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Showing 1–10 of 10 results
Advanced filters: Author: Yi-Lynn Liang Clear advanced filters
  • The glucagon-like peptide-1 receptor (GLP-1R) can be targeted in the treatment of diabetes, obesity and other metabolic disorders. Here, the authors assess the molecular mechanisms of peptide agonists binding to GLP-1R and the responses elucidated by these ligands, including distinct kinetics of G protein activation.

    • Giuseppe Deganutti
    • Yi-Lynn Liang
    • Denise Wootten
    ResearchOpen Access
    Nature Communications
    Volume: 13, P: 1-18
  • The structure of a complex containing calcitonin gene-related peptide, the human calcitonin gene-related peptide receptor and the Gs heterotrimer, determined using Volta phase-plate cryo-electron microscopy, provides structural insight into the regulation of G-protein-coupled receptors by receptor activity modifying protein 1.

    • Yi-Lynn Liang
    • Maryam Khoshouei
    • Patrick M. Sexton
    Research
    Nature
    Volume: 561, P: 492-497
  • The structure of GLP-1R and its G protein in complex with the small molecule TT-OAD2 sheds light on how the TT-OAD2 agonist can activate the receptor and provides insights into the development of therapeutic agents for metabolic disorders.

    • Peishen Zhao
    • Yi-Lynn Liang
    • Denise Wootten
    Research
    Nature
    Volume: 577, P: 432-436
  • The class B secretin GPCR (SecR) has broad physiological effects, with target potential for treatment of metabolic and cardiovascular disease. Here, authors present a cryo-EM structure and biochemical studies of secretin binding to the SecR:Gs complex which show that interactions between peptide and receptor were dynamic.

    • Maoqing Dong
    • Giuseppe Deganutti
    • Laurence J. Miller
    ResearchOpen Access
    Nature Communications
    Volume: 11, P: 1-17
  • Previously, peptide selectivity in the VPAC receptor family of GPCRs was poorly understood. Here, authors combine cryo-EM and MD data to understand binding and selectivity of VPAC1R and PAC1R peptide agonists that can guide future drug development.

    • Sarah J. Piper
    • Giuseppe Deganutti
    • Denise Wootten
    ResearchOpen Access
    Nature Communications
    Volume: 13, P: 1-20
  • There is a need to optimise cryo-EM data acquisition approaches to improve the resolution of GPCR cryo-EM structures to better than 2.5 Å, in order to use them for structure-based drug design purposes. Here, the authors present a systematic analysis of the main cryo-EM experimental parameters using three GPCRs as test cases, which is also of interest for the cryo-EM structure determination of other small membrane proteins.

    • Radostin Danev
    • Matthew Belousoff
    • Patrick M. Sexton
    ResearchOpen Access
    Nature Communications
    Volume: 12, P: 1-10
  • The cryo-electron microscopy structure of the human adenosine A1 receptor in complex with adenosine and heterotrimeric Gi2 protein provides molecular insights into receptor and G-protein selectivity.

    • Christopher J. Draper-Joyce
    • Maryam Khoshouei
    • Arthur Christopoulos
    Research
    Nature
    Volume: 558, P: 559-563