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Peter H. Seeburg

Researcher at Max Planck Society

Publications -  10
Citations -  3496

Peter H. Seeburg is an academic researcher from Max Planck Society. The author has contributed to research in topics: Glutamate receptor & AMPA receptor. The author has an hindex of 8, co-authored 10 publications receiving 3430 citations. Previous affiliations of Peter H. Seeburg include Heidelberg University.

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A family of AMPA-selective glutamate receptors

TL;DR: Four cloned cDNAs encoding 900-amino acid putative glutamate receptors with approximately 70 percent sequence identity were isolated from a rat brain cDNA library and in situ hybridization revealed differential expression patterns of the cognate mRNAs throughout the brain.
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Differences in Ca2+ permeability of AMPA-type glutamate receptor channels in neocortical neurons caused by differential GluR-B subunit expression

TL;DR: Using patch-clamp techniques in brain slices, it is found that the Ca2+ permeability of native AMPA-type GluRs was markedly higher in nonpyramidal (PCa/PK approximately 0.63) than in pyramidal neurons of rat neocortex, suggesting that differences in relative abundance of GluR-B-specific mRNA generate functional diversity in neurons with respect to Ca2- permeability.
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A mammalian RNA editing enzyme

TL;DR: The cloning of complementary DNA for RED1, a dsRNA adenosine deaminase expressed in brain and peripheral tissues that efficiently edits the Q/R site in GluR-B pre-mRNA in vitro is reported, indicating that members of an emerging gene family catalyse adenosines deamination in nuclear transcripts with distinct but overlapping substrate specificities.
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Ligand affinities at recombinant N-methyl-D-aspartate receptors depend on subunit composition.

TL;DR: The ligand preferences of recombinant NR1 homomeric and NR1-NR2 heteromeric NMDA receptors were examined by homogenate binding assay as discussed by the authors, and the binding affinities for most ligands were similar to those reported for native NMDA receptor.
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NMDA receptor channels: subunit-specific potentiation by reducing agents.

TL;DR: In 293 cells expressing NR1-NR2A channels dithiothreitol (DTT) rapidly potentiated L-glutamate-activated whole-cell currents and decreased the time course of desensitization and deactivation and part of the current potentiation and all kinetic changes reversed upon washout.