- Key Amino Acid Residues within the Third Membrane Domains of NR1 and NR2 Subunits Contribute to the Regulation of the Surface Delivery of N-methyl-D-aspartate Receptors2012 | Second Faculty of Medicine
- Structural features in the glycine-binding sites of the GluN1 and GluN3A subunits regulate the surface delivery of NMDA receptors2019 | Faculty of Science
- Two N-glycosylation Sites in the GluN1 Subunit Are Essential for Releasing N-methyl-D-aspartate (NMDA) Receptors from the Endoplasmic Reticulum2015 | Faculty of Science
- Polyomavirus Middle T-Antigen Is a Transmembrane Protein That Binds Signaling Proteins in Discrete Subcellular Membrane Sites2011 | Faculty of Science
- The Extracellular Domains of GluN Subunits Play an Essential Role in Processing NMDA Receptors in the ER2021 | Central Library of Charles University