Appropriate NR1-NR1 Disulfide-linked Homodimer Formation Is Requisite for Efficient Expression of Functional, Cell Surface N-Methyl-D-aspartate NR1/NR2 Receptors-Reference-Cited by-同舟云学术

Appropriate NR1-NR1 Disulfide-linked Homodimer Formation Is Requisite for Efficient Expression of Functional, Cell Surface N-Methyl-D-aspartate NR1/NR2 Receptors

Published:2004-04 Issue:15 Volume:279 Page:14703-14712
ISSN:0021-9258
Container-title:Journal of Biological Chemistry
language:en
Short-container-title:Journal of Biological Chemistry

Author:

Papadakis Michalis,Hawkins Lynda M.,Stephenson F. Anne

Publisher

Elsevier BV

Subject

Cell Biology,Molecular Biology,Biochemistry

Reference39 articles.

1. Excitatory glycine receptors containing the NR3 family of NMDA receptor subunits

2. Cysteine regulation of protein function – as exemplified by NMDA-receptor modulation

3. Mutational analysis of the glycine-binding site of the NMDA receptor: Structural similarity with bacterial amino acid-binding proteins

4. The glycine binding site of the N-methyl-D-aspartate receptor subunit NR1: identification of novel determinants of co-agonist potentiation in the extracellular M3-M4 loop region.

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