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John J. Hemperly

Researcher at Becton Dickinson

Publications -  37
Citations -  2290

John J. Hemperly is an academic researcher from Becton Dickinson. The author has contributed to research in topics: Neural cell adhesion molecule & Schizophrenia. The author has an hindex of 22, co-authored 37 publications receiving 2216 citations. Previous affiliations of John J. Hemperly include Research Triangle Park.

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NCAM140 Interacts with the Focal Adhesion Kinase p125fak and the SRC-related Tyrosine Kinase p59fyn

TL;DR: NCAM140 binding interactions at the cell surface induce the assembly of a molecular complex of NCAM140, p125fak, and p59fyn and activate the catalytic function of these tyrosine kinases, initiating a signaling cascade that may modulate growth cone migration.
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Contactin-associated protein (Caspr) and contactin form a complex that is targeted to the paranodal junctions during myelination.

TL;DR: It is reported that contactin colocalizes and forms a cis complex with Caspr in the paranodes and juxtamesaxon, suggesting that a preformed complex of Caspr and contactin is targeted to the paranodal junctions via extracellular interactions with myelinating glia.
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NCAM stimulates the Ras-MAPK pathway and CREB phosphorylation in neuronal cells.

TL;DR: An NCAM signal transduction mechanism with the potential for modulating the expression of genes needed for axonal growth, survival, and synaptic plasticity is defined.
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Induction of neurite outgrowth through contactin and Nr-CAM by extracellular regions of glial receptor tyrosine phosphatase beta.

TL;DR: The results suggest that binding of glial RPTPβ to the contactin/Nr-CAM complex is important for neurite growth and neuronal differentiation.
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Novel fluorescent technology platform for high throughput cytotoxicity and proliferation assays.

TL;DR: Data is presented illustrating the application of the Oxygen BioSensor technology for rapid, homogeneous detection and evaluation of metabolic activity of a variety of eukaryotic and prokaryotic cells, including mammalian cells, insect cells, yeast, and bacteria.