Glutamate Receptor Agonists as Triggers of Neurotoxicity: Decoding Pathways of Five Neurotoxins and Potential Therapeutic Targets. [PDF]
Turcatel GA, Moura S.
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Glutamate-associated research in Parkinson's disease: a bibliometric analysis. [PDF]
Chen YJ, Xie MR, Zhou SQ, Liu F.
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Candidate gene mutations of patients with astrocytoma who present with seizures: evidence from whole exome sequencing. [PDF]
Phabphal K +4 more
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ASTROGLIA: Molecular Mechanisms, Functional Roles, and Neurophysiological Implications in the Central Nervous System. [PDF]
Ortega A +5 more
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Modulation of Metabotropic Glutamate Receptors as a Strategy to Improve the Efficacy and Safety of Ketamine as an Antidepressant. [PDF]
Pałucha-Poniewiera A.
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The Role of Ion Channels and Transporters in Human Health and Diseases. [PDF]
Soda T.
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Cholesterol Localization around the Metabotropic Glutamate Receptor 2
The Journal of Physical Chemistry B, 2020The metabotropic glutamate receptor (mGluR) 2 plays a key role in the central nervous system. mGluR2 has been shown to be regulated by its surrounding lipid environment, especially by cholesterol, by an unknown mechanism. Here, using a combination of biochemical approaches, photo-cross-linking experiments, and molecular dynamics simulations we show the
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Pharmacology of Metabotropic Glutamate Receptor 2 Homo‐ and Heterodimers
The FASEB Journal, 2020Metabotropic Glutamate Receptors (mGluRs) are a family of class C g‐protein coupled receptors (GPCRs) that respond to glutamate as their native agonist. The eight members of the mGluR family are widely expressed across the nervous and are primarily charged with shaping and fine‐tuning neuronal excitability and ...
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Molecular Pharmacology, 2003Metabotropic glutamate receptor 2 (mGluR2) is a class 3 G protein-coupled receptor and an important mediator of synaptic activity in the central nervous system. Previous work demonstrated that mGluR2 couples to pertussis toxin (PTX)-sensitive G proteins. However, the specificity of mGluR2 coupling to individual members of the G(i/o) family is not known.
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Using an mGluR2 FRET-based binding assay, binders of the transmembrane region devoid of functional activity were identified. It is reported that slight chemical modifications of these SAMs can dramatically change activity of the resulting analogues without altering their affinities.
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