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Andre E. Nel

Researcher at University of California, Los Angeles

Publications -  423
Citations -  62202

Andre E. Nel is an academic researcher from University of California, Los Angeles. The author has contributed to research in topics: Biology & Paleontology. The author has an hindex of 105, co-authored 325 publications receiving 56090 citations. Previous affiliations of Andre E. Nel include Stellenbosch University & University of California, Berkeley.

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Journal Article

Reaction of T lymphocytes with anti-T3 induces translocation of C-kinase activity to the membrane and specific substrate phosphorylation.

TL;DR: Findings are consistent with an important role for C-kinase in transduction of membrane events by the T3-Ti complex, which is associated with increased intracellular Ca2+ and inositol-trisphosphate release.
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Nrf2 deficiency in dendritic cells enhances the adjuvant effect of ambient ultrafine particles on allergic sensitization.

TL;DR: It is concluded that Nrf2 deficiency in DC may promote a constitutive immune-polarizing cytokine milieu, which may have contributed to the augmented adjuvant effect of UFP on allergic sensitization.
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Polymyxin B causes coordinate inhibition of phorbol ester-induced C-kinase activity and proliferation of B lymphocytes

TL;DR: Polymyxin B is a potentially useful inhibitor of C-kinase activity, and that this enzyme may play an important role in mediating B cell responses.
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Use of a fluorescent phosphoprotein dye to characterize oxidative stress‐induced signaling pathway components in macrophage and epithelial cultures exposed to diesel exhaust particle chemicals

TL;DR: It is demonstrated that DEPs induced the phosphorylation of several phosphoproteins that belong to a number of signaling pathways as well as other oxidative stress pathways.
Journal Article

Protein kinase C plays a role in the induction of tyrosine phosphorylation of lymphoid microtubule-associated protein-2 kinase. Evidence for a CD3-associated cascade that includes pp56lck and that is defective in HPB-ALL.

TL;DR: In this article, the authors compared two lines that express biologically active CD3 receptors but differ in their biochemical activation pathways during ligation of this receptor, and found that defective stimulation of PKC by the CD3 receptor is responsible for its failure to activate MAP-2K in HPB-ALL.