Zobrazeno 1 - 10
of 34
pro vyhledávání: '"Alexandra Schumann"'
Autor:
Shannon N Mostyn, Katie A Wilson, Alexandra Schumann-Gillett, Zachary J Frangos, Susan Shimmon, Tristan Rawling, Renae M Ryan, Megan L O'Mara, Robert J Vandenberg
Publikováno v:
eLife, Vol 8 (2019)
The treatment of chronic pain is poorly managed by current analgesics, and there is a need for new classes of drugs. We recently developed a series of bioactive lipids that inhibit the human glycine transporter GlyT2 (SLC6A5) and provide analgesia in
Externí odkaz:
https://doaj.org/article/e4b5579816404d49a4828b1847e2f1d9
Autor:
Tzu-Ting Chiou, Philip Long, Alexandra Schumann-Gillett, Venkateswarlu Kanamarlapudi, Stefan A. Haas, Kirsten Harvey, Megan L. O’Mara, Angel L. De Blas, Vera M. Kalscheuer, Robert J. Harvey
Publikováno v:
Frontiers in Molecular Neuroscience, Vol 12 (2019)
The recruitment of inhibitory GABAA receptors to neuronal synapses requires a complex interplay between receptors, neuroligins, the scaffolding protein gephyrin and the GDP-GTP exchange factor collybistin (CB). Collybistin is regulated by protein-pro
Externí odkaz:
https://doaj.org/article/f9a09b1b8b95485cbec9f94068e7d8ad
Publikováno v:
ACS Chemical Neuroscience. 10:1668-1678
The endogenous lipids N-arachidonylglycine and oleoyl-l-carnitine are potential therapeutic leads in the treatment of chronic pain through their inhibition of the glycine transporter GlyT2. However, their mechanism of action is unknown. It has been h
Publikováno v:
European Biophysics Journal. 47:59-67
E-cadherin is a transmembrane glycoprotein that facilitates inter-cellular adhesion in the epithelium. The ectodomain of the native structure is comprised of five repeated immunoglobulin-like domains. All E-cadherin crystal structures show the protei
Autor:
Alexandra Schumann-Gillett, Renae M. Ryan, Susan Shimmon, Robert J. Vandenberg, Megan L. O'Mara, Katie A. Wilson, Shannon N. Mostyn, Tristan Rawling, Zachary J. Frangos
Publikováno v:
eLife
eLife, Vol 8 (2019)
eLife, Vol 8 (2019)
The treatment of chronic pain is poorly managed by current analgesics, and there is a need for new classes of drugs. We recently developed a series of bioactive lipids that inhibit the human glycine transporter GlyT2 (SLC6A5) and provide analgesia in
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::d86da3344d6491df8449e1c31d58838f
https://hdl.handle.net/10453/136615
https://hdl.handle.net/10453/136615
Publikováno v:
Biochimica et Biophysica Acta (BBA) - Biomembranes. 1858:776-782
The apparent activity of the multidrug transporter P-glycoprotein (P-gp) is enhanced by the presence of cholesterol. Whether this is due to the direct effect of cholesterol on the activity of P-gp, its effect on the local concentration of substrate i
Publikováno v:
Journal of chemical information and modeling. 59(5)
The human multidrug transporter P-glycoprotein (P-gp) transports over 200 chemically diverse substrates, influencing their bioavailability and tissue distribution. Pharmacological studies have identified both competitive and noncompetitive P-gp subst
The effects of oxidised phospholipids and cholesterol on the biophysical properties of POPC bilayers
Publikováno v:
Biochimica et biophysica acta. Biomembranes. 1861(1)
Oxidation of unsaturated membrane phospholipids by oxidative stress is associated with inflammation, infection, numerous diseases and neurodegenerative disorders. Lipid oxidation is observed in experimental samples when the parent lipid is exposed to
Publikováno v:
Neuroscience letters. 700
SLC6 neurotransmitter transporters facilitate the Na+- and Cl--dependent uptake of amino acids and amino acid derivatives into cells. Disrupting transport leads to a range of neurological disorders. However, the SLC6 substrate transport mechanism is
Publikováno v:
Scopus-Elsevier
Artiflcial magnetic dipole arrays arranged on a square lattice exhibit a fascinating variety and complexityof conflgurations. Among the 16 possible conflgurations, six fulflll the spin ice rule of two dipoles pointing intoa vertex and two point o