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Positive Modulatory Interactions of NMDA Receptor GluN1/2B Ligand Binding Domains Attenuate Antagonists Activity.
In: Frontiers in pharmacology, 8, p. 229. [Article]

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The N-terminal domain of the GluN3A subunit determines the efficacy of glycine-activated NMDA receptors.
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Schüler, Thomas ; Mesic, Ivana ; Madry, Christian ; Bartholomäus, Ingo ; Laube, Bodo (2008):
Formation of NR1/NR2 and NR1/NR3 heterodimers constitutes the initial step in N-methyl-D-aspartate receptor assembly.
In: The Journal of biological chemistry, 283 (1), pp. 37-46. ISSN 0021-9258,
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Madry, Christian ; Mesic, Ivana ; Betz, Heinrich ; Laube, Bodo (2007):
The N-terminal domains of both NR1 and NR2 subunits determine allosteric Zn2+ inhibition and glycine affinity of N-methyl-D-aspartate receptors.
In: Molecular pharmacology, 72 (6), pp. 1535-44. ISSN 1521-0111,
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Principal role of NR3 subunits in NR1/NR3 excitatory glycine receptor function.
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Ph.D. Thesis

Mesic, Ivana (2010):
Rolle der N-terminalen Domänen (NTDs) bei der Assemblierung und Funktion von N-Methyl-D-Aspartat (NMDA)-Rezeptoren.
Darmstadt, Technische Universität, TU Darmstadt,
[Ph.D. Thesis]