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Martin Grumet

Researcher at Rutgers University

Publications -  127
Citations -  11935

Martin Grumet is an academic researcher from Rutgers University. The author has contributed to research in topics: Cell adhesion molecule & Neural cell adhesion molecule. The author has an hindex of 61, co-authored 124 publications receiving 11478 citations. Previous affiliations of Martin Grumet include Rockefeller University & Johns Hopkins University.

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The neuronal chondroitin sulfate proteoglycan neurocan binds to the neural cell adhesion molecules Ng-CAM/L1/NILE and N-CAM, and inhibits neuronal adhesion and neurite outgrowth

TL;DR: Experiments using anti-Ng-CAM antibodies as a substrate indicate that neurocan has a direct inhibitory effect on neuronal adhesion and neurite growth, and a role for chondroitin sulfate in this process is indicated, although the core glycoprotein also has binding activity.
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Identification of a novel contactin-associated transmembrane receptor with multiple domains implicated in protein–protein interactions

TL;DR: The cloning of a novel contactin‐associated transmembrane receptor (p190/Caspr) containing a mosaic of domains implicated in protein–protein interactions is described, suggesting that Caspr may function as a signaling component of contactin enabling recruitment and activation of intracellular signaling pathways in neurons.
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The carbonic anhydrase domain of receptor tyrosine phosphatase β is a functional ligand for the axonal cell recognition molecule contactin

TL;DR: These experiments show that an individual domain of RPTP beta acts as a functional ligand for the neuronal receptor contactin, which may generate unidirectional or bidirectional signals during neural development.
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Cytotactin, an extracellular matrix protein of neural and non-neural tissues that mediates glia-neuron interaction

TL;DR: A survey of the times and sites of its appearance during embryogenesis is consistent with the hypothesis that cytotactin is a cell-substrate adhesion molecule that may mediate cell migration in a site-restricted fashion.
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Interactions of the chondroitin sulfate proteoglycan phosphacan, the extracellular domain of a receptor-type protein tyrosine phosphatase, with neurons, glia, and neural cell adhesion molecules.

TL;DR: The studies suggest that by binding to neural cell adhesion molecules, and possibly also by competing for ligands of the transmembrane phosphatase, phosphacan may play a major role in modulating neuronal and glial adhesion, neurite growth, and signal transduction during the development of the central nervous system.