B
Bernhard Bettler
Researcher at University of Basel
Publications - 222
Citations - 21637
Bernhard Bettler is an academic researcher from University of Basel. The author has contributed to research in topics: GABAB receptor & Receptor. The author has an hindex of 73, co-authored 217 publications receiving 20081 citations. Previous affiliations of Bernhard Bettler include Salk Institute for Biological Studies & Ciba Specialty Chemicals.
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Journal ArticleDOI
Gabab-receptor subtypes assemble into functional heteromeric complexes
Klemens Kaupmann,Barbara Malitschek,Valerie Schuler,Jakob Heid,Wolfgang Froestl,Pascal Beck,Johannes Mosbacher,Serge Bischoff,Ákos Kulik,Ryuichi Shigemoto,Andreas Karschin,Bernhard Bettler +11 more
TL;DR: A new GABAB receptor subtype is described, GABABR2, which does not bind available GABAB antagonists with measurable potency and exhibits a significant increase in agonist- and partial-agonist-binding potencies as compared with individual receptors.
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Expression cloning of GABA(B) receptors uncovers similarity to metabotropic glutamate receptors.
Klemens Kaupmann,Katharina Huggel,Jakob Heid,Peter J. Flor,Serge Bischoff,Stuart J. Mickel,Mcmaster Gary Kent,Christof Angst,Helmut Bittiger,Wolfgang Froestl,Bernhard Bettler +10 more
TL;DR: The cloning of GABAB receptors is reported and photoaffinity labelling experiments suggest that the cloned receptors correspond to two highly conserved GABAB receptor forms present in the vertebrate nervous system.
Journal ArticleDOI
Molecular Structure and Physiological Functions of GABAB Receptors
TL;DR: Current concepts on the molecular composition and function of GABA(B) receptors are reviewed and ongoing drug-discovery efforts are discussed, which are expected to broaden the spectrum of therapeutic applications.
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Cloning of a novel glutamate receptor subunit, GluR5 : expression in the nervous system during development
Bernhard Bettler,Jim Boulter,Irm Hermans-Borgmeyer,A O'Shea-Greenfield,Evan S. Deneris,Carl Moll,Uwe Borgmeyer,Michael Hollmann,Stephen F. Heinemann +8 more
TL;DR: The GluR5 protein forms homomeric ion channels in Xenopus oocytes that are weakly responsive to L-glutamate and is detected in areas of neuronal differentiation and synapse formation during embryogenesis.
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Cloning of a cDNA for a glutamate receptor subunit activated by kainate but not AMPA.
TL;DR: The cloning and expression of a functional rat glutamate receptor subunit cDNA, GluR6, which has a very different pharmacology from that of the GluLl–GluR4 class and exhibits an outwardly rectifying current–voltage relationship.