being able to predict the phenotypic outcome.
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Multiscale modeling of the causal functional roles of nsSNPs in a genome-wide association study: application to hypoxia
Li Xie,Clara Ng,Thahmina Ali,Raoul Valencia,Barbara L Ferreira,Vincent Xue,Maliha Tanweer,Dan Zhou,Gabriel G. Haddad,Gabriel G. Haddad,Philip E. Bourne,Lei Xie +11 more
TL;DR: It is demonstrated that the consolidation of statistical, structural, and network views of biomolecules and their interactions can provide new insight into the functional role of nsSNPs in Genome-Wide Association Studies, in a way that neither the knowledge of molecular structures nor biological networks alone could achieve.
Zeta Inhibitory Peptide Disrupts Electrostatic Interactions That Maintain Atypical Protein Kinase C in Its Active Conformation on the Scaffold p62
Li Chun Lisa Tsai,Lei Xie,Kim Dore,Li Xie,Jason C. Del Rio,Charles C. King,Guillermo Martinez-Ariza,Christopher Hulme,Roberto Malinow,Philip E. Bourne,Alexandra C. Newton +10 more
TL;DR: This study identifies an acidic surface on the aPKC scaffold, p62, that tethers the kinase's autoinhibitory pseudosubstrate to allow activity, and unveils a novel mechanism by which scaffolded aP KC is maintained in an active conformation.
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