Identification of Lectin-Purified Neural Glycoproteins, GPs 180, 116, and 110, with NMDA and AMPA Receptor Subunits: Conservation of Glycosylation at the Synapse-Reference-Cited by-同舟云学术

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Identification of Lectin-Purified Neural Glycoproteins, GPs 180, 116, and 110, with NMDA and AMPA Receptor Subunits: Conservation of Glycosylation at the Synapse

Published:2002-11-13 Issue:6 Volume:70 Page:2594-2605
ISSN:0022-3042
Container-title:Journal of Neurochemistry
language:en
Short-container-title:Journal of Neurochemistry

Author:

Clark R. A. C.,Gurd J. W.,Bissoon N.,Tricaud N.,Molnar E.,Zamze S. E.,Dwek R. A.,McIlhinney R. A. J.,Wing D. R.

Publisher

Wiley

Subject

Cellular and Molecular Neuroscience,Biochemistry

Link

http://onlinelibrary.wiley.com/wol1/doi/10.1046/j.1471-4159.1998.70062594.x/fullpdf

Cited by 37 articles. 订阅此论文施引文献订阅此论文施引文献，注册后可以免费订阅5篇论文的施引文献，订阅后可以查看论文全部施引文献

1. ConBr, the Lectin from Canavalia brasiliensis Mart. Seeds: Forty Years of Research;Current Protein & Peptide Science;2019-05-20

2. Intradomain Interactions in an NMDA Receptor Fragment Mediate N-Glycan Processing and Conformational Sampling;Structure;2019-01

3. ConA-Like Lectins: High Similarity Proteins as Models to Study Structure/Biological Activities Relationships;International Journal of Molecular Sciences;2018-12-21

4. Computer Simulations Predict High Structural Heterogeneity of Functional State of NMDA Receptors;Biophysical Journal;2018-09

5. N-Glycosylation Regulates the Trafficking and Surface Mobility of GluN3A-Containing NMDA Receptors;Frontiers in Molecular Neuroscience;2018-06-04

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