Cardiac Computed Tomography to exclude left atrial appendage thrombus in atrial arrhythmias prior to electrical cardioversion during the COVID-19 pandemic.

Nil.

Edge-Based Transfer Learning for Classroom Occupancy Detection in a Smart Campus Context.

Studies and systems that are aimed at the identification of the presence of people within an indoor environment and the monitoring of their activities and flows have been receiving more attention in recent years, specifically since the beginning of the COVID-19 pandemic. This paper proposes an approach for people counting that is based on the use of cameras and Raspberry Pi platforms, together with an edge-based transfer learning framework that is enriched with specific image processing strategies, with the aim of this approach being adopted in different indoor environments without the need for tailored training phases. The system was deployed on a university campus, which was chosen as the case study. The proposed system was able to work in classrooms with different characteristics. This paper reports a proposed architecture that could make the system scalable and privacy compliant and the evaluation tests that were conducted in different types of classrooms, which demonstrate the feasibility of this approach. Overall, the system was able to count the number of people in classrooms with a maximum mean absolute error of 1.23.

Characterization of Phosphopantetheinyl Hydrolase from Mycobacterium tuberculosis.

Phosphopantetheinyl hydrolase, PptH (Rv2795c), is a recently discovered enzyme from Mycobacterium tuberculosis that removes 4'-phosphopantetheine (Ppt) from holo-carrier proteins (CPs) and thereby opposes the action of phosphopantetheinyl transferases (PPTases). PptH is the first structurally characterized enzyme of the phosphopantetheinyl hydrolase family. However, conditions for optimal activity of PptH have not been defined, and only one substrate has been identified. Here, we provide biochemical characterization of PptH and demonstrate that the enzyme hydrolyzes Ppt in vitro from more than one M. tuberculosis holo-CP as well as holo-CPs from other organisms. PptH provided the only detectable activity in mycobacterial lysates that dephosphopantetheinylated acyl carrier protein M (AcpM), suggesting that PptH is the main Ppt hydrolase in M. tuberculosis. We could not detect a role for PptH in coenzyme A (CoA) salvage, and PptH was not required for virulence of M. tuberculosis during infection of mice. It remains to be determined why mycobacteria conserve a broadly acting phosphohydrolase that removes the Ppt prosthetic group from essential CPs. We speculate that the enzyme is critical for aspects of the life cycle of M. tuberculosis that are not routinely modeled. IMPORTANCE Tuberculosis (TB), caused by Mycobacterium tuberculosis, was the leading cause of death from an infectious disease before COVID, yet the in vivo essentiality and function of many of the protein-encoding genes expressed by M. tuberculosis are not known. We biochemically characterize M. tuberculosis's phosphopantetheinyl hydrolase, PptH, a protein unique to mycobacteria that removes an essential posttranslational modification on proteins involved in synthesis of lipids important for the bacterium's cell wall and virulence. We demonstrate that the enzyme has broad substrate specificity, but it does not appear to have a role in coenzyme A (CoA) salvage or virulence in a mouse model of TB.