R. Schoepfer

Publications105
h-index48
Citations11,345
Highly Influential Citations590
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Heteromeric NMDA Receptors: Molecular and Functional Distinction of Subtypes
TLDR
Molecular cloning identified three complementary DNA species of rat brain, encoding NMDA receptor subunits NMDAR2A (NR2A), NR2B, and NR2C, which are 55 to 70% ientical in sequence, and these are structurally related, with less than 20% sequence identity, to other excitatory amino acid receptor sub Units.
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A molecular determinant for submillisecond desensitization in glutamate receptors.
TLDR
These findings suggest that rapid desensitization of AMPA receptors can be regulated by the expression and alternative splicing of GluR-D gene transcripts.
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Single-channel conductances of NMDA receptors expressed from cloned cDNAs: comparison with native receptors
TLDR
Four cloned subunits of the NMDA receptor have been expressed, in pairs, in Xenopus oocytes, and their single-channel properties have been measured, and the conductances of the channels turn out to be useful diagnostic criteria for subunit composition.
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Multiple Structural Elements Determine Subunit Specificity of Mg2+ Block in NMDA Receptor Channels
TLDR
Differences in Mg2+ block as controlled by theNR2 subunits cannot be explained by a single structural determinant in addition to the N-site, and three elements of the NR2 subunit are the major determinants of subtype-specific differences of Mg 2+ block in heteromeric NMDA receptor channels.
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Control by asparagine residues of calcium permeability and magnesium blockade in the NMDA receptor.
TLDR
AMPA and NMDA receptor channels contain common structural motifs in their TM2 segments that are responsible for some of their ion selectivity and conductance properties.
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Global Identification and Characterization of Both O-GlcNAcylation and Phosphorylation at the Murine Synapse*
TLDR
Over 1750 and 16,500 sites of O-GlcNAcylation and phosphorylation from murine synaptosomes, respectively are identified, indicating the potential for crosstalk of phosphorylated with O- GlcNACylation via regulation of enzymatic activity.
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Single-channel currents from recombinant NM DANRla /NR2D receptors expressed in Xenopus oocytes
TLDR
The N Rla/N R2D channel is, like NRla/NR2C, a Tow conductance’ NMDA channel, but it can be distinguished from N RLA/ N R2C channels on the basis of transition asymmetry and differences in the open times of its main and sub-conductance levels.
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Neuron-glia communication via EphA4/ephrin-A3 modulates LTP through glial glutamate transport
TLDR
It is shown that long-term potentiation (LTP) at the CA3–CA1 synapse is modulated by EphA4 in the postsynaptic CA1 cell and by ephrin-A3, a ligand of EPhA4 that is found in astrocytes, suggesting that Eph a4/ephrin-A 3 signaling is a critical mechanism for astroCytes to regulate synaptic function and plasticity.
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Identification of Amino Acid Residues of the NR2A Subunit That Control Glutamate Potency in Recombinant NR1/NR2A NMDA Receptors
TLDR
It is shown that residues on the NR2A subunit control glutamate potency in recombinant NR1/NR2A receptors, without affecting glycine potency, and proposed that the glutamate binding site is located on NR2 subunits and (taking the data together with previous work) implies that each NMDA receptor subunit possesses a binding site for an agonist.
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O-Linked N-Acetylglucosamine Proteomics of Postsynaptic Density Preparations Using Lectin Weak Affinity Chromatography and Mass Spectrometry*S
TLDR
Methods for direct enrichment and identification of in vivo O-GlcNAc-modified peptides through lectin weak affinity chromatography (LWAC) and mass spectrometry are reported and suggest specific roles for O- GlcNAC modification in synaptic transmission, establish a basis for site-specific regulatory studies, and provide methods that will facilitate O- GloverNAc proteome analysis across a wide variety of cells and tissues.
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