Saliva is valuable in exposure assessment having been successfully used for drug and environmental pollutant detection, providing a surrogate measure of plasma concentrations. Pyrethroid biomarkers have not previously been assessed in saliva, although are prime candidates for saliva detection. This study's objectives were to 1) develop a liquid-liquid extraction (LLE) method to quantify six pyrethroid metabolites using gas chromatography/ion trap mass spectrometry and 2) assess its application for an occupationally exposed population.
View Article and Find Full Text PDFQuantifying Cu in post-detonation nuclear debris samples can provide important diagnostic information regarding the structural materials used within a nuclear device. However, this task is challenging due to the weak gamma emissions associated with the decay of Cu, its short half-life (12.701 h), and the presence of interfering fission product radioisotopes.
View Article and Find Full Text PDFTauopathies represent a diverse group of neurodegenerative disorders characterized by the abnormal aggregation of the microtubule-associated protein tau. Despite extensive research, the precise mechanisms underlying the complexity of different types of tau pathology remain incompletely understood. Here we describe an approach for proteomic profiling of aggregate-associated proteomes on slides with formalin-fixed, paraffin-embedded (FFPE) tissue that utilizes proximity labelling upon high preservation of aggregate morphology, which permits the profiling of pathological aggregates regardless of their size.
View Article and Find Full Text PDFA method has been developed to purify and measure platinum radioisotopes in the presence of fission products and environmental constituents. The method uses a combination of cation exchange and anion exchange chromatography and selective precipitation steps to remove other radioisotopes from the sample. The addition of stable platinum carrier allows for a gravimetric determination of the chemical yield of the procedure.
View Article and Find Full Text PDFBackground: Cytoplasmic mislocalization and aggregation of TAR DNA-binding protein-43 (TDP-43) is a hallmark of the amyotrophic lateral sclerosis and frontotemporal dementia (ALS/FTD) disease spectrum, causing both nuclear loss-of-function and cytoplasmic toxic gain-of-function phenotypes. While TDP-43 proteinopathy has been associated with defects in nucleocytoplasmic transport, this process is still poorly understood. Here we study the role of karyopherin-β1 (KPNB1) and other nuclear import receptors in regulating TDP-43 pathology.
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