The GluN1, GluN2A, and GluN2B pre-M1 linker is intolerant to genetic
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Descrição
Several aromatic residues around the pre-M1 helix are largely
Cross-subunit interactions that stabilize open states mediate
Hodgkin–Huxley–Katz Prize Lecture: Genetic and pharmacological
De Novo Mutations and Rare Variants Occurring in NMDA Receptors
Cross-subunit Interactions that Stabilize Open States Mediate
GluN2A and GluN2B NMDA receptors use distinct allosteric routes
Ion channel mutants N615I and V618G prevent Mg²⁺ block. a Mg²
Opportunities for Precision Treatment of GRIN2A and GRIN2B Gain-of
The GluN1, GluN2A, and GluN2B pre-M1 linker is intolerant to
Structure, Function, and Pharmacology of Glutamate Receptor Ion
Frontiers Surface Expression, Function, and Pharmacology of
Mechanistic Insight into NMDA Receptor Dysregulation by Rare
Molecular Mechanism of Disease-Associated Mutations in the Pre-M1
Structure, Function, and Pharmacology of Glutamate Receptor Ion
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