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Bernhard Dietzschold

Researcher at Thomas Jefferson University

Publications -  127
Citations -  8272

Bernhard Dietzschold is an academic researcher from Thomas Jefferson University. The author has contributed to research in topics: Rabies virus & Rabies. The author has an hindex of 53, co-authored 127 publications receiving 7993 citations. Previous affiliations of Bernhard Dietzschold include Wistar Institute.

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In vivo expression of inducible nitric oxide synthase in experimentally induced neurologic diseases

TL;DR: The results indicate that nitric oxide produced by cells induced by iNOS may be the toxic factor accounting for cell damage and this may open the door to approaches to the study of the pathogenesis of neurological diseases.
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Identification of the major multiphosphorylation site in mammalian neurofilaments.

TL;DR: A cross-reactive antigenic determinant shared by the peptides and the major NF phosphorylation site was shown to exist in neurofibrillary tangles of patients with Alzheimer disease as well as in two neuron-specific microtubule-associated proteins (MAPs)--i.e., MAP2 and tau.
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Expression of the Rabies Virus Glycoprotein in Transgenic Tomatoes

TL;DR: These transgenic plants should provide a valuable tool for the development of edible oral vaccines in light of the previous demonstration that orally administered rabies G-protein from the same ERA strain elicits protective immunity in animals.
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Pathogenicity of Different Rabies Virus Variants Inversely Correlates with Apoptosis and Rabies Virus Glycoprotein Expression in Infected Primary Neuron Cultures

TL;DR: Downregulation of G protein expression in neuronal cells evidently contributes to rabies virus pathogenesis by preventing apoptosis and the apparently associated failure of the axonal transport of N protein.
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Function and glycosylation of plant-derived antiviral monoclonal antibody

TL;DR: The plant-derived human anti-rabies mAb (mAbP) was as efficient as HRIG for post-exposure prophylaxis against rabies virus in hamsters, indicating that differences in N-glycosylation do not affect the efficacy of the antibody in this model.