@article{IR,
      author = {Oken, Adam and Krishnamurthy, Ipsita and Lisi, Nic and  Godsey, Michael H. and Mansoor, Steven E.},
      url = {http://digitalcollections.ohsu.edu/record/9572},
      title = {Molecular pharmacology of P2X7 receptor ligands visualized  by Cryo-EM},
      publisher = {Oregon Health and Science University},
      abstract = {Extracellular ATP is a critical signaling molecule that is  found in a wide range of concentrations across cellular  environments. The family of nonselective cation channels  that recognize extracellular ATP, termed P2X receptors  (P2XRs), is composed of seven sub-types (P2X1-P2X7) that  assemble as functional homo-trimeric and hetero-trimeric  ion channels. The therapeutic potential of P2XRs is an  emerging area of research, as overactive P2XRs have been  shown to play pathophysiological roles in  neuro-inflammation, vascular inflammation, and cell  division. Although there are currently no FDA-approved  drugs targeting P2XRs, structure-based drug design can  provide unique and insightful details into the intricacies  of each receptor to facilitate sub-type selective ligands.  Here, we highlight potential therapeutically targetable  sites in the P2XR family and how single-particle cryogenic  electron microscopy (cryo-EM) can be used to advance drug  discovery, focusing on two cryo-EM structures; the  endogenous agonist ATP bound to P2X7 and the noncompetitive  antagonist JNJ-47965567 bound to P2X7.},
      number = {IR},
      doi = {https://doi.org/10.6083/q811kk38w},
      recid = {9572},
      address = {2022},
}