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Randal J. Schoepp

Researcher at United States Department of the Army

Publications -  75
Citations -  3787

Randal J. Schoepp is an academic researcher from United States Department of the Army. The author has contributed to research in topics: Ebola virus & Virus. The author has an hindex of 29, co-authored 74 publications receiving 3371 citations. Previous affiliations of Randal J. Schoepp include United States Army Medical Research Institute of Infectious Diseases & University of North Carolina at Chapel Hill.

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Pathology of Fatal West Nile Virus Infections in Native and Exotic Birds during the 1999 Outbreak in New York City, New York

TL;DR: Using standard histologic and ultrastructural methods, virus isolation, immunohistochemistry, in situ hybridization and reverse-transcriptase polymerase chain reaction,West Nile virus was identified as the cause of clinical disease, severe pathologic changes, and death in 27 birds representing eight orders and 14 species and should aid diagnosticians faced with the emergence of West Nile virus in the United States.
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FDA-ARGOS is a database with public quality-controlled reference genomes for diagnostic use and regulatory science

TL;DR: This work describes FDA-ARGOS, a reference database for high-quality microbial reference genomes, and demonstrates its utility on the example of two use cases and provides quality control metrics for the FDA- ARGOS genomic database resource and outlines the need for genome quality gap filling in the public domain.
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Comprehensive Panel of Real-Time TaqMan™ Polymerase Chain Reaction Assays for Detection and Absolute Quantification of Filoviruses, Arenaviruses, and New World Hantaviruses

TL;DR: These real-time hemorrhagic fever virus assays are qualitative (presence of target), they are also quantitative (measure a single DNA/RNA target sequence in an unknown sample and express the final results as an absolute value) and can be used in viral load, vaccine, and antiviral drug studies.
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Three-dimensional structure of a membrane-containing virus

TL;DR: Three-dimensional structure of the ice-embedded intact Sindbis virus, reconstructed from electron images, unambiguously shows that proteins in both shells are arranged with the same icosahedral lattice of triangulation number T = 4.