RESUMEN
The microstructural evolutions of both uncarbonated and carbonated cement pastes subjected to various high temperatures (30 °C, 200 °C, 400 °C, 500 °C, 600 °C, 720 °C, and 950 °C) are presented in this study by the means of mercury intrusion porosimetry (MIP) and scanning electron microscopy (SEM). It was found that the thermal stabilities of uncarbonated cement pastes were significantly changed from 400 to 500 °C due to the decomposition of portlandite at this temperature range. More large pores and microcracks were generated from 600 to 720 °C, with the depolymerization of C-S-H. After carbonation, the microstructures of carbonated cement pastes remained unchanged below 500 °C and started to degrade at 600 °C, due to the decompositions of calcium carbonates and calcium modified silica gel. At 950 °C, both uncarbonated and carbonated cement pastes showed a loosely honeycombed microstructure, composed mainly of ß-C2S and lime. It can be concluded that carbonation improves the high-temperature resistance of cement pastes up to 500 °C, but this advantage is lost at temperatures over 600 °C.
RESUMEN
COVID-19, caused by Severe Acute Respiratory Syndrome Coronavirus 2 (SARS-CoV-2), has quickly become a global health crisis since the first report of infection in December of 2019. However, the infection spectrum of SARS-CoV-2 and its comprehensive protein-level interactions with hosts remain unclear. There is a massive amount of underutilized data and knowledge about RNA viruses highly relevant to SARS-CoV-2 and proteins of their hosts. More in-depth and more comprehensive analyses of that knowledge and data can shed new light on the molecular mechanisms underlying the COVID-19 pandemic and reveal potential risks. In this work, we constructed a multi-layer virus-host interaction network to incorporate these data and knowledge. We developed a machine-learning-based method to predict virus-host interactions at both protein and organism levels. Our approach revealed five potential infection targets of SARS-CoV-2 and 19 highly possible interactions between SARS-CoV-2 proteins and human proteins in the innate immune pathway.