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Showing 1–7 of 7 results
Advanced filters: Author: Azadeh Shahsavar Clear advanced filters
  • Neuropathic pain is commonly treated with opioids due to limited alternatives. Here, authors determine cryo-EM structures of the neuronal glycine transporter GlyT2 and develop a reversible inhibitor that provides analgesia in vivo without side effects.

    • Ryan P. Cantwell Chater
    • Julian Peiser-Oliver
    • Azadeh Shahsavar
    ResearchOpen Access
    Nature Communications
    P: 1-19
  • The astrocytic transporter, GAT3, is a drug target for epilepsy. Here, the authors report the structures of human GAT3, bound to an inhibitor, to substrate GABA, or in substrate-free state, revealing the mechanism of transport and selective inhibition.

    • Jonas Sigurd Mortensen
    • Francesco Bavo
    • Azadeh Shahsavar
    ResearchOpen Access
    Nature Communications
    P: 1-13
  • A study using cryo-electron microscopy has determined the structure of the human dopamine transporter with bound cocaine, revealing molecular details about neurotransmitter transport and how it is affected by neuropsychiatric drugs.

    • Jeppe C. Nielsen
    • Kristine Salomon
    • Claus J. Loland
    Research
    Nature
    Volume: 632, P: 678-685
  • Serial synchrotron crystallography reveals the structure of the human glycine transporter GlyT1, showing how a state-specific inhibitor exerts its effects, and potentially informing the design of new GlyT1 inhibitors to treat a range of disorders of the central nervous system.

    • Azadeh Shahsavar
    • Peter Stohler
    • Poul Nissen
    Research
    Nature
    Volume: 591, P: 677-681
  • Two new structural studies of the GABA transporter subtype GAT1 reveal detailed snapshots of the GABA transport cycle, providing new mechanistic insights and blueprints for rational design of novel leads that target GABAergic systems.

    • Azadeh Shahsavar
    • Petrine Wellendorph
    News & Views
    Nature Structural & Molecular Biology
    Volume: 30, P: 863-865
  • Neurotransmitter:sodium symporters (NSS) perform Na+-dependent amino-acid uptake, but a full structural description of their function is lacking. Here the authors present a structure of the bacterial NSS LeuT in the outward-oriented empty state and show that a Leu residue occupies the empty substrate site and is essential for function.

    • Lina Malinauskaite
    • Saida Said
    • Poul Nissen
    ResearchOpen Access
    Nature Communications
    Volume: 7, P: 1-11