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Showing 1–15 of 15 results
Advanced filters: Author: Claus J. Loland Clear advanced filters

  • The serotonin transporter (SERT) is a key antidepressant target. Here, authors present a cryo-EM structure where the antidepressant vilazodone spans the main SERT binding site toward a secondary pocket and provide further insights into ligand binding.

    • Iris E. Kalenderoglou
    • Andreas Nygaard
    • Claus J. Loland
    ResearchOpen Access
    Nature Communications
    Volume: 16, P: 1-15

  • 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

  • The serotonin transporter (SERT) is a target for antidepressants and psychostimulants. Through a combination of non-canonical amino acid incorporation, protein purification, and spectroscopic fluorescence techniques, this study reports on changes in conformational dynamics of SERT imposed by the binding of ions and ligands.

    • Andreas Nygaard
    • Linda G. Zachariassen
    • Claus J. Loland
    ResearchOpen Access
    Nature Communications
    Volume: 15, P: 1-14

  • Cryo-electron microscopy structures of the noradrenaline transporter (NET) reveal binding modes of adrenaline, coordination of sodium and chloride ion binding and the binding sites and mechanisms of inhibition by conotoxin, bupropion and ziprasidone.

    • Tuo Hu
    • Zhuoya Yu
    • Yan Zhao
    Research
    Nature
    Volume: 632, P: 930-937

  • Vilazodone (VLZ) is a drug for the treatment of major depressive disorders that targets the serotonin transporter (SERT). Here, the authors combine pharmacology measurements and cryo-EM structural analysis to characterize VLZ binding to SERT and observe that VLZ exhibits non-competitive inhibition of serotonin transport and binds with nanomolar affinity to an allosteric site in SERT.

    • Per Plenge
    • Dongxue Yang
    • Claus J. Loland
    ResearchOpen Access
    Nature Communications
    Volume: 12, P: 1-12

  • The dopamine transporter, DAT, controls dopamine signaling by facilitating its reuptake using the Na+ gradient as driving force. Here, the authors uncover that an antiport of K+ ions also contributes to setting the rate of DAT-mediated dopamine clearance.

    • Solveig G. Schmidt
    • Mette Galsgaard Malle
    • Claus J. Loland
    ResearchOpen Access
    Nature Communications
    Volume: 13, P: 1-12

  • The serotonin transporter (SERT) is responsible for re-uptake of serotonin into the presynaptic neuron and plays a key role in synaptic transmission. Here, the authors use hydrogen-deuterium exchange mass spectrometry to probe the conformational dynamics of human SERT in the absence and presence of known substrates and targeted drugs.

    • Ingvar R. Möller
    • Marika Slivacka
    • Kasper D. Rand
    ResearchOpen Access
    Nature Communications
    Volume: 10, P: 1-13

  • The serotonin transporter (SERT) terminates serotonin signaling and its activity is modulated by antidepressants. Here authors reveal the mechanistic details underlying the coupling between the two binding sites in SERT and a high-affinity ligand for the allosteric site.

    • Per Plenge
    • Ara M. Abramyan
    • Claus J. Loland
    ResearchOpen Access
    Nature Communications
    Volume: 11, P: 1-12

  • Neurotransmitter:sodium symporters (NSS) serve as targets for drugs including antidepressants and psychostimulants. Here authors report the X-ray structure of the prokaryotic NSS member, LeuT, in a Na+/substrate-bound, inward-facing occluded conformation which is a key intermediate in the LeuT transport cycle.

    • Kamil Gotfryd
    • Thomas Boesen
    • Ulrik Gether
    ResearchOpen Access
    Nature Communications
    Volume: 11, P: 1-14

  • The neurotransmitter transporter SERT counter transport K+ to transport serotonin. Here the authors show that the activity of the prokaryotic orthologue LeuT is also modulated by this cation, suggesting a general regulatory role for K+on neutrotrasmitter:sodium symporters function.

    • Christian B. Billesbølle
    • Jonas S. Mortensen
    • Claus J. Loland
    ResearchOpen Access
    Nature Communications
    Volume: 7, P: 1-12

  • The dopamine transporter is responsible for termination of neurotransmission through Na+-driven reuptake of neurotransmitter from the extracellular space. Here authors use hydrogen-deuterium exchange mass spectrometry to monitor Na+- and dopamine-induced conformational dynamics of the dopamine transporter.

    • Anne Kathrine Nielsen
    • Ingvar R. Möller
    • Claus J. Loland
    ResearchOpen Access
    Nature Communications
    Volume: 10, P: 1-14

  • Beuming and colleagues determined that the binding site for cocaine overlaps with that of dopamine on the dopamine transporter. Detailed modeling and mutagenesis experiments revealed that this site is deeply buried amongst several transmembrane domains.

    • Thijs Beuming
    • Julie Kniazeff
    • Claus J Loland
    Research
    Nature Neuroscience
    Volume: 11, P: 780-789