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Davin M. Henderson

Researcher at Colorado State University

Publications -  35
Citations -  1282

Davin M. Henderson is an academic researcher from Colorado State University. The author has contributed to research in topics: Chronic wasting disease & Transmissible spongiform encephalopathy. The author has an hindex of 19, co-authored 34 publications receiving 1019 citations. Previous affiliations of Davin M. Henderson include University of Minnesota.

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Rapid Antemortem Detection of CWD Prions in Deer Saliva

TL;DR: The modified RT-QuIC analysis described represents a non-invasive, rapid ante-mortem detection of prions in complex biologic fluids, excreta, or environmental samples as a tool for exploring prion trafficking, peripheralization, and dissemination.
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Quantitative assessment of prion infectivity in tissues and body fluids by real-time quaking-induced conversion.

TL;DR: Samples from deer infected with chronic wasting disease in RT-QuIC were used to show that serial dilution of prion seed was linearly related to the rate of amyloid formation over a range of 10(-3) to 10(-8) µg.
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In vitro detection of prionemia in TSE-infected cervids and hamsters.

TL;DR: Modification of the real time quaking-induced conversion (RT-QuIC) assay to detect blood-borne prions in whole blood from prion-infected preclinical white-tailed deer, muntjac deer, and Syrian hamsters is reported, offering promise for prionemia detection in other species, including humans.
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Disease-causing missense mutations in actin binding domain 1 of dystrophin induce thermodynamic instability and protein aggregation.

TL;DR: The results suggest that missense mutations in ABD1 may all cause loss of dystrophin function via protein instability and aggregation rather than through loss of ligand binding function, however, more severe disease progressions may be due to the combinatorial effects of some mutations on both protein aggregation and impaired actin-binding activity.
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Longitudinal detection of prion shedding in saliva and urine by chronic wasting disease-infected deer by real-time quaking-induced conversion.

TL;DR: An in vitro amplification assay is used to show that infectious doses of CWD prions are in fact shed throughout the multiyear disease course in deer, an important advance in assessing the risks posed by shed C WD prions to animals as well as humans.