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Showing 1–6 of 6 results
Advanced filters: Author: Jesse I. Mobbs Clear advanced filters

  • The A3 adenosine receptor is a promising drug target for cancer, inflammation, and glaucoma. Here, authors determine atomic structures of the human A3 receptor, identifying a previously hidden binding pocket that will aid in the development of more effective A3 receptor-targeted medicines.

    • Liudi Zhang
    • Jesse I. Mobbs
    • David M. Thal
    ResearchOpen Access
    Nature Communications
    Volume: 16, P: 1-19

  • The M5 muscarinic acetylcholine receptor represents a promising therapeutic target for neurological disorders. Here, the authors reveal a 2.1 Å cryo-EM structure of the M5 bound to a selective positive allosteric modulator site that enables structure-based drug design.

    • Wessel A. C. Burger
    • Jesse I. Mobbs
    • David M. Thal
    ResearchOpen Access
    Nature Communications
    Volume: 16, P: 1-15

  • The P2X1 receptor is a promising target for the development of a non-hormonal male contraceptive. Here, researchers determined the atomic structure of the P2X1 receptor, revealing opportunities for developing drugs to target this receptor.

    • Felix M. Bennetts
    • Hariprasad Venugopal
    • David M. Thal
    ResearchOpen Access
    Nature Communications
    Volume: 15, P: 1-14

  • The drug Xanomeline is progressing through clinical trials for the treatment of patients with schizophrenia. Here, the authors determine a cryo-EM structure of Xanomeline bound to its primary target revealing a dual binding mode mechanism.

    • Wessel A. C. Burger
    • Vi Pham
    • David M. Thal
    ResearchOpen Access
    Nature Communications
    Volume: 14, P: 1-11

  • HLA-C expression levels correlate with immune responses to pathogens and autoimmunity, and vary in an allele-specific manner across individuals. Here the authors identify factors that drive differential expression of HLA-C allomorphs at the cell surface, and influence the structure of the peptide-binding cleft and diversity of peptides bound by HLA-C molecules.

    • Gurman Kaur
    • Stephanie Gras
    • Lars Fugger
    ResearchOpen Access
    Nature Communications
    Volume: 8, P: 1-12