GABAB-receptor subtypes assemble into functional heteromeric complexes
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.
Expression cloning of GABA(B) receptors uncovers similarity to metabotropic glutamate receptors.
The cloning of GABA(B) receptors is reported and photoaffinity labelling experiments suggest that the cloned receptors correspond to two highly conserved GABA( B) receptor forms present in the vertebrate nervous system.
Expression cloning of GABAB receptors uncovers similarity to metabotropic glutamate receptors
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.
International Union of Pharmacology. XXXIII. Mammalian γ-Aminobutyric AcidB Receptors: Structure and Function
The emergence of high-affinity antagonists for GABAB receptors has enabled a synaptic role to be established, however, the antagonists have generally failed to establish the existence of pharmacologically distinct receptor types within the GABAB receptor class.
Positive allosteric modulation of native and recombinant gamma-aminobutyric acid(B) receptors by 2,6-Di-tert-butyl-4-(3-hydroxy-2,2-dimethyl-propyl)-phenol (CGP7930) and its aldehyde analog CGP13501.
It is shown that CGP7930 enhances the inhibitory effect of L-baclofen on the oscillatory activity of cultured cortical neurons and may represent a novel means of therapeutic interference with the GABA-ergic system.
International Union of Pharmacology. XXXIII. Mammalian gamma-aminobutyric acid(B) receptors: structure and function.
The gamma-aminobutyric acid(B) (GABA(B)) receptor was first demonstrated on presynaptic terminals where it serves as an autoreceptor and also as a heteroreceptor to influence transmitter release by…
Human gamma-aminobutyric acid type B receptors are differentially expressed and regulate inwardly rectifying K+ channels.
- K. Kaupmann, V. Schuler, B. Bettler
- BiologyProceedings of the National Academy of Sciences…
- 8 December 1998
The cloning and functional characterization of two human GABABRs are reported, and it is demonstrated that in transfected mammalian cells hR 1a and hR1b can modulate heteromeric Kir3.1/3.2 and Kir 3.4 channels, which supports the notion that Kir3 channels are the postsynaptic effectors of GABA BRs.
Epilepsy, Hyperalgesia, Impaired Memory, and Loss of Pre- and Postsynaptic GABAB Responses in Mice Lacking GABAB(1)
CGP 35348: a centrally active blocker of GABAB receptors.
Mutagenesis and Modeling of the GABAB Receptor Extracellular Domain Support a Venus Flytrap Mechanism for Ligand Binding*
A three-dimensional model of the LBP-like domain of the GABAB receptor was constructed based on the known structure of LBP and proposes that the initial step in the activation of the receptor by agonist results from the closure of the two lobes of the binding domain.