UC-491 Spectrum Analysis CLI Tool

The Spectrum Analysis CLI Tool takes in .mp4 recordings of a Spectrum Analyzer, converts them programmatically into values the application can understand and outputs this data into a .csv file. This file can be parsed/filtered by the user with commands during upload of the .mp4 recording, or anytime after the recording has been processed

Electrodeposition of bismuth at a graphene modified carbon electrode and its application as an easily regenerated sensor for the electrochemical determination of the antimicrobial drug metronidazole

Metronidazole is a well-known antimicrobial drug that belongs to the nitroimidazole family of antibiotics. It has been widely used in the treatment of infections, but its accumulation in aquatic environments is an emerging concern. In this study a glassy carbon electrode was modified with graphene (Gr) nanoplatelets and bismuth. Both the Gr and Bi were electrochemically deposited onto the glassy carbon and the modified electrode was employed in the electrochemical detection of metronidazole. At the modified electrode, the reduction of metronidazole was found to be an adsorption-controlled reaction. The optimised sensor, which was fabricated within 6 min, exhibited good selectivity in the presence of various inorganic and organic compounds, good recovery in tap water, and exhibited a linear calibration curve extending from 0.005 to 260 μM, with a limit of detection of 0.9 nM. The sensor was easily regenerated through the simple oxidation of the Bi deposit followed by a 100 s reduction period in the Bi(III) solution to give a newly generated surface. Good reproducibility was achieved using this simple regeneration approach

Kinesin light chain-1 serine-460 phosphorylation is altered in Alzheimer's disease and regulates axonal transport and processing of the amyloid precursor protein

Damage to axonal transport is an early pathogenic event in Alzheimer's disease. The amyloid precursor protein (APP) is a key axonal transport cargo since disruption to APP transport promotes amyloidogenic processing of APP. Moreover, altered APP processing itself disrupts axonal transport. The mechanisms that regulate axonal transport of APP are therefore directly relevant to Alzheimer's disease pathogenesis. APP is transported anterogradely through axons on kinesin-1 motors and one route for this transport involves calsyntenin-1, a type-1 membrane spanning protein that acts as a direct ligand for kinesin-1 light chains (KLCs). Thus, loss of calsyntenin-1 disrupts APP axonal transport and promotes amyloidogenic processing of APP. Phosphorylation of KLC1 on serine-460 has been shown to reduce anterograde axonal transport of calsyntenin-1 by inhibiting the KLC1-calsyntenin-1 interaction. Here we demonstrate that in Alzheimer's disease frontal cortex, KLC1 levels are reduced and the relative levels of KLC1 serine-460 phosphorylation are increased; these changes occur relatively early in the disease process. We also show that a KLC1 serine-460 phosphomimetic mutant inhibits axonal transport of APP in both mammalian neurons in culture and in Drosophila neurons in vivo. Finally, we demonstrate that expression of the KLC1 serine-460 phosphomimetic mutant promotes amyloidogenic processing of APP. Together, these results suggest that increased KLC1 serine-460 phosphorylation contributes to Alzheimer's disease

Comparison of morphological variation indicative of ploidy-level in Phragmites australis (Poaceae) from Eastern North America.

ABSTRACT. Variation in ploidy levels in Phragmites australis is a welldocumented phenomenon although North American populations are less studied than European ones. It has been suggested, based on morphological measurements, that native and introduced P. australis subspecies in North America represent different ploidy levels. The objectives of this study were to assess whether guard cell size and stomatal density, morphological differences indicative of variation in ploidy level between native and introduced P. australis, are truly associated with different ploidy levels as measured by flow cytometry. Significant differences in guard cell size and stomatal densities were found between subspecies, with native plants having larger guard cells and lower stomatal density. However, no differences in 2C DNA content were found. Although these morphological measurements are significantly correlated with subspecies and can be added to the list of useful morphological characters distinguishing the two subspecies, it does not appear that they are accurate indicators of ploidy levels. Potential implications of these differences on the invasion biology of introduced P. australis are discussed

The VAPB-PTPIP51 endoplasmic reticulum-mitochondria tethering proteins are present in neuronal synapses and regulate synaptic activity

Signaling between the endoplasmic reticulum (ER) and mitochondria regulates a number of key neuronal functions. This signaling involves close physical contacts between the two organelles that are mediated by “tethering proteins” that function to recruit regions of ER to the mitochondrial surface. The ER protein, vesicle-associated membrane protein-associated protein B (VAPB) and the mitochondrial membrane protein, protein tyrosine phosphatase interacting protein-51 (PTPIP51), interact to form one such tether. Recently, damage to ER-mitochondria signaling involving disruption of the VAPB-PTPIP51 tethers has been linked to the pathogenic process in Parkinson’s disease, fronto-temporal dementia (FTD) and related amyotrophic lateral sclerosis (ALS). Loss of neuronal synaptic function is a key feature of Parkinson’s disease and FTD/ALS but the roles that ER-mitochondria signaling and the VAPB-PTPIP51 tethers play in synaptic function are not known. Here, we demonstrate that the VAPB-PTPIP51 tethers regulate synaptic activity. VAPB and PTPIP51 localise and form contacts at synapses, and stimulating neuronal activity increases ER-mitochondria contacts and the VAPB-PTPIP51 interaction. Moreover, siRNA loss of VAPB or PTPIP51 perturbs synaptic function and dendritic spine morphology. Our results reveal a new role for the VAPB-PTPIP51 tethers in neurons and suggest that damage to ER-mitochondria signaling contributes to synaptic dysfunction in Parkinson’s disease and FTD/ALS