Zobrazeno 1 - 7
of 7
pro vyhledávání: '"René Weissensteiner"'
Autor:
Andreas Jurik, Thomas Stockner, Harald H. Sitte, René Weissensteiner, Gerhard F. Ecker, Michael Freissmuth
Publikováno v:
Springer Series in Biophysics ISBN: 9783642538384
Neurotransmitter:sodium symporters are located on presynaptic neurons and terminate neurotransmission by removing the monoamine substrates from the synaptic cleft. Until very recently, only several conformational snapshots/structures of a bacterial h
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_________::cc5b11b57c42ca3c75e6f1b79d66969f
https://doi.org/10.1007/978-3-642-53839-1_5
https://doi.org/10.1007/978-3-642-53839-1_5
Autor:
Walter Sandtner, Harald H. Sitte, Gerhard F. Ecker, Oliver Kudlacek, Andreas Jurik, Michael Freissmuth, Simon Bulling, Thomas Steinkellner, René Weissensteiner
Publikováno v:
Sensory Perception ISBN: 9783211997505
Cocaine and amphetamine are psychostimulant drugs that are illicitly used; they affect sensory perception by targeting the neurotransmitter: sodium symporters (NSS) at the synapses between neurons. They both increase the concentration of the neurotra
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_________::c57c6f5261db979f501de6da8ec49672
https://doi.org/10.1007/978-3-211-99751-2_11
https://doi.org/10.1007/978-3-211-99751-2_11
Autor:
Stefan Boehm, Gerhard F. Ecker, Petra Geier, Klaus Schicker, Therese Montgomery, René Weissensteiner, Florian Buchmayer, Valery N. Bochkov, Peter J. Hamilton, Thomas Steinkellner, Gerald Stübiger, Jae-Won Yang, Andreas Jurik, Aurelio Galli, Heinrich J.G. Matthies, Harald H. Sitte, Marie-Therese Winkler, Marion Holy
Publikováno v:
BMC Pharmacology
Background Neuronal functions, such as excitability or endoand exocytosis, require phosphatidylinositol-4,5-bisphosphate (PIP2) since ion channels and other proteins involved in these processes are regulated by PIP2. Monoamine transporters control ne
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::8902a7574196a21db161269e658df2c5
http://europepmc.org/articles/PMC3194251
http://europepmc.org/articles/PMC3194251
Publikováno v:
Scientia Pharmaceutica. 77:205-205
The serotonin transporter (SERT) is a presynaptic membrane protein that terminates neuronal transmission of serotonin (5HT) by transporting its substrate into the emitting neuron. Recently new crystal structures of the Leucine Transporter (LeuT) with
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_________::b2be2a3a91a97469b61b9aaea325631e
https://doi.org/10.3797/scipharm.oephg.21.po-06
https://doi.org/10.3797/scipharm.oephg.21.po-06
Publikováno v:
Scientia Pharmaceutica. 77:203-203
The human serotonin transporter (hSERT), embedded in the presynaptic membrane, is responsible for the reuptake of serotonin from the synaptic cleft, thus terminating neurotransmission. The structure of the SERT has not yet been resolved by experiment
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_________::800d337e582f209c51a8ce46929c68ae
https://doi.org/10.3797/scipharm.oephg.21.po-04
https://doi.org/10.3797/scipharm.oephg.21.po-04
Autor:
Thomas Stockner, Therese R Montgomery, Oliver Kudlacek, Rene Weissensteiner, Gerhard F Ecker, Michael Freissmuth, Harald H Sitte
Publikováno v:
PLoS Computational Biology, Vol 9, Iss 2, p e1002909 (2013)
The high-resolution crystal structure of the leucine transporter (LeuT) is frequently used as a template for homology models of the dopamine transporter (DAT). Although similar in structure, DAT differs considerably from LeuT in a number of ways: (i)
Externí odkaz:
https://doaj.org/article/036fd3d1414a46e38bcca194053a7f18
Autor:
René Weissensteiner, Subhodeep Sarker, Harald H. Sitte, Ilka Steiner, Sonja Sucic, Michael Freissmuth, Gerhard F. Ecker
Publikováno v:
BMC Pharmacology
The structure of the bacterial leucine transporter from Aquifex aeolicus (LeuT(Aa)) has been used as a model for mammalian Na(+)/Cl(-)-dependent transporters, in particular the serotonin transporter (SERT). The crystal structure of LeuT(Aa) liganded
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::dced79434d2ba303f1570a592ee80516