Liquefaction-Induced Lateral Ground Displacement

Ground displacements generated by liquefaction-induced lateral spread are a severe threat to engineered construction. During past earthquakes, lateral spread displacements have pulled apart or sheared shallow and deep foundations of buildings, severed pipelines and other structures and utilities that transect the ground displacement zone, buckled bridges or other structures constructed across the toe, and toppled retaining walls, bulkheads, etc. that lie in the path of the spreading ground. This paper presents a method for estimating probable free-field lateral displacements at sites susceptible to liquefaction. Free-field ground displacements are those that are not impeded by structural resistance, ground modification, or a natural boundary

Critical packing in granular shear bands

In a realistic three-dimensional setup, we simulate the slow deformation of idealized granular media composed of spheres undergoing an axisymmetric triaxial shear test. We follow the self-organization of the spontaneous strain localization process leading to a shear band and demonstrate the existence of a critical packing density inside this failure zone. The asymptotic criticality arising from the dynamic equilibrium of dilation and compaction is found to be restricted to the shear band, while the density outside of it keeps the memory of the initial packing. The critical density of the shear band depends on friction (and grain geometry) and in the limit of infinite friction it defines a specific packing state, namely the \emph{dynamic random loose packing}

LRR-protein RNH1 dampens the inflammasome activation and is associated with COVID-19 severity.

Inflammasomes are cytosolic innate immune sensors of pathogen infection and cellular damage that induce caspase-1-mediated inflammation upon activation. Although inflammation is protective, uncontrolled excessive inflammation can cause inflammatory diseases and can be detrimental, such as in coronavirus disease (COVID-19). However, the underlying mechanisms that control inflammasome activation are incompletely understood. Here we report that the leucine-rich repeat (LRR) protein ribonuclease inhibitor (RNH1), which shares homology with LRRs of NLRP (nucleotide-binding oligomerization domain, leucine-rich repeat, and pyrin domain containing) proteins, attenuates inflammasome activation. Deletion of RNH1 in macrophages increases interleukin (IL)-1β production and caspase-1 activation in response to inflammasome stimulation. Mechanistically, RNH1 decreases pro-IL-1β expression and induces proteasome-mediated caspase-1 degradation. Corroborating this, mouse models of monosodium urate (MSU)-induced peritonitis and lipopolysaccharide (LPS)-induced endotoxemia, which are dependent on caspase-1, respectively, show increased neutrophil infiltration and lethality in Rnh1 <sup>-/-</sup> mice compared with wild-type mice. Furthermore, RNH1 protein levels were negatively related with disease severity and inflammation in hospitalized COVID-19 patients. We propose that RNH1 is a new inflammasome regulator with relevance to COVID-19 severity