Scrapie, Biochemistry, Virology, Prion protein and PrPSc Proteins are his primary areas of study. His Scrapie study incorporates themes from In vitro, Recombinant DNA, Molecular biology, Hamster and Amyloid. His work in the fields of Protease, Gene isoform, Sulfation and Protein folding overlaps with other areas such as Congo red.
Bioassay is closely connected to Transmissible mink encephalopathy in his research, which is encompassed under the umbrella topic of Virology. His Prion protein study combines topics in areas such as Cerebrospinal fluid and Immunology. His PrPSc Proteins study deals with Transmissible spongiform encephalopathy intersecting with Cell-free system.
Byron Caughey mainly focuses on Scrapie, Virology, Biochemistry, Prion protein and In vitro. Byron Caughey interconnects Molecular biology, Cell culture, Recombinant DNA and In vivo in the investigation of issues within Scrapie. His Virology study which covers Transmissible spongiform encephalopathy that intersects with Chronic wasting disease.
Biochemistry is closely attributed to Amyloid in his research. His Amyloid research integrates issues from Fibril, Protein aggregation and Glycosaminoglycan. The study incorporates disciplines such as Immunology, Pathogenesis and Cell biology in addition to Prion protein.
The scientist’s investigation covers issues in Pathology, Disease, In vitro, Cerebrospinal fluid and Synucleinopathies. His research investigates the link between Disease and topics such as Neuroscience that cross with problems in Animal model. His research integrates issues of Infectivity, Scrapie and Olfactory mucosa in his study of In vitro.
His Scrapie research is multidisciplinary, relying on both Cell, Cell culture and Encephalopathy. Byron Caughey works mostly in the field of Biochemistry, limiting it down to topics relating to Progressive supranuclear palsy and, in certain cases, Thioflavin. In his work, Genetically modified mouse is strongly intertwined with Virology, which is a subfield of Asymptomatic.
Byron Caughey focuses on Pathology, Disease, Cerebrospinal fluid, Synucleinopathies and Dementia with Lewy bodies. The Neurodegeneration research Byron Caughey does as part of his general Disease study is frequently linked to other disciplines of science, such as Tolerability, therefore creating a link between diverse domains of science. His work in Cerebrospinal fluid addresses subjects such as Biomarker, which are connected to disciplines such as Protein Misfolding Cyclic Amplification, Transgene, Virology, Genetically modified mouse and Mesocricetus.
The concepts of his Synucleinopathies study are interwoven with issues in Lewy body and Biochemistry, Solubilization, Protein folding. The Dementia with Lewy bodies study combines topics in areas such as In vitro and Synuclein. Byron Caughey has included themes like Fibril, Alzheimer's disease and Recombinant DNA in his Molecular biology study.
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Protofibrils, pores, fibrils, and neurodegeneration: separating the responsible protein aggregates from the innocent bystanders.
Byron Caughey;Peter T. Lansbury.
Annual Review of Neuroscience (2003)
Cell-free formation of protease-resistant prion protein
David A. Kocisko;David A. Kocisko;Jon H. Come;Jon H. Come;Suzette A. Priola;Bruce Chesebro.
Secondary structure analysis of the scrapie-associated protein PrP 27-30 in water by infrared spectroscopy
Byron W. Caughey;Aichun Dong;Kolari S. Bhat;Darwin Ernst.
The most infectious prion protein particles
Jay R. Silveira;Gregory J. Raymond;Andrew G. Hughson;Richard E. Race.
The scrapie-associated form of PrP is made from a cell surface precursor that is both protease- and phospholipase-sensitive.
B. Caughey;G.J. Raymond.
Journal of Biological Chemistry (1991)
Anchorless prion protein results in infectious amyloid disease without clinical scrapie.
Bruce Chesebro;Matthew Trifilo;Richard Race;Kimberly Meade-White.
Non-genetic propagation of strain-specific properties of scrapie prion protein.
Richard A. Bessen;David A. Kocisko;David A. Kocisko;Gregory J. Raymond;Santosh Nandan.
N-terminal truncation of the scrapie-associated form of PrP by lysosomal protease(s): implications regarding the site of conversion of PrP to the protease-resistant state.
B Caughey;G J Raymond;D Ernst;R E Race.
Journal of Virology (1991)
Sulfated polyanion inhibition of scrapie-associated PrP accumulation in cultured cells.
B Caughey;G J Raymond.
Journal of Virology (1993)
Species specificity in the cell-free conversion of prion protein to protease-resistant forms : A model for the scrapie species barrier
David A. Kocisko;Suzette A. Priola;Gregory J. Raymond;Bruce Chesebro.
Proceedings of the National Academy of Sciences of the United States of America (1995)
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