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Cited by 464

The DOI matches its Crossref record; 4 of the 4 references it cites were found in a registry or an index.

Stimulation of Protein Tyrosine Phosphorylation by NMDA Receptor Activation

Bading, Hilmar, Greenberg, Michael E.·1991·Science

Abstract

The N -methyl-D-aspartate (NMDA) receptor, a subtype of glutamate receptors, plays a key role in synaptic plasticity in the nervous system. After NMDA receptor activation, calcium entry into the postsynaptic neuron is a critical initial event. However, the subsequent mechanisms by which the NMDA receptor signal is processed are incompletely understood. Stimulation of cultured rat hippocampal cells with glutamate resulted in the rapid and transient tyrosine phosphorylation of a 39-kilodalton protein (p39). Tyrosine phosphorylation of p39 was triggered by the NMDA receptor and required an influx of Ca 2+ from the extracellular medium. Because p39 was found to be highly related or identical to the microtubule-associated protein 2 kinase, the NMDA receptor signal may be processed by a sequential activation of protein kinases.

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Metadata

Authors
Bading, H., & Greenberg, M. E.
Venue
Science
Published
1991-08-23
Volume
253
Issue
5022
Pages
912-914
ISSN
  • 0036-8075 (ISSN-L)
  • 1095-9203
OpenAlex
W2094019443
Cited by
464
References
4
FWCI
10.77
Type
journal article
Language
en
Open access
closed

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CoChat. (2026). Citation check: Stimulation of Protein Tyrosine Phosphorylation by NMDA Receptor Activation. https://app.cochat.ai/papers/10.1126/science.1715095
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Bading, H., & Greenberg, M. E. (1991). Stimulation of Protein Tyrosine Phosphorylation by NMDA Receptor Activation. Science. https://doi.org/10.1126/science.1715095

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Contains information from the Semantic Scholar Academic Graph Datasets, made available under the ODC Attribution License (ODC-BY 1.0).

Semantic Scholar’s data is described in: Kinney, R., et al. (2023). The Semantic Scholar Open Data Platform. arXiv:2301.10140.