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Showing 1–5 of 5 results
Advanced filters: Author: Qing-tao He Clear advanced filters
  • The interaction between a GPCR, such as the vasopressin receptor-2 (V2R), and arrestin depends on the receptors’ phosphorylation pattern. Here authors use FRET and NMR to analyze the phosphorylation patterns of the V2R-arrestin complex and show that phospho-interactions are the key determinants of selective arrestin conformational states and correlated functions.

    • Qing-Tao He
    • Peng Xiao
    • Xiao Yu
    ResearchOpen Access
    Nature Communications
    Volume: 12, P: 1-16
  • Characterization of dynamic conformational changes in membrane protein complexes by NMR spectroscopy remains challenging. Here authors report the site-specific incorporation of 4-trimethylsilyl phenylalanine (TMSiPhe) into proteins, which enabled the characterization of multiple conformational states of a phospho-β2 adrenergic receptor/β-arrestin-1 complex in response to different receptor ligands.

    • Qi Liu
    • Qing-tao He
    • Jin-peng Sun
    ResearchOpen Access
    Nature Communications
    Volume: 11, P: 1-17
  • The description of the cryo-EM structure of an orphan adhesion GPCR–Gs protein complex in apo state facilitates the screening and identification of potential ligands of ADGRG2.

    • Hui Lin
    • Peng Xiao
    • Xiao Yu
    Research
    Nature Chemical Biology
    Volume: 18, P: 1196-1203
  • NMR and in vitro reconstitution indicate that GPCRs signal through SH3-containing proteins downstream of β-arrestin 1 proline regions and that arrestin allosterically activates downstream kinases by disrupting their autoinhibitory conformation.

    • Fan Yang
    • Peng Xiao
    • Jiangyun Wang
    Research
    Nature Chemical Biology
    Volume: 14, P: 876-886